data_2ARK
# 
_entry.id   2ARK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   2ARK         pdb_00002ark 10.2210/pdb2ark/pdb 
RCSB  RCSB034229   ?            ?                   
WWPDB D_1000034229 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2005-10-25 
2 'Structure model' 1 1 2008-04-30 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2022-04-13 
5 'Structure model' 1 4 2024-11-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' Advisory                    
3 3 'Structure model' 'Version format compliance' 
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Derived calculations'      
6 4 'Structure model' 'Structure summary'         
7 5 'Structure model' 'Data collection'           
8 5 'Structure model' 'Structure summary'         
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  4 'Structure model' audit_author              
2  4 'Structure model' citation_author           
3  4 'Structure model' database_2                
4  4 'Structure model' struct_conn               
5  4 'Structure model' struct_ref_seq_dif        
6  4 'Structure model' struct_site               
7  5 'Structure model' chem_comp_atom            
8  5 'Structure model' chem_comp_bond            
9  5 'Structure model' pdbx_entry_details        
10 5 'Structure model' pdbx_modification_feature 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_audit_author.identifier_ORCID'      
2 4 'Structure model' '_citation_author.identifier_ORCID'   
3 4 'Structure model' '_database_2.pdbx_DOI'                
4 4 'Structure model' '_database_2.pdbx_database_accession' 
5 4 'Structure model' '_struct_conn.pdbx_leaving_atom_flag' 
6 4 'Structure model' '_struct_ref_seq_dif.details'         
7 4 'Structure model' '_struct_site.pdbx_auth_asym_id'      
8 4 'Structure model' '_struct_site.pdbx_auth_comp_id'      
9 4 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2ARK 
_pdbx_database_status.recvd_initial_deposition_date   2005-08-19 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_database_related.db_name        TargetDB 
_pdbx_database_related.db_id          APC22280 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cuff, M.E.'                                    1 ?                   
'Quartey, P.'                                   2 ?                   
'Zhou, M.'                                      3 ?                   
'Cymborowski, M.'                               4 ?                   
'Minor, W.'                                     5 0000-0001-7075-7090 
'Joachimiak, A.'                                6 ?                   
'Midwest Center for Structural Genomics (MCSG)' 7 ?                   
# 
_citation.id                        primary 
_citation.title                     'Structure of a flavodoxin from Aquifex aeolicus' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cuff, M.E.'      1 ?                   
primary 'Quartey, P.'     2 ?                   
primary 'Zhou, M.'        3 ?                   
primary 'Cymborowski, M.' 4 ?                   
primary 'Minor, W.'       5 0000-0001-7075-7090 
primary 'Joachimiak, A.'  6 ?                   
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Flavodoxin      21072.107 6   ? ? ? ? 
2 non-polymer syn 'PHOSPHATE ION' 94.971    6   ? ? ? ? 
3 non-polymer syn GLYCEROL        92.094    6   ? ? ? ? 
4 water       nat water           18.015    420 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;SNA(MSE)GKVLVIYDTRTGNTKK(MSE)AELVAEGARSLEGTEVRLKHVDEATKEDVLWADGLAVGSPTN(MSE)GLVS
WK(MSE)KRFFDDVLGDLWGEIDGKIACAFSSSGGWGGGNEVAC(MSE)SILT(MSE)L(MSE)NFGFLVFGVTDYVGKK
FTLHYGAVVAGEPRSEEEKEACRRLGRRLAEWVAIFVDGRKELLEKIRKDPARFVD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNAMGKVLVIYDTRTGNTKKMAELVAEGARSLEGTEVRLKHVDEATKEDVLWADGLAVGSPTNMGLVSWKMKRFFDDVLG
DLWGEIDGKIACAFSSSGGWGGGNEVACMSILTMLMNFGFLVFGVTDYVGKKFTLHYGAVVAGEPRSEEEKEACRRLGRR
LAEWVAIFVDGRKELLEKIRKDPARFVD
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F 
_entity_poly.pdbx_target_identifier         APC22280 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PHOSPHATE ION' PO4 
3 GLYCEROL        GOL 
4 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASN n 
1 3   ALA n 
1 4   MSE n 
1 5   GLY n 
1 6   LYS n 
1 7   VAL n 
1 8   LEU n 
1 9   VAL n 
1 10  ILE n 
1 11  TYR n 
1 12  ASP n 
1 13  THR n 
1 14  ARG n 
1 15  THR n 
1 16  GLY n 
1 17  ASN n 
1 18  THR n 
1 19  LYS n 
1 20  LYS n 
1 21  MSE n 
1 22  ALA n 
1 23  GLU n 
1 24  LEU n 
1 25  VAL n 
1 26  ALA n 
1 27  GLU n 
1 28  GLY n 
1 29  ALA n 
1 30  ARG n 
1 31  SER n 
1 32  LEU n 
1 33  GLU n 
1 34  GLY n 
1 35  THR n 
1 36  GLU n 
1 37  VAL n 
1 38  ARG n 
1 39  LEU n 
1 40  LYS n 
1 41  HIS n 
1 42  VAL n 
1 43  ASP n 
1 44  GLU n 
1 45  ALA n 
1 46  THR n 
1 47  LYS n 
1 48  GLU n 
1 49  ASP n 
1 50  VAL n 
1 51  LEU n 
1 52  TRP n 
1 53  ALA n 
1 54  ASP n 
1 55  GLY n 
1 56  LEU n 
1 57  ALA n 
1 58  VAL n 
1 59  GLY n 
1 60  SER n 
1 61  PRO n 
1 62  THR n 
1 63  ASN n 
1 64  MSE n 
1 65  GLY n 
1 66  LEU n 
1 67  VAL n 
1 68  SER n 
1 69  TRP n 
1 70  LYS n 
1 71  MSE n 
1 72  LYS n 
1 73  ARG n 
1 74  PHE n 
1 75  PHE n 
1 76  ASP n 
1 77  ASP n 
1 78  VAL n 
1 79  LEU n 
1 80  GLY n 
1 81  ASP n 
1 82  LEU n 
1 83  TRP n 
1 84  GLY n 
1 85  GLU n 
1 86  ILE n 
1 87  ASP n 
1 88  GLY n 
1 89  LYS n 
1 90  ILE n 
1 91  ALA n 
1 92  CYS n 
1 93  ALA n 
1 94  PHE n 
1 95  SER n 
1 96  SER n 
1 97  SER n 
1 98  GLY n 
1 99  GLY n 
1 100 TRP n 
1 101 GLY n 
1 102 GLY n 
1 103 GLY n 
1 104 ASN n 
1 105 GLU n 
1 106 VAL n 
1 107 ALA n 
1 108 CYS n 
1 109 MSE n 
1 110 SER n 
1 111 ILE n 
1 112 LEU n 
1 113 THR n 
1 114 MSE n 
1 115 LEU n 
1 116 MSE n 
1 117 ASN n 
1 118 PHE n 
1 119 GLY n 
1 120 PHE n 
1 121 LEU n 
1 122 VAL n 
1 123 PHE n 
1 124 GLY n 
1 125 VAL n 
1 126 THR n 
1 127 ASP n 
1 128 TYR n 
1 129 VAL n 
1 130 GLY n 
1 131 LYS n 
1 132 LYS n 
1 133 PHE n 
1 134 THR n 
1 135 LEU n 
1 136 HIS n 
1 137 TYR n 
1 138 GLY n 
1 139 ALA n 
1 140 VAL n 
1 141 VAL n 
1 142 ALA n 
1 143 GLY n 
1 144 GLU n 
1 145 PRO n 
1 146 ARG n 
1 147 SER n 
1 148 GLU n 
1 149 GLU n 
1 150 GLU n 
1 151 LYS n 
1 152 GLU n 
1 153 ALA n 
1 154 CYS n 
1 155 ARG n 
1 156 ARG n 
1 157 LEU n 
1 158 GLY n 
1 159 ARG n 
1 160 ARG n 
1 161 LEU n 
1 162 ALA n 
1 163 GLU n 
1 164 TRP n 
1 165 VAL n 
1 166 ALA n 
1 167 ILE n 
1 168 PHE n 
1 169 VAL n 
1 170 ASP n 
1 171 GLY n 
1 172 ARG n 
1 173 LYS n 
1 174 GLU n 
1 175 LEU n 
1 176 LEU n 
1 177 GLU n 
1 178 LYS n 
1 179 ILE n 
1 180 ARG n 
1 181 LYS n 
1 182 ASP n 
1 183 PRO n 
1 184 ALA n 
1 185 ARG n 
1 186 PHE n 
1 187 VAL n 
1 188 ASP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     Aquifex 
_entity_src_gen.pdbx_gene_src_gene                 'fldA, floX' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Aquifex aeolicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     63363 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   'Escherichia coli' 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMCSG7 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE          ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE         ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE       ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'  ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE         ?                               'C3 H7 N O2 S'   121.158 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'  ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE          ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL         'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE        ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER            ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE       ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE          ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE           ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE       ?                               'C5 H11 N O2 S'  149.211 
MSE 'L-peptide linking' n SELENOMETHIONINE ?                               'C5 H11 N O2 Se' 196.106 
PHE 'L-peptide linking' y PHENYLALANINE    ?                               'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'  ?                               'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE          ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE           ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE        ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN       ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE         ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE           ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   -2  -2  SER SER A . n 
A 1 2   ASN 2   -1  -1  ASN ASN A . n 
A 1 3   ALA 3   0   0   ALA ALA A . n 
A 1 4   MSE 4   1   1   MSE MSE A . n 
A 1 5   GLY 5   2   2   GLY GLY A . n 
A 1 6   LYS 6   3   3   LYS LYS A . n 
A 1 7   VAL 7   4   4   VAL VAL A . n 
A 1 8   LEU 8   5   5   LEU LEU A . n 
A 1 9   VAL 9   6   6   VAL VAL A . n 
A 1 10  ILE 10  7   7   ILE ILE A . n 
A 1 11  TYR 11  8   8   TYR TYR A . n 
A 1 12  ASP 12  9   9   ASP ASP A . n 
A 1 13  THR 13  10  10  THR THR A . n 
A 1 14  ARG 14  11  11  ARG ARG A . n 
A 1 15  THR 15  12  12  THR THR A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  ASN 17  14  14  ASN ASN A . n 
A 1 18  THR 18  15  15  THR THR A . n 
A 1 19  LYS 19  16  16  LYS LYS A . n 
A 1 20  LYS 20  17  17  LYS LYS A . n 
A 1 21  MSE 21  18  18  MSE MSE A . n 
A 1 22  ALA 22  19  19  ALA ALA A . n 
A 1 23  GLU 23  20  20  GLU GLU A . n 
A 1 24  LEU 24  21  21  LEU LEU A . n 
A 1 25  VAL 25  22  22  VAL VAL A . n 
A 1 26  ALA 26  23  23  ALA ALA A . n 
A 1 27  GLU 27  24  24  GLU GLU A . n 
A 1 28  GLY 28  25  25  GLY GLY A . n 
A 1 29  ALA 29  26  26  ALA ALA A . n 
A 1 30  ARG 30  27  27  ARG ARG A . n 
A 1 31  SER 31  28  28  SER SER A . n 
A 1 32  LEU 32  29  29  LEU LEU A . n 
A 1 33  GLU 33  30  30  GLU GLU A . n 
A 1 34  GLY 34  31  31  GLY GLY A . n 
A 1 35  THR 35  32  32  THR THR A . n 
A 1 36  GLU 36  33  33  GLU GLU A . n 
A 1 37  VAL 37  34  34  VAL VAL A . n 
A 1 38  ARG 38  35  35  ARG ARG A . n 
A 1 39  LEU 39  36  36  LEU LEU A . n 
A 1 40  LYS 40  37  37  LYS LYS A . n 
A 1 41  HIS 41  38  38  HIS HIS A . n 
A 1 42  VAL 42  39  39  VAL VAL A . n 
A 1 43  ASP 43  40  40  ASP ASP A . n 
A 1 44  GLU 44  41  41  GLU GLU A . n 
A 1 45  ALA 45  42  42  ALA ALA A . n 
A 1 46  THR 46  43  43  THR THR A . n 
A 1 47  LYS 47  44  44  LYS LYS A . n 
A 1 48  GLU 48  45  45  GLU GLU A . n 
A 1 49  ASP 49  46  46  ASP ASP A . n 
A 1 50  VAL 50  47  47  VAL VAL A . n 
A 1 51  LEU 51  48  48  LEU LEU A . n 
A 1 52  TRP 52  49  49  TRP TRP A . n 
A 1 53  ALA 53  50  50  ALA ALA A . n 
A 1 54  ASP 54  51  51  ASP ASP A . n 
A 1 55  GLY 55  52  52  GLY GLY A . n 
A 1 56  LEU 56  53  53  LEU LEU A . n 
A 1 57  ALA 57  54  54  ALA ALA A . n 
A 1 58  VAL 58  55  55  VAL VAL A . n 
A 1 59  GLY 59  56  56  GLY GLY A . n 
A 1 60  SER 60  57  57  SER SER A . n 
A 1 61  PRO 61  58  58  PRO PRO A . n 
A 1 62  THR 62  59  59  THR THR A . n 
A 1 63  ASN 63  60  60  ASN ASN A . n 
A 1 64  MSE 64  61  61  MSE MSE A . n 
A 1 65  GLY 65  62  62  GLY GLY A . n 
A 1 66  LEU 66  63  63  LEU LEU A . n 
A 1 67  VAL 67  64  64  VAL VAL A . n 
A 1 68  SER 68  65  65  SER SER A . n 
A 1 69  TRP 69  66  66  TRP TRP A . n 
A 1 70  LYS 70  67  67  LYS LYS A . n 
A 1 71  MSE 71  68  68  MSE MSE A . n 
A 1 72  LYS 72  69  69  LYS LYS A . n 
A 1 73  ARG 73  70  70  ARG ARG A . n 
A 1 74  PHE 74  71  71  PHE PHE A . n 
A 1 75  PHE 75  72  72  PHE PHE A . n 
A 1 76  ASP 76  73  73  ASP ASP A . n 
A 1 77  ASP 77  74  74  ASP ASP A . n 
A 1 78  VAL 78  75  75  VAL VAL A . n 
A 1 79  LEU 79  76  76  LEU LEU A . n 
A 1 80  GLY 80  77  77  GLY GLY A . n 
A 1 81  ASP 81  78  78  ASP ASP A . n 
A 1 82  LEU 82  79  79  LEU LEU A . n 
A 1 83  TRP 83  80  80  TRP TRP A . n 
A 1 84  GLY 84  81  81  GLY GLY A . n 
A 1 85  GLU 85  82  82  GLU GLU A . n 
A 1 86  ILE 86  83  83  ILE ILE A . n 
A 1 87  ASP 87  84  84  ASP ASP A . n 
A 1 88  GLY 88  85  85  GLY GLY A . n 
A 1 89  LYS 89  86  86  LYS LYS A . n 
A 1 90  ILE 90  87  87  ILE ILE A . n 
A 1 91  ALA 91  88  88  ALA ALA A . n 
A 1 92  CYS 92  89  89  CYS CYS A . n 
A 1 93  ALA 93  90  90  ALA ALA A . n 
A 1 94  PHE 94  91  91  PHE PHE A . n 
A 1 95  SER 95  92  92  SER SER A . n 
A 1 96  SER 96  93  93  SER SER A . n 
A 1 97  SER 97  94  94  SER SER A . n 
A 1 98  GLY 98  95  95  GLY GLY A . n 
A 1 99  GLY 99  96  96  GLY GLY A . n 
A 1 100 TRP 100 97  97  TRP TRP A . n 
A 1 101 GLY 101 98  98  GLY GLY A . n 
A 1 102 GLY 102 99  99  GLY GLY A . n 
A 1 103 GLY 103 100 100 GLY GLY A . n 
A 1 104 ASN 104 101 101 ASN ASN A . n 
A 1 105 GLU 105 102 102 GLU GLU A . n 
A 1 106 VAL 106 103 103 VAL VAL A . n 
A 1 107 ALA 107 104 104 ALA ALA A . n 
A 1 108 CYS 108 105 105 CYS CYS A . n 
A 1 109 MSE 109 106 106 MSE MSE A . n 
A 1 110 SER 110 107 107 SER SER A . n 
A 1 111 ILE 111 108 108 ILE ILE A . n 
A 1 112 LEU 112 109 109 LEU LEU A . n 
A 1 113 THR 113 110 110 THR THR A . n 
A 1 114 MSE 114 111 111 MSE MSE A . n 
A 1 115 LEU 115 112 112 LEU LEU A . n 
A 1 116 MSE 116 113 113 MSE MSE A . n 
A 1 117 ASN 117 114 114 ASN ASN A . n 
A 1 118 PHE 118 115 115 PHE PHE A . n 
A 1 119 GLY 119 116 116 GLY GLY A . n 
A 1 120 PHE 120 117 117 PHE PHE A . n 
A 1 121 LEU 121 118 118 LEU LEU A . n 
A 1 122 VAL 122 119 119 VAL VAL A . n 
A 1 123 PHE 123 120 120 PHE PHE A . n 
A 1 124 GLY 124 121 121 GLY GLY A . n 
A 1 125 VAL 125 122 122 VAL VAL A . n 
A 1 126 THR 126 123 123 THR THR A . n 
A 1 127 ASP 127 124 124 ASP ASP A . n 
A 1 128 TYR 128 125 125 TYR TYR A . n 
A 1 129 VAL 129 126 126 VAL VAL A . n 
A 1 130 GLY 130 127 127 GLY GLY A . n 
A 1 131 LYS 131 128 128 LYS LYS A . n 
A 1 132 LYS 132 129 129 LYS LYS A . n 
A 1 133 PHE 133 130 130 PHE PHE A . n 
A 1 134 THR 134 131 131 THR THR A . n 
A 1 135 LEU 135 132 132 LEU LEU A . n 
A 1 136 HIS 136 133 133 HIS HIS A . n 
A 1 137 TYR 137 134 134 TYR TYR A . n 
A 1 138 GLY 138 135 135 GLY GLY A . n 
A 1 139 ALA 139 136 136 ALA ALA A . n 
A 1 140 VAL 140 137 137 VAL VAL A . n 
A 1 141 VAL 141 138 138 VAL VAL A . n 
A 1 142 ALA 142 139 139 ALA ALA A . n 
A 1 143 GLY 143 140 140 GLY GLY A . n 
A 1 144 GLU 144 141 141 GLU GLU A . n 
A 1 145 PRO 145 142 142 PRO PRO A . n 
A 1 146 ARG 146 143 143 ARG ARG A . n 
A 1 147 SER 147 144 144 SER SER A . n 
A 1 148 GLU 148 145 145 GLU GLU A . n 
A 1 149 GLU 149 146 146 GLU GLU A . n 
A 1 150 GLU 150 147 147 GLU GLU A . n 
A 1 151 LYS 151 148 148 LYS LYS A . n 
A 1 152 GLU 152 149 149 GLU GLU A . n 
A 1 153 ALA 153 150 150 ALA ALA A . n 
A 1 154 CYS 154 151 151 CYS CYS A . n 
A 1 155 ARG 155 152 152 ARG ARG A . n 
A 1 156 ARG 156 153 153 ARG ARG A . n 
A 1 157 LEU 157 154 154 LEU LEU A . n 
A 1 158 GLY 158 155 155 GLY GLY A . n 
A 1 159 ARG 159 156 156 ARG ARG A . n 
A 1 160 ARG 160 157 157 ARG ARG A . n 
A 1 161 LEU 161 158 158 LEU LEU A . n 
A 1 162 ALA 162 159 159 ALA ALA A . n 
A 1 163 GLU 163 160 160 GLU GLU A . n 
A 1 164 TRP 164 161 161 TRP TRP A . n 
A 1 165 VAL 165 162 162 VAL VAL A . n 
A 1 166 ALA 166 163 163 ALA ALA A . n 
A 1 167 ILE 167 164 164 ILE ILE A . n 
A 1 168 PHE 168 165 165 PHE PHE A . n 
A 1 169 VAL 169 166 166 VAL VAL A . n 
A 1 170 ASP 170 167 167 ASP ASP A . n 
A 1 171 GLY 171 168 168 GLY GLY A . n 
A 1 172 ARG 172 169 169 ARG ARG A . n 
A 1 173 LYS 173 170 170 LYS LYS A . n 
A 1 174 GLU 174 171 171 GLU GLU A . n 
A 1 175 LEU 175 172 172 LEU LEU A . n 
A 1 176 LEU 176 173 173 LEU LEU A . n 
A 1 177 GLU 177 174 174 GLU GLU A . n 
A 1 178 LYS 178 175 175 LYS LYS A . n 
A 1 179 ILE 179 176 176 ILE ILE A . n 
A 1 180 ARG 180 177 177 ARG ARG A . n 
A 1 181 LYS 181 178 178 LYS LYS A . n 
A 1 182 ASP 182 179 179 ASP ASP A . n 
A 1 183 PRO 183 180 180 PRO PRO A . n 
A 1 184 ALA 184 181 181 ALA ALA A . n 
A 1 185 ARG 185 182 182 ARG ARG A . n 
A 1 186 PHE 186 183 183 PHE PHE A . n 
A 1 187 VAL 187 184 184 VAL VAL A . n 
A 1 188 ASP 188 185 ?   ?   ?   A . n 
B 1 1   SER 1   -2  ?   ?   ?   B . n 
B 1 2   ASN 2   -1  -1  ASN ASN B . n 
B 1 3   ALA 3   0   0   ALA ALA B . n 
B 1 4   MSE 4   1   1   MSE MSE B . n 
B 1 5   GLY 5   2   2   GLY GLY B . n 
B 1 6   LYS 6   3   3   LYS LYS B . n 
B 1 7   VAL 7   4   4   VAL VAL B . n 
B 1 8   LEU 8   5   5   LEU LEU B . n 
B 1 9   VAL 9   6   6   VAL VAL B . n 
B 1 10  ILE 10  7   7   ILE ILE B . n 
B 1 11  TYR 11  8   8   TYR TYR B . n 
B 1 12  ASP 12  9   9   ASP ASP B . n 
B 1 13  THR 13  10  10  THR THR B . n 
B 1 14  ARG 14  11  11  ARG ARG B . n 
B 1 15  THR 15  12  12  THR THR B . n 
B 1 16  GLY 16  13  13  GLY GLY B . n 
B 1 17  ASN 17  14  14  ASN ASN B . n 
B 1 18  THR 18  15  15  THR THR B . n 
B 1 19  LYS 19  16  16  LYS LYS B . n 
B 1 20  LYS 20  17  17  LYS LYS B . n 
B 1 21  MSE 21  18  18  MSE MSE B . n 
B 1 22  ALA 22  19  19  ALA ALA B . n 
B 1 23  GLU 23  20  20  GLU GLU B . n 
B 1 24  LEU 24  21  21  LEU LEU B . n 
B 1 25  VAL 25  22  22  VAL VAL B . n 
B 1 26  ALA 26  23  23  ALA ALA B . n 
B 1 27  GLU 27  24  24  GLU GLU B . n 
B 1 28  GLY 28  25  25  GLY GLY B . n 
B 1 29  ALA 29  26  26  ALA ALA B . n 
B 1 30  ARG 30  27  27  ARG ARG B . n 
B 1 31  SER 31  28  28  SER SER B . n 
B 1 32  LEU 32  29  29  LEU LEU B . n 
B 1 33  GLU 33  30  30  GLU GLU B . n 
B 1 34  GLY 34  31  31  GLY GLY B . n 
B 1 35  THR 35  32  32  THR THR B . n 
B 1 36  GLU 36  33  33  GLU GLU B . n 
B 1 37  VAL 37  34  34  VAL VAL B . n 
B 1 38  ARG 38  35  35  ARG ARG B . n 
B 1 39  LEU 39  36  36  LEU LEU B . n 
B 1 40  LYS 40  37  37  LYS LYS B . n 
B 1 41  HIS 41  38  38  HIS HIS B . n 
B 1 42  VAL 42  39  39  VAL VAL B . n 
B 1 43  ASP 43  40  40  ASP ASP B . n 
B 1 44  GLU 44  41  41  GLU GLU B . n 
B 1 45  ALA 45  42  42  ALA ALA B . n 
B 1 46  THR 46  43  43  THR THR B . n 
B 1 47  LYS 47  44  44  LYS LYS B . n 
B 1 48  GLU 48  45  45  GLU GLU B . n 
B 1 49  ASP 49  46  46  ASP ASP B . n 
B 1 50  VAL 50  47  47  VAL VAL B . n 
B 1 51  LEU 51  48  48  LEU LEU B . n 
B 1 52  TRP 52  49  49  TRP TRP B . n 
B 1 53  ALA 53  50  50  ALA ALA B . n 
B 1 54  ASP 54  51  51  ASP ASP B . n 
B 1 55  GLY 55  52  52  GLY GLY B . n 
B 1 56  LEU 56  53  53  LEU LEU B . n 
B 1 57  ALA 57  54  54  ALA ALA B . n 
B 1 58  VAL 58  55  55  VAL VAL B . n 
B 1 59  GLY 59  56  56  GLY GLY B . n 
B 1 60  SER 60  57  57  SER SER B . n 
B 1 61  PRO 61  58  58  PRO PRO B . n 
B 1 62  THR 62  59  59  THR THR B . n 
B 1 63  ASN 63  60  60  ASN ASN B . n 
B 1 64  MSE 64  61  61  MSE MSE B . n 
B 1 65  GLY 65  62  62  GLY GLY B . n 
B 1 66  LEU 66  63  63  LEU LEU B . n 
B 1 67  VAL 67  64  64  VAL VAL B . n 
B 1 68  SER 68  65  65  SER SER B . n 
B 1 69  TRP 69  66  66  TRP TRP B . n 
B 1 70  LYS 70  67  67  LYS LYS B . n 
B 1 71  MSE 71  68  68  MSE MSE B . n 
B 1 72  LYS 72  69  69  LYS LYS B . n 
B 1 73  ARG 73  70  70  ARG ARG B . n 
B 1 74  PHE 74  71  71  PHE PHE B . n 
B 1 75  PHE 75  72  72  PHE PHE B . n 
B 1 76  ASP 76  73  73  ASP ASP B . n 
B 1 77  ASP 77  74  74  ASP ASP B . n 
B 1 78  VAL 78  75  75  VAL VAL B . n 
B 1 79  LEU 79  76  76  LEU LEU B . n 
B 1 80  GLY 80  77  77  GLY GLY B . n 
B 1 81  ASP 81  78  78  ASP ASP B . n 
B 1 82  LEU 82  79  79  LEU LEU B . n 
B 1 83  TRP 83  80  80  TRP TRP B . n 
B 1 84  GLY 84  81  81  GLY GLY B . n 
B 1 85  GLU 85  82  82  GLU GLU B . n 
B 1 86  ILE 86  83  83  ILE ILE B . n 
B 1 87  ASP 87  84  84  ASP ASP B . n 
B 1 88  GLY 88  85  85  GLY GLY B . n 
B 1 89  LYS 89  86  86  LYS LYS B . n 
B 1 90  ILE 90  87  87  ILE ILE B . n 
B 1 91  ALA 91  88  88  ALA ALA B . n 
B 1 92  CYS 92  89  89  CYS CYS B . n 
B 1 93  ALA 93  90  90  ALA ALA B . n 
B 1 94  PHE 94  91  91  PHE PHE B . n 
B 1 95  SER 95  92  92  SER SER B . n 
B 1 96  SER 96  93  93  SER SER B . n 
B 1 97  SER 97  94  94  SER SER B . n 
B 1 98  GLY 98  95  95  GLY GLY B . n 
B 1 99  GLY 99  96  96  GLY GLY B . n 
B 1 100 TRP 100 97  97  TRP TRP B . n 
B 1 101 GLY 101 98  98  GLY GLY B . n 
B 1 102 GLY 102 99  99  GLY GLY B . n 
B 1 103 GLY 103 100 100 GLY GLY B . n 
B 1 104 ASN 104 101 101 ASN ASN B . n 
B 1 105 GLU 105 102 102 GLU GLU B . n 
B 1 106 VAL 106 103 103 VAL VAL B . n 
B 1 107 ALA 107 104 104 ALA ALA B . n 
B 1 108 CYS 108 105 105 CYS CYS B . n 
B 1 109 MSE 109 106 106 MSE MSE B . n 
B 1 110 SER 110 107 107 SER SER B . n 
B 1 111 ILE 111 108 108 ILE ILE B . n 
B 1 112 LEU 112 109 109 LEU LEU B . n 
B 1 113 THR 113 110 110 THR THR B . n 
B 1 114 MSE 114 111 111 MSE MSE B . n 
B 1 115 LEU 115 112 112 LEU LEU B . n 
B 1 116 MSE 116 113 113 MSE MSE B . n 
B 1 117 ASN 117 114 114 ASN ASN B . n 
B 1 118 PHE 118 115 115 PHE PHE B . n 
B 1 119 GLY 119 116 116 GLY GLY B . n 
B 1 120 PHE 120 117 117 PHE PHE B . n 
B 1 121 LEU 121 118 118 LEU LEU B . n 
B 1 122 VAL 122 119 119 VAL VAL B . n 
B 1 123 PHE 123 120 120 PHE PHE B . n 
B 1 124 GLY 124 121 121 GLY GLY B . n 
B 1 125 VAL 125 122 122 VAL VAL B . n 
B 1 126 THR 126 123 123 THR THR B . n 
B 1 127 ASP 127 124 124 ASP ASP B . n 
B 1 128 TYR 128 125 125 TYR TYR B . n 
B 1 129 VAL 129 126 126 VAL VAL B . n 
B 1 130 GLY 130 127 127 GLY GLY B . n 
B 1 131 LYS 131 128 128 LYS LYS B . n 
B 1 132 LYS 132 129 129 LYS LYS B . n 
B 1 133 PHE 133 130 130 PHE PHE B . n 
B 1 134 THR 134 131 131 THR THR B . n 
B 1 135 LEU 135 132 132 LEU LEU B . n 
B 1 136 HIS 136 133 133 HIS HIS B . n 
B 1 137 TYR 137 134 134 TYR TYR B . n 
B 1 138 GLY 138 135 135 GLY GLY B . n 
B 1 139 ALA 139 136 136 ALA ALA B . n 
B 1 140 VAL 140 137 137 VAL VAL B . n 
B 1 141 VAL 141 138 138 VAL VAL B . n 
B 1 142 ALA 142 139 139 ALA ALA B . n 
B 1 143 GLY 143 140 140 GLY GLY B . n 
B 1 144 GLU 144 141 141 GLU GLU B . n 
B 1 145 PRO 145 142 142 PRO PRO B . n 
B 1 146 ARG 146 143 143 ARG ARG B . n 
B 1 147 SER 147 144 144 SER SER B . n 
B 1 148 GLU 148 145 145 GLU GLU B . n 
B 1 149 GLU 149 146 146 GLU GLU B . n 
B 1 150 GLU 150 147 147 GLU GLU B . n 
B 1 151 LYS 151 148 148 LYS LYS B . n 
B 1 152 GLU 152 149 149 GLU GLU B . n 
B 1 153 ALA 153 150 150 ALA ALA B . n 
B 1 154 CYS 154 151 151 CYS CYS B . n 
B 1 155 ARG 155 152 152 ARG ARG B . n 
B 1 156 ARG 156 153 153 ARG ARG B . n 
B 1 157 LEU 157 154 154 LEU LEU B . n 
B 1 158 GLY 158 155 155 GLY GLY B . n 
B 1 159 ARG 159 156 156 ARG ARG B . n 
B 1 160 ARG 160 157 157 ARG ARG B . n 
B 1 161 LEU 161 158 158 LEU LEU B . n 
B 1 162 ALA 162 159 159 ALA ALA B . n 
B 1 163 GLU 163 160 160 GLU GLU B . n 
B 1 164 TRP 164 161 161 TRP TRP B . n 
B 1 165 VAL 165 162 162 VAL VAL B . n 
B 1 166 ALA 166 163 163 ALA ALA B . n 
B 1 167 ILE 167 164 164 ILE ILE B . n 
B 1 168 PHE 168 165 165 PHE PHE B . n 
B 1 169 VAL 169 166 166 VAL VAL B . n 
B 1 170 ASP 170 167 167 ASP ASP B . n 
B 1 171 GLY 171 168 168 GLY GLY B . n 
B 1 172 ARG 172 169 169 ARG ARG B . n 
B 1 173 LYS 173 170 170 LYS LYS B . n 
B 1 174 GLU 174 171 171 GLU GLU B . n 
B 1 175 LEU 175 172 172 LEU LEU B . n 
B 1 176 LEU 176 173 173 LEU LEU B . n 
B 1 177 GLU 177 174 174 GLU GLU B . n 
B 1 178 LYS 178 175 175 LYS LYS B . n 
B 1 179 ILE 179 176 176 ILE ILE B . n 
B 1 180 ARG 180 177 177 ARG ARG B . n 
B 1 181 LYS 181 178 178 LYS LYS B . n 
B 1 182 ASP 182 179 179 ASP ASP B . n 
B 1 183 PRO 183 180 180 PRO PRO B . n 
B 1 184 ALA 184 181 181 ALA ALA B . n 
B 1 185 ARG 185 182 182 ARG ARG B . n 
B 1 186 PHE 186 183 183 PHE PHE B . n 
B 1 187 VAL 187 184 184 VAL VAL B . n 
B 1 188 ASP 188 185 ?   ?   ?   B . n 
C 1 1   SER 1   -2  ?   ?   ?   C . n 
C 1 2   ASN 2   -1  ?   ?   ?   C . n 
C 1 3   ALA 3   0   0   ALA ALA C . n 
C 1 4   MSE 4   1   1   MSE MSE C . n 
C 1 5   GLY 5   2   2   GLY GLY C . n 
C 1 6   LYS 6   3   3   LYS LYS C . n 
C 1 7   VAL 7   4   4   VAL VAL C . n 
C 1 8   LEU 8   5   5   LEU LEU C . n 
C 1 9   VAL 9   6   6   VAL VAL C . n 
C 1 10  ILE 10  7   7   ILE ILE C . n 
C 1 11  TYR 11  8   8   TYR TYR C . n 
C 1 12  ASP 12  9   9   ASP ASP C . n 
C 1 13  THR 13  10  10  THR THR C . n 
C 1 14  ARG 14  11  11  ARG ARG C . n 
C 1 15  THR 15  12  12  THR THR C . n 
C 1 16  GLY 16  13  13  GLY GLY C . n 
C 1 17  ASN 17  14  14  ASN ASN C . n 
C 1 18  THR 18  15  15  THR THR C . n 
C 1 19  LYS 19  16  16  LYS LYS C . n 
C 1 20  LYS 20  17  17  LYS LYS C . n 
C 1 21  MSE 21  18  18  MSE MSE C . n 
C 1 22  ALA 22  19  19  ALA ALA C . n 
C 1 23  GLU 23  20  20  GLU GLU C . n 
C 1 24  LEU 24  21  21  LEU LEU C . n 
C 1 25  VAL 25  22  22  VAL VAL C . n 
C 1 26  ALA 26  23  23  ALA ALA C . n 
C 1 27  GLU 27  24  24  GLU GLU C . n 
C 1 28  GLY 28  25  25  GLY GLY C . n 
C 1 29  ALA 29  26  26  ALA ALA C . n 
C 1 30  ARG 30  27  27  ARG ARG C . n 
C 1 31  SER 31  28  28  SER SER C . n 
C 1 32  LEU 32  29  29  LEU LEU C . n 
C 1 33  GLU 33  30  30  GLU GLU C . n 
C 1 34  GLY 34  31  31  GLY GLY C . n 
C 1 35  THR 35  32  32  THR THR C . n 
C 1 36  GLU 36  33  33  GLU GLU C . n 
C 1 37  VAL 37  34  34  VAL VAL C . n 
C 1 38  ARG 38  35  35  ARG ARG C . n 
C 1 39  LEU 39  36  36  LEU LEU C . n 
C 1 40  LYS 40  37  37  LYS LYS C . n 
C 1 41  HIS 41  38  38  HIS HIS C . n 
C 1 42  VAL 42  39  39  VAL VAL C . n 
C 1 43  ASP 43  40  40  ASP ASP C . n 
C 1 44  GLU 44  41  41  GLU GLU C . n 
C 1 45  ALA 45  42  42  ALA ALA C . n 
C 1 46  THR 46  43  43  THR THR C . n 
C 1 47  LYS 47  44  44  LYS LYS C . n 
C 1 48  GLU 48  45  45  GLU GLU C . n 
C 1 49  ASP 49  46  46  ASP ASP C . n 
C 1 50  VAL 50  47  47  VAL VAL C . n 
C 1 51  LEU 51  48  48  LEU LEU C . n 
C 1 52  TRP 52  49  49  TRP TRP C . n 
C 1 53  ALA 53  50  50  ALA ALA C . n 
C 1 54  ASP 54  51  51  ASP ASP C . n 
C 1 55  GLY 55  52  52  GLY GLY C . n 
C 1 56  LEU 56  53  53  LEU LEU C . n 
C 1 57  ALA 57  54  54  ALA ALA C . n 
C 1 58  VAL 58  55  55  VAL VAL C . n 
C 1 59  GLY 59  56  56  GLY GLY C . n 
C 1 60  SER 60  57  57  SER SER C . n 
C 1 61  PRO 61  58  58  PRO PRO C . n 
C 1 62  THR 62  59  59  THR THR C . n 
C 1 63  ASN 63  60  60  ASN ASN C . n 
C 1 64  MSE 64  61  61  MSE MSE C . n 
C 1 65  GLY 65  62  62  GLY GLY C . n 
C 1 66  LEU 66  63  63  LEU LEU C . n 
C 1 67  VAL 67  64  64  VAL VAL C . n 
C 1 68  SER 68  65  65  SER SER C . n 
C 1 69  TRP 69  66  66  TRP TRP C . n 
C 1 70  LYS 70  67  67  LYS LYS C . n 
C 1 71  MSE 71  68  68  MSE MSE C . n 
C 1 72  LYS 72  69  69  LYS LYS C . n 
C 1 73  ARG 73  70  70  ARG ARG C . n 
C 1 74  PHE 74  71  71  PHE PHE C . n 
C 1 75  PHE 75  72  72  PHE PHE C . n 
C 1 76  ASP 76  73  73  ASP ASP C . n 
C 1 77  ASP 77  74  74  ASP ASP C . n 
C 1 78  VAL 78  75  75  VAL VAL C . n 
C 1 79  LEU 79  76  76  LEU LEU C . n 
C 1 80  GLY 80  77  77  GLY GLY C . n 
C 1 81  ASP 81  78  78  ASP ASP C . n 
C 1 82  LEU 82  79  79  LEU LEU C . n 
C 1 83  TRP 83  80  80  TRP TRP C . n 
C 1 84  GLY 84  81  81  GLY GLY C . n 
C 1 85  GLU 85  82  82  GLU GLU C . n 
C 1 86  ILE 86  83  83  ILE ILE C . n 
C 1 87  ASP 87  84  84  ASP ASP C . n 
C 1 88  GLY 88  85  85  GLY GLY C . n 
C 1 89  LYS 89  86  86  LYS LYS C . n 
C 1 90  ILE 90  87  87  ILE ILE C . n 
C 1 91  ALA 91  88  88  ALA ALA C . n 
C 1 92  CYS 92  89  89  CYS CYS C . n 
C 1 93  ALA 93  90  90  ALA ALA C . n 
C 1 94  PHE 94  91  91  PHE PHE C . n 
C 1 95  SER 95  92  92  SER SER C . n 
C 1 96  SER 96  93  93  SER SER C . n 
C 1 97  SER 97  94  94  SER SER C . n 
C 1 98  GLY 98  95  95  GLY GLY C . n 
C 1 99  GLY 99  96  96  GLY GLY C . n 
C 1 100 TRP 100 97  97  TRP TRP C . n 
C 1 101 GLY 101 98  98  GLY GLY C . n 
C 1 102 GLY 102 99  99  GLY GLY C . n 
C 1 103 GLY 103 100 100 GLY GLY C . n 
C 1 104 ASN 104 101 101 ASN ASN C . n 
C 1 105 GLU 105 102 102 GLU GLU C . n 
C 1 106 VAL 106 103 103 VAL VAL C . n 
C 1 107 ALA 107 104 104 ALA ALA C . n 
C 1 108 CYS 108 105 105 CYS CYS C . n 
C 1 109 MSE 109 106 106 MSE MSE C . n 
C 1 110 SER 110 107 107 SER SER C . n 
C 1 111 ILE 111 108 108 ILE ILE C . n 
C 1 112 LEU 112 109 109 LEU LEU C . n 
C 1 113 THR 113 110 110 THR THR C . n 
C 1 114 MSE 114 111 111 MSE MSE C . n 
C 1 115 LEU 115 112 112 LEU LEU C . n 
C 1 116 MSE 116 113 113 MSE MSE C . n 
C 1 117 ASN 117 114 114 ASN ASN C . n 
C 1 118 PHE 118 115 115 PHE PHE C . n 
C 1 119 GLY 119 116 116 GLY GLY C . n 
C 1 120 PHE 120 117 117 PHE PHE C . n 
C 1 121 LEU 121 118 118 LEU LEU C . n 
C 1 122 VAL 122 119 119 VAL VAL C . n 
C 1 123 PHE 123 120 120 PHE PHE C . n 
C 1 124 GLY 124 121 121 GLY GLY C . n 
C 1 125 VAL 125 122 122 VAL VAL C . n 
C 1 126 THR 126 123 123 THR THR C . n 
C 1 127 ASP 127 124 124 ASP ASP C . n 
C 1 128 TYR 128 125 125 TYR TYR C . n 
C 1 129 VAL 129 126 126 VAL VAL C . n 
C 1 130 GLY 130 127 127 GLY GLY C . n 
C 1 131 LYS 131 128 128 LYS LYS C . n 
C 1 132 LYS 132 129 129 LYS LYS C . n 
C 1 133 PHE 133 130 130 PHE PHE C . n 
C 1 134 THR 134 131 131 THR THR C . n 
C 1 135 LEU 135 132 132 LEU LEU C . n 
C 1 136 HIS 136 133 133 HIS HIS C . n 
C 1 137 TYR 137 134 134 TYR TYR C . n 
C 1 138 GLY 138 135 135 GLY GLY C . n 
C 1 139 ALA 139 136 136 ALA ALA C . n 
C 1 140 VAL 140 137 137 VAL VAL C . n 
C 1 141 VAL 141 138 138 VAL VAL C . n 
C 1 142 ALA 142 139 139 ALA ALA C . n 
C 1 143 GLY 143 140 140 GLY GLY C . n 
C 1 144 GLU 144 141 141 GLU GLU C . n 
C 1 145 PRO 145 142 142 PRO PRO C . n 
C 1 146 ARG 146 143 143 ARG ARG C . n 
C 1 147 SER 147 144 144 SER SER C . n 
C 1 148 GLU 148 145 145 GLU GLU C . n 
C 1 149 GLU 149 146 146 GLU GLU C . n 
C 1 150 GLU 150 147 147 GLU GLU C . n 
C 1 151 LYS 151 148 148 LYS LYS C . n 
C 1 152 GLU 152 149 149 GLU GLU C . n 
C 1 153 ALA 153 150 150 ALA ALA C . n 
C 1 154 CYS 154 151 151 CYS CYS C . n 
C 1 155 ARG 155 152 152 ARG ARG C . n 
C 1 156 ARG 156 153 153 ARG ARG C . n 
C 1 157 LEU 157 154 154 LEU LEU C . n 
C 1 158 GLY 158 155 155 GLY GLY C . n 
C 1 159 ARG 159 156 156 ARG ARG C . n 
C 1 160 ARG 160 157 157 ARG ARG C . n 
C 1 161 LEU 161 158 158 LEU LEU C . n 
C 1 162 ALA 162 159 159 ALA ALA C . n 
C 1 163 GLU 163 160 160 GLU GLU C . n 
C 1 164 TRP 164 161 161 TRP TRP C . n 
C 1 165 VAL 165 162 162 VAL VAL C . n 
C 1 166 ALA 166 163 163 ALA ALA C . n 
C 1 167 ILE 167 164 164 ILE ILE C . n 
C 1 168 PHE 168 165 165 PHE PHE C . n 
C 1 169 VAL 169 166 166 VAL VAL C . n 
C 1 170 ASP 170 167 167 ASP ASP C . n 
C 1 171 GLY 171 168 168 GLY GLY C . n 
C 1 172 ARG 172 169 169 ARG ARG C . n 
C 1 173 LYS 173 170 170 LYS LYS C . n 
C 1 174 GLU 174 171 171 GLU GLU C . n 
C 1 175 LEU 175 172 172 LEU LEU C . n 
C 1 176 LEU 176 173 173 LEU LEU C . n 
C 1 177 GLU 177 174 174 GLU GLU C . n 
C 1 178 LYS 178 175 175 LYS LYS C . n 
C 1 179 ILE 179 176 176 ILE ILE C . n 
C 1 180 ARG 180 177 177 ARG ARG C . n 
C 1 181 LYS 181 178 178 LYS LYS C . n 
C 1 182 ASP 182 179 179 ASP ASP C . n 
C 1 183 PRO 183 180 180 PRO PRO C . n 
C 1 184 ALA 184 181 181 ALA ALA C . n 
C 1 185 ARG 185 182 182 ARG ARG C . n 
C 1 186 PHE 186 183 183 PHE PHE C . n 
C 1 187 VAL 187 184 184 VAL VAL C . n 
C 1 188 ASP 188 185 185 ASP ASP C . n 
D 1 1   SER 1   -2  -2  SER SER D . n 
D 1 2   ASN 2   -1  -1  ASN ASN D . n 
D 1 3   ALA 3   0   0   ALA ALA D . n 
D 1 4   MSE 4   1   1   MSE MSE D . n 
D 1 5   GLY 5   2   2   GLY GLY D . n 
D 1 6   LYS 6   3   3   LYS LYS D . n 
D 1 7   VAL 7   4   4   VAL VAL D . n 
D 1 8   LEU 8   5   5   LEU LEU D . n 
D 1 9   VAL 9   6   6   VAL VAL D . n 
D 1 10  ILE 10  7   7   ILE ILE D . n 
D 1 11  TYR 11  8   8   TYR TYR D . n 
D 1 12  ASP 12  9   9   ASP ASP D . n 
D 1 13  THR 13  10  10  THR THR D . n 
D 1 14  ARG 14  11  11  ARG ARG D . n 
D 1 15  THR 15  12  12  THR THR D . n 
D 1 16  GLY 16  13  13  GLY GLY D . n 
D 1 17  ASN 17  14  14  ASN ASN D . n 
D 1 18  THR 18  15  15  THR THR D . n 
D 1 19  LYS 19  16  16  LYS LYS D . n 
D 1 20  LYS 20  17  17  LYS LYS D . n 
D 1 21  MSE 21  18  18  MSE MSE D . n 
D 1 22  ALA 22  19  19  ALA ALA D . n 
D 1 23  GLU 23  20  20  GLU GLU D . n 
D 1 24  LEU 24  21  21  LEU LEU D . n 
D 1 25  VAL 25  22  22  VAL VAL D . n 
D 1 26  ALA 26  23  23  ALA ALA D . n 
D 1 27  GLU 27  24  24  GLU GLU D . n 
D 1 28  GLY 28  25  25  GLY GLY D . n 
D 1 29  ALA 29  26  26  ALA ALA D . n 
D 1 30  ARG 30  27  27  ARG ARG D . n 
D 1 31  SER 31  28  28  SER SER D . n 
D 1 32  LEU 32  29  29  LEU LEU D . n 
D 1 33  GLU 33  30  30  GLU GLU D . n 
D 1 34  GLY 34  31  31  GLY GLY D . n 
D 1 35  THR 35  32  32  THR THR D . n 
D 1 36  GLU 36  33  33  GLU GLU D . n 
D 1 37  VAL 37  34  34  VAL VAL D . n 
D 1 38  ARG 38  35  35  ARG ARG D . n 
D 1 39  LEU 39  36  36  LEU LEU D . n 
D 1 40  LYS 40  37  37  LYS LYS D . n 
D 1 41  HIS 41  38  38  HIS HIS D . n 
D 1 42  VAL 42  39  39  VAL VAL D . n 
D 1 43  ASP 43  40  40  ASP ASP D . n 
D 1 44  GLU 44  41  41  GLU GLU D . n 
D 1 45  ALA 45  42  42  ALA ALA D . n 
D 1 46  THR 46  43  43  THR THR D . n 
D 1 47  LYS 47  44  44  LYS LYS D . n 
D 1 48  GLU 48  45  45  GLU GLU D . n 
D 1 49  ASP 49  46  46  ASP ASP D . n 
D 1 50  VAL 50  47  47  VAL VAL D . n 
D 1 51  LEU 51  48  48  LEU LEU D . n 
D 1 52  TRP 52  49  49  TRP TRP D . n 
D 1 53  ALA 53  50  50  ALA ALA D . n 
D 1 54  ASP 54  51  51  ASP ASP D . n 
D 1 55  GLY 55  52  52  GLY GLY D . n 
D 1 56  LEU 56  53  53  LEU LEU D . n 
D 1 57  ALA 57  54  54  ALA ALA D . n 
D 1 58  VAL 58  55  55  VAL VAL D . n 
D 1 59  GLY 59  56  56  GLY GLY D . n 
D 1 60  SER 60  57  57  SER SER D . n 
D 1 61  PRO 61  58  58  PRO PRO D . n 
D 1 62  THR 62  59  59  THR THR D . n 
D 1 63  ASN 63  60  60  ASN ASN D . n 
D 1 64  MSE 64  61  61  MSE MSE D . n 
D 1 65  GLY 65  62  62  GLY GLY D . n 
D 1 66  LEU 66  63  63  LEU LEU D . n 
D 1 67  VAL 67  64  64  VAL VAL D . n 
D 1 68  SER 68  65  65  SER SER D . n 
D 1 69  TRP 69  66  66  TRP TRP D . n 
D 1 70  LYS 70  67  67  LYS LYS D . n 
D 1 71  MSE 71  68  68  MSE MSE D . n 
D 1 72  LYS 72  69  69  LYS LYS D . n 
D 1 73  ARG 73  70  70  ARG ARG D . n 
D 1 74  PHE 74  71  71  PHE PHE D . n 
D 1 75  PHE 75  72  72  PHE PHE D . n 
D 1 76  ASP 76  73  73  ASP ASP D . n 
D 1 77  ASP 77  74  74  ASP ASP D . n 
D 1 78  VAL 78  75  75  VAL VAL D . n 
D 1 79  LEU 79  76  76  LEU LEU D . n 
D 1 80  GLY 80  77  77  GLY GLY D . n 
D 1 81  ASP 81  78  78  ASP ASP D . n 
D 1 82  LEU 82  79  79  LEU LEU D . n 
D 1 83  TRP 83  80  80  TRP TRP D . n 
D 1 84  GLY 84  81  81  GLY GLY D . n 
D 1 85  GLU 85  82  82  GLU GLU D . n 
D 1 86  ILE 86  83  83  ILE ILE D . n 
D 1 87  ASP 87  84  84  ASP ASP D . n 
D 1 88  GLY 88  85  85  GLY GLY D . n 
D 1 89  LYS 89  86  86  LYS LYS D . n 
D 1 90  ILE 90  87  87  ILE ILE D . n 
D 1 91  ALA 91  88  88  ALA ALA D . n 
D 1 92  CYS 92  89  89  CYS CYS D . n 
D 1 93  ALA 93  90  90  ALA ALA D . n 
D 1 94  PHE 94  91  91  PHE PHE D . n 
D 1 95  SER 95  92  92  SER SER D . n 
D 1 96  SER 96  93  93  SER SER D . n 
D 1 97  SER 97  94  94  SER SER D . n 
D 1 98  GLY 98  95  95  GLY GLY D . n 
D 1 99  GLY 99  96  96  GLY GLY D . n 
D 1 100 TRP 100 97  97  TRP TRP D . n 
D 1 101 GLY 101 98  98  GLY GLY D . n 
D 1 102 GLY 102 99  99  GLY GLY D . n 
D 1 103 GLY 103 100 100 GLY GLY D . n 
D 1 104 ASN 104 101 101 ASN ASN D . n 
D 1 105 GLU 105 102 102 GLU GLU D . n 
D 1 106 VAL 106 103 103 VAL VAL D . n 
D 1 107 ALA 107 104 104 ALA ALA D . n 
D 1 108 CYS 108 105 105 CYS CYS D . n 
D 1 109 MSE 109 106 106 MSE MSE D . n 
D 1 110 SER 110 107 107 SER SER D . n 
D 1 111 ILE 111 108 108 ILE ILE D . n 
D 1 112 LEU 112 109 109 LEU LEU D . n 
D 1 113 THR 113 110 110 THR THR D . n 
D 1 114 MSE 114 111 111 MSE MSE D . n 
D 1 115 LEU 115 112 112 LEU LEU D . n 
D 1 116 MSE 116 113 113 MSE MSE D . n 
D 1 117 ASN 117 114 114 ASN ASN D . n 
D 1 118 PHE 118 115 115 PHE PHE D . n 
D 1 119 GLY 119 116 116 GLY GLY D . n 
D 1 120 PHE 120 117 117 PHE PHE D . n 
D 1 121 LEU 121 118 118 LEU LEU D . n 
D 1 122 VAL 122 119 119 VAL VAL D . n 
D 1 123 PHE 123 120 120 PHE PHE D . n 
D 1 124 GLY 124 121 121 GLY GLY D . n 
D 1 125 VAL 125 122 122 VAL VAL D . n 
D 1 126 THR 126 123 123 THR THR D . n 
D 1 127 ASP 127 124 124 ASP ASP D . n 
D 1 128 TYR 128 125 125 TYR TYR D . n 
D 1 129 VAL 129 126 126 VAL VAL D . n 
D 1 130 GLY 130 127 127 GLY GLY D . n 
D 1 131 LYS 131 128 128 LYS LYS D . n 
D 1 132 LYS 132 129 129 LYS LYS D . n 
D 1 133 PHE 133 130 130 PHE PHE D . n 
D 1 134 THR 134 131 131 THR THR D . n 
D 1 135 LEU 135 132 132 LEU LEU D . n 
D 1 136 HIS 136 133 133 HIS HIS D . n 
D 1 137 TYR 137 134 134 TYR TYR D . n 
D 1 138 GLY 138 135 135 GLY GLY D . n 
D 1 139 ALA 139 136 136 ALA ALA D . n 
D 1 140 VAL 140 137 137 VAL VAL D . n 
D 1 141 VAL 141 138 138 VAL VAL D . n 
D 1 142 ALA 142 139 139 ALA ALA D . n 
D 1 143 GLY 143 140 140 GLY GLY D . n 
D 1 144 GLU 144 141 141 GLU GLU D . n 
D 1 145 PRO 145 142 142 PRO PRO D . n 
D 1 146 ARG 146 143 143 ARG ARG D . n 
D 1 147 SER 147 144 144 SER SER D . n 
D 1 148 GLU 148 145 145 GLU GLU D . n 
D 1 149 GLU 149 146 146 GLU GLU D . n 
D 1 150 GLU 150 147 147 GLU GLU D . n 
D 1 151 LYS 151 148 148 LYS LYS D . n 
D 1 152 GLU 152 149 149 GLU GLU D . n 
D 1 153 ALA 153 150 150 ALA ALA D . n 
D 1 154 CYS 154 151 151 CYS CYS D . n 
D 1 155 ARG 155 152 152 ARG ARG D . n 
D 1 156 ARG 156 153 153 ARG ARG D . n 
D 1 157 LEU 157 154 154 LEU LEU D . n 
D 1 158 GLY 158 155 155 GLY GLY D . n 
D 1 159 ARG 159 156 156 ARG ARG D . n 
D 1 160 ARG 160 157 157 ARG ARG D . n 
D 1 161 LEU 161 158 158 LEU LEU D . n 
D 1 162 ALA 162 159 159 ALA ALA D . n 
D 1 163 GLU 163 160 160 GLU GLU D . n 
D 1 164 TRP 164 161 161 TRP TRP D . n 
D 1 165 VAL 165 162 162 VAL VAL D . n 
D 1 166 ALA 166 163 163 ALA ALA D . n 
D 1 167 ILE 167 164 164 ILE ILE D . n 
D 1 168 PHE 168 165 165 PHE PHE D . n 
D 1 169 VAL 169 166 166 VAL VAL D . n 
D 1 170 ASP 170 167 167 ASP ASP D . n 
D 1 171 GLY 171 168 168 GLY GLY D . n 
D 1 172 ARG 172 169 169 ARG ARG D . n 
D 1 173 LYS 173 170 170 LYS LYS D . n 
D 1 174 GLU 174 171 171 GLU GLU D . n 
D 1 175 LEU 175 172 172 LEU LEU D . n 
D 1 176 LEU 176 173 173 LEU LEU D . n 
D 1 177 GLU 177 174 174 GLU GLU D . n 
D 1 178 LYS 178 175 175 LYS LYS D . n 
D 1 179 ILE 179 176 176 ILE ILE D . n 
D 1 180 ARG 180 177 177 ARG ARG D . n 
D 1 181 LYS 181 178 178 LYS LYS D . n 
D 1 182 ASP 182 179 179 ASP ASP D . n 
D 1 183 PRO 183 180 180 PRO PRO D . n 
D 1 184 ALA 184 181 181 ALA ALA D . n 
D 1 185 ARG 185 182 182 ARG ARG D . n 
D 1 186 PHE 186 183 183 PHE PHE D . n 
D 1 187 VAL 187 184 184 VAL VAL D . n 
D 1 188 ASP 188 185 ?   ?   ?   D . n 
E 1 1   SER 1   -2  ?   ?   ?   E . n 
E 1 2   ASN 2   -1  ?   ?   ?   E . n 
E 1 3   ALA 3   0   ?   ?   ?   E . n 
E 1 4   MSE 4   1   1   MSE MSE E . n 
E 1 5   GLY 5   2   2   GLY GLY E . n 
E 1 6   LYS 6   3   3   LYS LYS E . n 
E 1 7   VAL 7   4   4   VAL VAL E . n 
E 1 8   LEU 8   5   5   LEU LEU E . n 
E 1 9   VAL 9   6   6   VAL VAL E . n 
E 1 10  ILE 10  7   7   ILE ILE E . n 
E 1 11  TYR 11  8   8   TYR TYR E . n 
E 1 12  ASP 12  9   9   ASP ASP E . n 
E 1 13  THR 13  10  10  THR THR E . n 
E 1 14  ARG 14  11  11  ARG ARG E . n 
E 1 15  THR 15  12  12  THR THR E . n 
E 1 16  GLY 16  13  13  GLY GLY E . n 
E 1 17  ASN 17  14  14  ASN ASN E . n 
E 1 18  THR 18  15  15  THR THR E . n 
E 1 19  LYS 19  16  16  LYS LYS E . n 
E 1 20  LYS 20  17  17  LYS LYS E . n 
E 1 21  MSE 21  18  18  MSE MSE E . n 
E 1 22  ALA 22  19  19  ALA ALA E . n 
E 1 23  GLU 23  20  20  GLU GLU E . n 
E 1 24  LEU 24  21  21  LEU LEU E . n 
E 1 25  VAL 25  22  22  VAL VAL E . n 
E 1 26  ALA 26  23  23  ALA ALA E . n 
E 1 27  GLU 27  24  24  GLU GLU E . n 
E 1 28  GLY 28  25  25  GLY GLY E . n 
E 1 29  ALA 29  26  26  ALA ALA E . n 
E 1 30  ARG 30  27  27  ARG ARG E . n 
E 1 31  SER 31  28  28  SER SER E . n 
E 1 32  LEU 32  29  29  LEU LEU E . n 
E 1 33  GLU 33  30  30  GLU GLU E . n 
E 1 34  GLY 34  31  31  GLY GLY E . n 
E 1 35  THR 35  32  32  THR THR E . n 
E 1 36  GLU 36  33  33  GLU GLU E . n 
E 1 37  VAL 37  34  34  VAL VAL E . n 
E 1 38  ARG 38  35  35  ARG ARG E . n 
E 1 39  LEU 39  36  36  LEU LEU E . n 
E 1 40  LYS 40  37  37  LYS LYS E . n 
E 1 41  HIS 41  38  38  HIS HIS E . n 
E 1 42  VAL 42  39  39  VAL VAL E . n 
E 1 43  ASP 43  40  40  ASP ASP E . n 
E 1 44  GLU 44  41  41  GLU GLU E . n 
E 1 45  ALA 45  42  42  ALA ALA E . n 
E 1 46  THR 46  43  43  THR THR E . n 
E 1 47  LYS 47  44  44  LYS LYS E . n 
E 1 48  GLU 48  45  45  GLU GLU E . n 
E 1 49  ASP 49  46  46  ASP ASP E . n 
E 1 50  VAL 50  47  47  VAL VAL E . n 
E 1 51  LEU 51  48  48  LEU LEU E . n 
E 1 52  TRP 52  49  49  TRP TRP E . n 
E 1 53  ALA 53  50  50  ALA ALA E . n 
E 1 54  ASP 54  51  51  ASP ASP E . n 
E 1 55  GLY 55  52  52  GLY GLY E . n 
E 1 56  LEU 56  53  53  LEU LEU E . n 
E 1 57  ALA 57  54  54  ALA ALA E . n 
E 1 58  VAL 58  55  55  VAL VAL E . n 
E 1 59  GLY 59  56  56  GLY GLY E . n 
E 1 60  SER 60  57  57  SER SER E . n 
E 1 61  PRO 61  58  58  PRO PRO E . n 
E 1 62  THR 62  59  59  THR THR E . n 
E 1 63  ASN 63  60  60  ASN ASN E . n 
E 1 64  MSE 64  61  61  MSE MSE E . n 
E 1 65  GLY 65  62  62  GLY GLY E . n 
E 1 66  LEU 66  63  63  LEU LEU E . n 
E 1 67  VAL 67  64  64  VAL VAL E . n 
E 1 68  SER 68  65  65  SER SER E . n 
E 1 69  TRP 69  66  66  TRP TRP E . n 
E 1 70  LYS 70  67  67  LYS LYS E . n 
E 1 71  MSE 71  68  68  MSE MSE E . n 
E 1 72  LYS 72  69  69  LYS LYS E . n 
E 1 73  ARG 73  70  70  ARG ARG E . n 
E 1 74  PHE 74  71  71  PHE PHE E . n 
E 1 75  PHE 75  72  72  PHE PHE E . n 
E 1 76  ASP 76  73  73  ASP ASP E . n 
E 1 77  ASP 77  74  74  ASP ASP E . n 
E 1 78  VAL 78  75  75  VAL VAL E . n 
E 1 79  LEU 79  76  76  LEU LEU E . n 
E 1 80  GLY 80  77  77  GLY GLY E . n 
E 1 81  ASP 81  78  78  ASP ASP E . n 
E 1 82  LEU 82  79  79  LEU LEU E . n 
E 1 83  TRP 83  80  80  TRP TRP E . n 
E 1 84  GLY 84  81  81  GLY GLY E . n 
E 1 85  GLU 85  82  82  GLU GLU E . n 
E 1 86  ILE 86  83  83  ILE ILE E . n 
E 1 87  ASP 87  84  84  ASP ASP E . n 
E 1 88  GLY 88  85  85  GLY GLY E . n 
E 1 89  LYS 89  86  86  LYS LYS E . n 
E 1 90  ILE 90  87  87  ILE ILE E . n 
E 1 91  ALA 91  88  88  ALA ALA E . n 
E 1 92  CYS 92  89  89  CYS CYS E . n 
E 1 93  ALA 93  90  90  ALA ALA E . n 
E 1 94  PHE 94  91  91  PHE PHE E . n 
E 1 95  SER 95  92  92  SER SER E . n 
E 1 96  SER 96  93  93  SER SER E . n 
E 1 97  SER 97  94  94  SER SER E . n 
E 1 98  GLY 98  95  95  GLY GLY E . n 
E 1 99  GLY 99  96  96  GLY GLY E . n 
E 1 100 TRP 100 97  97  TRP TRP E . n 
E 1 101 GLY 101 98  98  GLY GLY E . n 
E 1 102 GLY 102 99  99  GLY GLY E . n 
E 1 103 GLY 103 100 100 GLY GLY E . n 
E 1 104 ASN 104 101 101 ASN ASN E . n 
E 1 105 GLU 105 102 102 GLU GLU E . n 
E 1 106 VAL 106 103 103 VAL VAL E . n 
E 1 107 ALA 107 104 104 ALA ALA E . n 
E 1 108 CYS 108 105 105 CYS CYS E . n 
E 1 109 MSE 109 106 106 MSE MSE E . n 
E 1 110 SER 110 107 107 SER SER E . n 
E 1 111 ILE 111 108 108 ILE ILE E . n 
E 1 112 LEU 112 109 109 LEU LEU E . n 
E 1 113 THR 113 110 110 THR THR E . n 
E 1 114 MSE 114 111 111 MSE MSE E . n 
E 1 115 LEU 115 112 112 LEU LEU E . n 
E 1 116 MSE 116 113 113 MSE MSE E . n 
E 1 117 ASN 117 114 114 ASN ASN E . n 
E 1 118 PHE 118 115 115 PHE PHE E . n 
E 1 119 GLY 119 116 116 GLY GLY E . n 
E 1 120 PHE 120 117 117 PHE PHE E . n 
E 1 121 LEU 121 118 118 LEU LEU E . n 
E 1 122 VAL 122 119 119 VAL VAL E . n 
E 1 123 PHE 123 120 120 PHE PHE E . n 
E 1 124 GLY 124 121 121 GLY GLY E . n 
E 1 125 VAL 125 122 122 VAL VAL E . n 
E 1 126 THR 126 123 123 THR THR E . n 
E 1 127 ASP 127 124 124 ASP ASP E . n 
E 1 128 TYR 128 125 125 TYR TYR E . n 
E 1 129 VAL 129 126 126 VAL VAL E . n 
E 1 130 GLY 130 127 127 GLY GLY E . n 
E 1 131 LYS 131 128 128 LYS LYS E . n 
E 1 132 LYS 132 129 129 LYS LYS E . n 
E 1 133 PHE 133 130 130 PHE PHE E . n 
E 1 134 THR 134 131 131 THR THR E . n 
E 1 135 LEU 135 132 132 LEU LEU E . n 
E 1 136 HIS 136 133 133 HIS HIS E . n 
E 1 137 TYR 137 134 134 TYR TYR E . n 
E 1 138 GLY 138 135 135 GLY GLY E . n 
E 1 139 ALA 139 136 136 ALA ALA E . n 
E 1 140 VAL 140 137 137 VAL VAL E . n 
E 1 141 VAL 141 138 138 VAL VAL E . n 
E 1 142 ALA 142 139 139 ALA ALA E . n 
E 1 143 GLY 143 140 140 GLY GLY E . n 
E 1 144 GLU 144 141 141 GLU GLU E . n 
E 1 145 PRO 145 142 142 PRO PRO E . n 
E 1 146 ARG 146 143 143 ARG ARG E . n 
E 1 147 SER 147 144 144 SER SER E . n 
E 1 148 GLU 148 145 145 GLU GLU E . n 
E 1 149 GLU 149 146 146 GLU GLU E . n 
E 1 150 GLU 150 147 147 GLU GLU E . n 
E 1 151 LYS 151 148 148 LYS LYS E . n 
E 1 152 GLU 152 149 149 GLU GLU E . n 
E 1 153 ALA 153 150 150 ALA ALA E . n 
E 1 154 CYS 154 151 151 CYS CYS E . n 
E 1 155 ARG 155 152 152 ARG ARG E . n 
E 1 156 ARG 156 153 153 ARG ARG E . n 
E 1 157 LEU 157 154 154 LEU LEU E . n 
E 1 158 GLY 158 155 155 GLY GLY E . n 
E 1 159 ARG 159 156 156 ARG ARG E . n 
E 1 160 ARG 160 157 157 ARG ARG E . n 
E 1 161 LEU 161 158 158 LEU LEU E . n 
E 1 162 ALA 162 159 159 ALA ALA E . n 
E 1 163 GLU 163 160 160 GLU GLU E . n 
E 1 164 TRP 164 161 161 TRP TRP E . n 
E 1 165 VAL 165 162 162 VAL VAL E . n 
E 1 166 ALA 166 163 163 ALA ALA E . n 
E 1 167 ILE 167 164 164 ILE ILE E . n 
E 1 168 PHE 168 165 165 PHE PHE E . n 
E 1 169 VAL 169 166 166 VAL VAL E . n 
E 1 170 ASP 170 167 167 ASP ASP E . n 
E 1 171 GLY 171 168 168 GLY GLY E . n 
E 1 172 ARG 172 169 169 ARG ARG E . n 
E 1 173 LYS 173 170 170 LYS LYS E . n 
E 1 174 GLU 174 171 171 GLU GLU E . n 
E 1 175 LEU 175 172 172 LEU LEU E . n 
E 1 176 LEU 176 173 173 LEU LEU E . n 
E 1 177 GLU 177 174 174 GLU GLU E . n 
E 1 178 LYS 178 175 175 LYS LYS E . n 
E 1 179 ILE 179 176 176 ILE ILE E . n 
E 1 180 ARG 180 177 177 ARG ARG E . n 
E 1 181 LYS 181 178 178 LYS LYS E . n 
E 1 182 ASP 182 179 179 ASP ASP E . n 
E 1 183 PRO 183 180 180 PRO PRO E . n 
E 1 184 ALA 184 181 181 ALA ALA E . n 
E 1 185 ARG 185 182 182 ARG ARG E . n 
E 1 186 PHE 186 183 183 PHE PHE E . n 
E 1 187 VAL 187 184 184 VAL VAL E . n 
E 1 188 ASP 188 185 185 ASP ASP E . n 
F 1 1   SER 1   -2  ?   ?   ?   F . n 
F 1 2   ASN 2   -1  ?   ?   ?   F . n 
F 1 3   ALA 3   0   0   ALA ALA F . n 
F 1 4   MSE 4   1   1   MSE MSE F . n 
F 1 5   GLY 5   2   2   GLY GLY F . n 
F 1 6   LYS 6   3   3   LYS LYS F . n 
F 1 7   VAL 7   4   4   VAL VAL F . n 
F 1 8   LEU 8   5   5   LEU LEU F . n 
F 1 9   VAL 9   6   6   VAL VAL F . n 
F 1 10  ILE 10  7   7   ILE ILE F . n 
F 1 11  TYR 11  8   8   TYR TYR F . n 
F 1 12  ASP 12  9   9   ASP ASP F . n 
F 1 13  THR 13  10  10  THR THR F . n 
F 1 14  ARG 14  11  11  ARG ARG F . n 
F 1 15  THR 15  12  12  THR THR F . n 
F 1 16  GLY 16  13  13  GLY GLY F . n 
F 1 17  ASN 17  14  14  ASN ASN F . n 
F 1 18  THR 18  15  15  THR THR F . n 
F 1 19  LYS 19  16  16  LYS LYS F . n 
F 1 20  LYS 20  17  17  LYS LYS F . n 
F 1 21  MSE 21  18  18  MSE MSE F . n 
F 1 22  ALA 22  19  19  ALA ALA F . n 
F 1 23  GLU 23  20  20  GLU GLU F . n 
F 1 24  LEU 24  21  21  LEU LEU F . n 
F 1 25  VAL 25  22  22  VAL VAL F . n 
F 1 26  ALA 26  23  23  ALA ALA F . n 
F 1 27  GLU 27  24  24  GLU GLU F . n 
F 1 28  GLY 28  25  25  GLY GLY F . n 
F 1 29  ALA 29  26  26  ALA ALA F . n 
F 1 30  ARG 30  27  27  ARG ARG F . n 
F 1 31  SER 31  28  28  SER SER F . n 
F 1 32  LEU 32  29  29  LEU LEU F . n 
F 1 33  GLU 33  30  30  GLU GLU F . n 
F 1 34  GLY 34  31  31  GLY GLY F . n 
F 1 35  THR 35  32  32  THR THR F . n 
F 1 36  GLU 36  33  33  GLU GLU F . n 
F 1 37  VAL 37  34  34  VAL VAL F . n 
F 1 38  ARG 38  35  35  ARG ARG F . n 
F 1 39  LEU 39  36  36  LEU LEU F . n 
F 1 40  LYS 40  37  37  LYS LYS F . n 
F 1 41  HIS 41  38  38  HIS HIS F . n 
F 1 42  VAL 42  39  39  VAL VAL F . n 
F 1 43  ASP 43  40  40  ASP ASP F . n 
F 1 44  GLU 44  41  41  GLU GLU F . n 
F 1 45  ALA 45  42  42  ALA ALA F . n 
F 1 46  THR 46  43  43  THR THR F . n 
F 1 47  LYS 47  44  44  LYS LYS F . n 
F 1 48  GLU 48  45  45  GLU GLU F . n 
F 1 49  ASP 49  46  46  ASP ASP F . n 
F 1 50  VAL 50  47  47  VAL VAL F . n 
F 1 51  LEU 51  48  48  LEU LEU F . n 
F 1 52  TRP 52  49  49  TRP TRP F . n 
F 1 53  ALA 53  50  50  ALA ALA F . n 
F 1 54  ASP 54  51  51  ASP ASP F . n 
F 1 55  GLY 55  52  52  GLY GLY F . n 
F 1 56  LEU 56  53  53  LEU LEU F . n 
F 1 57  ALA 57  54  54  ALA ALA F . n 
F 1 58  VAL 58  55  55  VAL VAL F . n 
F 1 59  GLY 59  56  56  GLY GLY F . n 
F 1 60  SER 60  57  57  SER SER F . n 
F 1 61  PRO 61  58  58  PRO PRO F . n 
F 1 62  THR 62  59  59  THR THR F . n 
F 1 63  ASN 63  60  60  ASN ASN F . n 
F 1 64  MSE 64  61  61  MSE MSE F . n 
F 1 65  GLY 65  62  62  GLY GLY F . n 
F 1 66  LEU 66  63  63  LEU LEU F . n 
F 1 67  VAL 67  64  64  VAL VAL F . n 
F 1 68  SER 68  65  65  SER SER F . n 
F 1 69  TRP 69  66  66  TRP TRP F . n 
F 1 70  LYS 70  67  67  LYS LYS F . n 
F 1 71  MSE 71  68  68  MSE MSE F . n 
F 1 72  LYS 72  69  69  LYS LYS F . n 
F 1 73  ARG 73  70  70  ARG ARG F . n 
F 1 74  PHE 74  71  71  PHE PHE F . n 
F 1 75  PHE 75  72  72  PHE PHE F . n 
F 1 76  ASP 76  73  73  ASP ASP F . n 
F 1 77  ASP 77  74  74  ASP ASP F . n 
F 1 78  VAL 78  75  75  VAL VAL F . n 
F 1 79  LEU 79  76  76  LEU LEU F . n 
F 1 80  GLY 80  77  77  GLY GLY F . n 
F 1 81  ASP 81  78  78  ASP ASP F . n 
F 1 82  LEU 82  79  79  LEU LEU F . n 
F 1 83  TRP 83  80  80  TRP TRP F . n 
F 1 84  GLY 84  81  81  GLY GLY F . n 
F 1 85  GLU 85  82  82  GLU GLU F . n 
F 1 86  ILE 86  83  83  ILE ILE F . n 
F 1 87  ASP 87  84  84  ASP ASP F . n 
F 1 88  GLY 88  85  85  GLY GLY F . n 
F 1 89  LYS 89  86  86  LYS LYS F . n 
F 1 90  ILE 90  87  87  ILE ILE F . n 
F 1 91  ALA 91  88  88  ALA ALA F . n 
F 1 92  CYS 92  89  89  CYS CYS F . n 
F 1 93  ALA 93  90  90  ALA ALA F . n 
F 1 94  PHE 94  91  91  PHE PHE F . n 
F 1 95  SER 95  92  92  SER SER F . n 
F 1 96  SER 96  93  93  SER SER F . n 
F 1 97  SER 97  94  94  SER SER F . n 
F 1 98  GLY 98  95  95  GLY GLY F . n 
F 1 99  GLY 99  96  96  GLY GLY F . n 
F 1 100 TRP 100 97  97  TRP TRP F . n 
F 1 101 GLY 101 98  98  GLY GLY F . n 
F 1 102 GLY 102 99  99  GLY GLY F . n 
F 1 103 GLY 103 100 100 GLY GLY F . n 
F 1 104 ASN 104 101 101 ASN ASN F . n 
F 1 105 GLU 105 102 102 GLU GLU F . n 
F 1 106 VAL 106 103 103 VAL VAL F . n 
F 1 107 ALA 107 104 104 ALA ALA F . n 
F 1 108 CYS 108 105 105 CYS CYS F . n 
F 1 109 MSE 109 106 106 MSE MSE F . n 
F 1 110 SER 110 107 107 SER SER F . n 
F 1 111 ILE 111 108 108 ILE ILE F . n 
F 1 112 LEU 112 109 109 LEU LEU F . n 
F 1 113 THR 113 110 110 THR THR F . n 
F 1 114 MSE 114 111 111 MSE MSE F . n 
F 1 115 LEU 115 112 112 LEU LEU F . n 
F 1 116 MSE 116 113 113 MSE MSE F . n 
F 1 117 ASN 117 114 114 ASN ASN F . n 
F 1 118 PHE 118 115 115 PHE PHE F . n 
F 1 119 GLY 119 116 116 GLY GLY F . n 
F 1 120 PHE 120 117 117 PHE PHE F . n 
F 1 121 LEU 121 118 118 LEU LEU F . n 
F 1 122 VAL 122 119 119 VAL VAL F . n 
F 1 123 PHE 123 120 120 PHE PHE F . n 
F 1 124 GLY 124 121 121 GLY GLY F . n 
F 1 125 VAL 125 122 122 VAL VAL F . n 
F 1 126 THR 126 123 123 THR THR F . n 
F 1 127 ASP 127 124 124 ASP ASP F . n 
F 1 128 TYR 128 125 125 TYR TYR F . n 
F 1 129 VAL 129 126 126 VAL VAL F . n 
F 1 130 GLY 130 127 127 GLY GLY F . n 
F 1 131 LYS 131 128 128 LYS LYS F . n 
F 1 132 LYS 132 129 129 LYS LYS F . n 
F 1 133 PHE 133 130 130 PHE PHE F . n 
F 1 134 THR 134 131 131 THR THR F . n 
F 1 135 LEU 135 132 132 LEU LEU F . n 
F 1 136 HIS 136 133 133 HIS HIS F . n 
F 1 137 TYR 137 134 134 TYR TYR F . n 
F 1 138 GLY 138 135 135 GLY GLY F . n 
F 1 139 ALA 139 136 136 ALA ALA F . n 
F 1 140 VAL 140 137 137 VAL VAL F . n 
F 1 141 VAL 141 138 138 VAL VAL F . n 
F 1 142 ALA 142 139 139 ALA ALA F . n 
F 1 143 GLY 143 140 140 GLY GLY F . n 
F 1 144 GLU 144 141 141 GLU GLU F . n 
F 1 145 PRO 145 142 142 PRO PRO F . n 
F 1 146 ARG 146 143 143 ARG ARG F . n 
F 1 147 SER 147 144 144 SER SER F . n 
F 1 148 GLU 148 145 145 GLU GLU F . n 
F 1 149 GLU 149 146 146 GLU GLU F . n 
F 1 150 GLU 150 147 147 GLU GLU F . n 
F 1 151 LYS 151 148 148 LYS LYS F . n 
F 1 152 GLU 152 149 149 GLU GLU F . n 
F 1 153 ALA 153 150 150 ALA ALA F . n 
F 1 154 CYS 154 151 151 CYS CYS F . n 
F 1 155 ARG 155 152 152 ARG ARG F . n 
F 1 156 ARG 156 153 153 ARG ARG F . n 
F 1 157 LEU 157 154 154 LEU LEU F . n 
F 1 158 GLY 158 155 155 GLY GLY F . n 
F 1 159 ARG 159 156 156 ARG ARG F . n 
F 1 160 ARG 160 157 157 ARG ARG F . n 
F 1 161 LEU 161 158 158 LEU LEU F . n 
F 1 162 ALA 162 159 159 ALA ALA F . n 
F 1 163 GLU 163 160 160 GLU GLU F . n 
F 1 164 TRP 164 161 161 TRP TRP F . n 
F 1 165 VAL 165 162 162 VAL VAL F . n 
F 1 166 ALA 166 163 163 ALA ALA F . n 
F 1 167 ILE 167 164 164 ILE ILE F . n 
F 1 168 PHE 168 165 165 PHE PHE F . n 
F 1 169 VAL 169 166 166 VAL VAL F . n 
F 1 170 ASP 170 167 167 ASP ASP F . n 
F 1 171 GLY 171 168 168 GLY GLY F . n 
F 1 172 ARG 172 169 169 ARG ARG F . n 
F 1 173 LYS 173 170 170 LYS LYS F . n 
F 1 174 GLU 174 171 171 GLU GLU F . n 
F 1 175 LEU 175 172 172 LEU LEU F . n 
F 1 176 LEU 176 173 173 LEU LEU F . n 
F 1 177 GLU 177 174 174 GLU GLU F . n 
F 1 178 LYS 178 175 175 LYS LYS F . n 
F 1 179 ILE 179 176 176 ILE ILE F . n 
F 1 180 ARG 180 177 177 ARG ARG F . n 
F 1 181 LYS 181 178 178 LYS LYS F . n 
F 1 182 ASP 182 179 179 ASP ASP F . n 
F 1 183 PRO 183 180 180 PRO PRO F . n 
F 1 184 ALA 184 181 181 ALA ALA F . n 
F 1 185 ARG 185 182 182 ARG ARG F . n 
F 1 186 PHE 186 183 183 PHE PHE F . n 
F 1 187 VAL 187 184 184 VAL VAL F . n 
F 1 188 ASP 188 185 ?   ?   ?   F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 2 PO4 1  501 1   PO4 PO4 A . 
H 3 GOL 1  509 3   GOL GOL A . 
I 3 GOL 1  512 6   GOL GOL A . 
J 2 PO4 1  502 2   PO4 PO4 B . 
K 3 GOL 1  510 4   GOL GOL B . 
L 2 PO4 1  503 3   PO4 PO4 C . 
M 3 GOL 1  508 2   GOL GOL C . 
N 3 GOL 1  511 5   GOL GOL C . 
O 2 PO4 1  504 4   PO4 PO4 D . 
P 3 GOL 1  507 1   GOL GOL D . 
Q 2 PO4 1  505 5   PO4 PO4 E . 
R 2 PO4 1  506 6   PO4 PO4 F . 
S 4 HOH 1  513 1   HOH HOH A . 
S 4 HOH 2  514 2   HOH HOH A . 
S 4 HOH 3  515 3   HOH HOH A . 
S 4 HOH 4  516 5   HOH HOH A . 
S 4 HOH 5  517 13  HOH HOH A . 
S 4 HOH 6  518 22  HOH HOH A . 
S 4 HOH 7  519 25  HOH HOH A . 
S 4 HOH 8  520 26  HOH HOH A . 
S 4 HOH 9  521 28  HOH HOH A . 
S 4 HOH 10 522 36  HOH HOH A . 
S 4 HOH 11 523 43  HOH HOH A . 
S 4 HOH 12 524 53  HOH HOH A . 
S 4 HOH 13 525 54  HOH HOH A . 
S 4 HOH 14 526 57  HOH HOH A . 
S 4 HOH 15 527 60  HOH HOH A . 
S 4 HOH 16 528 66  HOH HOH A . 
S 4 HOH 17 529 74  HOH HOH A . 
S 4 HOH 18 530 75  HOH HOH A . 
S 4 HOH 19 531 83  HOH HOH A . 
S 4 HOH 20 532 84  HOH HOH A . 
S 4 HOH 21 533 88  HOH HOH A . 
S 4 HOH 22 534 92  HOH HOH A . 
S 4 HOH 23 535 95  HOH HOH A . 
S 4 HOH 24 536 97  HOH HOH A . 
S 4 HOH 25 537 108 HOH HOH A . 
S 4 HOH 26 538 109 HOH HOH A . 
S 4 HOH 27 539 120 HOH HOH A . 
S 4 HOH 28 540 129 HOH HOH A . 
S 4 HOH 29 541 133 HOH HOH A . 
S 4 HOH 30 542 135 HOH HOH A . 
S 4 HOH 31 543 141 HOH HOH A . 
S 4 HOH 32 544 142 HOH HOH A . 
S 4 HOH 33 545 144 HOH HOH A . 
S 4 HOH 34 546 147 HOH HOH A . 
S 4 HOH 35 547 155 HOH HOH A . 
S 4 HOH 36 548 173 HOH HOH A . 
S 4 HOH 37 549 176 HOH HOH A . 
S 4 HOH 38 550 180 HOH HOH A . 
S 4 HOH 39 551 186 HOH HOH A . 
S 4 HOH 40 552 191 HOH HOH A . 
S 4 HOH 41 553 195 HOH HOH A . 
S 4 HOH 42 554 209 HOH HOH A . 
S 4 HOH 43 555 210 HOH HOH A . 
S 4 HOH 44 556 213 HOH HOH A . 
S 4 HOH 45 557 253 HOH HOH A . 
S 4 HOH 46 558 262 HOH HOH A . 
S 4 HOH 47 559 271 HOH HOH A . 
S 4 HOH 48 560 274 HOH HOH A . 
S 4 HOH 49 561 277 HOH HOH A . 
S 4 HOH 50 562 291 HOH HOH A . 
S 4 HOH 51 563 298 HOH HOH A . 
S 4 HOH 52 564 299 HOH HOH A . 
S 4 HOH 53 565 300 HOH HOH A . 
S 4 HOH 54 566 324 HOH HOH A . 
S 4 HOH 55 567 344 HOH HOH A . 
S 4 HOH 56 568 347 HOH HOH A . 
S 4 HOH 57 569 353 HOH HOH A . 
S 4 HOH 58 570 359 HOH HOH A . 
S 4 HOH 59 571 363 HOH HOH A . 
S 4 HOH 60 572 369 HOH HOH A . 
S 4 HOH 61 573 372 HOH HOH A . 
S 4 HOH 62 574 376 HOH HOH A . 
S 4 HOH 63 575 388 HOH HOH A . 
S 4 HOH 64 576 392 HOH HOH A . 
S 4 HOH 65 577 401 HOH HOH A . 
S 4 HOH 66 578 405 HOH HOH A . 
S 4 HOH 67 579 409 HOH HOH A . 
S 4 HOH 68 580 412 HOH HOH A . 
S 4 HOH 69 581 413 HOH HOH A . 
T 4 HOH 1  511 7   HOH HOH B . 
T 4 HOH 2  512 8   HOH HOH B . 
T 4 HOH 3  513 11  HOH HOH B . 
T 4 HOH 4  514 15  HOH HOH B . 
T 4 HOH 5  515 21  HOH HOH B . 
T 4 HOH 6  516 30  HOH HOH B . 
T 4 HOH 7  517 38  HOH HOH B . 
T 4 HOH 8  518 42  HOH HOH B . 
T 4 HOH 9  519 44  HOH HOH B . 
T 4 HOH 10 520 45  HOH HOH B . 
T 4 HOH 11 521 49  HOH HOH B . 
T 4 HOH 12 522 55  HOH HOH B . 
T 4 HOH 13 523 56  HOH HOH B . 
T 4 HOH 14 524 69  HOH HOH B . 
T 4 HOH 15 525 70  HOH HOH B . 
T 4 HOH 16 526 103 HOH HOH B . 
T 4 HOH 17 527 104 HOH HOH B . 
T 4 HOH 18 528 106 HOH HOH B . 
T 4 HOH 19 529 117 HOH HOH B . 
T 4 HOH 20 530 119 HOH HOH B . 
T 4 HOH 21 531 121 HOH HOH B . 
T 4 HOH 22 532 127 HOH HOH B . 
T 4 HOH 23 533 136 HOH HOH B . 
T 4 HOH 24 534 139 HOH HOH B . 
T 4 HOH 25 535 148 HOH HOH B . 
T 4 HOH 26 536 150 HOH HOH B . 
T 4 HOH 27 537 152 HOH HOH B . 
T 4 HOH 28 538 159 HOH HOH B . 
T 4 HOH 29 539 161 HOH HOH B . 
T 4 HOH 30 540 164 HOH HOH B . 
T 4 HOH 31 541 168 HOH HOH B . 
T 4 HOH 32 542 172 HOH HOH B . 
T 4 HOH 33 543 177 HOH HOH B . 
T 4 HOH 34 544 179 HOH HOH B . 
T 4 HOH 35 545 181 HOH HOH B . 
T 4 HOH 36 546 182 HOH HOH B . 
T 4 HOH 37 547 185 HOH HOH B . 
T 4 HOH 38 548 187 HOH HOH B . 
T 4 HOH 39 549 190 HOH HOH B . 
T 4 HOH 40 550 193 HOH HOH B . 
T 4 HOH 41 551 204 HOH HOH B . 
T 4 HOH 42 552 223 HOH HOH B . 
T 4 HOH 43 553 228 HOH HOH B . 
T 4 HOH 44 554 229 HOH HOH B . 
T 4 HOH 45 555 236 HOH HOH B . 
T 4 HOH 46 556 254 HOH HOH B . 
T 4 HOH 47 557 256 HOH HOH B . 
T 4 HOH 48 558 257 HOH HOH B . 
T 4 HOH 49 559 259 HOH HOH B . 
T 4 HOH 50 560 260 HOH HOH B . 
T 4 HOH 51 561 261 HOH HOH B . 
T 4 HOH 52 562 266 HOH HOH B . 
T 4 HOH 53 563 268 HOH HOH B . 
T 4 HOH 54 564 272 HOH HOH B . 
T 4 HOH 55 565 278 HOH HOH B . 
T 4 HOH 56 566 285 HOH HOH B . 
T 4 HOH 57 567 286 HOH HOH B . 
T 4 HOH 58 568 287 HOH HOH B . 
T 4 HOH 59 569 292 HOH HOH B . 
T 4 HOH 60 570 297 HOH HOH B . 
T 4 HOH 61 571 307 HOH HOH B . 
T 4 HOH 62 572 309 HOH HOH B . 
T 4 HOH 63 573 310 HOH HOH B . 
T 4 HOH 64 574 312 HOH HOH B . 
T 4 HOH 65 575 313 HOH HOH B . 
T 4 HOH 66 576 315 HOH HOH B . 
T 4 HOH 67 577 316 HOH HOH B . 
T 4 HOH 68 578 318 HOH HOH B . 
T 4 HOH 69 579 320 HOH HOH B . 
T 4 HOH 70 580 321 HOH HOH B . 
T 4 HOH 71 581 322 HOH HOH B . 
T 4 HOH 72 582 327 HOH HOH B . 
T 4 HOH 73 583 328 HOH HOH B . 
T 4 HOH 74 584 330 HOH HOH B . 
T 4 HOH 75 585 331 HOH HOH B . 
T 4 HOH 76 586 332 HOH HOH B . 
T 4 HOH 77 587 336 HOH HOH B . 
T 4 HOH 78 588 338 HOH HOH B . 
T 4 HOH 79 589 342 HOH HOH B . 
T 4 HOH 80 590 343 HOH HOH B . 
T 4 HOH 81 591 348 HOH HOH B . 
T 4 HOH 82 592 351 HOH HOH B . 
T 4 HOH 83 593 354 HOH HOH B . 
T 4 HOH 84 594 355 HOH HOH B . 
T 4 HOH 85 595 362 HOH HOH B . 
T 4 HOH 86 596 366 HOH HOH B . 
T 4 HOH 87 597 370 HOH HOH B . 
T 4 HOH 88 598 379 HOH HOH B . 
T 4 HOH 89 599 382 HOH HOH B . 
T 4 HOH 90 600 389 HOH HOH B . 
T 4 HOH 91 601 394 HOH HOH B . 
T 4 HOH 92 602 399 HOH HOH B . 
T 4 HOH 93 603 403 HOH HOH B . 
T 4 HOH 94 604 404 HOH HOH B . 
T 4 HOH 95 605 407 HOH HOH B . 
U 4 HOH 1  512 16  HOH HOH C . 
U 4 HOH 2  513 18  HOH HOH C . 
U 4 HOH 3  514 24  HOH HOH C . 
U 4 HOH 4  515 32  HOH HOH C . 
U 4 HOH 5  516 34  HOH HOH C . 
U 4 HOH 6  517 37  HOH HOH C . 
U 4 HOH 7  518 40  HOH HOH C . 
U 4 HOH 8  519 46  HOH HOH C . 
U 4 HOH 9  520 48  HOH HOH C . 
U 4 HOH 10 521 52  HOH HOH C . 
U 4 HOH 11 522 62  HOH HOH C . 
U 4 HOH 12 523 63  HOH HOH C . 
U 4 HOH 13 524 65  HOH HOH C . 
U 4 HOH 14 525 72  HOH HOH C . 
U 4 HOH 15 526 76  HOH HOH C . 
U 4 HOH 16 527 80  HOH HOH C . 
U 4 HOH 17 528 87  HOH HOH C . 
U 4 HOH 18 529 89  HOH HOH C . 
U 4 HOH 19 530 91  HOH HOH C . 
U 4 HOH 20 531 102 HOH HOH C . 
U 4 HOH 21 532 105 HOH HOH C . 
U 4 HOH 22 533 107 HOH HOH C . 
U 4 HOH 23 534 112 HOH HOH C . 
U 4 HOH 24 535 114 HOH HOH C . 
U 4 HOH 25 536 115 HOH HOH C . 
U 4 HOH 26 537 122 HOH HOH C . 
U 4 HOH 27 538 125 HOH HOH C . 
U 4 HOH 28 539 126 HOH HOH C . 
U 4 HOH 29 540 140 HOH HOH C . 
U 4 HOH 30 541 143 HOH HOH C . 
U 4 HOH 31 542 153 HOH HOH C . 
U 4 HOH 32 543 166 HOH HOH C . 
U 4 HOH 33 544 167 HOH HOH C . 
U 4 HOH 34 545 175 HOH HOH C . 
U 4 HOH 35 546 194 HOH HOH C . 
U 4 HOH 36 547 196 HOH HOH C . 
U 4 HOH 37 548 202 HOH HOH C . 
U 4 HOH 38 549 205 HOH HOH C . 
U 4 HOH 39 550 224 HOH HOH C . 
U 4 HOH 40 551 225 HOH HOH C . 
U 4 HOH 41 552 241 HOH HOH C . 
U 4 HOH 42 553 243 HOH HOH C . 
U 4 HOH 43 554 244 HOH HOH C . 
U 4 HOH 44 555 246 HOH HOH C . 
U 4 HOH 45 556 250 HOH HOH C . 
U 4 HOH 46 557 255 HOH HOH C . 
U 4 HOH 47 558 306 HOH HOH C . 
U 4 HOH 48 559 325 HOH HOH C . 
U 4 HOH 49 560 335 HOH HOH C . 
U 4 HOH 50 561 383 HOH HOH C . 
U 4 HOH 51 562 397 HOH HOH C . 
U 4 HOH 52 563 402 HOH HOH C . 
U 4 HOH 53 564 411 HOH HOH C . 
U 4 HOH 54 565 414 HOH HOH C . 
U 4 HOH 55 566 417 HOH HOH C . 
V 4 HOH 1  508 9   HOH HOH D . 
V 4 HOH 2  509 12  HOH HOH D . 
V 4 HOH 3  510 14  HOH HOH D . 
V 4 HOH 4  511 20  HOH HOH D . 
V 4 HOH 5  512 39  HOH HOH D . 
V 4 HOH 6  513 41  HOH HOH D . 
V 4 HOH 7  514 58  HOH HOH D . 
V 4 HOH 8  515 68  HOH HOH D . 
V 4 HOH 9  516 73  HOH HOH D . 
V 4 HOH 10 517 93  HOH HOH D . 
V 4 HOH 11 518 96  HOH HOH D . 
V 4 HOH 12 519 99  HOH HOH D . 
V 4 HOH 13 520 110 HOH HOH D . 
V 4 HOH 14 521 118 HOH HOH D . 
V 4 HOH 15 522 124 HOH HOH D . 
V 4 HOH 16 523 128 HOH HOH D . 
V 4 HOH 17 524 130 HOH HOH D . 
V 4 HOH 18 525 131 HOH HOH D . 
V 4 HOH 19 526 132 HOH HOH D . 
V 4 HOH 20 527 134 HOH HOH D . 
V 4 HOH 21 528 137 HOH HOH D . 
V 4 HOH 22 529 138 HOH HOH D . 
V 4 HOH 23 530 145 HOH HOH D . 
V 4 HOH 24 531 157 HOH HOH D . 
V 4 HOH 25 532 171 HOH HOH D . 
V 4 HOH 26 533 178 HOH HOH D . 
V 4 HOH 27 534 183 HOH HOH D . 
V 4 HOH 28 535 188 HOH HOH D . 
V 4 HOH 29 536 189 HOH HOH D . 
V 4 HOH 30 537 192 HOH HOH D . 
V 4 HOH 31 538 200 HOH HOH D . 
V 4 HOH 32 539 203 HOH HOH D . 
V 4 HOH 33 540 206 HOH HOH D . 
V 4 HOH 34 541 220 HOH HOH D . 
V 4 HOH 35 542 222 HOH HOH D . 
V 4 HOH 36 543 230 HOH HOH D . 
V 4 HOH 37 544 232 HOH HOH D . 
V 4 HOH 38 545 233 HOH HOH D . 
V 4 HOH 39 546 235 HOH HOH D . 
V 4 HOH 40 547 237 HOH HOH D . 
V 4 HOH 41 548 238 HOH HOH D . 
V 4 HOH 42 549 239 HOH HOH D . 
V 4 HOH 43 550 245 HOH HOH D . 
V 4 HOH 44 551 247 HOH HOH D . 
V 4 HOH 45 552 248 HOH HOH D . 
V 4 HOH 46 553 249 HOH HOH D . 
V 4 HOH 47 554 258 HOH HOH D . 
V 4 HOH 48 555 267 HOH HOH D . 
V 4 HOH 49 556 273 HOH HOH D . 
V 4 HOH 50 557 279 HOH HOH D . 
V 4 HOH 51 558 280 HOH HOH D . 
V 4 HOH 52 559 281 HOH HOH D . 
V 4 HOH 53 560 283 HOH HOH D . 
V 4 HOH 54 561 293 HOH HOH D . 
V 4 HOH 55 562 296 HOH HOH D . 
V 4 HOH 56 563 304 HOH HOH D . 
V 4 HOH 57 564 305 HOH HOH D . 
V 4 HOH 58 565 319 HOH HOH D . 
V 4 HOH 59 566 334 HOH HOH D . 
V 4 HOH 60 567 340 HOH HOH D . 
V 4 HOH 61 568 349 HOH HOH D . 
V 4 HOH 62 569 357 HOH HOH D . 
V 4 HOH 63 570 358 HOH HOH D . 
V 4 HOH 64 571 360 HOH HOH D . 
V 4 HOH 65 572 365 HOH HOH D . 
V 4 HOH 66 573 371 HOH HOH D . 
V 4 HOH 67 574 377 HOH HOH D . 
V 4 HOH 68 575 381 HOH HOH D . 
V 4 HOH 69 576 387 HOH HOH D . 
V 4 HOH 70 577 390 HOH HOH D . 
V 4 HOH 71 578 408 HOH HOH D . 
V 4 HOH 72 579 410 HOH HOH D . 
V 4 HOH 73 580 416 HOH HOH D . 
V 4 HOH 74 581 419 HOH HOH D . 
V 4 HOH 75 582 420 HOH HOH D . 
W 4 HOH 1  506 10  HOH HOH E . 
W 4 HOH 2  507 19  HOH HOH E . 
W 4 HOH 3  508 27  HOH HOH E . 
W 4 HOH 4  509 29  HOH HOH E . 
W 4 HOH 5  510 31  HOH HOH E . 
W 4 HOH 6  511 47  HOH HOH E . 
W 4 HOH 7  512 50  HOH HOH E . 
W 4 HOH 8  513 51  HOH HOH E . 
W 4 HOH 9  514 59  HOH HOH E . 
W 4 HOH 10 515 64  HOH HOH E . 
W 4 HOH 11 516 67  HOH HOH E . 
W 4 HOH 12 517 77  HOH HOH E . 
W 4 HOH 13 518 79  HOH HOH E . 
W 4 HOH 14 519 86  HOH HOH E . 
W 4 HOH 15 520 111 HOH HOH E . 
W 4 HOH 16 521 113 HOH HOH E . 
W 4 HOH 17 522 123 HOH HOH E . 
W 4 HOH 18 523 151 HOH HOH E . 
W 4 HOH 19 524 154 HOH HOH E . 
W 4 HOH 20 525 156 HOH HOH E . 
W 4 HOH 21 526 163 HOH HOH E . 
W 4 HOH 22 527 201 HOH HOH E . 
W 4 HOH 23 528 214 HOH HOH E . 
W 4 HOH 24 529 215 HOH HOH E . 
W 4 HOH 25 530 216 HOH HOH E . 
W 4 HOH 26 531 217 HOH HOH E . 
W 4 HOH 27 532 219 HOH HOH E . 
W 4 HOH 28 533 231 HOH HOH E . 
W 4 HOH 29 534 251 HOH HOH E . 
W 4 HOH 30 535 252 HOH HOH E . 
W 4 HOH 31 536 265 HOH HOH E . 
W 4 HOH 32 537 282 HOH HOH E . 
W 4 HOH 33 538 284 HOH HOH E . 
W 4 HOH 34 539 317 HOH HOH E . 
W 4 HOH 35 540 341 HOH HOH E . 
W 4 HOH 36 541 345 HOH HOH E . 
W 4 HOH 37 542 361 HOH HOH E . 
W 4 HOH 38 543 364 HOH HOH E . 
W 4 HOH 39 544 368 HOH HOH E . 
W 4 HOH 40 545 374 HOH HOH E . 
W 4 HOH 41 546 380 HOH HOH E . 
W 4 HOH 42 547 391 HOH HOH E . 
X 4 HOH 1  507 4   HOH HOH F . 
X 4 HOH 2  508 6   HOH HOH F . 
X 4 HOH 3  509 17  HOH HOH F . 
X 4 HOH 4  510 23  HOH HOH F . 
X 4 HOH 5  511 33  HOH HOH F . 
X 4 HOH 6  512 35  HOH HOH F . 
X 4 HOH 7  513 61  HOH HOH F . 
X 4 HOH 8  514 71  HOH HOH F . 
X 4 HOH 9  515 78  HOH HOH F . 
X 4 HOH 10 516 81  HOH HOH F . 
X 4 HOH 11 517 82  HOH HOH F . 
X 4 HOH 12 518 85  HOH HOH F . 
X 4 HOH 13 519 90  HOH HOH F . 
X 4 HOH 14 520 94  HOH HOH F . 
X 4 HOH 15 521 98  HOH HOH F . 
X 4 HOH 16 522 100 HOH HOH F . 
X 4 HOH 17 523 101 HOH HOH F . 
X 4 HOH 18 524 116 HOH HOH F . 
X 4 HOH 19 525 146 HOH HOH F . 
X 4 HOH 20 526 149 HOH HOH F . 
X 4 HOH 21 527 158 HOH HOH F . 
X 4 HOH 22 528 160 HOH HOH F . 
X 4 HOH 23 529 162 HOH HOH F . 
X 4 HOH 24 530 165 HOH HOH F . 
X 4 HOH 25 531 169 HOH HOH F . 
X 4 HOH 26 532 170 HOH HOH F . 
X 4 HOH 27 533 174 HOH HOH F . 
X 4 HOH 28 534 184 HOH HOH F . 
X 4 HOH 29 535 197 HOH HOH F . 
X 4 HOH 30 536 198 HOH HOH F . 
X 4 HOH 31 537 199 HOH HOH F . 
X 4 HOH 32 538 207 HOH HOH F . 
X 4 HOH 33 539 208 HOH HOH F . 
X 4 HOH 34 540 211 HOH HOH F . 
X 4 HOH 35 541 212 HOH HOH F . 
X 4 HOH 36 542 218 HOH HOH F . 
X 4 HOH 37 543 221 HOH HOH F . 
X 4 HOH 38 544 226 HOH HOH F . 
X 4 HOH 39 545 227 HOH HOH F . 
X 4 HOH 40 546 234 HOH HOH F . 
X 4 HOH 41 547 240 HOH HOH F . 
X 4 HOH 42 548 242 HOH HOH F . 
X 4 HOH 43 549 263 HOH HOH F . 
X 4 HOH 44 550 264 HOH HOH F . 
X 4 HOH 45 551 269 HOH HOH F . 
X 4 HOH 46 552 270 HOH HOH F . 
X 4 HOH 47 553 275 HOH HOH F . 
X 4 HOH 48 554 276 HOH HOH F . 
X 4 HOH 49 555 288 HOH HOH F . 
X 4 HOH 50 556 289 HOH HOH F . 
X 4 HOH 51 557 290 HOH HOH F . 
X 4 HOH 52 558 294 HOH HOH F . 
X 4 HOH 53 559 295 HOH HOH F . 
X 4 HOH 54 560 301 HOH HOH F . 
X 4 HOH 55 561 302 HOH HOH F . 
X 4 HOH 56 562 303 HOH HOH F . 
X 4 HOH 57 563 308 HOH HOH F . 
X 4 HOH 58 564 311 HOH HOH F . 
X 4 HOH 59 565 314 HOH HOH F . 
X 4 HOH 60 566 323 HOH HOH F . 
X 4 HOH 61 567 326 HOH HOH F . 
X 4 HOH 62 568 329 HOH HOH F . 
X 4 HOH 63 569 333 HOH HOH F . 
X 4 HOH 64 570 337 HOH HOH F . 
X 4 HOH 65 571 339 HOH HOH F . 
X 4 HOH 66 572 346 HOH HOH F . 
X 4 HOH 67 573 350 HOH HOH F . 
X 4 HOH 68 574 352 HOH HOH F . 
X 4 HOH 69 575 356 HOH HOH F . 
X 4 HOH 70 576 367 HOH HOH F . 
X 4 HOH 71 577 373 HOH HOH F . 
X 4 HOH 72 578 375 HOH HOH F . 
X 4 HOH 73 579 378 HOH HOH F . 
X 4 HOH 74 580 384 HOH HOH F . 
X 4 HOH 75 581 385 HOH HOH F . 
X 4 HOH 76 582 386 HOH HOH F . 
X 4 HOH 77 583 393 HOH HOH F . 
X 4 HOH 78 584 395 HOH HOH F . 
X 4 HOH 79 585 396 HOH HOH F . 
X 4 HOH 80 586 398 HOH HOH F . 
X 4 HOH 81 587 400 HOH HOH F . 
X 4 HOH 82 588 406 HOH HOH F . 
X 4 HOH 83 589 415 HOH HOH F . 
X 4 HOH 84 590 418 HOH HOH F . 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      refinement        5.2.0005 ? 1  
SBC-Collect 'data collection' .        ? 2  
HKL-2000    'data scaling'    .        ? 3  
HKL-3000    phasing           .        ? 4  
SHELX       phasing           .        ? 5  
RESOLVE     phasing           .        ? 6  
DM          phasing           .        ? 7  
Coot        'model building'  .        ? 8  
O           'model building'  .        ? 9  
ARP/wARP    'model building'  .        ? 10 
# 
_cell.entry_id           2ARK 
_cell.length_a           112.846 
_cell.length_b           112.846 
_cell.length_c           150.648 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              36 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2ARK 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
# 
_exptl.entry_id          2ARK 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.3 
_exptl_crystal.density_percent_sol   45 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    'Na-HEPES, Na Citrate, glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           105 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   CUSTOM-MADE 
_diffrn_detector.pdbx_collection_date   2005-05-06 
_diffrn_detector.details                SBC3 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SAGITALLY FOCUSED Si(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             MAD 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
loop_
_diffrn_radiation_wavelength.id 
_diffrn_radiation_wavelength.wavelength 
_diffrn_radiation_wavelength.wt 
1 0.97911 1.0 
2 0.97924 1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 19-BM' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   19-BM 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        '0.97911, 0.97924' 
# 
_reflns.entry_id                     2ARK 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.d_resolution_high            2.4 
_reflns.d_resolution_low             36.0 
_reflns.number_all                   43827 
_reflns.number_obs                   43827 
_reflns.percent_possible_obs         99.6 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.40 
_reflns_shell.d_res_low              2.49 
_reflns_shell.percent_possible_all   98.8 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.72 
_reflns_shell.meanI_over_sigI_obs    1.8 
_reflns_shell.pdbx_redundancy        4.2 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2ARK 
_refine.ls_number_reflns_obs                     41563 
_refine.ls_number_reflns_all                     43765 
_refine.pdbx_ls_sigma_I                          0 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             36.00 
_refine.ls_d_res_high                            2.40 
_refine.ls_percent_reflns_obs                    99.62 
_refine.ls_R_factor_obs                          0.17396 
_refine.ls_R_factor_all                          0.17396 
_refine.ls_R_factor_R_work                       0.17079 
_refine.ls_R_factor_R_free                       0.23519 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  2202 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.928 
_refine.B_iso_mean                               29.432 
_refine.aniso_B[1][1]                            1.79 
_refine.aniso_B[2][2]                            1.79 
_refine.aniso_B[3][3]                            -2.69 
_refine.aniso_B[1][2]                            0.90 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          MAD 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD WITH PHASES' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.559 
_refine.pdbx_overall_ESU_R_Free                  0.269 
_refine.overall_SU_ML                            0.192 
_refine.overall_SU_B                             16.522 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8633 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         66 
_refine_hist.number_atoms_solvent             420 
_refine_hist.number_atoms_total               9119 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        36.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         0.019  0.022  ? 8843  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      1.717  1.962  ? 11878 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   6.990  5.000  ? 1110  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   33.960 23.156 ? 377   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   20.392 15.000 ? 1585  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   20.942 15.000 ? 72    'X-RAY DIFFRACTION' ? 
r_chiral_restr           0.137  0.200  ? 1284  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     0.007  0.020  ? 6530  'X-RAY DIFFRACTION' ? 
r_nbd_refined            0.208  0.200  ? 4473  'X-RAY DIFFRACTION' ? 
r_nbtor_refined          0.302  0.200  ? 5937  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    0.178  0.200  ? 499   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   0.212  0.200  ? 111   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 0.269  0.200  ? 33    'X-RAY DIFFRACTION' ? 
r_mcbond_it              0.968  1.500  ? 5599  'X-RAY DIFFRACTION' ? 
r_mcangle_it             1.249  2.000  ? 8671  'X-RAY DIFFRACTION' ? 
r_scbond_it              2.706  3.000  ? 3748  'X-RAY DIFFRACTION' ? 
r_scangle_it             3.631  4.500  ? 3207  'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.400 
_refine_ls_shell.d_res_low                        2.462 
_refine_ls_shell.number_reflns_R_work             3031 
_refine_ls_shell.R_factor_R_work                  0.225 
_refine_ls_shell.percent_reflns_obs               99.34 
_refine_ls_shell.R_factor_R_free                  0.348 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             149 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_all                     ? 
# 
_database_PDB_matrix.entry_id          2ARK 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  2ARK 
_struct.title                     'Structure of a flavodoxin from Aquifex aeolicus' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2ARK 
_struct_keywords.pdbx_keywords   'ELECTRON TRANSPORT' 
_struct_keywords.text            
;flavodoxin, Aquifex aeolicus, FMN, structural genomics, PSI, Protein Structure Initiative, Midwest Center for Structural Genomics, MCSG, ELECTRON TRANSPORT
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 1 ? 
F N N 1 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
J N N 2 ? 
K N N 3 ? 
L N N 2 ? 
M N N 3 ? 
N N N 3 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 2 ? 
R N N 2 ? 
S N N 4 ? 
T N N 4 ? 
U N N 4 ? 
V N N 4 ? 
W N N 4 ? 
X N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FLAV_AQUAE 
_struct_ref.pdbx_db_accession          O67866 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGKVLVIYDTRTGNTKKMAELVAEGARSLEGTEVRLKHVDEATKEDVLWADGLAVGSPTNMGLVSWKMKRFFDDVLGDLW
GEIDGKIACAFSSSGGWGGGNEVACMSILTMLMNFGFLVFGVTDYVGKKFTLHYGAVVAGEPRSEEEKEACRRLGRRLAE
WVAIFVDGRKELLEKIRKDPARFVD
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 2ARK A 4 ? 188 ? O67866 1 ? 185 ? 1 185 
2 1 2ARK B 4 ? 188 ? O67866 1 ? 185 ? 1 185 
3 1 2ARK C 4 ? 188 ? O67866 1 ? 185 ? 1 185 
4 1 2ARK D 4 ? 188 ? O67866 1 ? 185 ? 1 185 
5 1 2ARK E 4 ? 188 ? O67866 1 ? 185 ? 1 185 
6 1 2ARK F 4 ? 188 ? O67866 1 ? 185 ? 1 185 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2ARK SER A 1   ? UNP O67866 ?   ?   'cloning artifact' -2  1  
1 2ARK ASN A 2   ? UNP O67866 ?   ?   'cloning artifact' -1  2  
1 2ARK ALA A 3   ? UNP O67866 ?   ?   'cloning artifact' 0   3  
1 2ARK MSE A 4   ? UNP O67866 MET 1   'modified residue' 1   4  
1 2ARK MSE A 21  ? UNP O67866 MET 18  'modified residue' 18  5  
1 2ARK MSE A 64  ? UNP O67866 MET 61  'modified residue' 61  6  
1 2ARK MSE A 71  ? UNP O67866 MET 68  'modified residue' 68  7  
1 2ARK MSE A 109 ? UNP O67866 MET 106 'modified residue' 106 8  
1 2ARK MSE A 114 ? UNP O67866 MET 111 'modified residue' 111 9  
1 2ARK MSE A 116 ? UNP O67866 MET 113 'modified residue' 113 10 
2 2ARK SER B 1   ? UNP O67866 ?   ?   'cloning artifact' -2  11 
2 2ARK ASN B 2   ? UNP O67866 ?   ?   'cloning artifact' -1  12 
2 2ARK ALA B 3   ? UNP O67866 ?   ?   'cloning artifact' 0   13 
2 2ARK MSE B 4   ? UNP O67866 MET 1   'modified residue' 1   14 
2 2ARK MSE B 21  ? UNP O67866 MET 18  'modified residue' 18  15 
2 2ARK MSE B 64  ? UNP O67866 MET 61  'modified residue' 61  16 
2 2ARK MSE B 71  ? UNP O67866 MET 68  'modified residue' 68  17 
2 2ARK MSE B 109 ? UNP O67866 MET 106 'modified residue' 106 18 
2 2ARK MSE B 114 ? UNP O67866 MET 111 'modified residue' 111 19 
2 2ARK MSE B 116 ? UNP O67866 MET 113 'modified residue' 113 20 
3 2ARK SER C 1   ? UNP O67866 ?   ?   'cloning artifact' -2  21 
3 2ARK ASN C 2   ? UNP O67866 ?   ?   'cloning artifact' -1  22 
3 2ARK ALA C 3   ? UNP O67866 ?   ?   'cloning artifact' 0   23 
3 2ARK MSE C 4   ? UNP O67866 MET 1   'modified residue' 1   24 
3 2ARK MSE C 21  ? UNP O67866 MET 18  'modified residue' 18  25 
3 2ARK MSE C 64  ? UNP O67866 MET 61  'modified residue' 61  26 
3 2ARK MSE C 71  ? UNP O67866 MET 68  'modified residue' 68  27 
3 2ARK MSE C 109 ? UNP O67866 MET 106 'modified residue' 106 28 
3 2ARK MSE C 114 ? UNP O67866 MET 111 'modified residue' 111 29 
3 2ARK MSE C 116 ? UNP O67866 MET 113 'modified residue' 113 30 
4 2ARK SER D 1   ? UNP O67866 ?   ?   'cloning artifact' -2  31 
4 2ARK ASN D 2   ? UNP O67866 ?   ?   'cloning artifact' -1  32 
4 2ARK ALA D 3   ? UNP O67866 ?   ?   'cloning artifact' 0   33 
4 2ARK MSE D 4   ? UNP O67866 MET 1   'modified residue' 1   34 
4 2ARK MSE D 21  ? UNP O67866 MET 18  'modified residue' 18  35 
4 2ARK MSE D 64  ? UNP O67866 MET 61  'modified residue' 61  36 
4 2ARK MSE D 71  ? UNP O67866 MET 68  'modified residue' 68  37 
4 2ARK MSE D 109 ? UNP O67866 MET 106 'modified residue' 106 38 
4 2ARK MSE D 114 ? UNP O67866 MET 111 'modified residue' 111 39 
4 2ARK MSE D 116 ? UNP O67866 MET 113 'modified residue' 113 40 
5 2ARK SER E 1   ? UNP O67866 ?   ?   'cloning artifact' -2  41 
5 2ARK ASN E 2   ? UNP O67866 ?   ?   'cloning artifact' -1  42 
5 2ARK ALA E 3   ? UNP O67866 ?   ?   'cloning artifact' 0   43 
5 2ARK MSE E 4   ? UNP O67866 MET 1   'modified residue' 1   44 
5 2ARK MSE E 21  ? UNP O67866 MET 18  'modified residue' 18  45 
5 2ARK MSE E 64  ? UNP O67866 MET 61  'modified residue' 61  46 
5 2ARK MSE E 71  ? UNP O67866 MET 68  'modified residue' 68  47 
5 2ARK MSE E 109 ? UNP O67866 MET 106 'modified residue' 106 48 
5 2ARK MSE E 114 ? UNP O67866 MET 111 'modified residue' 111 49 
5 2ARK MSE E 116 ? UNP O67866 MET 113 'modified residue' 113 50 
6 2ARK SER F 1   ? UNP O67866 ?   ?   'cloning artifact' -2  51 
6 2ARK ASN F 2   ? UNP O67866 ?   ?   'cloning artifact' -1  52 
6 2ARK ALA F 3   ? UNP O67866 ?   ?   'cloning artifact' 0   53 
6 2ARK MSE F 4   ? UNP O67866 MET 1   'modified residue' 1   54 
6 2ARK MSE F 21  ? UNP O67866 MET 18  'modified residue' 18  55 
6 2ARK MSE F 64  ? UNP O67866 MET 61  'modified residue' 61  56 
6 2ARK MSE F 71  ? UNP O67866 MET 68  'modified residue' 68  57 
6 2ARK MSE F 109 ? UNP O67866 MET 106 'modified residue' 106 58 
6 2ARK MSE F 114 ? UNP O67866 MET 111 'modified residue' 111 59 
6 2ARK MSE F 116 ? UNP O67866 MET 113 'modified residue' 113 60 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA tetrameric 4 
2 author_defined_assembly              ?    tetrameric 4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 14580 ? 
1 MORE         -113  ? 
1 'SSA (A^2)'  23780 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1   A,B,C,D,G,H,I,J,K,L,M,N,O,P,S,T,U,V 
2 1,2 E,F,Q,R,W,X                         
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z    1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 4_556 y,x,-z+1 -0.5000000000 0.8660254038 0.0000000000 0.0000000000 0.8660254038 0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 150.6480000000 
# 
loop_
_struct_biol.id 
_struct_biol.details 
_struct_biol.pdbx_parent_biol_id 
1 'Unknown, but most likely the tetramer A,B,C,D.' ? 
2 ?                                                ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  GLY A 16  ? SER A 31  ? GLY A 13  SER A 28  1 ? 16 
HELX_P HELX_P2  2  THR A 46  ? ALA A 53  ? THR A 43  ALA A 50  1 ? 8  
HELX_P HELX_P3  3  SER A 68  ? VAL A 78  ? SER A 65  VAL A 75  1 ? 11 
HELX_P HELX_P4  4  LEU A 79  ? LEU A 82  ? LEU A 76  LEU A 79  5 ? 4  
HELX_P HELX_P5  5  GLY A 103 ? PHE A 118 ? GLY A 100 PHE A 115 1 ? 16 
HELX_P HELX_P6  6  SER A 147 ? VAL A 169 ? SER A 144 VAL A 166 1 ? 23 
HELX_P HELX_P7  7  GLU A 174 ? ASP A 182 ? GLU A 171 ASP A 179 1 ? 9  
HELX_P HELX_P8  8  PRO A 183 ? PHE A 186 ? PRO A 180 PHE A 183 5 ? 4  
HELX_P HELX_P9  9  GLY B 16  ? SER B 31  ? GLY B 13  SER B 28  1 ? 16 
HELX_P HELX_P10 10 THR B 46  ? ALA B 53  ? THR B 43  ALA B 50  1 ? 8  
HELX_P HELX_P11 11 SER B 68  ? VAL B 78  ? SER B 65  VAL B 75  1 ? 11 
HELX_P HELX_P12 12 LEU B 79  ? TRP B 83  ? LEU B 76  TRP B 80  5 ? 5  
HELX_P HELX_P13 13 GLY B 103 ? PHE B 118 ? GLY B 100 PHE B 115 1 ? 16 
HELX_P HELX_P14 14 SER B 147 ? VAL B 169 ? SER B 144 VAL B 166 1 ? 23 
HELX_P HELX_P15 15 LYS B 173 ? LYS B 181 ? LYS B 170 LYS B 178 1 ? 9  
HELX_P HELX_P16 16 ASP B 182 ? PHE B 186 ? ASP B 179 PHE B 183 5 ? 5  
HELX_P HELX_P17 17 GLY C 16  ? SER C 31  ? GLY C 13  SER C 28  1 ? 16 
HELX_P HELX_P18 18 THR C 46  ? ALA C 53  ? THR C 43  ALA C 50  1 ? 8  
HELX_P HELX_P19 19 SER C 68  ? VAL C 78  ? SER C 65  VAL C 75  1 ? 11 
HELX_P HELX_P20 20 LEU C 79  ? TRP C 83  ? LEU C 76  TRP C 80  5 ? 5  
HELX_P HELX_P21 21 GLY C 103 ? PHE C 118 ? GLY C 100 PHE C 115 1 ? 16 
HELX_P HELX_P22 22 SER C 147 ? VAL C 169 ? SER C 144 VAL C 166 1 ? 23 
HELX_P HELX_P23 23 ARG C 172 ? LYS C 181 ? ARG C 169 LYS C 178 1 ? 10 
HELX_P HELX_P24 24 ASP C 182 ? PHE C 186 ? ASP C 179 PHE C 183 5 ? 5  
HELX_P HELX_P25 25 GLY D 16  ? SER D 31  ? GLY D 13  SER D 28  1 ? 16 
HELX_P HELX_P26 26 THR D 46  ? ALA D 53  ? THR D 43  ALA D 50  1 ? 8  
HELX_P HELX_P27 27 SER D 68  ? VAL D 78  ? SER D 65  VAL D 75  1 ? 11 
HELX_P HELX_P28 28 LEU D 79  ? TRP D 83  ? LEU D 76  TRP D 80  5 ? 5  
HELX_P HELX_P29 29 GLY D 103 ? PHE D 118 ? GLY D 100 PHE D 115 1 ? 16 
HELX_P HELX_P30 30 SER D 147 ? VAL D 169 ? SER D 144 VAL D 166 1 ? 23 
HELX_P HELX_P31 31 LYS D 173 ? LYS D 181 ? LYS D 170 LYS D 178 1 ? 9  
HELX_P HELX_P32 32 ASP D 182 ? PHE D 186 ? ASP D 179 PHE D 183 5 ? 5  
HELX_P HELX_P33 33 GLY E 16  ? LEU E 32  ? GLY E 13  LEU E 29  1 ? 17 
HELX_P HELX_P34 34 THR E 46  ? ALA E 53  ? THR E 43  ALA E 50  1 ? 8  
HELX_P HELX_P35 35 SER E 68  ? VAL E 78  ? SER E 65  VAL E 75  1 ? 11 
HELX_P HELX_P36 36 LEU E 79  ? TRP E 83  ? LEU E 76  TRP E 80  5 ? 5  
HELX_P HELX_P37 37 GLY E 103 ? PHE E 118 ? GLY E 100 PHE E 115 1 ? 16 
HELX_P HELX_P38 38 SER E 147 ? VAL E 169 ? SER E 144 VAL E 166 1 ? 23 
HELX_P HELX_P39 39 LYS E 173 ? ASP E 182 ? LYS E 170 ASP E 179 1 ? 10 
HELX_P HELX_P40 40 PRO E 183 ? PHE E 186 ? PRO E 180 PHE E 183 5 ? 4  
HELX_P HELX_P41 41 GLY F 16  ? SER F 31  ? GLY F 13  SER F 28  1 ? 16 
HELX_P HELX_P42 42 ASP F 43  ? ALA F 45  ? ASP F 40  ALA F 42  5 ? 3  
HELX_P HELX_P43 43 THR F 46  ? ALA F 53  ? THR F 43  ALA F 50  1 ? 8  
HELX_P HELX_P44 44 SER F 68  ? VAL F 78  ? SER F 65  VAL F 75  1 ? 11 
HELX_P HELX_P45 45 LEU F 79  ? TRP F 83  ? LEU F 76  TRP F 80  5 ? 5  
HELX_P HELX_P46 46 GLY F 103 ? PHE F 118 ? GLY F 100 PHE F 115 1 ? 16 
HELX_P HELX_P47 47 SER F 147 ? VAL F 169 ? SER F 144 VAL F 166 1 ? 23 
HELX_P HELX_P48 48 GLU F 174 ? ASP F 182 ? GLU F 171 ASP F 179 1 ? 9  
HELX_P HELX_P49 49 PRO F 183 ? PHE F 186 ? PRO F 180 PHE F 183 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? A ALA 3   C ? ? ? 1_555 A MSE 4   N ? ? A ALA 0   A MSE 1   1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale2  covale both ? A MSE 4   C ? ? ? 1_555 A GLY 5   N ? ? A MSE 1   A GLY 2   1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale3  covale both ? A LYS 20  C ? ? ? 1_555 A MSE 21  N ? ? A LYS 17  A MSE 18  1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale4  covale both ? A MSE 21  C ? ? ? 1_555 A ALA 22  N ? ? A MSE 18  A ALA 19  1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale5  covale both ? A ASN 63  C ? ? ? 1_555 A MSE 64  N ? ? A ASN 60  A MSE 61  1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale6  covale both ? A MSE 64  C ? ? ? 1_555 A GLY 65  N ? ? A MSE 61  A GLY 62  1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale7  covale both ? A LYS 70  C ? ? ? 1_555 A MSE 71  N ? ? A LYS 67  A MSE 68  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale8  covale both ? A MSE 71  C ? ? ? 1_555 A LYS 72  N ? ? A MSE 68  A LYS 69  1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale9  covale both ? A CYS 108 C ? ? ? 1_555 A MSE 109 N ? ? A CYS 105 A MSE 106 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale10 covale both ? A MSE 109 C ? ? ? 1_555 A SER 110 N ? ? A MSE 106 A SER 107 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale11 covale both ? A THR 113 C ? ? ? 1_555 A MSE 114 N ? ? A THR 110 A MSE 111 1_555 ? ? ? ? ? ? ? 1.312 ? ? 
covale12 covale both ? A MSE 114 C ? ? ? 1_555 A LEU 115 N ? ? A MSE 111 A LEU 112 1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale13 covale both ? A LEU 115 C ? ? ? 1_555 A MSE 116 N ? ? A LEU 112 A MSE 113 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale14 covale both ? A MSE 116 C ? ? ? 1_555 A ASN 117 N ? ? A MSE 113 A ASN 114 1_555 ? ? ? ? ? ? ? 1.322 ? ? 
covale15 covale both ? B ALA 3   C ? ? ? 1_555 B MSE 4   N ? ? B ALA 0   B MSE 1   1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale16 covale both ? B MSE 4   C ? ? ? 1_555 B GLY 5   N ? ? B MSE 1   B GLY 2   1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale17 covale both ? B LYS 20  C ? ? ? 1_555 B MSE 21  N ? ? B LYS 17  B MSE 18  1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale18 covale both ? B MSE 21  C ? ? ? 1_555 B ALA 22  N ? ? B MSE 18  B ALA 19  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale19 covale both ? B ASN 63  C ? ? ? 1_555 B MSE 64  N ? ? B ASN 60  B MSE 61  1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale20 covale both ? B MSE 64  C ? ? ? 1_555 B GLY 65  N ? ? B MSE 61  B GLY 62  1_555 ? ? ? ? ? ? ? 1.321 ? ? 
covale21 covale both ? B LYS 70  C ? ? ? 1_555 B MSE 71  N ? ? B LYS 67  B MSE 68  1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale22 covale both ? B MSE 71  C ? ? ? 1_555 B LYS 72  N ? ? B MSE 68  B LYS 69  1_555 ? ? ? ? ? ? ? 1.320 ? ? 
covale23 covale both ? B CYS 108 C ? ? ? 1_555 B MSE 109 N ? ? B CYS 105 B MSE 106 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale24 covale both ? B MSE 109 C ? ? ? 1_555 B SER 110 N ? ? B MSE 106 B SER 107 1_555 ? ? ? ? ? ? ? 1.351 ? ? 
covale25 covale both ? B THR 113 C ? ? ? 1_555 B MSE 114 N ? ? B THR 110 B MSE 111 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale26 covale both ? B MSE 114 C ? ? ? 1_555 B LEU 115 N ? ? B MSE 111 B LEU 112 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale27 covale both ? B LEU 115 C ? ? ? 1_555 B MSE 116 N ? ? B LEU 112 B MSE 113 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale28 covale both ? B MSE 116 C ? ? ? 1_555 B ASN 117 N ? ? B MSE 113 B ASN 114 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale29 covale both ? C ALA 3   C ? ? ? 1_555 C MSE 4   N ? ? C ALA 0   C MSE 1   1_555 ? ? ? ? ? ? ? 1.341 ? ? 
covale30 covale both ? C MSE 4   C ? ? ? 1_555 C GLY 5   N ? ? C MSE 1   C GLY 2   1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale31 covale both ? C LYS 20  C ? ? ? 1_555 C MSE 21  N ? ? C LYS 17  C MSE 18  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale32 covale both ? C MSE 21  C ? ? ? 1_555 C ALA 22  N ? ? C MSE 18  C ALA 19  1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale33 covale both ? C ASN 63  C ? ? ? 1_555 C MSE 64  N ? ? C ASN 60  C MSE 61  1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale34 covale both ? C MSE 64  C ? ? ? 1_555 C GLY 65  N ? ? C MSE 61  C GLY 62  1_555 ? ? ? ? ? ? ? 1.341 ? ? 
covale35 covale both ? C LYS 70  C ? ? ? 1_555 C MSE 71  N ? ? C LYS 67  C MSE 68  1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale36 covale both ? C MSE 71  C ? ? ? 1_555 C LYS 72  N ? ? C MSE 68  C LYS 69  1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale37 covale both ? C CYS 108 C ? ? ? 1_555 C MSE 109 N ? ? C CYS 105 C MSE 106 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale38 covale both ? C MSE 109 C ? ? ? 1_555 C SER 110 N ? ? C MSE 106 C SER 107 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale39 covale both ? C THR 113 C ? ? ? 1_555 C MSE 114 N ? ? C THR 110 C MSE 111 1_555 ? ? ? ? ? ? ? 1.323 ? ? 
covale40 covale both ? C MSE 114 C ? ? ? 1_555 C LEU 115 N ? ? C MSE 111 C LEU 112 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale41 covale both ? C LEU 115 C ? ? ? 1_555 C MSE 116 N ? ? C LEU 112 C MSE 113 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale42 covale both ? C MSE 116 C ? ? ? 1_555 C ASN 117 N ? ? C MSE 113 C ASN 114 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale43 covale both ? D ALA 3   C ? ? ? 1_555 D MSE 4   N ? ? D ALA 0   D MSE 1   1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale44 covale both ? D MSE 4   C ? ? ? 1_555 D GLY 5   N ? ? D MSE 1   D GLY 2   1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale45 covale both ? D LYS 20  C ? ? ? 1_555 D MSE 21  N ? ? D LYS 17  D MSE 18  1_555 ? ? ? ? ? ? ? 1.342 ? ? 
covale46 covale both ? D MSE 21  C ? ? ? 1_555 D ALA 22  N ? ? D MSE 18  D ALA 19  1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale47 covale both ? D ASN 63  C ? ? ? 1_555 D MSE 64  N ? ? D ASN 60  D MSE 61  1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale48 covale both ? D MSE 64  C ? ? ? 1_555 D GLY 65  N ? ? D MSE 61  D GLY 62  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale49 covale both ? D LYS 70  C ? ? ? 1_555 D MSE 71  N ? ? D LYS 67  D MSE 68  1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale50 covale both ? D MSE 71  C ? ? ? 1_555 D LYS 72  N ? ? D MSE 68  D LYS 69  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale51 covale both ? D CYS 108 C ? ? ? 1_555 D MSE 109 N ? ? D CYS 105 D MSE 106 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale52 covale both ? D MSE 109 C ? ? ? 1_555 D SER 110 N ? ? D MSE 106 D SER 107 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale53 covale both ? D THR 113 C ? ? ? 1_555 D MSE 114 N ? ? D THR 110 D MSE 111 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale54 covale both ? D MSE 114 C ? ? ? 1_555 D LEU 115 N ? ? D MSE 111 D LEU 112 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale55 covale both ? D LEU 115 C ? ? ? 1_555 D MSE 116 N ? ? D LEU 112 D MSE 113 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale56 covale both ? D MSE 116 C ? ? ? 1_555 D ASN 117 N ? ? D MSE 113 D ASN 114 1_555 ? ? ? ? ? ? ? 1.320 ? ? 
covale57 covale both ? E MSE 4   C ? ? ? 1_555 E GLY 5   N ? ? E MSE 1   E GLY 2   1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale58 covale both ? E LYS 20  C ? ? ? 1_555 E MSE 21  N ? ? E LYS 17  E MSE 18  1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale59 covale both ? E MSE 21  C ? ? ? 1_555 E ALA 22  N ? ? E MSE 18  E ALA 19  1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale60 covale both ? E ASN 63  C ? ? ? 1_555 E MSE 64  N ? ? E ASN 60  E MSE 61  1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale61 covale both ? E MSE 64  C ? ? ? 1_555 E GLY 65  N ? ? E MSE 61  E GLY 62  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale62 covale both ? E LYS 70  C ? ? ? 1_555 E MSE 71  N ? ? E LYS 67  E MSE 68  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale63 covale both ? E MSE 71  C ? ? ? 1_555 E LYS 72  N ? ? E MSE 68  E LYS 69  1_555 ? ? ? ? ? ? ? 1.322 ? ? 
covale64 covale both ? E CYS 108 C ? ? ? 1_555 E MSE 109 N ? ? E CYS 105 E MSE 106 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale65 covale both ? E MSE 109 C ? ? ? 1_555 E SER 110 N ? ? E MSE 106 E SER 107 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale66 covale both ? E THR 113 C ? ? ? 1_555 E MSE 114 N ? ? E THR 110 E MSE 111 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale67 covale both ? E MSE 114 C ? ? ? 1_555 E LEU 115 N ? ? E MSE 111 E LEU 112 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale68 covale both ? E LEU 115 C ? ? ? 1_555 E MSE 116 N ? ? E LEU 112 E MSE 113 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale69 covale both ? E MSE 116 C ? ? ? 1_555 E ASN 117 N ? ? E MSE 113 E ASN 114 1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale70 covale both ? F ALA 3   C ? ? ? 1_555 F MSE 4   N ? ? F ALA 0   F MSE 1   1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale71 covale both ? F MSE 4   C ? ? ? 1_555 F GLY 5   N ? ? F MSE 1   F GLY 2   1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale72 covale both ? F LYS 20  C ? ? ? 1_555 F MSE 21  N ? ? F LYS 17  F MSE 18  1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale73 covale both ? F MSE 21  C ? ? ? 1_555 F ALA 22  N ? ? F MSE 18  F ALA 19  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale74 covale both ? F ASN 63  C ? ? ? 1_555 F MSE 64  N ? ? F ASN 60  F MSE 61  1_555 ? ? ? ? ? ? ? 1.323 ? ? 
covale75 covale both ? F MSE 64  C ? ? ? 1_555 F GLY 65  N ? ? F MSE 61  F GLY 62  1_555 ? ? ? ? ? ? ? 1.323 ? ? 
covale76 covale both ? F LYS 70  C ? ? ? 1_555 F MSE 71  N ? ? F LYS 67  F MSE 68  1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale77 covale both ? F MSE 71  C ? ? ? 1_555 F LYS 72  N ? ? F MSE 68  F LYS 69  1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale78 covale both ? F CYS 108 C ? ? ? 1_555 F MSE 109 N ? ? F CYS 105 F MSE 106 1_555 ? ? ? ? ? ? ? 1.323 ? ? 
covale79 covale both ? F MSE 109 C ? ? ? 1_555 F SER 110 N ? ? F MSE 106 F SER 107 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale80 covale both ? F THR 113 C ? ? ? 1_555 F MSE 114 N ? ? F THR 110 F MSE 111 1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale81 covale both ? F MSE 114 C ? ? ? 1_555 F LEU 115 N ? ? F MSE 111 F LEU 112 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale82 covale both ? F LEU 115 C ? ? ? 1_555 F MSE 116 N ? ? F LEU 112 F MSE 113 1_555 ? ? ? ? ? ? ? 1.320 ? ? 
covale83 covale both ? F MSE 116 C ? ? ? 1_555 F ASN 117 N ? ? F MSE 113 F ASN 114 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  MSE A 4   ? . . . . MSE A 1   ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
2  MSE A 21  ? . . . . MSE A 18  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
3  MSE A 64  ? . . . . MSE A 61  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
4  MSE A 71  ? . . . . MSE A 68  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
5  MSE A 109 ? . . . . MSE A 106 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
6  MSE A 114 ? . . . . MSE A 111 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
7  MSE A 116 ? . . . . MSE A 113 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
8  MSE B 4   ? . . . . MSE B 1   ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
9  MSE B 21  ? . . . . MSE B 18  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
10 MSE B 64  ? . . . . MSE B 61  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
11 MSE B 71  ? . . . . MSE B 68  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
12 MSE B 109 ? . . . . MSE B 106 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
13 MSE B 114 ? . . . . MSE B 111 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
14 MSE B 116 ? . . . . MSE B 113 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
15 MSE C 4   ? . . . . MSE C 1   ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
16 MSE C 21  ? . . . . MSE C 18  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
17 MSE C 64  ? . . . . MSE C 61  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
18 MSE C 71  ? . . . . MSE C 68  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
19 MSE C 109 ? . . . . MSE C 106 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
20 MSE C 114 ? . . . . MSE C 111 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
21 MSE C 116 ? . . . . MSE C 113 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
22 MSE D 4   ? . . . . MSE D 1   ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
23 MSE D 21  ? . . . . MSE D 18  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
24 MSE D 64  ? . . . . MSE D 61  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
25 MSE D 71  ? . . . . MSE D 68  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
26 MSE D 109 ? . . . . MSE D 106 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
27 MSE D 114 ? . . . . MSE D 111 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
28 MSE D 116 ? . . . . MSE D 113 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
29 MSE E 4   ? . . . . MSE E 1   ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
30 MSE E 21  ? . . . . MSE E 18  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
31 MSE E 64  ? . . . . MSE E 61  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
32 MSE E 71  ? . . . . MSE E 68  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
33 MSE E 109 ? . . . . MSE E 106 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
34 MSE E 114 ? . . . . MSE E 111 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
35 MSE E 116 ? . . . . MSE E 113 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
36 MSE F 4   ? . . . . MSE F 1   ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
37 MSE F 21  ? . . . . MSE F 18  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
38 MSE F 64  ? . . . . MSE F 61  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
39 MSE F 71  ? . . . . MSE F 68  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
40 MSE F 109 ? . . . . MSE F 106 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
41 MSE F 114 ? . . . . MSE F 111 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
42 MSE F 116 ? . . . . MSE F 113 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 5 ? 
C ? 2 ? 
D ? 5 ? 
E ? 5 ? 
F ? 2 ? 
G ? 5 ? 
H ? 5 ? 
I ? 2 ? 
J ? 5 ? 
K ? 5 ? 
L ? 2 ? 
M ? 5 ? 
N ? 5 ? 
O ? 2 ? 
P ? 5 ? 
Q ? 5 ? 
R ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
B 1 2 ? parallel      
B 2 3 ? parallel      
B 3 4 ? parallel      
B 4 5 ? parallel      
C 1 2 ? anti-parallel 
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? parallel      
D 4 5 ? parallel      
E 1 2 ? parallel      
E 2 3 ? parallel      
E 3 4 ? parallel      
E 4 5 ? parallel      
F 1 2 ? anti-parallel 
G 1 2 ? parallel      
G 2 3 ? parallel      
G 3 4 ? parallel      
G 4 5 ? parallel      
H 1 2 ? parallel      
H 2 3 ? parallel      
H 3 4 ? parallel      
H 4 5 ? parallel      
I 1 2 ? anti-parallel 
J 1 2 ? parallel      
J 2 3 ? parallel      
J 3 4 ? parallel      
J 4 5 ? parallel      
K 1 2 ? parallel      
K 2 3 ? parallel      
K 3 4 ? parallel      
K 4 5 ? parallel      
L 1 2 ? anti-parallel 
M 1 2 ? parallel      
M 2 3 ? parallel      
M 3 4 ? parallel      
M 4 5 ? parallel      
N 1 2 ? parallel      
N 2 3 ? parallel      
N 3 4 ? parallel      
N 4 5 ? parallel      
O 1 2 ? anti-parallel 
P 1 2 ? parallel      
P 2 3 ? parallel      
P 3 4 ? parallel      
P 4 5 ? parallel      
Q 1 2 ? parallel      
Q 2 3 ? parallel      
Q 3 4 ? parallel      
Q 4 5 ? parallel      
R 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 THR A 35  ? HIS A 41  ? THR A 32  HIS A 38  
A 2 GLY A 5   ? TYR A 11  ? GLY A 2   TYR A 8   
A 3 GLY A 55  ? PRO A 61  ? GLY A 52  PRO A 58  
A 4 ILE A 90  ? SER A 97  ? ILE A 87  SER A 94  
A 5 LEU A 121 ? VAL A 122 ? LEU A 118 VAL A 119 
B 1 THR A 35  ? HIS A 41  ? THR A 32  HIS A 38  
B 2 GLY A 5   ? TYR A 11  ? GLY A 2   TYR A 8   
B 3 GLY A 55  ? PRO A 61  ? GLY A 52  PRO A 58  
B 4 ILE A 90  ? SER A 97  ? ILE A 87  SER A 94  
B 5 ALA A 139 ? ALA A 142 ? ALA A 136 ALA A 139 
C 1 VAL A 125 ? GLY A 130 ? VAL A 122 GLY A 127 
C 2 PHE A 133 ? LEU A 135 ? PHE A 130 LEU A 132 
D 1 THR B 35  ? HIS B 41  ? THR B 32  HIS B 38  
D 2 GLY B 5   ? TYR B 11  ? GLY B 2   TYR B 8   
D 3 GLY B 55  ? PRO B 61  ? GLY B 52  PRO B 58  
D 4 ILE B 90  ? SER B 97  ? ILE B 87  SER B 94  
D 5 LEU B 121 ? VAL B 122 ? LEU B 118 VAL B 119 
E 1 THR B 35  ? HIS B 41  ? THR B 32  HIS B 38  
E 2 GLY B 5   ? TYR B 11  ? GLY B 2   TYR B 8   
E 3 GLY B 55  ? PRO B 61  ? GLY B 52  PRO B 58  
E 4 ILE B 90  ? SER B 97  ? ILE B 87  SER B 94  
E 5 ALA B 139 ? ALA B 142 ? ALA B 136 ALA B 139 
F 1 VAL B 125 ? GLY B 130 ? VAL B 122 GLY B 127 
F 2 PHE B 133 ? LEU B 135 ? PHE B 130 LEU B 132 
G 1 THR C 35  ? HIS C 41  ? THR C 32  HIS C 38  
G 2 GLY C 5   ? TYR C 11  ? GLY C 2   TYR C 8   
G 3 GLY C 55  ? PRO C 61  ? GLY C 52  PRO C 58  
G 4 ILE C 90  ? SER C 97  ? ILE C 87  SER C 94  
G 5 LEU C 121 ? VAL C 122 ? LEU C 118 VAL C 119 
H 1 THR C 35  ? HIS C 41  ? THR C 32  HIS C 38  
H 2 GLY C 5   ? TYR C 11  ? GLY C 2   TYR C 8   
H 3 GLY C 55  ? PRO C 61  ? GLY C 52  PRO C 58  
H 4 ILE C 90  ? SER C 97  ? ILE C 87  SER C 94  
H 5 ALA C 139 ? ALA C 142 ? ALA C 136 ALA C 139 
I 1 VAL C 125 ? GLY C 130 ? VAL C 122 GLY C 127 
I 2 PHE C 133 ? LEU C 135 ? PHE C 130 LEU C 132 
J 1 THR D 35  ? HIS D 41  ? THR D 32  HIS D 38  
J 2 GLY D 5   ? TYR D 11  ? GLY D 2   TYR D 8   
J 3 GLY D 55  ? PRO D 61  ? GLY D 52  PRO D 58  
J 4 ILE D 90  ? SER D 97  ? ILE D 87  SER D 94  
J 5 LEU D 121 ? VAL D 122 ? LEU D 118 VAL D 119 
K 1 THR D 35  ? HIS D 41  ? THR D 32  HIS D 38  
K 2 GLY D 5   ? TYR D 11  ? GLY D 2   TYR D 8   
K 3 GLY D 55  ? PRO D 61  ? GLY D 52  PRO D 58  
K 4 ILE D 90  ? SER D 97  ? ILE D 87  SER D 94  
K 5 ALA D 139 ? ALA D 142 ? ALA D 136 ALA D 139 
L 1 VAL D 125 ? GLY D 130 ? VAL D 122 GLY D 127 
L 2 PHE D 133 ? LEU D 135 ? PHE D 130 LEU D 132 
M 1 THR E 35  ? HIS E 41  ? THR E 32  HIS E 38  
M 2 GLY E 5   ? TYR E 11  ? GLY E 2   TYR E 8   
M 3 GLY E 55  ? PRO E 61  ? GLY E 52  PRO E 58  
M 4 ILE E 90  ? SER E 97  ? ILE E 87  SER E 94  
M 5 LEU E 121 ? VAL E 122 ? LEU E 118 VAL E 119 
N 1 THR E 35  ? HIS E 41  ? THR E 32  HIS E 38  
N 2 GLY E 5   ? TYR E 11  ? GLY E 2   TYR E 8   
N 3 GLY E 55  ? PRO E 61  ? GLY E 52  PRO E 58  
N 4 ILE E 90  ? SER E 97  ? ILE E 87  SER E 94  
N 5 ALA E 139 ? ALA E 142 ? ALA E 136 ALA E 139 
O 1 VAL E 125 ? GLY E 130 ? VAL E 122 GLY E 127 
O 2 PHE E 133 ? LEU E 135 ? PHE E 130 LEU E 132 
P 1 THR F 35  ? HIS F 41  ? THR F 32  HIS F 38  
P 2 GLY F 5   ? TYR F 11  ? GLY F 2   TYR F 8   
P 3 GLY F 55  ? PRO F 61  ? GLY F 52  PRO F 58  
P 4 ILE F 90  ? SER F 97  ? ILE F 87  SER F 94  
P 5 LEU F 121 ? VAL F 122 ? LEU F 118 VAL F 119 
Q 1 THR F 35  ? HIS F 41  ? THR F 32  HIS F 38  
Q 2 GLY F 5   ? TYR F 11  ? GLY F 2   TYR F 8   
Q 3 GLY F 55  ? PRO F 61  ? GLY F 52  PRO F 58  
Q 4 ILE F 90  ? SER F 97  ? ILE F 87  SER F 94  
Q 5 ALA F 139 ? ALA F 142 ? ALA F 136 ALA F 139 
R 1 VAL F 125 ? GLY F 130 ? VAL F 122 GLY F 127 
R 2 PHE F 133 ? LEU F 135 ? PHE F 130 LEU F 132 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O GLU A 36  ? O GLU A 33  N GLY A 5   ? N GLY A 2   
A 2 3 N LEU A 8   ? N LEU A 5   O ALA A 57  ? O ALA A 54  
A 3 4 N LEU A 56  ? N LEU A 53  O ILE A 90  ? O ILE A 87  
A 4 5 N ALA A 91  ? N ALA A 88  O LEU A 121 ? O LEU A 118 
B 1 2 O GLU A 36  ? O GLU A 33  N GLY A 5   ? N GLY A 2   
B 2 3 N LEU A 8   ? N LEU A 5   O ALA A 57  ? O ALA A 54  
B 3 4 N LEU A 56  ? N LEU A 53  O ILE A 90  ? O ILE A 87  
B 4 5 N SER A 95  ? N SER A 92  O ALA A 139 ? O ALA A 136 
C 1 2 N VAL A 125 ? N VAL A 122 O LEU A 135 ? O LEU A 132 
D 1 2 O ARG B 38  ? O ARG B 35  N VAL B 9   ? N VAL B 6   
D 2 3 N LEU B 8   ? N LEU B 5   O ALA B 57  ? O ALA B 54  
D 3 4 N LEU B 56  ? N LEU B 53  O ILE B 90  ? O ILE B 87  
D 4 5 N ALA B 91  ? N ALA B 88  O LEU B 121 ? O LEU B 118 
E 1 2 O ARG B 38  ? O ARG B 35  N VAL B 9   ? N VAL B 6   
E 2 3 N LEU B 8   ? N LEU B 5   O ALA B 57  ? O ALA B 54  
E 3 4 N LEU B 56  ? N LEU B 53  O ILE B 90  ? O ILE B 87  
E 4 5 N SER B 95  ? N SER B 92  O ALA B 139 ? O ALA B 136 
F 1 2 N VAL B 129 ? N VAL B 126 O PHE B 133 ? O PHE B 130 
G 1 2 O GLU C 36  ? O GLU C 33  N GLY C 5   ? N GLY C 2   
G 2 3 N LEU C 8   ? N LEU C 5   O GLY C 55  ? O GLY C 52  
G 3 4 N LEU C 56  ? N LEU C 53  O ILE C 90  ? O ILE C 87  
G 4 5 N ALA C 91  ? N ALA C 88  O LEU C 121 ? O LEU C 118 
H 1 2 O GLU C 36  ? O GLU C 33  N GLY C 5   ? N GLY C 2   
H 2 3 N LEU C 8   ? N LEU C 5   O GLY C 55  ? O GLY C 52  
H 3 4 N LEU C 56  ? N LEU C 53  O ILE C 90  ? O ILE C 87  
H 4 5 N SER C 97  ? N SER C 94  O VAL C 141 ? O VAL C 138 
I 1 2 N VAL C 125 ? N VAL C 122 O LEU C 135 ? O LEU C 132 
J 1 2 O GLU D 36  ? O GLU D 33  N GLY D 5   ? N GLY D 2   
J 2 3 N LEU D 8   ? N LEU D 5   O GLY D 55  ? O GLY D 52  
J 3 4 N LEU D 56  ? N LEU D 53  O ILE D 90  ? O ILE D 87  
J 4 5 N ALA D 91  ? N ALA D 88  O LEU D 121 ? O LEU D 118 
K 1 2 O GLU D 36  ? O GLU D 33  N GLY D 5   ? N GLY D 2   
K 2 3 N LEU D 8   ? N LEU D 5   O GLY D 55  ? O GLY D 52  
K 3 4 N LEU D 56  ? N LEU D 53  O ILE D 90  ? O ILE D 87  
K 4 5 N SER D 97  ? N SER D 94  O VAL D 141 ? O VAL D 138 
L 1 2 N VAL D 125 ? N VAL D 122 O LEU D 135 ? O LEU D 132 
M 1 2 O GLU E 36  ? O GLU E 33  N GLY E 5   ? N GLY E 2   
M 2 3 N LYS E 6   ? N LYS E 3   O GLY E 55  ? O GLY E 52  
M 3 4 N VAL E 58  ? N VAL E 55  O CYS E 92  ? O CYS E 89  
M 4 5 N ALA E 91  ? N ALA E 88  O LEU E 121 ? O LEU E 118 
N 1 2 O GLU E 36  ? O GLU E 33  N GLY E 5   ? N GLY E 2   
N 2 3 N LYS E 6   ? N LYS E 3   O GLY E 55  ? O GLY E 52  
N 3 4 N VAL E 58  ? N VAL E 55  O CYS E 92  ? O CYS E 89  
N 4 5 N SER E 95  ? N SER E 92  O ALA E 139 ? O ALA E 136 
O 1 2 N VAL E 129 ? N VAL E 126 O PHE E 133 ? O PHE E 130 
P 1 2 O GLU F 36  ? O GLU F 33  N GLY F 5   ? N GLY F 2   
P 2 3 N LEU F 8   ? N LEU F 5   O GLY F 55  ? O GLY F 52  
P 3 4 N VAL F 58  ? N VAL F 55  O CYS F 92  ? O CYS F 89  
P 4 5 N ALA F 91  ? N ALA F 88  O LEU F 121 ? O LEU F 118 
Q 1 2 O GLU F 36  ? O GLU F 33  N GLY F 5   ? N GLY F 2   
Q 2 3 N LEU F 8   ? N LEU F 5   O GLY F 55  ? O GLY F 52  
Q 3 4 N VAL F 58  ? N VAL F 55  O CYS F 92  ? O CYS F 89  
Q 4 5 N SER F 95  ? N SER F 92  O ALA F 139 ? O ALA F 136 
R 1 2 N VAL F 125 ? N VAL F 122 O LEU F 135 ? O LEU F 132 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A PO4 501 ? 9 'BINDING SITE FOR RESIDUE PO4 A 501' 
AC2 Software B PO4 502 ? 9 'BINDING SITE FOR RESIDUE PO4 B 502' 
AC3 Software C PO4 503 ? 8 'BINDING SITE FOR RESIDUE PO4 C 503' 
AC4 Software D PO4 504 ? 8 'BINDING SITE FOR RESIDUE PO4 D 504' 
AC5 Software E PO4 505 ? 8 'BINDING SITE FOR RESIDUE PO4 E 505' 
AC6 Software F PO4 506 ? 8 'BINDING SITE FOR RESIDUE PO4 F 506' 
AC7 Software D GOL 507 ? 7 'BINDING SITE FOR RESIDUE GOL D 507' 
AC8 Software C GOL 508 ? 6 'BINDING SITE FOR RESIDUE GOL C 508' 
AC9 Software A GOL 509 ? 6 'BINDING SITE FOR RESIDUE GOL A 509' 
BC1 Software B GOL 510 ? 4 'BINDING SITE FOR RESIDUE GOL B 510' 
BC2 Software C GOL 511 ? 3 'BINDING SITE FOR RESIDUE GOL C 511' 
BC3 Software A GOL 512 ? 3 'BINDING SITE FOR RESIDUE GOL A 512' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 9 THR A 13  ? THR A 10  . ? 1_555 ? 
2  AC1 9 ARG A 14  ? ARG A 11  . ? 1_555 ? 
3  AC1 9 THR A 15  ? THR A 12  . ? 1_555 ? 
4  AC1 9 GLY A 16  ? GLY A 13  . ? 1_555 ? 
5  AC1 9 ASN A 17  ? ASN A 14  . ? 1_555 ? 
6  AC1 9 THR A 18  ? THR A 15  . ? 1_555 ? 
7  AC1 9 PRO A 61  ? PRO A 58  . ? 1_555 ? 
8  AC1 9 HOH S .   ? HOH A 513 . ? 1_555 ? 
9  AC1 9 HOH S .   ? HOH A 576 . ? 1_555 ? 
10 AC2 9 THR B 13  ? THR B 10  . ? 1_555 ? 
11 AC2 9 ARG B 14  ? ARG B 11  . ? 1_555 ? 
12 AC2 9 THR B 15  ? THR B 12  . ? 1_555 ? 
13 AC2 9 GLY B 16  ? GLY B 13  . ? 1_555 ? 
14 AC2 9 ASN B 17  ? ASN B 14  . ? 1_555 ? 
15 AC2 9 THR B 18  ? THR B 15  . ? 1_555 ? 
16 AC2 9 PRO B 61  ? PRO B 58  . ? 1_555 ? 
17 AC2 9 HOH T .   ? HOH B 541 . ? 1_555 ? 
18 AC2 9 HOH T .   ? HOH B 564 . ? 1_555 ? 
19 AC3 8 THR C 13  ? THR C 10  . ? 1_555 ? 
20 AC3 8 ARG C 14  ? ARG C 11  . ? 1_555 ? 
21 AC3 8 THR C 15  ? THR C 12  . ? 1_555 ? 
22 AC3 8 GLY C 16  ? GLY C 13  . ? 1_555 ? 
23 AC3 8 ASN C 17  ? ASN C 14  . ? 1_555 ? 
24 AC3 8 THR C 18  ? THR C 15  . ? 1_555 ? 
25 AC3 8 PRO C 61  ? PRO C 58  . ? 1_555 ? 
26 AC3 8 HOH U .   ? HOH C 522 . ? 1_555 ? 
27 AC4 8 THR D 13  ? THR D 10  . ? 1_555 ? 
28 AC4 8 ARG D 14  ? ARG D 11  . ? 1_555 ? 
29 AC4 8 THR D 15  ? THR D 12  . ? 1_555 ? 
30 AC4 8 GLY D 16  ? GLY D 13  . ? 1_555 ? 
31 AC4 8 ASN D 17  ? ASN D 14  . ? 1_555 ? 
32 AC4 8 THR D 18  ? THR D 15  . ? 1_555 ? 
33 AC4 8 PRO D 61  ? PRO D 58  . ? 1_555 ? 
34 AC4 8 HOH V .   ? HOH D 522 . ? 1_555 ? 
35 AC5 8 THR E 13  ? THR E 10  . ? 1_555 ? 
36 AC5 8 ARG E 14  ? ARG E 11  . ? 1_555 ? 
37 AC5 8 THR E 15  ? THR E 12  . ? 1_555 ? 
38 AC5 8 GLY E 16  ? GLY E 13  . ? 1_555 ? 
39 AC5 8 ASN E 17  ? ASN E 14  . ? 1_555 ? 
40 AC5 8 THR E 18  ? THR E 15  . ? 1_555 ? 
41 AC5 8 PRO E 61  ? PRO E 58  . ? 1_555 ? 
42 AC5 8 HOH W .   ? HOH E 521 . ? 1_555 ? 
43 AC6 8 THR F 13  ? THR F 10  . ? 1_555 ? 
44 AC6 8 ARG F 14  ? ARG F 11  . ? 1_555 ? 
45 AC6 8 THR F 15  ? THR F 12  . ? 1_555 ? 
46 AC6 8 GLY F 16  ? GLY F 13  . ? 1_555 ? 
47 AC6 8 ASN F 17  ? ASN F 14  . ? 1_555 ? 
48 AC6 8 THR F 18  ? THR F 15  . ? 1_555 ? 
49 AC6 8 PRO F 61  ? PRO F 58  . ? 1_555 ? 
50 AC6 8 HOH X .   ? HOH F 519 . ? 1_555 ? 
51 AC7 7 GOL I .   ? GOL A 512 . ? 1_555 ? 
52 AC7 7 SER B 110 ? SER B 107 . ? 1_555 ? 
53 AC7 7 THR B 113 ? THR B 110 . ? 1_555 ? 
54 AC7 7 VAL D 106 ? VAL D 103 . ? 1_555 ? 
55 AC7 7 MSE D 109 ? MSE D 106 . ? 1_555 ? 
56 AC7 7 SER D 110 ? SER D 107 . ? 1_555 ? 
57 AC7 7 THR D 113 ? THR D 110 . ? 1_555 ? 
58 AC8 6 THR A 113 ? THR A 110 . ? 1_555 ? 
59 AC8 6 GOL I .   ? GOL A 512 . ? 1_555 ? 
60 AC8 6 VAL C 106 ? VAL C 103 . ? 1_555 ? 
61 AC8 6 MSE C 109 ? MSE C 106 . ? 1_555 ? 
62 AC8 6 SER C 110 ? SER C 107 . ? 1_555 ? 
63 AC8 6 THR C 113 ? THR C 110 . ? 1_555 ? 
64 AC9 6 ARG A 159 ? ARG A 156 . ? 1_555 ? 
65 AC9 6 ARG A 160 ? ARG A 157 . ? 1_555 ? 
66 AC9 6 GLU A 163 ? GLU A 160 . ? 1_555 ? 
67 AC9 6 ASP A 182 ? ASP A 179 . ? 1_555 ? 
68 AC9 6 HOH S .   ? HOH A 522 . ? 1_555 ? 
69 AC9 6 HOH S .   ? HOH A 524 . ? 1_555 ? 
70 BC1 4 ASP A 43  ? ASP A 40  . ? 2_754 ? 
71 BC1 4 HOH S .   ? HOH A 557 . ? 2_754 ? 
72 BC1 4 HOH T .   ? HOH B 538 . ? 1_555 ? 
73 BC1 4 GOL N .   ? GOL C 511 . ? 1_555 ? 
74 BC2 3 GOL K .   ? GOL B 510 . ? 1_555 ? 
75 BC2 3 TYR C 128 ? TYR C 125 . ? 1_555 ? 
76 BC2 3 HOH U .   ? HOH C 533 . ? 1_555 ? 
77 BC3 3 MSE A 109 ? MSE A 106 . ? 1_555 ? 
78 BC3 3 GOL M .   ? GOL C 508 . ? 1_555 ? 
79 BC3 3 GOL P .   ? GOL D 507 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   2ARK 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NZ  B LYS 67  ? ? O  B HOH 569 ? ? 2.12 
2 1 N   B ARG 11  ? ? O1 B PO4 502 ? ? 2.13 
3 1 N   A ARG 11  ? ? O2 A PO4 501 ? ? 2.13 
4 1 N   F ARG 11  ? ? O1 F PO4 506 ? ? 2.14 
5 1 OD2 C ASP 74  ? ? O  C HOH 548 ? ? 2.17 
6 1 O   C HOH 538 ? ? O  C HOH 544 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NZ 
_pdbx_validate_symm_contact.auth_asym_id_1    F 
_pdbx_validate_symm_contact.auth_comp_id_1    LYS 
_pdbx_validate_symm_contact.auth_seq_id_1     17 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    F 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     553 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   6_765 
_pdbx_validate_symm_contact.dist              2.11 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 N  C ALA 0   ? ? CA  C ALA 0   ? ? 1.676 1.459 0.217 0.020 N 
2  1 NE C ARG 169 ? ? CZ  C ARG 169 ? ? 1.471 1.326 0.145 0.013 N 
3  1 CZ C ARG 169 ? ? NH2 C ARG 169 ? ? 1.499 1.326 0.173 0.013 N 
4  1 N  D SER -2  ? ? CA  D SER -2  ? ? 1.654 1.459 0.195 0.020 N 
5  1 CA D SER -2  ? ? CB  D SER -2  ? ? 1.696 1.525 0.171 0.015 N 
6  1 CB D SER -2  ? ? OG  D SER -2  ? ? 1.779 1.418 0.361 0.013 N 
7  1 CD E GLU 30  ? ? OE1 E GLU 30  ? ? 1.349 1.252 0.097 0.011 N 
8  1 CD E GLU 30  ? ? OE2 E GLU 30  ? ? 1.370 1.252 0.118 0.011 N 
9  1 C  E GLU 30  ? ? O   E GLU 30  ? ? 1.429 1.229 0.200 0.019 N 
10 1 CG E ARG 169 ? ? CD  E ARG 169 ? ? 1.788 1.515 0.273 0.025 N 
11 1 CZ E ARG 169 ? ? NH2 E ARG 169 ? ? 1.641 1.326 0.315 0.013 N 
12 1 CD E GLU 171 ? ? OE1 E GLU 171 ? ? 1.512 1.252 0.260 0.011 N 
13 1 CD E GLU 171 ? ? OE2 E GLU 171 ? ? 1.537 1.252 0.285 0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB  A VAL 64  ? ? CA A VAL 64  ? ? C   A VAL 64  ? ? 97.99  111.40 -13.41 1.90 N 
2  1 NE  A ARG 70  ? ? CZ A ARG 70  ? ? NH1 A ARG 70  ? ? 116.27 120.30 -4.03  0.50 N 
3  1 NE  A ARG 70  ? ? CZ A ARG 70  ? ? NH2 A ARG 70  ? ? 123.60 120.30 3.30   0.50 N 
4  1 CB  B VAL 64  ? ? CA B VAL 64  ? ? C   B VAL 64  ? ? 99.72  111.40 -11.68 1.90 N 
5  1 CA  B LEU 132 ? ? CB B LEU 132 ? ? CG  B LEU 132 ? ? 134.88 115.30 19.58  2.30 N 
6  1 NE  B ARG 153 ? ? CZ B ARG 153 ? ? NH2 B ARG 153 ? ? 116.76 120.30 -3.54  0.50 N 
7  1 NE  B ARG 156 ? ? CZ B ARG 156 ? ? NH1 B ARG 156 ? ? 124.79 120.30 4.49   0.50 N 
8  1 NE  B ARG 156 ? ? CZ B ARG 156 ? ? NH2 B ARG 156 ? ? 116.38 120.30 -3.92  0.50 N 
9  1 N   C ALA 0   ? ? CA C ALA 0   ? ? CB  C ALA 0   ? ? 122.05 110.10 11.95  1.40 N 
10 1 CB  C VAL 64  ? ? CA C VAL 64  ? ? C   C VAL 64  ? ? 99.67  111.40 -11.73 1.90 N 
11 1 NE  C ARG 70  ? ? CZ C ARG 70  ? ? NH1 C ARG 70  ? ? 115.99 120.30 -4.31  0.50 N 
12 1 NE  C ARG 70  ? ? CZ C ARG 70  ? ? NH2 C ARG 70  ? ? 124.43 120.30 4.13   0.50 N 
13 1 NE  C ARG 169 ? ? CZ C ARG 169 ? ? NH1 C ARG 169 ? ? 108.85 120.30 -11.45 0.50 N 
14 1 NE  C ARG 169 ? ? CZ C ARG 169 ? ? NH2 C ARG 169 ? ? 127.44 120.30 7.14   0.50 N 
15 1 CA  D SER -2  ? ? CB D SER -2  ? ? OG  D SER -2  ? ? 92.34  111.20 -18.86 2.70 N 
16 1 CB  D VAL 64  ? ? CA D VAL 64  ? ? C   D VAL 64  ? ? 99.32  111.40 -12.08 1.90 N 
17 1 CA  D LEU 132 ? ? CB D LEU 132 ? ? CG  D LEU 132 ? ? 132.18 115.30 16.88  2.30 N 
18 1 NE  D ARG 156 ? ? CZ D ARG 156 ? ? NH1 D ARG 156 ? ? 123.50 120.30 3.20   0.50 N 
19 1 NE  D ARG 156 ? ? CZ D ARG 156 ? ? NH2 D ARG 156 ? ? 117.25 120.30 -3.05  0.50 N 
20 1 CB  E VAL 64  ? ? CA E VAL 64  ? ? C   E VAL 64  ? ? 99.35  111.40 -12.05 1.90 N 
21 1 NE  E ARG 156 ? ? CZ E ARG 156 ? ? NH1 E ARG 156 ? ? 123.57 120.30 3.27   0.50 N 
22 1 NE  E ARG 169 ? ? CZ E ARG 169 ? ? NH1 E ARG 169 ? ? 115.59 120.30 -4.71  0.50 N 
23 1 NE  E ARG 169 ? ? CZ E ARG 169 ? ? NH2 E ARG 169 ? ? 127.80 120.30 7.50   0.50 N 
24 1 OE1 E GLU 171 ? ? CD E GLU 171 ? ? OE2 E GLU 171 ? ? 132.00 123.30 8.70   1.20 N 
25 1 CB  F VAL 64  ? ? CA F VAL 64  ? ? C   F VAL 64  ? ? 99.92  111.40 -11.48 1.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL A 64  ? ? -39.79  148.47 
2  1 LEU A 132 ? ? -158.16 48.39  
3  1 ARG A 169 ? ? -62.61  69.34  
4  1 VAL B 64  ? ? -43.67  151.56 
5  1 LEU B 132 ? ? -156.97 50.01  
6  1 LEU C 132 ? ? -154.49 55.41  
7  1 SER D 65  ? ? -37.64  141.06 
8  1 ASP D 124 ? ? -34.16  131.06 
9  1 LEU D 132 ? ? -157.09 52.41  
10 1 ARG D 169 ? ? -67.48  73.74  
11 1 LEU E 132 ? ? -160.24 52.24  
12 1 VAL F 64  ? ? -39.61  151.23 
13 1 LYS F 129 ? ? -140.65 36.20  
14 1 LEU F 132 ? ? -162.80 47.85  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    GLU 
_pdbx_validate_planes.auth_asym_id    E 
_pdbx_validate_planes.auth_seq_id     171 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.070 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'PSI, Protein Structure Initiative' 
_pdbx_SG_project.full_name_of_center   'Midwest Center for Structural Genomics' 
_pdbx_SG_project.initial_of_center     MCSG 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A MSE 4   A MSE 1   ? MET SELENOMETHIONINE 
2  A MSE 21  A MSE 18  ? MET SELENOMETHIONINE 
3  A MSE 64  A MSE 61  ? MET SELENOMETHIONINE 
4  A MSE 71  A MSE 68  ? MET SELENOMETHIONINE 
5  A MSE 109 A MSE 106 ? MET SELENOMETHIONINE 
6  A MSE 114 A MSE 111 ? MET SELENOMETHIONINE 
7  A MSE 116 A MSE 113 ? MET SELENOMETHIONINE 
8  B MSE 4   B MSE 1   ? MET SELENOMETHIONINE 
9  B MSE 21  B MSE 18  ? MET SELENOMETHIONINE 
10 B MSE 64  B MSE 61  ? MET SELENOMETHIONINE 
11 B MSE 71  B MSE 68  ? MET SELENOMETHIONINE 
12 B MSE 109 B MSE 106 ? MET SELENOMETHIONINE 
13 B MSE 114 B MSE 111 ? MET SELENOMETHIONINE 
14 B MSE 116 B MSE 113 ? MET SELENOMETHIONINE 
15 C MSE 4   C MSE 1   ? MET SELENOMETHIONINE 
16 C MSE 21  C MSE 18  ? MET SELENOMETHIONINE 
17 C MSE 64  C MSE 61  ? MET SELENOMETHIONINE 
18 C MSE 71  C MSE 68  ? MET SELENOMETHIONINE 
19 C MSE 109 C MSE 106 ? MET SELENOMETHIONINE 
20 C MSE 114 C MSE 111 ? MET SELENOMETHIONINE 
21 C MSE 116 C MSE 113 ? MET SELENOMETHIONINE 
22 D MSE 4   D MSE 1   ? MET SELENOMETHIONINE 
23 D MSE 21  D MSE 18  ? MET SELENOMETHIONINE 
24 D MSE 64  D MSE 61  ? MET SELENOMETHIONINE 
25 D MSE 71  D MSE 68  ? MET SELENOMETHIONINE 
26 D MSE 109 D MSE 106 ? MET SELENOMETHIONINE 
27 D MSE 114 D MSE 111 ? MET SELENOMETHIONINE 
28 D MSE 116 D MSE 113 ? MET SELENOMETHIONINE 
29 E MSE 4   E MSE 1   ? MET SELENOMETHIONINE 
30 E MSE 21  E MSE 18  ? MET SELENOMETHIONINE 
31 E MSE 64  E MSE 61  ? MET SELENOMETHIONINE 
32 E MSE 71  E MSE 68  ? MET SELENOMETHIONINE 
33 E MSE 109 E MSE 106 ? MET SELENOMETHIONINE 
34 E MSE 114 E MSE 111 ? MET SELENOMETHIONINE 
35 E MSE 116 E MSE 113 ? MET SELENOMETHIONINE 
36 F MSE 4   F MSE 1   ? MET SELENOMETHIONINE 
37 F MSE 21  F MSE 18  ? MET SELENOMETHIONINE 
38 F MSE 64  F MSE 61  ? MET SELENOMETHIONINE 
39 F MSE 71  F MSE 68  ? MET SELENOMETHIONINE 
40 F MSE 109 F MSE 106 ? MET SELENOMETHIONINE 
41 F MSE 114 F MSE 111 ? MET SELENOMETHIONINE 
42 F MSE 116 F MSE 113 ? MET SELENOMETHIONINE 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.pdbx_refine_id 
1 ? refined 101.9727 77.9942  68.4892 -0.0998 -0.1692 -0.1998 0.0474  0.0169  -0.0117 2.1726 1.9199 2.8379 0.4254  0.2767  -0.2291 
0.0423  -0.0853 0.1868  0.0931  -0.0007 0.1025  -0.3235 -0.2397 -0.0416 'X-RAY DIFFRACTION' 
2 ? refined 95.9913  67.0376  48.0485 -0.1622 -0.0230 -0.2112 -0.0221 -0.0866 0.0248  1.9373 1.9752 2.8169 0.2688  -0.5745 0.2676  
-0.0252 0.2496  0.0471  -0.2436 0.0517  0.1384  -0.0145 -0.3803 -0.0265 'X-RAY DIFFRACTION' 
3 ? refined 117.9993 49.1923  62.9077 0.0586  -0.1541 -0.0401 0.0899  -0.0849 -0.0107 2.3491 1.7638 3.6712 0.1465  0.0497  0.4989  
0.1164  0.0159  -0.4954 0.1312  0.0232  -0.1310 0.7528  0.2980  -0.1396 'X-RAY DIFFRACTION' 
4 ? refined 129.0539 68.4178  53.5126 -0.2038 0.1568  -0.1042 -0.0530 0.0421  -0.0694 1.7056 1.8560 3.2695 0.3430  0.9812  -0.1937 
0.0282  0.3300  -0.0420 -0.1920 0.0434  -0.2748 -0.0970 0.8063  -0.0716 'X-RAY DIFFRACTION' 
5 ? refined 72.0786  102.7036 80.0249 -0.1993 -0.0178 0.1737  -0.0796 -0.0228 -0.1061 3.1924 2.5438 3.4315 -0.5267 -0.7265 -0.0238 
-0.0393 -0.2192 0.6783  0.1417  0.0768  -0.5851 -0.1736 0.6038  -0.0375 'X-RAY DIFFRACTION' 
6 ? refined 54.0756  81.0465  65.1059 -0.0090 -0.1725 -0.1878 -0.0506 0.0570  -0.0838 2.8861 2.4274 3.1592 -0.6349 0.0076  -0.5681 
0.0411  0.3611  -0.1476 -0.2152 -0.0273 0.0382  0.4958  -0.0455 -0.0138 'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.selection_details 
1  1 A -2  A 1 A 184 A 187 ? 'X-RAY DIFFRACTION' ? 
2  1 A 501 G 1 A 501 G 1   ? 'X-RAY DIFFRACTION' ? 
3  2 B -1  B 2 B 184 B 187 ? 'X-RAY DIFFRACTION' ? 
4  2 B 502 H 1 B 502 H 1   ? 'X-RAY DIFFRACTION' ? 
5  3 C 0   C 3 C 185 C 188 ? 'X-RAY DIFFRACTION' ? 
6  3 C 503 I 1 C 503 I 1   ? 'X-RAY DIFFRACTION' ? 
7  4 D -2  D 1 D 184 D 187 ? 'X-RAY DIFFRACTION' ? 
8  4 D 504 J 1 D 504 J 1   ? 'X-RAY DIFFRACTION' ? 
9  5 E 1   E 4 E 185 E 188 ? 'X-RAY DIFFRACTION' ? 
10 5 E 505 K 1 E 505 K 1   ? 'X-RAY DIFFRACTION' ? 
11 6 F 0   F 3 F 184 F 187 ? 'X-RAY DIFFRACTION' ? 
12 6 F 506 L 1 F 506 L 1   ? 'X-RAY DIFFRACTION' ? 
# 
_pdbx_database_remark.id     300 
_pdbx_database_remark.text   
;BIOMOLECULE:1, 2
This entry contains the crystallographic asymmetric unit 
which consists of 6 chain(s). See remark 350 for 
information on generating the biological molecule(s). 
According to authors, the biological unit is not known but 
most likely a tetramer.
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ASP 185 ? A ASP 188 
2  1 Y 1 B SER -2  ? B SER 1   
3  1 Y 1 B ASP 185 ? B ASP 188 
4  1 Y 1 C SER -2  ? C SER 1   
5  1 Y 1 C ASN -1  ? C ASN 2   
6  1 Y 1 D ASP 185 ? D ASP 188 
7  1 Y 1 E SER -2  ? E SER 1   
8  1 Y 1 E ASN -1  ? E ASN 2   
9  1 Y 1 E ALA 0   ? E ALA 3   
10 1 Y 1 F SER -2  ? F SER 1   
11 1 Y 1 F ASN -1  ? F ASN 2   
12 1 Y 1 F ASP 185 ? F ASP 188 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLU N    N  N N 88  
GLU CA   C  N S 89  
GLU C    C  N N 90  
GLU O    O  N N 91  
GLU CB   C  N N 92  
GLU CG   C  N N 93  
GLU CD   C  N N 94  
GLU OE1  O  N N 95  
GLU OE2  O  N N 96  
GLU OXT  O  N N 97  
GLU H    H  N N 98  
GLU H2   H  N N 99  
GLU HA   H  N N 100 
GLU HB2  H  N N 101 
GLU HB3  H  N N 102 
GLU HG2  H  N N 103 
GLU HG3  H  N N 104 
GLU HE2  H  N N 105 
GLU HXT  H  N N 106 
GLY N    N  N N 107 
GLY CA   C  N N 108 
GLY C    C  N N 109 
GLY O    O  N N 110 
GLY OXT  O  N N 111 
GLY H    H  N N 112 
GLY H2   H  N N 113 
GLY HA2  H  N N 114 
GLY HA3  H  N N 115 
GLY HXT  H  N N 116 
GOL C1   C  N N 117 
GOL O1   O  N N 118 
GOL C2   C  N N 119 
GOL O2   O  N N 120 
GOL C3   C  N N 121 
GOL O3   O  N N 122 
GOL H11  H  N N 123 
GOL H12  H  N N 124 
GOL HO1  H  N N 125 
GOL H2   H  N N 126 
GOL HO2  H  N N 127 
GOL H31  H  N N 128 
GOL H32  H  N N 129 
GOL HO3  H  N N 130 
HIS N    N  N N 131 
HIS CA   C  N S 132 
HIS C    C  N N 133 
HIS O    O  N N 134 
HIS CB   C  N N 135 
HIS CG   C  Y N 136 
HIS ND1  N  Y N 137 
HIS CD2  C  Y N 138 
HIS CE1  C  Y N 139 
HIS NE2  N  Y N 140 
HIS OXT  O  N N 141 
HIS H    H  N N 142 
HIS H2   H  N N 143 
HIS HA   H  N N 144 
HIS HB2  H  N N 145 
HIS HB3  H  N N 146 
HIS HD1  H  N N 147 
HIS HD2  H  N N 148 
HIS HE1  H  N N 149 
HIS HE2  H  N N 150 
HIS HXT  H  N N 151 
HOH O    O  N N 152 
HOH H1   H  N N 153 
HOH H2   H  N N 154 
ILE N    N  N N 155 
ILE CA   C  N S 156 
ILE C    C  N N 157 
ILE O    O  N N 158 
ILE CB   C  N S 159 
ILE CG1  C  N N 160 
ILE CG2  C  N N 161 
ILE CD1  C  N N 162 
ILE OXT  O  N N 163 
ILE H    H  N N 164 
ILE H2   H  N N 165 
ILE HA   H  N N 166 
ILE HB   H  N N 167 
ILE HG12 H  N N 168 
ILE HG13 H  N N 169 
ILE HG21 H  N N 170 
ILE HG22 H  N N 171 
ILE HG23 H  N N 172 
ILE HD11 H  N N 173 
ILE HD12 H  N N 174 
ILE HD13 H  N N 175 
ILE HXT  H  N N 176 
LEU N    N  N N 177 
LEU CA   C  N S 178 
LEU C    C  N N 179 
LEU O    O  N N 180 
LEU CB   C  N N 181 
LEU CG   C  N N 182 
LEU CD1  C  N N 183 
LEU CD2  C  N N 184 
LEU OXT  O  N N 185 
LEU H    H  N N 186 
LEU H2   H  N N 187 
LEU HA   H  N N 188 
LEU HB2  H  N N 189 
LEU HB3  H  N N 190 
LEU HG   H  N N 191 
LEU HD11 H  N N 192 
LEU HD12 H  N N 193 
LEU HD13 H  N N 194 
LEU HD21 H  N N 195 
LEU HD22 H  N N 196 
LEU HD23 H  N N 197 
LEU HXT  H  N N 198 
LYS N    N  N N 199 
LYS CA   C  N S 200 
LYS C    C  N N 201 
LYS O    O  N N 202 
LYS CB   C  N N 203 
LYS CG   C  N N 204 
LYS CD   C  N N 205 
LYS CE   C  N N 206 
LYS NZ   N  N N 207 
LYS OXT  O  N N 208 
LYS H    H  N N 209 
LYS H2   H  N N 210 
LYS HA   H  N N 211 
LYS HB2  H  N N 212 
LYS HB3  H  N N 213 
LYS HG2  H  N N 214 
LYS HG3  H  N N 215 
LYS HD2  H  N N 216 
LYS HD3  H  N N 217 
LYS HE2  H  N N 218 
LYS HE3  H  N N 219 
LYS HZ1  H  N N 220 
LYS HZ2  H  N N 221 
LYS HZ3  H  N N 222 
LYS HXT  H  N N 223 
MET N    N  N N 224 
MET CA   C  N S 225 
MET C    C  N N 226 
MET O    O  N N 227 
MET CB   C  N N 228 
MET CG   C  N N 229 
MET SD   S  N N 230 
MET CE   C  N N 231 
MET OXT  O  N N 232 
MET H    H  N N 233 
MET H2   H  N N 234 
MET HA   H  N N 235 
MET HB2  H  N N 236 
MET HB3  H  N N 237 
MET HG2  H  N N 238 
MET HG3  H  N N 239 
MET HE1  H  N N 240 
MET HE2  H  N N 241 
MET HE3  H  N N 242 
MET HXT  H  N N 243 
MSE N    N  N N 244 
MSE CA   C  N S 245 
MSE C    C  N N 246 
MSE O    O  N N 247 
MSE OXT  O  N N 248 
MSE CB   C  N N 249 
MSE CG   C  N N 250 
MSE SE   SE N N 251 
MSE CE   C  N N 252 
MSE H    H  N N 253 
MSE H2   H  N N 254 
MSE HA   H  N N 255 
MSE HXT  H  N N 256 
MSE HB2  H  N N 257 
MSE HB3  H  N N 258 
MSE HG2  H  N N 259 
MSE HG3  H  N N 260 
MSE HE1  H  N N 261 
MSE HE2  H  N N 262 
MSE HE3  H  N N 263 
PHE N    N  N N 264 
PHE CA   C  N S 265 
PHE C    C  N N 266 
PHE O    O  N N 267 
PHE CB   C  N N 268 
PHE CG   C  Y N 269 
PHE CD1  C  Y N 270 
PHE CD2  C  Y N 271 
PHE CE1  C  Y N 272 
PHE CE2  C  Y N 273 
PHE CZ   C  Y N 274 
PHE OXT  O  N N 275 
PHE H    H  N N 276 
PHE H2   H  N N 277 
PHE HA   H  N N 278 
PHE HB2  H  N N 279 
PHE HB3  H  N N 280 
PHE HD1  H  N N 281 
PHE HD2  H  N N 282 
PHE HE1  H  N N 283 
PHE HE2  H  N N 284 
PHE HZ   H  N N 285 
PHE HXT  H  N N 286 
PO4 P    P  N N 287 
PO4 O1   O  N N 288 
PO4 O2   O  N N 289 
PO4 O3   O  N N 290 
PO4 O4   O  N N 291 
PRO N    N  N N 292 
PRO CA   C  N S 293 
PRO C    C  N N 294 
PRO O    O  N N 295 
PRO CB   C  N N 296 
PRO CG   C  N N 297 
PRO CD   C  N N 298 
PRO OXT  O  N N 299 
PRO H    H  N N 300 
PRO HA   H  N N 301 
PRO HB2  H  N N 302 
PRO HB3  H  N N 303 
PRO HG2  H  N N 304 
PRO HG3  H  N N 305 
PRO HD2  H  N N 306 
PRO HD3  H  N N 307 
PRO HXT  H  N N 308 
SER N    N  N N 309 
SER CA   C  N S 310 
SER C    C  N N 311 
SER O    O  N N 312 
SER CB   C  N N 313 
SER OG   O  N N 314 
SER OXT  O  N N 315 
SER H    H  N N 316 
SER H2   H  N N 317 
SER HA   H  N N 318 
SER HB2  H  N N 319 
SER HB3  H  N N 320 
SER HG   H  N N 321 
SER HXT  H  N N 322 
THR N    N  N N 323 
THR CA   C  N S 324 
THR C    C  N N 325 
THR O    O  N N 326 
THR CB   C  N R 327 
THR OG1  O  N N 328 
THR CG2  C  N N 329 
THR OXT  O  N N 330 
THR H    H  N N 331 
THR H2   H  N N 332 
THR HA   H  N N 333 
THR HB   H  N N 334 
THR HG1  H  N N 335 
THR HG21 H  N N 336 
THR HG22 H  N N 337 
THR HG23 H  N N 338 
THR HXT  H  N N 339 
TRP N    N  N N 340 
TRP CA   C  N S 341 
TRP C    C  N N 342 
TRP O    O  N N 343 
TRP CB   C  N N 344 
TRP CG   C  Y N 345 
TRP CD1  C  Y N 346 
TRP CD2  C  Y N 347 
TRP NE1  N  Y N 348 
TRP CE2  C  Y N 349 
TRP CE3  C  Y N 350 
TRP CZ2  C  Y N 351 
TRP CZ3  C  Y N 352 
TRP CH2  C  Y N 353 
TRP OXT  O  N N 354 
TRP H    H  N N 355 
TRP H2   H  N N 356 
TRP HA   H  N N 357 
TRP HB2  H  N N 358 
TRP HB3  H  N N 359 
TRP HD1  H  N N 360 
TRP HE1  H  N N 361 
TRP HE3  H  N N 362 
TRP HZ2  H  N N 363 
TRP HZ3  H  N N 364 
TRP HH2  H  N N 365 
TRP HXT  H  N N 366 
TYR N    N  N N 367 
TYR CA   C  N S 368 
TYR C    C  N N 369 
TYR O    O  N N 370 
TYR CB   C  N N 371 
TYR CG   C  Y N 372 
TYR CD1  C  Y N 373 
TYR CD2  C  Y N 374 
TYR CE1  C  Y N 375 
TYR CE2  C  Y N 376 
TYR CZ   C  Y N 377 
TYR OH   O  N N 378 
TYR OXT  O  N N 379 
TYR H    H  N N 380 
TYR H2   H  N N 381 
TYR HA   H  N N 382 
TYR HB2  H  N N 383 
TYR HB3  H  N N 384 
TYR HD1  H  N N 385 
TYR HD2  H  N N 386 
TYR HE1  H  N N 387 
TYR HE2  H  N N 388 
TYR HH   H  N N 389 
TYR HXT  H  N N 390 
VAL N    N  N N 391 
VAL CA   C  N S 392 
VAL C    C  N N 393 
VAL O    O  N N 394 
VAL CB   C  N N 395 
VAL CG1  C  N N 396 
VAL CG2  C  N N 397 
VAL OXT  O  N N 398 
VAL H    H  N N 399 
VAL H2   H  N N 400 
VAL HA   H  N N 401 
VAL HB   H  N N 402 
VAL HG11 H  N N 403 
VAL HG12 H  N N 404 
VAL HG13 H  N N 405 
VAL HG21 H  N N 406 
VAL HG22 H  N N 407 
VAL HG23 H  N N 408 
VAL HXT  H  N N 409 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLU N   CA   sing N N 83  
GLU N   H    sing N N 84  
GLU N   H2   sing N N 85  
GLU CA  C    sing N N 86  
GLU CA  CB   sing N N 87  
GLU CA  HA   sing N N 88  
GLU C   O    doub N N 89  
GLU C   OXT  sing N N 90  
GLU CB  CG   sing N N 91  
GLU CB  HB2  sing N N 92  
GLU CB  HB3  sing N N 93  
GLU CG  CD   sing N N 94  
GLU CG  HG2  sing N N 95  
GLU CG  HG3  sing N N 96  
GLU CD  OE1  doub N N 97  
GLU CD  OE2  sing N N 98  
GLU OE2 HE2  sing N N 99  
GLU OXT HXT  sing N N 100 
GLY N   CA   sing N N 101 
GLY N   H    sing N N 102 
GLY N   H2   sing N N 103 
GLY CA  C    sing N N 104 
GLY CA  HA2  sing N N 105 
GLY CA  HA3  sing N N 106 
GLY C   O    doub N N 107 
GLY C   OXT  sing N N 108 
GLY OXT HXT  sing N N 109 
GOL C1  O1   sing N N 110 
GOL C1  C2   sing N N 111 
GOL C1  H11  sing N N 112 
GOL C1  H12  sing N N 113 
GOL O1  HO1  sing N N 114 
GOL C2  O2   sing N N 115 
GOL C2  C3   sing N N 116 
GOL C2  H2   sing N N 117 
GOL O2  HO2  sing N N 118 
GOL C3  O3   sing N N 119 
GOL C3  H31  sing N N 120 
GOL C3  H32  sing N N 121 
GOL O3  HO3  sing N N 122 
HIS N   CA   sing N N 123 
HIS N   H    sing N N 124 
HIS N   H2   sing N N 125 
HIS CA  C    sing N N 126 
HIS CA  CB   sing N N 127 
HIS CA  HA   sing N N 128 
HIS C   O    doub N N 129 
HIS C   OXT  sing N N 130 
HIS CB  CG   sing N N 131 
HIS CB  HB2  sing N N 132 
HIS CB  HB3  sing N N 133 
HIS CG  ND1  sing Y N 134 
HIS CG  CD2  doub Y N 135 
HIS ND1 CE1  doub Y N 136 
HIS ND1 HD1  sing N N 137 
HIS CD2 NE2  sing Y N 138 
HIS CD2 HD2  sing N N 139 
HIS CE1 NE2  sing Y N 140 
HIS CE1 HE1  sing N N 141 
HIS NE2 HE2  sing N N 142 
HIS OXT HXT  sing N N 143 
HOH O   H1   sing N N 144 
HOH O   H2   sing N N 145 
ILE N   CA   sing N N 146 
ILE N   H    sing N N 147 
ILE N   H2   sing N N 148 
ILE CA  C    sing N N 149 
ILE CA  CB   sing N N 150 
ILE CA  HA   sing N N 151 
ILE C   O    doub N N 152 
ILE C   OXT  sing N N 153 
ILE CB  CG1  sing N N 154 
ILE CB  CG2  sing N N 155 
ILE CB  HB   sing N N 156 
ILE CG1 CD1  sing N N 157 
ILE CG1 HG12 sing N N 158 
ILE CG1 HG13 sing N N 159 
ILE CG2 HG21 sing N N 160 
ILE CG2 HG22 sing N N 161 
ILE CG2 HG23 sing N N 162 
ILE CD1 HD11 sing N N 163 
ILE CD1 HD12 sing N N 164 
ILE CD1 HD13 sing N N 165 
ILE OXT HXT  sing N N 166 
LEU N   CA   sing N N 167 
LEU N   H    sing N N 168 
LEU N   H2   sing N N 169 
LEU CA  C    sing N N 170 
LEU CA  CB   sing N N 171 
LEU CA  HA   sing N N 172 
LEU C   O    doub N N 173 
LEU C   OXT  sing N N 174 
LEU CB  CG   sing N N 175 
LEU CB  HB2  sing N N 176 
LEU CB  HB3  sing N N 177 
LEU CG  CD1  sing N N 178 
LEU CG  CD2  sing N N 179 
LEU CG  HG   sing N N 180 
LEU CD1 HD11 sing N N 181 
LEU CD1 HD12 sing N N 182 
LEU CD1 HD13 sing N N 183 
LEU CD2 HD21 sing N N 184 
LEU CD2 HD22 sing N N 185 
LEU CD2 HD23 sing N N 186 
LEU OXT HXT  sing N N 187 
LYS N   CA   sing N N 188 
LYS N   H    sing N N 189 
LYS N   H2   sing N N 190 
LYS CA  C    sing N N 191 
LYS CA  CB   sing N N 192 
LYS CA  HA   sing N N 193 
LYS C   O    doub N N 194 
LYS C   OXT  sing N N 195 
LYS CB  CG   sing N N 196 
LYS CB  HB2  sing N N 197 
LYS CB  HB3  sing N N 198 
LYS CG  CD   sing N N 199 
LYS CG  HG2  sing N N 200 
LYS CG  HG3  sing N N 201 
LYS CD  CE   sing N N 202 
LYS CD  HD2  sing N N 203 
LYS CD  HD3  sing N N 204 
LYS CE  NZ   sing N N 205 
LYS CE  HE2  sing N N 206 
LYS CE  HE3  sing N N 207 
LYS NZ  HZ1  sing N N 208 
LYS NZ  HZ2  sing N N 209 
LYS NZ  HZ3  sing N N 210 
LYS OXT HXT  sing N N 211 
MET N   CA   sing N N 212 
MET N   H    sing N N 213 
MET N   H2   sing N N 214 
MET CA  C    sing N N 215 
MET CA  CB   sing N N 216 
MET CA  HA   sing N N 217 
MET C   O    doub N N 218 
MET C   OXT  sing N N 219 
MET CB  CG   sing N N 220 
MET CB  HB2  sing N N 221 
MET CB  HB3  sing N N 222 
MET CG  SD   sing N N 223 
MET CG  HG2  sing N N 224 
MET CG  HG3  sing N N 225 
MET SD  CE   sing N N 226 
MET CE  HE1  sing N N 227 
MET CE  HE2  sing N N 228 
MET CE  HE3  sing N N 229 
MET OXT HXT  sing N N 230 
MSE N   CA   sing N N 231 
MSE N   H    sing N N 232 
MSE N   H2   sing N N 233 
MSE CA  C    sing N N 234 
MSE CA  CB   sing N N 235 
MSE CA  HA   sing N N 236 
MSE C   O    doub N N 237 
MSE C   OXT  sing N N 238 
MSE OXT HXT  sing N N 239 
MSE CB  CG   sing N N 240 
MSE CB  HB2  sing N N 241 
MSE CB  HB3  sing N N 242 
MSE CG  SE   sing N N 243 
MSE CG  HG2  sing N N 244 
MSE CG  HG3  sing N N 245 
MSE SE  CE   sing N N 246 
MSE CE  HE1  sing N N 247 
MSE CE  HE2  sing N N 248 
MSE CE  HE3  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PO4 P   O1   doub N N 273 
PO4 P   O2   sing N N 274 
PO4 P   O3   sing N N 275 
PO4 P   O4   sing N N 276 
PRO N   CA   sing N N 277 
PRO N   CD   sing N N 278 
PRO N   H    sing N N 279 
PRO CA  C    sing N N 280 
PRO CA  CB   sing N N 281 
PRO CA  HA   sing N N 282 
PRO C   O    doub N N 283 
PRO C   OXT  sing N N 284 
PRO CB  CG   sing N N 285 
PRO CB  HB2  sing N N 286 
PRO CB  HB3  sing N N 287 
PRO CG  CD   sing N N 288 
PRO CG  HG2  sing N N 289 
PRO CG  HG3  sing N N 290 
PRO CD  HD2  sing N N 291 
PRO CD  HD3  sing N N 292 
PRO OXT HXT  sing N N 293 
SER N   CA   sing N N 294 
SER N   H    sing N N 295 
SER N   H2   sing N N 296 
SER CA  C    sing N N 297 
SER CA  CB   sing N N 298 
SER CA  HA   sing N N 299 
SER C   O    doub N N 300 
SER C   OXT  sing N N 301 
SER CB  OG   sing N N 302 
SER CB  HB2  sing N N 303 
SER CB  HB3  sing N N 304 
SER OG  HG   sing N N 305 
SER OXT HXT  sing N N 306 
THR N   CA   sing N N 307 
THR N   H    sing N N 308 
THR N   H2   sing N N 309 
THR CA  C    sing N N 310 
THR CA  CB   sing N N 311 
THR CA  HA   sing N N 312 
THR C   O    doub N N 313 
THR C   OXT  sing N N 314 
THR CB  OG1  sing N N 315 
THR CB  CG2  sing N N 316 
THR CB  HB   sing N N 317 
THR OG1 HG1  sing N N 318 
THR CG2 HG21 sing N N 319 
THR CG2 HG22 sing N N 320 
THR CG2 HG23 sing N N 321 
THR OXT HXT  sing N N 322 
TRP N   CA   sing N N 323 
TRP N   H    sing N N 324 
TRP N   H2   sing N N 325 
TRP CA  C    sing N N 326 
TRP CA  CB   sing N N 327 
TRP CA  HA   sing N N 328 
TRP C   O    doub N N 329 
TRP C   OXT  sing N N 330 
TRP CB  CG   sing N N 331 
TRP CB  HB2  sing N N 332 
TRP CB  HB3  sing N N 333 
TRP CG  CD1  doub Y N 334 
TRP CG  CD2  sing Y N 335 
TRP CD1 NE1  sing Y N 336 
TRP CD1 HD1  sing N N 337 
TRP CD2 CE2  doub Y N 338 
TRP CD2 CE3  sing Y N 339 
TRP NE1 CE2  sing Y N 340 
TRP NE1 HE1  sing N N 341 
TRP CE2 CZ2  sing Y N 342 
TRP CE3 CZ3  doub Y N 343 
TRP CE3 HE3  sing N N 344 
TRP CZ2 CH2  doub Y N 345 
TRP CZ2 HZ2  sing N N 346 
TRP CZ3 CH2  sing Y N 347 
TRP CZ3 HZ3  sing N N 348 
TRP CH2 HH2  sing N N 349 
TRP OXT HXT  sing N N 350 
TYR N   CA   sing N N 351 
TYR N   H    sing N N 352 
TYR N   H2   sing N N 353 
TYR CA  C    sing N N 354 
TYR CA  CB   sing N N 355 
TYR CA  HA   sing N N 356 
TYR C   O    doub N N 357 
TYR C   OXT  sing N N 358 
TYR CB  CG   sing N N 359 
TYR CB  HB2  sing N N 360 
TYR CB  HB3  sing N N 361 
TYR CG  CD1  doub Y N 362 
TYR CG  CD2  sing Y N 363 
TYR CD1 CE1  sing Y N 364 
TYR CD1 HD1  sing N N 365 
TYR CD2 CE2  doub Y N 366 
TYR CD2 HD2  sing N N 367 
TYR CE1 CZ   doub Y N 368 
TYR CE1 HE1  sing N N 369 
TYR CE2 CZ   sing Y N 370 
TYR CE2 HE2  sing N N 371 
TYR CZ  OH   sing N N 372 
TYR OH  HH   sing N N 373 
TYR OXT HXT  sing N N 374 
VAL N   CA   sing N N 375 
VAL N   H    sing N N 376 
VAL N   H2   sing N N 377 
VAL CA  C    sing N N 378 
VAL CA  CB   sing N N 379 
VAL CA  HA   sing N N 380 
VAL C   O    doub N N 381 
VAL C   OXT  sing N N 382 
VAL CB  CG1  sing N N 383 
VAL CB  CG2  sing N N 384 
VAL CB  HB   sing N N 385 
VAL CG1 HG11 sing N N 386 
VAL CG1 HG12 sing N N 387 
VAL CG1 HG13 sing N N 388 
VAL CG2 HG21 sing N N 389 
VAL CG2 HG22 sing N N 390 
VAL CG2 HG23 sing N N 391 
VAL OXT HXT  sing N N 392 
# 
_atom_sites.entry_id                    2ARK 
_atom_sites.fract_transf_matrix[1][1]   0.008862 
_atom_sites.fract_transf_matrix[1][2]   0.005116 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010233 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006638 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
P  
S  
SE 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 1   ? 77.760  87.986  69.475  1.00 39.32 ? -2  SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? 76.961  86.727  69.438  1.00 39.38 ? -2  SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? 77.858  85.577  69.015  1.00 39.88 ? -2  SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? 77.715  84.470  69.525  1.00 40.10 ? -2  SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? 75.735  86.842  68.523  1.00 39.03 ? -2  SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? 74.838  85.769  68.738  1.00 37.23 ? -2  SER A OG  1 
ATOM   7    N  N   . ASN A 1 2   ? 78.794  85.826  68.100  1.00 40.37 ? -1  ASN A N   1 
ATOM   8    C  CA  . ASN A 1 2   ? 79.874  84.855  67.890  1.00 41.08 ? -1  ASN A CA  1 
ATOM   9    C  C   . ASN A 1 2   ? 80.693  84.747  69.166  1.00 40.83 ? -1  ASN A C   1 
ATOM   10   O  O   . ASN A 1 2   ? 80.684  85.663  69.999  1.00 40.84 ? -1  ASN A O   1 
ATOM   11   C  CB  . ASN A 1 2   ? 80.787  85.240  66.723  1.00 41.48 ? -1  ASN A CB  1 
ATOM   12   C  CG  . ASN A 1 2   ? 80.277  84.724  65.369  1.00 43.06 ? -1  ASN A CG  1 
ATOM   13   O  OD1 . ASN A 1 2   ? 81.050  84.161  64.588  1.00 44.06 ? -1  ASN A OD1 1 
ATOM   14   N  ND2 . ASN A 1 2   ? 78.977  84.926  65.083  1.00 44.02 ? -1  ASN A ND2 1 
ATOM   15   N  N   . ALA A 1 3   ? 81.376  83.622  69.332  1.00 40.55 ? 0   ALA A N   1 
ATOM   16   C  CA  . ALA A 1 3   ? 82.247  83.446  70.478  1.00 40.16 ? 0   ALA A CA  1 
ATOM   17   C  C   . ALA A 1 3   ? 83.597  84.097  70.186  1.00 40.32 ? 0   ALA A C   1 
ATOM   18   O  O   . ALA A 1 3   ? 83.929  84.370  69.023  1.00 40.10 ? 0   ALA A O   1 
ATOM   19   C  CB  . ALA A 1 3   ? 82.406  81.972  70.782  1.00 40.03 ? 0   ALA A CB  1 
HETATM 20   N  N   . MSE A 1 4   ? 84.371  84.357  71.240  1.00 40.32 ? 1   MSE A N   1 
HETATM 21   C  CA  . MSE A 1 4   ? 85.775  84.738  71.076  1.00 41.23 ? 1   MSE A CA  1 
HETATM 22   C  C   . MSE A 1 4   ? 86.556  83.576  70.469  1.00 38.63 ? 1   MSE A C   1 
HETATM 23   O  O   . MSE A 1 4   ? 86.208  82.410  70.665  1.00 38.59 ? 1   MSE A O   1 
HETATM 24   C  CB  . MSE A 1 4   ? 86.403  85.108  72.422  1.00 40.53 ? 1   MSE A CB  1 
HETATM 25   C  CG  . MSE A 1 4   ? 85.884  86.370  73.060  1.00 43.29 ? 1   MSE A CG  1 
HETATM 26   SE SE  . MSE A 1 4   ? 86.588  86.647  74.921  1.00 48.93 ? 1   MSE A SE  1 
HETATM 27   C  CE  . MSE A 1 4   ? 88.279  87.706  74.448  1.00 46.94 ? 1   MSE A CE  1 
ATOM   28   N  N   . GLY A 1 5   ? 87.615  83.890  69.734  1.00 37.04 ? 2   GLY A N   1 
ATOM   29   C  CA  . GLY A 1 5   ? 88.582  82.875  69.323  1.00 34.36 ? 2   GLY A CA  1 
ATOM   30   C  C   . GLY A 1 5   ? 89.226  82.279  70.559  1.00 32.96 ? 2   GLY A C   1 
ATOM   31   O  O   . GLY A 1 5   ? 89.571  82.989  71.486  1.00 32.93 ? 2   GLY A O   1 
ATOM   32   N  N   . LYS A 1 6   ? 89.355  80.963  70.583  1.00 31.83 ? 3   LYS A N   1 
ATOM   33   C  CA  . LYS A 1 6   ? 89.883  80.233  71.735  1.00 30.87 ? 3   LYS A CA  1 
ATOM   34   C  C   . LYS A 1 6   ? 91.258  79.658  71.364  1.00 29.87 ? 3   LYS A C   1 
ATOM   35   O  O   . LYS A 1 6   ? 91.354  78.792  70.477  1.00 28.49 ? 3   LYS A O   1 
ATOM   36   C  CB  . LYS A 1 6   ? 88.916  79.104  72.129  1.00 31.23 ? 3   LYS A CB  1 
ATOM   37   C  CG  . LYS A 1 6   ? 87.694  79.541  72.889  1.00 31.00 ? 3   LYS A CG  1 
ATOM   38   C  CD  . LYS A 1 6   ? 86.463  78.880  72.310  1.00 34.65 ? 3   LYS A CD  1 
ATOM   39   C  CE  . LYS A 1 6   ? 86.013  77.646  73.067  1.00 35.73 ? 3   LYS A CE  1 
ATOM   40   N  NZ  . LYS A 1 6   ? 85.044  76.870  72.244  1.00 35.53 ? 3   LYS A NZ  1 
ATOM   41   N  N   . VAL A 1 7   ? 92.304  80.185  72.017  1.00 28.83 ? 4   VAL A N   1 
ATOM   42   C  CA  . VAL A 1 7   ? 93.696  79.785  71.767  1.00 28.19 ? 4   VAL A CA  1 
ATOM   43   C  C   . VAL A 1 7   ? 94.356  79.120  72.996  1.00 28.13 ? 4   VAL A C   1 
ATOM   44   O  O   . VAL A 1 7   ? 94.318  79.645  74.114  1.00 29.19 ? 4   VAL A O   1 
ATOM   45   C  CB  . VAL A 1 7   ? 94.527  80.995  71.232  1.00 28.15 ? 4   VAL A CB  1 
ATOM   46   C  CG1 . VAL A 1 7   ? 96.024  80.716  71.231  1.00 26.19 ? 4   VAL A CG1 1 
ATOM   47   C  CG2 . VAL A 1 7   ? 94.087  81.359  69.828  1.00 28.67 ? 4   VAL A CG2 1 
ATOM   48   N  N   . LEU A 1 8   ? 94.948  77.954  72.783  1.00 28.27 ? 5   LEU A N   1 
ATOM   49   C  CA  . LEU A 1 8   ? 95.698  77.231  73.824  1.00 27.92 ? 5   LEU A CA  1 
ATOM   50   C  C   . LEU A 1 8   ? 97.173  77.350  73.528  1.00 27.25 ? 5   LEU A C   1 
ATOM   51   O  O   . LEU A 1 8   ? 97.642  76.961  72.445  1.00 27.86 ? 5   LEU A O   1 
ATOM   52   C  CB  . LEU A 1 8   ? 95.328  75.744  73.835  1.00 27.39 ? 5   LEU A CB  1 
ATOM   53   C  CG  . LEU A 1 8   ? 95.392  74.865  75.093  1.00 29.98 ? 5   LEU A CG  1 
ATOM   54   C  CD1 . LEU A 1 8   ? 95.815  73.456  74.707  1.00 27.29 ? 5   LEU A CD1 1 
ATOM   55   C  CD2 . LEU A 1 8   ? 96.235  75.374  76.327  1.00 29.04 ? 5   LEU A CD2 1 
ATOM   56   N  N   . VAL A 1 9   ? 97.913  77.911  74.468  1.00 26.69 ? 6   VAL A N   1 
ATOM   57   C  CA  . VAL A 1 9   ? 99.362  77.860  74.386  1.00 25.80 ? 6   VAL A CA  1 
ATOM   58   C  C   . VAL A 1 9   ? 99.794  76.839  75.424  1.00 26.25 ? 6   VAL A C   1 
ATOM   59   O  O   . VAL A 1 9   ? 99.610  77.046  76.605  1.00 25.62 ? 6   VAL A O   1 
ATOM   60   C  CB  . VAL A 1 9   ? 100.033 79.237  74.608  1.00 25.62 ? 6   VAL A CB  1 
ATOM   61   C  CG1 . VAL A 1 9   ? 101.571 79.145  74.408  1.00 23.23 ? 6   VAL A CG1 1 
ATOM   62   C  CG2 . VAL A 1 9   ? 99.435  80.251  73.666  1.00 23.63 ? 6   VAL A CG2 1 
ATOM   63   N  N   . ILE A 1 10  ? 100.340 75.720  74.964  1.00 26.52 ? 7   ILE A N   1 
ATOM   64   C  CA  . ILE A 1 10  ? 100.737 74.652  75.877  1.00 27.67 ? 7   ILE A CA  1 
ATOM   65   C  C   . ILE A 1 10  ? 102.233 74.412  75.657  1.00 26.88 ? 7   ILE A C   1 
ATOM   66   O  O   . ILE A 1 10  ? 102.667 74.385  74.522  1.00 27.18 ? 7   ILE A O   1 
ATOM   67   C  CB  . ILE A 1 10  ? 99.841  73.383  75.649  1.00 27.73 ? 7   ILE A CB  1 
ATOM   68   C  CG1 . ILE A 1 10  ? 100.119 72.315  76.671  1.00 28.43 ? 7   ILE A CG1 1 
ATOM   69   C  CG2 . ILE A 1 10  ? 99.957  72.798  74.198  1.00 25.86 ? 7   ILE A CG2 1 
ATOM   70   C  CD1 . ILE A 1 10  ? 99.610  70.917  76.159  1.00 30.10 ? 7   ILE A CD1 1 
ATOM   71   N  N   . TYR A 1 11  ? 103.037 74.303  76.720  1.00 26.28 ? 8   TYR A N   1 
ATOM   72   C  CA  . TYR A 1 11  ? 104.520 74.199  76.551  1.00 24.89 ? 8   TYR A CA  1 
ATOM   73   C  C   . TYR A 1 11  ? 105.134 73.240  77.575  1.00 25.03 ? 8   TYR A C   1 
ATOM   74   O  O   . TYR A 1 11  ? 104.609 73.063  78.674  1.00 23.33 ? 8   TYR A O   1 
ATOM   75   C  CB  . TYR A 1 11  ? 105.206 75.584  76.639  1.00 23.94 ? 8   TYR A CB  1 
ATOM   76   C  CG  . TYR A 1 11  ? 105.054 76.168  78.012  1.00 23.81 ? 8   TYR A CG  1 
ATOM   77   C  CD1 . TYR A 1 11  ? 106.044 76.006  78.971  1.00 22.48 ? 8   TYR A CD1 1 
ATOM   78   C  CD2 . TYR A 1 11  ? 103.872 76.799  78.389  1.00 22.04 ? 8   TYR A CD2 1 
ATOM   79   C  CE1 . TYR A 1 11  ? 105.861 76.476  80.276  1.00 21.84 ? 8   TYR A CE1 1 
ATOM   80   C  CE2 . TYR A 1 11  ? 103.695 77.288  79.664  1.00 22.58 ? 8   TYR A CE2 1 
ATOM   81   C  CZ  . TYR A 1 11  ? 104.690 77.129  80.599  1.00 22.44 ? 8   TYR A CZ  1 
ATOM   82   O  OH  . TYR A 1 11  ? 104.492 77.594  81.871  1.00 23.95 ? 8   TYR A OH  1 
ATOM   83   N  N   . ASP A 1 12  ? 106.238 72.607  77.180  1.00 25.89 ? 9   ASP A N   1 
ATOM   84   C  CA  . ASP A 1 12  ? 107.164 71.991  78.099  1.00 26.56 ? 9   ASP A CA  1 
ATOM   85   C  C   . ASP A 1 12  ? 108.398 72.889  78.155  1.00 27.76 ? 9   ASP A C   1 
ATOM   86   O  O   . ASP A 1 12  ? 108.579 73.765  77.298  1.00 28.50 ? 9   ASP A O   1 
ATOM   87   C  CB  . ASP A 1 12  ? 107.533 70.589  77.624  1.00 26.76 ? 9   ASP A CB  1 
ATOM   88   C  CG  . ASP A 1 12  ? 108.206 69.751  78.718  1.00 27.37 ? 9   ASP A CG  1 
ATOM   89   O  OD1 . ASP A 1 12  ? 108.355 70.241  79.847  1.00 28.32 ? 9   ASP A OD1 1 
ATOM   90   O  OD2 . ASP A 1 12  ? 108.629 68.614  78.459  1.00 27.68 ? 9   ASP A OD2 1 
ATOM   91   N  N   . THR A 1 13  ? 109.253 72.681  79.150  1.00 28.68 ? 10  THR A N   1 
ATOM   92   C  CA  . THR A 1 13  ? 110.500 73.443  79.270  1.00 29.99 ? 10  THR A CA  1 
ATOM   93   C  C   . THR A 1 13  ? 111.552 72.691  80.140  1.00 31.09 ? 10  THR A C   1 
ATOM   94   O  O   . THR A 1 13  ? 111.206 72.009  81.099  1.00 30.62 ? 10  THR A O   1 
ATOM   95   C  CB  . THR A 1 13  ? 110.196 74.908  79.816  1.00 30.66 ? 10  THR A CB  1 
ATOM   96   O  OG1 . THR A 1 13  ? 111.378 75.702  79.766  1.00 31.16 ? 10  THR A OG1 1 
ATOM   97   C  CG2 . THR A 1 13  ? 109.641 74.890  81.261  1.00 28.25 ? 10  THR A CG2 1 
ATOM   98   N  N   . ARG A 1 14  ? 112.830 72.772  79.794  1.00 32.63 ? 11  ARG A N   1 
ATOM   99   C  CA  . ARG A 1 14  ? 113.857 72.364  80.769  1.00 34.38 ? 11  ARG A CA  1 
ATOM   100  C  C   . ARG A 1 14  ? 114.373 73.458  81.682  1.00 32.49 ? 11  ARG A C   1 
ATOM   101  O  O   . ARG A 1 14  ? 114.484 73.223  82.882  1.00 32.98 ? 11  ARG A O   1 
ATOM   102  C  CB  . ARG A 1 14  ? 115.026 71.527  80.211  1.00 34.76 ? 11  ARG A CB  1 
ATOM   103  C  CG  . ARG A 1 14  ? 115.386 71.650  78.732  1.00 38.13 ? 11  ARG A CG  1 
ATOM   104  C  CD  . ARG A 1 14  ? 116.923 71.314  78.529  1.00 39.41 ? 11  ARG A CD  1 
ATOM   105  N  NE  . ARG A 1 14  ? 117.367 69.905  78.361  1.00 44.00 ? 11  ARG A NE  1 
ATOM   106  C  CZ  . ARG A 1 14  ? 116.639 68.794  78.537  1.00 46.65 ? 11  ARG A CZ  1 
ATOM   107  N  NH1 . ARG A 1 14  ? 115.350 68.851  78.910  1.00 47.58 ? 11  ARG A NH1 1 
ATOM   108  N  NH2 . ARG A 1 14  ? 117.212 67.601  78.323  1.00 45.20 ? 11  ARG A NH2 1 
ATOM   109  N  N   . THR A 1 15  ? 114.650 74.642  81.134  1.00 31.34 ? 12  THR A N   1 
ATOM   110  C  CA  . THR A 1 15  ? 115.269 75.744  81.899  1.00 30.39 ? 12  THR A CA  1 
ATOM   111  C  C   . THR A 1 15  ? 114.417 76.984  82.054  1.00 29.23 ? 12  THR A C   1 
ATOM   112  O  O   . THR A 1 15  ? 114.777 77.887  82.816  1.00 29.20 ? 12  THR A O   1 
ATOM   113  C  CB  . THR A 1 15  ? 116.590 76.227  81.277  1.00 30.43 ? 12  THR A CB  1 
ATOM   114  O  OG1 . THR A 1 15  ? 116.351 76.632  79.912  1.00 31.78 ? 12  THR A OG1 1 
ATOM   115  C  CG2 . THR A 1 15  ? 117.621 75.133  81.343  1.00 30.70 ? 12  THR A CG2 1 
ATOM   116  N  N   . GLY A 1 16  ? 113.323 77.058  81.306  1.00 27.65 ? 13  GLY A N   1 
ATOM   117  C  CA  . GLY A 1 16  ? 112.483 78.233  81.328  1.00 25.81 ? 13  GLY A CA  1 
ATOM   118  C  C   . GLY A 1 16  ? 112.426 78.971  80.008  1.00 25.34 ? 13  GLY A C   1 
ATOM   119  O  O   . GLY A 1 16  ? 111.568 79.820  79.817  1.00 25.67 ? 13  GLY A O   1 
ATOM   120  N  N   . ASN A 1 17  ? 113.324 78.660  79.083  1.00 24.55 ? 14  ASN A N   1 
ATOM   121  C  CA  . ASN A 1 17  ? 113.423 79.429  77.852  1.00 23.57 ? 14  ASN A CA  1 
ATOM   122  C  C   . ASN A 1 17  ? 112.163 79.303  77.049  1.00 24.16 ? 14  ASN A C   1 
ATOM   123  O  O   . ASN A 1 17  ? 111.613 80.325  76.624  1.00 24.66 ? 14  ASN A O   1 
ATOM   124  C  CB  . ASN A 1 17  ? 114.634 79.004  77.046  1.00 22.95 ? 14  ASN A CB  1 
ATOM   125  C  CG  . ASN A 1 17  ? 115.936 79.346  77.741  1.00 24.93 ? 14  ASN A CG  1 
ATOM   126  O  OD1 . ASN A 1 17  ? 116.031 80.337  78.476  1.00 26.19 ? 14  ASN A OD1 1 
ATOM   127  N  ND2 . ASN A 1 17  ? 116.950 78.519  77.524  1.00 24.87 ? 14  ASN A ND2 1 
ATOM   128  N  N   . THR A 1 18  ? 111.685 78.062  76.863  1.00 23.53 ? 15  THR A N   1 
ATOM   129  C  CA  . THR A 1 18  ? 110.438 77.811  76.155  1.00 23.54 ? 15  THR A CA  1 
ATOM   130  C  C   . THR A 1 18  ? 109.217 78.412  76.887  1.00 24.62 ? 15  THR A C   1 
ATOM   131  O  O   . THR A 1 18  ? 108.266 78.838  76.204  1.00 25.04 ? 15  THR A O   1 
ATOM   132  C  CB  . THR A 1 18  ? 110.244 76.305  75.788  1.00 23.78 ? 15  THR A CB  1 
ATOM   133  O  OG1 . THR A 1 18  ? 111.453 75.835  75.175  1.00 24.18 ? 15  THR A OG1 1 
ATOM   134  C  CG2 . THR A 1 18  ? 109.079 76.093  74.777  1.00 20.75 ? 15  THR A CG2 1 
ATOM   135  N  N   . LYS A 1 19  ? 109.266 78.499  78.234  1.00 24.59 ? 16  LYS A N   1 
ATOM   136  C  CA  . LYS A 1 19  ? 108.248 79.221  79.013  1.00 24.98 ? 16  LYS A CA  1 
ATOM   137  C  C   . LYS A 1 19  ? 108.235 80.706  78.646  1.00 26.07 ? 16  LYS A C   1 
ATOM   138  O  O   . LYS A 1 19  ? 107.178 81.269  78.428  1.00 27.20 ? 16  LYS A O   1 
ATOM   139  C  CB  . LYS A 1 19  ? 108.396 79.039  80.550  1.00 25.23 ? 16  LYS A CB  1 
ATOM   140  C  CG  . LYS A 1 19  ? 107.077 79.409  81.368  1.00 24.98 ? 16  LYS A CG  1 
ATOM   141  C  CD  . LYS A 1 19  ? 107.302 79.964  82.764  1.00 23.96 ? 16  LYS A CD  1 
ATOM   142  C  CE  . LYS A 1 19  ? 105.998 80.140  83.566  1.00 25.23 ? 16  LYS A CE  1 
ATOM   143  N  NZ  . LYS A 1 19  ? 106.156 79.918  85.107  1.00 21.47 ? 16  LYS A NZ  1 
ATOM   144  N  N   . LYS A 1 20  ? 109.393 81.342  78.570  1.00 27.41 ? 17  LYS A N   1 
ATOM   145  C  CA  . LYS A 1 20  ? 109.473 82.735  78.130  1.00 29.14 ? 17  LYS A CA  1 
ATOM   146  C  C   . LYS A 1 20  ? 108.927 82.916  76.692  1.00 29.47 ? 17  LYS A C   1 
ATOM   147  O  O   . LYS A 1 20  ? 108.149 83.841  76.440  1.00 29.09 ? 17  LYS A O   1 
ATOM   148  C  CB  . LYS A 1 20  ? 110.898 83.286  78.293  1.00 29.99 ? 17  LYS A CB  1 
ATOM   149  C  CG  . LYS A 1 20  ? 111.215 83.777  79.729  1.00 34.03 ? 17  LYS A CG  1 
ATOM   150  C  CD  . LYS A 1 20  ? 111.341 82.602  80.732  1.00 38.60 ? 17  LYS A CD  1 
ATOM   151  C  CE  . LYS A 1 20  ? 110.772 82.876  82.185  1.00 38.54 ? 17  LYS A CE  1 
ATOM   152  N  NZ  . LYS A 1 20  ? 110.545 81.587  82.986  1.00 38.16 ? 17  LYS A NZ  1 
HETATM 153  N  N   . MSE A 1 21  ? 109.282 82.011  75.770  1.00 29.74 ? 18  MSE A N   1 
HETATM 154  C  CA  . MSE A 1 21  ? 108.642 81.991  74.443  1.00 31.04 ? 18  MSE A CA  1 
HETATM 155  C  C   . MSE A 1 21  ? 107.135 81.856  74.521  1.00 28.67 ? 18  MSE A C   1 
HETATM 156  O  O   . MSE A 1 21  ? 106.434 82.540  73.812  1.00 29.69 ? 18  MSE A O   1 
HETATM 157  C  CB  . MSE A 1 21  ? 109.155 80.853  73.576  1.00 30.16 ? 18  MSE A CB  1 
HETATM 158  C  CG  . MSE A 1 21  ? 110.634 80.869  73.323  1.00 31.87 ? 18  MSE A CG  1 
HETATM 159  SE SE  . MSE A 1 21  ? 111.154 79.422  72.116  1.00 39.05 ? 18  MSE A SE  1 
HETATM 160  C  CE  . MSE A 1 21  ? 110.621 80.254  70.355  1.00 31.42 ? 18  MSE A CE  1 
ATOM   161  N  N   . ALA A 1 22  ? 106.643 80.977  75.382  1.00 27.98 ? 19  ALA A N   1 
ATOM   162  C  CA  . ALA A 1 22  ? 105.204 80.651  75.472  1.00 26.61 ? 19  ALA A CA  1 
ATOM   163  C  C   . ALA A 1 22  ? 104.394 81.844  75.927  1.00 26.59 ? 19  ALA A C   1 
ATOM   164  O  O   . ALA A 1 22  ? 103.256 82.052  75.484  1.00 25.51 ? 19  ALA A O   1 
ATOM   165  C  CB  . ALA A 1 22  ? 105.006 79.511  76.421  1.00 26.18 ? 19  ALA A CB  1 
ATOM   166  N  N   . GLU A 1 23  ? 105.008 82.641  76.809  1.00 26.94 ? 20  GLU A N   1 
ATOM   167  C  CA  . GLU A 1 23  ? 104.351 83.808  77.371  1.00 27.58 ? 20  GLU A CA  1 
ATOM   168  C  C   . GLU A 1 23  ? 104.199 84.868  76.288  1.00 28.18 ? 20  GLU A C   1 
ATOM   169  O  O   . GLU A 1 23  ? 103.187 85.572  76.244  1.00 29.05 ? 20  GLU A O   1 
ATOM   170  C  CB  . GLU A 1 23  ? 105.143 84.353  78.551  1.00 27.14 ? 20  GLU A CB  1 
ATOM   171  C  CG  . GLU A 1 23  ? 104.992 83.572  79.823  1.00 28.49 ? 20  GLU A CG  1 
ATOM   172  C  CD  . GLU A 1 23  ? 106.044 83.943  80.869  1.00 32.28 ? 20  GLU A CD  1 
ATOM   173  O  OE1 . GLU A 1 23  ? 107.035 84.625  80.533  1.00 34.71 ? 20  GLU A OE1 1 
ATOM   174  O  OE2 . GLU A 1 23  ? 105.892 83.553  82.046  1.00 34.89 ? 20  GLU A OE2 1 
ATOM   175  N  N   . LEU A 1 24  ? 105.207 84.965  75.420  1.00 28.40 ? 21  LEU A N   1 
ATOM   176  C  CA  . LEU A 1 24  ? 105.226 85.908  74.310  1.00 28.39 ? 21  LEU A CA  1 
ATOM   177  C  C   . LEU A 1 24  ? 104.283 85.500  73.192  1.00 28.30 ? 21  LEU A C   1 
ATOM   178  O  O   . LEU A 1 24  ? 103.630 86.362  72.593  1.00 28.06 ? 21  LEU A O   1 
ATOM   179  C  CB  . LEU A 1 24  ? 106.641 86.075  73.774  1.00 28.25 ? 21  LEU A CB  1 
ATOM   180  C  CG  . LEU A 1 24  ? 107.550 86.910  74.694  1.00 28.89 ? 21  LEU A CG  1 
ATOM   181  C  CD1 . LEU A 1 24  ? 109.035 86.635  74.413  1.00 27.03 ? 21  LEU A CD1 1 
ATOM   182  C  CD2 . LEU A 1 24  ? 107.216 88.406  74.643  1.00 26.97 ? 21  LEU A CD2 1 
ATOM   183  N  N   . VAL A 1 25  ? 104.197 84.193  72.930  1.00 27.93 ? 22  VAL A N   1 
ATOM   184  C  CA  . VAL A 1 25  ? 103.195 83.657  71.995  1.00 27.29 ? 22  VAL A CA  1 
ATOM   185  C  C   . VAL A 1 25  ? 101.770 84.028  72.471  1.00 27.16 ? 22  VAL A C   1 
ATOM   186  O  O   . VAL A 1 25  ? 100.934 84.501  71.688  1.00 26.96 ? 22  VAL A O   1 
ATOM   187  C  CB  . VAL A 1 25  ? 103.341 82.105  71.794  1.00 27.34 ? 22  VAL A CB  1 
ATOM   188  C  CG1 . VAL A 1 25  ? 102.207 81.550  70.922  1.00 26.04 ? 22  VAL A CG1 1 
ATOM   189  C  CG2 . VAL A 1 25  ? 104.675 81.767  71.189  1.00 25.56 ? 22  VAL A CG2 1 
ATOM   190  N  N   . ALA A 1 26  ? 101.539 83.840  73.768  1.00 26.98 ? 23  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 26  ? 100.243 84.045  74.395  1.00 26.42 ? 23  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 26  ? 99.853  85.515  74.361  1.00 26.70 ? 23  ALA A C   1 
ATOM   193  O  O   . ALA A 1 26  ? 98.683  85.846  74.114  1.00 26.83 ? 23  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 26  ? 100.284 83.560  75.815  1.00 26.35 ? 23  ALA A CB  1 
ATOM   195  N  N   . GLU A 1 27  ? 100.831 86.384  74.642  1.00 26.21 ? 24  GLU A N   1 
ATOM   196  C  CA  . GLU A 1 27  ? 100.687 87.814  74.456  1.00 25.82 ? 24  GLU A CA  1 
ATOM   197  C  C   . GLU A 1 27  ? 100.419 88.154  72.982  1.00 25.43 ? 24  GLU A C   1 
ATOM   198  O  O   . GLU A 1 27  ? 99.578  88.983  72.683  1.00 24.91 ? 24  GLU A O   1 
ATOM   199  C  CB  . GLU A 1 27  ? 101.933 88.529  74.955  1.00 25.96 ? 24  GLU A CB  1 
ATOM   200  C  CG  . GLU A 1 27  ? 101.888 90.031  74.790  1.00 29.24 ? 24  GLU A CG  1 
ATOM   201  C  CD  . GLU A 1 27  ? 103.259 90.674  74.862  1.00 33.52 ? 24  GLU A CD  1 
ATOM   202  O  OE1 . GLU A 1 27  ? 103.531 91.600  74.064  1.00 35.20 ? 24  GLU A OE1 1 
ATOM   203  O  OE2 . GLU A 1 27  ? 104.065 90.247  75.711  1.00 34.95 ? 24  GLU A OE2 1 
ATOM   204  N  N   . GLY A 1 28  ? 101.140 87.509  72.064  1.00 25.78 ? 25  GLY A N   1 
ATOM   205  C  CA  . GLY A 1 28  ? 100.865 87.636  70.632  1.00 25.51 ? 25  GLY A CA  1 
ATOM   206  C  C   . GLY A 1 28  ? 99.387  87.420  70.298  1.00 25.54 ? 25  GLY A C   1 
ATOM   207  O  O   . GLY A 1 28  ? 98.795  88.247  69.611  1.00 25.13 ? 25  GLY A O   1 
ATOM   208  N  N   . ALA A 1 29  ? 98.798  86.320  70.796  1.00 25.63 ? 26  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 29  ? 97.410  85.970  70.509  1.00 26.22 ? 26  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 29  ? 96.419  86.912  71.174  1.00 27.28 ? 26  ALA A C   1 
ATOM   211  O  O   . ALA A 1 29  ? 95.402  87.273  70.582  1.00 27.95 ? 26  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 29  ? 97.125  84.536  70.925  1.00 26.23 ? 26  ALA A CB  1 
ATOM   213  N  N   . ARG A 1 30  ? 96.711  87.313  72.406  1.00 27.69 ? 27  ARG A N   1 
ATOM   214  C  CA  . ARG A 1 30  ? 95.824  88.192  73.151  1.00 28.55 ? 27  ARG A CA  1 
ATOM   215  C  C   . ARG A 1 30  ? 95.738  89.555  72.483  1.00 28.77 ? 27  ARG A C   1 
ATOM   216  O  O   . ARG A 1 30  ? 94.780  90.294  72.706  1.00 28.92 ? 27  ARG A O   1 
ATOM   217  C  CB  . ARG A 1 30  ? 96.273  88.339  74.614  1.00 28.39 ? 27  ARG A CB  1 
ATOM   218  C  CG  . ARG A 1 30  ? 95.979  87.109  75.473  1.00 29.39 ? 27  ARG A CG  1 
ATOM   219  C  CD  . ARG A 1 30  ? 96.101  87.429  76.959  1.00 31.09 ? 27  ARG A CD  1 
ATOM   220  N  NE  . ARG A 1 30  ? 97.420  87.067  77.456  1.00 34.74 ? 27  ARG A NE  1 
ATOM   221  C  CZ  . ARG A 1 30  ? 97.676  85.983  78.194  1.00 37.47 ? 27  ARG A CZ  1 
ATOM   222  N  NH1 . ARG A 1 30  ? 98.930  85.742  78.569  1.00 37.90 ? 27  ARG A NH1 1 
ATOM   223  N  NH2 . ARG A 1 30  ? 96.688  85.144  78.568  1.00 35.87 ? 27  ARG A NH2 1 
ATOM   224  N  N   . SER A 1 31  ? 96.726  89.866  71.639  1.00 29.21 ? 28  SER A N   1 
ATOM   225  C  CA  . SER A 1 31  ? 96.827  91.192  71.024  1.00 29.10 ? 28  SER A CA  1 
ATOM   226  C  C   . SER A 1 31  ? 95.752  91.394  69.952  1.00 29.24 ? 28  SER A C   1 
ATOM   227  O  O   . SER A 1 31  ? 95.386  92.524  69.650  1.00 28.94 ? 28  SER A O   1 
ATOM   228  C  CB  . SER A 1 31  ? 98.242  91.476  70.499  1.00 28.53 ? 28  SER A CB  1 
ATOM   229  O  OG  . SER A 1 31  ? 98.453  90.950  69.189  1.00 29.78 ? 28  SER A OG  1 
ATOM   230  N  N   . LEU A 1 32  ? 95.244  90.291  69.396  1.00 29.70 ? 29  LEU A N   1 
ATOM   231  C  CA  . LEU A 1 32  ? 94.100  90.345  68.484  1.00 29.79 ? 29  LEU A CA  1 
ATOM   232  C  C   . LEU A 1 32  ? 92.826  90.423  69.305  1.00 30.39 ? 29  LEU A C   1 
ATOM   233  O  O   . LEU A 1 32  ? 92.435  89.425  69.903  1.00 31.58 ? 29  LEU A O   1 
ATOM   234  C  CB  . LEU A 1 32  ? 94.024  89.080  67.624  1.00 28.77 ? 29  LEU A CB  1 
ATOM   235  C  CG  . LEU A 1 32  ? 93.545  89.125  66.154  1.00 27.22 ? 29  LEU A CG  1 
ATOM   236  C  CD1 . LEU A 1 32  ? 92.554  87.997  65.882  1.00 24.03 ? 29  LEU A CD1 1 
ATOM   237  C  CD2 . LEU A 1 32  ? 93.002  90.470  65.682  1.00 18.72 ? 29  LEU A CD2 1 
ATOM   238  N  N   . GLU A 1 33  ? 92.177  91.583  69.327  1.00 30.83 ? 30  GLU A N   1 
ATOM   239  C  CA  . GLU A 1 33  ? 90.930  91.767  70.058  1.00 31.32 ? 30  GLU A CA  1 
ATOM   240  C  C   . GLU A 1 33  ? 89.923  90.630  69.846  1.00 30.48 ? 30  GLU A C   1 
ATOM   241  O  O   . GLU A 1 33  ? 89.720  90.160  68.721  1.00 29.99 ? 30  GLU A O   1 
ATOM   242  C  CB  . GLU A 1 33  ? 90.293  93.098  69.672  1.00 31.29 ? 30  GLU A CB  1 
ATOM   243  C  CG  . GLU A 1 33  ? 90.434  94.216  70.727  1.00 33.54 ? 30  GLU A CG  1 
ATOM   244  C  CD  . GLU A 1 33  ? 90.253  95.627  70.122  1.00 33.81 ? 30  GLU A CD  1 
ATOM   245  O  OE1 . GLU A 1 33  ? 91.007  95.979  69.179  1.00 35.66 ? 30  GLU A OE1 1 
ATOM   246  O  OE2 . GLU A 1 33  ? 89.352  96.389  70.583  1.00 39.32 ? 30  GLU A OE2 1 
ATOM   247  N  N   . GLY A 1 34  ? 89.296  90.202  70.942  1.00 30.12 ? 31  GLY A N   1 
ATOM   248  C  CA  . GLY A 1 34  ? 88.279  89.150  70.900  1.00 29.54 ? 31  GLY A CA  1 
ATOM   249  C  C   . GLY A 1 34  ? 88.859  87.754  70.721  1.00 29.08 ? 31  GLY A C   1 
ATOM   250  O  O   . GLY A 1 34  ? 88.189  86.854  70.203  1.00 29.21 ? 31  GLY A O   1 
ATOM   251  N  N   . THR A 1 35  ? 90.118  87.591  71.120  1.00 28.15 ? 32  THR A N   1 
ATOM   252  C  CA  . THR A 1 35  ? 90.740  86.294  71.233  1.00 27.46 ? 32  THR A CA  1 
ATOM   253  C  C   . THR A 1 35  ? 90.987  86.019  72.702  1.00 28.07 ? 32  THR A C   1 
ATOM   254  O  O   . THR A 1 35  ? 91.550  86.842  73.439  1.00 27.46 ? 32  THR A O   1 
ATOM   255  C  CB  . THR A 1 35  ? 92.072  86.219  70.470  1.00 27.50 ? 32  THR A CB  1 
ATOM   256  O  OG1 . THR A 1 35  ? 91.863  86.592  69.102  1.00 26.11 ? 32  THR A OG1 1 
ATOM   257  C  CG2 . THR A 1 35  ? 92.668  84.807  70.545  1.00 25.75 ? 32  THR A CG2 1 
ATOM   258  N  N   . GLU A 1 36  ? 90.550  84.839  73.115  1.00 28.89 ? 33  GLU A N   1 
ATOM   259  C  CA  . GLU A 1 36  ? 90.743  84.346  74.460  1.00 29.17 ? 33  GLU A CA  1 
ATOM   260  C  C   . GLU A 1 36  ? 91.892  83.306  74.498  1.00 29.01 ? 33  GLU A C   1 
ATOM   261  O  O   . GLU A 1 36  ? 91.966  82.418  73.642  1.00 29.07 ? 33  GLU A O   1 
ATOM   262  C  CB  . GLU A 1 36  ? 89.451  83.721  74.904  1.00 28.51 ? 33  GLU A CB  1 
ATOM   263  C  CG  . GLU A 1 36  ? 89.433  83.455  76.341  1.00 31.31 ? 33  GLU A CG  1 
ATOM   264  C  CD  . GLU A 1 36  ? 88.130  82.872  76.771  1.00 33.04 ? 33  GLU A CD  1 
ATOM   265  O  OE1 . GLU A 1 36  ? 87.369  82.390  75.892  1.00 33.16 ? 33  GLU A OE1 1 
ATOM   266  O  OE2 . GLU A 1 36  ? 87.883  82.898  77.988  1.00 32.76 ? 33  GLU A OE2 1 
ATOM   267  N  N   . VAL A 1 37  ? 92.766  83.406  75.502  1.00 28.93 ? 34  VAL A N   1 
ATOM   268  C  CA  . VAL A 1 37  ? 93.975  82.569  75.564  1.00 28.75 ? 34  VAL A CA  1 
ATOM   269  C  C   . VAL A 1 37  ? 94.095  81.776  76.886  1.00 28.39 ? 34  VAL A C   1 
ATOM   270  O  O   . VAL A 1 37  ? 93.850  82.305  77.957  1.00 27.43 ? 34  VAL A O   1 
ATOM   271  C  CB  . VAL A 1 37  ? 95.257  83.431  75.275  1.00 28.79 ? 34  VAL A CB  1 
ATOM   272  C  CG1 . VAL A 1 37  ? 96.558  82.610  75.379  1.00 28.14 ? 34  VAL A CG1 1 
ATOM   273  C  CG2 . VAL A 1 37  ? 95.143  84.079  73.903  1.00 29.58 ? 34  VAL A CG2 1 
ATOM   274  N  N   . ARG A 1 38  ? 94.453  80.499  76.789  1.00 27.82 ? 35  ARG A N   1 
ATOM   275  C  CA  . ARG A 1 38  ? 94.801  79.716  77.971  1.00 27.65 ? 35  ARG A CA  1 
ATOM   276  C  C   . ARG A 1 38  ? 96.283  79.424  77.809  1.00 27.17 ? 35  ARG A C   1 
ATOM   277  O  O   . ARG A 1 38  ? 96.691  79.003  76.730  1.00 27.38 ? 35  ARG A O   1 
ATOM   278  C  CB  . ARG A 1 38  ? 93.974  78.420  78.050  1.00 27.03 ? 35  ARG A CB  1 
ATOM   279  C  CG  . ARG A 1 38  ? 92.946  78.445  79.105  1.00 28.06 ? 35  ARG A CG  1 
ATOM   280  C  CD  . ARG A 1 38  ? 91.515  78.124  78.660  1.00 30.23 ? 35  ARG A CD  1 
ATOM   281  N  NE  . ARG A 1 38  ? 91.112  76.763  78.991  1.00 30.64 ? 35  ARG A NE  1 
ATOM   282  C  CZ  . ARG A 1 38  ? 89.874  76.370  79.278  1.00 30.53 ? 35  ARG A CZ  1 
ATOM   283  N  NH1 . ARG A 1 38  ? 88.863  77.220  79.309  1.00 30.31 ? 35  ARG A NH1 1 
ATOM   284  N  NH2 . ARG A 1 38  ? 89.654  75.098  79.565  1.00 33.31 ? 35  ARG A NH2 1 
ATOM   285  N  N   . LEU A 1 39  ? 97.084  79.693  78.848  1.00 26.60 ? 36  LEU A N   1 
ATOM   286  C  CA  . LEU A 1 39  ? 98.529  79.339  78.872  1.00 25.66 ? 36  LEU A CA  1 
ATOM   287  C  C   . LEU A 1 39  ? 98.793  78.239  79.910  1.00 26.48 ? 36  LEU A C   1 
ATOM   288  O  O   . LEU A 1 39  ? 98.555  78.434  81.117  1.00 25.94 ? 36  LEU A O   1 
ATOM   289  C  CB  . LEU A 1 39  ? 99.359  80.584  79.169  1.00 25.03 ? 36  LEU A CB  1 
ATOM   290  C  CG  . LEU A 1 39  ? 100.875 80.521  79.362  1.00 25.76 ? 36  LEU A CG  1 
ATOM   291  C  CD1 . LEU A 1 39  ? 101.632 79.937  78.123  1.00 22.14 ? 36  LEU A CD1 1 
ATOM   292  C  CD2 . LEU A 1 39  ? 101.411 81.906  79.745  1.00 23.77 ? 36  LEU A CD2 1 
ATOM   293  N  N   . LYS A 1 40  ? 99.241  77.066  79.460  1.00 27.32 ? 37  LYS A N   1 
ATOM   294  C  CA  . LYS A 1 40  ? 99.510  75.952  80.411  1.00 28.76 ? 37  LYS A CA  1 
ATOM   295  C  C   . LYS A 1 40  ? 100.857 75.278  80.199  1.00 28.77 ? 37  LYS A C   1 
ATOM   296  O  O   . LYS A 1 40  ? 101.262 75.085  79.083  1.00 29.73 ? 37  LYS A O   1 
ATOM   297  C  CB  . LYS A 1 40  ? 98.423  74.871  80.338  1.00 29.40 ? 37  LYS A CB  1 
ATOM   298  C  CG  . LYS A 1 40  ? 96.978  75.378  80.319  1.00 30.88 ? 37  LYS A CG  1 
ATOM   299  C  CD  . LYS A 1 40  ? 96.284  75.327  81.657  1.00 31.01 ? 37  LYS A CD  1 
ATOM   300  C  CE  . LYS A 1 40  ? 94.867  75.967  81.525  1.00 33.89 ? 37  LYS A CE  1 
ATOM   301  N  NZ  . LYS A 1 40  ? 93.815  75.632  82.605  1.00 32.94 ? 37  LYS A NZ  1 
ATOM   302  N  N   . HIS A 1 41  ? 101.547 74.930  81.277  1.00 29.12 ? 38  HIS A N   1 
ATOM   303  C  CA  . HIS A 1 41  ? 102.629 73.949  81.216  1.00 29.35 ? 38  HIS A CA  1 
ATOM   304  C  C   . HIS A 1 41  ? 101.981 72.550  80.942  1.00 29.75 ? 38  HIS A C   1 
ATOM   305  O  O   . HIS A 1 41  ? 100.844 72.288  81.362  1.00 28.90 ? 38  HIS A O   1 
ATOM   306  C  CB  . HIS A 1 41  ? 103.450 73.988  82.523  1.00 28.62 ? 38  HIS A CB  1 
ATOM   307  C  CG  . HIS A 1 41  ? 104.562 72.987  82.581  1.00 29.94 ? 38  HIS A CG  1 
ATOM   308  N  ND1 . HIS A 1 41  ? 105.771 73.173  81.946  1.00 33.51 ? 38  HIS A ND1 1 
ATOM   309  C  CD2 . HIS A 1 41  ? 104.652 71.788  83.203  1.00 32.51 ? 38  HIS A CD2 1 
ATOM   310  C  CE1 . HIS A 1 41  ? 106.549 72.123  82.155  1.00 32.98 ? 38  HIS A CE1 1 
ATOM   311  N  NE2 . HIS A 1 41  ? 105.891 71.265  82.911  1.00 33.66 ? 38  HIS A NE2 1 
ATOM   312  N  N   . VAL A 1 42  ? 102.689 71.678  80.225  1.00 29.67 ? 39  VAL A N   1 
ATOM   313  C  CA  . VAL A 1 42  ? 102.202 70.323  79.953  1.00 30.54 ? 39  VAL A CA  1 
ATOM   314  C  C   . VAL A 1 42  ? 101.673 69.533  81.191  1.00 31.77 ? 39  VAL A C   1 
ATOM   315  O  O   . VAL A 1 42  ? 100.665 68.826  81.070  1.00 31.55 ? 39  VAL A O   1 
ATOM   316  C  CB  . VAL A 1 42  ? 103.228 69.477  79.140  1.00 29.66 ? 39  VAL A CB  1 
ATOM   317  C  CG1 . VAL A 1 42  ? 104.481 69.217  79.919  1.00 29.45 ? 39  VAL A CG1 1 
ATOM   318  C  CG2 . VAL A 1 42  ? 102.627 68.174  78.730  1.00 29.85 ? 39  VAL A CG2 1 
ATOM   319  N  N   . ASP A 1 43  ? 102.336 69.657  82.354  1.00 32.60 ? 40  ASP A N   1 
ATOM   320  C  CA  . ASP A 1 43  ? 101.917 68.967  83.588  1.00 33.88 ? 40  ASP A CA  1 
ATOM   321  C  C   . ASP A 1 43  ? 100.609 69.537  84.139  1.00 34.22 ? 40  ASP A C   1 
ATOM   322  O  O   . ASP A 1 43  ? 99.933  68.879  84.927  1.00 34.57 ? 40  ASP A O   1 
ATOM   323  C  CB  . ASP A 1 43  ? 102.924 69.153  84.726  1.00 34.90 ? 40  ASP A CB  1 
ATOM   324  C  CG  . ASP A 1 43  ? 104.292 68.553  84.454  1.00 37.11 ? 40  ASP A CG  1 
ATOM   325  O  OD1 . ASP A 1 43  ? 104.422 67.534  83.724  1.00 39.47 ? 40  ASP A OD1 1 
ATOM   326  O  OD2 . ASP A 1 43  ? 105.247 69.134  85.024  1.00 40.65 ? 40  ASP A OD2 1 
ATOM   327  N  N   . GLU A 1 44  ? 100.291 70.769  83.754  1.00 33.94 ? 41  GLU A N   1 
ATOM   328  C  CA  . GLU A 1 44  ? 99.083  71.479  84.152  1.00 34.75 ? 41  GLU A CA  1 
ATOM   329  C  C   . GLU A 1 44  ? 97.907  71.137  83.234  1.00 33.78 ? 41  GLU A C   1 
ATOM   330  O  O   . GLU A 1 44  ? 96.772  71.138  83.666  1.00 34.80 ? 41  GLU A O   1 
ATOM   331  C  CB  . GLU A 1 44  ? 99.376  72.970  83.980  1.00 34.98 ? 41  GLU A CB  1 
ATOM   332  C  CG  . GLU A 1 44  ? 99.018  73.918  85.087  1.00 36.95 ? 41  GLU A CG  1 
ATOM   333  C  CD  . GLU A 1 44  ? 99.181  75.417  84.650  1.00 38.04 ? 41  GLU A CD  1 
ATOM   334  O  OE1 . GLU A 1 44  ? 100.124 75.758  83.853  1.00 37.07 ? 41  GLU A OE1 1 
ATOM   335  O  OE2 . GLU A 1 44  ? 98.355  76.250  85.138  1.00 41.62 ? 41  GLU A OE2 1 
ATOM   336  N  N   . ALA A 1 45  ? 98.191  70.873  81.959  1.00 32.99 ? 42  ALA A N   1 
ATOM   337  C  CA  . ALA A 1 45  ? 97.188  70.809  80.885  1.00 32.06 ? 42  ALA A CA  1 
ATOM   338  C  C   . ALA A 1 45  ? 96.270  69.591  80.908  1.00 31.54 ? 42  ALA A C   1 
ATOM   339  O  O   . ALA A 1 45  ? 96.642  68.524  81.405  1.00 31.21 ? 42  ALA A O   1 
ATOM   340  C  CB  . ALA A 1 45  ? 97.865  70.916  79.524  1.00 32.08 ? 42  ALA A CB  1 
ATOM   341  N  N   . THR A 1 46  ? 95.068  69.760  80.362  1.00 30.75 ? 43  THR A N   1 
ATOM   342  C  CA  . THR A 1 46  ? 94.086  68.678  80.341  1.00 30.51 ? 43  THR A CA  1 
ATOM   343  C  C   . THR A 1 46  ? 93.547  68.449  78.928  1.00 30.46 ? 43  THR A C   1 
ATOM   344  O  O   . THR A 1 46  ? 93.624  69.326  78.072  1.00 30.74 ? 43  THR A O   1 
ATOM   345  C  CB  . THR A 1 46  ? 92.886  68.972  81.273  1.00 30.29 ? 43  THR A CB  1 
ATOM   346  O  OG1 . THR A 1 46  ? 92.278  70.205  80.871  1.00 31.69 ? 43  THR A OG1 1 
ATOM   347  C  CG2 . THR A 1 46  ? 93.317  69.096  82.724  1.00 29.08 ? 43  THR A CG2 1 
ATOM   348  N  N   . LYS A 1 47  ? 92.981  67.271  78.701  1.00 30.35 ? 44  LYS A N   1 
ATOM   349  C  CA  . LYS A 1 47  ? 92.292  66.987  77.453  1.00 30.06 ? 44  LYS A CA  1 
ATOM   350  C  C   . LYS A 1 47  ? 91.152  67.988  77.207  1.00 29.64 ? 44  LYS A C   1 
ATOM   351  O  O   . LYS A 1 47  ? 90.813  68.244  76.079  1.00 29.73 ? 44  LYS A O   1 
ATOM   352  C  CB  . LYS A 1 47  ? 91.843  65.501  77.366  1.00 29.73 ? 44  LYS A CB  1 
ATOM   353  C  CG  . LYS A 1 47  ? 90.573  65.096  78.140  1.00 30.15 ? 44  LYS A CG  1 
ATOM   354  C  CD  . LYS A 1 47  ? 90.332  63.564  78.035  1.00 30.05 ? 44  LYS A CD  1 
ATOM   355  C  CE  . LYS A 1 47  ? 88.856  63.135  78.201  1.00 30.36 ? 44  LYS A CE  1 
ATOM   356  N  NZ  . LYS A 1 47  ? 88.257  63.194  79.581  1.00 28.89 ? 44  LYS A NZ  1 
ATOM   357  N  N   . GLU A 1 48  ? 90.607  68.577  78.265  1.00 30.08 ? 45  GLU A N   1 
ATOM   358  C  CA  . GLU A 1 48  ? 89.526  69.569  78.147  1.00 30.63 ? 45  GLU A CA  1 
ATOM   359  C  C   . GLU A 1 48  ? 89.984  70.931  77.614  1.00 30.38 ? 45  GLU A C   1 
ATOM   360  O  O   . GLU A 1 48  ? 89.226  71.612  76.925  1.00 30.23 ? 45  GLU A O   1 
ATOM   361  C  CB  . GLU A 1 48  ? 88.788  69.755  79.489  1.00 30.99 ? 45  GLU A CB  1 
ATOM   362  C  CG  . GLU A 1 48  ? 87.810  68.628  79.851  1.00 33.08 ? 45  GLU A CG  1 
ATOM   363  C  CD  . GLU A 1 48  ? 88.500  67.369  80.400  1.00 35.87 ? 45  GLU A CD  1 
ATOM   364  O  OE1 . GLU A 1 48  ? 89.485  67.501  81.161  1.00 37.37 ? 45  GLU A OE1 1 
ATOM   365  O  OE2 . GLU A 1 48  ? 88.049  66.244  80.081  1.00 37.60 ? 45  GLU A OE2 1 
ATOM   366  N  N   . ASP A 1 49  ? 91.219  71.317  77.939  1.00 30.36 ? 46  ASP A N   1 
ATOM   367  C  CA  . ASP A 1 49  ? 91.862  72.504  77.364  1.00 30.10 ? 46  ASP A CA  1 
ATOM   368  C  C   . ASP A 1 49  ? 91.921  72.428  75.870  1.00 29.89 ? 46  ASP A C   1 
ATOM   369  O  O   . ASP A 1 49  ? 91.747  73.446  75.195  1.00 30.13 ? 46  ASP A O   1 
ATOM   370  C  CB  . ASP A 1 49  ? 93.294  72.665  77.882  1.00 29.98 ? 46  ASP A CB  1 
ATOM   371  C  CG  . ASP A 1 49  ? 93.337  73.070  79.335  1.00 30.92 ? 46  ASP A CG  1 
ATOM   372  O  OD1 . ASP A 1 49  ? 92.423  73.841  79.717  1.00 31.70 ? 46  ASP A OD1 1 
ATOM   373  O  OD2 . ASP A 1 49  ? 94.248  72.606  80.082  1.00 30.20 ? 46  ASP A OD2 1 
ATOM   374  N  N   . VAL A 1 50  ? 92.173  71.218  75.363  1.00 29.68 ? 47  VAL A N   1 
ATOM   375  C  CA  . VAL A 1 50  ? 92.402  70.992  73.941  1.00 29.26 ? 47  VAL A CA  1 
ATOM   376  C  C   . VAL A 1 50  ? 91.063  71.008  73.232  1.00 28.95 ? 47  VAL A C   1 
ATOM   377  O  O   . VAL A 1 50  ? 90.905  71.645  72.182  1.00 30.04 ? 47  VAL A O   1 
ATOM   378  C  CB  . VAL A 1 50  ? 93.229  69.668  73.691  1.00 29.93 ? 47  VAL A CB  1 
ATOM   379  C  CG1 . VAL A 1 50  ? 93.222  69.263  72.226  1.00 28.27 ? 47  VAL A CG1 1 
ATOM   380  C  CG2 . VAL A 1 50  ? 94.676  69.839  74.198  1.00 28.77 ? 47  VAL A CG2 1 
ATOM   381  N  N   . LEU A 1 51  ? 90.089  70.344  73.836  1.00 27.78 ? 48  LEU A N   1 
ATOM   382  C  CA  . LEU A 1 51  ? 88.698  70.403  73.386  1.00 26.96 ? 48  LEU A CA  1 
ATOM   383  C  C   . LEU A 1 51  ? 88.135  71.829  73.328  1.00 26.84 ? 48  LEU A C   1 
ATOM   384  O  O   . LEU A 1 51  ? 87.344  72.167  72.458  1.00 26.90 ? 48  LEU A O   1 
ATOM   385  C  CB  . LEU A 1 51  ? 87.833  69.551  74.310  1.00 26.26 ? 48  LEU A CB  1 
ATOM   386  C  CG  . LEU A 1 51  ? 88.001  68.049  74.146  1.00 25.34 ? 48  LEU A CG  1 
ATOM   387  C  CD1 . LEU A 1 51  ? 87.417  67.327  75.368  1.00 23.48 ? 48  LEU A CD1 1 
ATOM   388  C  CD2 . LEU A 1 51  ? 87.321  67.602  72.842  1.00 22.72 ? 48  LEU A CD2 1 
ATOM   389  N  N   . TRP A 1 52  ? 88.541  72.654  74.280  1.00 26.69 ? 49  TRP A N   1 
ATOM   390  C  CA  . TRP A 1 52  ? 88.150  74.047  74.322  1.00 26.38 ? 49  TRP A CA  1 
ATOM   391  C  C   . TRP A 1 52  ? 88.788  74.838  73.176  1.00 26.93 ? 49  TRP A C   1 
ATOM   392  O  O   . TRP A 1 52  ? 88.130  75.684  72.589  1.00 28.25 ? 49  TRP A O   1 
ATOM   393  C  CB  . TRP A 1 52  ? 88.529  74.602  75.698  1.00 25.58 ? 49  TRP A CB  1 
ATOM   394  C  CG  . TRP A 1 52  ? 88.368  76.057  75.870  1.00 25.34 ? 49  TRP A CG  1 
ATOM   395  C  CD1 . TRP A 1 52  ? 87.235  76.714  76.284  1.00 23.93 ? 49  TRP A CD1 1 
ATOM   396  C  CD2 . TRP A 1 52  ? 89.373  77.069  75.650  1.00 23.86 ? 49  TRP A CD2 1 
ATOM   397  N  NE1 . TRP A 1 52  ? 87.479  78.071  76.334  1.00 25.17 ? 49  TRP A NE1 1 
ATOM   398  C  CE2 . TRP A 1 52  ? 88.779  78.316  75.951  1.00 24.54 ? 49  TRP A CE2 1 
ATOM   399  C  CE3 . TRP A 1 52  ? 90.724  77.038  75.244  1.00 22.87 ? 49  TRP A CE3 1 
ATOM   400  C  CZ2 . TRP A 1 52  ? 89.488  79.533  75.851  1.00 24.19 ? 49  TRP A CZ2 1 
ATOM   401  C  CZ3 . TRP A 1 52  ? 91.427  78.243  75.154  1.00 22.54 ? 49  TRP A CZ3 1 
ATOM   402  C  CH2 . TRP A 1 52  ? 90.807  79.471  75.448  1.00 23.10 ? 49  TRP A CH2 1 
ATOM   403  N  N   . ALA A 1 53  ? 90.040  74.538  72.829  1.00 27.54 ? 50  ALA A N   1 
ATOM   404  C  CA  . ALA A 1 53  ? 90.831  75.340  71.875  1.00 28.01 ? 50  ALA A CA  1 
ATOM   405  C  C   . ALA A 1 53  ? 90.364  75.288  70.419  1.00 28.86 ? 50  ALA A C   1 
ATOM   406  O  O   . ALA A 1 53  ? 90.045  74.216  69.891  1.00 29.80 ? 50  ALA A O   1 
ATOM   407  C  CB  . ALA A 1 53  ? 92.300  74.952  71.948  1.00 27.26 ? 50  ALA A CB  1 
ATOM   408  N  N   . ASP A 1 54  ? 90.334  76.446  69.762  1.00 28.99 ? 51  ASP A N   1 
ATOM   409  C  CA  . ASP A 1 54  ? 90.180  76.482  68.302  1.00 29.05 ? 51  ASP A CA  1 
ATOM   410  C  C   . ASP A 1 54  ? 91.537  76.319  67.649  1.00 28.69 ? 51  ASP A C   1 
ATOM   411  O  O   . ASP A 1 54  ? 91.657  75.655  66.631  1.00 29.23 ? 51  ASP A O   1 
ATOM   412  C  CB  . ASP A 1 54  ? 89.535  77.797  67.845  1.00 28.78 ? 51  ASP A CB  1 
ATOM   413  C  CG  . ASP A 1 54  ? 88.115  77.935  68.338  1.00 29.69 ? 51  ASP A CG  1 
ATOM   414  O  OD1 . ASP A 1 54  ? 87.374  76.943  68.196  1.00 32.16 ? 51  ASP A OD1 1 
ATOM   415  O  OD2 . ASP A 1 54  ? 87.733  79.010  68.865  1.00 28.43 ? 51  ASP A OD2 1 
ATOM   416  N  N   . GLY A 1 55  ? 92.542  76.956  68.256  1.00 28.22 ? 52  GLY A N   1 
ATOM   417  C  CA  . GLY A 1 55  ? 93.910  76.969  67.800  1.00 27.07 ? 52  GLY A CA  1 
ATOM   418  C  C   . GLY A 1 55  ? 94.841  76.658  68.952  1.00 26.87 ? 52  GLY A C   1 
ATOM   419  O  O   . GLY A 1 55  ? 94.546  77.002  70.099  1.00 25.95 ? 52  GLY A O   1 
ATOM   420  N  N   . LEU A 1 56  ? 95.942  75.969  68.628  1.00 26.81 ? 53  LEU A N   1 
ATOM   421  C  CA  . LEU A 1 56  ? 96.977  75.558  69.589  1.00 27.82 ? 53  LEU A CA  1 
ATOM   422  C  C   . LEU A 1 56  ? 98.368  75.997  69.150  1.00 27.22 ? 53  LEU A C   1 
ATOM   423  O  O   . LEU A 1 56  ? 98.727  75.823  67.984  1.00 27.66 ? 53  LEU A O   1 
ATOM   424  C  CB  . LEU A 1 56  ? 97.037  74.030  69.723  1.00 28.40 ? 53  LEU A CB  1 
ATOM   425  C  CG  . LEU A 1 56  ? 95.852  73.295  70.321  1.00 30.69 ? 53  LEU A CG  1 
ATOM   426  C  CD1 . LEU A 1 56  ? 94.773  73.079  69.218  1.00 31.59 ? 53  LEU A CD1 1 
ATOM   427  C  CD2 . LEU A 1 56  ? 96.349  71.987  70.892  1.00 30.49 ? 53  LEU A CD2 1 
ATOM   428  N  N   . ALA A 1 57  ? 99.153  76.541  70.083  1.00 26.43 ? 54  ALA A N   1 
ATOM   429  C  CA  . ALA A 1 57  ? 100.597 76.656  69.887  1.00 25.51 ? 54  ALA A CA  1 
ATOM   430  C  C   . ALA A 1 57  ? 101.252 75.687  70.855  1.00 25.09 ? 54  ALA A C   1 
ATOM   431  O  O   . ALA A 1 57  ? 100.946 75.675  72.032  1.00 25.46 ? 54  ALA A O   1 
ATOM   432  C  CB  . ALA A 1 57  ? 101.076 78.096  70.112  1.00 25.17 ? 54  ALA A CB  1 
ATOM   433  N  N   . VAL A 1 58  ? 102.111 74.823  70.346  1.00 25.48 ? 55  VAL A N   1 
ATOM   434  C  CA  . VAL A 1 58  ? 102.702 73.794  71.182  1.00 24.95 ? 55  VAL A CA  1 
ATOM   435  C  C   . VAL A 1 58  ? 104.203 74.028  71.180  1.00 24.77 ? 55  VAL A C   1 
ATOM   436  O  O   . VAL A 1 58  ? 104.808 74.042  70.129  1.00 24.85 ? 55  VAL A O   1 
ATOM   437  C  CB  . VAL A 1 58  ? 102.357 72.368  70.631  1.00 25.39 ? 55  VAL A CB  1 
ATOM   438  C  CG1 . VAL A 1 58  ? 103.085 71.274  71.442  1.00 24.69 ? 55  VAL A CG1 1 
ATOM   439  C  CG2 . VAL A 1 58  ? 100.826 72.134  70.554  1.00 22.79 ? 55  VAL A CG2 1 
ATOM   440  N  N   . GLY A 1 59  ? 104.797 74.252  72.346  1.00 24.60 ? 56  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 59  ? 106.223 74.553  72.420  1.00 23.18 ? 56  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 59  ? 106.987 73.538  73.212  1.00 23.64 ? 56  GLY A C   1 
ATOM   443  O  O   . GLY A 1 59  ? 106.475 72.961  74.176  1.00 23.36 ? 56  GLY A O   1 
ATOM   444  N  N   . SER A 1 60  ? 108.217 73.288  72.801  1.00 23.47 ? 57  SER A N   1 
ATOM   445  C  CA  . SER A 1 60  ? 109.042 72.359  73.519  1.00 23.41 ? 57  SER A CA  1 
ATOM   446  C  C   . SER A 1 60  ? 110.474 72.813  73.412  1.00 23.72 ? 57  SER A C   1 
ATOM   447  O  O   . SER A 1 60  ? 110.852 73.396  72.388  1.00 25.14 ? 57  SER A O   1 
ATOM   448  C  CB  . SER A 1 60  ? 108.934 70.988  72.869  1.00 24.23 ? 57  SER A CB  1 
ATOM   449  O  OG  . SER A 1 60  ? 109.808 70.023  73.473  1.00 24.42 ? 57  SER A OG  1 
ATOM   450  N  N   . PRO A 1 61  ? 111.304 72.504  74.428  1.00 22.50 ? 58  PRO A N   1 
ATOM   451  C  CA  . PRO A 1 61  ? 112.742 72.634  74.189  1.00 22.05 ? 58  PRO A CA  1 
ATOM   452  C  C   . PRO A 1 61  ? 113.141 71.676  73.064  1.00 22.48 ? 58  PRO A C   1 
ATOM   453  O  O   . PRO A 1 61  ? 112.487 70.640  72.867  1.00 22.54 ? 58  PRO A O   1 
ATOM   454  C  CB  . PRO A 1 61  ? 113.359 72.180  75.526  1.00 22.37 ? 58  PRO A CB  1 
ATOM   455  C  CG  . PRO A 1 61  ? 112.273 71.330  76.204  1.00 22.30 ? 58  PRO A CG  1 
ATOM   456  C  CD  . PRO A 1 61  ? 110.988 71.994  75.775  1.00 22.17 ? 58  PRO A CD  1 
ATOM   457  N  N   . THR A 1 62  ? 114.186 71.994  72.310  1.00 22.74 ? 59  THR A N   1 
ATOM   458  C  CA  . THR A 1 62  ? 114.715 71.032  71.356  1.00 22.77 ? 59  THR A CA  1 
ATOM   459  C  C   . THR A 1 62  ? 115.458 69.980  72.122  1.00 23.18 ? 59  THR A C   1 
ATOM   460  O  O   . THR A 1 62  ? 116.523 70.241  72.633  1.00 22.70 ? 59  THR A O   1 
ATOM   461  C  CB  . THR A 1 62  ? 115.704 71.707  70.376  1.00 23.05 ? 59  THR A CB  1 
ATOM   462  O  OG1 . THR A 1 62  ? 114.989 72.688  69.632  1.00 25.80 ? 59  THR A OG1 1 
ATOM   463  C  CG2 . THR A 1 62  ? 116.326 70.680  69.381  1.00 21.10 ? 59  THR A CG2 1 
ATOM   464  N  N   . ASN A 1 63  ? 114.897 68.792  72.218  1.00 25.22 ? 60  ASN A N   1 
ATOM   465  C  CA  . ASN A 1 63  ? 115.563 67.706  72.941  1.00 26.85 ? 60  ASN A CA  1 
ATOM   466  C  C   . ASN A 1 63  ? 115.953 66.579  71.968  1.00 28.28 ? 60  ASN A C   1 
ATOM   467  O  O   . ASN A 1 63  ? 115.085 65.833  71.480  1.00 28.42 ? 60  ASN A O   1 
ATOM   468  C  CB  . ASN A 1 63  ? 114.690 67.164  74.092  1.00 26.60 ? 60  ASN A CB  1 
ATOM   469  C  CG  . ASN A 1 63  ? 114.526 68.160  75.269  1.00 26.68 ? 60  ASN A CG  1 
ATOM   470  O  OD1 . ASN A 1 63  ? 113.662 67.971  76.129  1.00 26.59 ? 60  ASN A OD1 1 
ATOM   471  N  ND2 . ASN A 1 63  ? 115.357 69.184  75.321  1.00 25.45 ? 60  ASN A ND2 1 
HETATM 472  N  N   . MSE A 1 64  ? 117.252 66.457  71.708  1.00 28.91 ? 61  MSE A N   1 
HETATM 473  C  CA  . MSE A 1 64  ? 117.769 65.538  70.717  1.00 30.91 ? 61  MSE A CA  1 
HETATM 474  C  C   . MSE A 1 64  ? 117.080 65.768  69.368  1.00 29.33 ? 61  MSE A C   1 
HETATM 475  O  O   . MSE A 1 64  ? 116.784 64.830  68.642  1.00 28.83 ? 61  MSE A O   1 
HETATM 476  C  CB  . MSE A 1 64  ? 117.657 64.083  71.177  1.00 34.06 ? 61  MSE A CB  1 
HETATM 477  C  CG  . MSE A 1 64  ? 118.288 63.789  72.545  1.00 41.66 ? 61  MSE A CG  1 
HETATM 478  SE SE  . MSE A 1 64  ? 120.274 64.328  72.731  1.00 69.60 ? 61  MSE A SE  1 
HETATM 479  C  CE  . MSE A 1 64  ? 120.226 66.460  73.120  1.00 51.55 ? 61  MSE A CE  1 
ATOM   480  N  N   . GLY A 1 65  ? 116.825 67.029  69.048  1.00 27.71 ? 62  GLY A N   1 
ATOM   481  C  CA  . GLY A 1 65  ? 116.252 67.398  67.764  1.00 26.38 ? 62  GLY A CA  1 
ATOM   482  C  C   . GLY A 1 65  ? 114.740 67.289  67.681  1.00 25.42 ? 62  GLY A C   1 
ATOM   483  O  O   . GLY A 1 65  ? 114.186 67.501  66.624  1.00 25.92 ? 62  GLY A O   1 
ATOM   484  N  N   . LEU A 1 66  ? 114.078 66.979  68.794  1.00 23.76 ? 63  LEU A N   1 
ATOM   485  C  CA  . LEU A 1 66  ? 112.677 66.592  68.802  1.00 22.64 ? 63  LEU A CA  1 
ATOM   486  C  C   . LEU A 1 66  ? 111.924 67.217  69.975  1.00 22.50 ? 63  LEU A C   1 
ATOM   487  O  O   . LEU A 1 66  ? 112.561 67.658  70.944  1.00 21.06 ? 63  LEU A O   1 
ATOM   488  C  CB  . LEU A 1 66  ? 112.543 65.050  68.896  1.00 21.34 ? 63  LEU A CB  1 
ATOM   489  C  CG  . LEU A 1 66  ? 113.071 64.158  67.752  1.00 21.70 ? 63  LEU A CG  1 
ATOM   490  C  CD1 . LEU A 1 66  ? 112.906 62.671  68.031  1.00 20.19 ? 63  LEU A CD1 1 
ATOM   491  C  CD2 . LEU A 1 66  ? 112.468 64.499  66.407  1.00 22.17 ? 63  LEU A CD2 1 
ATOM   492  N  N   . VAL A 1 67  ? 110.573 67.226  69.872  1.00 23.10 ? 64  VAL A N   1 
ATOM   493  C  CA  . VAL A 1 67  ? 109.677 67.395  71.031  1.00 23.24 ? 64  VAL A CA  1 
ATOM   494  C  C   . VAL A 1 67  ? 110.205 66.627  72.232  1.00 23.79 ? 64  VAL A C   1 
ATOM   495  O  O   . VAL A 1 67  ? 110.770 65.532  72.075  1.00 23.70 ? 64  VAL A O   1 
ATOM   496  C  CB  . VAL A 1 67  ? 108.294 66.709  70.928  1.00 23.42 ? 64  VAL A CB  1 
ATOM   497  C  CG1 . VAL A 1 67  ? 107.130 67.690  71.194  1.00 24.85 ? 64  VAL A CG1 1 
ATOM   498  C  CG2 . VAL A 1 67  ? 108.141 65.745  69.770  1.00 21.89 ? 64  VAL A CG2 1 
ATOM   499  N  N   . SER A 1 68  ? 109.933 67.163  73.424  1.00 23.22 ? 65  SER A N   1 
ATOM   500  C  CA  . SER A 1 68  ? 110.292 66.492  74.649  1.00 22.93 ? 65  SER A CA  1 
ATOM   501  C  C   . SER A 1 68  ? 109.400 65.271  74.897  1.00 23.00 ? 65  SER A C   1 
ATOM   502  O  O   . SER A 1 68  ? 108.265 65.141  74.360  1.00 23.06 ? 65  SER A O   1 
ATOM   503  C  CB  . SER A 1 68  ? 110.169 67.457  75.810  1.00 22.63 ? 65  SER A CB  1 
ATOM   504  O  OG  . SER A 1 68  ? 108.818 67.671  76.098  1.00 22.72 ? 65  SER A OG  1 
ATOM   505  N  N   . TRP A 1 69  ? 109.902 64.384  75.729  1.00 21.90 ? 66  TRP A N   1 
ATOM   506  C  CA  . TRP A 1 69  ? 109.171 63.184  76.028  1.00 21.72 ? 66  TRP A CA  1 
ATOM   507  C  C   . TRP A 1 69  ? 107.873 63.487  76.805  1.00 22.78 ? 66  TRP A C   1 
ATOM   508  O  O   . TRP A 1 69  ? 106.864 62.756  76.633  1.00 23.39 ? 66  TRP A O   1 
ATOM   509  C  CB  . TRP A 1 69  ? 110.074 62.153  76.721  1.00 20.05 ? 66  TRP A CB  1 
ATOM   510  C  CG  . TRP A 1 69  ? 110.385 62.382  78.165  1.00 19.31 ? 66  TRP A CG  1 
ATOM   511  C  CD1 . TRP A 1 69  ? 111.533 62.905  78.678  1.00 18.64 ? 66  TRP A CD1 1 
ATOM   512  C  CD2 . TRP A 1 69  ? 109.559 62.024  79.309  1.00 18.29 ? 66  TRP A CD2 1 
ATOM   513  N  NE1 . TRP A 1 69  ? 111.472 62.910  80.066  1.00 17.00 ? 66  TRP A NE1 1 
ATOM   514  C  CE2 . TRP A 1 69  ? 110.258 62.423  80.469  1.00 15.46 ? 66  TRP A CE2 1 
ATOM   515  C  CE3 . TRP A 1 69  ? 108.280 61.444  79.452  1.00 17.06 ? 66  TRP A CE3 1 
ATOM   516  C  CZ2 . TRP A 1 69  ? 109.737 62.240  81.765  1.00 18.84 ? 66  TRP A CZ2 1 
ATOM   517  C  CZ3 . TRP A 1 69  ? 107.752 61.285  80.732  1.00 17.00 ? 66  TRP A CZ3 1 
ATOM   518  C  CH2 . TRP A 1 69  ? 108.494 61.661  81.880  1.00 18.09 ? 66  TRP A CH2 1 
ATOM   519  N  N   . LYS A 1 70  ? 107.879 64.550  77.626  1.00 22.43 ? 67  LYS A N   1 
ATOM   520  C  CA  . LYS A 1 70  ? 106.674 64.902  78.377  1.00 23.80 ? 67  LYS A CA  1 
ATOM   521  C  C   . LYS A 1 70  ? 105.606 65.460  77.429  1.00 24.26 ? 67  LYS A C   1 
ATOM   522  O  O   . LYS A 1 70  ? 104.433 65.160  77.607  1.00 25.77 ? 67  LYS A O   1 
ATOM   523  C  CB  . LYS A 1 70  ? 106.939 65.822  79.604  1.00 23.46 ? 67  LYS A CB  1 
ATOM   524  C  CG  . LYS A 1 70  ? 107.329 65.062  80.904  1.00 23.87 ? 67  LYS A CG  1 
ATOM   525  C  CD  . LYS A 1 70  ? 107.319 65.982  82.116  1.00 23.60 ? 67  LYS A CD  1 
ATOM   526  C  CE  . LYS A 1 70  ? 107.819 65.333  83.396  1.00 26.40 ? 67  LYS A CE  1 
ATOM   527  N  NZ  . LYS A 1 70  ? 107.943 66.291  84.591  1.00 25.97 ? 67  LYS A NZ  1 
HETATM 528  N  N   . MSE A 1 71  ? 105.994 66.226  76.409  1.00 24.25 ? 68  MSE A N   1 
HETATM 529  C  CA  . MSE A 1 71  ? 105.011 66.675  75.445  1.00 24.50 ? 68  MSE A CA  1 
HETATM 530  C  C   . MSE A 1 71  ? 104.479 65.526  74.589  1.00 24.76 ? 68  MSE A C   1 
HETATM 531  O  O   . MSE A 1 71  ? 103.289 65.429  74.346  1.00 24.95 ? 68  MSE A O   1 
HETATM 532  C  CB  . MSE A 1 71  ? 105.533 67.815  74.590  1.00 25.01 ? 68  MSE A CB  1 
HETATM 533  C  CG  . MSE A 1 71  ? 104.474 68.391  73.681  1.00 26.78 ? 68  MSE A CG  1 
HETATM 534  SE SE  . MSE A 1 71  ? 103.006 69.340  74.692  1.00 42.19 ? 68  MSE A SE  1 
HETATM 535  C  CE  . MSE A 1 71  ? 103.987 70.925  75.324  1.00 33.97 ? 68  MSE A CE  1 
ATOM   536  N  N   . LYS A 1 72  ? 105.375 64.649  74.156  1.00 24.71 ? 69  LYS A N   1 
ATOM   537  C  CA  . LYS A 1 72  ? 105.014 63.442  73.442  1.00 24.16 ? 69  LYS A CA  1 
ATOM   538  C  C   . LYS A 1 72  ? 104.059 62.576  74.272  1.00 24.48 ? 69  LYS A C   1 
ATOM   539  O  O   . LYS A 1 72  ? 103.065 62.053  73.739  1.00 24.61 ? 69  LYS A O   1 
ATOM   540  C  CB  . LYS A 1 72  ? 106.299 62.667  73.055  1.00 23.82 ? 69  LYS A CB  1 
ATOM   541  C  CG  . LYS A 1 72  ? 106.074 61.495  72.134  1.00 24.63 ? 69  LYS A CG  1 
ATOM   542  C  CD  . LYS A 1 72  ? 105.754 61.918  70.673  1.00 25.09 ? 69  LYS A CD  1 
ATOM   543  C  CE  . LYS A 1 72  ? 104.823 60.916  69.966  1.00 21.57 ? 69  LYS A CE  1 
ATOM   544  N  NZ  . LYS A 1 72  ? 105.383 59.541  70.081  1.00 22.58 ? 69  LYS A NZ  1 
ATOM   545  N  N   . ARG A 1 73  ? 104.316 62.445  75.575  1.00 24.36 ? 70  ARG A N   1 
ATOM   546  C  CA  . ARG A 1 73  ? 103.466 61.591  76.427  1.00 24.08 ? 70  ARG A CA  1 
ATOM   547  C  C   . ARG A 1 73  ? 102.058 62.174  76.588  1.00 25.31 ? 70  ARG A C   1 
ATOM   548  O  O   . ARG A 1 73  ? 101.067 61.444  76.620  1.00 25.90 ? 70  ARG A O   1 
ATOM   549  C  CB  . ARG A 1 73  ? 104.123 61.378  77.782  1.00 23.67 ? 70  ARG A CB  1 
ATOM   550  C  CG  . ARG A 1 73  ? 103.331 60.534  78.800  1.00 21.72 ? 70  ARG A CG  1 
ATOM   551  C  CD  . ARG A 1 73  ? 103.455 61.256  80.097  1.00 20.03 ? 70  ARG A CD  1 
ATOM   552  N  NE  . ARG A 1 73  ? 104.181 60.493  81.053  1.00 20.64 ? 70  ARG A NE  1 
ATOM   553  C  CZ  . ARG A 1 73  ? 104.768 60.954  82.155  1.00 19.43 ? 70  ARG A CZ  1 
ATOM   554  N  NH1 . ARG A 1 73  ? 105.362 60.058  82.918  1.00 16.42 ? 70  ARG A NH1 1 
ATOM   555  N  NH2 . ARG A 1 73  ? 104.805 62.258  82.490  1.00 16.91 ? 70  ARG A NH2 1 
ATOM   556  N  N   . PHE A 1 74  ? 101.975 63.494  76.666  1.00 25.62 ? 71  PHE A N   1 
ATOM   557  C  CA  . PHE A 1 74  ? 100.713 64.162  76.744  1.00 27.00 ? 71  PHE A CA  1 
ATOM   558  C  C   . PHE A 1 74  ? 99.838  63.878  75.508  1.00 28.03 ? 71  PHE A C   1 
ATOM   559  O  O   . PHE A 1 74  ? 98.624  63.584  75.621  1.00 28.58 ? 71  PHE A O   1 
ATOM   560  C  CB  . PHE A 1 74  ? 100.935 65.673  76.917  1.00 27.46 ? 71  PHE A CB  1 
ATOM   561  C  CG  . PHE A 1 74  ? 99.662  66.451  77.004  1.00 28.81 ? 71  PHE A CG  1 
ATOM   562  C  CD1 . PHE A 1 74  ? 99.013  66.608  78.237  1.00 29.22 ? 71  PHE A CD1 1 
ATOM   563  C  CD2 . PHE A 1 74  ? 99.095  67.002  75.861  1.00 27.82 ? 71  PHE A CD2 1 
ATOM   564  C  CE1 . PHE A 1 74  ? 97.805  67.315  78.329  1.00 28.00 ? 71  PHE A CE1 1 
ATOM   565  C  CE2 . PHE A 1 74  ? 97.897  67.705  75.942  1.00 31.12 ? 71  PHE A CE2 1 
ATOM   566  C  CZ  . PHE A 1 74  ? 97.248  67.860  77.180  1.00 28.33 ? 71  PHE A CZ  1 
ATOM   567  N  N   . PHE A 1 75  ? 100.448 63.984  74.335  1.00 28.15 ? 72  PHE A N   1 
ATOM   568  C  CA  . PHE A 1 75  ? 99.759  63.667  73.110  1.00 28.86 ? 72  PHE A CA  1 
ATOM   569  C  C   . PHE A 1 75  ? 99.422  62.199  72.981  1.00 29.38 ? 72  PHE A C   1 
ATOM   570  O  O   . PHE A 1 75  ? 98.320  61.870  72.597  1.00 30.16 ? 72  PHE A O   1 
ATOM   571  C  CB  . PHE A 1 75  ? 100.523 64.218  71.892  1.00 29.23 ? 72  PHE A CB  1 
ATOM   572  C  CG  . PHE A 1 75  ? 100.256 65.669  71.659  1.00 28.08 ? 72  PHE A CG  1 
ATOM   573  C  CD1 . PHE A 1 75  ? 100.850 66.629  72.462  1.00 27.60 ? 72  PHE A CD1 1 
ATOM   574  C  CD2 . PHE A 1 75  ? 99.358  66.074  70.690  1.00 28.51 ? 72  PHE A CD2 1 
ATOM   575  C  CE1 . PHE A 1 75  ? 100.565 67.983  72.292  1.00 29.07 ? 72  PHE A CE1 1 
ATOM   576  C  CE2 . PHE A 1 75  ? 99.061  67.422  70.505  1.00 28.63 ? 72  PHE A CE2 1 
ATOM   577  C  CZ  . PHE A 1 75  ? 99.661  68.381  71.302  1.00 29.28 ? 72  PHE A CZ  1 
ATOM   578  N  N   . ASP A 1 76  ? 100.356 61.320  73.323  1.00 30.62 ? 73  ASP A N   1 
ATOM   579  C  CA  . ASP A 1 76  ? 100.153 59.893  73.131  1.00 31.84 ? 73  ASP A CA  1 
ATOM   580  C  C   . ASP A 1 76  ? 99.113  59.413  74.089  1.00 31.97 ? 73  ASP A C   1 
ATOM   581  O  O   . ASP A 1 76  ? 98.246  58.657  73.690  1.00 32.03 ? 73  ASP A O   1 
ATOM   582  C  CB  . ASP A 1 76  ? 101.436 59.058  73.357  1.00 32.68 ? 73  ASP A CB  1 
ATOM   583  C  CG  . ASP A 1 76  ? 102.457 59.203  72.233  1.00 35.28 ? 73  ASP A CG  1 
ATOM   584  O  OD1 . ASP A 1 76  ? 102.035 59.480  71.084  1.00 38.88 ? 73  ASP A OD1 1 
ATOM   585  O  OD2 . ASP A 1 76  ? 103.682 59.020  72.506  1.00 35.92 ? 73  ASP A OD2 1 
ATOM   586  N  N   . ASP A 1 77  ? 99.209  59.845  75.348  1.00 32.09 ? 74  ASP A N   1 
ATOM   587  C  CA  . ASP A 1 77  ? 98.483  59.189  76.429  1.00 32.87 ? 74  ASP A CA  1 
ATOM   588  C  C   . ASP A 1 77  ? 97.286  59.948  76.962  1.00 32.83 ? 74  ASP A C   1 
ATOM   589  O  O   . ASP A 1 77  ? 96.281  59.332  77.318  1.00 33.62 ? 74  ASP A O   1 
ATOM   590  C  CB  . ASP A 1 77  ? 99.422  58.816  77.587  1.00 33.08 ? 74  ASP A CB  1 
ATOM   591  C  CG  . ASP A 1 77  ? 100.390 57.667  77.236  1.00 35.48 ? 74  ASP A CG  1 
ATOM   592  O  OD1 . ASP A 1 77  ? 100.331 57.081  76.113  1.00 37.17 ? 74  ASP A OD1 1 
ATOM   593  O  OD2 . ASP A 1 77  ? 101.222 57.338  78.115  1.00 38.90 ? 74  ASP A OD2 1 
ATOM   594  N  N   . VAL A 1 78  ? 97.394  61.270  77.051  1.00 32.55 ? 75  VAL A N   1 
ATOM   595  C  CA  . VAL A 1 78  ? 96.266  62.099  77.505  1.00 32.03 ? 75  VAL A CA  1 
ATOM   596  C  C   . VAL A 1 78  ? 95.290  62.357  76.350  1.00 31.93 ? 75  VAL A C   1 
ATOM   597  O  O   . VAL A 1 78  ? 94.106  62.097  76.491  1.00 31.97 ? 75  VAL A O   1 
ATOM   598  C  CB  . VAL A 1 78  ? 96.732  63.425  78.213  1.00 32.23 ? 75  VAL A CB  1 
ATOM   599  C  CG1 . VAL A 1 78  ? 95.552  64.328  78.542  1.00 30.62 ? 75  VAL A CG1 1 
ATOM   600  C  CG2 . VAL A 1 78  ? 97.508  63.093  79.498  1.00 30.48 ? 75  VAL A CG2 1 
ATOM   601  N  N   . LEU A 1 79  ? 95.792  62.825  75.206  1.00 31.65 ? 76  LEU A N   1 
ATOM   602  C  CA  . LEU A 1 79  ? 94.936  63.082  74.048  1.00 31.31 ? 76  LEU A CA  1 
ATOM   603  C  C   . LEU A 1 79  ? 94.579  61.844  73.233  1.00 31.25 ? 76  LEU A C   1 
ATOM   604  O  O   . LEU A 1 79  ? 93.735  61.906  72.348  1.00 30.99 ? 76  LEU A O   1 
ATOM   605  C  CB  . LEU A 1 79  ? 95.549  64.131  73.139  1.00 31.51 ? 76  LEU A CB  1 
ATOM   606  C  CG  . LEU A 1 79  ? 95.841  65.507  73.716  1.00 31.29 ? 76  LEU A CG  1 
ATOM   607  C  CD1 . LEU A 1 79  ? 96.113  66.382  72.549  1.00 31.67 ? 76  LEU A CD1 1 
ATOM   608  C  CD2 . LEU A 1 79  ? 94.650  66.068  74.556  1.00 29.99 ? 76  LEU A CD2 1 
ATOM   609  N  N   . GLY A 1 80  ? 95.201  60.722  73.547  1.00 31.39 ? 77  GLY A N   1 
ATOM   610  C  CA  . GLY A 1 80  ? 94.984  59.489  72.797  1.00 32.06 ? 77  GLY A CA  1 
ATOM   611  C  C   . GLY A 1 80  ? 93.543  59.034  72.619  1.00 32.39 ? 77  GLY A C   1 
ATOM   612  O  O   . GLY A 1 80  ? 93.217  58.427  71.596  1.00 32.45 ? 77  GLY A O   1 
ATOM   613  N  N   . ASP A 1 81  ? 92.685  59.304  73.609  1.00 32.69 ? 78  ASP A N   1 
ATOM   614  C  CA  . ASP A 1 81  ? 91.251  58.979  73.509  1.00 33.08 ? 78  ASP A CA  1 
ATOM   615  C  C   . ASP A 1 81  ? 90.492  59.920  72.595  1.00 31.58 ? 78  ASP A C   1 
ATOM   616  O  O   . ASP A 1 81  ? 89.502  59.544  72.018  1.00 31.98 ? 78  ASP A O   1 
ATOM   617  C  CB  . ASP A 1 81  ? 90.574  58.929  74.893  1.00 34.04 ? 78  ASP A CB  1 
ATOM   618  C  CG  . ASP A 1 81  ? 90.751  57.563  75.595  1.00 37.66 ? 78  ASP A CG  1 
ATOM   619  O  OD1 . ASP A 1 81  ? 90.580  57.488  76.840  1.00 42.49 ? 78  ASP A OD1 1 
ATOM   620  O  OD2 . ASP A 1 81  ? 91.059  56.553  74.910  1.00 40.89 ? 78  ASP A OD2 1 
ATOM   621  N  N   . LEU A 1 82  ? 90.961  61.150  72.476  1.00 30.86 ? 79  LEU A N   1 
ATOM   622  C  CA  . LEU A 1 82  ? 90.352  62.136  71.582  1.00 29.84 ? 79  LEU A CA  1 
ATOM   623  C  C   . LEU A 1 82  ? 90.733  61.939  70.110  1.00 29.01 ? 79  LEU A C   1 
ATOM   624  O  O   . LEU A 1 82  ? 90.179  62.604  69.233  1.00 29.16 ? 79  LEU A O   1 
ATOM   625  C  CB  . LEU A 1 82  ? 90.742  63.549  72.024  1.00 29.70 ? 79  LEU A CB  1 
ATOM   626  C  CG  . LEU A 1 82  ? 90.191  64.044  73.367  1.00 30.32 ? 79  LEU A CG  1 
ATOM   627  C  CD1 . LEU A 1 82  ? 90.585  65.502  73.550  1.00 32.09 ? 79  LEU A CD1 1 
ATOM   628  C  CD2 . LEU A 1 82  ? 88.675  63.861  73.465  1.00 29.13 ? 79  LEU A CD2 1 
ATOM   629  N  N   . TRP A 1 83  ? 91.674  61.031  69.850  1.00 27.77 ? 80  TRP A N   1 
ATOM   630  C  CA  . TRP A 1 83  ? 92.257  60.903  68.535  1.00 26.86 ? 80  TRP A CA  1 
ATOM   631  C  C   . TRP A 1 83  ? 91.152  60.443  67.603  1.00 26.96 ? 80  TRP A C   1 
ATOM   632  O  O   . TRP A 1 83  ? 90.450  59.450  67.879  1.00 26.43 ? 80  TRP A O   1 
ATOM   633  C  CB  . TRP A 1 83  ? 93.460  59.938  68.507  1.00 26.16 ? 80  TRP A CB  1 
ATOM   634  C  CG  . TRP A 1 83  ? 94.134  59.868  67.125  1.00 26.26 ? 80  TRP A CG  1 
ATOM   635  C  CD1 . TRP A 1 83  ? 95.189  60.607  66.692  1.00 25.87 ? 80  TRP A CD1 1 
ATOM   636  C  CD2 . TRP A 1 83  ? 93.749  59.046  66.005  1.00 25.89 ? 80  TRP A CD2 1 
ATOM   637  N  NE1 . TRP A 1 83  ? 95.497  60.298  65.387  1.00 24.44 ? 80  TRP A NE1 1 
ATOM   638  C  CE2 . TRP A 1 83  ? 94.634  59.341  64.942  1.00 24.46 ? 80  TRP A CE2 1 
ATOM   639  C  CE3 . TRP A 1 83  ? 92.745  58.089  65.800  1.00 26.27 ? 80  TRP A CE3 1 
ATOM   640  C  CZ2 . TRP A 1 83  ? 94.562  58.708  63.699  1.00 24.87 ? 80  TRP A CZ2 1 
ATOM   641  C  CZ3 . TRP A 1 83  ? 92.667  57.463  64.552  1.00 26.55 ? 80  TRP A CZ3 1 
ATOM   642  C  CH2 . TRP A 1 83  ? 93.579  57.776  63.521  1.00 25.43 ? 80  TRP A CH2 1 
ATOM   643  N  N   . GLY A 1 84  ? 90.989  61.192  66.509  1.00 26.66 ? 81  GLY A N   1 
ATOM   644  C  CA  . GLY A 1 84  ? 90.036  60.826  65.481  1.00 26.09 ? 81  GLY A CA  1 
ATOM   645  C  C   . GLY A 1 84  ? 88.769  61.630  65.593  1.00 25.69 ? 81  GLY A C   1 
ATOM   646  O  O   . GLY A 1 84  ? 87.993  61.641  64.672  1.00 25.54 ? 81  GLY A O   1 
ATOM   647  N  N   . GLU A 1 85  ? 88.559  62.315  66.712  1.00 25.56 ? 82  GLU A N   1 
ATOM   648  C  CA  . GLU A 1 85  ? 87.323  63.077  66.880  1.00 26.48 ? 82  GLU A CA  1 
ATOM   649  C  C   . GLU A 1 85  ? 87.586  64.564  67.129  1.00 25.20 ? 82  GLU A C   1 
ATOM   650  O  O   . GLU A 1 85  ? 86.677  65.303  67.520  1.00 26.20 ? 82  GLU A O   1 
ATOM   651  C  CB  . GLU A 1 85  ? 86.430  62.472  67.980  1.00 25.63 ? 82  GLU A CB  1 
ATOM   652  C  CG  . GLU A 1 85  ? 86.904  62.825  69.404  1.00 29.37 ? 82  GLU A CG  1 
ATOM   653  C  CD  . GLU A 1 85  ? 85.966  62.334  70.524  1.00 29.35 ? 82  GLU A CD  1 
ATOM   654  O  OE1 . GLU A 1 85  ? 84.737  62.517  70.414  1.00 34.05 ? 82  GLU A OE1 1 
ATOM   655  O  OE2 . GLU A 1 85  ? 86.467  61.763  71.523  1.00 34.07 ? 82  GLU A OE2 1 
ATOM   656  N  N   . ILE A 1 86  ? 88.812  65.011  66.903  1.00 23.87 ? 83  ILE A N   1 
ATOM   657  C  CA  . ILE A 1 86  ? 89.117  66.433  67.066  1.00 23.02 ? 83  ILE A CA  1 
ATOM   658  C  C   . ILE A 1 86  ? 89.798  67.044  65.847  1.00 23.72 ? 83  ILE A C   1 
ATOM   659  O  O   . ILE A 1 86  ? 90.509  68.020  65.988  1.00 24.37 ? 83  ILE A O   1 
ATOM   660  C  CB  . ILE A 1 86  ? 89.931  66.761  68.375  1.00 22.48 ? 83  ILE A CB  1 
ATOM   661  C  CG1 . ILE A 1 86  ? 91.230  65.965  68.437  1.00 21.74 ? 83  ILE A CG1 1 
ATOM   662  C  CG2 . ILE A 1 86  ? 89.078  66.514  69.613  1.00 19.82 ? 83  ILE A CG2 1 
ATOM   663  C  CD1 . ILE A 1 86  ? 92.138  66.361  69.543  1.00 21.37 ? 83  ILE A CD1 1 
ATOM   664  N  N   . ASP A 1 87  ? 89.560  66.475  64.661  1.00 23.77 ? 84  ASP A N   1 
ATOM   665  C  CA  . ASP A 1 87  ? 90.140  66.959  63.407  1.00 23.79 ? 84  ASP A CA  1 
ATOM   666  C  C   . ASP A 1 87  ? 89.770  68.398  63.120  1.00 24.34 ? 84  ASP A C   1 
ATOM   667  O  O   . ASP A 1 87  ? 88.678  68.836  63.465  1.00 23.97 ? 84  ASP A O   1 
ATOM   668  C  CB  . ASP A 1 87  ? 89.657  66.118  62.235  1.00 23.52 ? 84  ASP A CB  1 
ATOM   669  C  CG  . ASP A 1 87  ? 90.079  64.653  62.326  1.00 23.75 ? 84  ASP A CG  1 
ATOM   670  O  OD1 . ASP A 1 87  ? 89.749  63.983  63.329  1.00 23.13 ? 84  ASP A OD1 1 
ATOM   671  O  OD2 . ASP A 1 87  ? 90.722  64.173  61.371  1.00 21.10 ? 84  ASP A OD2 1 
ATOM   672  N  N   . GLY A 1 88  ? 90.683  69.131  62.481  1.00 24.90 ? 85  GLY A N   1 
ATOM   673  C  CA  . GLY A 1 88  ? 90.377  70.484  62.018  1.00 25.12 ? 85  GLY A CA  1 
ATOM   674  C  C   . GLY A 1 88  ? 90.609  71.594  63.032  1.00 25.86 ? 85  GLY A C   1 
ATOM   675  O  O   . GLY A 1 88  ? 90.199  72.732  62.807  1.00 25.95 ? 85  GLY A O   1 
ATOM   676  N  N   . LYS A 1 89  ? 91.248  71.273  64.157  1.00 26.34 ? 86  LYS A N   1 
ATOM   677  C  CA  . LYS A 1 89  ? 91.806  72.315  65.008  1.00 26.60 ? 86  LYS A CA  1 
ATOM   678  C  C   . LYS A 1 89  ? 92.979  72.875  64.253  1.00 27.16 ? 86  LYS A C   1 
ATOM   679  O  O   . LYS A 1 89  ? 93.528  72.190  63.388  1.00 27.82 ? 86  LYS A O   1 
ATOM   680  C  CB  . LYS A 1 89  ? 92.220  71.796  66.391  1.00 26.41 ? 86  LYS A CB  1 
ATOM   681  C  CG  . LYS A 1 89  ? 91.050  71.691  67.328  1.00 25.06 ? 86  LYS A CG  1 
ATOM   682  C  CD  . LYS A 1 89  ? 91.408  71.043  68.644  1.00 26.77 ? 86  LYS A CD  1 
ATOM   683  C  CE  . LYS A 1 89  ? 90.152  70.426  69.245  1.00 24.65 ? 86  LYS A CE  1 
ATOM   684  N  NZ  . LYS A 1 89  ? 89.095  71.442  69.457  1.00 25.04 ? 86  LYS A NZ  1 
ATOM   685  N  N   . ILE A 1 90  ? 93.328  74.125  64.555  1.00 27.43 ? 87  ILE A N   1 
ATOM   686  C  CA  . ILE A 1 90  ? 94.425  74.831  63.915  1.00 27.52 ? 87  ILE A CA  1 
ATOM   687  C  C   . ILE A 1 90  ? 95.565  74.893  64.920  1.00 28.57 ? 87  ILE A C   1 
ATOM   688  O  O   . ILE A 1 90  ? 95.333  75.221  66.090  1.00 29.04 ? 87  ILE A O   1 
ATOM   689  C  CB  . ILE A 1 90  ? 93.985  76.251  63.469  1.00 27.51 ? 87  ILE A CB  1 
ATOM   690  C  CG1 . ILE A 1 90  ? 92.876  76.136  62.412  1.00 27.67 ? 87  ILE A CG1 1 
ATOM   691  C  CG2 . ILE A 1 90  ? 95.162  77.045  62.925  1.00 25.87 ? 87  ILE A CG2 1 
ATOM   692  C  CD1 . ILE A 1 90  ? 92.140  77.403  62.114  1.00 28.42 ? 87  ILE A CD1 1 
ATOM   693  N  N   . ALA A 1 91  ? 96.781  74.540  64.480  1.00 28.41 ? 88  ALA A N   1 
ATOM   694  C  CA  . ALA A 1 91  ? 97.943  74.445  65.374  1.00 28.00 ? 88  ALA A CA  1 
ATOM   695  C  C   . ALA A 1 91  ? 99.241  74.881  64.711  1.00 28.42 ? 88  ALA A C   1 
ATOM   696  O  O   . ALA A 1 91  ? 99.358  74.863  63.491  1.00 29.24 ? 88  ALA A O   1 
ATOM   697  C  CB  . ALA A 1 91  ? 98.093  73.032  65.922  1.00 27.10 ? 88  ALA A CB  1 
ATOM   698  N  N   . CYS A 1 92  ? 100.194 75.303  65.546  1.00 28.58 ? 89  CYS A N   1 
ATOM   699  C  CA  . CYS A 1 92  ? 101.585 75.621  65.170  1.00 27.72 ? 89  CYS A CA  1 
ATOM   700  C  C   . CYS A 1 92  ? 102.510 75.202  66.328  1.00 26.44 ? 89  CYS A C   1 
ATOM   701  O  O   . CYS A 1 92  ? 102.026 74.663  67.328  1.00 25.62 ? 89  CYS A O   1 
ATOM   702  C  CB  . CYS A 1 92  ? 101.718 77.107  64.889  1.00 27.55 ? 89  CYS A CB  1 
ATOM   703  S  SG  . CYS A 1 92  ? 101.180 78.154  66.287  1.00 30.78 ? 89  CYS A SG  1 
ATOM   704  N  N   . ALA A 1 93  ? 103.813 75.480  66.188  1.00 25.23 ? 90  ALA A N   1 
ATOM   705  C  CA  . ALA A 1 93  ? 104.876 74.906  67.015  1.00 24.39 ? 90  ALA A CA  1 
ATOM   706  C  C   . ALA A 1 93  ? 105.851 75.993  67.396  1.00 24.12 ? 90  ALA A C   1 
ATOM   707  O  O   . ALA A 1 93  ? 105.973 76.984  66.674  1.00 25.04 ? 90  ALA A O   1 
ATOM   708  C  CB  . ALA A 1 93  ? 105.631 73.765  66.220  1.00 23.74 ? 90  ALA A CB  1 
ATOM   709  N  N   . PHE A 1 94  ? 106.565 75.825  68.504  1.00 23.90 ? 91  PHE A N   1 
ATOM   710  C  CA  . PHE A 1 94  ? 107.733 76.698  68.790  1.00 23.82 ? 91  PHE A CA  1 
ATOM   711  C  C   . PHE A 1 94  ? 108.773 75.984  69.643  1.00 24.61 ? 91  PHE A C   1 
ATOM   712  O  O   . PHE A 1 94  ? 108.448 74.987  70.317  1.00 25.50 ? 91  PHE A O   1 
ATOM   713  C  CB  . PHE A 1 94  ? 107.328 78.045  69.379  1.00 23.06 ? 91  PHE A CB  1 
ATOM   714  C  CG  . PHE A 1 94  ? 106.522 77.953  70.670  1.00 24.17 ? 91  PHE A CG  1 
ATOM   715  C  CD1 . PHE A 1 94  ? 105.127 77.751  70.634  1.00 22.02 ? 91  PHE A CD1 1 
ATOM   716  C  CD2 . PHE A 1 94  ? 107.149 78.155  71.921  1.00 22.48 ? 91  PHE A CD2 1 
ATOM   717  C  CE1 . PHE A 1 94  ? 104.383 77.696  71.819  1.00 21.74 ? 91  PHE A CE1 1 
ATOM   718  C  CE2 . PHE A 1 94  ? 106.404 78.114  73.120  1.00 20.94 ? 91  PHE A CE2 1 
ATOM   719  C  CZ  . PHE A 1 94  ? 105.024 77.868  73.072  1.00 21.24 ? 91  PHE A CZ  1 
ATOM   720  N  N   . SER A 1 95  ? 110.019 76.440  69.610  1.00 24.02 ? 92  SER A N   1 
ATOM   721  C  CA  . SER A 1 95  ? 111.077 75.664  70.245  1.00 24.98 ? 92  SER A CA  1 
ATOM   722  C  C   . SER A 1 95  ? 112.335 76.490  70.468  1.00 25.65 ? 92  SER A C   1 
ATOM   723  O  O   . SER A 1 95  ? 112.682 77.382  69.657  1.00 24.93 ? 92  SER A O   1 
ATOM   724  C  CB  . SER A 1 95  ? 111.430 74.436  69.379  1.00 26.10 ? 92  SER A CB  1 
ATOM   725  O  OG  . SER A 1 95  ? 112.348 73.557  70.033  1.00 27.75 ? 92  SER A OG  1 
ATOM   726  N  N   . SER A 1 96  ? 113.008 76.183  71.576  1.00 25.86 ? 93  SER A N   1 
ATOM   727  C  CA  . SER A 1 96  ? 114.234 76.841  71.968  1.00 26.33 ? 93  SER A CA  1 
ATOM   728  C  C   . SER A 1 96  ? 115.254 75.724  71.968  1.00 26.63 ? 93  SER A C   1 
ATOM   729  O  O   . SER A 1 96  ? 114.958 74.629  72.458  1.00 27.47 ? 93  SER A O   1 
ATOM   730  C  CB  . SER A 1 96  ? 114.077 77.412  73.383  1.00 26.57 ? 93  SER A CB  1 
ATOM   731  O  OG  . SER A 1 96  ? 115.275 78.008  73.851  1.00 27.42 ? 93  SER A OG  1 
ATOM   732  N  N   . SER A 1 97  ? 116.437 75.985  71.412  1.00 26.81 ? 94  SER A N   1 
ATOM   733  C  CA  . SER A 1 97  ? 117.553 75.019  71.406  1.00 26.33 ? 94  SER A CA  1 
ATOM   734  C  C   . SER A 1 97  ? 118.765 75.620  72.073  1.00 25.48 ? 94  SER A C   1 
ATOM   735  O  O   . SER A 1 97  ? 118.741 76.762  72.458  1.00 25.35 ? 94  SER A O   1 
ATOM   736  C  CB  . SER A 1 97  ? 117.901 74.585  69.975  1.00 26.40 ? 94  SER A CB  1 
ATOM   737  O  OG  . SER A 1 97  ? 118.143 75.725  69.159  1.00 29.11 ? 94  SER A OG  1 
ATOM   738  N  N   . GLY A 1 98  ? 119.821 74.824  72.213  1.00 25.55 ? 95  GLY A N   1 
ATOM   739  C  CA  . GLY A 1 98  ? 121.070 75.247  72.818  1.00 24.85 ? 95  GLY A CA  1 
ATOM   740  C  C   . GLY A 1 98  ? 121.810 76.197  71.897  1.00 25.28 ? 95  GLY A C   1 
ATOM   741  O  O   . GLY A 1 98  ? 122.564 77.055  72.350  1.00 25.30 ? 95  GLY A O   1 
ATOM   742  N  N   . GLY A 1 99  ? 121.561 76.073  70.600  1.00 25.26 ? 96  GLY A N   1 
ATOM   743  C  CA  . GLY A 1 99  ? 122.328 76.816  69.619  1.00 25.39 ? 96  GLY A CA  1 
ATOM   744  C  C   . GLY A 1 99  ? 121.625 76.892  68.286  1.00 25.73 ? 96  GLY A C   1 
ATOM   745  O  O   . GLY A 1 99  ? 120.777 76.039  67.980  1.00 25.76 ? 96  GLY A O   1 
ATOM   746  N  N   . TRP A 1 100 ? 121.947 77.941  67.517  1.00 25.54 ? 97  TRP A N   1 
ATOM   747  C  CA  . TRP A 1 100 ? 121.611 78.008  66.094  1.00 25.11 ? 97  TRP A CA  1 
ATOM   748  C  C   . TRP A 1 100 ? 122.332 76.886  65.381  1.00 24.65 ? 97  TRP A C   1 
ATOM   749  O  O   . TRP A 1 100 ? 123.538 76.648  65.614  1.00 24.53 ? 97  TRP A O   1 
ATOM   750  C  CB  . TRP A 1 100 ? 121.985 79.382  65.499  1.00 25.69 ? 97  TRP A CB  1 
ATOM   751  C  CG  . TRP A 1 100 ? 121.241 80.431  66.181  1.00 25.60 ? 97  TRP A CG  1 
ATOM   752  C  CD1 . TRP A 1 100 ? 121.697 81.255  67.180  1.00 26.73 ? 97  TRP A CD1 1 
ATOM   753  C  CD2 . TRP A 1 100 ? 119.847 80.720  66.018  1.00 26.61 ? 97  TRP A CD2 1 
ATOM   754  N  NE1 . TRP A 1 100 ? 120.669 82.070  67.624  1.00 27.52 ? 97  TRP A NE1 1 
ATOM   755  C  CE2 . TRP A 1 100 ? 119.524 81.760  66.928  1.00 27.08 ? 97  TRP A CE2 1 
ATOM   756  C  CE3 . TRP A 1 100 ? 118.840 80.216  65.177  1.00 27.16 ? 97  TRP A CE3 1 
ATOM   757  C  CZ2 . TRP A 1 100 ? 118.232 82.310  67.015  1.00 26.08 ? 97  TRP A CZ2 1 
ATOM   758  C  CZ3 . TRP A 1 100 ? 117.541 80.767  65.271  1.00 27.01 ? 97  TRP A CZ3 1 
ATOM   759  C  CH2 . TRP A 1 100 ? 117.261 81.805  66.180  1.00 26.26 ? 97  TRP A CH2 1 
ATOM   760  N  N   . GLY A 1 101 ? 121.588 76.192  64.528  1.00 24.19 ? 98  GLY A N   1 
ATOM   761  C  CA  . GLY A 1 101 ? 122.070 74.981  63.869  1.00 24.34 ? 98  GLY A CA  1 
ATOM   762  C  C   . GLY A 1 101 ? 121.896 73.756  64.763  1.00 24.36 ? 98  GLY A C   1 
ATOM   763  O  O   . GLY A 1 101 ? 122.371 72.668  64.440  1.00 23.64 ? 98  GLY A O   1 
ATOM   764  N  N   . GLY A 1 102 ? 121.186 73.950  65.875  1.00 25.03 ? 99  GLY A N   1 
ATOM   765  C  CA  . GLY A 1 102 ? 121.041 72.947  66.925  1.00 25.63 ? 99  GLY A CA  1 
ATOM   766  C  C   . GLY A 1 102 ? 119.806 72.109  66.822  1.00 26.35 ? 99  GLY A C   1 
ATOM   767  O  O   . GLY A 1 102 ? 119.636 71.157  67.585  1.00 27.41 ? 99  GLY A O   1 
ATOM   768  N  N   . GLY A 1 103 ? 118.908 72.470  65.919  1.00 26.77 ? 100 GLY A N   1 
ATOM   769  C  CA  . GLY A 1 103 ? 117.803 71.572  65.598  1.00 27.42 ? 100 GLY A CA  1 
ATOM   770  C  C   . GLY A 1 103 ? 116.457 72.085  65.980  1.00 28.16 ? 100 GLY A C   1 
ATOM   771  O  O   . GLY A 1 103 ? 115.532 71.303  66.080  1.00 29.32 ? 100 GLY A O   1 
ATOM   772  N  N   . ASN A 1 104 ? 116.330 73.395  66.184  1.00 28.56 ? 101 ASN A N   1 
ATOM   773  C  CA  . ASN A 1 104 ? 115.044 73.988  66.555  1.00 28.80 ? 101 ASN A CA  1 
ATOM   774  C  C   . ASN A 1 104 ? 113.945 73.976  65.482  1.00 28.67 ? 101 ASN A C   1 
ATOM   775  O  O   . ASN A 1 104 ? 112.753 73.944  65.835  1.00 28.22 ? 101 ASN A O   1 
ATOM   776  C  CB  . ASN A 1 104 ? 115.170 75.374  67.211  1.00 28.81 ? 101 ASN A CB  1 
ATOM   777  C  CG  . ASN A 1 104 ? 116.076 76.338  66.447  1.00 32.40 ? 101 ASN A CG  1 
ATOM   778  O  OD1 . ASN A 1 104 ? 116.824 77.112  67.071  1.00 40.63 ? 101 ASN A OD1 1 
ATOM   779  N  ND2 . ASN A 1 104 ? 115.998 76.342  65.126  1.00 33.70 ? 101 ASN A ND2 1 
ATOM   780  N  N   . GLU A 1 105 ? 114.336 74.011  64.202  1.00 27.97 ? 102 GLU A N   1 
ATOM   781  C  CA  . GLU A 1 105 ? 113.351 73.885  63.128  1.00 28.31 ? 102 GLU A CA  1 
ATOM   782  C  C   . GLU A 1 105 ? 112.931 72.440  62.986  1.00 27.68 ? 102 GLU A C   1 
ATOM   783  O  O   . GLU A 1 105 ? 111.780 72.177  62.699  1.00 28.25 ? 102 GLU A O   1 
ATOM   784  C  CB  . GLU A 1 105 ? 113.849 74.432  61.794  1.00 27.98 ? 102 GLU A CB  1 
ATOM   785  C  CG  . GLU A 1 105 ? 114.242 75.903  61.852  1.00 30.29 ? 102 GLU A CG  1 
ATOM   786  C  CD  . GLU A 1 105 ? 114.940 76.348  60.586  1.00 33.78 ? 102 GLU A CD  1 
ATOM   787  O  OE1 . GLU A 1 105 ? 115.533 75.487  59.890  1.00 36.15 ? 102 GLU A OE1 1 
ATOM   788  O  OE2 . GLU A 1 105 ? 114.898 77.556  60.277  1.00 35.93 ? 102 GLU A OE2 1 
ATOM   789  N  N   . VAL A 1 106 ? 113.876 71.522  63.183  1.00 26.72 ? 103 VAL A N   1 
ATOM   790  C  CA  . VAL A 1 106 ? 113.601 70.106  63.137  1.00 26.13 ? 103 VAL A CA  1 
ATOM   791  C  C   . VAL A 1 106 ? 112.701 69.705  64.324  1.00 26.38 ? 103 VAL A C   1 
ATOM   792  O  O   . VAL A 1 106 ? 111.814 68.875  64.156  1.00 26.43 ? 103 VAL A O   1 
ATOM   793  C  CB  . VAL A 1 106 ? 114.910 69.277  63.084  1.00 26.48 ? 103 VAL A CB  1 
ATOM   794  C  CG1 . VAL A 1 106 ? 114.624 67.790  63.046  1.00 25.27 ? 103 VAL A CG1 1 
ATOM   795  C  CG2 . VAL A 1 106 ? 115.743 69.676  61.877  1.00 25.23 ? 103 VAL A CG2 1 
ATOM   796  N  N   . ALA A 1 107 ? 112.905 70.302  65.505  1.00 25.46 ? 104 ALA A N   1 
ATOM   797  C  CA  . ALA A 1 107 ? 112.006 70.032  66.649  1.00 24.89 ? 104 ALA A CA  1 
ATOM   798  C  C   . ALA A 1 107 ? 110.578 70.511  66.357  1.00 24.84 ? 104 ALA A C   1 
ATOM   799  O  O   . ALA A 1 107 ? 109.625 69.784  66.640  1.00 24.81 ? 104 ALA A O   1 
ATOM   800  C  CB  . ALA A 1 107 ? 112.537 70.652  67.969  1.00 24.24 ? 104 ALA A CB  1 
ATOM   801  N  N   . CYS A 1 108 ? 110.460 71.731  65.807  1.00 23.80 ? 105 CYS A N   1 
ATOM   802  C  CA  . CYS A 1 108 ? 109.241 72.250  65.260  1.00 24.02 ? 105 CYS A CA  1 
ATOM   803  C  C   . CYS A 1 108 ? 108.564 71.281  64.270  1.00 24.83 ? 105 CYS A C   1 
ATOM   804  O  O   . CYS A 1 108 ? 107.396 70.941  64.450  1.00 24.60 ? 105 CYS A O   1 
ATOM   805  C  CB  . CYS A 1 108 ? 109.487 73.608  64.611  1.00 23.53 ? 105 CYS A CB  1 
ATOM   806  S  SG  . CYS A 1 108 ? 109.542 74.921  65.833  1.00 24.70 ? 105 CYS A SG  1 
HETATM 807  N  N   . MSE A 1 109 ? 109.297 70.839  63.241  1.00 26.01 ? 106 MSE A N   1 
HETATM 808  C  CA  . MSE A 1 109 ? 108.815 69.810  62.324  1.00 26.94 ? 106 MSE A CA  1 
HETATM 809  C  C   . MSE A 1 109 ? 108.212 68.610  63.039  1.00 25.68 ? 106 MSE A C   1 
HETATM 810  O  O   . MSE A 1 109 ? 107.152 68.166  62.623  1.00 25.43 ? 106 MSE A O   1 
HETATM 811  C  CB  . MSE A 1 109 ? 109.890 69.333  61.366  1.00 27.72 ? 106 MSE A CB  1 
HETATM 812  C  CG  . MSE A 1 109 ? 110.168 70.304  60.259  1.00 37.65 ? 106 MSE A CG  1 
HETATM 813  SE SE  . MSE A 1 109 ? 108.582 70.731  59.102  1.00 57.82 ? 106 MSE A SE  1 
HETATM 814  C  CE  . MSE A 1 109 ? 107.855 69.000  58.962  1.00 47.04 ? 106 MSE A CE  1 
ATOM   815  N  N   . SER A 1 110 ? 108.848 68.124  64.109  1.00 23.79 ? 107 SER A N   1 
ATOM   816  C  CA  . SER A 1 110 ? 108.340 66.943  64.848  1.00 23.45 ? 107 SER A CA  1 
ATOM   817  C  C   . SER A 1 110 ? 107.080 67.242  65.676  1.00 23.66 ? 107 SER A C   1 
ATOM   818  O  O   . SER A 1 110 ? 106.205 66.377  65.818  1.00 24.21 ? 107 SER A O   1 
ATOM   819  C  CB  . SER A 1 110 ? 109.421 66.282  65.728  1.00 23.19 ? 107 SER A CB  1 
ATOM   820  O  OG  . SER A 1 110 ? 109.631 67.004  66.937  1.00 19.99 ? 107 SER A OG  1 
ATOM   821  N  N   . ILE A 1 111 ? 106.980 68.457  66.201  1.00 23.33 ? 108 ILE A N   1 
ATOM   822  C  CA  . ILE A 1 111 ? 105.742 68.934  66.817  1.00 23.36 ? 108 ILE A CA  1 
ATOM   823  C  C   . ILE A 1 111 ? 104.618 68.951  65.747  1.00 24.92 ? 108 ILE A C   1 
ATOM   824  O  O   . ILE A 1 111 ? 103.556 68.336  65.946  1.00 25.18 ? 108 ILE A O   1 
ATOM   825  C  CB  . ILE A 1 111 ? 105.914 70.343  67.488  1.00 22.50 ? 108 ILE A CB  1 
ATOM   826  C  CG1 . ILE A 1 111 ? 106.799 70.264  68.734  1.00 23.28 ? 108 ILE A CG1 1 
ATOM   827  C  CG2 . ILE A 1 111 ? 104.544 70.954  67.846  1.00 21.98 ? 108 ILE A CG2 1 
ATOM   828  C  CD1 . ILE A 1 111 ? 107.331 71.607  69.250  1.00 22.61 ? 108 ILE A CD1 1 
ATOM   829  N  N   . LEU A 1 112 ? 104.875 69.619  64.613  1.00 24.97 ? 109 LEU A N   1 
ATOM   830  C  CA  . LEU A 1 112 ? 103.929 69.680  63.510  1.00 25.83 ? 109 LEU A CA  1 
ATOM   831  C  C   . LEU A 1 112 ? 103.466 68.295  63.018  1.00 26.35 ? 109 LEU A C   1 
ATOM   832  O  O   . LEU A 1 112 ? 102.300 68.113  62.672  1.00 26.69 ? 109 LEU A O   1 
ATOM   833  C  CB  . LEU A 1 112 ? 104.487 70.522  62.347  1.00 25.46 ? 109 LEU A CB  1 
ATOM   834  C  CG  . LEU A 1 112 ? 104.655 72.021  62.661  1.00 25.17 ? 109 LEU A CG  1 
ATOM   835  C  CD1 . LEU A 1 112 ? 105.477 72.747  61.565  1.00 20.97 ? 109 LEU A CD1 1 
ATOM   836  C  CD2 . LEU A 1 112 ? 103.343 72.743  62.935  1.00 20.98 ? 109 LEU A CD2 1 
ATOM   837  N  N   . THR A 1 113 ? 104.362 67.317  63.004  1.00 27.06 ? 110 THR A N   1 
ATOM   838  C  CA  . THR A 1 113 ? 103.989 66.001  62.537  1.00 27.73 ? 110 THR A CA  1 
ATOM   839  C  C   . THR A 1 113 ? 103.088 65.284  63.509  1.00 28.57 ? 110 THR A C   1 
ATOM   840  O  O   . THR A 1 113 ? 102.200 64.537  63.122  1.00 28.64 ? 110 THR A O   1 
ATOM   841  C  CB  . THR A 1 113 ? 105.201 65.158  61.980  1.00 27.86 ? 110 THR A CB  1 
ATOM   842  O  OG1 . THR A 1 113 ? 105.289 63.873  62.624  1.00 27.81 ? 110 THR A OG1 1 
ATOM   843  C  CG2 . THR A 1 113 ? 106.460 65.890  62.115  1.00 26.10 ? 110 THR A CG2 1 
HETATM 844  N  N   . MSE A 1 114 ? 103.297 65.560  64.775  1.00 30.41 ? 111 MSE A N   1 
HETATM 845  C  CA  . MSE A 1 114 ? 102.474 65.047  65.831  1.00 33.68 ? 111 MSE A CA  1 
HETATM 846  C  C   . MSE A 1 114 ? 101.072 65.678  65.746  1.00 31.95 ? 111 MSE A C   1 
HETATM 847  O  O   . MSE A 1 114 ? 100.061 64.983  65.831  1.00 32.59 ? 111 MSE A O   1 
HETATM 848  C  CB  . MSE A 1 114 ? 103.172 65.395  67.135  1.00 32.84 ? 111 MSE A CB  1 
HETATM 849  C  CG  . MSE A 1 114 ? 102.698 64.674  68.323  1.00 35.65 ? 111 MSE A CG  1 
HETATM 850  SE SE  . MSE A 1 114 ? 103.663 65.281  69.943  1.00 44.05 ? 111 MSE A SE  1 
HETATM 851  C  CE  . MSE A 1 114 ? 103.327 67.339  69.935  1.00 31.95 ? 111 MSE A CE  1 
ATOM   852  N  N   . LEU A 1 115 ? 101.029 66.986  65.548  1.00 30.97 ? 112 LEU A N   1 
ATOM   853  C  CA  . LEU A 1 115 ? 99.793  67.710  65.402  1.00 30.94 ? 112 LEU A CA  1 
ATOM   854  C  C   . LEU A 1 115 ? 99.030  67.273  64.168  1.00 32.40 ? 112 LEU A C   1 
ATOM   855  O  O   . LEU A 1 115 ? 97.799  67.133  64.222  1.00 32.55 ? 112 LEU A O   1 
ATOM   856  C  CB  . LEU A 1 115 ? 100.034 69.229  65.368  1.00 29.14 ? 112 LEU A CB  1 
ATOM   857  C  CG  . LEU A 1 115 ? 100.617 69.810  66.656  1.00 28.94 ? 112 LEU A CG  1 
ATOM   858  C  CD1 . LEU A 1 115 ? 101.289 71.157  66.373  1.00 26.79 ? 112 LEU A CD1 1 
ATOM   859  C  CD2 . LEU A 1 115 ? 99.609  69.940  67.776  1.00 25.99 ? 112 LEU A CD2 1 
HETATM 860  N  N   . MSE A 1 116 ? 99.737  67.047  63.059  1.00 33.08 ? 113 MSE A N   1 
HETATM 861  C  CA  . MSE A 1 116 ? 99.072  66.609  61.841  1.00 35.56 ? 113 MSE A CA  1 
HETATM 862  C  C   . MSE A 1 116 ? 98.430  65.272  62.008  1.00 32.58 ? 113 MSE A C   1 
HETATM 863  O  O   . MSE A 1 116 ? 97.393  64.980  61.397  1.00 32.38 ? 113 MSE A O   1 
HETATM 864  C  CB  . MSE A 1 116 ? 100.015 66.581  60.661  1.00 34.08 ? 113 MSE A CB  1 
HETATM 865  C  CG  . MSE A 1 116 ? 100.201 67.952  60.106  1.00 38.18 ? 113 MSE A CG  1 
HETATM 866  SE SE  . MSE A 1 116 ? 101.256 67.951  58.448  1.00 48.52 ? 113 MSE A SE  1 
HETATM 867  C  CE  . MSE A 1 116 ? 103.103 67.438  59.244  1.00 39.13 ? 113 MSE A CE  1 
ATOM   868  N  N   . ASN A 1 117 ? 99.035  64.460  62.858  1.00 31.05 ? 114 ASN A N   1 
ATOM   869  C  CA  . ASN A 1 117 ? 98.546  63.118  63.055  1.00 29.97 ? 114 ASN A CA  1 
ATOM   870  C  C   . ASN A 1 117 ? 97.138  63.138  63.637  1.00 29.08 ? 114 ASN A C   1 
ATOM   871  O  O   . ASN A 1 117 ? 96.352  62.239  63.376  1.00 29.19 ? 114 ASN A O   1 
ATOM   872  C  CB  . ASN A 1 117 ? 99.506  62.351  63.956  1.00 30.49 ? 114 ASN A CB  1 
ATOM   873  C  CG  . ASN A 1 117 ? 99.367  60.873  63.818  1.00 29.43 ? 114 ASN A CG  1 
ATOM   874  O  OD1 . ASN A 1 117 ? 98.530  60.259  64.479  1.00 28.41 ? 114 ASN A OD1 1 
ATOM   875  N  ND2 . ASN A 1 117 ? 100.215 60.272  62.978  1.00 27.24 ? 114 ASN A ND2 1 
ATOM   876  N  N   . PHE A 1 118 ? 96.815  64.187  64.390  1.00 28.05 ? 115 PHE A N   1 
ATOM   877  C  CA  . PHE A 1 118 ? 95.483  64.343  64.961  1.00 27.57 ? 115 PHE A CA  1 
ATOM   878  C  C   . PHE A 1 118 ? 94.498  65.003  63.997  1.00 27.42 ? 115 PHE A C   1 
ATOM   879  O  O   . PHE A 1 118 ? 93.390  65.356  64.400  1.00 28.48 ? 115 PHE A O   1 
ATOM   880  C  CB  . PHE A 1 118 ? 95.547  65.156  66.258  1.00 27.52 ? 115 PHE A CB  1 
ATOM   881  C  CG  . PHE A 1 118 ? 95.911  64.346  67.475  1.00 27.80 ? 115 PHE A CG  1 
ATOM   882  C  CD1 . PHE A 1 118 ? 97.248  64.122  67.810  1.00 28.54 ? 115 PHE A CD1 1 
ATOM   883  C  CD2 . PHE A 1 118 ? 94.912  63.823  68.295  1.00 29.67 ? 115 PHE A CD2 1 
ATOM   884  C  CE1 . PHE A 1 118 ? 97.597  63.389  68.947  1.00 27.87 ? 115 PHE A CE1 1 
ATOM   885  C  CE2 . PHE A 1 118 ? 95.232  63.075  69.436  1.00 30.81 ? 115 PHE A CE2 1 
ATOM   886  C  CZ  . PHE A 1 118 ? 96.595  62.869  69.765  1.00 30.21 ? 115 PHE A CZ  1 
ATOM   887  N  N   . GLY A 1 119 ? 94.904  65.186  62.745  1.00 26.07 ? 116 GLY A N   1 
ATOM   888  C  CA  . GLY A 1 119 ? 94.054  65.731  61.744  1.00 25.66 ? 116 GLY A CA  1 
ATOM   889  C  C   . GLY A 1 119 ? 93.912  67.234  61.832  1.00 25.52 ? 116 GLY A C   1 
ATOM   890  O  O   . GLY A 1 119 ? 92.989  67.806  61.226  1.00 25.46 ? 116 GLY A O   1 
ATOM   891  N  N   . PHE A 1 120 ? 94.813  67.878  62.582  1.00 25.01 ? 117 PHE A N   1 
ATOM   892  C  CA  . PHE A 1 120 ? 94.846  69.340  62.678  1.00 24.36 ? 117 PHE A CA  1 
ATOM   893  C  C   . PHE A 1 120 ? 95.370  69.971  61.385  1.00 23.89 ? 117 PHE A C   1 
ATOM   894  O  O   . PHE A 1 120 ? 96.115  69.350  60.625  1.00 22.94 ? 117 PHE A O   1 
ATOM   895  C  CB  . PHE A 1 120 ? 95.732  69.799  63.846  1.00 25.05 ? 117 PHE A CB  1 
ATOM   896  C  CG  . PHE A 1 120 ? 95.280  69.321  65.205  1.00 25.18 ? 117 PHE A CG  1 
ATOM   897  C  CD1 . PHE A 1 120 ? 94.032  68.717  65.389  1.00 24.30 ? 117 PHE A CD1 1 
ATOM   898  C  CD2 . PHE A 1 120 ? 96.094  69.533  66.310  1.00 26.12 ? 117 PHE A CD2 1 
ATOM   899  C  CE1 . PHE A 1 120 ? 93.607  68.318  66.640  1.00 25.43 ? 117 PHE A CE1 1 
ATOM   900  C  CE2 . PHE A 1 120 ? 95.699  69.152  67.591  1.00 27.73 ? 117 PHE A CE2 1 
ATOM   901  C  CZ  . PHE A 1 120 ? 94.446  68.528  67.766  1.00 28.53 ? 117 PHE A CZ  1 
ATOM   902  N  N   . LEU A 1 121 ? 94.950  71.208  61.144  1.00 23.73 ? 118 LEU A N   1 
ATOM   903  C  CA  . LEU A 1 121 ? 95.499  72.050  60.084  1.00 23.69 ? 118 LEU A CA  1 
ATOM   904  C  C   . LEU A 1 121 ? 96.660  72.810  60.731  1.00 23.93 ? 118 LEU A C   1 
ATOM   905  O  O   . LEU A 1 121 ? 96.438  73.561  61.703  1.00 24.33 ? 118 LEU A O   1 
ATOM   906  C  CB  . LEU A 1 121 ? 94.455  73.053  59.591  1.00 23.49 ? 118 LEU A CB  1 
ATOM   907  C  CG  . LEU A 1 121 ? 93.262  72.815  58.651  1.00 24.42 ? 118 LEU A CG  1 
ATOM   908  C  CD1 . LEU A 1 121 ? 93.721  72.846  57.213  1.00 26.46 ? 118 LEU A CD1 1 
ATOM   909  C  CD2 . LEU A 1 121 ? 92.441  71.534  58.932  1.00 23.58 ? 118 LEU A CD2 1 
ATOM   910  N  N   . VAL A 1 122 ? 97.884  72.606  60.222  1.00 23.36 ? 119 VAL A N   1 
ATOM   911  C  CA  . VAL A 1 122 ? 99.084  73.242  60.777  1.00 22.39 ? 119 VAL A CA  1 
ATOM   912  C  C   . VAL A 1 122 ? 99.761  74.227  59.821  1.00 22.91 ? 119 VAL A C   1 
ATOM   913  O  O   . VAL A 1 122 ? 99.596  74.180  58.602  1.00 22.46 ? 119 VAL A O   1 
ATOM   914  C  CB  . VAL A 1 122 ? 100.098 72.188  61.296  1.00 23.10 ? 119 VAL A CB  1 
ATOM   915  C  CG1 . VAL A 1 122 ? 99.383  71.151  62.207  1.00 21.05 ? 119 VAL A CG1 1 
ATOM   916  C  CG2 . VAL A 1 122 ? 100.794 71.480  60.125  1.00 19.85 ? 119 VAL A CG2 1 
ATOM   917  N  N   . PHE A 1 123 ? 100.532 75.134  60.392  1.00 24.00 ? 120 PHE A N   1 
ATOM   918  C  CA  . PHE A 1 123 ? 101.108 76.225  59.616  1.00 25.18 ? 120 PHE A CA  1 
ATOM   919  C  C   . PHE A 1 123 ? 102.394 76.749  60.319  1.00 25.32 ? 120 PHE A C   1 
ATOM   920  O  O   . PHE A 1 123 ? 102.621 76.505  61.517  1.00 24.47 ? 120 PHE A O   1 
ATOM   921  C  CB  . PHE A 1 123 ? 100.063 77.366  59.475  1.00 24.20 ? 120 PHE A CB  1 
ATOM   922  C  CG  . PHE A 1 123 ? 99.781  78.062  60.770  1.00 25.04 ? 120 PHE A CG  1 
ATOM   923  C  CD1 . PHE A 1 123 ? 98.871  77.531  61.689  1.00 27.84 ? 120 PHE A CD1 1 
ATOM   924  C  CD2 . PHE A 1 123 ? 100.466 79.223  61.120  1.00 24.52 ? 120 PHE A CD2 1 
ATOM   925  C  CE1 . PHE A 1 123 ? 98.625  78.185  62.917  1.00 24.26 ? 120 PHE A CE1 1 
ATOM   926  C  CE2 . PHE A 1 123 ? 100.227 79.857  62.346  1.00 21.72 ? 120 PHE A CE2 1 
ATOM   927  C  CZ  . PHE A 1 123 ? 99.328  79.323  63.240  1.00 22.36 ? 120 PHE A CZ  1 
ATOM   928  N  N   . GLY A 1 124 ? 103.201 77.464  59.542  1.00 25.67 ? 121 GLY A N   1 
ATOM   929  C  CA  . GLY A 1 124 ? 104.270 78.331  60.040  1.00 26.08 ? 121 GLY A CA  1 
ATOM   930  C  C   . GLY A 1 124 ? 104.003 79.735  59.503  1.00 26.67 ? 121 GLY A C   1 
ATOM   931  O  O   . GLY A 1 124 ? 102.948 79.982  58.896  1.00 26.97 ? 121 GLY A O   1 
ATOM   932  N  N   . VAL A 1 125 ? 104.939 80.660  59.718  1.00 26.69 ? 122 VAL A N   1 
ATOM   933  C  CA  . VAL A 1 125 ? 104.721 82.076  59.382  1.00 25.90 ? 122 VAL A CA  1 
ATOM   934  C  C   . VAL A 1 125 ? 105.746 82.633  58.428  1.00 25.69 ? 122 VAL A C   1 
ATOM   935  O  O   . VAL A 1 125 ? 106.935 82.470  58.619  1.00 25.99 ? 122 VAL A O   1 
ATOM   936  C  CB  . VAL A 1 125 ? 104.641 82.965  60.660  1.00 26.33 ? 122 VAL A CB  1 
ATOM   937  C  CG1 . VAL A 1 125 ? 104.511 84.420  60.296  1.00 24.59 ? 122 VAL A CG1 1 
ATOM   938  C  CG2 . VAL A 1 125 ? 103.477 82.543  61.531  1.00 24.95 ? 122 VAL A CG2 1 
ATOM   939  N  N   . THR A 1 126 ? 105.274 83.305  57.387  1.00 26.38 ? 123 THR A N   1 
ATOM   940  C  CA  . THR A 1 126 ? 106.164 83.900  56.376  1.00 25.82 ? 123 THR A CA  1 
ATOM   941  C  C   . THR A 1 126 ? 106.833 85.186  56.858  1.00 25.34 ? 123 THR A C   1 
ATOM   942  O  O   . THR A 1 126 ? 107.952 85.497  56.459  1.00 25.36 ? 123 THR A O   1 
ATOM   943  C  CB  . THR A 1 126 ? 105.394 84.238  55.102  1.00 26.13 ? 123 THR A CB  1 
ATOM   944  O  OG1 . THR A 1 126 ? 104.182 84.892  55.459  1.00 25.80 ? 123 THR A OG1 1 
ATOM   945  C  CG2 . THR A 1 126 ? 105.063 82.966  54.292  1.00 26.60 ? 123 THR A CG2 1 
ATOM   946  N  N   . ASP A 1 127 ? 106.131 85.937  57.699  1.00 24.86 ? 124 ASP A N   1 
ATOM   947  C  CA  . ASP A 1 127 ? 106.613 87.234  58.201  1.00 24.88 ? 124 ASP A CA  1 
ATOM   948  C  C   . ASP A 1 127 ? 108.089 87.254  58.563  1.00 24.82 ? 124 ASP A C   1 
ATOM   949  O  O   . ASP A 1 127 ? 108.588 86.362  59.237  1.00 23.18 ? 124 ASP A O   1 
ATOM   950  C  CB  . ASP A 1 127 ? 105.815 87.680  59.435  1.00 24.31 ? 124 ASP A CB  1 
ATOM   951  C  CG  . ASP A 1 127 ? 104.355 87.808  59.150  1.00 24.28 ? 124 ASP A CG  1 
ATOM   952  O  OD1 . ASP A 1 127 ? 103.900 87.238  58.115  1.00 23.97 ? 124 ASP A OD1 1 
ATOM   953  O  OD2 . ASP A 1 127 ? 103.674 88.490  59.944  1.00 22.43 ? 124 ASP A OD2 1 
ATOM   954  N  N   . TYR A 1 128 ? 108.773 88.290  58.081  1.00 25.25 ? 125 TYR A N   1 
ATOM   955  C  CA  . TYR A 1 128 ? 110.072 88.642  58.612  1.00 25.78 ? 125 TYR A CA  1 
ATOM   956  C  C   . TYR A 1 128 ? 109.909 89.717  59.665  1.00 26.34 ? 125 TYR A C   1 
ATOM   957  O  O   . TYR A 1 128 ? 109.363 90.803  59.447  1.00 27.01 ? 125 TYR A O   1 
ATOM   958  C  CB  . TYR A 1 128 ? 111.010 89.114  57.544  1.00 25.68 ? 125 TYR A CB  1 
ATOM   959  C  CG  . TYR A 1 128 ? 111.765 88.022  56.864  1.00 25.80 ? 125 TYR A CG  1 
ATOM   960  C  CD1 . TYR A 1 128 ? 111.101 87.068  56.070  1.00 26.38 ? 125 TYR A CD1 1 
ATOM   961  C  CD2 . TYR A 1 128 ? 113.160 87.963  56.959  1.00 25.04 ? 125 TYR A CD2 1 
ATOM   962  C  CE1 . TYR A 1 128 ? 111.814 86.059  55.396  1.00 25.53 ? 125 TYR A CE1 1 
ATOM   963  C  CE2 . TYR A 1 128 ? 113.885 86.982  56.282  1.00 25.52 ? 125 TYR A CE2 1 
ATOM   964  C  CZ  . TYR A 1 128 ? 113.201 86.033  55.508  1.00 25.68 ? 125 TYR A CZ  1 
ATOM   965  O  OH  . TYR A 1 128 ? 113.918 85.083  54.843  1.00 26.33 ? 125 TYR A OH  1 
ATOM   966  N  N   . VAL A 1 129 ? 110.430 89.381  60.813  1.00 26.39 ? 126 VAL A N   1 
ATOM   967  C  CA  . VAL A 1 129 ? 110.165 90.061  62.019  1.00 27.23 ? 126 VAL A CA  1 
ATOM   968  C  C   . VAL A 1 129 ? 111.484 90.784  62.318  1.00 27.82 ? 126 VAL A C   1 
ATOM   969  O  O   . VAL A 1 129 ? 111.567 91.693  63.134  1.00 28.81 ? 126 VAL A O   1 
ATOM   970  C  CB  . VAL A 1 129 ? 109.720 88.951  62.979  1.00 27.22 ? 126 VAL A CB  1 
ATOM   971  C  CG1 . VAL A 1 129 ? 110.697 88.683  64.107  1.00 27.18 ? 126 VAL A CG1 1 
ATOM   972  C  CG2 . VAL A 1 129 ? 108.240 89.073  63.335  1.00 26.16 ? 126 VAL A CG2 1 
ATOM   973  N  N   . GLY A 1 130 ? 112.506 90.385  61.578  1.00 28.39 ? 127 GLY A N   1 
ATOM   974  C  CA  . GLY A 1 130 ? 113.806 91.046  61.555  1.00 28.82 ? 127 GLY A CA  1 
ATOM   975  C  C   . GLY A 1 130 ? 114.389 90.833  60.168  1.00 29.17 ? 127 GLY A C   1 
ATOM   976  O  O   . GLY A 1 130 ? 113.949 89.957  59.426  1.00 29.37 ? 127 GLY A O   1 
ATOM   977  N  N   . LYS A 1 131 ? 115.387 91.627  59.822  1.00 29.70 ? 128 LYS A N   1 
ATOM   978  C  CA  . LYS A 1 131 ? 115.956 91.645  58.472  1.00 29.71 ? 128 LYS A CA  1 
ATOM   979  C  C   . LYS A 1 131 ? 116.359 90.230  58.030  1.00 29.22 ? 128 LYS A C   1 
ATOM   980  O  O   . LYS A 1 131 ? 116.167 89.860  56.870  1.00 28.67 ? 128 LYS A O   1 
ATOM   981  C  CB  . LYS A 1 131 ? 117.156 92.586  58.455  1.00 29.51 ? 128 LYS A CB  1 
ATOM   982  C  CG  . LYS A 1 131 ? 117.506 93.175  57.130  1.00 31.79 ? 128 LYS A CG  1 
ATOM   983  C  CD  . LYS A 1 131 ? 118.493 94.325  57.392  1.00 36.11 ? 128 LYS A CD  1 
ATOM   984  C  CE  . LYS A 1 131 ? 118.355 95.471  56.385  1.00 36.11 ? 128 LYS A CE  1 
ATOM   985  N  NZ  . LYS A 1 131 ? 118.902 96.694  56.979  1.00 35.25 ? 128 LYS A NZ  1 
ATOM   986  N  N   . LYS A 1 132 ? 116.913 89.462  58.972  1.00 28.53 ? 129 LYS A N   1 
ATOM   987  C  CA  . LYS A 1 132 ? 117.311 88.065  58.753  1.00 28.11 ? 129 LYS A CA  1 
ATOM   988  C  C   . LYS A 1 132 ? 116.655 87.147  59.800  1.00 26.86 ? 129 LYS A C   1 
ATOM   989  O  O   . LYS A 1 132 ? 117.257 86.179  60.264  1.00 26.85 ? 129 LYS A O   1 
ATOM   990  C  CB  . LYS A 1 132 ? 118.840 87.936  58.839  1.00 28.48 ? 129 LYS A CB  1 
ATOM   991  C  CG  . LYS A 1 132 ? 119.549 88.522  57.676  1.00 31.12 ? 129 LYS A CG  1 
ATOM   992  C  CD  . LYS A 1 132 ? 120.990 88.044  57.542  1.00 35.36 ? 129 LYS A CD  1 
ATOM   993  C  CE  . LYS A 1 132 ? 121.440 88.184  56.066  1.00 37.94 ? 129 LYS A CE  1 
ATOM   994  N  NZ  . LYS A 1 132 ? 120.472 87.487  55.082  1.00 37.65 ? 129 LYS A NZ  1 
ATOM   995  N  N   . PHE A 1 133 ? 115.434 87.467  60.196  1.00 25.50 ? 130 PHE A N   1 
ATOM   996  C  CA  . PHE A 1 133 ? 114.808 86.728  61.255  1.00 24.62 ? 130 PHE A CA  1 
ATOM   997  C  C   . PHE A 1 133 ? 113.342 86.399  60.948  1.00 24.82 ? 130 PHE A C   1 
ATOM   998  O  O   . PHE A 1 133 ? 112.493 87.299  60.853  1.00 24.09 ? 130 PHE A O   1 
ATOM   999  C  CB  . PHE A 1 133 ? 114.974 87.430  62.620  1.00 24.44 ? 130 PHE A CB  1 
ATOM   1000 C  CG  . PHE A 1 133 ? 114.979 86.473  63.771  1.00 23.56 ? 130 PHE A CG  1 
ATOM   1001 C  CD1 . PHE A 1 133 ? 113.786 86.106  64.397  1.00 24.15 ? 130 PHE A CD1 1 
ATOM   1002 C  CD2 . PHE A 1 133 ? 116.159 85.882  64.189  1.00 24.26 ? 130 PHE A CD2 1 
ATOM   1003 C  CE1 . PHE A 1 133 ? 113.771 85.162  65.429  1.00 24.89 ? 130 PHE A CE1 1 
ATOM   1004 C  CE2 . PHE A 1 133 ? 116.169 84.958  65.245  1.00 25.56 ? 130 PHE A CE2 1 
ATOM   1005 C  CZ  . PHE A 1 133 ? 114.968 84.586  65.857  1.00 26.49 ? 130 PHE A CZ  1 
ATOM   1006 N  N   . THR A 1 134 ? 113.060 85.093  60.835  1.00 24.51 ? 131 THR A N   1 
ATOM   1007 C  CA  . THR A 1 134 ? 111.724 84.619  60.495  1.00 23.91 ? 131 THR A CA  1 
ATOM   1008 C  C   . THR A 1 134 ? 111.263 83.401  61.313  1.00 25.14 ? 131 THR A C   1 
ATOM   1009 O  O   . THR A 1 134 ? 111.864 83.055  62.337  1.00 25.90 ? 131 THR A O   1 
ATOM   1010 C  CB  . THR A 1 134 ? 111.556 84.443  58.968  1.00 23.25 ? 131 THR A CB  1 
ATOM   1011 O  OG1 . THR A 1 134 ? 110.174 84.323  58.650  1.00 21.21 ? 131 THR A OG1 1 
ATOM   1012 C  CG2 . THR A 1 134 ? 112.343 83.253  58.410  1.00 21.88 ? 131 THR A CG2 1 
ATOM   1013 N  N   . LEU A 1 135 ? 110.173 82.763  60.885  1.00 25.86 ? 132 LEU A N   1 
ATOM   1014 C  CA  . LEU A 1 135 ? 109.542 81.731  61.693  1.00 25.03 ? 132 LEU A CA  1 
ATOM   1015 C  C   . LEU A 1 135 ? 108.693 80.803  60.822  1.00 25.52 ? 132 LEU A C   1 
ATOM   1016 O  O   . LEU A 1 135 ? 107.543 80.451  61.159  1.00 25.76 ? 132 LEU A O   1 
ATOM   1017 C  CB  . LEU A 1 135 ? 108.740 82.377  62.840  1.00 24.91 ? 132 LEU A CB  1 
ATOM   1018 C  CG  . LEU A 1 135 ? 107.645 83.439  62.625  1.00 24.33 ? 132 LEU A CG  1 
ATOM   1019 C  CD1 . LEU A 1 135 ? 106.524 83.234  63.664  1.00 20.73 ? 132 LEU A CD1 1 
ATOM   1020 C  CD2 . LEU A 1 135 ? 108.213 84.882  62.666  1.00 21.93 ? 132 LEU A CD2 1 
ATOM   1021 N  N   . HIS A 1 136 ? 109.309 80.353  59.725  1.00 25.30 ? 133 HIS A N   1 
ATOM   1022 C  CA  . HIS A 1 136 ? 108.626 79.582  58.686  1.00 25.25 ? 133 HIS A CA  1 
ATOM   1023 C  C   . HIS A 1 136 ? 107.957 78.277  59.114  1.00 24.99 ? 133 HIS A C   1 
ATOM   1024 O  O   . HIS A 1 136 ? 106.954 77.862  58.504  1.00 24.83 ? 133 HIS A O   1 
ATOM   1025 C  CB  . HIS A 1 136 ? 109.568 79.321  57.485  1.00 24.48 ? 133 HIS A CB  1 
ATOM   1026 C  CG  . HIS A 1 136 ? 109.914 80.546  56.714  1.00 24.42 ? 133 HIS A CG  1 
ATOM   1027 N  ND1 . HIS A 1 136 ? 109.391 81.787  57.004  1.00 25.72 ? 133 HIS A ND1 1 
ATOM   1028 C  CD2 . HIS A 1 136 ? 110.715 80.722  55.637  1.00 25.50 ? 133 HIS A CD2 1 
ATOM   1029 C  CE1 . HIS A 1 136 ? 109.861 82.676  56.151  1.00 23.38 ? 133 HIS A CE1 1 
ATOM   1030 N  NE2 . HIS A 1 136 ? 110.661 82.053  55.307  1.00 24.56 ? 133 HIS A NE2 1 
ATOM   1031 N  N   . TYR A 1 137 ? 108.541 77.608  60.103  1.00 25.25 ? 134 TYR A N   1 
ATOM   1032 C  CA  . TYR A 1 137 ? 108.007 76.319  60.621  1.00 25.61 ? 134 TYR A CA  1 
ATOM   1033 C  C   . TYR A 1 137 ? 107.554 76.439  62.070  1.00 25.70 ? 134 TYR A C   1 
ATOM   1034 O  O   . TYR A 1 137 ? 107.021 75.494  62.663  1.00 27.16 ? 134 TYR A O   1 
ATOM   1035 C  CB  . TYR A 1 137 ? 108.985 75.143  60.355  1.00 25.57 ? 134 TYR A CB  1 
ATOM   1036 C  CG  . TYR A 1 137 ? 109.221 75.080  58.868  1.00 25.24 ? 134 TYR A CG  1 
ATOM   1037 C  CD1 . TYR A 1 137 ? 110.356 75.673  58.287  1.00 25.05 ? 134 TYR A CD1 1 
ATOM   1038 C  CD2 . TYR A 1 137 ? 108.243 74.560  58.029  1.00 26.03 ? 134 TYR A CD2 1 
ATOM   1039 C  CE1 . TYR A 1 137 ? 110.528 75.696  56.866  1.00 26.31 ? 134 TYR A CE1 1 
ATOM   1040 C  CE2 . TYR A 1 137 ? 108.388 74.589  56.599  1.00 25.63 ? 134 TYR A CE2 1 
ATOM   1041 C  CZ  . TYR A 1 137 ? 109.537 75.143  56.035  1.00 26.41 ? 134 TYR A CZ  1 
ATOM   1042 O  OH  . TYR A 1 137 ? 109.681 75.159  54.640  1.00 27.92 ? 134 TYR A OH  1 
ATOM   1043 N  N   . GLY A 1 138 ? 107.739 77.628  62.619  1.00 25.17 ? 135 GLY A N   1 
ATOM   1044 C  CA  . GLY A 1 138 ? 107.320 77.929  63.980  1.00 25.20 ? 135 GLY A CA  1 
ATOM   1045 C  C   . GLY A 1 138 ? 108.325 78.890  64.550  1.00 24.98 ? 135 GLY A C   1 
ATOM   1046 O  O   . GLY A 1 138 ? 109.393 79.106  63.956  1.00 25.94 ? 135 GLY A O   1 
ATOM   1047 N  N   . ALA A 1 139 ? 108.001 79.479  65.682  1.00 25.00 ? 136 ALA A N   1 
ATOM   1048 C  CA  . ALA A 1 139 ? 108.948 80.378  66.334  1.00 25.50 ? 136 ALA A CA  1 
ATOM   1049 C  C   . ALA A 1 139 ? 110.124 79.572  66.920  1.00 25.30 ? 136 ALA A C   1 
ATOM   1050 O  O   . ALA A 1 139 ? 109.922 78.601  67.612  1.00 25.95 ? 136 ALA A O   1 
ATOM   1051 C  CB  . ALA A 1 139 ? 108.238 81.246  67.396  1.00 24.84 ? 136 ALA A CB  1 
ATOM   1052 N  N   . VAL A 1 140 ? 111.355 79.956  66.596  1.00 25.91 ? 137 VAL A N   1 
ATOM   1053 C  CA  . VAL A 1 140 ? 112.556 79.259  67.086  1.00 25.43 ? 137 VAL A CA  1 
ATOM   1054 C  C   . VAL A 1 140 ? 113.570 80.305  67.626  1.00 26.37 ? 137 VAL A C   1 
ATOM   1055 O  O   . VAL A 1 140 ? 113.667 81.424  67.094  1.00 25.89 ? 137 VAL A O   1 
ATOM   1056 C  CB  . VAL A 1 140 ? 113.212 78.341  65.967  1.00 25.75 ? 137 VAL A CB  1 
ATOM   1057 C  CG1 . VAL A 1 140 ? 112.257 77.191  65.539  1.00 23.35 ? 137 VAL A CG1 1 
ATOM   1058 C  CG2 . VAL A 1 140 ? 113.646 79.180  64.716  1.00 23.84 ? 137 VAL A CG2 1 
ATOM   1059 N  N   . VAL A 1 141 ? 114.298 79.937  68.682  1.00 26.30 ? 138 VAL A N   1 
ATOM   1060 C  CA  . VAL A 1 141 ? 115.295 80.788  69.313  1.00 27.01 ? 138 VAL A CA  1 
ATOM   1061 C  C   . VAL A 1 141 ? 116.400 79.882  69.852  1.00 27.55 ? 138 VAL A C   1 
ATOM   1062 O  O   . VAL A 1 141 ? 116.153 78.710  70.159  1.00 28.34 ? 138 VAL A O   1 
ATOM   1063 C  CB  . VAL A 1 141 ? 114.674 81.646  70.501  1.00 27.67 ? 138 VAL A CB  1 
ATOM   1064 C  CG1 . VAL A 1 141 ? 115.750 82.461  71.176  1.00 28.53 ? 138 VAL A CG1 1 
ATOM   1065 C  CG2 . VAL A 1 141 ? 113.552 82.611  69.999  1.00 25.97 ? 138 VAL A CG2 1 
ATOM   1066 N  N   . ALA A 1 142 ? 117.626 80.383  69.951  1.00 27.54 ? 139 ALA A N   1 
ATOM   1067 C  CA  . ALA A 1 142 ? 118.613 79.672  70.734  1.00 28.25 ? 139 ALA A CA  1 
ATOM   1068 C  C   . ALA A 1 142 ? 118.669 80.301  72.135  1.00 28.99 ? 139 ALA A C   1 
ATOM   1069 O  O   . ALA A 1 142 ? 118.863 81.522  72.278  1.00 29.54 ? 139 ALA A O   1 
ATOM   1070 C  CB  . ALA A 1 142 ? 119.958 79.675  70.057  1.00 27.80 ? 139 ALA A CB  1 
ATOM   1071 N  N   . GLY A 1 143 ? 118.462 79.484  73.163  1.00 28.98 ? 140 GLY A N   1 
ATOM   1072 C  CA  . GLY A 1 143 ? 118.359 79.985  74.536  1.00 29.34 ? 140 GLY A CA  1 
ATOM   1073 C  C   . GLY A 1 143 ? 117.088 80.784  74.807  1.00 30.18 ? 140 GLY A C   1 
ATOM   1074 O  O   . GLY A 1 143 ? 116.021 80.490  74.262  1.00 29.28 ? 140 GLY A O   1 
ATOM   1075 N  N   . GLU A 1 144 ? 117.206 81.811  75.649  1.00 31.15 ? 141 GLU A N   1 
ATOM   1076 C  CA  . GLU A 1 144 ? 116.071 82.665  75.987  1.00 32.63 ? 141 GLU A CA  1 
ATOM   1077 C  C   . GLU A 1 144 ? 115.782 83.734  74.887  1.00 32.48 ? 141 GLU A C   1 
ATOM   1078 O  O   . GLU A 1 144 ? 116.711 84.303  74.315  1.00 32.04 ? 141 GLU A O   1 
ATOM   1079 C  CB  . GLU A 1 144 ? 116.302 83.311  77.363  1.00 31.84 ? 141 GLU A CB  1 
ATOM   1080 C  CG  . GLU A 1 144 ? 115.259 84.351  77.763  1.00 33.60 ? 141 GLU A CG  1 
ATOM   1081 C  CD  . GLU A 1 144 ? 115.611 85.130  79.029  1.00 35.93 ? 141 GLU A CD  1 
ATOM   1082 O  OE1 . GLU A 1 144 ? 116.788 85.116  79.481  1.00 39.48 ? 141 GLU A OE1 1 
ATOM   1083 O  OE2 . GLU A 1 144 ? 114.687 85.763  79.586  1.00 40.46 ? 141 GLU A OE2 1 
ATOM   1084 N  N   . PRO A 1 145 ? 114.488 84.016  74.609  1.00 33.26 ? 142 PRO A N   1 
ATOM   1085 C  CA  . PRO A 1 145 ? 114.199 85.106  73.656  1.00 34.17 ? 142 PRO A CA  1 
ATOM   1086 C  C   . PRO A 1 145 ? 114.594 86.441  74.268  1.00 34.97 ? 142 PRO A C   1 
ATOM   1087 O  O   . PRO A 1 145 ? 113.885 86.951  75.140  1.00 35.38 ? 142 PRO A O   1 
ATOM   1088 C  CB  . PRO A 1 145 ? 112.669 85.044  73.460  1.00 34.40 ? 142 PRO A CB  1 
ATOM   1089 C  CG  . PRO A 1 145 ? 112.149 83.980  74.413  1.00 32.96 ? 142 PRO A CG  1 
ATOM   1090 C  CD  . PRO A 1 145 ? 113.270 83.367  75.155  1.00 32.63 ? 142 PRO A CD  1 
ATOM   1091 N  N   . ARG A 1 146 ? 115.726 86.990  73.832  1.00 35.70 ? 143 ARG A N   1 
ATOM   1092 C  CA  . ARG A 1 146 ? 116.278 88.207  74.448  1.00 36.14 ? 143 ARG A CA  1 
ATOM   1093 C  C   . ARG A 1 146 ? 116.186 89.405  73.529  1.00 35.66 ? 143 ARG A C   1 
ATOM   1094 O  O   . ARG A 1 146 ? 115.808 90.482  73.967  1.00 36.00 ? 143 ARG A O   1 
ATOM   1095 C  CB  . ARG A 1 146 ? 117.729 88.006  74.885  1.00 36.35 ? 143 ARG A CB  1 
ATOM   1096 C  CG  . ARG A 1 146 ? 117.907 86.983  76.005  1.00 40.12 ? 143 ARG A CG  1 
ATOM   1097 C  CD  . ARG A 1 146 ? 119.257 87.153  76.693  1.00 46.12 ? 143 ARG A CD  1 
ATOM   1098 N  NE  . ARG A 1 146 ? 119.351 88.367  77.532  1.00 52.59 ? 143 ARG A NE  1 
ATOM   1099 C  CZ  . ARG A 1 146 ? 118.327 88.988  78.146  1.00 55.35 ? 143 ARG A CZ  1 
ATOM   1100 N  NH1 . ARG A 1 146 ? 118.557 90.081  78.873  1.00 54.04 ? 143 ARG A NH1 1 
ATOM   1101 N  NH2 . ARG A 1 146 ? 117.071 88.528  78.044  1.00 56.03 ? 143 ARG A NH2 1 
ATOM   1102 N  N   . SER A 1 147 ? 116.547 89.219  72.264  1.00 35.34 ? 144 SER A N   1 
ATOM   1103 C  CA  . SER A 1 147 ? 116.584 90.320  71.312  1.00 35.23 ? 144 SER A CA  1 
ATOM   1104 C  C   . SER A 1 147 ? 115.182 90.691  70.856  1.00 35.47 ? 144 SER A C   1 
ATOM   1105 O  O   . SER A 1 147 ? 114.244 89.884  70.925  1.00 35.43 ? 144 SER A O   1 
ATOM   1106 C  CB  . SER A 1 147 ? 117.471 89.997  70.105  1.00 34.92 ? 144 SER A CB  1 
ATOM   1107 O  OG  . SER A 1 147 ? 116.788 89.235  69.121  1.00 35.04 ? 144 SER A OG  1 
ATOM   1108 N  N   . GLU A 1 148 ? 115.058 91.924  70.383  1.00 35.59 ? 145 GLU A N   1 
ATOM   1109 C  CA  . GLU A 1 148 ? 113.794 92.440  69.904  1.00 35.85 ? 145 GLU A CA  1 
ATOM   1110 C  C   . GLU A 1 148 ? 113.121 91.536  68.846  1.00 35.40 ? 145 GLU A C   1 
ATOM   1111 O  O   . GLU A 1 148 ? 111.920 91.253  68.938  1.00 34.81 ? 145 GLU A O   1 
ATOM   1112 C  CB  . GLU A 1 148 ? 113.954 93.888  69.410  1.00 36.06 ? 145 GLU A CB  1 
ATOM   1113 C  CG  . GLU A 1 148 ? 112.641 94.652  69.456  1.00 39.27 ? 145 GLU A CG  1 
ATOM   1114 C  CD  . GLU A 1 148 ? 111.754 94.179  70.633  1.00 44.60 ? 145 GLU A CD  1 
ATOM   1115 O  OE1 . GLU A 1 148 ? 111.995 94.661  71.784  1.00 43.58 ? 145 GLU A OE1 1 
ATOM   1116 O  OE2 . GLU A 1 148 ? 110.847 93.304  70.401  1.00 45.14 ? 145 GLU A OE2 1 
ATOM   1117 N  N   . GLU A 1 149 ? 113.898 91.073  67.865  1.00 34.57 ? 146 GLU A N   1 
ATOM   1118 C  CA  . GLU A 1 149 ? 113.345 90.201  66.835  1.00 34.60 ? 146 GLU A CA  1 
ATOM   1119 C  C   . GLU A 1 149 ? 112.973 88.793  67.366  1.00 33.74 ? 146 GLU A C   1 
ATOM   1120 O  O   . GLU A 1 149 ? 111.966 88.213  66.930  1.00 33.31 ? 146 GLU A O   1 
ATOM   1121 C  CB  . GLU A 1 149 ? 114.245 90.156  65.588  1.00 34.32 ? 146 GLU A CB  1 
ATOM   1122 C  CG  . GLU A 1 149 ? 115.692 89.730  65.817  1.00 35.40 ? 146 GLU A CG  1 
ATOM   1123 C  CD  . GLU A 1 149 ? 116.580 89.955  64.576  1.00 36.29 ? 146 GLU A CD  1 
ATOM   1124 O  OE1 . GLU A 1 149 ? 117.584 89.217  64.401  1.00 37.19 ? 146 GLU A OE1 1 
ATOM   1125 O  OE2 . GLU A 1 149 ? 116.268 90.866  63.769  1.00 38.50 ? 146 GLU A OE2 1 
ATOM   1126 N  N   . GLU A 1 150 ? 113.749 88.278  68.327  1.00 32.66 ? 147 GLU A N   1 
ATOM   1127 C  CA  . GLU A 1 150 ? 113.428 87.009  68.973  1.00 32.19 ? 147 GLU A CA  1 
ATOM   1128 C  C   . GLU A 1 150 ? 112.123 87.099  69.740  1.00 31.92 ? 147 GLU A C   1 
ATOM   1129 O  O   . GLU A 1 150 ? 111.304 86.188  69.663  1.00 31.83 ? 147 GLU A O   1 
ATOM   1130 C  CB  . GLU A 1 150 ? 114.546 86.551  69.901  1.00 31.96 ? 147 GLU A CB  1 
ATOM   1131 C  CG  . GLU A 1 150 ? 115.768 86.155  69.134  1.00 33.19 ? 147 GLU A CG  1 
ATOM   1132 C  CD  . GLU A 1 150 ? 116.957 85.835  70.010  1.00 35.22 ? 147 GLU A CD  1 
ATOM   1133 O  OE1 . GLU A 1 150 ? 117.062 86.363  71.146  1.00 35.57 ? 147 GLU A OE1 1 
ATOM   1134 O  OE2 . GLU A 1 150 ? 117.794 85.030  69.546  1.00 37.07 ? 147 GLU A OE2 1 
ATOM   1135 N  N   . LYS A 1 151 ? 111.934 88.206  70.469  1.00 31.43 ? 148 LYS A N   1 
ATOM   1136 C  CA  . LYS A 1 151 ? 110.701 88.422  71.237  1.00 31.01 ? 148 LYS A CA  1 
ATOM   1137 C  C   . LYS A 1 151 ? 109.520 88.566  70.279  1.00 29.77 ? 148 LYS A C   1 
ATOM   1138 O  O   . LYS A 1 151 ? 108.438 88.010  70.516  1.00 29.22 ? 148 LYS A O   1 
ATOM   1139 C  CB  . LYS A 1 151 ? 110.846 89.599  72.221  1.00 30.64 ? 148 LYS A CB  1 
ATOM   1140 C  CG  . LYS A 1 151 ? 112.006 89.385  73.232  1.00 33.24 ? 148 LYS A CG  1 
ATOM   1141 C  CD  . LYS A 1 151 ? 111.859 90.107  74.593  1.00 32.41 ? 148 LYS A CD  1 
ATOM   1142 C  CE  . LYS A 1 151 ? 112.718 91.395  74.725  1.00 37.88 ? 148 LYS A CE  1 
ATOM   1143 N  NZ  . LYS A 1 151 ? 112.780 92.003  76.145  1.00 36.09 ? 148 LYS A NZ  1 
ATOM   1144 N  N   . GLU A 1 152 ? 109.770 89.254  69.164  1.00 29.18 ? 149 GLU A N   1 
ATOM   1145 C  CA  . GLU A 1 152 ? 108.739 89.556  68.164  1.00 28.22 ? 149 GLU A CA  1 
ATOM   1146 C  C   . GLU A 1 152 ? 108.320 88.337  67.355  1.00 27.86 ? 149 GLU A C   1 
ATOM   1147 O  O   . GLU A 1 152 ? 107.144 88.198  67.040  1.00 27.81 ? 149 GLU A O   1 
ATOM   1148 C  CB  . GLU A 1 152 ? 109.152 90.738  67.261  1.00 27.94 ? 149 GLU A CB  1 
ATOM   1149 C  CG  . GLU A 1 152 ? 108.026 91.342  66.394  1.00 26.79 ? 149 GLU A CG  1 
ATOM   1150 C  CD  . GLU A 1 152 ? 106.724 91.659  67.151  1.00 28.50 ? 149 GLU A CD  1 
ATOM   1151 O  OE1 . GLU A 1 152 ? 105.645 91.463  66.552  1.00 28.45 ? 149 GLU A OE1 1 
ATOM   1152 O  OE2 . GLU A 1 152 ? 106.760 92.090  68.338  1.00 29.30 ? 149 GLU A OE2 1 
ATOM   1153 N  N   . ALA A 1 153 ? 109.271 87.450  67.041  1.00 27.50 ? 150 ALA A N   1 
ATOM   1154 C  CA  . ALA A 1 153 ? 108.955 86.154  66.397  1.00 26.39 ? 150 ALA A CA  1 
ATOM   1155 C  C   . ALA A 1 153 ? 107.892 85.395  67.197  1.00 26.51 ? 150 ALA A C   1 
ATOM   1156 O  O   . ALA A 1 153 ? 106.955 84.842  66.622  1.00 25.86 ? 150 ALA A O   1 
ATOM   1157 C  CB  . ALA A 1 153 ? 110.216 85.309  66.252  1.00 25.48 ? 150 ALA A CB  1 
ATOM   1158 N  N   . CYS A 1 154 ? 108.056 85.398  68.526  1.00 26.68 ? 151 CYS A N   1 
ATOM   1159 C  CA  . CYS A 1 154 ? 107.196 84.674  69.454  1.00 27.62 ? 151 CYS A CA  1 
ATOM   1160 C  C   . CYS A 1 154 ? 105.828 85.271  69.477  1.00 27.30 ? 151 CYS A C   1 
ATOM   1161 O  O   . CYS A 1 154 ? 104.844 84.574  69.380  1.00 28.74 ? 151 CYS A O   1 
ATOM   1162 C  CB  . CYS A 1 154 ? 107.773 84.686  70.867  1.00 27.26 ? 151 CYS A CB  1 
ATOM   1163 S  SG  . CYS A 1 154 ? 109.272 83.683  71.057  1.00 32.23 ? 151 CYS A SG  1 
ATOM   1164 N  N   . ARG A 1 155 ? 105.774 86.576  69.603  1.00 27.38 ? 152 ARG A N   1 
ATOM   1165 C  CA  . ARG A 1 155 ? 104.542 87.296  69.482  1.00 26.72 ? 152 ARG A CA  1 
ATOM   1166 C  C   . ARG A 1 155 ? 103.844 87.047  68.146  1.00 27.11 ? 152 ARG A C   1 
ATOM   1167 O  O   . ARG A 1 155 ? 102.633 86.791  68.118  1.00 27.50 ? 152 ARG A O   1 
ATOM   1168 C  CB  . ARG A 1 155 ? 104.813 88.773  69.672  1.00 26.80 ? 152 ARG A CB  1 
ATOM   1169 C  CG  . ARG A 1 155 ? 105.239 89.185  71.063  1.00 24.33 ? 152 ARG A CG  1 
ATOM   1170 C  CD  . ARG A 1 155 ? 105.098 90.725  71.210  1.00 24.91 ? 152 ARG A CD  1 
ATOM   1171 N  NE  . ARG A 1 155 ? 105.844 91.201  72.373  1.00 25.98 ? 152 ARG A NE  1 
ATOM   1172 C  CZ  . ARG A 1 155 ? 107.069 91.728  72.328  1.00 27.39 ? 152 ARG A CZ  1 
ATOM   1173 N  NH1 . ARG A 1 155 ? 107.689 91.895  71.158  1.00 27.80 ? 152 ARG A NH1 1 
ATOM   1174 N  NH2 . ARG A 1 155 ? 107.674 92.109  73.459  1.00 26.13 ? 152 ARG A NH2 1 
ATOM   1175 N  N   . ARG A 1 156 ? 104.590 87.105  67.047  1.00 26.79 ? 153 ARG A N   1 
ATOM   1176 C  CA  . ARG A 1 156 ? 103.983 86.940  65.723  1.00 27.07 ? 153 ARG A CA  1 
ATOM   1177 C  C   . ARG A 1 156 ? 103.268 85.593  65.525  1.00 27.67 ? 153 ARG A C   1 
ATOM   1178 O  O   . ARG A 1 156 ? 102.185 85.540  64.904  1.00 27.82 ? 153 ARG A O   1 
ATOM   1179 C  CB  . ARG A 1 156 ? 104.993 87.162  64.591  1.00 26.91 ? 153 ARG A CB  1 
ATOM   1180 C  CG  . ARG A 1 156 ? 104.328 87.247  63.212  1.00 26.45 ? 153 ARG A CG  1 
ATOM   1181 C  CD  . ARG A 1 156 ? 103.360 88.468  63.153  1.00 27.58 ? 153 ARG A CD  1 
ATOM   1182 N  NE  . ARG A 1 156 ? 104.018 89.621  63.752  1.00 25.84 ? 153 ARG A NE  1 
ATOM   1183 C  CZ  . ARG A 1 156 ? 104.784 90.477  63.089  1.00 23.61 ? 153 ARG A CZ  1 
ATOM   1184 N  NH1 . ARG A 1 156 ? 105.358 91.464  63.740  1.00 20.60 ? 153 ARG A NH1 1 
ATOM   1185 N  NH2 . ARG A 1 156 ? 104.959 90.363  61.785  1.00 22.53 ? 153 ARG A NH2 1 
ATOM   1186 N  N   . LEU A 1 157 ? 103.881 84.520  66.036  1.00 27.44 ? 154 LEU A N   1 
ATOM   1187 C  CA  . LEU A 1 157 ? 103.259 83.209  66.021  1.00 27.04 ? 154 LEU A CA  1 
ATOM   1188 C  C   . LEU A 1 157 ? 101.852 83.207  66.607  1.00 27.17 ? 154 LEU A C   1 
ATOM   1189 O  O   . LEU A 1 157 ? 100.921 82.743  65.967  1.00 26.71 ? 154 LEU A O   1 
ATOM   1190 C  CB  . LEU A 1 157 ? 104.134 82.184  66.735  1.00 26.38 ? 154 LEU A CB  1 
ATOM   1191 C  CG  . LEU A 1 157 ? 103.623 80.739  66.494  1.00 26.47 ? 154 LEU A CG  1 
ATOM   1192 C  CD1 . LEU A 1 157 ? 103.877 80.213  65.016  1.00 24.91 ? 154 LEU A CD1 1 
ATOM   1193 C  CD2 . LEU A 1 157 ? 104.175 79.817  67.529  1.00 22.09 ? 154 LEU A CD2 1 
ATOM   1194 N  N   . GLY A 1 158 ? 101.707 83.731  67.831  1.00 27.82 ? 155 GLY A N   1 
ATOM   1195 C  CA  . GLY A 1 158 ? 100.421 83.777  68.514  1.00 27.25 ? 155 GLY A CA  1 
ATOM   1196 C  C   . GLY A 1 158 ? 99.425  84.663  67.797  1.00 27.27 ? 155 GLY A C   1 
ATOM   1197 O  O   . GLY A 1 158 ? 98.233  84.332  67.736  1.00 27.50 ? 155 GLY A O   1 
ATOM   1198 N  N   . ARG A 1 159 ? 99.925  85.789  67.278  1.00 26.86 ? 156 ARG A N   1 
ATOM   1199 C  CA  . ARG A 1 159 ? 99.190  86.738  66.424  1.00 26.98 ? 156 ARG A CA  1 
ATOM   1200 C  C   . ARG A 1 159 ? 98.578  86.047  65.203  1.00 26.45 ? 156 ARG A C   1 
ATOM   1201 O  O   . ARG A 1 159 ? 97.386  86.190  64.941  1.00 25.97 ? 156 ARG A O   1 
ATOM   1202 C  CB  . ARG A 1 159 ? 100.159 87.804  65.899  1.00 27.03 ? 156 ARG A CB  1 
ATOM   1203 C  CG  . ARG A 1 159 ? 99.651  89.211  65.743  1.00 27.44 ? 156 ARG A CG  1 
ATOM   1204 C  CD  . ARG A 1 159 ? 98.237  89.394  65.216  1.00 31.19 ? 156 ARG A CD  1 
ATOM   1205 N  NE  . ARG A 1 159 ? 97.540  90.298  66.113  1.00 34.62 ? 156 ARG A NE  1 
ATOM   1206 C  CZ  . ARG A 1 159 ? 97.128  91.537  65.863  1.00 33.69 ? 156 ARG A CZ  1 
ATOM   1207 N  NH1 . ARG A 1 159 ? 97.228  92.107  64.677  1.00 35.85 ? 156 ARG A NH1 1 
ATOM   1208 N  NH2 . ARG A 1 159 ? 96.559  92.193  66.840  1.00 33.34 ? 156 ARG A NH2 1 
ATOM   1209 N  N   . ARG A 1 160 ? 99.418  85.345  64.442  1.00 26.03 ? 157 ARG A N   1 
ATOM   1210 C  CA  . ARG A 1 160 ? 98.962  84.650  63.252  1.00 26.18 ? 157 ARG A CA  1 
ATOM   1211 C  C   . ARG A 1 160 ? 98.019  83.500  63.607  1.00 26.78 ? 157 ARG A C   1 
ATOM   1212 O  O   . ARG A 1 160 ? 97.039  83.259  62.906  1.00 27.67 ? 157 ARG A O   1 
ATOM   1213 C  CB  . ARG A 1 160 ? 100.145 84.201  62.384  1.00 25.60 ? 157 ARG A CB  1 
ATOM   1214 C  CG  . ARG A 1 160 ? 99.778  83.761  60.945  1.00 24.74 ? 157 ARG A CG  1 
ATOM   1215 C  CD  . ARG A 1 160 ? 99.055  84.809  60.073  1.00 24.18 ? 157 ARG A CD  1 
ATOM   1216 N  NE  . ARG A 1 160 ? 99.517  86.186  60.290  1.00 26.91 ? 157 ARG A NE  1 
ATOM   1217 C  CZ  . ARG A 1 160 ? 100.681 86.692  59.853  1.00 26.23 ? 157 ARG A CZ  1 
ATOM   1218 N  NH1 . ARG A 1 160 ? 101.535 85.948  59.152  1.00 22.81 ? 157 ARG A NH1 1 
ATOM   1219 N  NH2 . ARG A 1 160 ? 100.987 87.956  60.125  1.00 24.64 ? 157 ARG A NH2 1 
ATOM   1220 N  N   . LEU A 1 161 ? 98.305  82.802  64.706  1.00 27.11 ? 158 LEU A N   1 
ATOM   1221 C  CA  . LEU A 1 161 ? 97.401  81.772  65.219  1.00 26.25 ? 158 LEU A CA  1 
ATOM   1222 C  C   . LEU A 1 161 ? 96.020  82.353  65.473  1.00 25.63 ? 158 LEU A C   1 
ATOM   1223 O  O   . LEU A 1 161 ? 95.019  81.788  65.025  1.00 26.51 ? 158 LEU A O   1 
ATOM   1224 C  CB  . LEU A 1 161 ? 97.942  81.191  66.513  1.00 25.96 ? 158 LEU A CB  1 
ATOM   1225 C  CG  . LEU A 1 161 ? 97.648  79.744  66.922  1.00 26.21 ? 158 LEU A CG  1 
ATOM   1226 C  CD1 . LEU A 1 161 ? 97.686  79.656  68.423  1.00 18.59 ? 158 LEU A CD1 1 
ATOM   1227 C  CD2 . LEU A 1 161 ? 96.363  79.109  66.339  1.00 23.77 ? 158 LEU A CD2 1 
ATOM   1228 N  N   . ALA A 1 162 ? 95.973  83.492  66.159  1.00 25.20 ? 159 ALA A N   1 
ATOM   1229 C  CA  . ALA A 1 162 ? 94.710  84.121  66.541  1.00 24.90 ? 159 ALA A CA  1 
ATOM   1230 C  C   . ALA A 1 162 ? 93.976  84.624  65.304  1.00 25.25 ? 159 ALA A C   1 
ATOM   1231 O  O   . ALA A 1 162 ? 92.747  84.535  65.216  1.00 25.53 ? 159 ALA A O   1 
ATOM   1232 C  CB  . ALA A 1 162 ? 94.958  85.254  67.509  1.00 24.72 ? 159 ALA A CB  1 
ATOM   1233 N  N   . GLU A 1 163 ? 94.744  85.145  64.356  1.00 25.29 ? 160 GLU A N   1 
ATOM   1234 C  CA  . GLU A 1 163 ? 94.239  85.588  63.064  1.00 25.63 ? 160 GLU A CA  1 
ATOM   1235 C  C   . GLU A 1 163 ? 93.669  84.447  62.221  1.00 25.60 ? 160 GLU A C   1 
ATOM   1236 O  O   . GLU A 1 163 ? 92.630  84.611  61.618  1.00 25.39 ? 160 GLU A O   1 
ATOM   1237 C  CB  . GLU A 1 163 ? 95.338  86.323  62.319  1.00 25.01 ? 160 GLU A CB  1 
ATOM   1238 C  CG  . GLU A 1 163 ? 95.625  87.716  62.897  1.00 26.50 ? 160 GLU A CG  1 
ATOM   1239 C  CD  . GLU A 1 163 ? 96.907  88.365  62.322  1.00 27.31 ? 160 GLU A CD  1 
ATOM   1240 O  OE1 . GLU A 1 163 ? 97.775  87.614  61.797  1.00 28.99 ? 160 GLU A OE1 1 
ATOM   1241 O  OE2 . GLU A 1 163 ? 97.048  89.615  62.421  1.00 26.08 ? 160 GLU A OE2 1 
ATOM   1242 N  N   . TRP A 1 164 ? 94.326  83.283  62.192  1.00 26.16 ? 161 TRP A N   1 
ATOM   1243 C  CA  . TRP A 1 164 ? 93.779  82.144  61.437  1.00 26.35 ? 161 TRP A CA  1 
ATOM   1244 C  C   . TRP A 1 164 ? 92.501  81.618  62.111  1.00 26.24 ? 161 TRP A C   1 
ATOM   1245 O  O   . TRP A 1 164 ? 91.530  81.255  61.436  1.00 25.48 ? 161 TRP A O   1 
ATOM   1246 C  CB  . TRP A 1 164 ? 94.791  80.997  61.291  1.00 26.40 ? 161 TRP A CB  1 
ATOM   1247 C  CG  . TRP A 1 164 ? 95.988  81.237  60.390  1.00 26.77 ? 161 TRP A CG  1 
ATOM   1248 C  CD1 . TRP A 1 164 ? 97.197  80.670  60.533  1.00 26.27 ? 161 TRP A CD1 1 
ATOM   1249 C  CD2 . TRP A 1 164 ? 96.078  82.080  59.220  1.00 26.79 ? 161 TRP A CD2 1 
ATOM   1250 N  NE1 . TRP A 1 164 ? 98.055  81.091  59.544  1.00 25.97 ? 161 TRP A NE1 1 
ATOM   1251 C  CE2 . TRP A 1 164 ? 97.399  81.950  58.717  1.00 25.84 ? 161 TRP A CE2 1 
ATOM   1252 C  CE3 . TRP A 1 164 ? 95.182  82.934  58.555  1.00 28.72 ? 161 TRP A CE3 1 
ATOM   1253 C  CZ2 . TRP A 1 164 ? 97.860  82.641  57.591  1.00 24.14 ? 161 TRP A CZ2 1 
ATOM   1254 C  CZ3 . TRP A 1 164 ? 95.632  83.626  57.418  1.00 26.54 ? 161 TRP A CZ3 1 
ATOM   1255 C  CH2 . TRP A 1 164 ? 96.971  83.465  56.951  1.00 27.11 ? 161 TRP A CH2 1 
ATOM   1256 N  N   . VAL A 1 165 ? 92.512  81.574  63.444  1.00 26.24 ? 162 VAL A N   1 
ATOM   1257 C  CA  . VAL A 1 165 ? 91.294  81.252  64.201  1.00 26.06 ? 162 VAL A CA  1 
ATOM   1258 C  C   . VAL A 1 165 ? 90.158  82.213  63.865  1.00 26.09 ? 162 VAL A C   1 
ATOM   1259 O  O   . VAL A 1 165 ? 89.048  81.785  63.621  1.00 26.87 ? 162 VAL A O   1 
ATOM   1260 C  CB  . VAL A 1 165 ? 91.543  81.229  65.716  1.00 26.03 ? 162 VAL A CB  1 
ATOM   1261 C  CG1 . VAL A 1 165 ? 90.205  81.284  66.502  1.00 25.26 ? 162 VAL A CG1 1 
ATOM   1262 C  CG2 . VAL A 1 165 ? 92.385  80.004  66.100  1.00 24.84 ? 162 VAL A CG2 1 
ATOM   1263 N  N   . ALA A 1 166 ? 90.462  83.503  63.822  1.00 26.50 ? 163 ALA A N   1 
ATOM   1264 C  CA  . ALA A 1 166 ? 89.499  84.567  63.537  1.00 26.58 ? 163 ALA A CA  1 
ATOM   1265 C  C   . ALA A 1 166 ? 88.930  84.490  62.126  1.00 27.30 ? 163 ALA A C   1 
ATOM   1266 O  O   . ALA A 1 166 ? 87.743  84.782  61.907  1.00 27.88 ? 163 ALA A O   1 
ATOM   1267 C  CB  . ALA A 1 166 ? 90.158  85.924  63.748  1.00 26.15 ? 163 ALA A CB  1 
ATOM   1268 N  N   . ILE A 1 167 ? 89.787  84.140  61.171  1.00 27.72 ? 164 ILE A N   1 
ATOM   1269 C  CA  . ILE A 1 167 ? 89.401  84.045  59.758  1.00 28.13 ? 164 ILE A CA  1 
ATOM   1270 C  C   . ILE A 1 167 ? 88.566  82.801  59.513  1.00 28.16 ? 164 ILE A C   1 
ATOM   1271 O  O   . ILE A 1 167 ? 87.438  82.890  59.030  1.00 28.48 ? 164 ILE A O   1 
ATOM   1272 C  CB  . ILE A 1 167 ? 90.645  84.073  58.820  1.00 28.16 ? 164 ILE A CB  1 
ATOM   1273 C  CG1 . ILE A 1 167 ? 91.231  85.484  58.788  1.00 27.90 ? 164 ILE A CG1 1 
ATOM   1274 C  CG2 . ILE A 1 167 ? 90.302  83.629  57.397  1.00 26.92 ? 164 ILE A CG2 1 
ATOM   1275 C  CD1 . ILE A 1 167 ? 92.625  85.542  58.175  1.00 28.62 ? 164 ILE A CD1 1 
ATOM   1276 N  N   . PHE A 1 168 ? 89.119  81.657  59.895  1.00 28.23 ? 165 PHE A N   1 
ATOM   1277 C  CA  . PHE A 1 168 ? 88.578  80.358  59.547  1.00 28.16 ? 165 PHE A CA  1 
ATOM   1278 C  C   . PHE A 1 168 ? 87.533  79.787  60.486  1.00 28.14 ? 165 PHE A C   1 
ATOM   1279 O  O   . PHE A 1 168 ? 86.710  79.001  60.038  1.00 28.07 ? 165 PHE A O   1 
ATOM   1280 C  CB  . PHE A 1 168 ? 89.725  79.359  59.347  1.00 28.74 ? 165 PHE A CB  1 
ATOM   1281 C  CG  . PHE A 1 168 ? 90.694  79.786  58.287  1.00 30.05 ? 165 PHE A CG  1 
ATOM   1282 C  CD1 . PHE A 1 168 ? 92.039  79.983  58.594  1.00 30.83 ? 165 PHE A CD1 1 
ATOM   1283 C  CD2 . PHE A 1 168 ? 90.244  80.044  56.975  1.00 30.28 ? 165 PHE A CD2 1 
ATOM   1284 C  CE1 . PHE A 1 168 ? 92.940  80.398  57.610  1.00 31.15 ? 165 PHE A CE1 1 
ATOM   1285 C  CE2 . PHE A 1 168 ? 91.121  80.464  55.991  1.00 30.77 ? 165 PHE A CE2 1 
ATOM   1286 C  CZ  . PHE A 1 168 ? 92.480  80.649  56.308  1.00 30.95 ? 165 PHE A CZ  1 
ATOM   1287 N  N   . VAL A 1 169 ? 87.544  80.142  61.768  1.00 28.30 ? 166 VAL A N   1 
ATOM   1288 C  CA  . VAL A 1 169 ? 86.453  79.655  62.621  1.00 28.97 ? 166 VAL A CA  1 
ATOM   1289 C  C   . VAL A 1 169 ? 85.441  80.720  63.000  1.00 30.01 ? 166 VAL A C   1 
ATOM   1290 O  O   . VAL A 1 169 ? 84.241  80.443  63.021  1.00 29.99 ? 166 VAL A O   1 
ATOM   1291 C  CB  . VAL A 1 169 ? 86.888  78.741  63.837  1.00 28.71 ? 166 VAL A CB  1 
ATOM   1292 C  CG1 . VAL A 1 169 ? 88.340  78.243  63.694  1.00 28.44 ? 166 VAL A CG1 1 
ATOM   1293 C  CG2 . VAL A 1 169 ? 86.649  79.394  65.160  1.00 27.87 ? 166 VAL A CG2 1 
ATOM   1294 N  N   . ASP A 1 170 ? 85.915  81.937  63.269  1.00 31.14 ? 167 ASP A N   1 
ATOM   1295 C  CA  . ASP A 1 170 ? 85.014  83.045  63.550  1.00 32.44 ? 167 ASP A CA  1 
ATOM   1296 C  C   . ASP A 1 170 ? 84.433  83.616  62.258  1.00 32.26 ? 167 ASP A C   1 
ATOM   1297 O  O   . ASP A 1 170 ? 83.334  84.153  62.248  1.00 32.05 ? 167 ASP A O   1 
ATOM   1298 C  CB  . ASP A 1 170 ? 85.706  84.163  64.325  1.00 33.36 ? 167 ASP A CB  1 
ATOM   1299 C  CG  . ASP A 1 170 ? 84.718  85.241  64.785  1.00 37.61 ? 167 ASP A CG  1 
ATOM   1300 O  OD1 . ASP A 1 170 ? 84.845  86.427  64.360  1.00 40.85 ? 167 ASP A OD1 1 
ATOM   1301 O  OD2 . ASP A 1 170 ? 83.778  84.886  65.548  1.00 41.98 ? 167 ASP A OD2 1 
ATOM   1302 N  N   . GLY A 1 171 ? 85.188  83.512  61.175  1.00 32.45 ? 168 GLY A N   1 
ATOM   1303 C  CA  . GLY A 1 171 ? 84.693  83.900  59.883  1.00 32.40 ? 168 GLY A CA  1 
ATOM   1304 C  C   . GLY A 1 171 ? 84.923  85.336  59.473  1.00 32.43 ? 168 GLY A C   1 
ATOM   1305 O  O   . GLY A 1 171 ? 84.268  85.784  58.554  1.00 32.00 ? 168 GLY A O   1 
ATOM   1306 N  N   . ARG A 1 172 ? 85.843  86.049  60.133  1.00 33.02 ? 169 ARG A N   1 
ATOM   1307 C  CA  . ARG A 1 172 ? 86.338  87.363  59.645  1.00 33.81 ? 169 ARG A CA  1 
ATOM   1308 C  C   . ARG A 1 172 ? 87.062  87.269  58.278  1.00 34.52 ? 169 ARG A C   1 
ATOM   1309 O  O   . ARG A 1 172 ? 88.279  87.461  58.182  1.00 34.84 ? 169 ARG A O   1 
ATOM   1310 C  CB  . ARG A 1 172 ? 87.231  88.071  60.695  1.00 33.55 ? 169 ARG A CB  1 
ATOM   1311 C  CG  . ARG A 1 172 ? 86.532  88.371  62.044  1.00 33.90 ? 169 ARG A CG  1 
ATOM   1312 C  CD  . ARG A 1 172 ? 87.391  89.210  62.999  1.00 34.05 ? 169 ARG A CD  1 
ATOM   1313 N  NE  . ARG A 1 172 ? 87.550  88.540  64.300  1.00 35.28 ? 169 ARG A NE  1 
ATOM   1314 C  CZ  . ARG A 1 172 ? 88.400  88.914  65.268  1.00 35.96 ? 169 ARG A CZ  1 
ATOM   1315 N  NH1 . ARG A 1 172 ? 88.461  88.217  66.405  1.00 35.84 ? 169 ARG A NH1 1 
ATOM   1316 N  NH2 . ARG A 1 172 ? 89.189  89.981  65.116  1.00 33.82 ? 169 ARG A NH2 1 
ATOM   1317 N  N   . LYS A 1 173 ? 86.291  86.988  57.231  1.00 35.57 ? 170 LYS A N   1 
ATOM   1318 C  CA  . LYS A 1 173 ? 86.791  86.803  55.864  1.00 36.91 ? 170 LYS A CA  1 
ATOM   1319 C  C   . LYS A 1 173 ? 87.632  87.968  55.375  1.00 37.43 ? 170 LYS A C   1 
ATOM   1320 O  O   . LYS A 1 173 ? 88.486  87.787  54.499  1.00 37.68 ? 170 LYS A O   1 
ATOM   1321 C  CB  . LYS A 1 173 ? 85.626  86.577  54.876  1.00 36.94 ? 170 LYS A CB  1 
ATOM   1322 C  CG  . LYS A 1 173 ? 84.753  85.366  55.202  1.00 39.01 ? 170 LYS A CG  1 
ATOM   1323 C  CD  . LYS A 1 173 ? 84.254  84.635  53.948  1.00 42.96 ? 170 LYS A CD  1 
ATOM   1324 C  CE  . LYS A 1 173 ? 82.810  85.006  53.595  1.00 44.02 ? 170 LYS A CE  1 
ATOM   1325 N  NZ  . LYS A 1 173 ? 82.147  83.916  52.809  1.00 44.56 ? 170 LYS A NZ  1 
ATOM   1326 N  N   . GLU A 1 174 ? 87.371  89.150  55.940  1.00 37.97 ? 171 GLU A N   1 
ATOM   1327 C  CA  . GLU A 1 174 ? 88.003  90.414  55.537  1.00 38.66 ? 171 GLU A CA  1 
ATOM   1328 C  C   . GLU A 1 174 ? 89.473  90.527  55.982  1.00 38.04 ? 171 GLU A C   1 
ATOM   1329 O  O   . GLU A 1 174 ? 90.271  91.226  55.356  1.00 38.02 ? 171 GLU A O   1 
ATOM   1330 C  CB  . GLU A 1 174 ? 87.191  91.600  56.081  1.00 39.42 ? 171 GLU A CB  1 
ATOM   1331 C  CG  . GLU A 1 174 ? 87.189  91.721  57.653  1.00 43.17 ? 171 GLU A CG  1 
ATOM   1332 C  CD  . GLU A 1 174 ? 85.914  91.193  58.354  1.00 46.25 ? 171 GLU A CD  1 
ATOM   1333 O  OE1 . GLU A 1 174 ? 85.869  91.246  59.610  1.00 47.18 ? 171 GLU A OE1 1 
ATOM   1334 O  OE2 . GLU A 1 174 ? 84.959  90.743  57.668  1.00 48.50 ? 171 GLU A OE2 1 
ATOM   1335 N  N   . LEU A 1 175 ? 89.813  89.837  57.065  1.00 37.37 ? 172 LEU A N   1 
ATOM   1336 C  CA  . LEU A 1 175 ? 91.170  89.821  57.597  1.00 36.85 ? 172 LEU A CA  1 
ATOM   1337 C  C   . LEU A 1 175 ? 92.190  89.167  56.676  1.00 35.95 ? 172 LEU A C   1 
ATOM   1338 O  O   . LEU A 1 175 ? 93.387  89.447  56.784  1.00 35.91 ? 172 LEU A O   1 
ATOM   1339 C  CB  . LEU A 1 175 ? 91.213  89.083  58.937  1.00 37.04 ? 172 LEU A CB  1 
ATOM   1340 C  CG  . LEU A 1 175 ? 91.385  89.852  60.248  1.00 38.93 ? 172 LEU A CG  1 
ATOM   1341 C  CD1 . LEU A 1 175 ? 91.542  88.874  61.426  1.00 37.65 ? 172 LEU A CD1 1 
ATOM   1342 C  CD2 . LEU A 1 175 ? 92.558  90.849  60.174  1.00 40.08 ? 172 LEU A CD2 1 
ATOM   1343 N  N   . LEU A 1 176 ? 91.737  88.278  55.798  1.00 34.77 ? 173 LEU A N   1 
ATOM   1344 C  CA  . LEU A 1 176 ? 92.664  87.538  54.942  1.00 34.15 ? 173 LEU A CA  1 
ATOM   1345 C  C   . LEU A 1 176 ? 93.476  88.499  54.068  1.00 34.02 ? 173 LEU A C   1 
ATOM   1346 O  O   . LEU A 1 176 ? 94.716  88.455  54.078  1.00 33.92 ? 173 LEU A O   1 
ATOM   1347 C  CB  . LEU A 1 176 ? 91.923  86.520  54.076  1.00 33.49 ? 173 LEU A CB  1 
ATOM   1348 C  CG  . LEU A 1 176 ? 92.423  85.073  54.011  1.00 33.22 ? 173 LEU A CG  1 
ATOM   1349 C  CD1 . LEU A 1 176 ? 91.855  84.433  52.744  1.00 31.24 ? 173 LEU A CD1 1 
ATOM   1350 C  CD2 . LEU A 1 176 ? 93.946  84.924  54.083  1.00 28.58 ? 173 LEU A CD2 1 
ATOM   1351 N  N   . GLU A 1 177 ? 92.770  89.377  53.352  1.00 33.82 ? 174 GLU A N   1 
ATOM   1352 C  CA  . GLU A 1 177 ? 93.387  90.361  52.471  1.00 33.83 ? 174 GLU A CA  1 
ATOM   1353 C  C   . GLU A 1 177 ? 94.157  91.423  53.235  1.00 33.06 ? 174 GLU A C   1 
ATOM   1354 O  O   . GLU A 1 177 ? 95.209  91.870  52.789  1.00 32.90 ? 174 GLU A O   1 
ATOM   1355 C  CB  . GLU A 1 177 ? 92.338  91.005  51.554  1.00 34.45 ? 174 GLU A CB  1 
ATOM   1356 C  CG  . GLU A 1 177 ? 92.844  91.363  50.135  1.00 37.45 ? 174 GLU A CG  1 
ATOM   1357 C  CD  . GLU A 1 177 ? 93.660  90.223  49.463  1.00 41.80 ? 174 GLU A CD  1 
ATOM   1358 O  OE1 . GLU A 1 177 ? 94.570  90.557  48.678  1.00 43.65 ? 174 GLU A OE1 1 
ATOM   1359 O  OE2 . GLU A 1 177 ? 93.410  89.006  49.714  1.00 41.68 ? 174 GLU A OE2 1 
ATOM   1360 N  N   . LYS A 1 178 ? 93.632  91.837  54.378  1.00 32.62 ? 175 LYS A N   1 
ATOM   1361 C  CA  . LYS A 1 178 ? 94.354  92.745  55.238  1.00 33.05 ? 175 LYS A CA  1 
ATOM   1362 C  C   . LYS A 1 178 ? 95.761  92.185  55.501  1.00 32.04 ? 175 LYS A C   1 
ATOM   1363 O  O   . LYS A 1 178 ? 96.765  92.887  55.305  1.00 31.76 ? 175 LYS A O   1 
ATOM   1364 C  CB  . LYS A 1 178 ? 93.599  92.957  56.552  1.00 33.08 ? 175 LYS A CB  1 
ATOM   1365 C  CG  . LYS A 1 178 ? 94.530  93.262  57.758  1.00 35.77 ? 175 LYS A CG  1 
ATOM   1366 C  CD  . LYS A 1 178 ? 93.807  93.835  59.006  1.00 35.86 ? 175 LYS A CD  1 
ATOM   1367 C  CE  . LYS A 1 178 ? 93.262  95.236  58.782  1.00 38.56 ? 175 LYS A CE  1 
ATOM   1368 N  NZ  . LYS A 1 178 ? 94.367  96.224  58.828  1.00 41.31 ? 175 LYS A NZ  1 
ATOM   1369 N  N   . ILE A 1 179 ? 95.824  90.918  55.931  1.00 31.09 ? 176 ILE A N   1 
ATOM   1370 C  CA  . ILE A 1 179 ? 97.082  90.276  56.251  1.00 29.87 ? 176 ILE A CA  1 
ATOM   1371 C  C   . ILE A 1 179 ? 97.965  90.101  55.018  1.00 29.64 ? 176 ILE A C   1 
ATOM   1372 O  O   . ILE A 1 179 ? 99.164  90.361  55.075  1.00 29.82 ? 176 ILE A O   1 
ATOM   1373 C  CB  . ILE A 1 179 ? 96.887  88.943  57.017  1.00 30.20 ? 176 ILE A CB  1 
ATOM   1374 C  CG1 . ILE A 1 179 ? 96.287  89.200  58.408  1.00 29.37 ? 176 ILE A CG1 1 
ATOM   1375 C  CG2 . ILE A 1 179 ? 98.215  88.166  57.164  1.00 28.18 ? 176 ILE A CG2 1 
ATOM   1376 C  CD1 . ILE A 1 179 ? 95.493  87.989  58.942  1.00 29.24 ? 176 ILE A CD1 1 
ATOM   1377 N  N   . ARG A 1 180 ? 97.377  89.707  53.900  1.00 28.86 ? 177 ARG A N   1 
ATOM   1378 C  CA  . ARG A 1 180 ? 98.168  89.376  52.732  1.00 28.67 ? 177 ARG A CA  1 
ATOM   1379 C  C   . ARG A 1 180 ? 98.907  90.572  52.179  1.00 29.19 ? 177 ARG A C   1 
ATOM   1380 O  O   . ARG A 1 180 ? 100.025 90.429  51.652  1.00 29.12 ? 177 ARG A O   1 
ATOM   1381 C  CB  . ARG A 1 180 ? 97.306  88.727  51.650  1.00 28.25 ? 177 ARG A CB  1 
ATOM   1382 C  CG  . ARG A 1 180 ? 96.964  87.312  51.964  1.00 26.56 ? 177 ARG A CG  1 
ATOM   1383 C  CD  . ARG A 1 180 ? 95.994  86.771  50.977  1.00 24.70 ? 177 ARG A CD  1 
ATOM   1384 N  NE  . ARG A 1 180 ? 95.833  85.341  51.190  1.00 24.45 ? 177 ARG A NE  1 
ATOM   1385 C  CZ  . ARG A 1 180 ? 94.937  84.574  50.581  1.00 23.00 ? 177 ARG A CZ  1 
ATOM   1386 N  NH1 . ARG A 1 180 ? 94.092  85.091  49.716  1.00 23.22 ? 177 ARG A NH1 1 
ATOM   1387 N  NH2 . ARG A 1 180 ? 94.888  83.284  50.854  1.00 24.00 ? 177 ARG A NH2 1 
ATOM   1388 N  N   . LYS A 1 181 ? 98.280  91.744  52.328  1.00 29.77 ? 178 LYS A N   1 
ATOM   1389 C  CA  . LYS A 1 181 ? 98.738  92.996  51.729  1.00 30.01 ? 178 LYS A CA  1 
ATOM   1390 C  C   . LYS A 1 181 ? 99.430  93.938  52.724  1.00 29.72 ? 178 LYS A C   1 
ATOM   1391 O  O   . LYS A 1 181 ? 99.908  95.018  52.338  1.00 29.23 ? 178 LYS A O   1 
ATOM   1392 C  CB  . LYS A 1 181 ? 97.566  93.697  51.026  1.00 30.51 ? 178 LYS A CB  1 
ATOM   1393 C  CG  . LYS A 1 181 ? 96.824  92.824  49.994  1.00 32.00 ? 178 LYS A CG  1 
ATOM   1394 C  CD  . LYS A 1 181 ? 97.626  92.578  48.684  1.00 33.95 ? 178 LYS A CD  1 
ATOM   1395 C  CE  . LYS A 1 181 ? 96.707  92.084  47.539  1.00 32.93 ? 178 LYS A CE  1 
ATOM   1396 N  NZ  . LYS A 1 181 ? 97.122  92.516  46.162  1.00 33.44 ? 178 LYS A NZ  1 
ATOM   1397 N  N   . ASP A 1 182 ? 99.498  93.507  53.986  1.00 29.42 ? 179 ASP A N   1 
ATOM   1398 C  CA  . ASP A 1 182 ? 100.158 94.261  55.059  1.00 29.71 ? 179 ASP A CA  1 
ATOM   1399 C  C   . ASP A 1 182 ? 101.693 94.356  54.931  1.00 29.50 ? 179 ASP A C   1 
ATOM   1400 O  O   . ASP A 1 182 ? 102.393 93.350  55.106  1.00 29.86 ? 179 ASP A O   1 
ATOM   1401 C  CB  . ASP A 1 182 ? 99.785  93.688  56.427  1.00 29.86 ? 179 ASP A CB  1 
ATOM   1402 C  CG  . ASP A 1 182 ? 100.335 94.514  57.586  1.00 30.25 ? 179 ASP A CG  1 
ATOM   1403 O  OD1 . ASP A 1 182 ? 100.216 94.071  58.737  1.00 34.00 ? 179 ASP A OD1 1 
ATOM   1404 O  OD2 . ASP A 1 182 ? 100.885 95.608  57.370  1.00 31.75 ? 179 ASP A OD2 1 
ATOM   1405 N  N   . PRO A 1 183 ? 102.217 95.572  54.645  1.00 28.89 ? 180 PRO A N   1 
ATOM   1406 C  CA  . PRO A 1 183 ? 103.669 95.760  54.478  1.00 28.59 ? 180 PRO A CA  1 
ATOM   1407 C  C   . PRO A 1 183 ? 104.522 95.585  55.763  1.00 28.14 ? 180 PRO A C   1 
ATOM   1408 O  O   . PRO A 1 183 ? 105.708 95.265  55.667  1.00 28.33 ? 180 PRO A O   1 
ATOM   1409 C  CB  . PRO A 1 183 ? 103.786 97.179  53.902  1.00 28.09 ? 180 PRO A CB  1 
ATOM   1410 C  CG  . PRO A 1 183 ? 102.541 97.875  54.328  1.00 28.69 ? 180 PRO A CG  1 
ATOM   1411 C  CD  . PRO A 1 183 ? 101.465 96.829  54.454  1.00 29.00 ? 180 PRO A CD  1 
ATOM   1412 N  N   . ALA A 1 184 ? 103.929 95.783  56.938  1.00 27.68 ? 181 ALA A N   1 
ATOM   1413 C  CA  . ALA A 1 184 ? 104.628 95.570  58.209  1.00 27.89 ? 181 ALA A CA  1 
ATOM   1414 C  C   . ALA A 1 184 ? 105.107 94.117  58.458  1.00 28.09 ? 181 ALA A C   1 
ATOM   1415 O  O   . ALA A 1 184 ? 105.976 93.889  59.309  1.00 28.70 ? 181 ALA A O   1 
ATOM   1416 C  CB  . ALA A 1 184 ? 103.766 96.040  59.376  1.00 27.44 ? 181 ALA A CB  1 
ATOM   1417 N  N   . ARG A 1 185 ? 104.547 93.144  57.737  1.00 27.81 ? 182 ARG A N   1 
ATOM   1418 C  CA  . ARG A 1 185 ? 104.908 91.732  57.911  1.00 27.76 ? 182 ARG A CA  1 
ATOM   1419 C  C   . ARG A 1 185 ? 106.346 91.428  57.470  1.00 28.32 ? 182 ARG A C   1 
ATOM   1420 O  O   . ARG A 1 185 ? 106.891 90.360  57.758  1.00 28.37 ? 182 ARG A O   1 
ATOM   1421 C  CB  . ARG A 1 185 ? 103.920 90.830  57.167  1.00 26.93 ? 182 ARG A CB  1 
ATOM   1422 C  CG  . ARG A 1 185 ? 102.542 90.760  57.782  1.00 25.73 ? 182 ARG A CG  1 
ATOM   1423 C  CD  . ARG A 1 185 ? 101.584 90.094  56.837  1.00 25.02 ? 182 ARG A CD  1 
ATOM   1424 N  NE  . ARG A 1 185 ? 102.111 88.789  56.422  1.00 26.11 ? 182 ARG A NE  1 
ATOM   1425 C  CZ  . ARG A 1 185 ? 101.970 88.225  55.221  1.00 25.40 ? 182 ARG A CZ  1 
ATOM   1426 N  NH1 . ARG A 1 185 ? 102.529 87.042  55.023  1.00 25.09 ? 182 ARG A NH1 1 
ATOM   1427 N  NH2 . ARG A 1 185 ? 101.304 88.824  54.223  1.00 21.01 ? 182 ARG A NH2 1 
ATOM   1428 N  N   . PHE A 1 186 ? 106.958 92.369  56.766  1.00 29.32 ? 183 PHE A N   1 
ATOM   1429 C  CA  . PHE A 1 186 ? 108.300 92.170  56.212  1.00 30.11 ? 183 PHE A CA  1 
ATOM   1430 C  C   . PHE A 1 186 ? 109.211 93.351  56.493  1.00 30.92 ? 183 PHE A C   1 
ATOM   1431 O  O   . PHE A 1 186 ? 109.110 94.403  55.859  1.00 30.97 ? 183 PHE A O   1 
ATOM   1432 C  CB  . PHE A 1 186 ? 108.213 91.814  54.720  1.00 29.32 ? 183 PHE A CB  1 
ATOM   1433 C  CG  . PHE A 1 186 ? 107.401 90.585  54.482  1.00 28.19 ? 183 PHE A CG  1 
ATOM   1434 C  CD1 . PHE A 1 186 ? 106.047 90.682  54.122  1.00 26.82 ? 183 PHE A CD1 1 
ATOM   1435 C  CD2 . PHE A 1 186 ? 107.960 89.326  54.706  1.00 23.74 ? 183 PHE A CD2 1 
ATOM   1436 C  CE1 . PHE A 1 186 ? 105.270 89.536  53.951  1.00 25.31 ? 183 PHE A CE1 1 
ATOM   1437 C  CE2 . PHE A 1 186 ? 107.199 88.189  54.543  1.00 25.54 ? 183 PHE A CE2 1 
ATOM   1438 C  CZ  . PHE A 1 186 ? 105.844 88.289  54.167  1.00 26.68 ? 183 PHE A CZ  1 
ATOM   1439 N  N   . VAL A 1 187 ? 110.083 93.145  57.478  1.00 32.01 ? 184 VAL A N   1 
ATOM   1440 C  CA  . VAL A 1 187 ? 111.043 94.136  57.917  1.00 33.00 ? 184 VAL A CA  1 
ATOM   1441 C  C   . VAL A 1 187 ? 112.157 94.362  56.889  1.00 33.52 ? 184 VAL A C   1 
ATOM   1442 O  O   . VAL A 1 187 ? 112.449 95.511  56.524  1.00 33.79 ? 184 VAL A O   1 
ATOM   1443 C  CB  . VAL A 1 187 ? 111.656 93.727  59.253  1.00 33.35 ? 184 VAL A CB  1 
ATOM   1444 C  CG1 . VAL A 1 187 ? 113.002 94.431  59.462  1.00 35.00 ? 184 VAL A CG1 1 
ATOM   1445 C  CG2 . VAL A 1 187 ? 110.690 94.052  60.391  1.00 32.54 ? 184 VAL A CG2 1 
ATOM   1446 N  N   . ASN B 1 2   ? 73.862  78.807  48.997  1.00 45.14 ? -1  ASN B N   1 
ATOM   1447 C  CA  . ASN B 1 2   ? 74.969  79.155  48.054  1.00 45.18 ? -1  ASN B CA  1 
ATOM   1448 C  C   . ASN B 1 2   ? 76.299  78.435  48.348  1.00 45.09 ? -1  ASN B C   1 
ATOM   1449 O  O   . ASN B 1 2   ? 77.341  79.092  48.460  1.00 45.18 ? -1  ASN B O   1 
ATOM   1450 C  CB  . ASN B 1 2   ? 75.164  80.690  47.981  1.00 45.38 ? -1  ASN B CB  1 
ATOM   1451 C  CG  . ASN B 1 2   ? 75.311  81.353  49.362  1.00 45.74 ? -1  ASN B CG  1 
ATOM   1452 O  OD1 . ASN B 1 2   ? 76.108  80.926  50.199  1.00 46.71 ? -1  ASN B OD1 1 
ATOM   1453 N  ND2 . ASN B 1 2   ? 74.553  82.416  49.586  1.00 46.14 ? -1  ASN B ND2 1 
ATOM   1454 N  N   . ALA B 1 3   ? 76.258  77.098  48.469  1.00 44.77 ? 0   ALA B N   1 
ATOM   1455 C  CA  . ALA B 1 3   ? 77.454  76.274  48.784  1.00 44.20 ? 0   ALA B CA  1 
ATOM   1456 C  C   . ALA B 1 3   ? 78.519  76.322  47.671  1.00 43.74 ? 0   ALA B C   1 
ATOM   1457 O  O   . ALA B 1 3   ? 78.196  76.140  46.487  1.00 43.96 ? 0   ALA B O   1 
ATOM   1458 C  CB  . ALA B 1 3   ? 77.062  74.827  49.117  1.00 44.12 ? 0   ALA B CB  1 
HETATM 1459 N  N   . MSE B 1 4   ? 79.774  76.572  48.062  1.00 42.63 ? 1   MSE B N   1 
HETATM 1460 C  CA  . MSE B 1 4   ? 80.810  77.049  47.133  1.00 42.09 ? 1   MSE B CA  1 
HETATM 1461 C  C   . MSE B 1 4   ? 82.221  76.710  47.589  1.00 40.29 ? 1   MSE B C   1 
HETATM 1462 O  O   . MSE B 1 4   ? 82.545  76.847  48.779  1.00 40.59 ? 1   MSE B O   1 
HETATM 1463 C  CB  . MSE B 1 4   ? 80.682  78.572  46.974  1.00 43.29 ? 1   MSE B CB  1 
HETATM 1464 C  CG  . MSE B 1 4   ? 81.767  79.247  46.137  1.00 48.63 ? 1   MSE B CG  1 
HETATM 1465 SE SE  . MSE B 1 4   ? 81.978  78.517  44.296  1.00 63.96 ? 1   MSE B SE  1 
HETATM 1466 C  CE  . MSE B 1 4   ? 80.155  78.856  43.583  1.00 57.59 ? 1   MSE B CE  1 
ATOM   1467 N  N   . GLY B 1 5   ? 83.076  76.291  46.657  1.00 38.16 ? 2   GLY B N   1 
ATOM   1468 C  CA  . GLY B 1 5   ? 84.475  75.988  46.992  1.00 35.39 ? 2   GLY B CA  1 
ATOM   1469 C  C   . GLY B 1 5   ? 85.377  75.774  45.801  1.00 33.57 ? 2   GLY B C   1 
ATOM   1470 O  O   . GLY B 1 5   ? 84.941  75.210  44.800  1.00 32.92 ? 2   GLY B O   1 
ATOM   1471 N  N   . LYS B 1 6   ? 86.639  76.203  45.931  1.00 32.00 ? 3   LYS B N   1 
ATOM   1472 C  CA  . LYS B 1 6   ? 87.631  76.191  44.831  1.00 30.24 ? 3   LYS B CA  1 
ATOM   1473 C  C   . LYS B 1 6   ? 88.882  75.375  45.175  1.00 29.97 ? 3   LYS B C   1 
ATOM   1474 O  O   . LYS B 1 6   ? 89.672  75.735  46.061  1.00 29.04 ? 3   LYS B O   1 
ATOM   1475 C  CB  . LYS B 1 6   ? 87.975  77.623  44.396  1.00 29.76 ? 3   LYS B CB  1 
ATOM   1476 C  CG  . LYS B 1 6   ? 86.829  78.283  43.627  1.00 29.50 ? 3   LYS B CG  1 
ATOM   1477 C  CD  . LYS B 1 6   ? 86.769  79.791  43.734  1.00 29.30 ? 3   LYS B CD  1 
ATOM   1478 C  CE  . LYS B 1 6   ? 85.763  80.359  42.709  1.00 28.78 ? 3   LYS B CE  1 
ATOM   1479 N  NZ  . LYS B 1 6   ? 85.355  81.784  42.932  1.00 26.68 ? 3   LYS B NZ  1 
ATOM   1480 N  N   . VAL B 1 7   ? 89.030  74.250  44.482  1.00 29.50 ? 4   VAL B N   1 
ATOM   1481 C  CA  . VAL B 1 7   ? 90.113  73.306  44.737  1.00 29.31 ? 4   VAL B CA  1 
ATOM   1482 C  C   . VAL B 1 7   ? 90.964  73.127  43.483  1.00 29.35 ? 4   VAL B C   1 
ATOM   1483 O  O   . VAL B 1 7   ? 90.417  73.008  42.372  1.00 30.37 ? 4   VAL B O   1 
ATOM   1484 C  CB  . VAL B 1 7   ? 89.561  71.939  45.210  1.00 29.24 ? 4   VAL B CB  1 
ATOM   1485 C  CG1 . VAL B 1 7   ? 90.645  70.911  45.307  1.00 28.14 ? 4   VAL B CG1 1 
ATOM   1486 C  CG2 . VAL B 1 7   ? 88.873  72.094  46.570  1.00 29.91 ? 4   VAL B CG2 1 
ATOM   1487 N  N   . LEU B 1 8   ? 92.290  73.187  43.660  1.00 28.33 ? 5   LEU B N   1 
ATOM   1488 C  CA  . LEU B 1 8   ? 93.272  72.884  42.613  1.00 27.79 ? 5   LEU B CA  1 
ATOM   1489 C  C   . LEU B 1 8   ? 93.923  71.558  42.954  1.00 27.32 ? 5   LEU B C   1 
ATOM   1490 O  O   . LEU B 1 8   ? 94.512  71.427  44.033  1.00 27.06 ? 5   LEU B O   1 
ATOM   1491 C  CB  . LEU B 1 8   ? 94.395  73.923  42.648  1.00 27.25 ? 5   LEU B CB  1 
ATOM   1492 C  CG  . LEU B 1 8   ? 95.257  74.348  41.452  1.00 28.22 ? 5   LEU B CG  1 
ATOM   1493 C  CD1 . LEU B 1 8   ? 96.726  74.547  41.871  1.00 26.08 ? 5   LEU B CD1 1 
ATOM   1494 C  CD2 . LEU B 1 8   ? 95.099  73.531  40.132  1.00 24.74 ? 5   LEU B CD2 1 
ATOM   1495 N  N   . VAL B 1 9   ? 93.839  70.581  42.061  1.00 26.57 ? 6   VAL B N   1 
ATOM   1496 C  CA  . VAL B 1 9   ? 94.706  69.428  42.183  1.00 25.85 ? 6   VAL B CA  1 
ATOM   1497 C  C   . VAL B 1 9   ? 95.808  69.612  41.171  1.00 26.13 ? 6   VAL B C   1 
ATOM   1498 O  O   . VAL B 1 9   ? 95.559  69.634  39.978  1.00 26.17 ? 6   VAL B O   1 
ATOM   1499 C  CB  . VAL B 1 9   ? 93.985  68.098  41.951  1.00 25.61 ? 6   VAL B CB  1 
ATOM   1500 C  CG1 . VAL B 1 9   ? 94.968  66.974  42.041  1.00 26.00 ? 6   VAL B CG1 1 
ATOM   1501 C  CG2 . VAL B 1 9   ? 92.906  67.907  42.985  1.00 24.32 ? 6   VAL B CG2 1 
ATOM   1502 N  N   . ILE B 1 10  ? 97.034  69.761  41.650  1.00 26.49 ? 7   ILE B N   1 
ATOM   1503 C  CA  . ILE B 1 10  ? 98.176  69.949  40.756  1.00 26.83 ? 7   ILE B CA  1 
ATOM   1504 C  C   . ILE B 1 10  ? 99.121  68.772  41.008  1.00 26.74 ? 7   ILE B C   1 
ATOM   1505 O  O   . ILE B 1 10  ? 99.279  68.333  42.138  1.00 27.95 ? 7   ILE B O   1 
ATOM   1506 C  CB  . ILE B 1 10  ? 98.841  71.381  40.952  1.00 26.82 ? 7   ILE B CB  1 
ATOM   1507 C  CG1 . ILE B 1 10  ? 99.913  71.652  39.908  1.00 27.02 ? 7   ILE B CG1 1 
ATOM   1508 C  CG2 . ILE B 1 10  ? 99.385  71.577  42.377  1.00 26.73 ? 7   ILE B CG2 1 
ATOM   1509 C  CD1 . ILE B 1 10  ? 100.904 72.735  40.314  1.00 27.29 ? 7   ILE B CD1 1 
ATOM   1510 N  N   . TYR B 1 11  ? 99.733  68.238  39.969  1.00 26.40 ? 8   TYR B N   1 
ATOM   1511 C  CA  . TYR B 1 11  ? 100.524 67.031  40.117  1.00 26.45 ? 8   TYR B CA  1 
ATOM   1512 C  C   . TYR B 1 11  ? 101.655 66.978  39.065  1.00 27.27 ? 8   TYR B C   1 
ATOM   1513 O  O   . TYR B 1 11  ? 101.626 67.657  38.027  1.00 26.56 ? 8   TYR B O   1 
ATOM   1514 C  CB  . TYR B 1 11  ? 99.619  65.783  39.980  1.00 26.05 ? 8   TYR B CB  1 
ATOM   1515 C  CG  . TYR B 1 11  ? 99.084  65.604  38.552  1.00 25.19 ? 8   TYR B CG  1 
ATOM   1516 C  CD1 . TYR B 1 11  ? 99.811  64.879  37.599  1.00 24.91 ? 8   TYR B CD1 1 
ATOM   1517 C  CD2 . TYR B 1 11  ? 97.891  66.196  38.153  1.00 22.34 ? 8   TYR B CD2 1 
ATOM   1518 C  CE1 . TYR B 1 11  ? 99.351  64.731  36.278  1.00 25.81 ? 8   TYR B CE1 1 
ATOM   1519 C  CE2 . TYR B 1 11  ? 97.407  66.039  36.838  1.00 24.60 ? 8   TYR B CE2 1 
ATOM   1520 C  CZ  . TYR B 1 11  ? 98.141  65.303  35.900  1.00 25.99 ? 8   TYR B CZ  1 
ATOM   1521 O  OH  . TYR B 1 11  ? 97.682  65.164  34.582  1.00 26.07 ? 8   TYR B OH  1 
ATOM   1522 N  N   . ASP B 1 12  ? 102.641 66.141  39.356  1.00 27.88 ? 9   ASP B N   1 
ATOM   1523 C  CA  . ASP B 1 12  ? 103.696 65.820  38.435  1.00 28.17 ? 9   ASP B CA  1 
ATOM   1524 C  C   . ASP B 1 12  ? 103.724 64.315  38.443  1.00 28.47 ? 9   ASP B C   1 
ATOM   1525 O  O   . ASP B 1 12  ? 103.090 63.693  39.271  1.00 28.70 ? 9   ASP B O   1 
ATOM   1526 C  CB  . ASP B 1 12  ? 105.033 66.385  38.941  1.00 28.31 ? 9   ASP B CB  1 
ATOM   1527 C  CG  . ASP B 1 12  ? 106.136 66.261  37.915  1.00 28.38 ? 9   ASP B CG  1 
ATOM   1528 O  OD1 . ASP B 1 12  ? 105.828 65.998  36.738  1.00 30.84 ? 9   ASP B OD1 1 
ATOM   1529 O  OD2 . ASP B 1 12  ? 107.313 66.395  38.272  1.00 30.64 ? 9   ASP B OD2 1 
ATOM   1530 N  N   . THR B 1 13  ? 104.471 63.719  37.529  1.00 29.32 ? 10  THR B N   1 
ATOM   1531 C  CA  . THR B 1 13  ? 104.415 62.286  37.329  1.00 30.17 ? 10  THR B CA  1 
ATOM   1532 C  C   . THR B 1 13  ? 105.597 61.896  36.482  1.00 30.99 ? 10  THR B C   1 
ATOM   1533 O  O   . THR B 1 13  ? 106.014 62.667  35.619  1.00 31.82 ? 10  THR B O   1 
ATOM   1534 C  CB  . THR B 1 13  ? 103.063 61.885  36.649  1.00 30.33 ? 10  THR B CB  1 
ATOM   1535 O  OG1 . THR B 1 13  ? 102.827 60.489  36.816  1.00 31.46 ? 10  THR B OG1 1 
ATOM   1536 C  CG2 . THR B 1 13  ? 103.025 62.238  35.189  1.00 28.84 ? 10  THR B CG2 1 
ATOM   1537 N  N   . ARG B 1 14  ? 106.146 60.718  36.758  1.00 31.71 ? 11  ARG B N   1 
ATOM   1538 C  CA  . ARG B 1 14  ? 107.215 60.104  35.972  1.00 33.02 ? 11  ARG B CA  1 
ATOM   1539 C  C   . ARG B 1 14  ? 106.680 59.078  34.977  1.00 31.39 ? 11  ARG B C   1 
ATOM   1540 O  O   . ARG B 1 14  ? 107.137 59.054  33.837  1.00 33.19 ? 11  ARG B O   1 
ATOM   1541 C  CB  . ARG B 1 14  ? 108.294 59.463  36.876  1.00 33.27 ? 11  ARG B CB  1 
ATOM   1542 C  CG  . ARG B 1 14  ? 109.337 58.584  36.083  1.00 36.34 ? 11  ARG B CG  1 
ATOM   1543 C  CD  . ARG B 1 14  ? 110.415 57.940  37.000  1.00 37.84 ? 11  ARG B CD  1 
ATOM   1544 N  NE  . ARG B 1 14  ? 109.851 56.982  37.974  1.00 47.52 ? 11  ARG B NE  1 
ATOM   1545 C  CZ  . ARG B 1 14  ? 109.844 55.644  37.841  1.00 50.00 ? 11  ARG B CZ  1 
ATOM   1546 N  NH1 . ARG B 1 14  ? 109.289 54.904  38.806  1.00 51.42 ? 11  ARG B NH1 1 
ATOM   1547 N  NH2 . ARG B 1 14  ? 110.376 55.036  36.767  1.00 49.11 ? 11  ARG B NH2 1 
ATOM   1548 N  N   . THR B 1 15  ? 105.743 58.230  35.393  1.00 29.62 ? 12  THR B N   1 
ATOM   1549 C  CA  . THR B 1 15  ? 105.198 57.163  34.536  1.00 28.14 ? 12  THR B CA  1 
ATOM   1550 C  C   . THR B 1 15  ? 103.668 57.178  34.469  1.00 27.30 ? 12  THR B C   1 
ATOM   1551 O  O   . THR B 1 15  ? 103.062 56.410  33.708  1.00 26.08 ? 12  THR B O   1 
ATOM   1552 C  CB  . THR B 1 15  ? 105.628 55.748  34.990  1.00 28.54 ? 12  THR B CB  1 
ATOM   1553 O  OG1 . THR B 1 15  ? 105.313 55.571  36.379  1.00 28.22 ? 12  THR B OG1 1 
ATOM   1554 C  CG2 . THR B 1 15  ? 107.100 55.506  34.764  1.00 28.29 ? 12  THR B CG2 1 
ATOM   1555 N  N   . GLY B 1 16  ? 103.053 58.030  35.286  1.00 25.98 ? 13  GLY B N   1 
ATOM   1556 C  CA  . GLY B 1 16  ? 101.637 58.290  35.188  1.00 25.67 ? 13  GLY B CA  1 
ATOM   1557 C  C   . GLY B 1 16  ? 100.832 57.857  36.396  1.00 25.71 ? 13  GLY B C   1 
ATOM   1558 O  O   . GLY B 1 16  ? 99.615  58.097  36.445  1.00 26.01 ? 13  GLY B O   1 
ATOM   1559 N  N   . ASN B 1 17  ? 101.492 57.200  37.353  1.00 25.13 ? 14  ASN B N   1 
ATOM   1560 C  CA  . ASN B 1 17  ? 100.836 56.685  38.563  1.00 24.91 ? 14  ASN B CA  1 
ATOM   1561 C  C   . ASN B 1 17  ? 100.225 57.779  39.438  1.00 25.29 ? 14  ASN B C   1 
ATOM   1562 O  O   . ASN B 1 17  ? 99.111  57.632  39.979  1.00 25.90 ? 14  ASN B O   1 
ATOM   1563 C  CB  . ASN B 1 17  ? 101.826 55.847  39.369  1.00 24.59 ? 14  ASN B CB  1 
ATOM   1564 C  CG  . ASN B 1 17  ? 102.185 54.545  38.669  1.00 25.10 ? 14  ASN B CG  1 
ATOM   1565 O  OD1 . ASN B 1 17  ? 101.355 53.940  38.006  1.00 25.10 ? 14  ASN B OD1 1 
ATOM   1566 N  ND2 . ASN B 1 17  ? 103.413 54.101  38.834  1.00 26.31 ? 14  ASN B ND2 1 
ATOM   1567 N  N   . THR B 1 18  ? 100.954 58.880  39.558  1.00 25.12 ? 15  THR B N   1 
ATOM   1568 C  CA  . THR B 1 18  ? 100.529 60.022  40.330  1.00 25.29 ? 15  THR B CA  1 
ATOM   1569 C  C   . THR B 1 18  ? 99.422  60.807  39.608  1.00 25.95 ? 15  THR B C   1 
ATOM   1570 O  O   . THR B 1 18  ? 98.581  61.422  40.273  1.00 25.82 ? 15  THR B O   1 
ATOM   1571 C  CB  . THR B 1 18  ? 101.740 60.903  40.703  1.00 25.58 ? 15  THR B CB  1 
ATOM   1572 O  OG1 . THR B 1 18  ? 102.738 60.071  41.310  1.00 24.99 ? 15  THR B OG1 1 
ATOM   1573 C  CG2 . THR B 1 18  ? 101.361 62.011  41.694  1.00 25.02 ? 15  THR B CG2 1 
ATOM   1574 N  N   . LYS B 1 19  ? 99.404  60.775  38.272  1.00 26.05 ? 16  LYS B N   1 
ATOM   1575 C  CA  . LYS B 1 19  ? 98.221  61.250  37.521  1.00 26.87 ? 16  LYS B CA  1 
ATOM   1576 C  C   . LYS B 1 19  ? 96.946  60.454  37.900  1.00 27.85 ? 16  LYS B C   1 
ATOM   1577 O  O   . LYS B 1 19  ? 95.885  61.032  38.144  1.00 28.14 ? 16  LYS B O   1 
ATOM   1578 C  CB  . LYS B 1 19  ? 98.467  61.231  36.009  1.00 26.55 ? 16  LYS B CB  1 
ATOM   1579 C  CG  . LYS B 1 19  ? 97.262  61.624  35.154  1.00 26.04 ? 16  LYS B CG  1 
ATOM   1580 C  CD  . LYS B 1 19  ? 97.562  61.553  33.666  1.00 24.84 ? 16  LYS B CD  1 
ATOM   1581 C  CE  . LYS B 1 19  ? 96.653  62.461  32.841  1.00 24.16 ? 16  LYS B CE  1 
ATOM   1582 N  NZ  . LYS B 1 19  ? 96.963  62.538  31.334  1.00 21.32 ? 16  LYS B NZ  1 
ATOM   1583 N  N   . LYS B 1 20  ? 97.064  59.136  37.978  1.00 28.96 ? 17  LYS B N   1 
ATOM   1584 C  CA  . LYS B 1 20  ? 95.943  58.306  38.393  1.00 30.77 ? 17  LYS B CA  1 
ATOM   1585 C  C   . LYS B 1 20  ? 95.436  58.686  39.772  1.00 31.41 ? 17  LYS B C   1 
ATOM   1586 O  O   . LYS B 1 20  ? 94.235  58.726  39.983  1.00 31.74 ? 17  LYS B O   1 
ATOM   1587 C  CB  . LYS B 1 20  ? 96.286  56.813  38.328  1.00 30.68 ? 17  LYS B CB  1 
ATOM   1588 C  CG  . LYS B 1 20  ? 95.823  56.160  37.027  1.00 35.61 ? 17  LYS B CG  1 
ATOM   1589 C  CD  . LYS B 1 20  ? 96.456  56.836  35.788  1.00 40.58 ? 17  LYS B CD  1 
ATOM   1590 C  CE  . LYS B 1 20  ? 95.444  56.989  34.642  1.00 43.00 ? 17  LYS B CE  1 
ATOM   1591 N  NZ  . LYS B 1 20  ? 95.796  58.136  33.721  1.00 43.23 ? 17  LYS B NZ  1 
HETATM 1592 N  N   . MSE B 1 21  ? 96.352  58.954  40.709  1.00 32.20 ? 18  MSE B N   1 
HETATM 1593 C  CA  . MSE B 1 21  ? 95.987  59.421  42.045  1.00 32.87 ? 18  MSE B CA  1 
HETATM 1594 C  C   . MSE B 1 21  ? 95.298  60.771  41.973  1.00 31.32 ? 18  MSE B C   1 
HETATM 1595 O  O   . MSE B 1 21  ? 94.263  60.973  42.598  1.00 31.45 ? 18  MSE B O   1 
HETATM 1596 C  CB  . MSE B 1 21  ? 97.206  59.544  42.931  1.00 31.83 ? 18  MSE B CB  1 
HETATM 1597 C  CG  . MSE B 1 21  ? 97.936  58.259  43.172  1.00 33.87 ? 18  MSE B CG  1 
HETATM 1598 SE SE  . MSE B 1 21  ? 99.501  58.527  44.426  1.00 39.10 ? 18  MSE B SE  1 
HETATM 1599 C  CE  . MSE B 1 21  ? 98.461  58.781  46.176  1.00 32.12 ? 18  MSE B CE  1 
ATOM   1600 N  N   . ALA B 1 22  ? 95.872  61.673  41.181  1.00 30.25 ? 19  ALA B N   1 
ATOM   1601 C  CA  . ALA B 1 22  ? 95.408  63.049  41.061  1.00 29.05 ? 19  ALA B CA  1 
ATOM   1602 C  C   . ALA B 1 22  ? 93.992  63.117  40.532  1.00 28.61 ? 19  ALA B C   1 
ATOM   1603 O  O   . ALA B 1 22  ? 93.225  63.981  40.946  1.00 28.29 ? 19  ALA B O   1 
ATOM   1604 C  CB  . ALA B 1 22  ? 96.346  63.853  40.174  1.00 28.59 ? 19  ALA B CB  1 
ATOM   1605 N  N   . GLU B 1 23  ? 93.657  62.202  39.622  1.00 28.14 ? 20  GLU B N   1 
ATOM   1606 C  CA  . GLU B 1 23  ? 92.272  62.052  39.123  1.00 27.70 ? 20  GLU B CA  1 
ATOM   1607 C  C   . GLU B 1 23  ? 91.343  61.594  40.232  1.00 27.48 ? 20  GLU B C   1 
ATOM   1608 O  O   . GLU B 1 23  ? 90.220  62.059  40.321  1.00 27.87 ? 20  GLU B O   1 
ATOM   1609 C  CB  . GLU B 1 23  ? 92.213  61.123  37.918  1.00 26.97 ? 20  GLU B CB  1 
ATOM   1610 C  CG  . GLU B 1 23  ? 92.784  61.792  36.675  1.00 28.27 ? 20  GLU B CG  1 
ATOM   1611 C  CD  . GLU B 1 23  ? 93.181  60.819  35.573  1.00 31.25 ? 20  GLU B CD  1 
ATOM   1612 O  OE1 . GLU B 1 23  ? 93.310  59.595  35.866  1.00 31.25 ? 20  GLU B OE1 1 
ATOM   1613 O  OE2 . GLU B 1 23  ? 93.353  61.294  34.406  1.00 31.31 ? 20  GLU B OE2 1 
ATOM   1614 N  N   . LEU B 1 24  ? 91.823  60.732  41.119  1.00 26.98 ? 21  LEU B N   1 
ATOM   1615 C  CA  . LEU B 1 24  ? 90.982  60.292  42.220  1.00 26.96 ? 21  LEU B CA  1 
ATOM   1616 C  C   . LEU B 1 24  ? 90.791  61.358  43.304  1.00 26.85 ? 21  LEU B C   1 
ATOM   1617 O  O   . LEU B 1 24  ? 89.696  61.493  43.869  1.00 27.40 ? 21  LEU B O   1 
ATOM   1618 C  CB  . LEU B 1 24  ? 91.457  58.952  42.784  1.00 26.68 ? 21  LEU B CB  1 
ATOM   1619 C  CG  . LEU B 1 24  ? 91.286  57.744  41.837  1.00 27.23 ? 21  LEU B CG  1 
ATOM   1620 C  CD1 . LEU B 1 24  ? 92.246  56.608  42.239  1.00 25.14 ? 21  LEU B CD1 1 
ATOM   1621 C  CD2 . LEU B 1 24  ? 89.802  57.250  41.695  1.00 23.29 ? 21  LEU B CD2 1 
ATOM   1622 N  N   . VAL B 1 25  ? 91.828  62.145  43.541  1.00 26.73 ? 22  VAL B N   1 
ATOM   1623 C  CA  . VAL B 1 25  ? 91.782  63.267  44.472  1.00 26.64 ? 22  VAL B CA  1 
ATOM   1624 C  C   . VAL B 1 25  ? 90.761  64.297  44.014  1.00 27.43 ? 22  VAL B C   1 
ATOM   1625 O  O   . VAL B 1 25  ? 89.861  64.691  44.796  1.00 28.65 ? 22  VAL B O   1 
ATOM   1626 C  CB  . VAL B 1 25  ? 93.182  63.942  44.658  1.00 26.65 ? 22  VAL B CB  1 
ATOM   1627 C  CG1 . VAL B 1 25  ? 93.068  65.143  45.613  1.00 24.68 ? 22  VAL B CG1 1 
ATOM   1628 C  CG2 . VAL B 1 25  ? 94.227  62.917  45.143  1.00 23.93 ? 22  VAL B CG2 1 
ATOM   1629 N  N   . ALA B 1 26  ? 90.888  64.716  42.752  1.00 27.31 ? 23  ALA B N   1 
ATOM   1630 C  CA  . ALA B 1 26  ? 89.933  65.610  42.105  1.00 27.43 ? 23  ALA B CA  1 
ATOM   1631 C  C   . ALA B 1 26  ? 88.512  65.082  42.217  1.00 27.41 ? 23  ALA B C   1 
ATOM   1632 O  O   . ALA B 1 26  ? 87.580  65.866  42.434  1.00 27.96 ? 23  ALA B O   1 
ATOM   1633 C  CB  . ALA B 1 26  ? 90.286  65.829  40.618  1.00 26.83 ? 23  ALA B CB  1 
ATOM   1634 N  N   . GLU B 1 27  ? 88.319  63.777  42.056  1.00 27.13 ? 24  GLU B N   1 
ATOM   1635 C  CA  . GLU B 1 27  ? 86.948  63.283  42.090  1.00 27.84 ? 24  GLU B CA  1 
ATOM   1636 C  C   . GLU B 1 27  ? 86.421  63.225  43.518  1.00 27.83 ? 24  GLU B C   1 
ATOM   1637 O  O   . GLU B 1 27  ? 85.241  63.423  43.745  1.00 28.61 ? 24  GLU B O   1 
ATOM   1638 C  CB  . GLU B 1 27  ? 86.761  61.969  41.346  1.00 27.62 ? 24  GLU B CB  1 
ATOM   1639 C  CG  . GLU B 1 27  ? 86.912  60.731  42.176  1.00 30.51 ? 24  GLU B CG  1 
ATOM   1640 C  CD  . GLU B 1 27  ? 86.088  59.579  41.629  1.00 33.18 ? 24  GLU B CD  1 
ATOM   1641 O  OE1 . GLU B 1 27  ? 84.950  59.418  42.110  1.00 34.11 ? 24  GLU B OE1 1 
ATOM   1642 O  OE2 . GLU B 1 27  ? 86.574  58.851  40.723  1.00 32.05 ? 24  GLU B OE2 1 
ATOM   1643 N  N   . GLY B 1 28  ? 87.297  62.965  44.472  1.00 27.69 ? 25  GLY B N   1 
ATOM   1644 C  CA  . GLY B 1 28  ? 86.954  63.126  45.868  1.00 27.43 ? 25  GLY B CA  1 
ATOM   1645 C  C   . GLY B 1 28  ? 86.527  64.544  46.190  1.00 27.71 ? 25  GLY B C   1 
ATOM   1646 O  O   . GLY B 1 28  ? 85.502  64.726  46.841  1.00 28.65 ? 25  GLY B O   1 
ATOM   1647 N  N   . ALA B 1 29  ? 87.297  65.553  45.764  1.00 27.52 ? 26  ALA B N   1 
ATOM   1648 C  CA  . ALA B 1 29  ? 86.884  66.960  45.958  1.00 26.97 ? 26  ALA B CA  1 
ATOM   1649 C  C   . ALA B 1 29  ? 85.554  67.304  45.258  1.00 27.49 ? 26  ALA B C   1 
ATOM   1650 O  O   . ALA B 1 29  ? 84.717  68.031  45.831  1.00 27.88 ? 26  ALA B O   1 
ATOM   1651 C  CB  . ALA B 1 29  ? 87.945  67.891  45.512  1.00 26.54 ? 26  ALA B CB  1 
ATOM   1652 N  N   . ARG B 1 30  ? 85.354  66.787  44.042  1.00 26.90 ? 27  ARG B N   1 
ATOM   1653 C  CA  . ARG B 1 30  ? 84.131  67.063  43.281  1.00 27.39 ? 27  ARG B CA  1 
ATOM   1654 C  C   . ARG B 1 30  ? 82.888  66.443  43.910  1.00 27.02 ? 27  ARG B C   1 
ATOM   1655 O  O   . ARG B 1 30  ? 81.773  66.879  43.646  1.00 26.67 ? 27  ARG B O   1 
ATOM   1656 C  CB  . ARG B 1 30  ? 84.257  66.597  41.834  1.00 27.43 ? 27  ARG B CB  1 
ATOM   1657 C  CG  . ARG B 1 30  ? 84.956  67.577  40.915  1.00 29.52 ? 27  ARG B CG  1 
ATOM   1658 C  CD  . ARG B 1 30  ? 84.745  67.190  39.436  1.00 33.97 ? 27  ARG B CD  1 
ATOM   1659 N  NE  . ARG B 1 30  ? 85.313  65.861  39.206  1.00 37.99 ? 27  ARG B NE  1 
ATOM   1660 C  CZ  . ARG B 1 30  ? 86.500  65.619  38.642  1.00 38.76 ? 27  ARG B CZ  1 
ATOM   1661 N  NH1 . ARG B 1 30  ? 86.919  64.348  38.542  1.00 37.80 ? 27  ARG B NH1 1 
ATOM   1662 N  NH2 . ARG B 1 30  ? 87.253  66.629  38.162  1.00 34.76 ? 27  ARG B NH2 1 
ATOM   1663 N  N   . SER B 1 31  ? 83.092  65.445  44.759  1.00 27.04 ? 28  SER B N   1 
ATOM   1664 C  CA  . SER B 1 31  ? 81.999  64.742  45.408  1.00 27.49 ? 28  SER B CA  1 
ATOM   1665 C  C   . SER B 1 31  ? 81.233  65.641  46.396  1.00 27.67 ? 28  SER B C   1 
ATOM   1666 O  O   . SER B 1 31  ? 80.059  65.399  46.662  1.00 27.48 ? 28  SER B O   1 
ATOM   1667 C  CB  . SER B 1 31  ? 82.497  63.437  46.078  1.00 26.91 ? 28  SER B CB  1 
ATOM   1668 O  OG  . SER B 1 31  ? 82.975  63.649  47.391  1.00 26.84 ? 28  SER B OG  1 
ATOM   1669 N  N   . LEU B 1 32  ? 81.902  66.663  46.938  1.00 28.81 ? 29  LEU B N   1 
ATOM   1670 C  CA  . LEU B 1 32  ? 81.260  67.635  47.820  1.00 29.46 ? 29  LEU B CA  1 
ATOM   1671 C  C   . LEU B 1 32  ? 80.599  68.689  46.950  1.00 30.27 ? 29  LEU B C   1 
ATOM   1672 O  O   . LEU B 1 32  ? 81.284  69.470  46.268  1.00 30.29 ? 29  LEU B O   1 
ATOM   1673 C  CB  . LEU B 1 32  ? 82.266  68.304  48.745  1.00 29.45 ? 29  LEU B CB  1 
ATOM   1674 C  CG  . LEU B 1 32  ? 81.935  68.631  50.216  1.00 30.22 ? 29  LEU B CG  1 
ATOM   1675 C  CD1 . LEU B 1 32  ? 82.518  69.994  50.619  1.00 28.42 ? 29  LEU B CD1 1 
ATOM   1676 C  CD2 . LEU B 1 32  ? 80.462  68.562  50.552  1.00 29.73 ? 29  LEU B CD2 1 
ATOM   1677 N  N   . GLU B 1 33  ? 79.266  68.689  46.985  1.00 30.82 ? 30  GLU B N   1 
ATOM   1678 C  CA  . GLU B 1 33  ? 78.416  69.568  46.193  1.00 31.42 ? 30  GLU B CA  1 
ATOM   1679 C  C   . GLU B 1 33  ? 78.816  71.026  46.310  1.00 31.35 ? 30  GLU B C   1 
ATOM   1680 O  O   . GLU B 1 33  ? 79.013  71.539  47.409  1.00 31.19 ? 30  GLU B O   1 
ATOM   1681 C  CB  . GLU B 1 33  ? 76.954  69.375  46.632  1.00 31.95 ? 30  GLU B CB  1 
ATOM   1682 C  CG  . GLU B 1 33  ? 75.908  70.283  45.970  1.00 33.51 ? 30  GLU B CG  1 
ATOM   1683 C  CD  . GLU B 1 33  ? 75.621  69.915  44.529  1.00 36.21 ? 30  GLU B CD  1 
ATOM   1684 O  OE1 . GLU B 1 33  ? 76.505  69.337  43.860  1.00 36.89 ? 30  GLU B OE1 1 
ATOM   1685 O  OE2 . GLU B 1 33  ? 74.498  70.209  44.057  1.00 37.96 ? 30  GLU B OE2 1 
ATOM   1686 N  N   . GLY B 1 34  ? 78.940  71.681  45.161  1.00 31.86 ? 31  GLY B N   1 
ATOM   1687 C  CA  . GLY B 1 34  ? 79.310  73.086  45.109  1.00 32.27 ? 31  GLY B CA  1 
ATOM   1688 C  C   . GLY B 1 34  ? 80.810  73.308  45.147  1.00 33.04 ? 31  GLY B C   1 
ATOM   1689 O  O   . GLY B 1 34  ? 81.254  74.424  45.397  1.00 34.08 ? 31  GLY B O   1 
ATOM   1690 N  N   . THR B 1 35  ? 81.592  72.255  44.911  1.00 32.59 ? 32  THR B N   1 
ATOM   1691 C  CA  . THR B 1 35  ? 83.045  72.360  44.910  1.00 32.54 ? 32  THR B CA  1 
ATOM   1692 C  C   . THR B 1 35  ? 83.575  72.308  43.482  1.00 32.90 ? 32  THR B C   1 
ATOM   1693 O  O   . THR B 1 35  ? 83.541  71.259  42.819  1.00 32.57 ? 32  THR B O   1 
ATOM   1694 C  CB  . THR B 1 35  ? 83.745  71.239  45.736  1.00 32.31 ? 32  THR B CB  1 
ATOM   1695 O  OG1 . THR B 1 35  ? 83.335  71.301  47.103  1.00 31.64 ? 32  THR B OG1 1 
ATOM   1696 C  CG2 . THR B 1 35  ? 85.256  71.392  45.671  1.00 32.49 ? 32  THR B CG2 1 
ATOM   1697 N  N   . GLU B 1 36  ? 84.085  73.448  43.026  1.00 32.95 ? 33  GLU B N   1 
ATOM   1698 C  CA  . GLU B 1 36  ? 84.767  73.509  41.758  1.00 33.22 ? 33  GLU B CA  1 
ATOM   1699 C  C   . GLU B 1 36  ? 86.214  73.021  41.874  1.00 32.77 ? 33  GLU B C   1 
ATOM   1700 O  O   . GLU B 1 36  ? 86.979  73.453  42.754  1.00 32.76 ? 33  GLU B O   1 
ATOM   1701 C  CB  . GLU B 1 36  ? 84.718  74.908  41.178  1.00 33.50 ? 33  GLU B CB  1 
ATOM   1702 C  CG  . GLU B 1 36  ? 85.299  74.902  39.809  1.00 36.68 ? 33  GLU B CG  1 
ATOM   1703 C  CD  . GLU B 1 36  ? 84.939  76.098  39.010  1.00 41.47 ? 33  GLU B CD  1 
ATOM   1704 O  OE1 . GLU B 1 36  ? 85.326  76.114  37.812  1.00 43.23 ? 33  GLU B OE1 1 
ATOM   1705 O  OE2 . GLU B 1 36  ? 84.278  77.009  39.577  1.00 43.82 ? 33  GLU B OE2 1 
ATOM   1706 N  N   . VAL B 1 37  ? 86.578  72.110  40.978  1.00 32.28 ? 34  VAL B N   1 
ATOM   1707 C  CA  . VAL B 1 37  ? 87.899  71.490  40.992  1.00 31.61 ? 34  VAL B CA  1 
ATOM   1708 C  C   . VAL B 1 37  ? 88.592  71.760  39.671  1.00 31.16 ? 34  VAL B C   1 
ATOM   1709 O  O   . VAL B 1 37  ? 87.982  71.681  38.607  1.00 30.75 ? 34  VAL B O   1 
ATOM   1710 C  CB  . VAL B 1 37  ? 87.804  69.978  41.229  1.00 31.73 ? 34  VAL B CB  1 
ATOM   1711 C  CG1 . VAL B 1 37  ? 89.190  69.337  41.283  1.00 30.96 ? 34  VAL B CG1 1 
ATOM   1712 C  CG2 . VAL B 1 37  ? 87.033  69.703  42.516  1.00 32.20 ? 34  VAL B CG2 1 
ATOM   1713 N  N   . ARG B 1 38  ? 89.868  72.098  39.766  1.00 30.26 ? 35  ARG B N   1 
ATOM   1714 C  CA  . ARG B 1 38  ? 90.714  72.318  38.622  1.00 29.83 ? 35  ARG B CA  1 
ATOM   1715 C  C   . ARG B 1 38  ? 91.789  71.232  38.757  1.00 29.71 ? 35  ARG B C   1 
ATOM   1716 O  O   . ARG B 1 38  ? 92.401  71.068  39.824  1.00 29.87 ? 35  ARG B O   1 
ATOM   1717 C  CB  . ARG B 1 38  ? 91.315  73.711  38.749  1.00 29.65 ? 35  ARG B CB  1 
ATOM   1718 C  CG  . ARG B 1 38  ? 91.350  74.568  37.533  1.00 30.44 ? 35  ARG B CG  1 
ATOM   1719 C  CD  . ARG B 1 38  ? 90.477  75.796  37.705  1.00 31.06 ? 35  ARG B CD  1 
ATOM   1720 N  NE  . ARG B 1 38  ? 91.202  77.052  37.475  1.00 30.68 ? 35  ARG B NE  1 
ATOM   1721 C  CZ  . ARG B 1 38  ? 90.618  78.242  37.306  1.00 31.52 ? 35  ARG B CZ  1 
ATOM   1722 N  NH1 . ARG B 1 38  ? 89.291  78.361  37.301  1.00 31.12 ? 35  ARG B NH1 1 
ATOM   1723 N  NH2 . ARG B 1 38  ? 91.360  79.326  37.131  1.00 30.19 ? 35  ARG B NH2 1 
ATOM   1724 N  N   . LEU B 1 39  ? 91.987  70.453  37.704  1.00 29.68 ? 36  LEU B N   1 
ATOM   1725 C  CA  . LEU B 1 39  ? 92.997  69.394  37.706  1.00 29.53 ? 36  LEU B CA  1 
ATOM   1726 C  C   . LEU B 1 39  ? 94.064  69.713  36.664  1.00 30.20 ? 36  LEU B C   1 
ATOM   1727 O  O   . LEU B 1 39  ? 93.757  69.803  35.472  1.00 29.48 ? 36  LEU B O   1 
ATOM   1728 C  CB  . LEU B 1 39  ? 92.354  68.049  37.383  1.00 29.16 ? 36  LEU B CB  1 
ATOM   1729 C  CG  . LEU B 1 39  ? 93.296  66.860  37.216  1.00 28.83 ? 36  LEU B CG  1 
ATOM   1730 C  CD1 . LEU B 1 39  ? 93.998  66.544  38.521  1.00 27.65 ? 36  LEU B CD1 1 
ATOM   1731 C  CD2 . LEU B 1 39  ? 92.501  65.666  36.751  1.00 28.10 ? 36  LEU B CD2 1 
ATOM   1732 N  N   . LYS B 1 40  ? 95.314  69.892  37.106  1.00 30.76 ? 37  LYS B N   1 
ATOM   1733 C  CA  . LYS B 1 40  ? 96.396  70.281  36.181  1.00 31.22 ? 37  LYS B CA  1 
ATOM   1734 C  C   . LYS B 1 40  ? 97.706  69.530  36.386  1.00 30.94 ? 37  LYS B C   1 
ATOM   1735 O  O   . LYS B 1 40  ? 98.138  69.326  37.499  1.00 30.58 ? 37  LYS B O   1 
ATOM   1736 C  CB  . LYS B 1 40  ? 96.678  71.780  36.295  1.00 31.94 ? 37  LYS B CB  1 
ATOM   1737 C  CG  . LYS B 1 40  ? 95.443  72.684  36.205  1.00 31.81 ? 37  LYS B CG  1 
ATOM   1738 C  CD  . LYS B 1 40  ? 95.265  73.307  34.862  1.00 32.57 ? 37  LYS B CD  1 
ATOM   1739 C  CE  . LYS B 1 40  ? 93.981  74.143  34.869  1.00 35.10 ? 37  LYS B CE  1 
ATOM   1740 N  NZ  . LYS B 1 40  ? 93.745  74.935  33.608  1.00 33.33 ? 37  LYS B NZ  1 
ATOM   1741 N  N   . HIS B 1 41  ? 98.339  69.131  35.292  1.00 30.94 ? 38  HIS B N   1 
ATOM   1742 C  CA  . HIS B 1 41  ? 99.738  68.748  35.332  1.00 30.95 ? 38  HIS B CA  1 
ATOM   1743 C  C   . HIS B 1 41  ? 100.563 70.012  35.650  1.00 31.32 ? 38  HIS B C   1 
ATOM   1744 O  O   . HIS B 1 41  ? 100.117 71.110  35.327  1.00 31.34 ? 38  HIS B O   1 
ATOM   1745 C  CB  . HIS B 1 41  ? 100.158 68.171  33.983  1.00 30.26 ? 38  HIS B CB  1 
ATOM   1746 C  CG  . HIS B 1 41  ? 101.484 67.493  34.020  1.00 30.41 ? 38  HIS B CG  1 
ATOM   1747 N  ND1 . HIS B 1 41  ? 102.640 68.105  33.605  1.00 32.04 ? 38  HIS B ND1 1 
ATOM   1748 C  CD2 . HIS B 1 41  ? 101.851 66.277  34.485  1.00 32.39 ? 38  HIS B CD2 1 
ATOM   1749 C  CE1 . HIS B 1 41  ? 103.663 67.288  33.783  1.00 33.08 ? 38  HIS B CE1 1 
ATOM   1750 N  NE2 . HIS B 1 41  ? 103.209 66.165  34.303  1.00 33.42 ? 38  HIS B NE2 1 
ATOM   1751 N  N   . VAL B 1 42  ? 101.735 69.878  36.280  1.00 31.56 ? 39  VAL B N   1 
ATOM   1752 C  CA  . VAL B 1 42  ? 102.599 71.048  36.516  1.00 32.33 ? 39  VAL B CA  1 
ATOM   1753 C  C   . VAL B 1 42  ? 102.925 71.804  35.248  1.00 32.63 ? 39  VAL B C   1 
ATOM   1754 O  O   . VAL B 1 42  ? 103.043 73.026  35.273  1.00 32.86 ? 39  VAL B O   1 
ATOM   1755 C  CB  . VAL B 1 42  ? 103.984 70.730  37.126  1.00 31.95 ? 39  VAL B CB  1 
ATOM   1756 C  CG1 . VAL B 1 42  ? 104.124 71.366  38.463  1.00 32.76 ? 39  VAL B CG1 1 
ATOM   1757 C  CG2 . VAL B 1 42  ? 104.253 69.271  37.145  1.00 32.75 ? 39  VAL B CG2 1 
ATOM   1758 N  N   . ASP B 1 43  ? 103.108 71.083  34.145  1.00 33.16 ? 40  ASP B N   1 
ATOM   1759 C  CA  . ASP B 1 43  ? 103.444 71.745  32.877  1.00 34.09 ? 40  ASP B CA  1 
ATOM   1760 C  C   . ASP B 1 43  ? 102.381 72.704  32.376  1.00 33.61 ? 40  ASP B C   1 
ATOM   1761 O  O   . ASP B 1 43  ? 102.709 73.641  31.686  1.00 34.38 ? 40  ASP B O   1 
ATOM   1762 C  CB  . ASP B 1 43  ? 103.860 70.748  31.792  1.00 34.39 ? 40  ASP B CB  1 
ATOM   1763 C  CG  . ASP B 1 43  ? 105.259 70.187  32.029  1.00 36.68 ? 40  ASP B CG  1 
ATOM   1764 O  OD1 . ASP B 1 43  ? 105.750 69.426  31.171  1.00 38.96 ? 40  ASP B OD1 1 
ATOM   1765 O  OD2 . ASP B 1 43  ? 105.866 70.494  33.085  1.00 39.15 ? 40  ASP B OD2 1 
ATOM   1766 N  N   . GLU B 1 44  ? 101.125 72.497  32.749  1.00 33.50 ? 41  GLU B N   1 
ATOM   1767 C  CA  . GLU B 1 44  ? 100.047 73.363  32.282  1.00 33.84 ? 41  GLU B CA  1 
ATOM   1768 C  C   . GLU B 1 44  ? 99.493  74.274  33.387  1.00 33.25 ? 41  GLU B C   1 
ATOM   1769 O  O   . GLU B 1 44  ? 98.670  75.148  33.131  1.00 34.18 ? 41  GLU B O   1 
ATOM   1770 C  CB  . GLU B 1 44  ? 98.936  72.519  31.634  1.00 33.58 ? 41  GLU B CB  1 
ATOM   1771 C  CG  . GLU B 1 44  ? 98.171  71.676  32.637  1.00 35.41 ? 41  GLU B CG  1 
ATOM   1772 C  CD  . GLU B 1 44  ? 97.325  70.562  32.024  1.00 36.02 ? 41  GLU B CD  1 
ATOM   1773 O  OE1 . GLU B 1 44  ? 97.231  69.451  32.633  1.00 38.44 ? 41  GLU B OE1 1 
ATOM   1774 O  OE2 . GLU B 1 44  ? 96.730  70.798  30.954  1.00 40.86 ? 41  GLU B OE2 1 
ATOM   1775 N  N   . ALA B 1 45  ? 99.950  74.079  34.616  1.00 32.70 ? 42  ALA B N   1 
ATOM   1776 C  CA  . ALA B 1 45  ? 99.468  74.856  35.768  1.00 31.89 ? 42  ALA B CA  1 
ATOM   1777 C  C   . ALA B 1 45  ? 99.996  76.277  35.691  1.00 31.52 ? 42  ALA B C   1 
ATOM   1778 O  O   . ALA B 1 45  ? 101.103 76.502  35.194  1.00 31.24 ? 42  ALA B O   1 
ATOM   1779 C  CB  . ALA B 1 45  ? 99.893  74.195  37.092  1.00 31.06 ? 42  ALA B CB  1 
ATOM   1780 N  N   . THR B 1 46  ? 99.196  77.225  36.174  1.00 31.30 ? 43  THR B N   1 
ATOM   1781 C  CA  . THR B 1 46  ? 99.593  78.623  36.218  1.00 31.10 ? 43  THR B CA  1 
ATOM   1782 C  C   . THR B 1 46  ? 99.532  79.188  37.629  1.00 31.62 ? 43  THR B C   1 
ATOM   1783 O  O   . THR B 1 46  ? 98.818  78.681  38.489  1.00 32.32 ? 43  THR B O   1 
ATOM   1784 C  CB  . THR B 1 46  ? 98.703  79.529  35.325  1.00 31.15 ? 43  THR B CB  1 
ATOM   1785 O  OG1 . THR B 1 46  ? 97.391  79.594  35.884  1.00 30.44 ? 43  THR B OG1 1 
ATOM   1786 C  CG2 . THR B 1 46  ? 98.646  79.039  33.870  1.00 29.02 ? 43  THR B CG2 1 
ATOM   1787 N  N   . LYS B 1 47  ? 100.323 80.231  37.845  1.00 32.18 ? 44  LYS B N   1 
ATOM   1788 C  CA  . LYS B 1 47  ? 100.200 81.181  38.947  1.00 32.51 ? 44  LYS B CA  1 
ATOM   1789 C  C   . LYS B 1 47  ? 98.735  81.443  39.312  1.00 32.53 ? 44  LYS B C   1 
ATOM   1790 O  O   . LYS B 1 47  ? 98.353  81.358  40.485  1.00 32.19 ? 44  LYS B O   1 
ATOM   1791 C  CB  . LYS B 1 47  ? 100.805 82.482  38.443  1.00 32.39 ? 44  LYS B CB  1 
ATOM   1792 C  CG  . LYS B 1 47  ? 101.276 83.479  39.450  1.00 33.43 ? 44  LYS B CG  1 
ATOM   1793 C  CD  . LYS B 1 47  ? 101.870 84.702  38.704  1.00 33.42 ? 44  LYS B CD  1 
ATOM   1794 C  CE  . LYS B 1 47  ? 100.811 85.719  38.315  1.00 34.99 ? 44  LYS B CE  1 
ATOM   1795 N  NZ  . LYS B 1 47  ? 101.150 86.476  37.081  1.00 34.88 ? 44  LYS B NZ  1 
ATOM   1796 N  N   . GLU B 1 48  ? 97.934  81.773  38.292  1.00 32.44 ? 45  GLU B N   1 
ATOM   1797 C  CA  . GLU B 1 48  ? 96.516  82.143  38.448  1.00 32.47 ? 45  GLU B CA  1 
ATOM   1798 C  C   . GLU B 1 48  ? 95.633  81.033  38.992  1.00 31.35 ? 45  GLU B C   1 
ATOM   1799 O  O   . GLU B 1 48  ? 94.640  81.310  39.666  1.00 31.67 ? 45  GLU B O   1 
ATOM   1800 C  CB  . GLU B 1 48  ? 95.925  82.637  37.123  1.00 32.74 ? 45  GLU B CB  1 
ATOM   1801 C  CG  . GLU B 1 48  ? 96.401  84.026  36.680  1.00 35.45 ? 45  GLU B CG  1 
ATOM   1802 C  CD  . GLU B 1 48  ? 97.831  84.038  36.131  1.00 38.00 ? 45  GLU B CD  1 
ATOM   1803 O  OE1 . GLU B 1 48  ? 98.344  82.970  35.733  1.00 39.85 ? 45  GLU B OE1 1 
ATOM   1804 O  OE2 . GLU B 1 48  ? 98.451  85.122  36.107  1.00 38.94 ? 45  GLU B OE2 1 
ATOM   1805 N  N   . ASP B 1 49  ? 95.971  79.782  38.690  1.00 30.16 ? 46  ASP B N   1 
ATOM   1806 C  CA  . ASP B 1 49  ? 95.211  78.651  39.230  1.00 29.14 ? 46  ASP B CA  1 
ATOM   1807 C  C   . ASP B 1 49  ? 95.350  78.603  40.734  1.00 28.51 ? 46  ASP B C   1 
ATOM   1808 O  O   . ASP B 1 49  ? 94.395  78.245  41.431  1.00 29.54 ? 46  ASP B O   1 
ATOM   1809 C  CB  . ASP B 1 49  ? 95.691  77.315  38.678  1.00 29.12 ? 46  ASP B CB  1 
ATOM   1810 C  CG  . ASP B 1 49  ? 95.339  77.116  37.229  1.00 29.61 ? 46  ASP B CG  1 
ATOM   1811 O  OD1 . ASP B 1 49  ? 94.200  77.474  36.809  1.00 31.57 ? 46  ASP B OD1 1 
ATOM   1812 O  OD2 . ASP B 1 49  ? 96.222  76.590  36.517  1.00 28.19 ? 46  ASP B OD2 1 
ATOM   1813 N  N   . VAL B 1 50  ? 96.541  78.941  41.222  1.00 26.70 ? 47  VAL B N   1 
ATOM   1814 C  CA  . VAL B 1 50  ? 96.829  78.935  42.639  1.00 25.58 ? 47  VAL B CA  1 
ATOM   1815 C  C   . VAL B 1 50  ? 96.094  80.094  43.321  1.00 25.77 ? 47  VAL B C   1 
ATOM   1816 O  O   . VAL B 1 50  ? 95.546  79.923  44.407  1.00 26.82 ? 47  VAL B O   1 
ATOM   1817 C  CB  . VAL B 1 50  ? 98.373  78.953  42.906  1.00 25.19 ? 47  VAL B CB  1 
ATOM   1818 C  CG1 . VAL B 1 50  ? 98.688  78.983  44.385  1.00 24.56 ? 47  VAL B CG1 1 
ATOM   1819 C  CG2 . VAL B 1 50  ? 98.998  77.760  42.313  1.00 22.21 ? 47  VAL B CG2 1 
ATOM   1820 N  N   . LEU B 1 51  ? 96.052  81.255  42.681  1.00 25.48 ? 48  LEU B N   1 
ATOM   1821 C  CA  . LEU B 1 51  ? 95.312  82.398  43.206  1.00 25.66 ? 48  LEU B CA  1 
ATOM   1822 C  C   . LEU B 1 51  ? 93.812  82.129  43.279  1.00 26.19 ? 48  LEU B C   1 
ATOM   1823 O  O   . LEU B 1 51  ? 93.133  82.576  44.208  1.00 26.60 ? 48  LEU B O   1 
ATOM   1824 C  CB  . LEU B 1 51  ? 95.550  83.632  42.341  1.00 25.37 ? 48  LEU B CB  1 
ATOM   1825 C  CG  . LEU B 1 51  ? 96.899  84.335  42.433  1.00 25.01 ? 48  LEU B CG  1 
ATOM   1826 C  CD1 . LEU B 1 51  ? 97.070  85.256  41.224  1.00 22.51 ? 48  LEU B CD1 1 
ATOM   1827 C  CD2 . LEU B 1 51  ? 97.032  85.102  43.738  1.00 22.16 ? 48  LEU B CD2 1 
ATOM   1828 N  N   . TRP B 1 52  ? 93.307  81.411  42.282  1.00 26.21 ? 49  TRP B N   1 
ATOM   1829 C  CA  . TRP B 1 52  ? 91.913  81.030  42.208  1.00 26.65 ? 49  TRP B CA  1 
ATOM   1830 C  C   . TRP B 1 52  ? 91.505  80.035  43.311  1.00 27.18 ? 49  TRP B C   1 
ATOM   1831 O  O   . TRP B 1 52  ? 90.392  80.127  43.852  1.00 27.06 ? 49  TRP B O   1 
ATOM   1832 C  CB  . TRP B 1 52  ? 91.638  80.463  40.813  1.00 26.37 ? 49  TRP B CB  1 
ATOM   1833 C  CG  . TRP B 1 52  ? 90.335  79.791  40.646  1.00 26.16 ? 49  TRP B CG  1 
ATOM   1834 C  CD1 . TRP B 1 52  ? 89.162  80.359  40.225  1.00 25.97 ? 49  TRP B CD1 1 
ATOM   1835 C  CD2 . TRP B 1 52  ? 90.053  78.403  40.869  1.00 26.65 ? 49  TRP B CD2 1 
ATOM   1836 N  NE1 . TRP B 1 52  ? 88.164  79.412  40.184  1.00 25.01 ? 49  TRP B NE1 1 
ATOM   1837 C  CE2 . TRP B 1 52  ? 88.683  78.201  40.560  1.00 26.69 ? 49  TRP B CE2 1 
ATOM   1838 C  CE3 . TRP B 1 52  ? 90.824  77.307  41.299  1.00 27.65 ? 49  TRP B CE3 1 
ATOM   1839 C  CZ2 . TRP B 1 52  ? 88.063  76.948  40.673  1.00 26.96 ? 49  TRP B CZ2 1 
ATOM   1840 C  CZ3 . TRP B 1 52  ? 90.206  76.057  41.420  1.00 26.87 ? 49  TRP B CZ3 1 
ATOM   1841 C  CH2 . TRP B 1 52  ? 88.840  75.890  41.089  1.00 26.74 ? 49  TRP B CH2 1 
ATOM   1842 N  N   . ALA B 1 53  ? 92.400  79.105  43.647  1.00 27.52 ? 50  ALA B N   1 
ATOM   1843 C  CA  . ALA B 1 53  ? 92.088  78.026  44.605  1.00 28.56 ? 50  ALA B CA  1 
ATOM   1844 C  C   . ALA B 1 53  ? 92.025  78.473  46.069  1.00 29.57 ? 50  ALA B C   1 
ATOM   1845 O  O   . ALA B 1 53  ? 92.917  79.204  46.550  1.00 29.95 ? 50  ALA B O   1 
ATOM   1846 C  CB  . ALA B 1 53  ? 93.097  76.892  44.476  1.00 28.07 ? 50  ALA B CB  1 
ATOM   1847 N  N   . ASP B 1 54  ? 90.985  78.017  46.770  1.00 29.96 ? 51  ASP B N   1 
ATOM   1848 C  CA  . ASP B 1 54  ? 90.930  78.099  48.235  1.00 30.31 ? 51  ASP B CA  1 
ATOM   1849 C  C   . ASP B 1 54  ? 91.811  77.034  48.866  1.00 30.34 ? 51  ASP B C   1 
ATOM   1850 O  O   . ASP B 1 54  ? 92.417  77.276  49.916  1.00 31.28 ? 51  ASP B O   1 
ATOM   1851 C  CB  . ASP B 1 54  ? 89.500  77.918  48.752  1.00 30.13 ? 51  ASP B CB  1 
ATOM   1852 C  CG  . ASP B 1 54  ? 88.551  78.945  48.198  1.00 32.24 ? 51  ASP B CG  1 
ATOM   1853 O  OD1 . ASP B 1 54  ? 88.848  80.166  48.320  1.00 34.80 ? 51  ASP B OD1 1 
ATOM   1854 O  OD2 . ASP B 1 54  ? 87.509  78.533  47.633  1.00 32.41 ? 51  ASP B OD2 1 
ATOM   1855 N  N   . GLY B 1 55  ? 91.857  75.861  48.225  1.00 29.63 ? 52  GLY B N   1 
ATOM   1856 C  CA  . GLY B 1 55  ? 92.542  74.690  48.721  1.00 28.33 ? 52  GLY B CA  1 
ATOM   1857 C  C   . GLY B 1 55  ? 93.317  74.016  47.610  1.00 28.47 ? 52  GLY B C   1 
ATOM   1858 O  O   . GLY B 1 55  ? 92.869  74.015  46.462  1.00 28.39 ? 52  GLY B O   1 
ATOM   1859 N  N   . LEU B 1 56  ? 94.489  73.471  47.947  1.00 28.22 ? 53  LEU B N   1 
ATOM   1860 C  CA  . LEU B 1 56  ? 95.347  72.767  46.995  1.00 29.00 ? 53  LEU B CA  1 
ATOM   1861 C  C   . LEU B 1 56  ? 95.632  71.355  47.410  1.00 27.98 ? 53  LEU B C   1 
ATOM   1862 O  O   . LEU B 1 56  ? 95.897  71.112  48.557  1.00 29.00 ? 53  LEU B O   1 
ATOM   1863 C  CB  . LEU B 1 56  ? 96.701  73.462  46.888  1.00 29.25 ? 53  LEU B CB  1 
ATOM   1864 C  CG  . LEU B 1 56  ? 96.699  74.776  46.121  1.00 33.01 ? 53  LEU B CG  1 
ATOM   1865 C  CD1 . LEU B 1 56  ? 96.217  75.886  47.079  1.00 33.75 ? 53  LEU B CD1 1 
ATOM   1866 C  CD2 . LEU B 1 56  ? 98.107  75.070  45.587  1.00 33.55 ? 53  LEU B CD2 1 
ATOM   1867 N  N   . ALA B 1 57  ? 95.612  70.429  46.468  1.00 27.97 ? 54  ALA B N   1 
ATOM   1868 C  CA  . ALA B 1 57  ? 96.229  69.110  46.650  1.00 27.65 ? 54  ALA B CA  1 
ATOM   1869 C  C   . ALA B 1 57  ? 97.395  69.012  45.696  1.00 27.47 ? 54  ALA B C   1 
ATOM   1870 O  O   . ALA B 1 57  ? 97.251  69.240  44.511  1.00 28.60 ? 54  ALA B O   1 
ATOM   1871 C  CB  . ALA B 1 57  ? 95.246  68.001  46.383  1.00 26.70 ? 54  ALA B CB  1 
ATOM   1872 N  N   . VAL B 1 58  ? 98.556  68.658  46.211  1.00 27.33 ? 55  VAL B N   1 
ATOM   1873 C  CA  . VAL B 1 58  ? 99.773  68.687  45.418  1.00 26.21 ? 55  VAL B CA  1 
ATOM   1874 C  C   . VAL B 1 58  ? 100.399 67.301  45.369  1.00 25.87 ? 55  VAL B C   1 
ATOM   1875 O  O   . VAL B 1 58  ? 100.772 66.752  46.400  1.00 25.14 ? 55  VAL B O   1 
ATOM   1876 C  CB  . VAL B 1 58  ? 100.779 69.730  45.988  1.00 26.14 ? 55  VAL B CB  1 
ATOM   1877 C  CG1 . VAL B 1 58  ? 102.095 69.749  45.169  1.00 25.39 ? 55  VAL B CG1 1 
ATOM   1878 C  CG2 . VAL B 1 58  ? 100.122 71.120  46.044  1.00 24.78 ? 55  VAL B CG2 1 
ATOM   1879 N  N   . GLY B 1 59  ? 100.539 66.763  44.154  1.00 25.52 ? 56  GLY B N   1 
ATOM   1880 C  CA  . GLY B 1 59  ? 101.049 65.415  43.979  1.00 24.90 ? 56  GLY B CA  1 
ATOM   1881 C  C   . GLY B 1 59  ? 102.388 65.352  43.303  1.00 24.75 ? 56  GLY B C   1 
ATOM   1882 O  O   . GLY B 1 59  ? 102.700 66.159  42.436  1.00 25.60 ? 56  GLY B O   1 
ATOM   1883 N  N   . SER B 1 60  ? 103.197 64.383  43.687  1.00 24.39 ? 57  SER B N   1 
ATOM   1884 C  CA  . SER B 1 60  ? 104.433 64.151  42.968  1.00 23.67 ? 57  SER B CA  1 
ATOM   1885 C  C   . SER B 1 60  ? 104.769 62.699  43.119  1.00 23.31 ? 57  SER B C   1 
ATOM   1886 O  O   . SER B 1 60  ? 104.370 62.099  44.098  1.00 23.68 ? 57  SER B O   1 
ATOM   1887 C  CB  . SER B 1 60  ? 105.570 65.041  43.506  1.00 24.21 ? 57  SER B CB  1 
ATOM   1888 O  OG  . SER B 1 60  ? 106.845 64.469  43.248  1.00 22.56 ? 57  SER B OG  1 
ATOM   1889 N  N   . PRO B 1 61  ? 105.519 62.132  42.156  1.00 23.35 ? 58  PRO B N   1 
ATOM   1890 C  CA  . PRO B 1 61  ? 106.160 60.843  42.418  1.00 22.88 ? 58  PRO B CA  1 
ATOM   1891 C  C   . PRO B 1 61  ? 107.232 61.035  43.508  1.00 23.45 ? 58  PRO B C   1 
ATOM   1892 O  O   . PRO B 1 61  ? 107.817 62.111  43.620  1.00 23.29 ? 58  PRO B O   1 
ATOM   1893 C  CB  . PRO B 1 61  ? 106.825 60.498  41.070  1.00 22.69 ? 58  PRO B CB  1 
ATOM   1894 C  CG  . PRO B 1 61  ? 107.013 61.802  40.362  1.00 22.20 ? 58  PRO B CG  1 
ATOM   1895 C  CD  . PRO B 1 61  ? 105.869 62.680  40.820  1.00 23.48 ? 58  PRO B CD  1 
ATOM   1896 N  N   . THR B 1 62  ? 107.486 60.028  44.327  1.00 23.75 ? 59  THR B N   1 
ATOM   1897 C  CA  . THR B 1 62  ? 108.594 60.154  45.228  1.00 23.47 ? 59  THR B CA  1 
ATOM   1898 C  C   . THR B 1 62  ? 109.876 59.865  44.455  1.00 24.47 ? 59  THR B C   1 
ATOM   1899 O  O   . THR B 1 62  ? 110.073 58.796  43.900  1.00 23.91 ? 59  THR B O   1 
ATOM   1900 C  CB  . THR B 1 62  ? 108.383 59.439  46.618  1.00 23.77 ? 59  THR B CB  1 
ATOM   1901 O  OG1 . THR B 1 62  ? 109.533 58.674  47.004  1.00 24.06 ? 59  THR B OG1 1 
ATOM   1902 C  CG2 . THR B 1 62  ? 107.152 58.639  46.647  1.00 19.39 ? 59  THR B CG2 1 
ATOM   1903 N  N   . ASN B 1 63  ? 110.687 60.904  44.343  1.00 25.14 ? 60  ASN B N   1 
ATOM   1904 C  CA  . ASN B 1 63  ? 111.894 60.852  43.587  1.00 26.20 ? 60  ASN B CA  1 
ATOM   1905 C  C   . ASN B 1 63  ? 113.022 61.109  44.571  1.00 27.20 ? 60  ASN B C   1 
ATOM   1906 O  O   . ASN B 1 63  ? 113.253 62.249  44.974  1.00 27.63 ? 60  ASN B O   1 
ATOM   1907 C  CB  . ASN B 1 63  ? 111.868 61.936  42.507  1.00 26.05 ? 60  ASN B CB  1 
ATOM   1908 C  CG  . ASN B 1 63  ? 110.862 61.652  41.381  1.00 26.25 ? 60  ASN B CG  1 
ATOM   1909 O  OD1 . ASN B 1 63  ? 110.626 62.515  40.554  1.00 29.21 ? 60  ASN B OD1 1 
ATOM   1910 N  ND2 . ASN B 1 63  ? 110.285 60.453  41.335  1.00 25.77 ? 60  ASN B ND2 1 
HETATM 1911 N  N   . MSE B 1 64  ? 113.696 60.039  44.980  1.00 28.27 ? 61  MSE B N   1 
HETATM 1912 C  CA  . MSE B 1 64  ? 114.758 60.089  45.978  1.00 29.90 ? 61  MSE B CA  1 
HETATM 1913 C  C   . MSE B 1 64  ? 114.234 60.594  47.326  1.00 28.18 ? 61  MSE B C   1 
HETATM 1914 O  O   . MSE B 1 64  ? 114.895 61.369  47.975  1.00 28.62 ? 61  MSE B O   1 
HETATM 1915 C  CB  . MSE B 1 64  ? 115.925 60.971  45.525  1.00 32.43 ? 61  MSE B CB  1 
HETATM 1916 C  CG  . MSE B 1 64  ? 116.387 60.758  44.122  1.00 38.84 ? 61  MSE B CG  1 
HETATM 1917 SE SE  . MSE B 1 64  ? 117.248 59.007  43.991  1.00 63.99 ? 61  MSE B SE  1 
HETATM 1918 C  CE  . MSE B 1 64  ? 115.876 57.854  42.968  1.00 46.82 ? 61  MSE B CE  1 
ATOM   1919 N  N   . GLY B 1 65  ? 113.046 60.167  47.715  1.00 27.07 ? 62  GLY B N   1 
ATOM   1920 C  CA  . GLY B 1 65  ? 112.408 60.592  48.962  1.00 26.16 ? 62  GLY B CA  1 
ATOM   1921 C  C   . GLY B 1 65  ? 111.718 61.932  48.951  1.00 25.97 ? 62  GLY B C   1 
ATOM   1922 O  O   . GLY B 1 65  ? 111.154 62.320  49.948  1.00 26.27 ? 62  GLY B O   1 
ATOM   1923 N  N   . LEU B 1 66  ? 111.756 62.649  47.828  1.00 25.74 ? 63  LEU B N   1 
ATOM   1924 C  CA  . LEU B 1 66  ? 111.337 64.061  47.797  1.00 25.20 ? 63  LEU B CA  1 
ATOM   1925 C  C   . LEU B 1 66  ? 110.391 64.369  46.635  1.00 25.59 ? 63  LEU B C   1 
ATOM   1926 O  O   . LEU B 1 66  ? 110.287 63.550  45.683  1.00 24.74 ? 63  LEU B O   1 
ATOM   1927 C  CB  . LEU B 1 66  ? 112.581 64.968  47.679  1.00 24.73 ? 63  LEU B CB  1 
ATOM   1928 C  CG  . LEU B 1 66  ? 113.703 64.942  48.732  1.00 23.93 ? 63  LEU B CG  1 
ATOM   1929 C  CD1 . LEU B 1 66  ? 114.786 65.881  48.310  1.00 22.41 ? 63  LEU B CD1 1 
ATOM   1930 C  CD2 . LEU B 1 66  ? 113.176 65.318  50.181  1.00 22.80 ? 63  LEU B CD2 1 
ATOM   1931 N  N   . VAL B 1 67  ? 109.725 65.549  46.702  1.00 25.59 ? 64  VAL B N   1 
ATOM   1932 C  CA  . VAL B 1 67  ? 109.069 66.156  45.515  1.00 24.32 ? 64  VAL B CA  1 
ATOM   1933 C  C   . VAL B 1 67  ? 109.976 66.066  44.278  1.00 23.65 ? 64  VAL B C   1 
ATOM   1934 O  O   . VAL B 1 67  ? 111.199 66.114  44.402  1.00 24.50 ? 64  VAL B O   1 
ATOM   1935 C  CB  . VAL B 1 67  ? 108.875 67.692  45.586  1.00 24.84 ? 64  VAL B CB  1 
ATOM   1936 C  CG1 . VAL B 1 67  ? 107.460 68.118  45.219  1.00 23.51 ? 64  VAL B CG1 1 
ATOM   1937 C  CG2 . VAL B 1 67  ? 109.480 68.373  46.806  1.00 24.52 ? 64  VAL B CG2 1 
ATOM   1938 N  N   . SER B 1 68  ? 109.387 66.010  43.093  1.00 22.52 ? 65  SER B N   1 
ATOM   1939 C  CA  . SER B 1 68  ? 110.154 65.984  41.868  1.00 22.11 ? 65  SER B CA  1 
ATOM   1940 C  C   . SER B 1 68  ? 110.745 67.373  41.650  1.00 21.19 ? 65  SER B C   1 
ATOM   1941 O  O   . SER B 1 68  ? 110.254 68.349  42.220  1.00 20.74 ? 65  SER B O   1 
ATOM   1942 C  CB  . SER B 1 68  ? 109.232 65.653  40.717  1.00 21.93 ? 65  SER B CB  1 
ATOM   1943 O  OG  . SER B 1 68  ? 108.350 66.748  40.520  1.00 22.55 ? 65  SER B OG  1 
ATOM   1944 N  N   . TRP B 1 69  ? 111.798 67.467  40.844  1.00 20.60 ? 66  TRP B N   1 
ATOM   1945 C  CA  . TRP B 1 69  ? 112.441 68.768  40.599  1.00 20.63 ? 66  TRP B CA  1 
ATOM   1946 C  C   . TRP B 1 69  ? 111.549 69.747  39.829  1.00 21.29 ? 66  TRP B C   1 
ATOM   1947 O  O   . TRP B 1 69  ? 111.633 70.949  40.057  1.00 22.29 ? 66  TRP B O   1 
ATOM   1948 C  CB  . TRP B 1 69  ? 113.813 68.644  39.924  1.00 18.97 ? 66  TRP B CB  1 
ATOM   1949 C  CG  . TRP B 1 69  ? 113.873 68.203  38.464  1.00 19.01 ? 66  TRP B CG  1 
ATOM   1950 C  CD1 . TRP B 1 69  ? 114.119 66.931  38.007  1.00 16.53 ? 66  TRP B CD1 1 
ATOM   1951 C  CD2 . TRP B 1 69  ? 113.767 69.033  37.278  1.00 16.31 ? 66  TRP B CD2 1 
ATOM   1952 N  NE1 . TRP B 1 69  ? 114.174 66.927  36.643  1.00 14.90 ? 66  TRP B NE1 1 
ATOM   1953 C  CE2 . TRP B 1 69  ? 113.938 68.189  36.167  1.00 14.96 ? 66  TRP B CE2 1 
ATOM   1954 C  CE3 . TRP B 1 69  ? 113.540 70.397  37.057  1.00 16.50 ? 66  TRP B CE3 1 
ATOM   1955 C  CZ2 . TRP B 1 69  ? 113.877 68.662  34.837  1.00 18.15 ? 66  TRP B CZ2 1 
ATOM   1956 C  CZ3 . TRP B 1 69  ? 113.480 70.872  35.727  1.00 16.26 ? 66  TRP B CZ3 1 
ATOM   1957 C  CH2 . TRP B 1 69  ? 113.657 70.003  34.642  1.00 17.17 ? 66  TRP B CH2 1 
ATOM   1958 N  N   . LYS B 1 70  ? 110.713 69.219  38.941  1.00 21.30 ? 67  LYS B N   1 
ATOM   1959 C  CA  . LYS B 1 70  ? 109.800 69.999  38.137  1.00 22.54 ? 67  LYS B CA  1 
ATOM   1960 C  C   . LYS B 1 70  ? 108.720 70.674  39.009  1.00 23.35 ? 67  LYS B C   1 
ATOM   1961 O  O   . LYS B 1 70  ? 108.431 71.862  38.831  1.00 24.15 ? 67  LYS B O   1 
ATOM   1962 C  CB  . LYS B 1 70  ? 109.181 69.120  37.020  1.00 22.31 ? 67  LYS B CB  1 
ATOM   1963 C  CG  . LYS B 1 70  ? 109.910 69.144  35.687  1.00 22.52 ? 67  LYS B CG  1 
ATOM   1964 C  CD  . LYS B 1 70  ? 109.156 68.316  34.623  1.00 22.04 ? 67  LYS B CD  1 
ATOM   1965 C  CE  . LYS B 1 70  ? 109.972 68.202  33.348  1.00 22.11 ? 67  LYS B CE  1 
ATOM   1966 N  NZ  . LYS B 1 70  ? 109.307 67.508  32.138  1.00 19.87 ? 67  LYS B NZ  1 
HETATM 1967 N  N   . MSE B 1 71  ? 108.135 69.923  39.931  1.00 23.81 ? 68  MSE B N   1 
HETATM 1968 C  CA  . MSE B 1 71  ? 107.252 70.466  40.957  1.00 25.12 ? 68  MSE B CA  1 
HETATM 1969 C  C   . MSE B 1 71  ? 107.985 71.453  41.893  1.00 25.18 ? 68  MSE B C   1 
HETATM 1970 O  O   . MSE B 1 71  ? 107.449 72.491  42.273  1.00 25.78 ? 68  MSE B O   1 
HETATM 1971 C  CB  . MSE B 1 71  ? 106.615 69.317  41.763  1.00 24.93 ? 68  MSE B CB  1 
HETATM 1972 C  CG  . MSE B 1 71  ? 105.545 69.770  42.751  1.00 29.80 ? 68  MSE B CG  1 
HETATM 1973 SE SE  . MSE B 1 71  ? 104.008 70.694  41.826  1.00 44.56 ? 68  MSE B SE  1 
HETATM 1974 C  CE  . MSE B 1 71  ? 102.988 69.075  41.244  1.00 35.76 ? 68  MSE B CE  1 
ATOM   1975 N  N   . LYS B 1 72  ? 109.204 71.133  42.284  1.00 24.65 ? 69  LYS B N   1 
ATOM   1976 C  CA  . LYS B 1 72  ? 109.987 72.086  43.080  1.00 24.88 ? 69  LYS B CA  1 
ATOM   1977 C  C   . LYS B 1 72  ? 110.176 73.395  42.288  1.00 24.58 ? 69  LYS B C   1 
ATOM   1978 O  O   . LYS B 1 72  ? 109.925 74.485  42.786  1.00 25.70 ? 69  LYS B O   1 
ATOM   1979 C  CB  . LYS B 1 72  ? 111.337 71.462  43.454  1.00 24.04 ? 69  LYS B CB  1 
ATOM   1980 C  CG  . LYS B 1 72  ? 112.134 72.225  44.387  1.00 24.56 ? 69  LYS B CG  1 
ATOM   1981 C  CD  . LYS B 1 72  ? 111.568 72.168  45.833  1.00 25.22 ? 69  LYS B CD  1 
ATOM   1982 C  CE  . LYS B 1 72  ? 111.747 73.522  46.544  1.00 22.65 ? 69  LYS B CE  1 
ATOM   1983 N  NZ  . LYS B 1 72  ? 113.191 73.909  46.509  1.00 20.79 ? 69  LYS B NZ  1 
ATOM   1984 N  N   . ARG B 1 73  ? 110.595 73.267  41.042  1.00 23.97 ? 70  ARG B N   1 
ATOM   1985 C  CA  . ARG B 1 73  ? 110.787 74.394  40.149  1.00 23.30 ? 70  ARG B CA  1 
ATOM   1986 C  C   . ARG B 1 73  ? 109.517 75.257  39.980  1.00 23.44 ? 70  ARG B C   1 
ATOM   1987 O  O   . ARG B 1 73  ? 109.598 76.481  40.023  1.00 22.93 ? 70  ARG B O   1 
ATOM   1988 C  CB  . ARG B 1 73  ? 111.307 73.893  38.815  1.00 22.64 ? 70  ARG B CB  1 
ATOM   1989 C  CG  . ARG B 1 73  ? 111.651 74.999  37.810  1.00 22.39 ? 70  ARG B CG  1 
ATOM   1990 C  CD  . ARG B 1 73  ? 111.122 74.551  36.498  1.00 21.18 ? 70  ARG B CD  1 
ATOM   1991 N  NE  . ARG B 1 73  ? 112.188 74.333  35.566  1.00 22.90 ? 70  ARG B NE  1 
ATOM   1992 C  CZ  . ARG B 1 73  ? 112.084 73.672  34.415  1.00 23.12 ? 70  ARG B CZ  1 
ATOM   1993 N  NH1 . ARG B 1 73  ? 113.163 73.581  33.654  1.00 20.32 ? 70  ARG B NH1 1 
ATOM   1994 N  NH2 . ARG B 1 73  ? 110.945 73.088  34.033  1.00 20.86 ? 70  ARG B NH2 1 
ATOM   1995 N  N   . PHE B 1 74  ? 108.356 74.618  39.804  1.00 23.69 ? 71  PHE B N   1 
ATOM   1996 C  CA  . PHE B 1 74  ? 107.087 75.318  39.794  1.00 23.93 ? 71  PHE B CA  1 
ATOM   1997 C  C   . PHE B 1 74  ? 106.928 76.243  41.039  1.00 24.72 ? 71  PHE B C   1 
ATOM   1998 O  O   . PHE B 1 74  ? 106.674 77.441  40.921  1.00 24.70 ? 71  PHE B O   1 
ATOM   1999 C  CB  . PHE B 1 74  ? 105.918 74.324  39.670  1.00 24.23 ? 71  PHE B CB  1 
ATOM   2000 C  CG  . PHE B 1 74  ? 104.588 74.990  39.588  1.00 24.70 ? 71  PHE B CG  1 
ATOM   2001 C  CD1 . PHE B 1 74  ? 104.163 75.580  38.387  1.00 25.24 ? 71  PHE B CD1 1 
ATOM   2002 C  CD2 . PHE B 1 74  ? 103.789 75.109  40.722  1.00 25.83 ? 71  PHE B CD2 1 
ATOM   2003 C  CE1 . PHE B 1 74  ? 102.945 76.246  38.307  1.00 25.79 ? 71  PHE B CE1 1 
ATOM   2004 C  CE2 . PHE B 1 74  ? 102.568 75.797  40.651  1.00 27.80 ? 71  PHE B CE2 1 
ATOM   2005 C  CZ  . PHE B 1 74  ? 102.148 76.360  39.438  1.00 23.61 ? 71  PHE B CZ  1 
ATOM   2006 N  N   . PHE B 1 75  ? 107.096 75.687  42.225  1.00 25.64 ? 72  PHE B N   1 
ATOM   2007 C  CA  . PHE B 1 75  ? 107.031 76.472  43.451  1.00 26.56 ? 72  PHE B CA  1 
ATOM   2008 C  C   . PHE B 1 75  ? 108.109 77.553  43.633  1.00 27.61 ? 72  PHE B C   1 
ATOM   2009 O  O   . PHE B 1 75  ? 107.784 78.678  44.032  1.00 26.67 ? 72  PHE B O   1 
ATOM   2010 C  CB  . PHE B 1 75  ? 106.957 75.528  44.652  1.00 27.16 ? 72  PHE B CB  1 
ATOM   2011 C  CG  . PHE B 1 75  ? 105.571 75.039  44.909  1.00 27.71 ? 72  PHE B CG  1 
ATOM   2012 C  CD1 . PHE B 1 75  ? 104.984 74.123  44.057  1.00 28.10 ? 72  PHE B CD1 1 
ATOM   2013 C  CD2 . PHE B 1 75  ? 104.829 75.547  45.963  1.00 29.84 ? 72  PHE B CD2 1 
ATOM   2014 C  CE1 . PHE B 1 75  ? 103.677 73.704  44.253  1.00 29.73 ? 72  PHE B CE1 1 
ATOM   2015 C  CE2 . PHE B 1 75  ? 103.532 75.129  46.178  1.00 30.18 ? 72  PHE B CE2 1 
ATOM   2016 C  CZ  . PHE B 1 75  ? 102.943 74.220  45.311  1.00 29.44 ? 72  PHE B CZ  1 
ATOM   2017 N  N   . ASP B 1 76  ? 109.371 77.219  43.336  1.00 28.70 ? 73  ASP B N   1 
ATOM   2018 C  CA  . ASP B 1 76  ? 110.481 78.157  43.463  1.00 30.44 ? 73  ASP B CA  1 
ATOM   2019 C  C   . ASP B 1 76  ? 110.353 79.353  42.522  1.00 31.27 ? 73  ASP B C   1 
ATOM   2020 O  O   . ASP B 1 76  ? 110.581 80.499  42.933  1.00 32.06 ? 73  ASP B O   1 
ATOM   2021 C  CB  . ASP B 1 76  ? 111.846 77.471  43.176  1.00 31.05 ? 73  ASP B CB  1 
ATOM   2022 C  CG  . ASP B 1 76  ? 112.346 76.596  44.324  1.00 32.37 ? 73  ASP B CG  1 
ATOM   2023 O  OD1 . ASP B 1 76  ? 111.832 76.710  45.452  1.00 34.78 ? 73  ASP B OD1 1 
ATOM   2024 O  OD2 . ASP B 1 76  ? 113.267 75.770  44.082  1.00 35.77 ? 73  ASP B OD2 1 
ATOM   2025 N  N   . ASP B 1 77  ? 110.001 79.069  41.269  1.00 31.73 ? 74  ASP B N   1 
ATOM   2026 C  CA  . ASP B 1 77  ? 110.172 79.999  40.177  1.00 32.57 ? 74  ASP B CA  1 
ATOM   2027 C  C   . ASP B 1 77  ? 108.873 80.576  39.597  1.00 33.41 ? 74  ASP B C   1 
ATOM   2028 O  O   . ASP B 1 77  ? 108.864 81.734  39.162  1.00 34.27 ? 74  ASP B O   1 
ATOM   2029 C  CB  . ASP B 1 77  ? 111.047 79.384  39.056  1.00 32.89 ? 74  ASP B CB  1 
ATOM   2030 C  CG  . ASP B 1 77  ? 112.529 79.128  39.487  1.00 33.25 ? 74  ASP B CG  1 
ATOM   2031 O  OD1 . ASP B 1 77  ? 112.961 79.483  40.607  1.00 33.61 ? 74  ASP B OD1 1 
ATOM   2032 O  OD2 . ASP B 1 77  ? 113.282 78.557  38.675  1.00 34.19 ? 74  ASP B OD2 1 
ATOM   2033 N  N   . VAL B 1 78  ? 107.781 79.817  39.552  1.00 33.81 ? 75  VAL B N   1 
ATOM   2034 C  CA  . VAL B 1 78  ? 106.526 80.451  39.100  1.00 33.60 ? 75  VAL B CA  1 
ATOM   2035 C  C   . VAL B 1 78  ? 105.652 80.958  40.244  1.00 34.07 ? 75  VAL B C   1 
ATOM   2036 O  O   . VAL B 1 78  ? 105.052 82.028  40.132  1.00 34.52 ? 75  VAL B O   1 
ATOM   2037 C  CB  . VAL B 1 78  ? 105.741 79.686  37.952  1.00 33.57 ? 75  VAL B CB  1 
ATOM   2038 C  CG1 . VAL B 1 78  ? 106.352 78.339  37.630  1.00 33.57 ? 75  VAL B CG1 1 
ATOM   2039 C  CG2 . VAL B 1 78  ? 104.205 79.656  38.186  1.00 31.83 ? 75  VAL B CG2 1 
ATOM   2040 N  N   . LEU B 1 79  ? 105.607 80.224  41.352  1.00 34.06 ? 76  LEU B N   1 
ATOM   2041 C  CA  . LEU B 1 79  ? 104.864 80.698  42.514  1.00 33.80 ? 76  LEU B CA  1 
ATOM   2042 C  C   . LEU B 1 79  ? 105.678 81.636  43.389  1.00 33.33 ? 76  LEU B C   1 
ATOM   2043 O  O   . LEU B 1 79  ? 105.122 82.316  44.232  1.00 33.69 ? 76  LEU B O   1 
ATOM   2044 C  CB  . LEU B 1 79  ? 104.321 79.545  43.332  1.00 33.67 ? 76  LEU B CB  1 
ATOM   2045 C  CG  . LEU B 1 79  ? 103.408 78.571  42.601  1.00 34.70 ? 76  LEU B CG  1 
ATOM   2046 C  CD1 . LEU B 1 79  ? 102.694 77.754  43.672  1.00 35.23 ? 76  LEU B CD1 1 
ATOM   2047 C  CD2 . LEU B 1 79  ? 102.397 79.283  41.665  1.00 32.71 ? 76  LEU B CD2 1 
ATOM   2048 N  N   . GLY B 1 80  ? 106.988 81.682  43.172  1.00 33.13 ? 77  GLY B N   1 
ATOM   2049 C  CA  . GLY B 1 80  ? 107.884 82.567  43.919  1.00 33.07 ? 77  GLY B CA  1 
ATOM   2050 C  C   . GLY B 1 80  ? 107.471 84.035  43.992  1.00 33.03 ? 77  GLY B C   1 
ATOM   2051 O  O   . GLY B 1 80  ? 107.693 84.684  44.990  1.00 32.66 ? 77  GLY B O   1 
ATOM   2052 N  N   . ASP B 1 81  ? 106.866 84.558  42.931  1.00 33.29 ? 78  ASP B N   1 
ATOM   2053 C  CA  . ASP B 1 81  ? 106.387 85.945  42.916  1.00 33.33 ? 78  ASP B CA  1 
ATOM   2054 C  C   . ASP B 1 81  ? 105.232 86.238  43.867  1.00 31.82 ? 78  ASP B C   1 
ATOM   2055 O  O   . ASP B 1 81  ? 105.064 87.375  44.307  1.00 31.25 ? 78  ASP B O   1 
ATOM   2056 C  CB  . ASP B 1 81  ? 105.974 86.342  41.495  1.00 34.39 ? 78  ASP B CB  1 
ATOM   2057 C  CG  . ASP B 1 81  ? 107.145 86.803  40.661  1.00 37.52 ? 78  ASP B CG  1 
ATOM   2058 O  OD1 . ASP B 1 81  ? 108.117 87.353  41.254  1.00 39.65 ? 78  ASP B OD1 1 
ATOM   2059 O  OD2 . ASP B 1 81  ? 107.084 86.618  39.411  1.00 41.67 ? 78  ASP B OD2 1 
ATOM   2060 N  N   . LEU B 1 82  ? 104.422 85.218  44.134  1.00 30.57 ? 79  LEU B N   1 
ATOM   2061 C  CA  . LEU B 1 82  ? 103.302 85.309  45.085  1.00 29.84 ? 79  LEU B CA  1 
ATOM   2062 C  C   . LEU B 1 82  ? 103.700 85.067  46.550  1.00 28.78 ? 79  LEU B C   1 
ATOM   2063 O  O   . LEU B 1 82  ? 102.894 85.248  47.461  1.00 28.93 ? 79  LEU B O   1 
ATOM   2064 C  CB  . LEU B 1 82  ? 102.206 84.324  44.698  1.00 29.30 ? 79  LEU B CB  1 
ATOM   2065 C  CG  . LEU B 1 82  ? 101.624 84.455  43.290  1.00 30.89 ? 79  LEU B CG  1 
ATOM   2066 C  CD1 . LEU B 1 82  ? 100.518 83.390  43.081  1.00 30.39 ? 79  LEU B CD1 1 
ATOM   2067 C  CD2 . LEU B 1 82  ? 101.118 85.874  43.025  1.00 29.57 ? 79  LEU B CD2 1 
ATOM   2068 N  N   . TRP B 1 83  ? 104.942 84.643  46.763  1.00 27.91 ? 80  TRP B N   1 
ATOM   2069 C  CA  . TRP B 1 83  ? 105.418 84.311  48.094  1.00 26.59 ? 80  TRP B CA  1 
ATOM   2070 C  C   . TRP B 1 83  ? 105.258 85.509  49.022  1.00 26.93 ? 80  TRP B C   1 
ATOM   2071 O  O   . TRP B 1 83  ? 105.768 86.603  48.754  1.00 26.96 ? 80  TRP B O   1 
ATOM   2072 C  CB  . TRP B 1 83  ? 106.879 83.815  48.075  1.00 24.76 ? 80  TRP B CB  1 
ATOM   2073 C  CG  . TRP B 1 83  ? 107.270 83.266  49.415  1.00 23.06 ? 80  TRP B CG  1 
ATOM   2074 C  CD1 . TRP B 1 83  ? 107.153 81.983  49.835  1.00 20.52 ? 80  TRP B CD1 1 
ATOM   2075 C  CD2 . TRP B 1 83  ? 107.766 84.015  50.534  1.00 20.75 ? 80  TRP B CD2 1 
ATOM   2076 N  NE1 . TRP B 1 83  ? 107.570 81.871  51.139  1.00 19.99 ? 80  TRP B NE1 1 
ATOM   2077 C  CE2 . TRP B 1 83  ? 107.952 83.105  51.592  1.00 19.72 ? 80  TRP B CE2 1 
ATOM   2078 C  CE3 . TRP B 1 83  ? 108.077 85.366  50.736  1.00 20.23 ? 80  TRP B CE3 1 
ATOM   2079 C  CZ2 . TRP B 1 83  ? 108.439 83.492  52.840  1.00 19.45 ? 80  TRP B CZ2 1 
ATOM   2080 C  CZ3 . TRP B 1 83  ? 108.570 85.752  51.979  1.00 22.27 ? 80  TRP B CZ3 1 
ATOM   2081 C  CH2 . TRP B 1 83  ? 108.744 84.811  53.013  1.00 21.59 ? 80  TRP B CH2 1 
ATOM   2082 N  N   . GLY B 1 84  ? 104.537 85.288  50.114  1.00 27.42 ? 81  GLY B N   1 
ATOM   2083 C  CA  . GLY B 1 84  ? 104.329 86.325  51.090  1.00 27.54 ? 81  GLY B CA  1 
ATOM   2084 C  C   . GLY B 1 84  ? 102.990 87.004  50.983  1.00 27.58 ? 81  GLY B C   1 
ATOM   2085 O  O   . GLY B 1 84  ? 102.653 87.836  51.813  1.00 28.35 ? 81  GLY B O   1 
ATOM   2086 N  N   . GLU B 1 85  ? 102.197 86.657  49.987  1.00 27.63 ? 82  GLU B N   1 
ATOM   2087 C  CA  . GLU B 1 85  ? 100.886 87.283  49.882  1.00 28.18 ? 82  GLU B CA  1 
ATOM   2088 C  C   . GLU B 1 85  ? 99.743  86.336  49.567  1.00 27.10 ? 82  GLU B C   1 
ATOM   2089 O  O   . GLU B 1 85  ? 98.634  86.779  49.267  1.00 27.44 ? 82  GLU B O   1 
ATOM   2090 C  CB  . GLU B 1 85  ? 100.914 88.481  48.907  1.00 28.27 ? 82  GLU B CB  1 
ATOM   2091 C  CG  . GLU B 1 85  ? 101.453 88.220  47.525  1.00 30.04 ? 82  GLU B CG  1 
ATOM   2092 C  CD  . GLU B 1 85  ? 101.856 89.526  46.817  1.00 30.77 ? 82  GLU B CD  1 
ATOM   2093 O  OE1 . GLU B 1 85  ? 102.462 89.464  45.725  1.00 31.40 ? 82  GLU B OE1 1 
ATOM   2094 O  OE2 . GLU B 1 85  ? 101.572 90.618  47.369  1.00 35.09 ? 82  GLU B OE2 1 
ATOM   2095 N  N   . ILE B 1 86  ? 100.013 85.037  49.615  1.00 26.17 ? 83  ILE B N   1 
ATOM   2096 C  CA  . ILE B 1 86  ? 98.960  84.052  49.415  1.00 25.26 ? 83  ILE B CA  1 
ATOM   2097 C  C   . ILE B 1 86  ? 98.860  83.128  50.616  1.00 25.25 ? 83  ILE B C   1 
ATOM   2098 O  O   . ILE B 1 86  ? 98.435  81.981  50.466  1.00 24.86 ? 83  ILE B O   1 
ATOM   2099 C  CB  . ILE B 1 86  ? 99.092  83.238  48.088  1.00 25.68 ? 83  ILE B CB  1 
ATOM   2100 C  CG1 . ILE B 1 86  ? 100.434 82.507  47.984  1.00 25.53 ? 83  ILE B CG1 1 
ATOM   2101 C  CG2 . ILE B 1 86  ? 98.849  84.125  46.864  1.00 25.78 ? 83  ILE B CG2 1 
ATOM   2102 C  CD1 . ILE B 1 86  ? 100.479 81.444  46.903  1.00 24.50 ? 83  ILE B CD1 1 
ATOM   2103 N  N   . ASP B 1 87  ? 99.227  83.652  51.800  1.00 24.79 ? 84  ASP B N   1 
ATOM   2104 C  CA  . ASP B 1 87  ? 99.153  82.929  53.069  1.00 24.74 ? 84  ASP B CA  1 
ATOM   2105 C  C   . ASP B 1 87  ? 97.723  82.600  53.370  1.00 25.01 ? 84  ASP B C   1 
ATOM   2106 O  O   . ASP B 1 87  ? 96.841  83.402  53.105  1.00 25.68 ? 84  ASP B O   1 
ATOM   2107 C  CB  . ASP B 1 87  ? 99.667  83.780  54.230  1.00 24.33 ? 84  ASP B CB  1 
ATOM   2108 C  CG  . ASP B 1 87  ? 101.119 84.217  54.063  1.00 25.56 ? 84  ASP B CG  1 
ATOM   2109 O  OD1 . ASP B 1 87  ? 101.470 84.903  53.051  1.00 23.25 ? 84  ASP B OD1 1 
ATOM   2110 O  OD2 . ASP B 1 87  ? 101.899 83.914  54.993  1.00 23.05 ? 84  ASP B OD2 1 
ATOM   2111 N  N   . GLY B 1 88  ? 97.487  81.424  53.925  1.00 24.99 ? 85  GLY B N   1 
ATOM   2112 C  CA  . GLY B 1 88  ? 96.160  81.054  54.362  1.00 25.96 ? 85  GLY B CA  1 
ATOM   2113 C  C   . GLY B 1 88  ? 95.380  80.162  53.419  1.00 26.82 ? 85  GLY B C   1 
ATOM   2114 O  O   . GLY B 1 88  ? 94.214  79.819  53.699  1.00 27.60 ? 85  GLY B O   1 
ATOM   2115 N  N   . LYS B 1 89  ? 95.985  79.795  52.291  1.00 26.83 ? 86  LYS B N   1 
ATOM   2116 C  CA  . LYS B 1 89  ? 95.400  78.748  51.462  1.00 26.55 ? 86  LYS B CA  1 
ATOM   2117 C  C   . LYS B 1 89  ? 95.506  77.442  52.244  1.00 26.87 ? 86  LYS B C   1 
ATOM   2118 O  O   . LYS B 1 89  ? 96.351  77.307  53.146  1.00 26.37 ? 86  LYS B O   1 
ATOM   2119 C  CB  . LYS B 1 89  ? 96.070  78.669  50.090  1.00 26.54 ? 86  LYS B CB  1 
ATOM   2120 C  CG  . LYS B 1 89  ? 95.958  79.974  49.343  1.00 25.01 ? 86  LYS B CG  1 
ATOM   2121 C  CD  . LYS B 1 89  ? 96.100  79.814  47.866  1.00 25.69 ? 86  LYS B CD  1 
ATOM   2122 C  CE  . LYS B 1 89  ? 95.924  81.166  47.186  1.00 25.76 ? 86  LYS B CE  1 
ATOM   2123 N  NZ  . LYS B 1 89  ? 94.474  81.480  46.914  1.00 25.86 ? 86  LYS B NZ  1 
ATOM   2124 N  N   . ILE B 1 90  ? 94.589  76.519  51.969  1.00 27.24 ? 87  ILE B N   1 
ATOM   2125 C  CA  . ILE B 1 90  ? 94.606  75.212  52.639  1.00 27.52 ? 87  ILE B CA  1 
ATOM   2126 C  C   . ILE B 1 90  ? 95.221  74.198  51.669  1.00 27.38 ? 87  ILE B C   1 
ATOM   2127 O  O   . ILE B 1 90  ? 94.949  74.245  50.465  1.00 26.54 ? 87  ILE B O   1 
ATOM   2128 C  CB  . ILE B 1 90  ? 93.187  74.767  53.123  1.00 28.16 ? 87  ILE B CB  1 
ATOM   2129 C  CG1 . ILE B 1 90  ? 92.578  75.833  54.051  1.00 27.07 ? 87  ILE B CG1 1 
ATOM   2130 C  CG2 . ILE B 1 90  ? 93.285  73.401  53.825  1.00 28.28 ? 87  ILE B CG2 1 
ATOM   2131 C  CD1 . ILE B 1 90  ? 91.096  75.707  54.278  1.00 26.67 ? 87  ILE B CD1 1 
ATOM   2132 N  N   . ALA B 1 91  ? 96.064  73.301  52.175  1.00 26.89 ? 88  ALA B N   1 
ATOM   2133 C  CA  . ALA B 1 91  ? 96.792  72.418  51.266  1.00 26.50 ? 88  ALA B CA  1 
ATOM   2134 C  C   . ALA B 1 91  ? 97.159  71.074  51.869  1.00 26.60 ? 88  ALA B C   1 
ATOM   2135 O  O   . ALA B 1 91  ? 97.294  70.929  53.080  1.00 26.07 ? 88  ALA B O   1 
ATOM   2136 C  CB  . ALA B 1 91  ? 98.042  73.139  50.723  1.00 26.21 ? 88  ALA B CB  1 
ATOM   2137 N  N   . CYS B 1 92  ? 97.324  70.082  50.998  1.00 27.01 ? 89  CYS B N   1 
ATOM   2138 C  CA  . CYS B 1 92  ? 97.675  68.731  51.414  1.00 26.18 ? 89  CYS B CA  1 
ATOM   2139 C  C   . CYS B 1 92  ? 98.458  68.126  50.259  1.00 25.28 ? 89  CYS B C   1 
ATOM   2140 O  O   . CYS B 1 92  ? 98.654  68.794  49.245  1.00 24.71 ? 89  CYS B O   1 
ATOM   2141 C  CB  . CYS B 1 92  ? 96.408  67.942  51.722  1.00 26.61 ? 89  CYS B CB  1 
ATOM   2142 S  SG  . CYS B 1 92  ? 95.291  67.787  50.305  1.00 28.86 ? 89  CYS B SG  1 
ATOM   2143 N  N   . ALA B 1 93  ? 98.878  66.869  50.397  1.00 24.38 ? 90  ALA B N   1 
ATOM   2144 C  CA  . ALA B 1 93  ? 99.958  66.298  49.565  1.00 24.15 ? 90  ALA B CA  1 
ATOM   2145 C  C   . ALA B 1 93  ? 99.660  64.847  49.223  1.00 24.32 ? 90  ALA B C   1 
ATOM   2146 O  O   . ALA B 1 93  ? 98.943  64.141  49.975  1.00 24.58 ? 90  ALA B O   1 
ATOM   2147 C  CB  . ALA B 1 93  ? 101.303 66.357  50.325  1.00 22.28 ? 90  ALA B CB  1 
ATOM   2148 N  N   . PHE B 1 94  ? 100.224 64.375  48.118  1.00 24.43 ? 91  PHE B N   1 
ATOM   2149 C  CA  . PHE B 1 94  ? 100.107 62.942  47.807  1.00 25.50 ? 91  PHE B CA  1 
ATOM   2150 C  C   . PHE B 1 94  ? 101.238 62.439  46.962  1.00 25.96 ? 91  PHE B C   1 
ATOM   2151 O  O   . PHE B 1 94  ? 101.827 63.212  46.196  1.00 26.25 ? 91  PHE B O   1 
ATOM   2152 C  CB  . PHE B 1 94  ? 98.754  62.562  47.188  1.00 24.83 ? 91  PHE B CB  1 
ATOM   2153 C  CG  . PHE B 1 94  ? 98.442  63.245  45.872  1.00 25.79 ? 91  PHE B CG  1 
ATOM   2154 C  CD1 . PHE B 1 94  ? 97.887  64.527  45.854  1.00 24.17 ? 91  PHE B CD1 1 
ATOM   2155 C  CD2 . PHE B 1 94  ? 98.624  62.573  44.660  1.00 25.28 ? 91  PHE B CD2 1 
ATOM   2156 C  CE1 . PHE B 1 94  ? 97.535  65.136  44.656  1.00 27.21 ? 91  PHE B CE1 1 
ATOM   2157 C  CE2 . PHE B 1 94  ? 98.280  63.176  43.434  1.00 26.52 ? 91  PHE B CE2 1 
ATOM   2158 C  CZ  . PHE B 1 94  ? 97.744  64.465  43.422  1.00 26.03 ? 91  PHE B CZ  1 
ATOM   2159 N  N   . SER B 1 95  ? 101.530 61.143  47.092  1.00 25.85 ? 92  SER B N   1 
ATOM   2160 C  CA  . SER B 1 95  ? 102.686 60.604  46.434  1.00 26.64 ? 92  SER B CA  1 
ATOM   2161 C  C   . SER B 1 95  ? 102.586 59.151  46.092  1.00 26.51 ? 92  SER B C   1 
ATOM   2162 O  O   . SER B 1 95  ? 102.040 58.329  46.855  1.00 26.55 ? 92  SER B O   1 
ATOM   2163 C  CB  . SER B 1 95  ? 103.949 60.866  47.270  1.00 26.88 ? 92  SER B CB  1 
ATOM   2164 O  OG  . SER B 1 95  ? 105.119 60.713  46.481  1.00 29.22 ? 92  SER B OG  1 
ATOM   2165 N  N   . SER B 1 96  ? 103.134 58.843  44.923  1.00 26.59 ? 93  SER B N   1 
ATOM   2166 C  CA  . SER B 1 96  ? 103.307 57.470  44.488  1.00 26.75 ? 93  SER B CA  1 
ATOM   2167 C  C   . SER B 1 96  ? 104.777 57.159  44.524  1.00 26.53 ? 93  SER B C   1 
ATOM   2168 O  O   . SER B 1 96  ? 105.573 57.909  43.991  1.00 26.39 ? 93  SER B O   1 
ATOM   2169 C  CB  . SER B 1 96  ? 102.806 57.296  43.064  1.00 26.62 ? 93  SER B CB  1 
ATOM   2170 O  OG  . SER B 1 96  ? 102.957 55.939  42.685  1.00 27.89 ? 93  SER B OG  1 
ATOM   2171 N  N   . SER B 1 97  ? 105.141 56.066  45.167  1.00 27.30 ? 94  SER B N   1 
ATOM   2172 C  CA  . SER B 1 97  ? 106.524 55.621  45.178  1.00 28.63 ? 94  SER B CA  1 
ATOM   2173 C  C   . SER B 1 97  ? 106.625 54.269  44.511  1.00 28.08 ? 94  SER B C   1 
ATOM   2174 O  O   . SER B 1 97  ? 105.605 53.650  44.231  1.00 28.45 ? 94  SER B O   1 
ATOM   2175 C  CB  . SER B 1 97  ? 107.083 55.572  46.614  1.00 29.04 ? 94  SER B CB  1 
ATOM   2176 O  OG  . SER B 1 97  ? 106.568 54.469  47.351  1.00 32.15 ? 94  SER B OG  1 
ATOM   2177 N  N   . GLY B 1 98  ? 107.859 53.833  44.242  1.00 28.24 ? 95  GLY B N   1 
ATOM   2178 C  CA  . GLY B 1 98  ? 108.146 52.504  43.683  1.00 27.24 ? 95  GLY B CA  1 
ATOM   2179 C  C   . GLY B 1 98  ? 107.862 51.363  44.652  1.00 27.61 ? 95  GLY B C   1 
ATOM   2180 O  O   . GLY B 1 98  ? 107.705 50.202  44.243  1.00 27.86 ? 95  GLY B O   1 
ATOM   2181 N  N   . GLY B 1 99  ? 107.779 51.671  45.942  1.00 27.19 ? 96  GLY B N   1 
ATOM   2182 C  CA  . GLY B 1 99  ? 107.559 50.612  46.910  1.00 27.19 ? 96  GLY B CA  1 
ATOM   2183 C  C   . GLY B 1 99  ? 107.103 51.120  48.246  1.00 26.35 ? 96  GLY B C   1 
ATOM   2184 O  O   . GLY B 1 99  ? 107.308 52.276  48.556  1.00 26.63 ? 96  GLY B O   1 
ATOM   2185 N  N   . TRP B 1 100 ? 106.444 50.252  49.003  1.00 26.36 ? 97  TRP B N   1 
ATOM   2186 C  CA  . TRP B 1 100 ? 106.193 50.463  50.431  1.00 26.29 ? 97  TRP B CA  1 
ATOM   2187 C  C   . TRP B 1 100 ? 107.518 50.364  51.163  1.00 25.35 ? 97  TRP B C   1 
ATOM   2188 O  O   . TRP B 1 100 ? 108.322 49.477  50.890  1.00 24.07 ? 97  TRP B O   1 
ATOM   2189 C  CB  . TRP B 1 100 ? 105.187 49.443  50.960  1.00 27.29 ? 97  TRP B CB  1 
ATOM   2190 C  CG  . TRP B 1 100 ? 103.851 49.608  50.290  1.00 28.87 ? 97  TRP B CG  1 
ATOM   2191 C  CD1 . TRP B 1 100 ? 103.311 48.805  49.308  1.00 29.75 ? 97  TRP B CD1 1 
ATOM   2192 C  CD2 . TRP B 1 100 ? 102.908 50.669  50.501  1.00 29.96 ? 97  TRP B CD2 1 
ATOM   2193 N  NE1 . TRP B 1 100 ? 102.088 49.299  48.912  1.00 30.39 ? 97  TRP B NE1 1 
ATOM   2194 C  CE2 . TRP B 1 100 ? 101.810 50.434  49.633  1.00 31.21 ? 97  TRP B CE2 1 
ATOM   2195 C  CE3 . TRP B 1 100 ? 102.868 51.780  51.355  1.00 29.94 ? 97  TRP B CE3 1 
ATOM   2196 C  CZ2 . TRP B 1 100 ? 100.687 51.278  49.593  1.00 30.34 ? 97  TRP B CZ2 1 
ATOM   2197 C  CZ3 . TRP B 1 100 ? 101.748 52.617  51.316  1.00 29.77 ? 97  TRP B CZ3 1 
ATOM   2198 C  CH2 . TRP B 1 100 ? 100.676 52.363  50.440  1.00 28.63 ? 97  TRP B CH2 1 
ATOM   2199 N  N   . GLY B 1 101 ? 107.740 51.320  52.060  1.00 25.35 ? 98  GLY B N   1 
ATOM   2200 C  CA  . GLY B 1 101 ? 109.032 51.545  52.696  1.00 25.35 ? 98  GLY B CA  1 
ATOM   2201 C  C   . GLY B 1 101 ? 109.917 52.378  51.786  1.00 25.81 ? 98  GLY B C   1 
ATOM   2202 O  O   . GLY B 1 101 ? 111.083 52.632  52.108  1.00 26.20 ? 98  GLY B O   1 
ATOM   2203 N  N   . GLY B 1 102 ? 109.349 52.815  50.658  1.00 25.68 ? 99  GLY B N   1 
ATOM   2204 C  CA  . GLY B 1 102 ? 110.089 53.486  49.595  1.00 26.22 ? 99  GLY B CA  1 
ATOM   2205 C  C   . GLY B 1 102 ? 110.200 54.989  49.697  1.00 27.00 ? 99  GLY B C   1 
ATOM   2206 O  O   . GLY B 1 102 ? 110.827 55.597  48.857  1.00 27.19 ? 99  GLY B O   1 
ATOM   2207 N  N   . GLY B 1 103 ? 109.575 55.586  50.714  1.00 27.67 ? 100 GLY B N   1 
ATOM   2208 C  CA  . GLY B 1 103 ? 109.683 57.014  50.971  1.00 28.38 ? 100 GLY B CA  1 
ATOM   2209 C  C   . GLY B 1 103 ? 108.506 57.906  50.616  1.00 29.20 ? 100 GLY B C   1 
ATOM   2210 O  O   . GLY B 1 103 ? 108.658 59.141  50.579  1.00 29.50 ? 100 GLY B O   1 
ATOM   2211 N  N   . ASN B 1 104 ? 107.333 57.317  50.368  1.00 29.54 ? 101 ASN B N   1 
ATOM   2212 C  CA  . ASN B 1 104 ? 106.181 58.125  49.979  1.00 30.09 ? 101 ASN B CA  1 
ATOM   2213 C  C   . ASN B 1 104 ? 105.653 59.099  51.022  1.00 30.23 ? 101 ASN B C   1 
ATOM   2214 O  O   . ASN B 1 104 ? 105.265 60.212  50.668  1.00 30.98 ? 101 ASN B O   1 
ATOM   2215 C  CB  . ASN B 1 104 ? 105.048 57.338  49.304  1.00 30.88 ? 101 ASN B CB  1 
ATOM   2216 C  CG  . ASN B 1 104 ? 104.705 56.035  49.981  1.00 34.34 ? 101 ASN B CG  1 
ATOM   2217 O  OD1 . ASN B 1 104 ? 104.316 55.070  49.303  1.00 42.43 ? 101 ASN B OD1 1 
ATOM   2218 N  ND2 . ASN B 1 104 ? 104.789 55.988  51.287  1.00 35.40 ? 101 ASN B ND2 1 
ATOM   2219 N  N   . GLU B 1 105 ? 105.652 58.687  52.291  1.00 29.71 ? 102 GLU B N   1 
ATOM   2220 C  CA  . GLU B 1 105 ? 105.334 59.570  53.401  1.00 29.65 ? 102 GLU B CA  1 
ATOM   2221 C  C   . GLU B 1 105 ? 106.426 60.655  53.567  1.00 28.41 ? 102 GLU B C   1 
ATOM   2222 O  O   . GLU B 1 105 ? 106.131 61.787  53.898  1.00 28.23 ? 102 GLU B O   1 
ATOM   2223 C  CB  . GLU B 1 105 ? 105.185 58.771  54.710  1.00 30.05 ? 102 GLU B CB  1 
ATOM   2224 C  CG  . GLU B 1 105 ? 103.989 57.835  54.774  1.00 30.66 ? 102 GLU B CG  1 
ATOM   2225 C  CD  . GLU B 1 105 ? 104.034 56.902  55.977  1.00 31.15 ? 102 GLU B CD  1 
ATOM   2226 O  OE1 . GLU B 1 105 ? 104.846 57.131  56.887  1.00 32.83 ? 102 GLU B OE1 1 
ATOM   2227 O  OE2 . GLU B 1 105 ? 103.257 55.911  56.006  1.00 37.87 ? 102 GLU B OE2 1 
ATOM   2228 N  N   . VAL B 1 106 ? 107.684 60.315  53.324  1.00 27.12 ? 103 VAL B N   1 
ATOM   2229 C  CA  . VAL B 1 106 ? 108.733 61.335  53.389  1.00 26.25 ? 103 VAL B CA  1 
ATOM   2230 C  C   . VAL B 1 106 ? 108.586 62.354  52.249  1.00 26.62 ? 103 VAL B C   1 
ATOM   2231 O  O   . VAL B 1 106 ? 108.720 63.540  52.482  1.00 27.28 ? 103 VAL B O   1 
ATOM   2232 C  CB  . VAL B 1 106 ? 110.143 60.705  53.485  1.00 26.15 ? 103 VAL B CB  1 
ATOM   2233 C  CG1 . VAL B 1 106 ? 111.219 61.743  53.534  1.00 22.37 ? 103 VAL B CG1 1 
ATOM   2234 C  CG2 . VAL B 1 106 ? 110.219 59.808  54.742  1.00 26.69 ? 103 VAL B CG2 1 
ATOM   2235 N  N   . ALA B 1 107 ? 108.265 61.892  51.035  1.00 26.43 ? 104 ALA B N   1 
ATOM   2236 C  CA  . ALA B 1 107 ? 107.993 62.785  49.927  1.00 25.61 ? 104 ALA B CA  1 
ATOM   2237 C  C   . ALA B 1 107 ? 106.791 63.697  50.198  1.00 25.98 ? 104 ALA B C   1 
ATOM   2238 O  O   . ALA B 1 107 ? 106.837 64.893  49.884  1.00 26.25 ? 104 ALA B O   1 
ATOM   2239 C  CB  . ALA B 1 107 ? 107.824 61.983  48.590  1.00 24.96 ? 104 ALA B CB  1 
ATOM   2240 N  N   . CYS B 1 108 ? 105.711 63.126  50.744  1.00 26.14 ? 105 CYS B N   1 
ATOM   2241 C  CA  . CYS B 1 108 ? 104.612 63.912  51.319  1.00 26.55 ? 105 CYS B CA  1 
ATOM   2242 C  C   . CYS B 1 108 ? 105.068 64.973  52.344  1.00 26.46 ? 105 CYS B C   1 
ATOM   2243 O  O   . CYS B 1 108 ? 104.620 66.115  52.256  1.00 27.03 ? 105 CYS B O   1 
ATOM   2244 C  CB  . CYS B 1 108 ? 103.524 63.002  51.926  1.00 26.28 ? 105 CYS B CB  1 
ATOM   2245 S  SG  . CYS B 1 108 ? 102.431 62.298  50.697  1.00 26.15 ? 105 CYS B SG  1 
HETATM 2246 N  N   . MSE B 1 109 ? 105.941 64.620  53.297  1.00 27.26 ? 106 MSE B N   1 
HETATM 2247 C  CA  . MSE B 1 109 ? 106.555 65.637  54.217  1.00 28.11 ? 106 MSE B CA  1 
HETATM 2248 C  C   . MSE B 1 109 ? 107.206 66.800  53.442  1.00 27.29 ? 106 MSE B C   1 
HETATM 2249 O  O   . MSE B 1 109 ? 107.028 67.973  53.832  1.00 26.87 ? 106 MSE B O   1 
HETATM 2250 C  CB  . MSE B 1 109 ? 107.594 65.042  55.178  1.00 28.67 ? 106 MSE B CB  1 
HETATM 2251 C  CG  . MSE B 1 109 ? 107.051 64.341  56.441  1.00 38.64 ? 106 MSE B CG  1 
HETATM 2252 SE SE  . MSE B 1 109 ? 105.447 65.299  57.375  1.00 61.23 ? 106 MSE B SE  1 
HETATM 2253 C  CE  . MSE B 1 109 ? 106.344 66.973  57.692  1.00 45.22 ? 106 MSE B CE  1 
ATOM   2254 N  N   . SER B 1 110 ? 107.954 66.473  52.366  1.00 25.33 ? 107 SER B N   1 
ATOM   2255 C  CA  . SER B 1 110 ? 108.678 67.508  51.567  1.00 24.79 ? 107 SER B CA  1 
ATOM   2256 C  C   . SER B 1 110 ? 107.718 68.467  50.849  1.00 23.76 ? 107 SER B C   1 
ATOM   2257 O  O   . SER B 1 110 ? 107.934 69.665  50.838  1.00 23.48 ? 107 SER B O   1 
ATOM   2258 C  CB  . SER B 1 110 ? 109.740 66.933  50.594  1.00 23.92 ? 107 SER B CB  1 
ATOM   2259 O  OG  . SER B 1 110 ? 109.131 66.269  49.478  1.00 21.62 ? 107 SER B OG  1 
ATOM   2260 N  N   . ILE B 1 111 ? 106.661 67.920  50.278  1.00 23.96 ? 108 ILE B N   1 
ATOM   2261 C  CA  . ILE B 1 111 ? 105.571 68.711  49.716  1.00 24.31 ? 108 ILE B CA  1 
ATOM   2262 C  C   . ILE B 1 111 ? 104.957 69.652  50.760  1.00 24.98 ? 108 ILE B C   1 
ATOM   2263 O  O   . ILE B 1 111 ? 104.793 70.843  50.499  1.00 24.36 ? 108 ILE B O   1 
ATOM   2264 C  CB  . ILE B 1 111 ? 104.503 67.808  49.106  1.00 24.40 ? 108 ILE B CB  1 
ATOM   2265 C  CG1 . ILE B 1 111 ? 105.046 67.188  47.806  1.00 23.42 ? 108 ILE B CG1 1 
ATOM   2266 C  CG2 . ILE B 1 111 ? 103.259 68.615  48.795  1.00 24.25 ? 108 ILE B CG2 1 
ATOM   2267 C  CD1 . ILE B 1 111 ? 104.398 65.869  47.390  1.00 22.83 ? 108 ILE B CD1 1 
ATOM   2268 N  N   . LEU B 1 112 ? 104.682 69.118  51.954  1.00 25.55 ? 109 LEU B N   1 
ATOM   2269 C  CA  . LEU B 1 112 ? 104.104 69.888  53.045  1.00 25.77 ? 109 LEU B CA  1 
ATOM   2270 C  C   . LEU B 1 112 ? 105.019 70.992  53.579  1.00 26.35 ? 109 LEU B C   1 
ATOM   2271 O  O   . LEU B 1 112 ? 104.553 72.023  54.031  1.00 26.84 ? 109 LEU B O   1 
ATOM   2272 C  CB  . LEU B 1 112 ? 103.693 68.956  54.192  1.00 25.39 ? 109 LEU B CB  1 
ATOM   2273 C  CG  . LEU B 1 112 ? 102.535 67.997  53.942  1.00 25.58 ? 109 LEU B CG  1 
ATOM   2274 C  CD1 . LEU B 1 112 ? 102.379 67.104  55.157  1.00 24.84 ? 109 LEU B CD1 1 
ATOM   2275 C  CD2 . LEU B 1 112 ? 101.209 68.669  53.606  1.00 24.55 ? 109 LEU B CD2 1 
ATOM   2276 N  N   . THR B 1 113 ? 106.316 70.746  53.547  1.00 26.94 ? 110 THR B N   1 
ATOM   2277 C  CA  . THR B 1 113 ? 107.328 71.692  53.946  1.00 27.15 ? 110 THR B CA  1 
ATOM   2278 C  C   . THR B 1 113 ? 107.296 72.874  53.022  1.00 28.53 ? 110 THR B C   1 
ATOM   2279 O  O   . THR B 1 113 ? 107.401 74.014  53.454  1.00 28.14 ? 110 THR B O   1 
ATOM   2280 C  CB  . THR B 1 113 ? 108.708 71.018  53.840  1.00 26.83 ? 110 THR B CB  1 
ATOM   2281 O  OG1 . THR B 1 113 ? 108.767 69.987  54.814  1.00 27.30 ? 110 THR B OG1 1 
ATOM   2282 C  CG2 . THR B 1 113 ? 109.876 71.992  54.057  1.00 25.19 ? 110 THR B CG2 1 
HETATM 2283 N  N   . MSE B 1 114 ? 107.181 72.565  51.734  1.00 29.19 ? 111 MSE B N   1 
HETATM 2284 C  CA  . MSE B 1 114 ? 107.157 73.529  50.687  1.00 31.73 ? 111 MSE B CA  1 
HETATM 2285 C  C   . MSE B 1 114 ? 105.877 74.388  50.789  1.00 29.80 ? 111 MSE B C   1 
HETATM 2286 O  O   . MSE B 1 114 ? 105.947 75.615  50.754  1.00 30.00 ? 111 MSE B O   1 
HETATM 2287 C  CB  . MSE B 1 114 ? 107.253 72.758  49.386  1.00 30.27 ? 111 MSE B CB  1 
HETATM 2288 C  CG  . MSE B 1 114 ? 107.656 73.522  48.197  1.00 33.57 ? 111 MSE B CG  1 
HETATM 2289 SE SE  . MSE B 1 114 ? 107.729 72.291  46.608  1.00 42.87 ? 111 MSE B SE  1 
HETATM 2290 C  CE  . MSE B 1 114 ? 105.789 71.661  46.487  1.00 34.11 ? 111 MSE B CE  1 
ATOM   2291 N  N   . LEU B 1 115 ? 104.723 73.751  50.951  1.00 28.75 ? 112 LEU B N   1 
ATOM   2292 C  CA  . LEU B 1 115 ? 103.470 74.468  51.123  1.00 28.42 ? 112 LEU B CA  1 
ATOM   2293 C  C   . LEU B 1 115 ? 103.395 75.337  52.389  1.00 29.05 ? 112 LEU B C   1 
ATOM   2294 O  O   . LEU B 1 115 ? 102.884 76.446  52.340  1.00 28.91 ? 112 LEU B O   1 
ATOM   2295 C  CB  . LEU B 1 115 ? 102.299 73.485  51.128  1.00 28.13 ? 112 LEU B CB  1 
ATOM   2296 C  CG  . LEU B 1 115 ? 102.117 72.643  49.882  1.00 26.05 ? 112 LEU B CG  1 
ATOM   2297 C  CD1 . LEU B 1 115 ? 101.305 71.371  50.238  1.00 24.56 ? 112 LEU B CD1 1 
ATOM   2298 C  CD2 . LEU B 1 115 ? 101.481 73.469  48.747  1.00 24.70 ? 112 LEU B CD2 1 
HETATM 2299 N  N   . MSE B 1 116 ? 103.893 74.837  53.516  1.00 29.41 ? 113 MSE B N   1 
HETATM 2300 C  CA  . MSE B 1 116 ? 104.009 75.633  54.740  1.00 31.90 ? 113 MSE B CA  1 
HETATM 2301 C  C   . MSE B 1 116 ? 104.862 76.875  54.566  1.00 28.49 ? 113 MSE B C   1 
HETATM 2302 O  O   . MSE B 1 116 ? 104.614 77.898  55.206  1.00 27.38 ? 113 MSE B O   1 
HETATM 2303 C  CB  . MSE B 1 116 ? 104.542 74.798  55.905  1.00 30.21 ? 113 MSE B CB  1 
HETATM 2304 C  CG  . MSE B 1 116 ? 103.525 73.838  56.457  1.00 33.07 ? 113 MSE B CG  1 
HETATM 2305 SE SE  . MSE B 1 116 ? 104.145 73.011  58.147  1.00 46.24 ? 113 MSE B SE  1 
HETATM 2306 C  CE  . MSE B 1 116 ? 105.071 71.323  57.391  1.00 37.23 ? 113 MSE B CE  1 
ATOM   2307 N  N   . ASN B 1 117 ? 105.847 76.788  53.680  1.00 27.02 ? 114 ASN B N   1 
ATOM   2308 C  CA  . ASN B 1 117 ? 106.732 77.906  53.441  1.00 26.82 ? 114 ASN B CA  1 
ATOM   2309 C  C   . ASN B 1 117 ? 105.993 79.115  52.882  1.00 26.03 ? 114 ASN B C   1 
ATOM   2310 O  O   . ASN B 1 117 ? 106.416 80.257  53.090  1.00 25.67 ? 114 ASN B O   1 
ATOM   2311 C  CB  . ASN B 1 117 ? 107.859 77.499  52.496  1.00 27.59 ? 114 ASN B CB  1 
ATOM   2312 C  CG  . ASN B 1 117 ? 109.181 78.218  52.801  1.00 28.24 ? 114 ASN B CG  1 
ATOM   2313 O  OD1 . ASN B 1 117 ? 109.432 79.323  52.305  1.00 29.13 ? 114 ASN B OD1 1 
ATOM   2314 N  ND2 . ASN B 1 117 ? 110.043 77.569  53.584  1.00 28.02 ? 114 ASN B ND2 1 
ATOM   2315 N  N   . PHE B 1 118 ? 104.902 78.843  52.170  1.00 25.48 ? 115 PHE B N   1 
ATOM   2316 C  CA  . PHE B 1 118 ? 104.013 79.866  51.616  1.00 25.63 ? 115 PHE B CA  1 
ATOM   2317 C  C   . PHE B 1 118 ? 102.970 80.410  52.606  1.00 25.30 ? 115 PHE B C   1 
ATOM   2318 O  O   . PHE B 1 118 ? 102.201 81.285  52.265  1.00 25.81 ? 115 PHE B O   1 
ATOM   2319 C  CB  . PHE B 1 118 ? 103.326 79.321  50.365  1.00 25.39 ? 115 PHE B CB  1 
ATOM   2320 C  CG  . PHE B 1 118 ? 104.177 79.439  49.111  1.00 28.65 ? 115 PHE B CG  1 
ATOM   2321 C  CD1 . PHE B 1 118 ? 105.131 78.449  48.789  1.00 28.37 ? 115 PHE B CD1 1 
ATOM   2322 C  CD2 . PHE B 1 118 ? 104.056 80.566  48.256  1.00 27.96 ? 115 PHE B CD2 1 
ATOM   2323 C  CE1 . PHE B 1 118 ? 105.939 78.579  47.619  1.00 28.44 ? 115 PHE B CE1 1 
ATOM   2324 C  CE2 . PHE B 1 118 ? 104.858 80.688  47.093  1.00 26.32 ? 115 PHE B CE2 1 
ATOM   2325 C  CZ  . PHE B 1 118 ? 105.777 79.687  46.775  1.00 26.21 ? 115 PHE B CZ  1 
ATOM   2326 N  N   . GLY B 1 119 ? 102.946 79.890  53.826  1.00 24.69 ? 116 GLY B N   1 
ATOM   2327 C  CA  . GLY B 1 119 ? 101.967 80.306  54.805  1.00 24.61 ? 116 GLY B CA  1 
ATOM   2328 C  C   . GLY B 1 119 ? 100.646 79.574  54.683  1.00 24.90 ? 116 GLY B C   1 
ATOM   2329 O  O   . GLY B 1 119 ? 99.649  79.986  55.295  1.00 25.09 ? 116 GLY B O   1 
ATOM   2330 N  N   . PHE B 1 120 ? 100.623 78.497  53.895  1.00 24.01 ? 117 PHE B N   1 
ATOM   2331 C  CA  . PHE B 1 120 ? 99.459  77.648  53.818  1.00 23.83 ? 117 PHE B CA  1 
ATOM   2332 C  C   . PHE B 1 120 ? 99.236  76.888  55.140  1.00 24.46 ? 117 PHE B C   1 
ATOM   2333 O  O   . PHE B 1 120 ? 100.187 76.612  55.902  1.00 22.90 ? 117 PHE B O   1 
ATOM   2334 C  CB  . PHE B 1 120 ? 99.591  76.638  52.667  1.00 24.37 ? 117 PHE B CB  1 
ATOM   2335 C  CG  . PHE B 1 120 ? 99.724  77.259  51.293  1.00 23.92 ? 117 PHE B CG  1 
ATOM   2336 C  CD1 . PHE B 1 120 ? 99.620  78.637  51.096  1.00 23.17 ? 117 PHE B CD1 1 
ATOM   2337 C  CD2 . PHE B 1 120 ? 99.922  76.448  50.191  1.00 25.24 ? 117 PHE B CD2 1 
ATOM   2338 C  CE1 . PHE B 1 120 ? 99.743  79.197  49.815  1.00 25.52 ? 117 PHE B CE1 1 
ATOM   2339 C  CE2 . PHE B 1 120 ? 100.030 77.000  48.892  1.00 26.95 ? 117 PHE B CE2 1 
ATOM   2340 C  CZ  . PHE B 1 120 ? 99.939  78.386  48.714  1.00 25.75 ? 117 PHE B CZ  1 
ATOM   2341 N  N   . LEU B 1 121 ? 97.964  76.579  55.400  1.00 25.09 ? 118 LEU B N   1 
ATOM   2342 C  CA  . LEU B 1 121 ? 97.545  75.718  56.502  1.00 25.94 ? 118 LEU B CA  1 
ATOM   2343 C  C   . LEU B 1 121 ? 97.456  74.380  55.868  1.00 25.41 ? 118 LEU B C   1 
ATOM   2344 O  O   . LEU B 1 121 ? 96.854  74.232  54.834  1.00 26.70 ? 118 LEU B O   1 
ATOM   2345 C  CB  . LEU B 1 121 ? 96.169  76.085  57.023  1.00 26.15 ? 118 LEU B CB  1 
ATOM   2346 C  CG  . LEU B 1 121 ? 95.874  77.436  57.692  1.00 28.32 ? 118 LEU B CG  1 
ATOM   2347 C  CD1 . LEU B 1 121 ? 95.691  77.245  59.170  1.00 29.14 ? 118 LEU B CD1 1 
ATOM   2348 C  CD2 . LEU B 1 121 ? 96.897  78.536  57.396  1.00 27.86 ? 118 LEU B CD2 1 
ATOM   2349 N  N   . VAL B 1 122 ? 98.043  73.391  56.502  1.00 25.51 ? 119 VAL B N   1 
ATOM   2350 C  CA  . VAL B 1 122 ? 98.412  72.160  55.826  1.00 24.22 ? 119 VAL B CA  1 
ATOM   2351 C  C   . VAL B 1 122 ? 97.891  71.027  56.700  1.00 24.83 ? 119 VAL B C   1 
ATOM   2352 O  O   . VAL B 1 122 ? 97.855  71.147  57.932  1.00 23.87 ? 119 VAL B O   1 
ATOM   2353 C  CB  . VAL B 1 122 ? 99.997  72.253  55.668  1.00 25.22 ? 119 VAL B CB  1 
ATOM   2354 C  CG1 . VAL B 1 122 ? 100.833 71.175  56.418  1.00 20.52 ? 119 VAL B CG1 1 
ATOM   2355 C  CG2 . VAL B 1 122 ? 100.398 72.606  54.231  1.00 20.41 ? 119 VAL B CG2 1 
ATOM   2356 N  N   . PHE B 1 123 ? 97.464  69.935  56.089  1.00 24.55 ? 120 PHE B N   1 
ATOM   2357 C  CA  . PHE B 1 123 ? 96.909  68.844  56.884  1.00 24.95 ? 120 PHE B CA  1 
ATOM   2358 C  C   . PHE B 1 123 ? 97.156  67.479  56.227  1.00 25.41 ? 120 PHE B C   1 
ATOM   2359 O  O   . PHE B 1 123 ? 97.474  67.403  55.023  1.00 25.18 ? 120 PHE B O   1 
ATOM   2360 C  CB  . PHE B 1 123 ? 95.399  69.056  57.075  1.00 23.62 ? 120 PHE B CB  1 
ATOM   2361 C  CG  . PHE B 1 123 ? 94.636  68.906  55.803  1.00 22.58 ? 120 PHE B CG  1 
ATOM   2362 C  CD1 . PHE B 1 123 ? 94.559  69.965  54.900  1.00 20.13 ? 120 PHE B CD1 1 
ATOM   2363 C  CD2 . PHE B 1 123 ? 94.031  67.688  55.476  1.00 20.69 ? 120 PHE B CD2 1 
ATOM   2364 C  CE1 . PHE B 1 123 ? 93.905  69.824  53.692  1.00 18.38 ? 120 PHE B CE1 1 
ATOM   2365 C  CE2 . PHE B 1 123 ? 93.356  67.543  54.294  1.00 19.52 ? 120 PHE B CE2 1 
ATOM   2366 C  CZ  . PHE B 1 123 ? 93.299  68.615  53.379  1.00 21.18 ? 120 PHE B CZ  1 
ATOM   2367 N  N   . GLY B 1 124 ? 96.995  66.414  57.024  1.00 25.91 ? 121 GLY B N   1 
ATOM   2368 C  CA  . GLY B 1 124 ? 96.736  65.032  56.485  1.00 25.89 ? 121 GLY B CA  1 
ATOM   2369 C  C   . GLY B 1 124 ? 95.398  64.487  57.009  1.00 26.09 ? 121 GLY B C   1 
ATOM   2370 O  O   . GLY B 1 124 ? 94.628  65.212  57.643  1.00 26.08 ? 121 GLY B O   1 
ATOM   2371 N  N   . VAL B 1 125 ? 95.129  63.206  56.782  1.00 26.37 ? 122 VAL B N   1 
ATOM   2372 C  CA  . VAL B 1 125 ? 93.835  62.595  57.124  1.00 25.56 ? 122 VAL B CA  1 
ATOM   2373 C  C   . VAL B 1 125 ? 93.965  61.400  58.078  1.00 25.58 ? 122 VAL B C   1 
ATOM   2374 O  O   . VAL B 1 125 ? 94.764  60.456  57.864  1.00 24.95 ? 122 VAL B O   1 
ATOM   2375 C  CB  . VAL B 1 125 ? 93.047  62.220  55.824  1.00 26.36 ? 122 VAL B CB  1 
ATOM   2376 C  CG1 . VAL B 1 125 ? 91.693  61.538  56.112  1.00 24.81 ? 122 VAL B CG1 1 
ATOM   2377 C  CG2 . VAL B 1 125 ? 92.853  63.462  54.965  1.00 24.45 ? 122 VAL B CG2 1 
ATOM   2378 N  N   . THR B 1 126 ? 93.175  61.480  59.150  1.00 25.48 ? 123 THR B N   1 
ATOM   2379 C  CA  . THR B 1 126 ? 93.122  60.458  60.193  1.00 25.81 ? 123 THR B CA  1 
ATOM   2380 C  C   . THR B 1 126 ? 92.431  59.177  59.722  1.00 25.53 ? 123 THR B C   1 
ATOM   2381 O  O   . THR B 1 126 ? 92.843  58.076  60.115  1.00 25.23 ? 123 THR B O   1 
ATOM   2382 C  CB  . THR B 1 126 ? 92.372  60.965  61.439  1.00 26.00 ? 123 THR B CB  1 
ATOM   2383 O  OG1 . THR B 1 126 ? 91.153  61.614  61.038  1.00 27.22 ? 123 THR B OG1 1 
ATOM   2384 C  CG2 . THR B 1 126 ? 93.222  61.920  62.228  1.00 25.77 ? 123 THR B CG2 1 
ATOM   2385 N  N   . ASP B 1 127 ? 91.396  59.358  58.890  1.00 25.14 ? 124 ASP B N   1 
ATOM   2386 C  CA  . ASP B 1 127 ? 90.515  58.312  58.376  1.00 25.66 ? 124 ASP B CA  1 
ATOM   2387 C  C   . ASP B 1 127 ? 91.249  57.055  57.989  1.00 25.96 ? 124 ASP B C   1 
ATOM   2388 O  O   . ASP B 1 127 ? 92.242  57.115  57.255  1.00 26.41 ? 124 ASP B O   1 
ATOM   2389 C  CB  . ASP B 1 127 ? 89.740  58.781  57.130  1.00 25.51 ? 124 ASP B CB  1 
ATOM   2390 C  CG  . ASP B 1 127 ? 88.757  59.920  57.412  1.00 26.88 ? 124 ASP B CG  1 
ATOM   2391 O  OD1 . ASP B 1 127 ? 88.924  60.604  58.433  1.00 26.53 ? 124 ASP B OD1 1 
ATOM   2392 O  OD2 . ASP B 1 127 ? 87.832  60.165  56.572  1.00 27.70 ? 124 ASP B OD2 1 
ATOM   2393 N  N   . TYR B 1 128 ? 90.750  55.923  58.475  1.00 26.04 ? 125 TYR B N   1 
ATOM   2394 C  CA  . TYR B 1 128 ? 91.182  54.628  57.974  1.00 26.81 ? 125 TYR B CA  1 
ATOM   2395 C  C   . TYR B 1 128 ? 90.195  54.155  56.929  1.00 27.26 ? 125 TYR B C   1 
ATOM   2396 O  O   . TYR B 1 128 ? 88.998  54.034  57.168  1.00 27.88 ? 125 TYR B O   1 
ATOM   2397 C  CB  . TYR B 1 128 ? 91.249  53.594  59.071  1.00 26.35 ? 125 TYR B CB  1 
ATOM   2398 C  CG  . TYR B 1 128 ? 92.561  53.529  59.741  1.00 26.99 ? 125 TYR B CG  1 
ATOM   2399 C  CD1 . TYR B 1 128 ? 93.092  54.648  60.411  1.00 27.10 ? 125 TYR B CD1 1 
ATOM   2400 C  CD2 . TYR B 1 128 ? 93.296  52.352  59.716  1.00 26.81 ? 125 TYR B CD2 1 
ATOM   2401 C  CE1 . TYR B 1 128 ? 94.331  54.581  61.050  1.00 26.67 ? 125 TYR B CE1 1 
ATOM   2402 C  CE2 . TYR B 1 128 ? 94.523  52.261  60.357  1.00 27.25 ? 125 TYR B CE2 1 
ATOM   2403 C  CZ  . TYR B 1 128 ? 95.035  53.370  61.019  1.00 26.72 ? 125 TYR B CZ  1 
ATOM   2404 O  OH  . TYR B 1 128 ? 96.245  53.247  61.640  1.00 27.34 ? 125 TYR B OH  1 
ATOM   2405 N  N   . VAL B 1 129 ? 90.748  53.804  55.795  1.00 27.51 ? 126 VAL B N   1 
ATOM   2406 C  CA  . VAL B 1 129 ? 90.022  53.658  54.563  1.00 27.38 ? 126 VAL B CA  1 
ATOM   2407 C  C   . VAL B 1 129 ? 90.019  52.157  54.273  1.00 27.84 ? 126 VAL B C   1 
ATOM   2408 O  O   . VAL B 1 129 ? 89.155  51.644  53.577  1.00 28.89 ? 126 VAL B O   1 
ATOM   2409 C  CB  . VAL B 1 129 ? 90.732  54.609  53.557  1.00 26.96 ? 126 VAL B CB  1 
ATOM   2410 C  CG1 . VAL B 1 129 ? 91.483  53.910  52.456  1.00 26.26 ? 126 VAL B CG1 1 
ATOM   2411 C  CG2 . VAL B 1 129 ? 89.828  55.798  53.158  1.00 26.86 ? 126 VAL B CG2 1 
ATOM   2412 N  N   . GLY B 1 130 ? 90.972  51.461  54.875  1.00 28.14 ? 127 GLY B N   1 
ATOM   2413 C  CA  . GLY B 1 130 ? 90.966  50.014  55.015  1.00 29.49 ? 127 GLY B CA  1 
ATOM   2414 C  C   . GLY B 1 130 ? 91.379  49.757  56.455  1.00 30.75 ? 127 GLY B C   1 
ATOM   2415 O  O   . GLY B 1 130 ? 91.727  50.695  57.178  1.00 31.92 ? 127 GLY B O   1 
ATOM   2416 N  N   . LYS B 1 131 ? 91.369  48.503  56.885  1.00 31.38 ? 128 LYS B N   1 
ATOM   2417 C  CA  . LYS B 1 131 ? 91.692  48.195  58.265  1.00 31.89 ? 128 LYS B CA  1 
ATOM   2418 C  C   . LYS B 1 131 ? 93.144  48.485  58.650  1.00 31.17 ? 128 LYS B C   1 
ATOM   2419 O  O   . LYS B 1 131 ? 93.423  48.772  59.811  1.00 31.45 ? 128 LYS B O   1 
ATOM   2420 C  CB  . LYS B 1 131 ? 91.261  46.762  58.647  1.00 33.16 ? 128 LYS B CB  1 
ATOM   2421 C  CG  . LYS B 1 131 ? 91.951  45.622  57.897  1.00 35.29 ? 128 LYS B CG  1 
ATOM   2422 C  CD  . LYS B 1 131 ? 92.989  44.862  58.761  1.00 38.61 ? 128 LYS B CD  1 
ATOM   2423 C  CE  . LYS B 1 131 ? 93.496  43.562  58.047  1.00 38.56 ? 128 LYS B CE  1 
ATOM   2424 N  NZ  . LYS B 1 131 ? 94.206  43.796  56.723  1.00 40.07 ? 128 LYS B NZ  1 
ATOM   2425 N  N   . LYS B 1 132 ? 94.048  48.406  57.679  1.00 30.19 ? 129 LYS B N   1 
ATOM   2426 C  CA  . LYS B 1 132 ? 95.460  48.737  57.859  1.00 29.40 ? 129 LYS B CA  1 
ATOM   2427 C  C   . LYS B 1 132 ? 95.860  49.749  56.791  1.00 27.86 ? 129 LYS B C   1 
ATOM   2428 O  O   . LYS B 1 132 ? 96.969  49.684  56.262  1.00 26.65 ? 129 LYS B O   1 
ATOM   2429 C  CB  . LYS B 1 132 ? 96.336  47.500  57.643  1.00 29.42 ? 129 LYS B CB  1 
ATOM   2430 C  CG  . LYS B 1 132 ? 96.330  46.478  58.730  1.00 31.26 ? 129 LYS B CG  1 
ATOM   2431 C  CD  . LYS B 1 132 ? 97.018  45.180  58.230  1.00 32.14 ? 129 LYS B CD  1 
ATOM   2432 C  CE  . LYS B 1 132 ? 97.420  44.254  59.401  1.00 34.85 ? 129 LYS B CE  1 
ATOM   2433 N  NZ  . LYS B 1 132 ? 96.274  43.660  60.174  1.00 34.02 ? 129 LYS B NZ  1 
ATOM   2434 N  N   . PHE B 1 133 ? 94.953  50.661  56.444  1.00 27.03 ? 130 PHE B N   1 
ATOM   2435 C  CA  . PHE B 1 133 ? 95.240  51.614  55.376  1.00 26.87 ? 130 PHE B CA  1 
ATOM   2436 C  C   . PHE B 1 133 ? 94.703  53.036  55.605  1.00 26.60 ? 130 PHE B C   1 
ATOM   2437 O  O   . PHE B 1 133 ? 93.482  53.275  55.680  1.00 25.41 ? 130 PHE B O   1 
ATOM   2438 C  CB  . PHE B 1 133 ? 94.756  51.070  54.022  1.00 26.80 ? 130 PHE B CB  1 
ATOM   2439 C  CG  . PHE B 1 133 ? 95.527  51.597  52.851  1.00 26.46 ? 130 PHE B CG  1 
ATOM   2440 C  CD1 . PHE B 1 133 ? 95.150  52.774  52.223  1.00 25.45 ? 130 PHE B CD1 1 
ATOM   2441 C  CD2 . PHE B 1 133 ? 96.624  50.902  52.360  1.00 27.60 ? 130 PHE B CD2 1 
ATOM   2442 C  CE1 . PHE B 1 133 ? 95.859  53.259  51.130  1.00 23.61 ? 130 PHE B CE1 1 
ATOM   2443 C  CE2 . PHE B 1 133 ? 97.331  51.380  51.273  1.00 25.69 ? 130 PHE B CE2 1 
ATOM   2444 C  CZ  . PHE B 1 133 ? 96.943  52.561  50.661  1.00 25.72 ? 130 PHE B CZ  1 
ATOM   2445 N  N   . THR B 1 134 ? 95.650  53.975  55.662  1.00 26.71 ? 131 THR B N   1 
ATOM   2446 C  CA  . THR B 1 134 ? 95.341  55.356  56.012  1.00 26.27 ? 131 THR B CA  1 
ATOM   2447 C  C   . THR B 1 134 ? 96.134  56.388  55.204  1.00 26.60 ? 131 THR B C   1 
ATOM   2448 O  O   . THR B 1 134 ? 96.714  56.046  54.158  1.00 26.45 ? 131 THR B O   1 
ATOM   2449 C  CB  . THR B 1 134 ? 95.388  55.577  57.528  1.00 25.51 ? 131 THR B CB  1 
ATOM   2450 O  OG1 . THR B 1 134 ? 94.819  56.847  57.845  1.00 25.44 ? 131 THR B OG1 1 
ATOM   2451 C  CG2 . THR B 1 134 ? 96.784  55.441  58.076  1.00 24.63 ? 131 THR B CG2 1 
ATOM   2452 N  N   . LEU B 1 135 ? 96.089  57.646  55.648  1.00 26.33 ? 132 LEU B N   1 
ATOM   2453 C  CA  . LEU B 1 135 ? 96.673  58.753  54.902  1.00 26.70 ? 132 LEU B CA  1 
ATOM   2454 C  C   . LEU B 1 135 ? 97.031  59.987  55.755  1.00 27.05 ? 132 LEU B C   1 
ATOM   2455 O  O   . LEU B 1 135 ? 96.705  61.124  55.382  1.00 26.80 ? 132 LEU B O   1 
ATOM   2456 C  CB  . LEU B 1 135 ? 95.829  59.094  53.663  1.00 26.33 ? 132 LEU B CB  1 
ATOM   2457 C  CG  . LEU B 1 135 ? 94.299  59.194  53.365  1.00 27.64 ? 132 LEU B CG  1 
ATOM   2458 C  CD1 . LEU B 1 135 ? 93.286  58.325  54.166  1.00 27.02 ? 132 LEU B CD1 1 
ATOM   2459 C  CD2 . LEU B 1 135 ? 93.852  60.632  53.317  1.00 25.01 ? 132 LEU B CD2 1 
ATOM   2460 N  N   . HIS B 1 136 ? 97.753  59.744  56.861  1.00 26.15 ? 133 HIS B N   1 
ATOM   2461 C  CA  . HIS B 1 136 ? 98.011  60.758  57.882  1.00 26.24 ? 133 HIS B CA  1 
ATOM   2462 C  C   . HIS B 1 136 ? 98.787  61.996  57.410  1.00 26.83 ? 133 HIS B C   1 
ATOM   2463 O  O   . HIS B 1 136 ? 98.686  63.058  58.036  1.00 27.64 ? 133 HIS B O   1 
ATOM   2464 C  CB  . HIS B 1 136 ? 98.677  60.150  59.154  1.00 25.36 ? 133 HIS B CB  1 
ATOM   2465 C  CG  . HIS B 1 136 ? 97.844  59.118  59.875  1.00 26.15 ? 133 HIS B CG  1 
ATOM   2466 N  ND1 . HIS B 1 136 ? 96.477  58.974  59.694  1.00 24.07 ? 133 HIS B ND1 1 
ATOM   2467 C  CD2 . HIS B 1 136 ? 98.195  58.187  60.803  1.00 26.90 ? 133 HIS B CD2 1 
ATOM   2468 C  CE1 . HIS B 1 136 ? 96.030  58.004  60.474  1.00 23.92 ? 133 HIS B CE1 1 
ATOM   2469 N  NE2 . HIS B 1 136 ? 97.049  57.513  61.162  1.00 24.34 ? 133 HIS B NE2 1 
ATOM   2470 N  N   . TYR B 1 137 ? 99.584  61.860  56.352  1.00 26.81 ? 134 TYR B N   1 
ATOM   2471 C  CA  . TYR B 1 137 ? 100.466 62.941  55.894  1.00 26.76 ? 134 TYR B CA  1 
ATOM   2472 C  C   . TYR B 1 137 ? 100.189 63.236  54.443  1.00 26.64 ? 134 TYR B C   1 
ATOM   2473 O  O   . TYR B 1 137 ? 100.818 64.087  53.821  1.00 26.45 ? 134 TYR B O   1 
ATOM   2474 C  CB  . TYR B 1 137 ? 101.961 62.621  56.195  1.00 26.85 ? 134 TYR B CB  1 
ATOM   2475 C  CG  . TYR B 1 137 ? 102.146 62.462  57.710  1.00 27.35 ? 134 TYR B CG  1 
ATOM   2476 C  CD1 . TYR B 1 137 ? 102.286 61.201  58.299  1.00 25.59 ? 134 TYR B CD1 1 
ATOM   2477 C  CD2 . TYR B 1 137 ? 102.061 63.563  58.549  1.00 27.29 ? 134 TYR B CD2 1 
ATOM   2478 C  CE1 . TYR B 1 137 ? 102.397 61.062  59.706  1.00 24.03 ? 134 TYR B CE1 1 
ATOM   2479 C  CE2 . TYR B 1 137 ? 102.170 63.430  59.961  1.00 27.87 ? 134 TYR B CE2 1 
ATOM   2480 C  CZ  . TYR B 1 137 ? 102.334 62.170  60.512  1.00 25.67 ? 134 TYR B CZ  1 
ATOM   2481 O  OH  . TYR B 1 137 ? 102.420 62.040  61.873  1.00 27.52 ? 134 TYR B OH  1 
ATOM   2482 N  N   . GLY B 1 138 ? 99.197  62.520  53.930  1.00 27.05 ? 135 GLY B N   1 
ATOM   2483 C  CA  . GLY B 1 138 ? 98.774  62.616  52.560  1.00 26.58 ? 135 GLY B CA  1 
ATOM   2484 C  C   . GLY B 1 138 ? 98.504  61.232  52.035  1.00 26.38 ? 135 GLY B C   1 
ATOM   2485 O  O   . GLY B 1 138 ? 98.871  60.242  52.673  1.00 27.28 ? 135 GLY B O   1 
ATOM   2486 N  N   . ALA B 1 139 ? 97.828  61.168  50.891  1.00 26.00 ? 136 ALA B N   1 
ATOM   2487 C  CA  . ALA B 1 139 ? 97.564  59.903  50.211  1.00 25.29 ? 136 ALA B CA  1 
ATOM   2488 C  C   . ALA B 1 139 ? 98.865  59.336  49.623  1.00 24.79 ? 136 ALA B C   1 
ATOM   2489 O  O   . ALA B 1 139 ? 99.566  59.997  48.899  1.00 24.92 ? 136 ALA B O   1 
ATOM   2490 C  CB  . ALA B 1 139 ? 96.520  60.101  49.141  1.00 23.49 ? 136 ALA B CB  1 
ATOM   2491 N  N   . VAL B 1 140 ? 99.170  58.089  49.936  1.00 25.44 ? 137 VAL B N   1 
ATOM   2492 C  CA  . VAL B 1 140 ? 100.372 57.434  49.450  1.00 25.00 ? 137 VAL B CA  1 
ATOM   2493 C  C   . VAL B 1 140 ? 99.997  56.048  48.893  1.00 26.41 ? 137 VAL B C   1 
ATOM   2494 O  O   . VAL B 1 140 ? 99.133  55.335  49.443  1.00 27.10 ? 137 VAL B O   1 
ATOM   2495 C  CB  . VAL B 1 140 ? 101.443 57.320  50.590  1.00 25.19 ? 137 VAL B CB  1 
ATOM   2496 C  CG1 . VAL B 1 140 ? 101.963 58.706  51.010  1.00 22.08 ? 137 VAL B CG1 1 
ATOM   2497 C  CG2 . VAL B 1 140 ? 100.869 56.582  51.792  1.00 23.99 ? 137 VAL B CG2 1 
ATOM   2498 N  N   . VAL B 1 141 ? 100.649 55.667  47.804  1.00 26.57 ? 138 VAL B N   1 
ATOM   2499 C  CA  . VAL B 1 141 ? 100.448 54.369  47.178  1.00 26.85 ? 138 VAL B CA  1 
ATOM   2500 C  C   . VAL B 1 141 ? 101.817 53.924  46.659  1.00 27.22 ? 138 VAL B C   1 
ATOM   2501 O  O   . VAL B 1 141 ? 102.666 54.757  46.422  1.00 27.87 ? 138 VAL B O   1 
ATOM   2502 C  CB  . VAL B 1 141 ? 99.434  54.475  45.987  1.00 27.32 ? 138 VAL B CB  1 
ATOM   2503 C  CG1 . VAL B 1 141 ? 99.290  53.142  45.302  1.00 26.67 ? 138 VAL B CG1 1 
ATOM   2504 C  CG2 . VAL B 1 141 ? 98.039  54.984  46.472  1.00 27.82 ? 138 VAL B CG2 1 
ATOM   2505 N  N   . ALA B 1 142 ? 102.055 52.625  46.511  1.00 27.40 ? 139 ALA B N   1 
ATOM   2506 C  CA  . ALA B 1 142 ? 103.211 52.168  45.759  1.00 27.81 ? 139 ALA B CA  1 
ATOM   2507 C  C   . ALA B 1 142 ? 102.701 51.832  44.371  1.00 28.72 ? 139 ALA B C   1 
ATOM   2508 O  O   . ALA B 1 142 ? 101.804 50.979  44.223  1.00 29.04 ? 139 ALA B O   1 
ATOM   2509 C  CB  . ALA B 1 142 ? 103.844 50.946  46.389  1.00 27.61 ? 139 ALA B CB  1 
ATOM   2510 N  N   . GLY B 1 143 ? 103.266 52.501  43.362  1.00 28.93 ? 140 GLY B N   1 
ATOM   2511 C  CA  . GLY B 1 143 ? 102.834 52.331  41.986  1.00 29.25 ? 140 GLY B CA  1 
ATOM   2512 C  C   . GLY B 1 143 ? 101.477 52.959  41.727  1.00 30.07 ? 140 GLY B C   1 
ATOM   2513 O  O   . GLY B 1 143 ? 101.148 54.029  42.251  1.00 29.29 ? 140 GLY B O   1 
ATOM   2514 N  N   . GLU B 1 144 ? 100.691 52.276  40.906  1.00 31.13 ? 141 GLU B N   1 
ATOM   2515 C  CA  . GLU B 1 144 ? 99.364  52.732  40.525  1.00 33.03 ? 141 GLU B CA  1 
ATOM   2516 C  C   . GLU B 1 144 ? 98.351  52.363  41.614  1.00 32.81 ? 141 GLU B C   1 
ATOM   2517 O  O   . GLU B 1 144 ? 98.394  51.245  42.130  1.00 33.04 ? 141 GLU B O   1 
ATOM   2518 C  CB  . GLU B 1 144 ? 99.000  52.114  39.168  1.00 32.56 ? 141 GLU B CB  1 
ATOM   2519 C  CG  . GLU B 1 144 ? 97.601  52.394  38.645  1.00 33.98 ? 141 GLU B CG  1 
ATOM   2520 C  CD  . GLU B 1 144 ? 97.424  51.928  37.189  1.00 35.70 ? 141 GLU B CD  1 
ATOM   2521 O  OE1 . GLU B 1 144 ? 98.396  51.370  36.603  1.00 36.89 ? 141 GLU B OE1 1 
ATOM   2522 O  OE2 . GLU B 1 144 ? 96.318  52.130  36.618  1.00 39.11 ? 141 GLU B OE2 1 
ATOM   2523 N  N   . PRO B 1 145 ? 97.453  53.308  41.977  1.00 33.21 ? 142 PRO B N   1 
ATOM   2524 C  CA  . PRO B 1 145 ? 96.347  52.988  42.892  1.00 33.72 ? 142 PRO B CA  1 
ATOM   2525 C  C   . PRO B 1 145 ? 95.383  51.994  42.237  1.00 34.51 ? 142 PRO B C   1 
ATOM   2526 O  O   . PRO B 1 145 ? 94.613  52.356  41.333  1.00 34.74 ? 142 PRO B O   1 
ATOM   2527 C  CB  . PRO B 1 145 ? 95.667  54.349  43.134  1.00 33.16 ? 142 PRO B CB  1 
ATOM   2528 C  CG  . PRO B 1 145 ? 96.004  55.155  41.959  1.00 32.51 ? 142 PRO B CG  1 
ATOM   2529 C  CD  . PRO B 1 145 ? 97.402  54.716  41.542  1.00 33.15 ? 142 PRO B CD  1 
ATOM   2530 N  N   . ARG B 1 146 ? 95.458  50.740  42.668  1.00 35.24 ? 143 ARG B N   1 
ATOM   2531 C  CA  . ARG B 1 146 ? 94.662  49.689  42.051  1.00 36.45 ? 143 ARG B CA  1 
ATOM   2532 C  C   . ARG B 1 146 ? 93.636  49.076  42.999  1.00 35.54 ? 143 ARG B C   1 
ATOM   2533 O  O   . ARG B 1 146 ? 92.511  48.840  42.591  1.00 35.49 ? 143 ARG B O   1 
ATOM   2534 C  CB  . ARG B 1 146 ? 95.553  48.637  41.386  1.00 36.09 ? 143 ARG B CB  1 
ATOM   2535 C  CG  . ARG B 1 146 ? 96.184  49.147  40.085  1.00 38.58 ? 143 ARG B CG  1 
ATOM   2536 C  CD  . ARG B 1 146 ? 96.882  48.036  39.289  1.00 39.74 ? 143 ARG B CD  1 
ATOM   2537 N  NE  . ARG B 1 146 ? 98.156  47.628  39.902  1.00 46.79 ? 143 ARG B NE  1 
ATOM   2538 C  CZ  . ARG B 1 146 ? 99.069  46.838  39.323  1.00 48.65 ? 143 ARG B CZ  1 
ATOM   2539 N  NH1 . ARG B 1 146 ? 100.191 46.539  39.976  1.00 49.95 ? 143 ARG B NH1 1 
ATOM   2540 N  NH2 . ARG B 1 146 ? 98.873  46.344  38.098  1.00 48.83 ? 143 ARG B NH2 1 
ATOM   2541 N  N   . SER B 1 147 ? 94.005  48.841  44.258  1.00 35.13 ? 144 SER B N   1 
ATOM   2542 C  CA  . SER B 1 147 ? 93.059  48.281  45.205  1.00 34.28 ? 144 SER B CA  1 
ATOM   2543 C  C   . SER B 1 147 ? 92.040  49.345  45.531  1.00 34.04 ? 144 SER B C   1 
ATOM   2544 O  O   . SER B 1 147 ? 92.237  50.525  45.230  1.00 33.98 ? 144 SER B O   1 
ATOM   2545 C  CB  . SER B 1 147 ? 93.744  47.821  46.472  1.00 34.02 ? 144 SER B CB  1 
ATOM   2546 O  OG  . SER B 1 147 ? 93.915  48.912  47.358  1.00 35.41 ? 144 SER B OG  1 
ATOM   2547 N  N   . GLU B 1 148 ? 90.944  48.913  46.134  1.00 34.01 ? 145 GLU B N   1 
ATOM   2548 C  CA  . GLU B 1 148 ? 89.833  49.778  46.449  1.00 33.75 ? 145 GLU B CA  1 
ATOM   2549 C  C   . GLU B 1 148 ? 90.206  50.712  47.599  1.00 33.08 ? 145 GLU B C   1 
ATOM   2550 O  O   . GLU B 1 148 ? 89.808  51.873  47.605  1.00 32.88 ? 145 GLU B O   1 
ATOM   2551 C  CB  . GLU B 1 148 ? 88.586  48.928  46.738  1.00 34.33 ? 145 GLU B CB  1 
ATOM   2552 C  CG  . GLU B 1 148 ? 87.285  49.726  46.832  1.00 37.04 ? 145 GLU B CG  1 
ATOM   2553 C  CD  . GLU B 1 148 ? 87.169  50.847  45.766  1.00 40.54 ? 145 GLU B CD  1 
ATOM   2554 O  OE1 . GLU B 1 148 ? 87.389  52.039  46.161  1.00 37.66 ? 145 GLU B OE1 1 
ATOM   2555 O  OE2 . GLU B 1 148 ? 86.869  50.513  44.563  1.00 37.29 ? 145 GLU B OE2 1 
ATOM   2556 N  N   . GLU B 1 149 ? 90.987  50.197  48.552  1.00 32.49 ? 146 GLU B N   1 
ATOM   2557 C  CA  . GLU B 1 149 ? 91.686  50.991  49.582  1.00 32.22 ? 146 GLU B CA  1 
ATOM   2558 C  C   . GLU B 1 149 ? 92.550  52.164  49.021  1.00 31.24 ? 146 GLU B C   1 
ATOM   2559 O  O   . GLU B 1 149 ? 92.432  53.311  49.467  1.00 30.40 ? 146 GLU B O   1 
ATOM   2560 C  CB  . GLU B 1 149 ? 92.654  50.096  50.343  1.00 32.19 ? 146 GLU B CB  1 
ATOM   2561 C  CG  . GLU B 1 149 ? 92.111  49.253  51.418  1.00 34.91 ? 146 GLU B CG  1 
ATOM   2562 C  CD  . GLU B 1 149 ? 93.232  48.443  52.064  1.00 37.68 ? 146 GLU B CD  1 
ATOM   2563 O  OE1 . GLU B 1 149 ? 94.246  48.180  51.355  1.00 35.52 ? 146 GLU B OE1 1 
ATOM   2564 O  OE2 . GLU B 1 149 ? 93.113  48.103  53.275  1.00 39.57 ? 146 GLU B OE2 1 
ATOM   2565 N  N   . GLU B 1 150 ? 93.457  51.845  48.092  1.00 29.91 ? 147 GLU B N   1 
ATOM   2566 C  CA  . GLU B 1 150 ? 94.318  52.865  47.478  1.00 29.61 ? 147 GLU B CA  1 
ATOM   2567 C  C   . GLU B 1 150 ? 93.512  53.956  46.765  1.00 28.28 ? 147 GLU B C   1 
ATOM   2568 O  O   . GLU B 1 150 ? 93.714  55.154  46.999  1.00 27.59 ? 147 GLU B O   1 
ATOM   2569 C  CB  . GLU B 1 150 ? 95.337  52.208  46.542  1.00 29.39 ? 147 GLU B CB  1 
ATOM   2570 C  CG  . GLU B 1 150 ? 96.263  51.254  47.293  1.00 31.68 ? 147 GLU B CG  1 
ATOM   2571 C  CD  . GLU B 1 150 ? 97.052  50.342  46.378  1.00 34.80 ? 147 GLU B CD  1 
ATOM   2572 O  OE1 . GLU B 1 150 ? 96.571  50.005  45.271  1.00 35.90 ? 147 GLU B OE1 1 
ATOM   2573 O  OE2 . GLU B 1 150 ? 98.162  49.936  46.785  1.00 37.73 ? 147 GLU B OE2 1 
ATOM   2574 N  N   . LYS B 1 151 ? 92.557  53.521  45.950  1.00 27.57 ? 148 LYS B N   1 
ATOM   2575 C  CA  . LYS B 1 151 ? 91.660  54.428  45.239  1.00 27.14 ? 148 LYS B CA  1 
ATOM   2576 C  C   . LYS B 1 151 ? 90.857  55.312  46.209  1.00 26.96 ? 148 LYS B C   1 
ATOM   2577 O  O   . LYS B 1 151 ? 90.763  56.538  46.027  1.00 26.27 ? 148 LYS B O   1 
ATOM   2578 C  CB  . LYS B 1 151 ? 90.747  53.633  44.299  1.00 27.43 ? 148 LYS B CB  1 
ATOM   2579 C  CG  . LYS B 1 151 ? 91.467  52.938  43.114  1.00 27.49 ? 148 LYS B CG  1 
ATOM   2580 C  CD  . LYS B 1 151 ? 90.424  52.275  42.186  1.00 26.53 ? 148 LYS B CD  1 
ATOM   2581 C  CE  . LYS B 1 151 ? 91.048  51.402  41.110  1.00 27.83 ? 148 LYS B CE  1 
ATOM   2582 N  NZ  . LYS B 1 151 ? 90.051  50.805  40.101  1.00 28.49 ? 148 LYS B NZ  1 
ATOM   2583 N  N   . GLU B 1 152 ? 90.335  54.697  47.271  1.00 27.34 ? 149 GLU B N   1 
ATOM   2584 C  CA  . GLU B 1 152 ? 89.551  55.421  48.268  1.00 28.10 ? 149 GLU B CA  1 
ATOM   2585 C  C   . GLU B 1 152 ? 90.364  56.390  49.103  1.00 28.67 ? 149 GLU B C   1 
ATOM   2586 O  O   . GLU B 1 152 ? 89.857  57.462  49.444  1.00 29.59 ? 149 GLU B O   1 
ATOM   2587 C  CB  . GLU B 1 152 ? 88.764  54.470  49.163  1.00 28.36 ? 149 GLU B CB  1 
ATOM   2588 C  CG  . GLU B 1 152 ? 87.691  55.139  50.057  1.00 29.67 ? 149 GLU B CG  1 
ATOM   2589 C  CD  . GLU B 1 152 ? 86.671  55.989  49.294  1.00 32.05 ? 149 GLU B CD  1 
ATOM   2590 O  OE1 . GLU B 1 152 ? 86.222  56.994  49.885  1.00 31.80 ? 149 GLU B OE1 1 
ATOM   2591 O  OE2 . GLU B 1 152 ? 86.307  55.668  48.120  1.00 34.78 ? 149 GLU B OE2 1 
ATOM   2592 N  N   . ALA B 1 153 ? 91.609  56.026  49.444  1.00 28.72 ? 150 ALA B N   1 
ATOM   2593 C  CA  . ALA B 1 153 ? 92.539  56.945  50.117  1.00 27.90 ? 150 ALA B CA  1 
ATOM   2594 C  C   . ALA B 1 153 ? 92.751  58.237  49.306  1.00 28.04 ? 150 ALA B C   1 
ATOM   2595 O  O   . ALA B 1 153 ? 92.752  59.323  49.853  1.00 27.89 ? 150 ALA B O   1 
ATOM   2596 C  CB  . ALA B 1 153 ? 93.878  56.248  50.372  1.00 27.77 ? 150 ALA B CB  1 
ATOM   2597 N  N   . CYS B 1 154 ? 92.930  58.091  47.998  1.00 28.14 ? 151 CYS B N   1 
ATOM   2598 C  CA  . CYS B 1 154 ? 93.066  59.213  47.085  1.00 29.15 ? 151 CYS B CA  1 
ATOM   2599 C  C   . CYS B 1 154 ? 91.800  60.068  47.037  1.00 29.24 ? 151 CYS B C   1 
ATOM   2600 O  O   . CYS B 1 154 ? 91.868  61.291  46.997  1.00 29.58 ? 151 CYS B O   1 
ATOM   2601 C  CB  . CYS B 1 154 ? 93.358  58.673  45.683  1.00 28.54 ? 151 CYS B CB  1 
ATOM   2602 S  SG  . CYS B 1 154 ? 95.029  58.025  45.485  1.00 32.13 ? 151 CYS B SG  1 
ATOM   2603 N  N   . ARG B 1 155 ? 90.641  59.410  46.995  1.00 29.49 ? 152 ARG B N   1 
ATOM   2604 C  CA  . ARG B 1 155 ? 89.365  60.107  47.009  1.00 28.77 ? 152 ARG B CA  1 
ATOM   2605 C  C   . ARG B 1 155 ? 89.156  60.827  48.317  1.00 28.55 ? 152 ARG B C   1 
ATOM   2606 O  O   . ARG B 1 155 ? 88.704  61.960  48.330  1.00 29.02 ? 152 ARG B O   1 
ATOM   2607 C  CB  . ARG B 1 155 ? 88.226  59.135  46.801  1.00 28.75 ? 152 ARG B CB  1 
ATOM   2608 C  CG  . ARG B 1 155 ? 88.086  58.656  45.395  1.00 28.00 ? 152 ARG B CG  1 
ATOM   2609 C  CD  . ARG B 1 155 ? 86.807  57.865  45.285  1.00 25.08 ? 152 ARG B CD  1 
ATOM   2610 N  NE  . ARG B 1 155 ? 86.810  56.983  44.127  1.00 24.00 ? 152 ARG B NE  1 
ATOM   2611 C  CZ  . ARG B 1 155 ? 86.952  55.658  44.178  1.00 21.78 ? 152 ARG B CZ  1 
ATOM   2612 N  NH1 . ARG B 1 155 ? 87.101  55.017  45.339  1.00 18.13 ? 152 ARG B NH1 1 
ATOM   2613 N  NH2 . ARG B 1 155 ? 86.916  54.975  43.045  1.00 19.96 ? 152 ARG B NH2 1 
ATOM   2614 N  N   . ARG B 1 156 ? 89.503  60.173  49.417  1.00 27.87 ? 153 ARG B N   1 
ATOM   2615 C  CA  . ARG B 1 156 ? 89.294  60.745  50.722  1.00 27.68 ? 153 ARG B CA  1 
ATOM   2616 C  C   . ARG B 1 156 ? 90.041  62.056  50.985  1.00 28.45 ? 153 ARG B C   1 
ATOM   2617 O  O   . ARG B 1 156 ? 89.492  62.959  51.661  1.00 28.70 ? 153 ARG B O   1 
ATOM   2618 C  CB  . ARG B 1 156 ? 89.626  59.744  51.830  1.00 27.53 ? 153 ARG B CB  1 
ATOM   2619 C  CG  . ARG B 1 156 ? 89.042  60.229  53.125  1.00 28.38 ? 153 ARG B CG  1 
ATOM   2620 C  CD  . ARG B 1 156 ? 87.481  60.147  53.053  1.00 29.34 ? 153 ARG B CD  1 
ATOM   2621 N  NE  . ARG B 1 156 ? 87.171  59.217  54.110  1.00 32.79 ? 153 ARG B NE  1 
ATOM   2622 C  CZ  . ARG B 1 156 ? 86.734  57.979  53.972  1.00 30.76 ? 153 ARG B CZ  1 
ATOM   2623 N  NH1 . ARG B 1 156 ? 86.409  57.469  52.790  1.00 26.34 ? 153 ARG B NH1 1 
ATOM   2624 N  NH2 . ARG B 1 156 ? 86.596  57.269  55.080  1.00 29.93 ? 153 ARG B NH2 1 
ATOM   2625 N  N   . LEU B 1 157 ? 91.292  62.129  50.490  1.00 28.36 ? 154 LEU B N   1 
ATOM   2626 C  CA  . LEU B 1 157 ? 92.140  63.315  50.554  1.00 27.64 ? 154 LEU B CA  1 
ATOM   2627 C  C   . LEU B 1 157 ? 91.430  64.504  49.904  1.00 27.26 ? 154 LEU B C   1 
ATOM   2628 O  O   . LEU B 1 157 ? 91.359  65.593  50.491  1.00 27.24 ? 154 LEU B O   1 
ATOM   2629 C  CB  . LEU B 1 157 ? 93.521  63.045  49.896  1.00 27.14 ? 154 LEU B CB  1 
ATOM   2630 C  CG  . LEU B 1 157 ? 94.568  64.147  50.153  1.00 27.20 ? 154 LEU B CG  1 
ATOM   2631 C  CD1 . LEU B 1 157 ? 95.167  64.064  51.563  1.00 25.60 ? 154 LEU B CD1 1 
ATOM   2632 C  CD2 . LEU B 1 157 ? 95.683  64.177  49.089  1.00 27.37 ? 154 LEU B CD2 1 
ATOM   2633 N  N   . GLY B 1 158 ? 90.878  64.279  48.713  1.00 26.50 ? 155 GLY B N   1 
ATOM   2634 C  CA  . GLY B 1 158 ? 90.124  65.315  48.010  1.00 26.02 ? 155 GLY B CA  1 
ATOM   2635 C  C   . GLY B 1 158 ? 88.891  65.755  48.768  1.00 26.52 ? 155 GLY B C   1 
ATOM   2636 O  O   . GLY B 1 158 ? 88.644  66.970  48.918  1.00 26.90 ? 155 GLY B O   1 
ATOM   2637 N  N   . ARG B 1 159 ? 88.129  64.771  49.260  1.00 26.25 ? 156 ARG B N   1 
ATOM   2638 C  CA  . ARG B 1 159 ? 86.964  65.003  50.120  1.00 26.51 ? 156 ARG B CA  1 
ATOM   2639 C  C   . ARG B 1 159 ? 87.299  65.933  51.269  1.00 26.24 ? 156 ARG B C   1 
ATOM   2640 O  O   . ARG B 1 159 ? 86.718  67.022  51.390  1.00 26.82 ? 156 ARG B O   1 
ATOM   2641 C  CB  . ARG B 1 159 ? 86.475  63.695  50.734  1.00 26.40 ? 156 ARG B CB  1 
ATOM   2642 C  CG  . ARG B 1 159 ? 85.009  63.434  50.624  1.00 26.47 ? 156 ARG B CG  1 
ATOM   2643 C  CD  . ARG B 1 159 ? 84.045  64.396  51.304  1.00 25.99 ? 156 ARG B CD  1 
ATOM   2644 N  NE  . ARG B 1 159 ? 82.987  64.647  50.355  1.00 26.83 ? 156 ARG B NE  1 
ATOM   2645 C  CZ  . ARG B 1 159 ? 81.661  64.562  50.508  1.00 25.10 ? 156 ARG B CZ  1 
ATOM   2646 N  NH1 . ARG B 1 159 ? 81.048  64.297  51.651  1.00 20.31 ? 156 ARG B NH1 1 
ATOM   2647 N  NH2 . ARG B 1 159 ? 80.930  64.815  49.439  1.00 23.87 ? 156 ARG B NH2 1 
ATOM   2648 N  N   . ARG B 1 160 ? 88.231  65.489  52.110  1.00 25.66 ? 157 ARG B N   1 
ATOM   2649 C  CA  . ARG B 1 160 ? 88.586  66.223  53.327  1.00 25.53 ? 157 ARG B CA  1 
ATOM   2650 C  C   . ARG B 1 160 ? 89.076  67.626  52.993  1.00 24.89 ? 157 ARG B C   1 
ATOM   2651 O  O   . ARG B 1 160 ? 88.772  68.574  53.704  1.00 25.23 ? 157 ARG B O   1 
ATOM   2652 C  CB  . ARG B 1 160 ? 89.596  65.435  54.173  1.00 25.21 ? 157 ARG B CB  1 
ATOM   2653 C  CG  . ARG B 1 160 ? 89.880  66.007  55.567  1.00 26.17 ? 157 ARG B CG  1 
ATOM   2654 C  CD  . ARG B 1 160 ? 88.654  66.046  56.518  1.00 24.87 ? 157 ARG B CD  1 
ATOM   2655 N  NE  . ARG B 1 160 ? 87.672  64.982  56.269  1.00 26.00 ? 157 ARG B NE  1 
ATOM   2656 C  CZ  . ARG B 1 160 ? 87.795  63.715  56.677  1.00 25.94 ? 157 ARG B CZ  1 
ATOM   2657 N  NH1 . ARG B 1 160 ? 88.884  63.323  57.323  1.00 22.29 ? 157 ARG B NH1 1 
ATOM   2658 N  NH2 . ARG B 1 160 ? 86.845  62.825  56.389  1.00 22.35 ? 157 ARG B NH2 1 
ATOM   2659 N  N   . LEU B 1 161 ? 89.784  67.751  51.879  1.00 24.94 ? 158 LEU B N   1 
ATOM   2660 C  CA  . LEU B 1 161 ? 90.208  69.052  51.359  1.00 25.12 ? 158 LEU B CA  1 
ATOM   2661 C  C   . LEU B 1 161 ? 89.012  69.939  51.066  1.00 24.65 ? 158 LEU B C   1 
ATOM   2662 O  O   . LEU B 1 161 ? 89.001  71.087  51.484  1.00 25.34 ? 158 LEU B O   1 
ATOM   2663 C  CB  . LEU B 1 161 ? 91.028  68.903  50.079  1.00 24.99 ? 158 LEU B CB  1 
ATOM   2664 C  CG  . LEU B 1 161 ? 92.117  69.918  49.687  1.00 25.71 ? 158 LEU B CG  1 
ATOM   2665 C  CD1 . LEU B 1 161 ? 92.121  70.067  48.199  1.00 20.26 ? 158 LEU B CD1 1 
ATOM   2666 C  CD2 . LEU B 1 161 ? 92.128  71.289  50.408  1.00 24.10 ? 158 LEU B CD2 1 
ATOM   2667 N  N   . ALA B 1 162 ? 88.030  69.400  50.342  1.00 24.48 ? 159 ALA B N   1 
ATOM   2668 C  CA  . ALA B 1 162 ? 86.786  70.090  50.009  1.00 23.67 ? 159 ALA B CA  1 
ATOM   2669 C  C   . ALA B 1 162 ? 86.037  70.441  51.266  1.00 23.62 ? 159 ALA B C   1 
ATOM   2670 O  O   . ALA B 1 162 ? 85.502  71.547  51.394  1.00 23.21 ? 159 ALA B O   1 
ATOM   2671 C  CB  . ALA B 1 162 ? 85.903  69.206  49.107  1.00 23.83 ? 159 ALA B CB  1 
ATOM   2672 N  N   . GLU B 1 163 ? 85.997  69.489  52.191  1.00 23.53 ? 160 GLU B N   1 
ATOM   2673 C  CA  . GLU B 1 163 ? 85.331  69.704  53.474  1.00 24.28 ? 160 GLU B CA  1 
ATOM   2674 C  C   . GLU B 1 163 ? 85.943  70.833  54.288  1.00 24.57 ? 160 GLU B C   1 
ATOM   2675 O  O   . GLU B 1 163 ? 85.224  71.682  54.817  1.00 25.04 ? 160 GLU B O   1 
ATOM   2676 C  CB  . GLU B 1 163 ? 85.290  68.407  54.282  1.00 24.16 ? 160 GLU B CB  1 
ATOM   2677 C  CG  . GLU B 1 163 ? 84.171  67.453  53.799  1.00 24.41 ? 160 GLU B CG  1 
ATOM   2678 C  CD  . GLU B 1 163 ? 84.421  66.025  54.251  1.00 25.79 ? 160 GLU B CD  1 
ATOM   2679 O  OE1 . GLU B 1 163 ? 85.551  65.759  54.722  1.00 26.80 ? 160 GLU B OE1 1 
ATOM   2680 O  OE2 . GLU B 1 163 ? 83.488  65.184  54.176  1.00 26.49 ? 160 GLU B OE2 1 
ATOM   2681 N  N   . TRP B 1 164 ? 87.269  70.850  54.378  1.00 24.91 ? 161 TRP B N   1 
ATOM   2682 C  CA  . TRP B 1 164 ? 87.983  71.906  55.097  1.00 24.71 ? 161 TRP B CA  1 
ATOM   2683 C  C   . TRP B 1 164 ? 87.794  73.284  54.447  1.00 24.33 ? 161 TRP B C   1 
ATOM   2684 O  O   . TRP B 1 164 ? 87.660  74.295  55.137  1.00 23.93 ? 161 TRP B O   1 
ATOM   2685 C  CB  . TRP B 1 164 ? 89.482  71.583  55.168  1.00 24.98 ? 161 TRP B CB  1 
ATOM   2686 C  CG  . TRP B 1 164 ? 89.904  70.514  56.114  1.00 24.91 ? 161 TRP B CG  1 
ATOM   2687 C  CD1 . TRP B 1 164 ? 91.071  69.848  56.056  1.00 24.53 ? 161 TRP B CD1 1 
ATOM   2688 C  CD2 . TRP B 1 164 ? 89.210  70.005  57.283  1.00 25.25 ? 161 TRP B CD2 1 
ATOM   2689 N  NE1 . TRP B 1 164 ? 91.179  68.974  57.096  1.00 24.70 ? 161 TRP B NE1 1 
ATOM   2690 C  CE2 . TRP B 1 164 ? 90.052  69.026  57.863  1.00 23.39 ? 161 TRP B CE2 1 
ATOM   2691 C  CE3 . TRP B 1 164 ? 87.959  70.252  57.870  1.00 24.94 ? 161 TRP B CE3 1 
ATOM   2692 C  CZ2 . TRP B 1 164 ? 89.707  68.295  59.015  1.00 22.95 ? 161 TRP B CZ2 1 
ATOM   2693 C  CZ3 . TRP B 1 164 ? 87.611  69.518  59.030  1.00 25.39 ? 161 TRP B CZ3 1 
ATOM   2694 C  CH2 . TRP B 1 164 ? 88.485  68.543  59.578  1.00 23.56 ? 161 TRP B CH2 1 
ATOM   2695 N  N   . VAL B 1 165 ? 87.786  73.321  53.113  1.00 24.04 ? 162 VAL B N   1 
ATOM   2696 C  CA  . VAL B 1 165 ? 87.450  74.544  52.396  1.00 23.52 ? 162 VAL B CA  1 
ATOM   2697 C  C   . VAL B 1 165 ? 85.988  74.981  52.737  1.00 23.69 ? 162 VAL B C   1 
ATOM   2698 O  O   . VAL B 1 165 ? 85.721  76.156  53.034  1.00 23.91 ? 162 VAL B O   1 
ATOM   2699 C  CB  . VAL B 1 165 ? 87.694  74.380  50.860  1.00 24.02 ? 162 VAL B CB  1 
ATOM   2700 C  CG1 . VAL B 1 165 ? 87.067  75.566  50.056  1.00 23.61 ? 162 VAL B CG1 1 
ATOM   2701 C  CG2 . VAL B 1 165 ? 89.182  74.222  50.549  1.00 22.94 ? 162 VAL B CG2 1 
ATOM   2702 N  N   . ALA B 1 166 ? 85.064  74.018  52.746  1.00 23.25 ? 163 ALA B N   1 
ATOM   2703 C  CA  . ALA B 1 166 ? 83.657  74.277  53.066  1.00 22.61 ? 163 ALA B CA  1 
ATOM   2704 C  C   . ALA B 1 166 ? 83.479  74.811  54.478  1.00 22.86 ? 163 ALA B C   1 
ATOM   2705 O  O   . ALA B 1 166 ? 82.690  75.729  54.698  1.00 22.79 ? 163 ALA B O   1 
ATOM   2706 C  CB  . ALA B 1 166 ? 82.816  73.015  52.866  1.00 21.61 ? 163 ALA B CB  1 
ATOM   2707 N  N   . ILE B 1 167 ? 84.189  74.220  55.440  1.00 23.10 ? 164 ILE B N   1 
ATOM   2708 C  CA  . ILE B 1 167 ? 84.011  74.590  56.843  1.00 23.01 ? 164 ILE B CA  1 
ATOM   2709 C  C   . ILE B 1 167 ? 84.679  75.907  57.148  1.00 23.91 ? 164 ILE B C   1 
ATOM   2710 O  O   . ILE B 1 167 ? 84.044  76.785  57.746  1.00 25.14 ? 164 ILE B O   1 
ATOM   2711 C  CB  . ILE B 1 167 ? 84.510  73.509  57.790  1.00 22.85 ? 164 ILE B CB  1 
ATOM   2712 C  CG1 . ILE B 1 167 ? 83.637  72.260  57.631  1.00 23.51 ? 164 ILE B CG1 1 
ATOM   2713 C  CG2 . ILE B 1 167 ? 84.469  73.980  59.250  1.00 22.40 ? 164 ILE B CG2 1 
ATOM   2714 C  CD1 . ILE B 1 167 ? 84.278  71.005  58.121  1.00 21.24 ? 164 ILE B CD1 1 
ATOM   2715 N  N   . PHE B 1 168 ? 85.913  76.068  56.685  1.00 24.54 ? 165 PHE B N   1 
ATOM   2716 C  CA  . PHE B 1 168 ? 86.780  77.191  57.065  1.00 26.17 ? 165 PHE B CA  1 
ATOM   2717 C  C   . PHE B 1 168 ? 86.771  78.387  56.135  1.00 26.86 ? 165 PHE B C   1 
ATOM   2718 O  O   . PHE B 1 168 ? 86.959  79.499  56.597  1.00 26.82 ? 165 PHE B O   1 
ATOM   2719 C  CB  . PHE B 1 168 ? 88.236  76.720  57.262  1.00 26.97 ? 165 PHE B CB  1 
ATOM   2720 C  CG  . PHE B 1 168 ? 88.381  75.683  58.327  1.00 26.57 ? 165 PHE B CG  1 
ATOM   2721 C  CD1 . PHE B 1 168 ? 88.815  74.412  58.008  1.00 25.60 ? 165 PHE B CD1 1 
ATOM   2722 C  CD2 . PHE B 1 168 ? 88.015  75.974  59.652  1.00 26.82 ? 165 PHE B CD2 1 
ATOM   2723 C  CE1 . PHE B 1 168 ? 88.947  73.430  59.002  1.00 27.26 ? 165 PHE B CE1 1 
ATOM   2724 C  CE2 . PHE B 1 168 ? 88.113  75.015  60.644  1.00 27.96 ? 165 PHE B CE2 1 
ATOM   2725 C  CZ  . PHE B 1 168 ? 88.595  73.728  60.317  1.00 28.24 ? 165 PHE B CZ  1 
ATOM   2726 N  N   . VAL B 1 169 ? 86.571  78.159  54.831  1.00 27.94 ? 166 VAL B N   1 
ATOM   2727 C  CA  . VAL B 1 169 ? 86.470  79.256  53.873  1.00 27.91 ? 166 VAL B CA  1 
ATOM   2728 C  C   . VAL B 1 169 ? 85.007  79.641  53.632  1.00 28.70 ? 166 VAL B C   1 
ATOM   2729 O  O   . VAL B 1 169 ? 84.660  80.825  53.708  1.00 28.56 ? 166 VAL B O   1 
ATOM   2730 C  CB  . VAL B 1 169 ? 87.177  78.947  52.541  1.00 27.84 ? 166 VAL B CB  1 
ATOM   2731 C  CG1 . VAL B 1 169 ? 87.242  80.199  51.690  1.00 26.55 ? 166 VAL B CG1 1 
ATOM   2732 C  CG2 . VAL B 1 169 ? 88.586  78.433  52.784  1.00 27.44 ? 166 VAL B CG2 1 
ATOM   2733 N  N   . ASP B 1 170 ? 84.163  78.639  53.361  1.00 29.58 ? 167 ASP B N   1 
ATOM   2734 C  CA  . ASP B 1 170 ? 82.748  78.848  53.015  1.00 29.92 ? 167 ASP B CA  1 
ATOM   2735 C  C   . ASP B 1 170 ? 81.839  78.984  54.222  1.00 29.75 ? 167 ASP B C   1 
ATOM   2736 O  O   . ASP B 1 170 ? 80.670  79.271  54.081  1.00 30.06 ? 167 ASP B O   1 
ATOM   2737 C  CB  . ASP B 1 170 ? 82.234  77.701  52.152  1.00 30.56 ? 167 ASP B CB  1 
ATOM   2738 C  CG  . ASP B 1 170 ? 81.032  78.101  51.293  1.00 32.28 ? 167 ASP B CG  1 
ATOM   2739 O  OD1 . ASP B 1 170 ? 80.208  77.213  50.952  1.00 33.91 ? 167 ASP B OD1 1 
ATOM   2740 O  OD2 . ASP B 1 170 ? 80.923  79.304  50.945  1.00 32.99 ? 167 ASP B OD2 1 
ATOM   2741 N  N   . GLY B 1 171 ? 82.369  78.751  55.412  1.00 30.24 ? 168 GLY B N   1 
ATOM   2742 C  CA  . GLY B 1 171 ? 81.638  79.012  56.650  1.00 30.02 ? 168 GLY B CA  1 
ATOM   2743 C  C   . GLY B 1 171 ? 80.585  77.985  57.011  1.00 30.27 ? 168 GLY B C   1 
ATOM   2744 O  O   . GLY B 1 171 ? 79.606  78.328  57.658  1.00 30.32 ? 168 GLY B O   1 
ATOM   2745 N  N   . ARG B 1 172 ? 80.775  76.728  56.612  1.00 30.75 ? 169 ARG B N   1 
ATOM   2746 C  CA  . ARG B 1 172 ? 79.798  75.669  56.917  1.00 31.46 ? 169 ARG B CA  1 
ATOM   2747 C  C   . ARG B 1 172 ? 80.138  74.840  58.157  1.00 31.69 ? 169 ARG B C   1 
ATOM   2748 O  O   . ARG B 1 172 ? 80.601  73.708  58.071  1.00 32.09 ? 169 ARG B O   1 
ATOM   2749 C  CB  . ARG B 1 172 ? 79.532  74.802  55.691  1.00 31.53 ? 169 ARG B CB  1 
ATOM   2750 C  CG  . ARG B 1 172 ? 78.443  75.415  54.837  1.00 32.91 ? 169 ARG B CG  1 
ATOM   2751 C  CD  . ARG B 1 172 ? 78.718  75.221  53.377  1.00 36.84 ? 169 ARG B CD  1 
ATOM   2752 N  NE  . ARG B 1 172 ? 78.487  73.839  52.966  1.00 38.29 ? 169 ARG B NE  1 
ATOM   2753 C  CZ  . ARG B 1 172 ? 79.096  73.256  51.937  1.00 37.60 ? 169 ARG B CZ  1 
ATOM   2754 N  NH1 . ARG B 1 172 ? 79.985  73.929  51.196  1.00 36.05 ? 169 ARG B NH1 1 
ATOM   2755 N  NH2 . ARG B 1 172 ? 78.817  71.991  51.661  1.00 37.73 ? 169 ARG B NH2 1 
ATOM   2756 N  N   . LYS B 1 173 ? 79.874  75.440  59.309  1.00 32.03 ? 170 LYS B N   1 
ATOM   2757 C  CA  . LYS B 1 173 ? 80.300  74.956  60.614  1.00 32.32 ? 170 LYS B CA  1 
ATOM   2758 C  C   . LYS B 1 173 ? 79.619  73.659  61.066  1.00 32.49 ? 170 LYS B C   1 
ATOM   2759 O  O   . LYS B 1 173 ? 80.186  72.891  61.842  1.00 32.55 ? 170 LYS B O   1 
ATOM   2760 C  CB  . LYS B 1 173 ? 80.093  76.074  61.635  1.00 32.67 ? 170 LYS B CB  1 
ATOM   2761 C  CG  . LYS B 1 173 ? 80.736  77.408  61.171  1.00 34.38 ? 170 LYS B CG  1 
ATOM   2762 C  CD  . LYS B 1 173 ? 79.977  78.656  61.649  1.00 34.92 ? 170 LYS B CD  1 
ATOM   2763 C  CE  . LYS B 1 173 ? 80.425  79.088  63.039  1.00 37.09 ? 170 LYS B CE  1 
ATOM   2764 N  NZ  . LYS B 1 173 ? 80.169  80.539  63.372  1.00 37.39 ? 170 LYS B NZ  1 
ATOM   2765 N  N   . GLU B 1 174 ? 78.419  73.400  60.565  1.00 32.36 ? 171 GLU B N   1 
ATOM   2766 C  CA  . GLU B 1 174 ? 77.719  72.160  60.875  1.00 32.45 ? 171 GLU B CA  1 
ATOM   2767 C  C   . GLU B 1 174 ? 78.429  70.911  60.343  1.00 31.62 ? 171 GLU B C   1 
ATOM   2768 O  O   . GLU B 1 174 ? 78.177  69.813  60.842  1.00 31.41 ? 171 GLU B O   1 
ATOM   2769 C  CB  . GLU B 1 174 ? 76.289  72.170  60.329  1.00 32.85 ? 171 GLU B CB  1 
ATOM   2770 C  CG  . GLU B 1 174 ? 75.758  73.531  59.901  1.00 36.43 ? 171 GLU B CG  1 
ATOM   2771 C  CD  . GLU B 1 174 ? 76.313  73.987  58.542  1.00 39.90 ? 171 GLU B CD  1 
ATOM   2772 O  OE1 . GLU B 1 174 ? 76.109  73.275  57.514  1.00 39.60 ? 171 GLU B OE1 1 
ATOM   2773 O  OE2 . GLU B 1 174 ? 76.953  75.068  58.526  1.00 40.48 ? 171 GLU B OE2 1 
ATOM   2774 N  N   . LEU B 1 175 ? 79.278  71.055  59.325  1.00 30.64 ? 172 LEU B N   1 
ATOM   2775 C  CA  . LEU B 1 175 ? 79.959  69.875  58.781  1.00 30.57 ? 172 LEU B CA  1 
ATOM   2776 C  C   . LEU B 1 175 ? 81.015  69.344  59.728  1.00 30.33 ? 172 LEU B C   1 
ATOM   2777 O  O   . LEU B 1 175 ? 81.286  68.144  59.715  1.00 30.48 ? 172 LEU B O   1 
ATOM   2778 C  CB  . LEU B 1 175 ? 80.640  70.122  57.432  1.00 30.03 ? 172 LEU B CB  1 
ATOM   2779 C  CG  . LEU B 1 175 ? 79.951  70.528  56.140  1.00 31.80 ? 172 LEU B CG  1 
ATOM   2780 C  CD1 . LEU B 1 175 ? 80.954  70.275  55.002  1.00 31.58 ? 172 LEU B CD1 1 
ATOM   2781 C  CD2 . LEU B 1 175 ? 78.601  69.800  55.898  1.00 31.61 ? 172 LEU B CD2 1 
ATOM   2782 N  N   . LEU B 1 176 ? 81.620  70.242  60.517  1.00 30.20 ? 173 LEU B N   1 
ATOM   2783 C  CA  . LEU B 1 176 ? 82.743  69.900  61.400  1.00 30.02 ? 173 LEU B CA  1 
ATOM   2784 C  C   . LEU B 1 176 ? 82.418  68.761  62.369  1.00 30.51 ? 173 LEU B C   1 
ATOM   2785 O  O   . LEU B 1 176 ? 83.160  67.753  62.431  1.00 30.88 ? 173 LEU B O   1 
ATOM   2786 C  CB  . LEU B 1 176 ? 83.264  71.135  62.153  1.00 29.47 ? 173 LEU B CB  1 
ATOM   2787 C  CG  . LEU B 1 176 ? 84.546  70.965  62.987  1.00 30.28 ? 173 LEU B CG  1 
ATOM   2788 C  CD1 . LEU B 1 176 ? 85.714  70.346  62.174  1.00 27.90 ? 173 LEU B CD1 1 
ATOM   2789 C  CD2 . LEU B 1 176 ? 84.980  72.280  63.658  1.00 29.85 ? 173 LEU B CD2 1 
ATOM   2790 N  N   . GLU B 1 177 ? 81.319  68.915  63.107  1.00 30.19 ? 174 GLU B N   1 
ATOM   2791 C  CA  . GLU B 1 177 ? 80.919  67.928  64.105  1.00 31.02 ? 174 GLU B CA  1 
ATOM   2792 C  C   . GLU B 1 177 ? 80.416  66.648  63.450  1.00 30.85 ? 174 GLU B C   1 
ATOM   2793 O  O   . GLU B 1 177 ? 80.559  65.562  64.011  1.00 30.97 ? 174 GLU B O   1 
ATOM   2794 C  CB  . GLU B 1 177 ? 79.854  68.511  65.050  1.00 31.11 ? 174 GLU B CB  1 
ATOM   2795 C  CG  . GLU B 1 177 ? 79.433  67.598  66.206  1.00 33.44 ? 174 GLU B CG  1 
ATOM   2796 C  CD  . GLU B 1 177 ? 80.600  67.218  67.143  1.00 36.25 ? 174 GLU B CD  1 
ATOM   2797 O  OE1 . GLU B 1 177 ? 80.417  66.238  67.914  1.00 35.98 ? 174 GLU B OE1 1 
ATOM   2798 O  OE2 . GLU B 1 177 ? 81.678  67.890  67.105  1.00 36.63 ? 174 GLU B OE2 1 
ATOM   2799 N  N   . LYS B 1 178 ? 79.824  66.790  62.266  1.00 31.24 ? 175 LYS B N   1 
ATOM   2800 C  CA  . LYS B 1 178 ? 79.354  65.647  61.472  1.00 31.39 ? 175 LYS B CA  1 
ATOM   2801 C  C   . LYS B 1 178 ? 80.515  64.748  61.019  1.00 30.78 ? 175 LYS B C   1 
ATOM   2802 O  O   . LYS B 1 178 ? 80.428  63.516  61.099  1.00 30.80 ? 175 LYS B O   1 
ATOM   2803 C  CB  . LYS B 1 178 ? 78.465  66.114  60.296  1.00 31.48 ? 175 LYS B CB  1 
ATOM   2804 C  CG  . LYS B 1 178 ? 77.126  66.703  60.795  1.00 32.42 ? 175 LYS B CG  1 
ATOM   2805 C  CD  . LYS B 1 178 ? 76.024  66.853  59.724  1.00 31.84 ? 175 LYS B CD  1 
ATOM   2806 C  CE  . LYS B 1 178 ? 74.763  67.466  60.382  1.00 32.35 ? 175 LYS B CE  1 
ATOM   2807 N  NZ  . LYS B 1 178 ? 73.537  67.450  59.516  1.00 32.27 ? 175 LYS B NZ  1 
ATOM   2808 N  N   . ILE B 1 179 ? 81.599  65.379  60.569  1.00 30.11 ? 176 ILE B N   1 
ATOM   2809 C  CA  . ILE B 1 179 ? 82.821  64.682  60.208  1.00 29.51 ? 176 ILE B CA  1 
ATOM   2810 C  C   . ILE B 1 179 ? 83.427  64.046  61.458  1.00 29.43 ? 176 ILE B C   1 
ATOM   2811 O  O   . ILE B 1 179 ? 83.795  62.869  61.442  1.00 29.26 ? 176 ILE B O   1 
ATOM   2812 C  CB  . ILE B 1 179 ? 83.847  65.643  59.531  1.00 29.31 ? 176 ILE B CB  1 
ATOM   2813 C  CG1 . ILE B 1 179 ? 83.322  66.110  58.171  1.00 30.30 ? 176 ILE B CG1 1 
ATOM   2814 C  CG2 . ILE B 1 179 ? 85.192  64.979  59.359  1.00 27.73 ? 176 ILE B CG2 1 
ATOM   2815 C  CD1 . ILE B 1 179 ? 84.010  67.360  57.656  1.00 30.98 ? 176 ILE B CD1 1 
ATOM   2816 N  N   . ARG B 1 180 ? 83.518  64.819  62.545  1.00 29.17 ? 177 ARG B N   1 
ATOM   2817 C  CA  . ARG B 1 180 ? 84.211  64.348  63.749  1.00 29.02 ? 177 ARG B CA  1 
ATOM   2818 C  C   . ARG B 1 180 ? 83.625  63.069  64.337  1.00 28.80 ? 177 ARG B C   1 
ATOM   2819 O  O   . ARG B 1 180 ? 84.374  62.201  64.833  1.00 28.04 ? 177 ARG B O   1 
ATOM   2820 C  CB  . ARG B 1 180 ? 84.314  65.452  64.815  1.00 29.11 ? 177 ARG B CB  1 
ATOM   2821 C  CG  . ARG B 1 180 ? 85.397  66.480  64.504  1.00 28.48 ? 177 ARG B CG  1 
ATOM   2822 C  CD  . ARG B 1 180 ? 85.283  67.653  65.422  1.00 27.93 ? 177 ARG B CD  1 
ATOM   2823 N  NE  . ARG B 1 180 ? 86.454  68.520  65.378  1.00 26.63 ? 177 ARG B NE  1 
ATOM   2824 C  CZ  . ARG B 1 180 ? 86.588  69.642  66.083  1.00 25.65 ? 177 ARG B CZ  1 
ATOM   2825 N  NH1 . ARG B 1 180 ? 85.614  70.059  66.887  1.00 24.68 ? 177 ARG B NH1 1 
ATOM   2826 N  NH2 . ARG B 1 180 ? 87.700  70.347  65.984  1.00 24.88 ? 177 ARG B NH2 1 
ATOM   2827 N  N   . LYS B 1 181 ? 82.300  62.951  64.245  1.00 28.87 ? 178 LYS B N   1 
ATOM   2828 C  CA  . LYS B 1 181 ? 81.571  61.875  64.902  1.00 29.23 ? 178 LYS B CA  1 
ATOM   2829 C  C   . LYS B 1 181 ? 81.117  60.794  63.909  1.00 29.37 ? 178 LYS B C   1 
ATOM   2830 O  O   . LYS B 1 181 ? 80.353  59.900  64.265  1.00 29.52 ? 178 LYS B O   1 
ATOM   2831 C  CB  . LYS B 1 181 ? 80.418  62.449  65.779  1.00 28.91 ? 178 LYS B CB  1 
ATOM   2832 C  CG  . LYS B 1 181 ? 80.760  62.688  67.307  1.00 29.45 ? 178 LYS B CG  1 
ATOM   2833 C  CD  . LYS B 1 181 ? 82.004  63.588  67.539  1.00 30.63 ? 178 LYS B CD  1 
ATOM   2834 C  CE  . LYS B 1 181 ? 82.512  63.676  68.996  1.00 29.44 ? 178 LYS B CE  1 
ATOM   2835 N  NZ  . LYS B 1 181 ? 81.713  64.510  69.990  1.00 26.78 ? 178 LYS B NZ  1 
ATOM   2836 N  N   . ASP B 1 182 ? 81.611  60.858  62.669  1.00 29.83 ? 179 ASP B N   1 
ATOM   2837 C  CA  . ASP B 1 182 ? 81.200  59.911  61.623  1.00 29.70 ? 179 ASP B CA  1 
ATOM   2838 C  C   . ASP B 1 182 ? 81.961  58.583  61.727  1.00 30.13 ? 179 ASP B C   1 
ATOM   2839 O  O   . ASP B 1 182 ? 83.173  58.554  61.495  1.00 29.59 ? 179 ASP B O   1 
ATOM   2840 C  CB  . ASP B 1 182 ? 81.359  60.525  60.232  1.00 30.15 ? 179 ASP B CB  1 
ATOM   2841 C  CG  . ASP B 1 182 ? 81.116  59.515  59.080  1.00 30.06 ? 179 ASP B CG  1 
ATOM   2842 O  OD1 . ASP B 1 182 ? 81.603  59.748  57.961  1.00 31.47 ? 179 ASP B OD1 1 
ATOM   2843 O  OD2 . ASP B 1 182 ? 80.453  58.491  59.273  1.00 30.20 ? 179 ASP B OD2 1 
ATOM   2844 N  N   . PRO B 1 183 ? 81.237  57.475  62.077  1.00 30.65 ? 180 PRO B N   1 
ATOM   2845 C  CA  . PRO B 1 183 ? 81.822  56.129  62.246  1.00 30.36 ? 180 PRO B CA  1 
ATOM   2846 C  C   . PRO B 1 183 ? 82.422  55.563  60.975  1.00 30.30 ? 180 PRO B C   1 
ATOM   2847 O  O   . PRO B 1 183 ? 83.340  54.745  61.054  1.00 30.94 ? 180 PRO B O   1 
ATOM   2848 C  CB  . PRO B 1 183 ? 80.631  55.263  62.677  1.00 30.29 ? 180 PRO B CB  1 
ATOM   2849 C  CG  . PRO B 1 183 ? 79.597  56.231  63.162  1.00 30.78 ? 180 PRO B CG  1 
ATOM   2850 C  CD  . PRO B 1 183 ? 79.778  57.461  62.331  1.00 30.37 ? 180 PRO B CD  1 
ATOM   2851 N  N   . ALA B 1 184 ? 81.915  55.999  59.822  1.00 29.67 ? 181 ALA B N   1 
ATOM   2852 C  CA  . ALA B 1 184 ? 82.360  55.499  58.530  1.00 29.35 ? 181 ALA B CA  1 
ATOM   2853 C  C   . ALA B 1 184 ? 83.781  55.927  58.174  1.00 29.26 ? 181 ALA B C   1 
ATOM   2854 O  O   . ALA B 1 184 ? 84.374  55.418  57.222  1.00 29.50 ? 181 ALA B O   1 
ATOM   2855 C  CB  . ALA B 1 184 ? 81.369  55.911  57.411  1.00 29.32 ? 181 ALA B CB  1 
ATOM   2856 N  N   . ARG B 1 185 ? 84.329  56.866  58.927  1.00 29.10 ? 182 ARG B N   1 
ATOM   2857 C  CA  . ARG B 1 185 ? 85.656  57.358  58.653  1.00 28.80 ? 182 ARG B CA  1 
ATOM   2858 C  C   . ARG B 1 185 ? 86.712  56.313  59.020  1.00 29.27 ? 182 ARG B C   1 
ATOM   2859 O  O   . ARG B 1 185 ? 87.881  56.441  58.643  1.00 29.62 ? 182 ARG B O   1 
ATOM   2860 C  CB  . ARG B 1 185 ? 85.883  58.664  59.406  1.00 28.84 ? 182 ARG B CB  1 
ATOM   2861 C  CG  . ARG B 1 185 ? 85.151  59.889  58.820  1.00 28.91 ? 182 ARG B CG  1 
ATOM   2862 C  CD  . ARG B 1 185 ? 85.364  61.129  59.704  1.00 29.09 ? 182 ARG B CD  1 
ATOM   2863 N  NE  . ARG B 1 185 ? 86.776  61.267  60.065  1.00 30.71 ? 182 ARG B NE  1 
ATOM   2864 C  CZ  . ARG B 1 185 ? 87.233  61.639  61.251  1.00 30.19 ? 182 ARG B CZ  1 
ATOM   2865 N  NH1 . ARG B 1 185 ? 88.537  61.697  61.441  1.00 31.49 ? 182 ARG B NH1 1 
ATOM   2866 N  NH2 . ARG B 1 185 ? 86.399  61.938  62.242  1.00 29.62 ? 182 ARG B NH2 1 
ATOM   2867 N  N   . PHE B 1 186 ? 86.297  55.270  59.741  1.00 29.71 ? 183 PHE B N   1 
ATOM   2868 C  CA  . PHE B 1 186 ? 87.225  54.244  60.238  1.00 30.29 ? 183 PHE B CA  1 
ATOM   2869 C  C   . PHE B 1 186 ? 86.757  52.838  59.914  1.00 31.06 ? 183 PHE B C   1 
ATOM   2870 O  O   . PHE B 1 186 ? 85.864  52.306  60.565  1.00 31.26 ? 183 PHE B O   1 
ATOM   2871 C  CB  . PHE B 1 186 ? 87.542  54.439  61.751  1.00 29.40 ? 183 PHE B CB  1 
ATOM   2872 C  CG  . PHE B 1 186 ? 88.152  55.777  62.042  1.00 29.04 ? 183 PHE B CG  1 
ATOM   2873 C  CD1 . PHE B 1 186 ? 87.344  56.869  62.393  1.00 28.28 ? 183 PHE B CD1 1 
ATOM   2874 C  CD2 . PHE B 1 186 ? 89.520  55.985  61.859  1.00 28.12 ? 183 PHE B CD2 1 
ATOM   2875 C  CE1 . PHE B 1 186 ? 87.901  58.136  62.590  1.00 27.65 ? 183 PHE B CE1 1 
ATOM   2876 C  CE2 . PHE B 1 186 ? 90.087  57.259  62.056  1.00 27.79 ? 183 PHE B CE2 1 
ATOM   2877 C  CZ  . PHE B 1 186 ? 89.283  58.324  62.420  1.00 27.50 ? 183 PHE B CZ  1 
ATOM   2878 N  N   . VAL B 1 187 ? 87.375  52.253  58.888  1.00 32.22 ? 184 VAL B N   1 
ATOM   2879 C  CA  . VAL B 1 187 ? 87.158  50.853  58.526  1.00 32.67 ? 184 VAL B CA  1 
ATOM   2880 C  C   . VAL B 1 187 ? 87.992  49.980  59.438  1.00 33.57 ? 184 VAL B C   1 
ATOM   2881 O  O   . VAL B 1 187 ? 87.505  49.559  60.485  1.00 34.91 ? 184 VAL B O   1 
ATOM   2882 C  CB  . VAL B 1 187 ? 87.534  50.563  57.065  1.00 32.52 ? 184 VAL B CB  1 
ATOM   2883 C  CG1 . VAL B 1 187 ? 87.416  49.077  56.773  1.00 32.97 ? 184 VAL B CG1 1 
ATOM   2884 C  CG2 . VAL B 1 187 ? 86.657  51.365  56.133  1.00 31.48 ? 184 VAL B CG2 1 
ATOM   2885 N  N   . ALA C 1 3   ? 137.581 38.250  62.097  1.00 47.61 ? 0   ALA C N   1 
ATOM   2886 C  CA  . ALA C 1 3   ? 136.040 38.700  61.616  1.00 47.53 ? 0   ALA C CA  1 
ATOM   2887 C  C   . ALA C 1 3   ? 135.307 39.214  62.878  1.00 47.57 ? 0   ALA C C   1 
ATOM   2888 O  O   . ALA C 1 3   ? 135.193 38.485  63.883  1.00 47.54 ? 0   ALA C O   1 
ATOM   2889 C  CB  . ALA C 1 3   ? 135.205 37.837  60.862  1.00 47.55 ? 0   ALA C CB  1 
HETATM 2890 N  N   . MSE C 1 4   ? 134.822 40.463  62.820  1.00 47.54 ? 1   MSE C N   1 
HETATM 2891 C  CA  . MSE C 1 4   ? 134.397 41.196  64.030  1.00 47.56 ? 1   MSE C CA  1 
HETATM 2892 C  C   . MSE C 1 4   ? 133.276 42.243  63.893  1.00 45.58 ? 1   MSE C C   1 
HETATM 2893 O  O   . MSE C 1 4   ? 133.271 43.054  62.959  1.00 45.75 ? 1   MSE C O   1 
HETATM 2894 C  CB  . MSE C 1 4   ? 135.617 41.871  64.661  1.00 49.52 ? 1   MSE C CB  1 
HETATM 2895 C  CG  . MSE C 1 4   ? 136.150 41.128  65.850  1.00 53.87 ? 1   MSE C CG  1 
HETATM 2896 SE SE  . MSE C 1 4   ? 134.745 41.012  67.240  1.00 68.15 ? 1   MSE C SE  1 
HETATM 2897 C  CE  . MSE C 1 4   ? 135.748 39.579  68.463  1.00 57.88 ? 1   MSE C CE  1 
ATOM   2898 N  N   . GLY C 1 5   ? 132.354 42.251  64.853  1.00 43.05 ? 2   GLY C N   1 
ATOM   2899 C  CA  . GLY C 1 5   ? 131.301 43.260  64.870  1.00 39.84 ? 2   GLY C CA  1 
ATOM   2900 C  C   . GLY C 1 5   ? 130.463 43.253  66.129  1.00 37.68 ? 2   GLY C C   1 
ATOM   2901 O  O   . GLY C 1 5   ? 130.146 42.192  66.666  1.00 37.47 ? 2   GLY C O   1 
ATOM   2902 N  N   . LYS C 1 6   ? 130.104 44.446  66.598  1.00 35.36 ? 3   LYS C N   1 
ATOM   2903 C  CA  . LYS C 1 6   ? 129.255 44.588  67.775  1.00 33.32 ? 3   LYS C CA  1 
ATOM   2904 C  C   . LYS C 1 6   ? 127.981 45.382  67.430  1.00 32.07 ? 3   LYS C C   1 
ATOM   2905 O  O   . LYS C 1 6   ? 128.035 46.575  67.150  1.00 30.89 ? 3   LYS C O   1 
ATOM   2906 C  CB  . LYS C 1 6   ? 130.024 45.228  68.951  1.00 33.26 ? 3   LYS C CB  1 
ATOM   2907 C  CG  . LYS C 1 6   ? 131.389 44.598  69.313  1.00 32.98 ? 3   LYS C CG  1 
ATOM   2908 C  CD  . LYS C 1 6   ? 131.890 45.125  70.655  1.00 33.60 ? 3   LYS C CD  1 
ATOM   2909 C  CE  . LYS C 1 6   ? 133.402 45.440  70.676  1.00 34.61 ? 3   LYS C CE  1 
ATOM   2910 N  NZ  . LYS C 1 6   ? 134.308 44.264  70.973  1.00 33.47 ? 3   LYS C NZ  1 
ATOM   2911 N  N   . VAL C 1 7   ? 126.841 44.699  67.444  1.00 31.22 ? 4   VAL C N   1 
ATOM   2912 C  CA  . VAL C 1 7   ? 125.553 45.307  67.069  1.00 30.79 ? 4   VAL C CA  1 
ATOM   2913 C  C   . VAL C 1 7   ? 124.531 45.290  68.216  1.00 30.44 ? 4   VAL C C   1 
ATOM   2914 O  O   . VAL C 1 7   ? 124.251 44.241  68.803  1.00 31.27 ? 4   VAL C O   1 
ATOM   2915 C  CB  . VAL C 1 7   ? 124.954 44.644  65.791  1.00 30.36 ? 4   VAL C CB  1 
ATOM   2916 C  CG1 . VAL C 1 7   ? 123.448 44.843  65.711  1.00 30.04 ? 4   VAL C CG1 1 
ATOM   2917 C  CG2 . VAL C 1 7   ? 125.606 45.192  64.556  1.00 30.04 ? 4   VAL C CG2 1 
ATOM   2918 N  N   . LEU C 1 8   ? 123.985 46.455  68.534  1.00 29.76 ? 5   LEU C N   1 
ATOM   2919 C  CA  . LEU C 1 8   ? 122.940 46.548  69.532  1.00 29.80 ? 5   LEU C CA  1 
ATOM   2920 C  C   . LEU C 1 8   ? 121.617 46.825  68.829  1.00 29.25 ? 5   LEU C C   1 
ATOM   2921 O  O   . LEU C 1 8   ? 121.526 47.753  68.057  1.00 29.69 ? 5   LEU C O   1 
ATOM   2922 C  CB  . LEU C 1 8   ? 123.266 47.678  70.502  1.00 29.95 ? 5   LEU C CB  1 
ATOM   2923 C  CG  . LEU C 1 8   ? 122.552 47.911  71.847  1.00 30.49 ? 5   LEU C CG  1 
ATOM   2924 C  CD1 . LEU C 1 8   ? 121.768 49.201  71.834  1.00 30.33 ? 5   LEU C CD1 1 
ATOM   2925 C  CD2 . LEU C 1 8   ? 121.710 46.753  72.350  1.00 29.57 ? 5   LEU C CD2 1 
ATOM   2926 N  N   . VAL C 1 9   ? 120.609 45.999  69.084  1.00 28.62 ? 6   VAL C N   1 
ATOM   2927 C  CA  . VAL C 1 9   ? 119.251 46.250  68.626  1.00 27.66 ? 6   VAL C CA  1 
ATOM   2928 C  C   . VAL C 1 9   ? 118.405 46.604  69.851  1.00 27.61 ? 6   VAL C C   1 
ATOM   2929 O  O   . VAL C 1 9   ? 118.257 45.815  70.770  1.00 27.61 ? 6   VAL C O   1 
ATOM   2930 C  CB  . VAL C 1 9   ? 118.661 45.022  67.906  1.00 27.91 ? 6   VAL C CB  1 
ATOM   2931 C  CG1 . VAL C 1 9   ? 117.224 45.275  67.483  1.00 28.02 ? 6   VAL C CG1 1 
ATOM   2932 C  CG2 . VAL C 1 9   ? 119.523 44.628  66.708  1.00 26.74 ? 6   VAL C CG2 1 
ATOM   2933 N  N   . ILE C 1 10  ? 117.860 47.806  69.866  1.00 27.36 ? 7   ILE C N   1 
ATOM   2934 C  CA  . ILE C 1 10  ? 117.113 48.253  70.997  1.00 27.80 ? 7   ILE C CA  1 
ATOM   2935 C  C   . ILE C 1 10  ? 115.726 48.672  70.534  1.00 27.67 ? 7   ILE C C   1 
ATOM   2936 O  O   . ILE C 1 10  ? 115.567 49.216  69.454  1.00 27.80 ? 7   ILE C O   1 
ATOM   2937 C  CB  . ILE C 1 10  ? 117.878 49.372  71.740  1.00 28.23 ? 7   ILE C CB  1 
ATOM   2938 C  CG1 . ILE C 1 10  ? 117.083 49.856  72.945  1.00 29.10 ? 7   ILE C CG1 1 
ATOM   2939 C  CG2 . ILE C 1 10  ? 118.212 50.510  70.797  1.00 29.07 ? 7   ILE C CG2 1 
ATOM   2940 C  CD1 . ILE C 1 10  ? 117.690 51.064  73.592  1.00 33.03 ? 7   ILE C CD1 1 
ATOM   2941 N  N   . TYR C 1 11  ? 114.703 48.412  71.332  1.00 27.38 ? 8   TYR C N   1 
ATOM   2942 C  CA  . TYR C 1 11  ? 113.346 48.644  70.838  1.00 26.86 ? 8   TYR C CA  1 
ATOM   2943 C  C   . TYR C 1 11  ? 112.420 48.993  71.979  1.00 27.24 ? 8   TYR C C   1 
ATOM   2944 O  O   . TYR C 1 11  ? 112.672 48.654  73.132  1.00 25.96 ? 8   TYR C O   1 
ATOM   2945 C  CB  . TYR C 1 11  ? 112.796 47.414  70.077  1.00 26.67 ? 8   TYR C CB  1 
ATOM   2946 C  CG  . TYR C 1 11  ? 112.624 46.187  70.987  1.00 25.45 ? 8   TYR C CG  1 
ATOM   2947 C  CD1 . TYR C 1 11  ? 111.384 45.870  71.535  1.00 23.29 ? 8   TYR C CD1 1 
ATOM   2948 C  CD2 . TYR C 1 11  ? 113.717 45.390  71.328  1.00 24.76 ? 8   TYR C CD2 1 
ATOM   2949 C  CE1 . TYR C 1 11  ? 111.226 44.793  72.386  1.00 24.84 ? 8   TYR C CE1 1 
ATOM   2950 C  CE2 . TYR C 1 11  ? 113.570 44.279  72.185  1.00 25.70 ? 8   TYR C CE2 1 
ATOM   2951 C  CZ  . TYR C 1 11  ? 112.314 43.995  72.703  1.00 25.84 ? 8   TYR C CZ  1 
ATOM   2952 O  OH  . TYR C 1 11  ? 112.146 42.924  73.558  1.00 27.74 ? 8   TYR C OH  1 
ATOM   2953 N  N   . ASP C 1 12  ? 111.346 49.692  71.627  1.00 27.95 ? 9   ASP C N   1 
ATOM   2954 C  CA  . ASP C 1 12  ? 110.199 49.826  72.488  1.00 28.52 ? 9   ASP C CA  1 
ATOM   2955 C  C   . ASP C 1 12  ? 109.074 49.090  71.757  1.00 29.11 ? 9   ASP C C   1 
ATOM   2956 O  O   . ASP C 1 12  ? 109.089 48.974  70.523  1.00 28.55 ? 9   ASP C O   1 
ATOM   2957 C  CB  . ASP C 1 12  ? 109.852 51.320  72.692  1.00 28.68 ? 9   ASP C CB  1 
ATOM   2958 C  CG  . ASP C 1 12  ? 108.783 51.533  73.764  1.00 28.79 ? 9   ASP C CG  1 
ATOM   2959 O  OD1 . ASP C 1 12  ? 108.545 50.585  74.561  1.00 30.23 ? 9   ASP C OD1 1 
ATOM   2960 O  OD2 . ASP C 1 12  ? 108.183 52.631  73.811  1.00 25.94 ? 9   ASP C OD2 1 
ATOM   2961 N  N   . THR C 1 13  ? 108.109 48.599  72.520  1.00 30.03 ? 10  THR C N   1 
ATOM   2962 C  CA  . THR C 1 13  ? 106.915 47.968  71.972  1.00 31.16 ? 10  THR C CA  1 
ATOM   2963 C  C   . THR C 1 13  ? 105.772 48.177  72.961  1.00 32.36 ? 10  THR C C   1 
ATOM   2964 O  O   . THR C 1 13  ? 105.996 48.268  74.169  1.00 32.20 ? 10  THR C O   1 
ATOM   2965 C  CB  . THR C 1 13  ? 107.127 46.444  71.661  1.00 31.24 ? 10  THR C CB  1 
ATOM   2966 O  OG1 . THR C 1 13  ? 106.026 45.937  70.893  1.00 32.32 ? 10  THR C OG1 1 
ATOM   2967 C  CG2 . THR C 1 13  ? 107.278 45.606  72.926  1.00 30.02 ? 10  THR C CG2 1 
ATOM   2968 N  N   . ARG C 1 14  ? 104.556 48.290  72.452  1.00 33.40 ? 11  ARG C N   1 
ATOM   2969 C  CA  . ARG C 1 14  ? 103.389 48.391  73.314  1.00 35.17 ? 11  ARG C CA  1 
ATOM   2970 C  C   . ARG C 1 14  ? 102.635 47.081  73.205  1.00 35.12 ? 11  ARG C C   1 
ATOM   2971 O  O   . ARG C 1 14  ? 102.128 46.547  74.186  1.00 35.69 ? 11  ARG C O   1 
ATOM   2972 C  CB  . ARG C 1 14  ? 102.496 49.569  72.883  1.00 36.12 ? 11  ARG C CB  1 
ATOM   2973 C  CG  . ARG C 1 14  ? 101.371 49.966  73.875  1.00 39.66 ? 11  ARG C CG  1 
ATOM   2974 C  CD  . ARG C 1 14  ? 101.861 50.795  75.099  1.00 45.71 ? 11  ARG C CD  1 
ATOM   2975 N  NE  . ARG C 1 14  ? 102.204 52.191  74.774  1.00 50.16 ? 11  ARG C NE  1 
ATOM   2976 C  CZ  . ARG C 1 14  ? 101.342 53.216  74.732  1.00 51.38 ? 11  ARG C CZ  1 
ATOM   2977 N  NH1 . ARG C 1 14  ? 100.049 53.014  74.988  1.00 50.65 ? 11  ARG C NH1 1 
ATOM   2978 N  NH2 . ARG C 1 14  ? 101.778 54.454  74.429  1.00 50.97 ? 11  ARG C NH2 1 
ATOM   2979 N  N   . THR C 1 15  ? 102.632 46.538  72.002  1.00 35.23 ? 12  THR C N   1 
ATOM   2980 C  CA  . THR C 1 15  ? 101.697 45.501  71.614  1.00 34.94 ? 12  THR C CA  1 
ATOM   2981 C  C   . THR C 1 15  ? 102.434 44.199  71.180  1.00 33.95 ? 12  THR C C   1 
ATOM   2982 O  O   . THR C 1 15  ? 101.820 43.151  71.023  1.00 32.92 ? 12  THR C O   1 
ATOM   2983 C  CB  . THR C 1 15  ? 100.768 46.127  70.515  1.00 35.39 ? 12  THR C CB  1 
ATOM   2984 O  OG1 . THR C 1 15  ? 99.393  46.013  70.894  1.00 37.23 ? 12  THR C OG1 1 
ATOM   2985 C  CG2 . THR C 1 15  ? 101.014 45.564  69.131  1.00 35.30 ? 12  THR C CG2 1 
ATOM   2986 N  N   . GLY C 1 16  ? 103.759 44.287  71.014  1.00 33.36 ? 13  GLY C N   1 
ATOM   2987 C  CA  . GLY C 1 16  ? 104.584 43.147  70.615  1.00 32.21 ? 13  GLY C CA  1 
ATOM   2988 C  C   . GLY C 1 16  ? 105.090 43.233  69.180  1.00 31.74 ? 13  GLY C C   1 
ATOM   2989 O  O   . GLY C 1 16  ? 106.062 42.562  68.817  1.00 31.66 ? 13  GLY C O   1 
ATOM   2990 N  N   . ASN C 1 17  ? 104.438 44.063  68.363  1.00 30.92 ? 14  ASN C N   1 
ATOM   2991 C  CA  . ASN C 1 17  ? 104.736 44.157  66.925  1.00 30.19 ? 14  ASN C CA  1 
ATOM   2992 C  C   . ASN C 1 17  ? 106.151 44.562  66.589  1.00 29.47 ? 14  ASN C C   1 
ATOM   2993 O  O   . ASN C 1 17  ? 106.764 43.995  65.688  1.00 29.45 ? 14  ASN C O   1 
ATOM   2994 C  CB  . ASN C 1 17  ? 103.764 45.103  66.223  1.00 30.06 ? 14  ASN C CB  1 
ATOM   2995 C  CG  . ASN C 1 17  ? 102.352 44.577  66.219  1.00 30.57 ? 14  ASN C CG  1 
ATOM   2996 O  OD1 . ASN C 1 17  ? 102.128 43.365  66.310  1.00 30.00 ? 14  ASN C OD1 1 
ATOM   2997 N  ND2 . ASN C 1 17  ? 101.384 45.483  66.102  1.00 31.20 ? 14  ASN C ND2 1 
ATOM   2998 N  N   . THR C 1 18  ? 106.657 45.548  67.318  1.00 29.08 ? 15  THR C N   1 
ATOM   2999 C  CA  . THR C 1 18  ? 107.984 46.082  67.069  1.00 28.84 ? 15  THR C CA  1 
ATOM   3000 C  C   . THR C 1 18  ? 109.014 45.123  67.605  1.00 28.67 ? 15  THR C C   1 
ATOM   3001 O  O   . THR C 1 18  ? 110.096 45.014  67.026  1.00 28.21 ? 15  THR C O   1 
ATOM   3002 C  CB  . THR C 1 18  ? 108.161 47.517  67.651  1.00 28.80 ? 15  THR C CB  1 
ATOM   3003 O  OG1 . THR C 1 18  ? 107.135 48.370  67.123  1.00 28.02 ? 15  THR C OG1 1 
ATOM   3004 C  CG2 . THR C 1 18  ? 109.486 48.111  67.254  1.00 29.29 ? 15  THR C CG2 1 
ATOM   3005 N  N   . LYS C 1 19  ? 108.662 44.424  68.699  1.00 29.23 ? 16  LYS C N   1 
ATOM   3006 C  CA  . LYS C 1 19  ? 109.492 43.364  69.271  1.00 29.65 ? 16  LYS C CA  1 
ATOM   3007 C  C   . LYS C 1 19  ? 109.715 42.261  68.230  1.00 30.07 ? 16  LYS C C   1 
ATOM   3008 O  O   . LYS C 1 19  ? 110.840 41.845  67.984  1.00 30.08 ? 16  LYS C O   1 
ATOM   3009 C  CB  . LYS C 1 19  ? 108.875 42.782  70.555  1.00 29.70 ? 16  LYS C CB  1 
ATOM   3010 C  CG  . LYS C 1 19  ? 109.737 41.662  71.188  1.00 29.47 ? 16  LYS C CG  1 
ATOM   3011 C  CD  . LYS C 1 19  ? 109.309 41.291  72.617  1.00 29.48 ? 16  LYS C CD  1 
ATOM   3012 C  CE  . LYS C 1 19  ? 110.128 40.103  73.146  1.00 29.37 ? 16  LYS C CE  1 
ATOM   3013 N  NZ  . LYS C 1 19  ? 109.632 39.577  74.472  1.00 28.39 ? 16  LYS C NZ  1 
ATOM   3014 N  N   . LYS C 1 20  ? 108.635 41.816  67.605  1.00 30.83 ? 17  LYS C N   1 
ATOM   3015 C  CA  . LYS C 1 20  ? 108.718 40.853  66.510  1.00 31.80 ? 17  LYS C CA  1 
ATOM   3016 C  C   . LYS C 1 20  ? 109.691 41.326  65.423  1.00 32.30 ? 17  LYS C C   1 
ATOM   3017 O  O   . LYS C 1 20  ? 110.501 40.547  64.938  1.00 32.53 ? 17  LYS C O   1 
ATOM   3018 C  CB  . LYS C 1 20  ? 107.328 40.583  65.917  1.00 31.59 ? 17  LYS C CB  1 
ATOM   3019 C  CG  . LYS C 1 20  ? 106.360 39.873  66.854  1.00 31.79 ? 17  LYS C CG  1 
ATOM   3020 C  CD  . LYS C 1 20  ? 106.603 38.363  66.915  1.00 32.91 ? 17  LYS C CD  1 
ATOM   3021 C  CE  . LYS C 1 20  ? 105.715 37.695  67.978  1.00 33.67 ? 17  LYS C CE  1 
ATOM   3022 N  NZ  . LYS C 1 20  ? 105.933 36.197  68.102  1.00 32.44 ? 17  LYS C NZ  1 
HETATM 3023 N  N   . MSE C 1 21  ? 109.621 42.603  65.056  1.00 32.95 ? 18  MSE C N   1 
HETATM 3024 C  CA  . MSE C 1 21  ? 110.579 43.189  64.111  1.00 34.40 ? 18  MSE C CA  1 
HETATM 3025 C  C   . MSE C 1 21  ? 112.024 43.133  64.626  1.00 32.75 ? 18  MSE C C   1 
HETATM 3026 O  O   . MSE C 1 21  ? 112.913 42.672  63.921  1.00 32.55 ? 18  MSE C O   1 
HETATM 3027 C  CB  . MSE C 1 21  ? 110.216 44.626  63.805  1.00 33.34 ? 18  MSE C CB  1 
HETATM 3028 C  CG  . MSE C 1 21  ? 108.903 44.818  63.097  1.00 35.18 ? 18  MSE C CG  1 
HETATM 3029 SE SE  . MSE C 1 21  ? 108.569 46.763  62.715  1.00 41.76 ? 18  MSE C SE  1 
HETATM 3030 C  CE  . MSE C 1 21  ? 109.998 47.054  61.336  1.00 35.68 ? 18  MSE C CE  1 
ATOM   3031 N  N   . ALA C 1 22  ? 112.239 43.595  65.860  1.00 32.00 ? 19  ALA C N   1 
ATOM   3032 C  CA  . ALA C 1 22  ? 113.569 43.627  66.489  1.00 31.04 ? 19  ALA C CA  1 
ATOM   3033 C  C   . ALA C 1 22  ? 114.263 42.257  66.475  1.00 30.71 ? 19  ALA C C   1 
ATOM   3034 O  O   . ALA C 1 22  ? 115.457 42.148  66.163  1.00 30.26 ? 19  ALA C O   1 
ATOM   3035 C  CB  . ALA C 1 22  ? 113.467 44.167  67.910  1.00 30.26 ? 19  ALA C CB  1 
ATOM   3036 N  N   . GLU C 1 23  ? 113.497 41.218  66.799  1.00 29.98 ? 20  GLU C N   1 
ATOM   3037 C  CA  . GLU C 1 23  ? 113.990 39.854  66.759  1.00 30.05 ? 20  GLU C CA  1 
ATOM   3038 C  C   . GLU C 1 23  ? 114.509 39.491  65.360  1.00 29.60 ? 20  GLU C C   1 
ATOM   3039 O  O   . GLU C 1 23  ? 115.550 38.832  65.233  1.00 30.33 ? 20  GLU C O   1 
ATOM   3040 C  CB  . GLU C 1 23  ? 112.907 38.867  67.226  1.00 29.95 ? 20  GLU C CB  1 
ATOM   3041 C  CG  . GLU C 1 23  ? 112.502 39.013  68.711  1.00 29.77 ? 20  GLU C CG  1 
ATOM   3042 C  CD  . GLU C 1 23  ? 111.146 38.365  69.048  1.00 30.74 ? 20  GLU C CD  1 
ATOM   3043 O  OE1 . GLU C 1 23  ? 110.413 37.926  68.127  1.00 31.59 ? 20  GLU C OE1 1 
ATOM   3044 O  OE2 . GLU C 1 23  ? 110.805 38.297  70.252  1.00 33.42 ? 20  GLU C OE2 1 
ATOM   3045 N  N   . LEU C 1 24  ? 113.795 39.919  64.321  1.00 28.58 ? 21  LEU C N   1 
ATOM   3046 C  CA  . LEU C 1 24  ? 114.221 39.676  62.943  1.00 27.74 ? 21  LEU C CA  1 
ATOM   3047 C  C   . LEU C 1 24  ? 115.417 40.536  62.521  1.00 27.54 ? 21  LEU C C   1 
ATOM   3048 O  O   . LEU C 1 24  ? 116.304 40.053  61.798  1.00 27.77 ? 21  LEU C O   1 
ATOM   3049 C  CB  . LEU C 1 24  ? 113.062 39.842  61.974  1.00 27.33 ? 21  LEU C CB  1 
ATOM   3050 C  CG  . LEU C 1 24  ? 111.922 38.851  62.156  1.00 27.08 ? 21  LEU C CG  1 
ATOM   3051 C  CD1 . LEU C 1 24  ? 110.656 39.429  61.539  1.00 26.96 ? 21  LEU C CD1 1 
ATOM   3052 C  CD2 . LEU C 1 24  ? 112.283 37.528  61.514  1.00 26.82 ? 21  LEU C CD2 1 
ATOM   3053 N  N   . VAL C 1 25  ? 115.448 41.792  62.975  1.00 26.89 ? 22  VAL C N   1 
ATOM   3054 C  CA  . VAL C 1 25  ? 116.620 42.667  62.799  1.00 26.54 ? 22  VAL C CA  1 
ATOM   3055 C  C   . VAL C 1 25  ? 117.878 42.007  63.375  1.00 26.73 ? 22  VAL C C   1 
ATOM   3056 O  O   . VAL C 1 25  ? 118.872 41.835  62.665  1.00 26.72 ? 22  VAL C O   1 
ATOM   3057 C  CB  . VAL C 1 25  ? 116.407 44.080  63.428  1.00 26.55 ? 22  VAL C CB  1 
ATOM   3058 C  CG1 . VAL C 1 25  ? 117.652 44.950  63.257  1.00 25.58 ? 22  VAL C CG1 1 
ATOM   3059 C  CG2 . VAL C 1 25  ? 115.205 44.766  62.808  1.00 26.53 ? 22  VAL C CG2 1 
ATOM   3060 N  N   . ALA C 1 26  ? 117.807 41.622  64.649  1.00 26.61 ? 23  ALA C N   1 
ATOM   3061 C  CA  . ALA C 1 26  ? 118.868 40.885  65.322  1.00 27.31 ? 23  ALA C CA  1 
ATOM   3062 C  C   . ALA C 1 26  ? 119.362 39.650  64.531  1.00 28.02 ? 23  ALA C C   1 
ATOM   3063 O  O   . ALA C 1 26  ? 120.572 39.465  64.320  1.00 28.08 ? 23  ALA C O   1 
ATOM   3064 C  CB  . ALA C 1 26  ? 118.406 40.471  66.719  1.00 27.00 ? 23  ALA C CB  1 
ATOM   3065 N  N   . GLU C 1 27  ? 118.426 38.803  64.115  1.00 28.54 ? 24  GLU C N   1 
ATOM   3066 C  CA  . GLU C 1 27  ? 118.729 37.636  63.291  1.00 29.42 ? 24  GLU C CA  1 
ATOM   3067 C  C   . GLU C 1 27  ? 119.499 38.029  62.028  1.00 28.92 ? 24  GLU C C   1 
ATOM   3068 O  O   . GLU C 1 27  ? 120.505 37.417  61.689  1.00 28.87 ? 24  GLU C O   1 
ATOM   3069 C  CB  . GLU C 1 27  ? 117.423 36.938  62.907  1.00 29.62 ? 24  GLU C CB  1 
ATOM   3070 C  CG  . GLU C 1 27  ? 117.565 35.773  61.942  1.00 30.88 ? 24  GLU C CG  1 
ATOM   3071 C  CD  . GLU C 1 27  ? 116.221 35.273  61.446  1.00 31.73 ? 24  GLU C CD  1 
ATOM   3072 O  OE1 . GLU C 1 27  ? 116.128 34.915  60.245  1.00 34.80 ? 24  GLU C OE1 1 
ATOM   3073 O  OE2 . GLU C 1 27  ? 115.256 35.257  62.253  1.00 35.01 ? 24  GLU C OE2 1 
ATOM   3074 N  N   . GLY C 1 28  ? 119.022 39.059  61.335  1.00 28.74 ? 25  GLY C N   1 
ATOM   3075 C  CA  . GLY C 1 28  ? 119.722 39.553  60.163  1.00 28.41 ? 25  GLY C CA  1 
ATOM   3076 C  C   . GLY C 1 28  ? 121.160 39.948  60.453  1.00 27.69 ? 25  GLY C C   1 
ATOM   3077 O  O   . GLY C 1 28  ? 122.054 39.696  59.651  1.00 27.94 ? 25  GLY C O   1 
ATOM   3078 N  N   . ALA C 1 29  ? 121.374 40.556  61.609  1.00 27.62 ? 26  ALA C N   1 
ATOM   3079 C  CA  . ALA C 1 29  ? 122.687 41.009  62.009  1.00 27.54 ? 26  ALA C CA  1 
ATOM   3080 C  C   . ALA C 1 29  ? 123.545 39.802  62.326  1.00 28.15 ? 26  ALA C C   1 
ATOM   3081 O  O   . ALA C 1 29  ? 124.664 39.706  61.835  1.00 28.63 ? 26  ALA C O   1 
ATOM   3082 C  CB  . ALA C 1 29  ? 122.590 41.952  63.169  1.00 26.72 ? 26  ALA C CB  1 
ATOM   3083 N  N   . ARG C 1 30  ? 123.003 38.856  63.095  1.00 28.70 ? 27  ARG C N   1 
ATOM   3084 C  CA  . ARG C 1 30  ? 123.683 37.577  63.362  1.00 29.07 ? 27  ARG C CA  1 
ATOM   3085 C  C   . ARG C 1 30  ? 124.025 36.776  62.099  1.00 29.55 ? 27  ARG C C   1 
ATOM   3086 O  O   . ARG C 1 30  ? 125.062 36.134  62.041  1.00 29.00 ? 27  ARG C O   1 
ATOM   3087 C  CB  . ARG C 1 30  ? 122.877 36.710  64.322  1.00 28.62 ? 27  ARG C CB  1 
ATOM   3088 C  CG  . ARG C 1 30  ? 123.039 37.107  65.767  1.00 29.36 ? 27  ARG C CG  1 
ATOM   3089 C  CD  . ARG C 1 30  ? 122.348 36.126  66.696  1.00 30.91 ? 27  ARG C CD  1 
ATOM   3090 N  NE  . ARG C 1 30  ? 120.895 36.191  66.571  1.00 32.38 ? 27  ARG C NE  1 
ATOM   3091 C  CZ  . ARG C 1 30  ? 120.095 36.854  67.405  1.00 34.11 ? 27  ARG C CZ  1 
ATOM   3092 N  NH1 . ARG C 1 30  ? 118.783 36.849  67.185  1.00 34.20 ? 27  ARG C NH1 1 
ATOM   3093 N  NH2 . ARG C 1 30  ? 120.594 37.511  68.463  1.00 33.67 ? 27  ARG C NH2 1 
ATOM   3094 N  N   . SER C 1 31  ? 123.171 36.833  61.082  1.00 30.53 ? 28  SER C N   1 
ATOM   3095 C  CA  . SER C 1 31  ? 123.425 36.066  59.855  1.00 31.55 ? 28  SER C CA  1 
ATOM   3096 C  C   . SER C 1 31  ? 124.787 36.391  59.229  1.00 31.81 ? 28  SER C C   1 
ATOM   3097 O  O   . SER C 1 31  ? 125.334 35.565  58.494  1.00 32.01 ? 28  SER C O   1 
ATOM   3098 C  CB  . SER C 1 31  ? 122.290 36.238  58.832  1.00 31.67 ? 28  SER C CB  1 
ATOM   3099 O  OG  . SER C 1 31  ? 122.382 37.478  58.152  1.00 32.10 ? 28  SER C OG  1 
ATOM   3100 N  N   . LEU C 1 32  ? 125.323 37.584  59.515  1.00 32.41 ? 29  LEU C N   1 
ATOM   3101 C  CA  . LEU C 1 32  ? 126.698 37.919  59.125  1.00 32.88 ? 29  LEU C CA  1 
ATOM   3102 C  C   . LEU C 1 32  ? 127.727 37.411  60.142  1.00 33.71 ? 29  LEU C C   1 
ATOM   3103 O  O   . LEU C 1 32  ? 127.734 37.792  61.319  1.00 33.83 ? 29  LEU C O   1 
ATOM   3104 C  CB  . LEU C 1 32  ? 126.912 39.411  58.827  1.00 32.62 ? 29  LEU C CB  1 
ATOM   3105 C  CG  . LEU C 1 32  ? 128.294 39.721  58.211  1.00 32.06 ? 29  LEU C CG  1 
ATOM   3106 C  CD1 . LEU C 1 32  ? 128.414 39.239  56.748  1.00 29.81 ? 29  LEU C CD1 1 
ATOM   3107 C  CD2 . LEU C 1 32  ? 128.658 41.202  58.332  1.00 30.73 ? 29  LEU C CD2 1 
ATOM   3108 N  N   . GLU C 1 33  ? 128.603 36.559  59.628  1.00 34.08 ? 30  GLU C N   1 
ATOM   3109 C  CA  . GLU C 1 33  ? 129.584 35.809  60.379  1.00 34.81 ? 30  GLU C CA  1 
ATOM   3110 C  C   . GLU C 1 33  ? 130.593 36.687  61.160  1.00 34.45 ? 30  GLU C C   1 
ATOM   3111 O  O   . GLU C 1 33  ? 131.259 37.555  60.583  1.00 34.54 ? 30  GLU C O   1 
ATOM   3112 C  CB  . GLU C 1 33  ? 130.292 34.858  59.400  1.00 35.10 ? 30  GLU C CB  1 
ATOM   3113 C  CG  . GLU C 1 33  ? 129.318 34.144  58.365  1.00 37.89 ? 30  GLU C CG  1 
ATOM   3114 C  CD  . GLU C 1 33  ? 128.853 35.027  57.144  1.00 39.21 ? 30  GLU C CD  1 
ATOM   3115 O  OE1 . GLU C 1 33  ? 127.663 34.919  56.726  1.00 38.84 ? 30  GLU C OE1 1 
ATOM   3116 O  OE2 . GLU C 1 33  ? 129.677 35.810  56.600  1.00 38.43 ? 30  GLU C OE2 1 
ATOM   3117 N  N   . GLY C 1 34  ? 130.693 36.447  62.473  1.00 34.00 ? 31  GLY C N   1 
ATOM   3118 C  CA  . GLY C 1 34  ? 131.583 37.206  63.355  1.00 33.36 ? 31  GLY C CA  1 
ATOM   3119 C  C   . GLY C 1 34  ? 130.903 38.362  64.081  1.00 33.32 ? 31  GLY C C   1 
ATOM   3120 O  O   . GLY C 1 34  ? 131.524 39.013  64.930  1.00 33.54 ? 31  GLY C O   1 
ATOM   3121 N  N   . THR C 1 35  ? 129.635 38.618  63.743  1.00 32.63 ? 32  THR C N   1 
ATOM   3122 C  CA  . THR C 1 35  ? 128.840 39.686  64.363  1.00 32.32 ? 32  THR C CA  1 
ATOM   3123 C  C   . THR C 1 35  ? 128.257 39.219  65.689  1.00 32.06 ? 32  THR C C   1 
ATOM   3124 O  O   . THR C 1 35  ? 127.528 38.229  65.733  1.00 32.25 ? 32  THR C O   1 
ATOM   3125 C  CB  . THR C 1 35  ? 127.655 40.120  63.451  1.00 31.82 ? 32  THR C CB  1 
ATOM   3126 O  OG1 . THR C 1 35  ? 128.155 40.662  62.234  1.00 32.21 ? 32  THR C OG1 1 
ATOM   3127 C  CG2 . THR C 1 35  ? 126.822 41.157  64.105  1.00 31.46 ? 32  THR C CG2 1 
ATOM   3128 N  N   . GLU C 1 36  ? 128.580 39.935  66.763  1.00 31.79 ? 33  GLU C N   1 
ATOM   3129 C  CA  . GLU C 1 36  ? 127.937 39.735  68.059  1.00 31.59 ? 33  GLU C CA  1 
ATOM   3130 C  C   . GLU C 1 36  ? 126.759 40.717  68.142  1.00 30.92 ? 33  GLU C C   1 
ATOM   3131 O  O   . GLU C 1 36  ? 126.860 41.867  67.707  1.00 30.91 ? 33  GLU C O   1 
ATOM   3132 C  CB  . GLU C 1 36  ? 128.947 39.967  69.187  1.00 31.56 ? 33  GLU C CB  1 
ATOM   3133 C  CG  . GLU C 1 36  ? 128.519 39.489  70.582  1.00 32.38 ? 33  GLU C CG  1 
ATOM   3134 C  CD  . GLU C 1 36  ? 129.597 39.745  71.648  1.00 32.91 ? 33  GLU C CD  1 
ATOM   3135 O  OE1 . GLU C 1 36  ? 129.239 40.000  72.825  1.00 33.69 ? 33  GLU C OE1 1 
ATOM   3136 O  OE2 . GLU C 1 36  ? 130.805 39.691  71.306  1.00 34.77 ? 33  GLU C OE2 1 
ATOM   3137 N  N   . VAL C 1 37  ? 125.636 40.248  68.676  1.00 30.17 ? 34  VAL C N   1 
ATOM   3138 C  CA  . VAL C 1 37  ? 124.401 41.016  68.672  1.00 29.29 ? 34  VAL C CA  1 
ATOM   3139 C  C   . VAL C 1 37  ? 123.761 40.999  70.053  1.00 29.21 ? 34  VAL C C   1 
ATOM   3140 O  O   . VAL C 1 37  ? 123.572 39.927  70.629  1.00 28.05 ? 34  VAL C O   1 
ATOM   3141 C  CB  . VAL C 1 37  ? 123.384 40.480  67.599  1.00 29.33 ? 34  VAL C CB  1 
ATOM   3142 C  CG1 . VAL C 1 37  ? 121.997 41.123  67.758  1.00 28.43 ? 34  VAL C CG1 1 
ATOM   3143 C  CG2 . VAL C 1 37  ? 123.900 40.726  66.196  1.00 28.38 ? 34  VAL C CG2 1 
ATOM   3144 N  N   . ARG C 1 38  ? 123.425 42.188  70.576  1.00 29.05 ? 35  ARG C N   1 
ATOM   3145 C  CA  . ARG C 1 38  ? 122.587 42.281  71.774  1.00 29.25 ? 35  ARG C CA  1 
ATOM   3146 C  C   . ARG C 1 38  ? 121.214 42.759  71.368  1.00 29.78 ? 35  ARG C C   1 
ATOM   3147 O  O   . ARG C 1 38  ? 121.086 43.716  70.590  1.00 30.48 ? 35  ARG C O   1 
ATOM   3148 C  CB  . ARG C 1 38  ? 123.160 43.233  72.826  1.00 28.79 ? 35  ARG C CB  1 
ATOM   3149 C  CG  . ARG C 1 38  ? 124.392 42.745  73.518  1.00 28.71 ? 35  ARG C CG  1 
ATOM   3150 C  CD  . ARG C 1 38  ? 124.962 43.813  74.433  1.00 27.86 ? 35  ARG C CD  1 
ATOM   3151 N  NE  . ARG C 1 38  ? 126.235 43.365  74.977  1.00 29.04 ? 35  ARG C NE  1 
ATOM   3152 C  CZ  . ARG C 1 38  ? 127.059 44.085  75.738  1.00 27.76 ? 35  ARG C CZ  1 
ATOM   3153 N  NH1 . ARG C 1 38  ? 128.191 43.531  76.159  1.00 23.66 ? 35  ARG C NH1 1 
ATOM   3154 N  NH2 . ARG C 1 38  ? 126.761 45.340  76.077  1.00 26.22 ? 35  ARG C NH2 1 
ATOM   3155 N  N   . LEU C 1 39  ? 120.194 42.102  71.914  1.00 30.11 ? 36  LEU C N   1 
ATOM   3156 C  CA  . LEU C 1 39  ? 118.803 42.494  71.722  1.00 30.58 ? 36  LEU C CA  1 
ATOM   3157 C  C   . LEU C 1 39  ? 118.181 42.989  73.049  1.00 30.74 ? 36  LEU C C   1 
ATOM   3158 O  O   . LEU C 1 39  ? 117.925 42.198  73.955  1.00 30.72 ? 36  LEU C O   1 
ATOM   3159 C  CB  . LEU C 1 39  ? 117.995 41.339  71.094  1.00 30.26 ? 36  LEU C CB  1 
ATOM   3160 C  CG  . LEU C 1 39  ? 116.472 41.529  70.928  1.00 30.67 ? 36  LEU C CG  1 
ATOM   3161 C  CD1 . LEU C 1 39  ? 116.150 42.590  69.892  1.00 28.67 ? 36  LEU C CD1 1 
ATOM   3162 C  CD2 . LEU C 1 39  ? 115.736 40.224  70.614  1.00 30.66 ? 36  LEU C CD2 1 
ATOM   3163 N  N   . LYS C 1 40  ? 117.941 44.296  73.155  1.00 30.91 ? 37  LYS C N   1 
ATOM   3164 C  CA  . LYS C 1 40  ? 117.422 44.878  74.396  1.00 31.48 ? 37  LYS C CA  1 
ATOM   3165 C  C   . LYS C 1 40  ? 116.152 45.699  74.190  1.00 31.81 ? 37  LYS C C   1 
ATOM   3166 O  O   . LYS C 1 40  ? 116.070 46.535  73.277  1.00 31.66 ? 37  LYS C O   1 
ATOM   3167 C  CB  . LYS C 1 40  ? 118.482 45.773  75.068  1.00 31.47 ? 37  LYS C CB  1 
ATOM   3168 C  CG  . LYS C 1 40  ? 119.889 45.168  75.219  1.00 32.00 ? 37  LYS C CG  1 
ATOM   3169 C  CD  . LYS C 1 40  ? 120.130 44.532  76.583  1.00 33.26 ? 37  LYS C CD  1 
ATOM   3170 C  CE  . LYS C 1 40  ? 119.843 43.047  76.591  1.00 33.62 ? 37  LYS C CE  1 
ATOM   3171 N  NZ  . LYS C 1 40  ? 120.703 42.350  77.591  1.00 34.98 ? 37  LYS C NZ  1 
ATOM   3172 N  N   . HIS C 1 41  ? 115.164 45.445  75.044  1.00 32.19 ? 38  HIS C N   1 
ATOM   3173 C  CA  . HIS C 1 41  ? 114.032 46.357  75.267  1.00 32.42 ? 38  HIS C CA  1 
ATOM   3174 C  C   . HIS C 1 41  ? 114.604 47.628  75.932  1.00 32.19 ? 38  HIS C C   1 
ATOM   3175 O  O   . HIS C 1 41  ? 115.581 47.512  76.691  1.00 32.11 ? 38  HIS C O   1 
ATOM   3176 C  CB  . HIS C 1 41  ? 113.031 45.673  76.216  1.00 32.19 ? 38  HIS C CB  1 
ATOM   3177 C  CG  . HIS C 1 41  ? 111.689 46.336  76.284  1.00 33.54 ? 38  HIS C CG  1 
ATOM   3178 N  ND1 . HIS C 1 41  ? 111.524 47.666  76.605  1.00 34.47 ? 38  HIS C ND1 1 
ATOM   3179 C  CD2 . HIS C 1 41  ? 110.444 45.841  76.083  1.00 34.99 ? 38  HIS C CD2 1 
ATOM   3180 C  CE1 . HIS C 1 41  ? 110.237 47.966  76.579  1.00 35.19 ? 38  HIS C CE1 1 
ATOM   3181 N  NE2 . HIS C 1 41  ? 109.560 46.875  76.268  1.00 34.29 ? 38  HIS C NE2 1 
ATOM   3182 N  N   . VAL C 1 42  ? 114.016 48.810  75.687  1.00 31.69 ? 39  VAL C N   1 
ATOM   3183 C  CA  . VAL C 1 42  ? 114.513 50.057  76.340  1.00 31.92 ? 39  VAL C CA  1 
ATOM   3184 C  C   . VAL C 1 42  ? 114.551 49.966  77.844  1.00 32.52 ? 39  VAL C C   1 
ATOM   3185 O  O   . VAL C 1 42  ? 115.351 50.664  78.483  1.00 33.27 ? 39  VAL C O   1 
ATOM   3186 C  CB  . VAL C 1 42  ? 113.714 51.367  76.047  1.00 31.08 ? 39  VAL C CB  1 
ATOM   3187 C  CG1 . VAL C 1 42  ? 114.236 52.034  74.849  1.00 30.74 ? 39  VAL C CG1 1 
ATOM   3188 C  CG2 . VAL C 1 42  ? 112.197 51.131  76.000  1.00 30.53 ? 39  VAL C CG2 1 
ATOM   3189 N  N   . ASP C 1 43  ? 113.669 49.142  78.408  1.00 32.94 ? 40  ASP C N   1 
ATOM   3190 C  CA  . ASP C 1 43  ? 113.575 49.037  79.861  1.00 33.95 ? 40  ASP C CA  1 
ATOM   3191 C  C   . ASP C 1 43  ? 114.787 48.315  80.474  1.00 33.77 ? 40  ASP C C   1 
ATOM   3192 O  O   . ASP C 1 43  ? 115.090 48.504  81.656  1.00 34.79 ? 40  ASP C O   1 
ATOM   3193 C  CB  . ASP C 1 43  ? 112.255 48.378  80.280  1.00 34.31 ? 40  ASP C CB  1 
ATOM   3194 C  CG  . ASP C 1 43  ? 111.027 49.280  80.035  1.00 36.79 ? 40  ASP C CG  1 
ATOM   3195 O  OD1 . ASP C 1 43  ? 109.887 48.748  80.079  1.00 38.80 ? 40  ASP C OD1 1 
ATOM   3196 O  OD2 . ASP C 1 43  ? 111.181 50.509  79.800  1.00 38.87 ? 40  ASP C OD2 1 
ATOM   3197 N  N   . GLU C 1 44  ? 115.477 47.498  79.679  1.00 32.87 ? 41  GLU C N   1 
ATOM   3198 C  CA  . GLU C 1 44  ? 116.637 46.768  80.163  1.00 32.38 ? 41  GLU C CA  1 
ATOM   3199 C  C   . GLU C 1 44  ? 117.938 47.231  79.515  1.00 31.89 ? 41  GLU C C   1 
ATOM   3200 O  O   . GLU C 1 44  ? 119.025 46.790  79.889  1.00 31.76 ? 41  GLU C O   1 
ATOM   3201 C  CB  . GLU C 1 44  ? 116.425 45.260  79.989  1.00 32.76 ? 41  GLU C CB  1 
ATOM   3202 C  CG  . GLU C 1 44  ? 115.463 44.926  78.860  1.00 33.30 ? 41  GLU C CG  1 
ATOM   3203 C  CD  . GLU C 1 44  ? 115.621 43.523  78.329  1.00 32.30 ? 41  GLU C CD  1 
ATOM   3204 O  OE1 . GLU C 1 44  ? 116.192 42.701  79.078  1.00 33.36 ? 41  GLU C OE1 1 
ATOM   3205 O  OE2 . GLU C 1 44  ? 115.185 43.250  77.170  1.00 29.82 ? 41  GLU C OE2 1 
ATOM   3206 N  N   . ALA C 1 45  ? 117.814 48.139  78.547  1.00 31.92 ? 42  ALA C N   1 
ATOM   3207 C  CA  . ALA C 1 45  ? 118.959 48.753  77.882  1.00 31.20 ? 42  ALA C CA  1 
ATOM   3208 C  C   . ALA C 1 45  ? 119.708 49.674  78.861  1.00 31.24 ? 42  ALA C C   1 
ATOM   3209 O  O   . ALA C 1 45  ? 119.082 50.282  79.744  1.00 31.18 ? 42  ALA C O   1 
ATOM   3210 C  CB  . ALA C 1 45  ? 118.491 49.505  76.686  1.00 30.69 ? 42  ALA C CB  1 
ATOM   3211 N  N   . THR C 1 46  ? 121.035 49.742  78.726  1.00 30.81 ? 43  THR C N   1 
ATOM   3212 C  CA  . THR C 1 46  ? 121.887 50.584  79.592  1.00 30.57 ? 43  THR C CA  1 
ATOM   3213 C  C   . THR C 1 46  ? 122.839 51.430  78.737  1.00 30.73 ? 43  THR C C   1 
ATOM   3214 O  O   . THR C 1 46  ? 123.093 51.089  77.585  1.00 30.21 ? 43  THR C O   1 
ATOM   3215 C  CB  . THR C 1 46  ? 122.792 49.739  80.521  1.00 30.27 ? 43  THR C CB  1 
ATOM   3216 O  OG1 . THR C 1 46  ? 123.679 48.956  79.708  1.00 29.86 ? 43  THR C OG1 1 
ATOM   3217 C  CG2 . THR C 1 46  ? 121.974 48.825  81.442  1.00 29.54 ? 43  THR C CG2 1 
ATOM   3218 N  N   . LYS C 1 47  ? 123.413 52.488  79.307  1.00 31.02 ? 44  LYS C N   1 
ATOM   3219 C  CA  . LYS C 1 47  ? 124.362 53.297  78.546  1.00 31.92 ? 44  LYS C CA  1 
ATOM   3220 C  C   . LYS C 1 47  ? 125.642 52.523  78.183  1.00 31.93 ? 44  LYS C C   1 
ATOM   3221 O  O   . LYS C 1 47  ? 126.341 52.885  77.220  1.00 31.97 ? 44  LYS C O   1 
ATOM   3222 C  CB  . LYS C 1 47  ? 124.642 54.669  79.206  1.00 32.12 ? 44  LYS C CB  1 
ATOM   3223 C  CG  . LYS C 1 47  ? 125.200 54.650  80.618  1.00 33.16 ? 44  LYS C CG  1 
ATOM   3224 C  CD  . LYS C 1 47  ? 125.486 56.089  81.121  1.00 33.24 ? 44  LYS C CD  1 
ATOM   3225 C  CE  . LYS C 1 47  ? 126.099 56.095  82.537  1.00 35.09 ? 44  LYS C CE  1 
ATOM   3226 N  NZ  . LYS C 1 47  ? 126.639 57.447  82.898  1.00 37.26 ? 44  LYS C NZ  1 
ATOM   3227 N  N   . GLU C 1 48  ? 125.927 51.452  78.934  1.00 31.71 ? 45  GLU C N   1 
ATOM   3228 C  CA  . GLU C 1 48  ? 127.089 50.595  78.667  1.00 31.42 ? 45  GLU C CA  1 
ATOM   3229 C  C   . GLU C 1 48  ? 126.880 49.688  77.431  1.00 30.49 ? 45  GLU C C   1 
ATOM   3230 O  O   . GLU C 1 48  ? 127.842 49.359  76.734  1.00 30.28 ? 45  GLU C O   1 
ATOM   3231 C  CB  . GLU C 1 48  ? 127.509 49.805  79.921  1.00 31.72 ? 45  GLU C CB  1 
ATOM   3232 C  CG  . GLU C 1 48  ? 127.983 50.685  81.129  1.00 34.90 ? 45  GLU C CG  1 
ATOM   3233 C  CD  . GLU C 1 48  ? 126.834 51.359  81.943  1.00 38.81 ? 45  GLU C CD  1 
ATOM   3234 O  OE1 . GLU C 1 48  ? 125.701 50.812  81.991  1.00 39.43 ? 45  GLU C OE1 1 
ATOM   3235 O  OE2 . GLU C 1 48  ? 127.073 52.444  82.547  1.00 39.35 ? 45  GLU C OE2 1 
ATOM   3236 N  N   . ASP C 1 49  ? 125.632 49.302  77.162  1.00 29.93 ? 46  ASP C N   1 
ATOM   3237 C  CA  . ASP C 1 49  ? 125.229 48.714  75.857  1.00 29.88 ? 46  ASP C CA  1 
ATOM   3238 C  C   . ASP C 1 49  ? 125.563 49.592  74.650  1.00 29.04 ? 46  ASP C C   1 
ATOM   3239 O  O   . ASP C 1 49  ? 126.140 49.131  73.676  1.00 29.62 ? 46  ASP C O   1 
ATOM   3240 C  CB  . ASP C 1 49  ? 123.718 48.434  75.813  1.00 29.81 ? 46  ASP C CB  1 
ATOM   3241 C  CG  . ASP C 1 49  ? 123.307 47.270  76.696  1.00 31.48 ? 46  ASP C CG  1 
ATOM   3242 O  OD1 . ASP C 1 49  ? 124.088 46.292  76.801  1.00 32.98 ? 46  ASP C OD1 1 
ATOM   3243 O  OD2 . ASP C 1 49  ? 122.199 47.341  77.281  1.00 32.19 ? 46  ASP C OD2 1 
ATOM   3244 N  N   . VAL C 1 50  ? 125.170 50.856  74.719  1.00 28.41 ? 47  VAL C N   1 
ATOM   3245 C  CA  . VAL C 1 50  ? 125.434 51.816  73.655  1.00 27.33 ? 47  VAL C CA  1 
ATOM   3246 C  C   . VAL C 1 50  ? 126.942 52.067  73.519  1.00 27.22 ? 47  VAL C C   1 
ATOM   3247 O  O   . VAL C 1 50  ? 127.436 52.269  72.420  1.00 27.71 ? 47  VAL C O   1 
ATOM   3248 C  CB  . VAL C 1 50  ? 124.676 53.125  73.926  1.00 27.04 ? 47  VAL C CB  1 
ATOM   3249 C  CG1 . VAL C 1 50  ? 125.014 54.184  72.892  1.00 25.87 ? 47  VAL C CG1 1 
ATOM   3250 C  CG2 . VAL C 1 50  ? 123.199 52.846  73.949  1.00 26.84 ? 47  VAL C CG2 1 
ATOM   3251 N  N   . LEU C 1 51  ? 127.669 52.041  74.633  1.00 26.21 ? 48  LEU C N   1 
ATOM   3252 C  CA  . LEU C 1 51  ? 129.117 52.164  74.595  1.00 25.47 ? 48  LEU C CA  1 
ATOM   3253 C  C   . LEU C 1 51  ? 129.784 50.928  74.000  1.00 25.48 ? 48  LEU C C   1 
ATOM   3254 O  O   . LEU C 1 51  ? 130.800 51.041  73.312  1.00 25.12 ? 48  LEU C O   1 
ATOM   3255 C  CB  . LEU C 1 51  ? 129.676 52.443  75.994  1.00 24.88 ? 48  LEU C CB  1 
ATOM   3256 C  CG  . LEU C 1 51  ? 129.400 53.813  76.618  1.00 23.58 ? 48  LEU C CG  1 
ATOM   3257 C  CD1 . LEU C 1 51  ? 129.663 53.783  78.148  1.00 20.78 ? 48  LEU C CD1 1 
ATOM   3258 C  CD2 . LEU C 1 51  ? 130.216 54.905  75.940  1.00 21.33 ? 48  LEU C CD2 1 
ATOM   3259 N  N   . TRP C 1 52  ? 129.216 49.753  74.277  1.00 25.79 ? 49  TRP C N   1 
ATOM   3260 C  CA  . TRP C 1 52  ? 129.719 48.489  73.729  1.00 25.93 ? 49  TRP C CA  1 
ATOM   3261 C  C   . TRP C 1 52  ? 129.499 48.406  72.209  1.00 26.41 ? 49  TRP C C   1 
ATOM   3262 O  O   . TRP C 1 52  ? 130.328 47.867  71.475  1.00 26.97 ? 49  TRP C O   1 
ATOM   3263 C  CB  . TRP C 1 52  ? 129.072 47.311  74.463  1.00 25.76 ? 49  TRP C CB  1 
ATOM   3264 C  CG  . TRP C 1 52  ? 129.237 45.953  73.802  1.00 26.35 ? 49  TRP C CG  1 
ATOM   3265 C  CD1 . TRP C 1 52  ? 130.251 45.045  74.015  1.00 25.95 ? 49  TRP C CD1 1 
ATOM   3266 C  CD2 . TRP C 1 52  ? 128.351 45.346  72.838  1.00 26.20 ? 49  TRP C CD2 1 
ATOM   3267 N  NE1 . TRP C 1 52  ? 130.051 43.926  73.240  1.00 25.76 ? 49  TRP C NE1 1 
ATOM   3268 C  CE2 . TRP C 1 52  ? 128.899 44.077  72.508  1.00 26.65 ? 49  TRP C CE2 1 
ATOM   3269 C  CE3 . TRP C 1 52  ? 127.150 45.751  72.222  1.00 25.65 ? 49  TRP C CE3 1 
ATOM   3270 C  CZ2 . TRP C 1 52  ? 128.287 43.202  71.578  1.00 25.64 ? 49  TRP C CZ2 1 
ATOM   3271 C  CZ3 . TRP C 1 52  ? 126.542 44.886  71.297  1.00 25.91 ? 49  TRP C CZ3 1 
ATOM   3272 C  CH2 . TRP C 1 52  ? 127.117 43.621  70.988  1.00 26.24 ? 49  TRP C CH2 1 
ATOM   3273 N  N   . ALA C 1 53  ? 128.389 48.954  71.744  1.00 26.51 ? 50  ALA C N   1 
ATOM   3274 C  CA  . ALA C 1 53  ? 127.975 48.822  70.351  1.00 27.56 ? 50  ALA C CA  1 
ATOM   3275 C  C   . ALA C 1 53  ? 128.828 49.583  69.321  1.00 28.02 ? 50  ALA C C   1 
ATOM   3276 O  O   . ALA C 1 53  ? 129.189 50.732  69.526  1.00 28.11 ? 50  ALA C O   1 
ATOM   3277 C  CB  . ALA C 1 53  ? 126.494 49.220  70.221  1.00 26.85 ? 50  ALA C CB  1 
ATOM   3278 N  N   . ASP C 1 54  ? 129.138 48.932  68.208  1.00 29.13 ? 51  ASP C N   1 
ATOM   3279 C  CA  . ASP C 1 54  ? 129.669 49.632  67.034  1.00 30.60 ? 51  ASP C CA  1 
ATOM   3280 C  C   . ASP C 1 54  ? 128.550 50.195  66.179  1.00 30.96 ? 51  ASP C C   1 
ATOM   3281 O  O   . ASP C 1 54  ? 128.699 51.250  65.561  1.00 31.60 ? 51  ASP C O   1 
ATOM   3282 C  CB  . ASP C 1 54  ? 130.499 48.696  66.163  1.00 30.86 ? 51  ASP C CB  1 
ATOM   3283 C  CG  . ASP C 1 54  ? 131.659 48.105  66.899  1.00 32.88 ? 51  ASP C CG  1 
ATOM   3284 O  OD1 . ASP C 1 54  ? 132.344 48.847  67.643  1.00 36.29 ? 51  ASP C OD1 1 
ATOM   3285 O  OD2 . ASP C 1 54  ? 131.887 46.888  66.731  1.00 35.71 ? 51  ASP C OD2 1 
ATOM   3286 N  N   . GLY C 1 55  ? 127.445 49.460  66.133  1.00 31.35 ? 52  GLY C N   1 
ATOM   3287 C  CA  . GLY C 1 55  ? 126.280 49.814  65.336  1.00 31.34 ? 52  GLY C CA  1 
ATOM   3288 C  C   . GLY C 1 55  ? 125.004 49.531  66.103  1.00 31.40 ? 52  GLY C C   1 
ATOM   3289 O  O   . GLY C 1 55  ? 124.973 48.622  66.949  1.00 31.21 ? 52  GLY C O   1 
ATOM   3290 N  N   . LEU C 1 56  ? 123.965 50.327  65.817  1.00 31.13 ? 53  LEU C N   1 
ATOM   3291 C  CA  . LEU C 1 56  ? 122.684 50.258  66.518  1.00 31.25 ? 53  LEU C CA  1 
ATOM   3292 C  C   . LEU C 1 56  ? 121.517 50.243  65.542  1.00 30.74 ? 53  LEU C C   1 
ATOM   3293 O  O   . LEU C 1 56  ? 121.554 50.926  64.522  1.00 30.45 ? 53  LEU C O   1 
ATOM   3294 C  CB  . LEU C 1 56  ? 122.511 51.465  67.437  1.00 31.51 ? 53  LEU C CB  1 
ATOM   3295 C  CG  . LEU C 1 56  ? 123.220 51.640  68.768  1.00 32.66 ? 53  LEU C CG  1 
ATOM   3296 C  CD1 . LEU C 1 56  ? 124.717 51.921  68.580  1.00 34.11 ? 53  LEU C CD1 1 
ATOM   3297 C  CD2 . LEU C 1 56  ? 122.555 52.828  69.490  1.00 32.43 ? 53  LEU C CD2 1 
ATOM   3298 N  N   . ALA C 1 57  ? 120.489 49.460  65.865  1.00 30.24 ? 54  ALA C N   1 
ATOM   3299 C  CA  . ALA C 1 57  ? 119.196 49.512  65.172  1.00 29.90 ? 54  ALA C CA  1 
ATOM   3300 C  C   . ALA C 1 57  ? 118.180 49.830  66.243  1.00 29.36 ? 54  ALA C C   1 
ATOM   3301 O  O   . ALA C 1 57  ? 118.080 49.124  67.228  1.00 29.45 ? 54  ALA C O   1 
ATOM   3302 C  CB  . ALA C 1 57  ? 118.869 48.188  64.509  1.00 29.94 ? 54  ALA C CB  1 
ATOM   3303 N  N   . VAL C 1 58  ? 117.457 50.923  66.068  1.00 29.18 ? 55  VAL C N   1 
ATOM   3304 C  CA  . VAL C 1 58  ? 116.627 51.469  67.129  1.00 28.30 ? 55  VAL C CA  1 
ATOM   3305 C  C   . VAL C 1 58  ? 115.195 51.410  66.631  1.00 28.05 ? 55  VAL C C   1 
ATOM   3306 O  O   . VAL C 1 58  ? 114.900 51.914  65.533  1.00 27.91 ? 55  VAL C O   1 
ATOM   3307 C  CB  . VAL C 1 58  ? 117.078 52.915  67.510  1.00 28.44 ? 55  VAL C CB  1 
ATOM   3308 C  CG1 . VAL C 1 58  ? 116.200 53.492  68.610  1.00 27.18 ? 55  VAL C CG1 1 
ATOM   3309 C  CG2 . VAL C 1 58  ? 118.572 52.940  67.936  1.00 27.01 ? 55  VAL C CG2 1 
ATOM   3310 N  N   . GLY C 1 59  ? 114.334 50.747  67.409  1.00 27.28 ? 56  GLY C N   1 
ATOM   3311 C  CA  . GLY C 1 59  ? 112.953 50.457  66.996  1.00 27.24 ? 56  GLY C CA  1 
ATOM   3312 C  C   . GLY C 1 59  ? 111.862 50.982  67.916  1.00 26.42 ? 56  GLY C C   1 
ATOM   3313 O  O   . GLY C 1 59  ? 111.918 50.786  69.101  1.00 26.08 ? 56  GLY C O   1 
ATOM   3314 N  N   . SER C 1 60  ? 110.854 51.646  67.362  1.00 26.71 ? 57  SER C N   1 
ATOM   3315 C  CA  . SER C 1 60  ? 109.717 52.105  68.152  1.00 26.25 ? 57  SER C CA  1 
ATOM   3316 C  C   . SER C 1 60  ? 108.414 51.848  67.387  1.00 25.69 ? 57  SER C C   1 
ATOM   3317 O  O   . SER C 1 60  ? 108.411 51.856  66.157  1.00 25.90 ? 57  SER C O   1 
ATOM   3318 C  CB  . SER C 1 60  ? 109.876 53.601  68.456  1.00 26.37 ? 57  SER C CB  1 
ATOM   3319 O  OG  . SER C 1 60  ? 108.653 54.213  68.867  1.00 26.90 ? 57  SER C OG  1 
ATOM   3320 N  N   . PRO C 1 61  ? 107.303 51.628  68.106  1.00 24.99 ? 58  PRO C N   1 
ATOM   3321 C  CA  . PRO C 1 61  ? 106.026 51.773  67.426  1.00 24.39 ? 58  PRO C CA  1 
ATOM   3322 C  C   . PRO C 1 61  ? 105.906 53.184  66.834  1.00 24.25 ? 58  PRO C C   1 
ATOM   3323 O  O   . PRO C 1 61  ? 106.546 54.101  67.316  1.00 24.59 ? 58  PRO C O   1 
ATOM   3324 C  CB  . PRO C 1 61  ? 104.996 51.562  68.543  1.00 23.81 ? 58  PRO C CB  1 
ATOM   3325 C  CG  . PRO C 1 61  ? 105.737 51.647  69.795  1.00 23.95 ? 58  PRO C CG  1 
ATOM   3326 C  CD  . PRO C 1 61  ? 107.134 51.257  69.519  1.00 24.68 ? 58  PRO C CD  1 
ATOM   3327 N  N   . THR C 1 62  ? 105.128 53.343  65.770  1.00 24.11 ? 59  THR C N   1 
ATOM   3328 C  CA  . THR C 1 62  ? 104.827 54.654  65.260  1.00 24.15 ? 59  THR C CA  1 
ATOM   3329 C  C   . THR C 1 62  ? 103.793 55.263  66.208  1.00 24.73 ? 59  THR C C   1 
ATOM   3330 O  O   . THR C 1 62  ? 102.665 54.788  66.280  1.00 24.84 ? 59  THR C O   1 
ATOM   3331 C  CB  . THR C 1 62  ? 104.279 54.568  63.796  1.00 24.33 ? 59  THR C CB  1 
ATOM   3332 O  OG1 . THR C 1 62  ? 105.277 53.987  62.942  1.00 23.78 ? 59  THR C OG1 1 
ATOM   3333 C  CG2 . THR C 1 62  ? 103.865 55.939  63.272  1.00 21.72 ? 59  THR C CG2 1 
ATOM   3334 N  N   . ASN C 1 63  ? 104.180 56.279  66.971  1.00 25.38 ? 60  ASN C N   1 
ATOM   3335 C  CA  . ASN C 1 63  ? 103.223 56.893  67.899  1.00 25.58 ? 60  ASN C CA  1 
ATOM   3336 C  C   . ASN C 1 63  ? 103.006 58.346  67.525  1.00 25.34 ? 60  ASN C C   1 
ATOM   3337 O  O   . ASN C 1 63  ? 103.899 59.157  67.698  1.00 25.80 ? 60  ASN C O   1 
ATOM   3338 C  CB  . ASN C 1 63  ? 103.687 56.762  69.365  1.00 25.71 ? 60  ASN C CB  1 
ATOM   3339 C  CG  . ASN C 1 63  ? 103.548 55.332  69.932  1.00 27.12 ? 60  ASN C CG  1 
ATOM   3340 O  OD1 . ASN C 1 63  ? 104.172 55.011  70.941  1.00 28.11 ? 60  ASN C OD1 1 
ATOM   3341 N  ND2 . ASN C 1 63  ? 102.726 54.486  69.299  1.00 27.53 ? 60  ASN C ND2 1 
HETATM 3342 N  N   . MSE C 1 64  ? 101.830 58.664  67.005  1.00 25.45 ? 61  MSE C N   1 
HETATM 3343 C  CA  . MSE C 1 64  ? 101.568 59.975  66.412  1.00 26.26 ? 61  MSE C CA  1 
HETATM 3344 C  C   . MSE C 1 64  ? 102.641 60.391  65.397  1.00 25.56 ? 61  MSE C C   1 
HETATM 3345 O  O   . MSE C 1 64  ? 103.017 61.556  65.360  1.00 25.13 ? 61  MSE C O   1 
HETATM 3346 C  CB  . MSE C 1 64  ? 101.395 61.074  67.488  1.00 28.04 ? 61  MSE C CB  1 
HETATM 3347 C  CG  . MSE C 1 64  ? 100.398 60.762  68.612  1.00 30.62 ? 61  MSE C CG  1 
HETATM 3348 SE SE  . MSE C 1 64  ? 98.616  60.229  67.890  1.00 47.19 ? 61  MSE C SE  1 
HETATM 3349 C  CE  . MSE C 1 64  ? 97.679  59.624  69.752  1.00 35.17 ? 61  MSE C CE  1 
ATOM   3350 N  N   . GLY C 1 65  ? 103.121 59.434  64.589  1.00 25.22 ? 62  GLY C N   1 
ATOM   3351 C  CA  . GLY C 1 65  ? 104.177 59.638  63.572  1.00 24.64 ? 62  GLY C CA  1 
ATOM   3352 C  C   . GLY C 1 65  ? 105.612 59.766  64.084  1.00 25.27 ? 62  GLY C C   1 
ATOM   3353 O  O   . GLY C 1 65  ? 106.519 60.100  63.314  1.00 25.40 ? 62  GLY C O   1 
ATOM   3354 N  N   . LEU C 1 66  ? 105.826 59.518  65.378  1.00 24.75 ? 63  LEU C N   1 
ATOM   3355 C  CA  . LEU C 1 66  ? 107.130 59.665  66.008  1.00 24.55 ? 63  LEU C CA  1 
ATOM   3356 C  C   . LEU C 1 66  ? 107.521 58.478  66.898  1.00 25.53 ? 63  LEU C C   1 
ATOM   3357 O  O   . LEU C 1 66  ? 106.664 57.627  67.233  1.00 25.90 ? 63  LEU C O   1 
ATOM   3358 C  CB  . LEU C 1 66  ? 107.112 60.923  66.852  1.00 25.11 ? 63  LEU C CB  1 
ATOM   3359 C  CG  . LEU C 1 66  ? 106.749 62.259  66.165  1.00 23.37 ? 63  LEU C CG  1 
ATOM   3360 C  CD1 . LEU C 1 66  ? 106.673 63.323  67.208  1.00 22.73 ? 63  LEU C CD1 1 
ATOM   3361 C  CD2 . LEU C 1 66  ? 107.747 62.624  65.096  1.00 17.02 ? 63  LEU C CD2 1 
ATOM   3362 N  N   . VAL C 1 67  ? 108.814 58.403  67.253  1.00 26.11 ? 64  VAL C N   1 
ATOM   3363 C  CA  . VAL C 1 67  ? 109.304 57.557  68.357  1.00 25.85 ? 64  VAL C CA  1 
ATOM   3364 C  C   . VAL C 1 67  ? 108.399 57.674  69.559  1.00 25.96 ? 64  VAL C C   1 
ATOM   3365 O  O   . VAL C 1 67  ? 107.911 58.769  69.886  1.00 26.31 ? 64  VAL C O   1 
ATOM   3366 C  CB  . VAL C 1 67  ? 110.652 58.055  68.992  1.00 26.92 ? 64  VAL C CB  1 
ATOM   3367 C  CG1 . VAL C 1 67  ? 111.724 56.951  69.037  1.00 25.61 ? 64  VAL C CG1 1 
ATOM   3368 C  CG2 . VAL C 1 67  ? 111.132 59.386  68.457  1.00 25.91 ? 64  VAL C CG2 1 
ATOM   3369 N  N   . SER C 1 68  ? 108.234 56.568  70.274  1.00 25.69 ? 65  SER C N   1 
ATOM   3370 C  CA  . SER C 1 68  ? 107.420 56.571  71.482  1.00 24.76 ? 65  SER C CA  1 
ATOM   3371 C  C   . SER C 1 68  ? 108.033 57.528  72.515  1.00 24.35 ? 65  SER C C   1 
ATOM   3372 O  O   . SER C 1 68  ? 109.229 57.852  72.443  1.00 23.39 ? 65  SER C O   1 
ATOM   3373 C  CB  . SER C 1 68  ? 107.335 55.161  72.044  1.00 24.04 ? 65  SER C CB  1 
ATOM   3374 O  OG  . SER C 1 68  ? 108.611 54.770  72.495  1.00 24.43 ? 65  SER C OG  1 
ATOM   3375 N  N   . TRP C 1 69  ? 107.215 57.988  73.462  1.00 23.47 ? 66  TRP C N   1 
ATOM   3376 C  CA  . TRP C 1 69  ? 107.751 58.791  74.546  1.00 23.17 ? 66  TRP C CA  1 
ATOM   3377 C  C   . TRP C 1 69  ? 108.752 58.029  75.457  1.00 24.08 ? 66  TRP C C   1 
ATOM   3378 O  O   . TRP C 1 69  ? 109.705 58.637  75.952  1.00 23.97 ? 66  TRP C O   1 
ATOM   3379 C  CB  . TRP C 1 69  ? 106.654 59.492  75.345  1.00 20.89 ? 66  TRP C CB  1 
ATOM   3380 C  CG  . TRP C 1 69  ? 105.784 58.641  76.215  1.00 20.89 ? 66  TRP C CG  1 
ATOM   3381 C  CD1 . TRP C 1 69  ? 104.524 58.189  75.922  1.00 20.57 ? 66  TRP C CD1 1 
ATOM   3382 C  CD2 . TRP C 1 69  ? 106.056 58.199  77.558  1.00 19.48 ? 66  TRP C CD2 1 
ATOM   3383 N  NE1 . TRP C 1 69  ? 104.009 57.482  76.980  1.00 17.68 ? 66  TRP C NE1 1 
ATOM   3384 C  CE2 . TRP C 1 69  ? 104.922 57.470  77.997  1.00 19.45 ? 66  TRP C CE2 1 
ATOM   3385 C  CE3 . TRP C 1 69  ? 107.149 58.338  78.427  1.00 19.40 ? 66  TRP C CE3 1 
ATOM   3386 C  CZ2 . TRP C 1 69  ? 104.845 56.881  79.276  1.00 19.03 ? 66  TRP C CZ2 1 
ATOM   3387 C  CZ3 . TRP C 1 69  ? 107.076 57.745  79.693  1.00 19.42 ? 66  TRP C CZ3 1 
ATOM   3388 C  CH2 . TRP C 1 69  ? 105.928 57.027  80.102  1.00 19.62 ? 66  TRP C CH2 1 
ATOM   3389 N  N   . LYS C 1 70  ? 108.535 56.721  75.652  1.00 25.23 ? 67  LYS C N   1 
ATOM   3390 C  CA  . LYS C 1 70  ? 109.429 55.859  76.474  1.00 26.31 ? 67  LYS C CA  1 
ATOM   3391 C  C   . LYS C 1 70  ? 110.832 55.757  75.884  1.00 26.30 ? 67  LYS C C   1 
ATOM   3392 O  O   . LYS C 1 70  ? 111.813 55.866  76.600  1.00 26.07 ? 67  LYS C O   1 
ATOM   3393 C  CB  . LYS C 1 70  ? 108.826 54.452  76.684  1.00 26.68 ? 67  LYS C CB  1 
ATOM   3394 C  CG  . LYS C 1 70  ? 107.999 54.290  77.960  1.00 29.65 ? 67  LYS C CG  1 
ATOM   3395 C  CD  . LYS C 1 70  ? 106.914 53.213  77.821  1.00 36.78 ? 67  LYS C CD  1 
ATOM   3396 C  CE  . LYS C 1 70  ? 107.385 51.791  78.241  1.00 40.03 ? 67  LYS C CE  1 
ATOM   3397 N  NZ  . LYS C 1 70  ? 107.034 51.483  79.691  1.00 41.43 ? 67  LYS C NZ  1 
HETATM 3398 N  N   . MSE C 1 71  ? 110.904 55.592  74.568  1.00 27.11 ? 68  MSE C N   1 
HETATM 3399 C  CA  . MSE C 1 71  ? 112.153 55.563  73.845  1.00 28.44 ? 68  MSE C CA  1 
HETATM 3400 C  C   . MSE C 1 71  ? 112.879 56.922  73.988  1.00 27.41 ? 68  MSE C C   1 
HETATM 3401 O  O   . MSE C 1 71  ? 114.063 56.990  74.338  1.00 27.57 ? 68  MSE C O   1 
HETATM 3402 C  CB  . MSE C 1 71  ? 111.865 55.187  72.385  1.00 29.65 ? 68  MSE C CB  1 
HETATM 3403 C  CG  . MSE C 1 71  ? 113.082 55.005  71.449  1.00 38.40 ? 68  MSE C CG  1 
HETATM 3404 SE SE  . MSE C 1 71  ? 114.511 53.807  72.157  1.00 65.07 ? 68  MSE C SE  1 
HETATM 3405 C  CE  . MSE C 1 71  ? 113.911 52.088  71.273  1.00 55.59 ? 68  MSE C CE  1 
ATOM   3406 N  N   . LYS C 1 72  ? 112.141 57.995  73.739  1.00 26.29 ? 69  LYS C N   1 
ATOM   3407 C  CA  . LYS C 1 72  ? 112.600 59.376  73.912  1.00 25.10 ? 69  LYS C CA  1 
ATOM   3408 C  C   . LYS C 1 72  ? 113.129 59.688  75.333  1.00 24.31 ? 69  LYS C C   1 
ATOM   3409 O  O   . LYS C 1 72  ? 114.191 60.297  75.454  1.00 24.35 ? 69  LYS C O   1 
ATOM   3410 C  CB  . LYS C 1 72  ? 111.461 60.320  73.510  1.00 25.17 ? 69  LYS C CB  1 
ATOM   3411 C  CG  . LYS C 1 72  ? 111.838 61.759  73.293  1.00 26.32 ? 69  LYS C CG  1 
ATOM   3412 C  CD  . LYS C 1 72  ? 112.411 62.011  71.903  1.00 24.49 ? 69  LYS C CD  1 
ATOM   3413 C  CE  . LYS C 1 72  ? 113.554 63.015  71.949  1.00 23.07 ? 69  LYS C CE  1 
ATOM   3414 N  NZ  . LYS C 1 72  ? 113.276 64.278  72.718  1.00 20.45 ? 69  LYS C NZ  1 
ATOM   3415 N  N   . ARG C 1 73  ? 112.418 59.255  76.389  1.00 23.05 ? 70  ARG C N   1 
ATOM   3416 C  CA  . ARG C 1 73  ? 112.886 59.388  77.755  1.00 22.21 ? 70  ARG C CA  1 
ATOM   3417 C  C   . ARG C 1 73  ? 114.250 58.752  77.892  1.00 22.73 ? 70  ARG C C   1 
ATOM   3418 O  O   . ARG C 1 73  ? 115.162 59.336  78.528  1.00 21.39 ? 70  ARG C O   1 
ATOM   3419 C  CB  . ARG C 1 73  ? 111.986 58.646  78.739  1.00 22.46 ? 70  ARG C CB  1 
ATOM   3420 C  CG  . ARG C 1 73  ? 111.229 59.492  79.643  1.00 22.46 ? 70  ARG C CG  1 
ATOM   3421 C  CD  . ARG C 1 73  ? 111.533 59.417  81.108  1.00 22.80 ? 70  ARG C CD  1 
ATOM   3422 N  NE  . ARG C 1 73  ? 111.081 58.172  81.657  1.00 24.04 ? 70  ARG C NE  1 
ATOM   3423 C  CZ  . ARG C 1 73  ? 111.023 57.824  82.939  1.00 22.73 ? 70  ARG C CZ  1 
ATOM   3424 N  NH1 . ARG C 1 73  ? 110.669 56.589  83.182  1.00 22.18 ? 70  ARG C NH1 1 
ATOM   3425 N  NH2 . ARG C 1 73  ? 111.272 58.650  83.957  1.00 23.06 ? 70  ARG C NH2 1 
ATOM   3426 N  N   . PHE C 1 74  ? 114.371 57.539  77.329  1.00 22.45 ? 71  PHE C N   1 
ATOM   3427 C  CA  . PHE C 1 74  ? 115.589 56.764  77.468  1.00 24.07 ? 71  PHE C CA  1 
ATOM   3428 C  C   . PHE C 1 74  ? 116.790 57.519  76.881  1.00 24.66 ? 71  PHE C C   1 
ATOM   3429 O  O   . PHE C 1 74  ? 117.848 57.591  77.470  1.00 24.01 ? 71  PHE C O   1 
ATOM   3430 C  CB  . PHE C 1 74  ? 115.447 55.363  76.842  1.00 24.49 ? 71  PHE C CB  1 
ATOM   3431 C  CG  . PHE C 1 74  ? 116.685 54.529  76.983  1.00 24.20 ? 71  PHE C CG  1 
ATOM   3432 C  CD1 . PHE C 1 74  ? 116.970 53.905  78.177  1.00 23.51 ? 71  PHE C CD1 1 
ATOM   3433 C  CD2 . PHE C 1 74  ? 117.581 54.393  75.912  1.00 26.80 ? 71  PHE C CD2 1 
ATOM   3434 C  CE1 . PHE C 1 74  ? 118.120 53.152  78.331  1.00 25.31 ? 71  PHE C CE1 1 
ATOM   3435 C  CE2 . PHE C 1 74  ? 118.743 53.641  76.052  1.00 25.25 ? 71  PHE C CE2 1 
ATOM   3436 C  CZ  . PHE C 1 74  ? 119.007 53.020  77.266  1.00 25.74 ? 71  PHE C CZ  1 
ATOM   3437 N  N   . PHE C 1 75  ? 116.585 58.112  75.719  1.00 26.42 ? 72  PHE C N   1 
ATOM   3438 C  CA  . PHE C 1 75  ? 117.608 58.905  75.088  1.00 27.73 ? 72  PHE C CA  1 
ATOM   3439 C  C   . PHE C 1 75  ? 117.907 60.189  75.838  1.00 28.39 ? 72  PHE C C   1 
ATOM   3440 O  O   . PHE C 1 75  ? 119.074 60.443  76.150  1.00 28.81 ? 72  PHE C O   1 
ATOM   3441 C  CB  . PHE C 1 75  ? 117.232 59.138  73.623  1.00 28.84 ? 72  PHE C CB  1 
ATOM   3442 C  CG  . PHE C 1 75  ? 117.706 58.034  72.725  1.00 29.92 ? 72  PHE C CG  1 
ATOM   3443 C  CD1 . PHE C 1 75  ? 116.981 56.843  72.621  1.00 28.30 ? 72  PHE C CD1 1 
ATOM   3444 C  CD2 . PHE C 1 75  ? 118.911 58.167  72.020  1.00 32.27 ? 72  PHE C CD2 1 
ATOM   3445 C  CE1 . PHE C 1 75  ? 117.416 55.796  71.801  1.00 28.72 ? 72  PHE C CE1 1 
ATOM   3446 C  CE2 . PHE C 1 75  ? 119.368 57.122  71.197  1.00 33.72 ? 72  PHE C CE2 1 
ATOM   3447 C  CZ  . PHE C 1 75  ? 118.611 55.928  71.097  1.00 31.49 ? 72  PHE C CZ  1 
ATOM   3448 N  N   . ASP C 1 76  ? 116.867 60.966  76.157  1.00 28.81 ? 73  ASP C N   1 
ATOM   3449 C  CA  . ASP C 1 76  ? 117.030 62.213  76.889  1.00 30.40 ? 73  ASP C CA  1 
ATOM   3450 C  C   . ASP C 1 76  ? 117.719 61.941  78.268  1.00 30.51 ? 73  ASP C C   1 
ATOM   3451 O  O   . ASP C 1 76  ? 118.756 62.545  78.566  1.00 31.29 ? 73  ASP C O   1 
ATOM   3452 C  CB  . ASP C 1 76  ? 115.681 62.982  77.035  1.00 30.33 ? 73  ASP C CB  1 
ATOM   3453 C  CG  . ASP C 1 76  ? 115.126 63.535  75.676  1.00 35.16 ? 73  ASP C CG  1 
ATOM   3454 O  OD1 . ASP C 1 76  ? 115.902 63.554  74.678  1.00 39.82 ? 73  ASP C OD1 1 
ATOM   3455 O  OD2 . ASP C 1 76  ? 113.910 63.955  75.588  1.00 35.06 ? 73  ASP C OD2 1 
ATOM   3456 N  N   . ASP C 1 77  ? 117.187 61.000  79.058  1.00 29.97 ? 74  ASP C N   1 
ATOM   3457 C  CA  . ASP C 1 77  ? 117.602 60.815  80.463  1.00 29.64 ? 74  ASP C CA  1 
ATOM   3458 C  C   . ASP C 1 77  ? 118.776 59.892  80.702  1.00 29.46 ? 74  ASP C C   1 
ATOM   3459 O  O   . ASP C 1 77  ? 119.625 60.193  81.502  1.00 29.31 ? 74  ASP C O   1 
ATOM   3460 C  CB  . ASP C 1 77  ? 116.445 60.293  81.320  1.00 29.51 ? 74  ASP C CB  1 
ATOM   3461 C  CG  . ASP C 1 77  ? 115.367 61.330  81.565  1.00 29.11 ? 74  ASP C CG  1 
ATOM   3462 O  OD1 . ASP C 1 77  ? 115.415 62.452  80.979  1.00 27.07 ? 74  ASP C OD1 1 
ATOM   3463 O  OD2 . ASP C 1 77  ? 114.461 60.994  82.367  1.00 29.04 ? 74  ASP C OD2 1 
ATOM   3464 N  N   . VAL C 1 78  ? 118.817 58.737  80.063  1.00 29.97 ? 75  VAL C N   1 
ATOM   3465 C  CA  . VAL C 1 78  ? 119.933 57.873  80.350  1.00 30.52 ? 75  VAL C CA  1 
ATOM   3466 C  C   . VAL C 1 78  ? 121.132 58.053  79.426  1.00 31.01 ? 75  VAL C C   1 
ATOM   3467 O  O   . VAL C 1 78  ? 122.241 58.254  79.930  1.00 32.12 ? 75  VAL C O   1 
ATOM   3468 C  CB  . VAL C 1 78  ? 119.538 56.410  80.809  1.00 30.82 ? 75  VAL C CB  1 
ATOM   3469 C  CG1 . VAL C 1 78  ? 118.061 56.152  80.607  1.00 31.16 ? 75  VAL C CG1 1 
ATOM   3470 C  CG2 . VAL C 1 78  ? 120.456 55.318  80.256  1.00 29.67 ? 75  VAL C CG2 1 
ATOM   3471 N  N   . LEU C 1 79  ? 120.927 58.076  78.114  1.00 31.06 ? 76  LEU C N   1 
ATOM   3472 C  CA  . LEU C 1 79  ? 122.053 58.251  77.192  1.00 31.46 ? 76  LEU C CA  1 
ATOM   3473 C  C   . LEU C 1 79  ? 122.476 59.707  77.086  1.00 31.89 ? 76  LEU C C   1 
ATOM   3474 O  O   . LEU C 1 79  ? 123.513 60.011  76.516  1.00 31.78 ? 76  LEU C O   1 
ATOM   3475 C  CB  . LEU C 1 79  ? 121.738 57.700  75.809  1.00 31.50 ? 76  LEU C CB  1 
ATOM   3476 C  CG  . LEU C 1 79  ? 121.159 56.299  75.853  1.00 32.17 ? 76  LEU C CG  1 
ATOM   3477 C  CD1 . LEU C 1 79  ? 120.729 55.855  74.491  1.00 34.24 ? 76  LEU C CD1 1 
ATOM   3478 C  CD2 . LEU C 1 79  ? 122.161 55.310  76.463  1.00 33.06 ? 76  LEU C CD2 1 
ATOM   3479 N  N   . GLY C 1 80  ? 121.672 60.606  77.643  1.00 32.28 ? 77  GLY C N   1 
ATOM   3480 C  CA  . GLY C 1 80  ? 121.972 62.029  77.602  1.00 32.39 ? 77  GLY C CA  1 
ATOM   3481 C  C   . GLY C 1 80  ? 123.380 62.360  78.062  1.00 32.52 ? 77  GLY C C   1 
ATOM   3482 O  O   . GLY C 1 80  ? 124.075 63.126  77.403  1.00 33.17 ? 77  GLY C O   1 
ATOM   3483 N  N   . ASP C 1 81  ? 123.801 61.790  79.187  1.00 32.38 ? 78  ASP C N   1 
ATOM   3484 C  CA  . ASP C 1 81  ? 125.131 62.050  79.727  1.00 32.90 ? 78  ASP C CA  1 
ATOM   3485 C  C   . ASP C 1 81  ? 126.298 61.682  78.762  1.00 31.81 ? 78  ASP C C   1 
ATOM   3486 O  O   . ASP C 1 81  ? 127.410 62.216  78.879  1.00 31.96 ? 78  ASP C O   1 
ATOM   3487 C  CB  . ASP C 1 81  ? 125.278 61.440  81.144  1.00 33.94 ? 78  ASP C CB  1 
ATOM   3488 C  CG  . ASP C 1 81  ? 124.422 62.213  82.225  1.00 37.90 ? 78  ASP C CG  1 
ATOM   3489 O  OD1 . ASP C 1 81  ? 123.984 63.373  81.957  1.00 41.58 ? 78  ASP C OD1 1 
ATOM   3490 O  OD2 . ASP C 1 81  ? 124.180 61.680  83.345  1.00 38.13 ? 78  ASP C OD2 1 
ATOM   3491 N  N   . LEU C 1 82  ? 126.018 60.817  77.791  1.00 29.96 ? 79  LEU C N   1 
ATOM   3492 C  CA  . LEU C 1 82  ? 127.002 60.394  76.809  1.00 27.91 ? 79  LEU C CA  1 
ATOM   3493 C  C   . LEU C 1 82  ? 127.135 61.345  75.621  1.00 26.93 ? 79  LEU C C   1 
ATOM   3494 O  O   . LEU C 1 82  ? 127.974 61.129  74.749  1.00 26.17 ? 79  LEU C O   1 
ATOM   3495 C  CB  . LEU C 1 82  ? 126.637 59.019  76.266  1.00 27.75 ? 79  LEU C CB  1 
ATOM   3496 C  CG  . LEU C 1 82  ? 126.634 57.797  77.176  1.00 28.33 ? 79  LEU C CG  1 
ATOM   3497 C  CD1 . LEU C 1 82  ? 126.278 56.602  76.295  1.00 29.90 ? 79  LEU C CD1 1 
ATOM   3498 C  CD2 . LEU C 1 82  ? 127.964 57.588  77.891  1.00 26.79 ? 79  LEU C CD2 1 
ATOM   3499 N  N   . TRP C 1 83  ? 126.296 62.376  75.569  1.00 25.47 ? 80  TRP C N   1 
ATOM   3500 C  CA  . TRP C 1 83  ? 126.249 63.230  74.400  1.00 24.67 ? 80  TRP C CA  1 
ATOM   3501 C  C   . TRP C 1 83  ? 127.575 63.997  74.204  1.00 24.26 ? 80  TRP C C   1 
ATOM   3502 O  O   . TRP C 1 83  ? 128.076 64.638  75.122  1.00 23.74 ? 80  TRP C O   1 
ATOM   3503 C  CB  . TRP C 1 83  ? 125.058 64.194  74.478  1.00 23.69 ? 80  TRP C CB  1 
ATOM   3504 C  CG  . TRP C 1 83  ? 124.897 65.007  73.234  1.00 23.59 ? 80  TRP C CG  1 
ATOM   3505 C  CD1 . TRP C 1 83  ? 124.157 64.682  72.134  1.00 23.15 ? 80  TRP C CD1 1 
ATOM   3506 C  CD2 . TRP C 1 83  ? 125.510 66.287  72.942  1.00 23.24 ? 80  TRP C CD2 1 
ATOM   3507 N  NE1 . TRP C 1 83  ? 124.250 65.689  71.190  1.00 22.68 ? 80  TRP C NE1 1 
ATOM   3508 C  CE2 . TRP C 1 83  ? 125.081 66.672  71.654  1.00 21.83 ? 80  TRP C CE2 1 
ATOM   3509 C  CE3 . TRP C 1 83  ? 126.366 67.138  73.648  1.00 23.70 ? 80  TRP C CE3 1 
ATOM   3510 C  CZ2 . TRP C 1 83  ? 125.476 67.869  71.059  1.00 22.41 ? 80  TRP C CZ2 1 
ATOM   3511 C  CZ3 . TRP C 1 83  ? 126.768 68.332  73.051  1.00 23.73 ? 80  TRP C CZ3 1 
ATOM   3512 C  CH2 . TRP C 1 83  ? 126.325 68.678  71.758  1.00 23.33 ? 80  TRP C CH2 1 
ATOM   3513 N  N   . GLY C 1 84  ? 128.124 63.931  72.999  1.00 24.02 ? 81  GLY C N   1 
ATOM   3514 C  CA  . GLY C 1 84  ? 129.313 64.697  72.677  1.00 24.43 ? 81  GLY C CA  1 
ATOM   3515 C  C   . GLY C 1 84  ? 130.569 63.846  72.682  1.00 24.96 ? 81  GLY C C   1 
ATOM   3516 O  O   . GLY C 1 84  ? 131.635 64.317  72.303  1.00 24.79 ? 81  GLY C O   1 
ATOM   3517 N  N   . GLU C 1 85  ? 130.432 62.589  73.105  1.00 25.49 ? 82  GLU C N   1 
ATOM   3518 C  CA  . GLU C 1 85  ? 131.550 61.681  73.235  1.00 26.76 ? 82  GLU C CA  1 
ATOM   3519 C  C   . GLU C 1 85  ? 131.295 60.288  72.640  1.00 25.92 ? 82  GLU C C   1 
ATOM   3520 O  O   . GLU C 1 85  ? 132.102 59.373  72.813  1.00 26.47 ? 82  GLU C O   1 
ATOM   3521 C  CB  . GLU C 1 85  ? 131.992 61.605  74.701  1.00 26.96 ? 82  GLU C CB  1 
ATOM   3522 C  CG  . GLU C 1 85  ? 130.985 61.007  75.666  1.00 29.17 ? 82  GLU C CG  1 
ATOM   3523 C  CD  . GLU C 1 85  ? 131.537 60.930  77.101  1.00 30.65 ? 82  GLU C CD  1 
ATOM   3524 O  OE1 . GLU C 1 85  ? 131.551 59.807  77.663  1.00 35.49 ? 82  GLU C OE1 1 
ATOM   3525 O  OE2 . GLU C 1 85  ? 131.969 61.981  77.661  1.00 34.62 ? 82  GLU C OE2 1 
ATOM   3526 N  N   . ILE C 1 86  ? 130.200 60.128  71.907  1.00 25.10 ? 83  ILE C N   1 
ATOM   3527 C  CA  . ILE C 1 86  ? 129.947 58.854  71.238  1.00 24.19 ? 83  ILE C CA  1 
ATOM   3528 C  C   . ILE C 1 86  ? 129.753 58.980  69.723  1.00 24.52 ? 83  ILE C C   1 
ATOM   3529 O  O   . ILE C 1 86  ? 129.245 58.069  69.079  1.00 24.48 ? 83  ILE C O   1 
ATOM   3530 C  CB  . ILE C 1 86  ? 128.830 57.993  71.937  1.00 24.10 ? 83  ILE C CB  1 
ATOM   3531 C  CG1 . ILE C 1 86  ? 127.486 58.730  71.997  1.00 22.42 ? 83  ILE C CG1 1 
ATOM   3532 C  CG2 . ILE C 1 86  ? 129.317 57.540  73.346  1.00 22.97 ? 83  ILE C CG2 1 
ATOM   3533 C  CD1 . ILE C 1 86  ? 126.322 57.844  72.460  1.00 22.61 ? 83  ILE C CD1 1 
ATOM   3534 N  N   . ASP C 1 87  ? 130.191 60.108  69.163  1.00 24.68 ? 84  ASP C N   1 
ATOM   3535 C  CA  . ASP C 1 87  ? 130.037 60.383  67.732  1.00 24.91 ? 84  ASP C CA  1 
ATOM   3536 C  C   . ASP C 1 87  ? 130.654 59.244  66.934  1.00 25.25 ? 84  ASP C C   1 
ATOM   3537 O  O   . ASP C 1 87  ? 131.589 58.611  67.403  1.00 25.73 ? 84  ASP C O   1 
ATOM   3538 C  CB  . ASP C 1 87  ? 130.733 61.702  67.343  1.00 24.85 ? 84  ASP C CB  1 
ATOM   3539 C  CG  . ASP C 1 87  ? 130.262 62.896  68.169  1.00 24.83 ? 84  ASP C CG  1 
ATOM   3540 O  OD1 . ASP C 1 87  ? 130.418 62.866  69.431  1.00 23.78 ? 84  ASP C OD1 1 
ATOM   3541 O  OD2 . ASP C 1 87  ? 129.774 63.869  67.540  1.00 19.90 ? 84  ASP C OD2 1 
ATOM   3542 N  N   . GLY C 1 88  ? 130.124 58.975  65.743  1.00 25.62 ? 85  GLY C N   1 
ATOM   3543 C  CA  . GLY C 1 88  ? 130.718 57.979  64.843  1.00 25.93 ? 85  GLY C CA  1 
ATOM   3544 C  C   . GLY C 1 88  ? 130.251 56.543  65.052  1.00 26.15 ? 85  GLY C C   1 
ATOM   3545 O  O   . GLY C 1 88  ? 130.753 55.629  64.401  1.00 27.00 ? 85  GLY C O   1 
ATOM   3546 N  N   . LYS C 1 89  ? 129.321 56.319  65.976  1.00 25.60 ? 86  LYS C N   1 
ATOM   3547 C  CA  . LYS C 1 89  ? 128.655 55.034  66.029  1.00 24.82 ? 86  LYS C CA  1 
ATOM   3548 C  C   . LYS C 1 89  ? 127.772 54.982  64.792  1.00 25.30 ? 86  LYS C C   1 
ATOM   3549 O  O   . LYS C 1 89  ? 127.401 56.033  64.253  1.00 25.79 ? 86  LYS C O   1 
ATOM   3550 C  CB  . LYS C 1 89  ? 127.854 54.888  67.314  1.00 24.67 ? 86  LYS C CB  1 
ATOM   3551 C  CG  . LYS C 1 89  ? 128.745 54.531  68.499  1.00 23.39 ? 86  LYS C CG  1 
ATOM   3552 C  CD  . LYS C 1 89  ? 127.988 54.239  69.759  1.00 19.59 ? 86  LYS C CD  1 
ATOM   3553 C  CE  . LYS C 1 89  ? 128.954 54.235  70.913  1.00 21.89 ? 86  LYS C CE  1 
ATOM   3554 N  NZ  . LYS C 1 89  ? 129.951 53.098  70.825  1.00 23.62 ? 86  LYS C NZ  1 
ATOM   3555 N  N   . ILE C 1 90  ? 127.465 53.780  64.308  1.00 24.89 ? 87  ILE C N   1 
ATOM   3556 C  CA  . ILE C 1 90  ? 126.667 53.641  63.088  1.00 24.40 ? 87  ILE C CA  1 
ATOM   3557 C  C   . ILE C 1 90  ? 125.264 53.168  63.468  1.00 24.38 ? 87  ILE C C   1 
ATOM   3558 O  O   . ILE C 1 90  ? 125.137 52.253  64.274  1.00 25.12 ? 87  ILE C O   1 
ATOM   3559 C  CB  . ILE C 1 90  ? 127.346 52.672  62.092  1.00 24.76 ? 87  ILE C CB  1 
ATOM   3560 C  CG1 . ILE C 1 90  ? 128.672 53.295  61.585  1.00 24.00 ? 87  ILE C CG1 1 
ATOM   3561 C  CG2 . ILE C 1 90  ? 126.360 52.296  60.944  1.00 24.53 ? 87  ILE C CG2 1 
ATOM   3562 C  CD1 . ILE C 1 90  ? 129.761 52.306  61.105  1.00 23.47 ? 87  ILE C CD1 1 
ATOM   3563 N  N   . ALA C 1 91  ? 124.215 53.797  62.937  1.00 23.67 ? 88  ALA C N   1 
ATOM   3564 C  CA  . ALA C 1 91  ? 122.852 53.484  63.392  1.00 23.63 ? 88  ALA C CA  1 
ATOM   3565 C  C   . ALA C 1 91  ? 121.816 53.553  62.276  1.00 23.90 ? 88  ALA C C   1 
ATOM   3566 O  O   . ALA C 1 91  ? 122.037 54.203  61.264  1.00 24.74 ? 88  ALA C O   1 
ATOM   3567 C  CB  . ALA C 1 91  ? 122.446 54.363  64.585  1.00 22.15 ? 88  ALA C CB  1 
ATOM   3568 N  N   . CYS C 1 92  ? 120.703 52.847  62.471  1.00 24.28 ? 89  CYS C N   1 
ATOM   3569 C  CA  . CYS C 1 92  ? 119.562 52.828  61.543  1.00 24.50 ? 89  CYS C CA  1 
ATOM   3570 C  C   . CYS C 1 92  ? 118.301 52.657  62.375  1.00 23.67 ? 89  CYS C C   1 
ATOM   3571 O  O   . CYS C 1 92  ? 118.405 52.473  63.586  1.00 24.11 ? 89  CYS C O   1 
ATOM   3572 C  CB  . CYS C 1 92  ? 119.698 51.674  60.551  1.00 23.53 ? 89  CYS C CB  1 
ATOM   3573 S  SG  . CYS C 1 92  ? 119.822 50.095  61.371  1.00 26.04 ? 89  CYS C SG  1 
ATOM   3574 N  N   . ALA C 1 93  ? 117.141 52.669  61.719  1.00 23.00 ? 90  ALA C N   1 
ATOM   3575 C  CA  . ALA C 1 93  ? 115.830 52.706  62.371  1.00 23.14 ? 90  ALA C CA  1 
ATOM   3576 C  C   . ALA C 1 93  ? 114.817 51.669  61.852  1.00 23.33 ? 90  ALA C C   1 
ATOM   3577 O  O   . ALA C 1 93  ? 114.889 51.198  60.704  1.00 23.65 ? 90  ALA C O   1 
ATOM   3578 C  CB  . ALA C 1 93  ? 115.237 54.110  62.235  1.00 22.40 ? 90  ALA C CB  1 
ATOM   3579 N  N   . PHE C 1 94  ? 113.867 51.305  62.703  1.00 23.80 ? 91  PHE C N   1 
ATOM   3580 C  CA  . PHE C 1 94  ? 112.696 50.556  62.241  1.00 23.97 ? 91  PHE C CA  1 
ATOM   3581 C  C   . PHE C 1 94  ? 111.411 50.900  63.017  1.00 24.32 ? 91  PHE C C   1 
ATOM   3582 O  O   . PHE C 1 94  ? 111.480 51.378  64.152  1.00 24.91 ? 91  PHE C O   1 
ATOM   3583 C  CB  . PHE C 1 94  ? 112.981 49.055  62.226  1.00 23.39 ? 91  PHE C CB  1 
ATOM   3584 C  CG  . PHE C 1 94  ? 113.389 48.465  63.578  1.00 24.71 ? 91  PHE C CG  1 
ATOM   3585 C  CD1 . PHE C 1 94  ? 114.709 48.601  64.064  1.00 20.92 ? 91  PHE C CD1 1 
ATOM   3586 C  CD2 . PHE C 1 94  ? 112.469 47.691  64.335  1.00 23.94 ? 91  PHE C CD2 1 
ATOM   3587 C  CE1 . PHE C 1 94  ? 115.085 48.030  65.300  1.00 21.19 ? 91  PHE C CE1 1 
ATOM   3588 C  CE2 . PHE C 1 94  ? 112.861 47.111  65.587  1.00 21.57 ? 91  PHE C CE2 1 
ATOM   3589 C  CZ  . PHE C 1 94  ? 114.162 47.277  66.046  1.00 21.09 ? 91  PHE C CZ  1 
ATOM   3590 N  N   . SER C 1 95  ? 110.248 50.625  62.430  1.00 24.34 ? 92  SER C N   1 
ATOM   3591 C  CA  . SER C 1 95  ? 108.992 51.010  63.061  1.00 24.59 ? 92  SER C CA  1 
ATOM   3592 C  C   . SER C 1 95  ? 107.759 50.206  62.583  1.00 24.99 ? 92  SER C C   1 
ATOM   3593 O  O   . SER C 1 95  ? 107.593 49.937  61.388  1.00 25.08 ? 92  SER C O   1 
ATOM   3594 C  CB  . SER C 1 95  ? 108.753 52.513  62.855  1.00 24.38 ? 92  SER C CB  1 
ATOM   3595 O  OG  . SER C 1 95  ? 107.783 52.994  63.757  1.00 24.06 ? 92  SER C OG  1 
ATOM   3596 N  N   . SER C 1 96  ? 106.902 49.835  63.529  1.00 24.15 ? 93  SER C N   1 
ATOM   3597 C  CA  . SER C 1 96  ? 105.605 49.281  63.203  1.00 24.09 ? 93  SER C CA  1 
ATOM   3598 C  C   . SER C 1 96  ? 104.508 50.320  63.465  1.00 24.03 ? 93  SER C C   1 
ATOM   3599 O  O   . SER C 1 96  ? 104.509 51.015  64.489  1.00 24.67 ? 93  SER C O   1 
ATOM   3600 C  CB  . SER C 1 96  ? 105.358 48.015  64.017  1.00 24.12 ? 93  SER C CB  1 
ATOM   3601 O  OG  . SER C 1 96  ? 104.035 47.572  63.856  1.00 23.53 ? 93  SER C OG  1 
ATOM   3602 N  N   . SER C 1 97  ? 103.580 50.444  62.527  1.00 23.92 ? 94  SER C N   1 
ATOM   3603 C  CA  . SER C 1 97  ? 102.485 51.411  62.633  1.00 23.48 ? 94  SER C CA  1 
ATOM   3604 C  C   . SER C 1 97  ? 101.156 50.679  62.486  1.00 22.93 ? 94  SER C C   1 
ATOM   3605 O  O   . SER C 1 97  ? 101.141 49.504  62.141  1.00 22.82 ? 94  SER C O   1 
ATOM   3606 C  CB  . SER C 1 97  ? 102.627 52.475  61.538  1.00 23.80 ? 94  SER C CB  1 
ATOM   3607 O  OG  . SER C 1 97  ? 102.448 51.908  60.256  1.00 23.86 ? 94  SER C OG  1 
ATOM   3608 N  N   . GLY C 1 98  ? 100.052 51.374  62.745  1.00 22.61 ? 95  GLY C N   1 
ATOM   3609 C  CA  . GLY C 1 98  ? 98.708  50.800  62.628  1.00 21.64 ? 95  GLY C CA  1 
ATOM   3610 C  C   . GLY C 1 98  ? 98.242  50.602  61.193  1.00 21.72 ? 95  GLY C C   1 
ATOM   3611 O  O   . GLY C 1 98  ? 97.524  49.651  60.882  1.00 22.54 ? 95  GLY C O   1 
ATOM   3612 N  N   . GLY C 1 99  ? 98.638  51.492  60.304  1.00 21.34 ? 96  GLY C N   1 
ATOM   3613 C  CA  . GLY C 1 99  ? 98.275  51.339  58.898  1.00 20.49 ? 96  GLY C CA  1 
ATOM   3614 C  C   . GLY C 1 99  ? 99.390  51.775  57.967  1.00 20.54 ? 96  GLY C C   1 
ATOM   3615 O  O   . GLY C 1 99  ? 100.302 52.520  58.365  1.00 20.44 ? 96  GLY C O   1 
ATOM   3616 N  N   . TRP C 1 100 ? 99.333  51.282  56.733  1.00 19.60 ? 97  TRP C N   1 
ATOM   3617 C  CA  . TRP C 1 100 ? 100.129 51.821  55.666  1.00 19.25 ? 97  TRP C CA  1 
ATOM   3618 C  C   . TRP C 1 100 ? 99.619  53.248  55.407  1.00 19.51 ? 97  TRP C C   1 
ATOM   3619 O  O   . TRP C 1 100 ? 98.400  53.493  55.395  1.00 19.22 ? 97  TRP C O   1 
ATOM   3620 C  CB  . TRP C 1 100 ? 99.994  50.906  54.466  1.00 19.50 ? 97  TRP C CB  1 
ATOM   3621 C  CG  . TRP C 1 100 ? 100.733 49.585  54.704  1.00 20.37 ? 97  TRP C CG  1 
ATOM   3622 C  CD1 . TRP C 1 100 ? 100.179 48.327  54.895  1.00 20.21 ? 97  TRP C CD1 1 
ATOM   3623 C  CD2 . TRP C 1 100 ? 102.156 49.414  54.808  1.00 20.13 ? 97  TRP C CD2 1 
ATOM   3624 N  NE1 . TRP C 1 100 ? 101.177 47.402  55.094  1.00 20.27 ? 97  TRP C NE1 1 
ATOM   3625 C  CE2 . TRP C 1 100 ? 102.398 48.040  55.049  1.00 20.94 ? 97  TRP C CE2 1 
ATOM   3626 C  CE3 . TRP C 1 100 ? 103.255 50.292  54.713  1.00 19.91 ? 97  TRP C CE3 1 
ATOM   3627 C  CZ2 . TRP C 1 100 ? 103.710 47.519  55.188  1.00 19.78 ? 97  TRP C CZ2 1 
ATOM   3628 C  CZ3 . TRP C 1 100 ? 104.547 49.776  54.854  1.00 19.77 ? 97  TRP C CZ3 1 
ATOM   3629 C  CH2 . TRP C 1 100 ? 104.759 48.400  55.088  1.00 19.25 ? 97  TRP C CH2 1 
ATOM   3630 N  N   . GLY C 1 101 ? 100.555 54.190  55.280  1.00 19.86 ? 98  GLY C N   1 
ATOM   3631 C  CA  . GLY C 1 101 ? 100.246 55.622  55.172  1.00 19.97 ? 98  GLY C CA  1 
ATOM   3632 C  C   . GLY C 1 101 ? 99.976  56.245  56.521  1.00 20.33 ? 98  GLY C C   1 
ATOM   3633 O  O   . GLY C 1 101 ? 99.452  57.359  56.606  1.00 19.67 ? 98  GLY C O   1 
ATOM   3634 N  N   . GLY C 1 102 ? 100.308 55.486  57.566  1.00 21.05 ? 99  GLY C N   1 
ATOM   3635 C  CA  . GLY C 1 102 ? 100.103 55.879  58.945  1.00 22.97 ? 99  GLY C CA  1 
ATOM   3636 C  C   . GLY C 1 102 ? 101.298 56.528  59.615  1.00 24.39 ? 99  GLY C C   1 
ATOM   3637 O  O   . GLY C 1 102 ? 101.240 56.863  60.786  1.00 25.89 ? 99  GLY C O   1 
ATOM   3638 N  N   . GLY C 1 103 ? 102.395 56.715  58.902  1.00 24.86 ? 100 GLY C N   1 
ATOM   3639 C  CA  . GLY C 1 103 ? 103.488 57.467  59.486  1.00 25.05 ? 100 GLY C CA  1 
ATOM   3640 C  C   . GLY C 1 103 ? 104.694 56.654  59.860  1.00 25.36 ? 100 GLY C C   1 
ATOM   3641 O  O   . GLY C 1 103 ? 105.560 57.153  60.569  1.00 25.56 ? 100 GLY C O   1 
ATOM   3642 N  N   . ASN C 1 104 ? 104.785 55.406  59.410  1.00 25.90 ? 101 ASN C N   1 
ATOM   3643 C  CA  . ASN C 1 104 ? 105.965 54.621  59.769  1.00 26.91 ? 101 ASN C CA  1 
ATOM   3644 C  C   . ASN C 1 104 ? 107.317 55.119  59.238  1.00 26.81 ? 101 ASN C C   1 
ATOM   3645 O  O   . ASN C 1 104 ? 108.332 54.909  59.901  1.00 27.15 ? 101 ASN C O   1 
ATOM   3646 C  CB  . ASN C 1 104 ? 105.804 53.105  59.568  1.00 27.84 ? 101 ASN C CB  1 
ATOM   3647 C  CG  . ASN C 1 104 ? 105.159 52.732  58.244  1.00 29.89 ? 101 ASN C CG  1 
ATOM   3648 O  OD1 . ASN C 1 104 ? 104.228 51.927  58.234  1.00 36.70 ? 101 ASN C OD1 1 
ATOM   3649 N  ND2 . ASN C 1 104 ? 105.667 53.261  57.133  1.00 27.63 ? 101 ASN C ND2 1 
ATOM   3650 N  N   . GLU C 1 105 ? 107.349 55.812  58.094  1.00 26.54 ? 102 GLU C N   1 
ATOM   3651 C  CA  . GLU C 1 105 ? 108.643 56.335  57.586  1.00 26.36 ? 102 GLU C CA  1 
ATOM   3652 C  C   . GLU C 1 105 ? 109.020 57.597  58.333  1.00 25.71 ? 102 GLU C C   1 
ATOM   3653 O  O   . GLU C 1 105 ? 110.197 57.858  58.569  1.00 26.18 ? 102 GLU C O   1 
ATOM   3654 C  CB  . GLU C 1 105 ? 108.592 56.627  56.100  1.00 26.36 ? 102 GLU C CB  1 
ATOM   3655 C  CG  . GLU C 1 105 ? 108.295 55.429  55.203  1.00 27.77 ? 102 GLU C CG  1 
ATOM   3656 C  CD  . GLU C 1 105 ? 107.992 55.852  53.754  1.00 28.56 ? 102 GLU C CD  1 
ATOM   3657 O  OE1 . GLU C 1 105 ? 107.532 56.998  53.521  1.00 32.67 ? 102 GLU C OE1 1 
ATOM   3658 O  OE2 . GLU C 1 105 ? 108.197 55.028  52.839  1.00 30.96 ? 102 GLU C OE2 1 
ATOM   3659 N  N   . VAL C 1 106 ? 108.003 58.374  58.696  1.00 24.99 ? 103 VAL C N   1 
ATOM   3660 C  CA  . VAL C 1 106 ? 108.156 59.579  59.446  1.00 24.12 ? 103 VAL C CA  1 
ATOM   3661 C  C   . VAL C 1 106 ? 108.674 59.245  60.851  1.00 25.04 ? 103 VAL C C   1 
ATOM   3662 O  O   . VAL C 1 106 ? 109.592 59.924  61.366  1.00 25.53 ? 103 VAL C O   1 
ATOM   3663 C  CB  . VAL C 1 106 ? 106.811 60.389  59.449  1.00 24.65 ? 103 VAL C CB  1 
ATOM   3664 C  CG1 . VAL C 1 106 ? 106.919 61.629  60.299  1.00 23.44 ? 103 VAL C CG1 1 
ATOM   3665 C  CG2 . VAL C 1 106 ? 106.440 60.809  58.037  1.00 22.71 ? 103 VAL C CG2 1 
ATOM   3666 N  N   . ALA C 1 107 ? 108.123 58.188  61.461  1.00 25.23 ? 104 ALA C N   1 
ATOM   3667 C  CA  . ALA C 1 107 ? 108.614 57.679  62.765  1.00 25.30 ? 104 ALA C CA  1 
ATOM   3668 C  C   . ALA C 1 107 ? 110.076 57.293  62.680  1.00 25.54 ? 104 ALA C C   1 
ATOM   3669 O  O   . ALA C 1 107 ? 110.855 57.690  63.526  1.00 26.05 ? 104 ALA C O   1 
ATOM   3670 C  CB  . ALA C 1 107 ? 107.778 56.491  63.283  1.00 24.13 ? 104 ALA C CB  1 
ATOM   3671 N  N   . CYS C 1 108 ? 110.443 56.520  61.659  1.00 26.27 ? 105 CYS C N   1 
ATOM   3672 C  CA  . CYS C 1 108 ? 111.859 56.241  61.352  1.00 26.71 ? 105 CYS C CA  1 
ATOM   3673 C  C   . CYS C 1 108 ? 112.722 57.517  61.211  1.00 26.65 ? 105 CYS C C   1 
ATOM   3674 O  O   . CYS C 1 108 ? 113.799 57.599  61.797  1.00 26.32 ? 105 CYS C O   1 
ATOM   3675 C  CB  . CYS C 1 108 ? 111.971 55.400  60.077  1.00 26.56 ? 105 CYS C CB  1 
ATOM   3676 S  SG  . CYS C 1 108 ? 111.470 53.650  60.272  1.00 28.19 ? 105 CYS C SG  1 
HETATM 3677 N  N   . MSE C 1 109 ? 112.268 58.485  60.412  1.00 27.15 ? 106 MSE C N   1 
HETATM 3678 C  CA  . MSE C 1 109 ? 112.943 59.776  60.288  1.00 27.86 ? 106 MSE C CA  1 
HETATM 3679 C  C   . MSE C 1 109 ? 113.261 60.403  61.666  1.00 27.30 ? 106 MSE C C   1 
HETATM 3680 O  O   . MSE C 1 109 ? 114.377 60.918  61.877  1.00 26.70 ? 106 MSE C O   1 
HETATM 3681 C  CB  . MSE C 1 109 ? 112.103 60.746  59.483  1.00 28.96 ? 106 MSE C CB  1 
HETATM 3682 C  CG  . MSE C 1 109 ? 112.246 60.666  57.974  1.00 38.65 ? 106 MSE C CG  1 
HETATM 3683 SE SE  . MSE C 1 109 ? 114.142 60.564  57.236  1.00 60.44 ? 106 MSE C SE  1 
HETATM 3684 C  CE  . MSE C 1 109 ? 114.989 61.957  58.370  1.00 46.55 ? 106 MSE C CE  1 
ATOM   3685 N  N   . SER C 1 110 ? 112.282 60.347  62.578  1.00 25.45 ? 107 SER C N   1 
ATOM   3686 C  CA  . SER C 1 110 ? 112.410 60.901  63.926  1.00 25.22 ? 107 SER C CA  1 
ATOM   3687 C  C   . SER C 1 110 ? 113.393 60.125  64.793  1.00 24.78 ? 107 SER C C   1 
ATOM   3688 O  O   . SER C 1 110 ? 114.136 60.714  65.549  1.00 24.04 ? 107 SER C O   1 
ATOM   3689 C  CB  . SER C 1 110 ? 111.045 61.007  64.617  1.00 25.44 ? 107 SER C CB  1 
ATOM   3690 O  OG  . SER C 1 110 ? 110.622 59.757  65.148  1.00 25.89 ? 107 SER C OG  1 
ATOM   3691 N  N   . ILE C 1 111 ? 113.427 58.812  64.658  1.00 24.47 ? 108 ILE C N   1 
ATOM   3692 C  CA  . ILE C 1 111 ? 114.518 58.037  65.259  1.00 24.60 ? 108 ILE C CA  1 
ATOM   3693 C  C   . ILE C 1 111 ? 115.902 58.438  64.713  1.00 25.35 ? 108 ILE C C   1 
ATOM   3694 O  O   . ILE C 1 111 ? 116.850 58.601  65.488  1.00 24.58 ? 108 ILE C O   1 
ATOM   3695 C  CB  . ILE C 1 111 ? 114.304 56.533  65.101  1.00 24.22 ? 108 ILE C CB  1 
ATOM   3696 C  CG1 . ILE C 1 111 ? 113.004 56.103  65.771  1.00 24.75 ? 108 ILE C CG1 1 
ATOM   3697 C  CG2 . ILE C 1 111 ? 115.466 55.750  65.704  1.00 24.21 ? 108 ILE C CG2 1 
ATOM   3698 C  CD1 . ILE C 1 111 ? 112.560 54.704  65.347  1.00 24.77 ? 108 ILE C CD1 1 
ATOM   3699 N  N   . LEU C 1 112 ? 116.021 58.602  63.392  1.00 25.70 ? 109 LEU C N   1 
ATOM   3700 C  CA  . LEU C 1 112 ? 117.311 58.965  62.773  1.00 26.29 ? 109 LEU C CA  1 
ATOM   3701 C  C   . LEU C 1 112 ? 117.773 60.370  63.163  1.00 26.29 ? 109 LEU C C   1 
ATOM   3702 O  O   . LEU C 1 112 ? 118.968 60.621  63.284  1.00 26.44 ? 109 LEU C O   1 
ATOM   3703 C  CB  . LEU C 1 112 ? 117.246 58.883  61.243  1.00 25.92 ? 109 LEU C CB  1 
ATOM   3704 C  CG  . LEU C 1 112 ? 116.978 57.495  60.667  1.00 28.76 ? 109 LEU C CG  1 
ATOM   3705 C  CD1 . LEU C 1 112 ? 116.691 57.548  59.153  1.00 26.74 ? 109 LEU C CD1 1 
ATOM   3706 C  CD2 . LEU C 1 112 ? 118.085 56.534  60.982  1.00 27.33 ? 109 LEU C CD2 1 
ATOM   3707 N  N   . THR C 1 113 ? 116.817 61.282  63.273  1.00 26.85 ? 110 THR C N   1 
ATOM   3708 C  CA  . THR C 1 113 ? 117.017 62.611  63.784  1.00 28.10 ? 110 THR C CA  1 
ATOM   3709 C  C   . THR C 1 113 ? 117.649 62.594  65.183  1.00 29.47 ? 110 THR C C   1 
ATOM   3710 O  O   . THR C 1 113 ? 118.647 63.279  65.451  1.00 29.33 ? 110 THR C O   1 
ATOM   3711 C  CB  . THR C 1 113 ? 115.680 63.316  63.845  1.00 27.53 ? 110 THR C CB  1 
ATOM   3712 O  OG1 . THR C 1 113 ? 115.277 63.565  62.512  1.00 28.74 ? 110 THR C OG1 1 
ATOM   3713 C  CG2 . THR C 1 113 ? 115.778 64.650  64.591  1.00 26.77 ? 110 THR C CG2 1 
HETATM 3714 N  N   . MSE C 1 114 ? 117.043 61.820  66.068  1.00 30.07 ? 111 MSE C N   1 
HETATM 3715 C  CA  . MSE C 1 114 ? 117.567 61.609  67.386  1.00 32.93 ? 111 MSE C CA  1 
HETATM 3716 C  C   . MSE C 1 114 ? 119.010 61.055  67.352  1.00 31.03 ? 111 MSE C C   1 
HETATM 3717 O  O   . MSE C 1 114 ? 119.908 61.590  68.016  1.00 31.85 ? 111 MSE C O   1 
HETATM 3718 C  CB  . MSE C 1 114 ? 116.630 60.671  68.103  1.00 31.44 ? 111 MSE C CB  1 
HETATM 3719 C  CG  . MSE C 1 114 ? 116.541 60.887  69.566  1.00 35.19 ? 111 MSE C CG  1 
HETATM 3720 SE SE  . MSE C 1 114 ? 115.168 59.680  70.324  1.00 43.22 ? 111 MSE C SE  1 
HETATM 3721 C  CE  . MSE C 1 114 ? 115.692 57.936  69.487  1.00 36.36 ? 111 MSE C CE  1 
ATOM   3722 N  N   . LEU C 1 115 ? 119.240 60.022  66.545  1.00 30.01 ? 112 LEU C N   1 
ATOM   3723 C  CA  . LEU C 1 115 ? 120.546 59.364  66.462  1.00 28.66 ? 112 LEU C CA  1 
ATOM   3724 C  C   . LEU C 1 115 ? 121.612 60.262  65.846  1.00 29.22 ? 112 LEU C C   1 
ATOM   3725 O  O   . LEU C 1 115 ? 122.749 60.291  66.311  1.00 28.67 ? 112 LEU C O   1 
ATOM   3726 C  CB  . LEU C 1 115 ? 120.451 58.035  65.718  1.00 27.13 ? 112 LEU C CB  1 
ATOM   3727 C  CG  . LEU C 1 115 ? 119.492 56.966  66.254  1.00 26.54 ? 112 LEU C CG  1 
ATOM   3728 C  CD1 . LEU C 1 115 ? 119.153 55.963  65.155  1.00 21.52 ? 112 LEU C CD1 1 
ATOM   3729 C  CD2 . LEU C 1 115 ? 120.019 56.250  67.504  1.00 25.92 ? 112 LEU C CD2 1 
HETATM 3730 N  N   . MSE C 1 116 ? 121.244 61.004  64.809  1.00 29.54 ? 113 MSE C N   1 
HETATM 3731 C  CA  . MSE C 1 116 ? 122.146 61.973  64.241  1.00 32.66 ? 113 MSE C CA  1 
HETATM 3732 C  C   . MSE C 1 116 ? 122.603 63.051  65.230  1.00 30.05 ? 113 MSE C C   1 
HETATM 3733 O  O   . MSE C 1 116 ? 123.718 63.573  65.117  1.00 29.43 ? 113 MSE C O   1 
HETATM 3734 C  CB  . MSE C 1 116 ? 121.498 62.620  63.056  1.00 31.67 ? 113 MSE C CB  1 
HETATM 3735 C  CG  . MSE C 1 116 ? 121.675 61.840  61.807  1.00 34.63 ? 113 MSE C CG  1 
HETATM 3736 SE SE  . MSE C 1 116 ? 121.105 62.919  60.284  1.00 46.20 ? 113 MSE C SE  1 
HETATM 3737 C  CE  . MSE C 1 116 ? 119.044 62.819  60.595  1.00 35.61 ? 113 MSE C CE  1 
ATOM   3738 N  N   . ASN C 1 117 ? 121.739 63.366  66.193  1.00 28.42 ? 114 ASN C N   1 
ATOM   3739 C  CA  . ASN C 1 117 ? 122.061 64.312  67.243  1.00 27.86 ? 114 ASN C CA  1 
ATOM   3740 C  C   . ASN C 1 117 ? 123.190 63.797  68.112  1.00 27.23 ? 114 ASN C C   1 
ATOM   3741 O  O   . ASN C 1 117 ? 123.933 64.577  68.644  1.00 27.57 ? 114 ASN C O   1 
ATOM   3742 C  CB  . ASN C 1 117 ? 120.846 64.613  68.122  1.00 27.60 ? 114 ASN C CB  1 
ATOM   3743 C  CG  . ASN C 1 117 ? 120.838 66.024  68.598  1.00 27.49 ? 114 ASN C CG  1 
ATOM   3744 O  OD1 . ASN C 1 117 ? 121.321 66.307  69.696  1.00 32.39 ? 114 ASN C OD1 1 
ATOM   3745 N  ND2 . ASN C 1 117 ? 120.308 66.948  67.781  1.00 26.26 ? 114 ASN C ND2 1 
ATOM   3746 N  N   . PHE C 1 118 ? 123.331 62.481  68.241  1.00 26.63 ? 115 PHE C N   1 
ATOM   3747 C  CA  . PHE C 1 118 ? 124.458 61.927  68.987  1.00 26.04 ? 115 PHE C CA  1 
ATOM   3748 C  C   . PHE C 1 118 ? 125.770 61.877  68.182  1.00 24.92 ? 115 PHE C C   1 
ATOM   3749 O  O   . PHE C 1 118 ? 126.773 61.456  68.702  1.00 24.07 ? 115 PHE C O   1 
ATOM   3750 C  CB  . PHE C 1 118 ? 124.097 60.580  69.621  1.00 26.08 ? 115 PHE C CB  1 
ATOM   3751 C  CG  . PHE C 1 118 ? 123.249 60.722  70.855  1.00 28.30 ? 115 PHE C CG  1 
ATOM   3752 C  CD1 . PHE C 1 118 ? 121.864 60.999  70.748  1.00 30.29 ? 115 PHE C CD1 1 
ATOM   3753 C  CD2 . PHE C 1 118 ? 123.828 60.651  72.124  1.00 26.91 ? 115 PHE C CD2 1 
ATOM   3754 C  CE1 . PHE C 1 118 ? 121.070 61.181  71.896  1.00 30.39 ? 115 PHE C CE1 1 
ATOM   3755 C  CE2 . PHE C 1 118 ? 123.054 60.810  73.272  1.00 28.30 ? 115 PHE C CE2 1 
ATOM   3756 C  CZ  . PHE C 1 118 ? 121.670 61.068  73.162  1.00 29.39 ? 115 PHE C CZ  1 
ATOM   3757 N  N   . GLY C 1 119 ? 125.748 62.375  66.942  1.00 24.54 ? 116 GLY C N   1 
ATOM   3758 C  CA  . GLY C 1 119 ? 126.911 62.373  66.030  1.00 23.89 ? 116 GLY C CA  1 
ATOM   3759 C  C   . GLY C 1 119 ? 127.107 61.037  65.321  1.00 23.95 ? 116 GLY C C   1 
ATOM   3760 O  O   . GLY C 1 119 ? 128.182 60.757  64.768  1.00 24.02 ? 116 GLY C O   1 
ATOM   3761 N  N   . PHE C 1 120 ? 126.074 60.197  65.340  1.00 23.92 ? 117 PHE C N   1 
ATOM   3762 C  CA  . PHE C 1 120 ? 126.115 58.894  64.661  1.00 23.70 ? 117 PHE C CA  1 
ATOM   3763 C  C   . PHE C 1 120 ? 126.067 59.063  63.153  1.00 24.20 ? 117 PHE C C   1 
ATOM   3764 O  O   . PHE C 1 120 ? 125.475 60.030  62.642  1.00 24.22 ? 117 PHE C O   1 
ATOM   3765 C  CB  . PHE C 1 120 ? 124.911 58.062  65.092  1.00 23.90 ? 117 PHE C CB  1 
ATOM   3766 C  CG  . PHE C 1 120 ? 124.932 57.642  66.546  1.00 24.78 ? 117 PHE C CG  1 
ATOM   3767 C  CD1 . PHE C 1 120 ? 125.965 58.050  67.412  1.00 24.41 ? 117 PHE C CD1 1 
ATOM   3768 C  CD2 . PHE C 1 120 ? 123.903 56.848  67.054  1.00 24.42 ? 117 PHE C CD2 1 
ATOM   3769 C  CE1 . PHE C 1 120 ? 125.986 57.652  68.753  1.00 25.72 ? 117 PHE C CE1 1 
ATOM   3770 C  CE2 . PHE C 1 120 ? 123.904 56.450  68.395  1.00 25.39 ? 117 PHE C CE2 1 
ATOM   3771 C  CZ  . PHE C 1 120 ? 124.952 56.854  69.251  1.00 25.71 ? 117 PHE C CZ  1 
ATOM   3772 N  N   . LEU C 1 121 ? 126.695 58.129  62.442  1.00 24.72 ? 118 LEU C N   1 
ATOM   3773 C  CA  . LEU C 1 121 ? 126.515 57.979  61.011  1.00 25.20 ? 118 LEU C CA  1 
ATOM   3774 C  C   . LEU C 1 121 ? 125.258 57.114  60.835  1.00 25.21 ? 118 LEU C C   1 
ATOM   3775 O  O   . LEU C 1 121 ? 125.127 56.046  61.434  1.00 25.06 ? 118 LEU C O   1 
ATOM   3776 C  CB  . LEU C 1 121 ? 127.711 57.274  60.381  1.00 25.25 ? 118 LEU C CB  1 
ATOM   3777 C  CG  . LEU C 1 121 ? 129.129 57.858  60.254  1.00 27.52 ? 118 LEU C CG  1 
ATOM   3778 C  CD1 . LEU C 1 121 ? 129.437 58.378  58.833  1.00 27.20 ? 118 LEU C CD1 1 
ATOM   3779 C  CD2 . LEU C 1 121 ? 129.481 58.888  61.317  1.00 25.90 ? 118 LEU C CD2 1 
ATOM   3780 N  N   . VAL C 1 122 ? 124.346 57.580  59.991  1.00 25.25 ? 119 VAL C N   1 
ATOM   3781 C  CA  . VAL C 1 122 ? 122.976 57.083  59.974  1.00 25.17 ? 119 VAL C CA  1 
ATOM   3782 C  C   . VAL C 1 122 ? 122.609 56.699  58.538  1.00 25.39 ? 119 VAL C C   1 
ATOM   3783 O  O   . VAL C 1 122 ? 123.074 57.345  57.601  1.00 25.07 ? 119 VAL C O   1 
ATOM   3784 C  CB  . VAL C 1 122 ? 122.101 58.177  60.628  1.00 24.90 ? 119 VAL C CB  1 
ATOM   3785 C  CG1 . VAL C 1 122 ? 121.008 58.705  59.763  1.00 24.71 ? 119 VAL C CG1 1 
ATOM   3786 C  CG2 . VAL C 1 122 ? 121.659 57.782  62.025  1.00 25.64 ? 119 VAL C CG2 1 
ATOM   3787 N  N   . PHE C 1 123 ? 121.822 55.632  58.357  1.00 25.21 ? 120 PHE C N   1 
ATOM   3788 C  CA  . PHE C 1 123 ? 121.528 55.131  57.000  1.00 25.14 ? 120 PHE C CA  1 
ATOM   3789 C  C   . PHE C 1 123 ? 120.175 54.403  56.895  1.00 25.01 ? 120 PHE C C   1 
ATOM   3790 O  O   . PHE C 1 123 ? 119.586 53.964  57.903  1.00 23.88 ? 120 PHE C O   1 
ATOM   3791 C  CB  . PHE C 1 123 ? 122.647 54.158  56.543  1.00 24.44 ? 120 PHE C CB  1 
ATOM   3792 C  CG  . PHE C 1 123 ? 122.599 52.837  57.284  1.00 24.56 ? 120 PHE C CG  1 
ATOM   3793 C  CD1 . PHE C 1 123 ? 123.114 52.732  58.577  1.00 22.62 ? 120 PHE C CD1 1 
ATOM   3794 C  CD2 . PHE C 1 123 ? 121.938 51.748  56.745  1.00 22.20 ? 120 PHE C CD2 1 
ATOM   3795 C  CE1 . PHE C 1 123 ? 123.009 51.575  59.274  1.00 21.07 ? 120 PHE C CE1 1 
ATOM   3796 C  CE2 . PHE C 1 123 ? 121.842 50.572  57.460  1.00 22.20 ? 120 PHE C CE2 1 
ATOM   3797 C  CZ  . PHE C 1 123 ? 122.390 50.482  58.712  1.00 21.18 ? 120 PHE C CZ  1 
ATOM   3798 N  N   . GLY C 1 124 ? 119.723 54.260  55.645  1.00 25.63 ? 121 GLY C N   1 
ATOM   3799 C  CA  . GLY C 1 124 ? 118.635 53.341  55.272  1.00 26.15 ? 121 GLY C CA  1 
ATOM   3800 C  C   . GLY C 1 124 ? 119.148 52.335  54.249  1.00 27.42 ? 121 GLY C C   1 
ATOM   3801 O  O   . GLY C 1 124 ? 120.345 52.332  53.902  1.00 27.43 ? 121 GLY C O   1 
ATOM   3802 N  N   . VAL C 1 125 ? 118.248 51.471  53.758  1.00 28.22 ? 122 VAL C N   1 
ATOM   3803 C  CA  . VAL C 1 125 ? 118.617 50.388  52.839  1.00 27.35 ? 122 VAL C CA  1 
ATOM   3804 C  C   . VAL C 1 125 ? 117.890 50.542  51.500  1.00 27.39 ? 122 VAL C C   1 
ATOM   3805 O  O   . VAL C 1 125 ? 116.657 50.629  51.460  1.00 27.74 ? 122 VAL C O   1 
ATOM   3806 C  CB  . VAL C 1 125 ? 118.316 48.991  53.491  1.00 27.60 ? 122 VAL C CB  1 
ATOM   3807 C  CG1 . VAL C 1 125 ? 118.440 47.817  52.476  1.00 26.77 ? 122 VAL C CG1 1 
ATOM   3808 C  CG2 . VAL C 1 125 ? 119.201 48.763  54.697  1.00 25.93 ? 122 VAL C CG2 1 
ATOM   3809 N  N   . THR C 1 126 ? 118.658 50.558  50.412  1.00 26.90 ? 123 THR C N   1 
ATOM   3810 C  CA  . THR C 1 126 ? 118.129 50.620  49.044  1.00 26.29 ? 123 THR C CA  1 
ATOM   3811 C  C   . THR C 1 126 ? 117.383 49.360  48.552  1.00 27.02 ? 123 THR C C   1 
ATOM   3812 O  O   . THR C 1 126 ? 116.453 49.454  47.729  1.00 27.02 ? 123 THR C O   1 
ATOM   3813 C  CB  . THR C 1 126 ? 119.246 50.924  48.034  1.00 25.64 ? 123 THR C CB  1 
ATOM   3814 O  OG1 . THR C 1 126 ? 120.283 49.954  48.174  1.00 24.77 ? 123 THR C OG1 1 
ATOM   3815 C  CG2 . THR C 1 126 ? 119.810 52.332  48.223  1.00 24.56 ? 123 THR C CG2 1 
ATOM   3816 N  N   . ASP C 1 127 ? 117.805 48.198  49.047  1.00 27.37 ? 124 ASP C N   1 
ATOM   3817 C  CA  . ASP C 1 127 ? 117.326 46.887  48.602  1.00 27.94 ? 124 ASP C CA  1 
ATOM   3818 C  C   . ASP C 1 127 ? 115.816 46.742  48.457  1.00 28.30 ? 124 ASP C C   1 
ATOM   3819 O  O   . ASP C 1 127 ? 115.059 47.134  49.337  1.00 28.66 ? 124 ASP C O   1 
ATOM   3820 C  CB  . ASP C 1 127 ? 117.807 45.798  49.570  1.00 28.39 ? 124 ASP C CB  1 
ATOM   3821 C  CG  . ASP C 1 127 ? 119.329 45.744  49.711  1.00 29.11 ? 124 ASP C CG  1 
ATOM   3822 O  OD1 . ASP C 1 127 ? 119.799 44.704  50.235  1.00 28.78 ? 124 ASP C OD1 1 
ATOM   3823 O  OD2 . ASP C 1 127 ? 120.043 46.714  49.311  1.00 28.19 ? 124 ASP C OD2 1 
ATOM   3824 N  N   . TYR C 1 128 ? 115.387 46.184  47.325  1.00 28.89 ? 125 TYR C N   1 
ATOM   3825 C  CA  . TYR C 1 128 ? 114.006 45.685  47.161  1.00 28.93 ? 125 TYR C CA  1 
ATOM   3826 C  C   . TYR C 1 128 ? 113.945 44.198  47.555  1.00 28.82 ? 125 TYR C C   1 
ATOM   3827 O  O   . TYR C 1 128 ? 114.453 43.301  46.872  1.00 28.98 ? 125 TYR C O   1 
ATOM   3828 C  CB  . TYR C 1 128 ? 113.445 45.941  45.744  1.00 28.56 ? 125 TYR C CB  1 
ATOM   3829 C  CG  . TYR C 1 128 ? 112.813 47.327  45.593  1.00 28.95 ? 125 TYR C CG  1 
ATOM   3830 C  CD1 . TYR C 1 128 ? 113.564 48.482  45.830  1.00 27.41 ? 125 TYR C CD1 1 
ATOM   3831 C  CD2 . TYR C 1 128 ? 111.469 47.483  45.209  1.00 27.71 ? 125 TYR C CD2 1 
ATOM   3832 C  CE1 . TYR C 1 128 ? 113.009 49.745  45.705  1.00 27.48 ? 125 TYR C CE1 1 
ATOM   3833 C  CE2 . TYR C 1 128 ? 110.901 48.767  45.084  1.00 28.28 ? 125 TYR C CE2 1 
ATOM   3834 C  CZ  . TYR C 1 128 ? 111.691 49.890  45.329  1.00 28.24 ? 125 TYR C CZ  1 
ATOM   3835 O  OH  . TYR C 1 128 ? 111.188 51.171  45.208  1.00 28.85 ? 125 TYR C OH  1 
ATOM   3836 N  N   . VAL C 1 129 ? 113.313 43.982  48.686  1.00 28.23 ? 126 VAL C N   1 
ATOM   3837 C  CA  . VAL C 1 129 ? 113.208 42.705  49.325  1.00 28.07 ? 126 VAL C CA  1 
ATOM   3838 C  C   . VAL C 1 129 ? 111.951 42.005  48.785  1.00 28.13 ? 126 VAL C C   1 
ATOM   3839 O  O   . VAL C 1 129 ? 111.824 40.792  48.840  1.00 28.06 ? 126 VAL C O   1 
ATOM   3840 C  CB  . VAL C 1 129 ? 113.225 42.986  50.857  1.00 28.27 ? 126 VAL C CB  1 
ATOM   3841 C  CG1 . VAL C 1 129 ? 112.188 42.218  51.633  1.00 28.55 ? 126 VAL C CG1 1 
ATOM   3842 C  CG2 . VAL C 1 129 ? 114.639 42.848  51.397  1.00 27.22 ? 126 VAL C CG2 1 
ATOM   3843 N  N   . GLY C 1 130 ? 111.040 42.807  48.249  1.00 28.65 ? 127 GLY C N   1 
ATOM   3844 C  CA  . GLY C 1 130 ? 109.896 42.365  47.457  1.00 28.67 ? 127 GLY C CA  1 
ATOM   3845 C  C   . GLY C 1 130 ? 109.712 43.308  46.270  1.00 29.07 ? 127 GLY C C   1 
ATOM   3846 O  O   . GLY C 1 130 ? 110.292 44.405  46.225  1.00 29.09 ? 127 GLY C O   1 
ATOM   3847 N  N   . LYS C 1 131 ? 108.887 42.896  45.317  1.00 29.23 ? 128 LYS C N   1 
ATOM   3848 C  CA  . LYS C 1 131 ? 108.711 43.625  44.065  1.00 29.66 ? 128 LYS C CA  1 
ATOM   3849 C  C   . LYS C 1 131 ? 108.324 45.085  44.293  1.00 29.63 ? 128 LYS C C   1 
ATOM   3850 O  O   . LYS C 1 131 ? 108.820 45.963  43.586  1.00 30.24 ? 128 LYS C O   1 
ATOM   3851 C  CB  . LYS C 1 131 ? 107.705 42.904  43.153  1.00 29.75 ? 128 LYS C CB  1 
ATOM   3852 C  CG  . LYS C 1 131 ? 107.954 43.110  41.669  1.00 31.21 ? 128 LYS C CG  1 
ATOM   3853 C  CD  . LYS C 1 131 ? 107.548 41.885  40.813  1.00 33.37 ? 128 LYS C CD  1 
ATOM   3854 C  CE  . LYS C 1 131 ? 106.034 41.641  40.722  1.00 34.05 ? 128 LYS C CE  1 
ATOM   3855 N  NZ  . LYS C 1 131 ? 105.677 40.670  39.635  1.00 32.35 ? 128 LYS C NZ  1 
ATOM   3856 N  N   . LYS C 1 132 ? 107.452 45.342  45.273  1.00 29.09 ? 129 LYS C N   1 
ATOM   3857 C  CA  . LYS C 1 132 ? 107.088 46.713  45.661  1.00 28.83 ? 129 LYS C CA  1 
ATOM   3858 C  C   . LYS C 1 132 ? 107.253 46.898  47.183  1.00 27.47 ? 129 LYS C C   1 
ATOM   3859 O  O   . LYS C 1 132 ? 106.456 47.550  47.866  1.00 27.38 ? 129 LYS C O   1 
ATOM   3860 C  CB  . LYS C 1 132 ? 105.689 47.143  45.140  1.00 28.93 ? 129 LYS C CB  1 
ATOM   3861 C  CG  . LYS C 1 132 ? 104.573 46.084  45.230  1.00 31.35 ? 129 LYS C CG  1 
ATOM   3862 C  CD  . LYS C 1 132 ? 103.119 46.652  45.297  1.00 31.37 ? 129 LYS C CD  1 
ATOM   3863 C  CE  . LYS C 1 132 ? 102.624 47.181  43.942  1.00 36.05 ? 129 LYS C CE  1 
ATOM   3864 N  NZ  . LYS C 1 132 ? 101.161 46.900  43.691  1.00 36.13 ? 129 LYS C NZ  1 
ATOM   3865 N  N   . PHE C 1 133 ? 108.319 46.307  47.698  1.00 26.03 ? 130 PHE C N   1 
ATOM   3866 C  CA  . PHE C 1 133 ? 108.609 46.360  49.102  1.00 24.99 ? 130 PHE C CA  1 
ATOM   3867 C  C   . PHE C 1 133 ? 110.112 46.663  49.312  1.00 24.54 ? 130 PHE C C   1 
ATOM   3868 O  O   . PHE C 1 133 ? 110.982 45.989  48.758  1.00 24.16 ? 130 PHE C O   1 
ATOM   3869 C  CB  . PHE C 1 133 ? 108.153 45.058  49.796  1.00 24.37 ? 130 PHE C CB  1 
ATOM   3870 C  CG  . PHE C 1 133 ? 107.845 45.248  51.235  1.00 24.64 ? 130 PHE C CG  1 
ATOM   3871 C  CD1 . PHE C 1 133 ? 108.848 45.095  52.204  1.00 23.88 ? 130 PHE C CD1 1 
ATOM   3872 C  CD2 . PHE C 1 133 ? 106.573 45.674  51.637  1.00 25.22 ? 130 PHE C CD2 1 
ATOM   3873 C  CE1 . PHE C 1 133 ? 108.584 45.328  53.549  1.00 23.56 ? 130 PHE C CE1 1 
ATOM   3874 C  CE2 . PHE C 1 133 ? 106.303 45.922  52.998  1.00 26.13 ? 130 PHE C CE2 1 
ATOM   3875 C  CZ  . PHE C 1 133 ? 107.317 45.749  53.956  1.00 24.20 ? 130 PHE C CZ  1 
ATOM   3876 N  N   . THR C 1 134 ? 110.388 47.709  50.090  1.00 24.51 ? 131 THR C N   1 
ATOM   3877 C  CA  . THR C 1 134 ? 111.752 48.185  50.384  1.00 23.96 ? 131 THR C CA  1 
ATOM   3878 C  C   . THR C 1 134 ? 111.858 48.803  51.791  1.00 24.34 ? 131 THR C C   1 
ATOM   3879 O  O   . THR C 1 134 ? 110.939 48.672  52.580  1.00 24.27 ? 131 THR C O   1 
ATOM   3880 C  CB  . THR C 1 134 ? 112.311 49.123  49.260  1.00 23.70 ? 131 THR C CB  1 
ATOM   3881 O  OG1 . THR C 1 134 ? 113.621 49.571  49.612  1.00 21.84 ? 131 THR C OG1 1 
ATOM   3882 C  CG2 . THR C 1 134 ? 111.414 50.302  48.976  1.00 22.94 ? 131 THR C CG2 1 
ATOM   3883 N  N   . LEU C 1 135 ? 112.983 49.445  52.117  1.00 25.11 ? 132 LEU C N   1 
ATOM   3884 C  CA  . LEU C 1 135 ? 113.199 49.979  53.469  1.00 25.21 ? 132 LEU C CA  1 
ATOM   3885 C  C   . LEU C 1 135 ? 114.168 51.135  53.449  1.00 25.80 ? 132 LEU C C   1 
ATOM   3886 O  O   . LEU C 1 135 ? 115.174 51.129  54.173  1.00 26.27 ? 132 LEU C O   1 
ATOM   3887 C  CB  . LEU C 1 135 ? 113.667 48.877  54.452  1.00 25.05 ? 132 LEU C CB  1 
ATOM   3888 C  CG  . LEU C 1 135 ? 114.821 47.925  54.062  1.00 24.74 ? 132 LEU C CG  1 
ATOM   3889 C  CD1 . LEU C 1 135 ? 115.543 47.362  55.285  1.00 22.99 ? 132 LEU C CD1 1 
ATOM   3890 C  CD2 . LEU C 1 135 ? 114.309 46.814  53.177  1.00 23.52 ? 132 LEU C CD2 1 
ATOM   3891 N  N   . HIS C 1 136 ? 113.853 52.145  52.639  1.00 26.55 ? 133 HIS C N   1 
ATOM   3892 C  CA  . HIS C 1 136 ? 114.787 53.282  52.403  1.00 26.92 ? 133 HIS C CA  1 
ATOM   3893 C  C   . HIS C 1 136 ? 115.231 54.115  53.623  1.00 26.67 ? 133 HIS C C   1 
ATOM   3894 O  O   . HIS C 1 136 ? 116.290 54.716  53.580  1.00 25.71 ? 133 HIS C O   1 
ATOM   3895 C  CB  . HIS C 1 136 ? 114.254 54.213  51.307  1.00 26.36 ? 133 HIS C CB  1 
ATOM   3896 C  CG  . HIS C 1 136 ? 114.189 53.578  49.956  1.00 27.12 ? 133 HIS C CG  1 
ATOM   3897 N  ND1 . HIS C 1 136 ? 114.763 52.356  49.676  1.00 26.76 ? 133 HIS C ND1 1 
ATOM   3898 C  CD2 . HIS C 1 136 ? 113.638 54.009  48.797  1.00 26.00 ? 133 HIS C CD2 1 
ATOM   3899 C  CE1 . HIS C 1 136 ? 114.549 52.056  48.408  1.00 26.39 ? 133 HIS C CE1 1 
ATOM   3900 N  NE2 . HIS C 1 136 ? 113.874 53.044  47.854  1.00 26.37 ? 133 HIS C NE2 1 
ATOM   3901 N  N   . TYR C 1 137 ? 114.402 54.153  54.673  1.00 26.92 ? 134 TYR C N   1 
ATOM   3902 C  CA  . TYR C 1 137 ? 114.620 55.023  55.856  1.00 27.28 ? 134 TYR C CA  1 
ATOM   3903 C  C   . TYR C 1 137 ? 114.644 54.181  57.140  1.00 27.61 ? 134 TYR C C   1 
ATOM   3904 O  O   . TYR C 1 137 ? 114.718 54.713  58.265  1.00 28.40 ? 134 TYR C O   1 
ATOM   3905 C  CB  . TYR C 1 137 ? 113.587 56.193  55.903  1.00 26.68 ? 134 TYR C CB  1 
ATOM   3906 C  CG  . TYR C 1 137 ? 113.719 57.028  54.644  1.00 26.67 ? 134 TYR C CG  1 
ATOM   3907 C  CD1 . TYR C 1 137 ? 112.772 56.939  53.593  1.00 26.77 ? 134 TYR C CD1 1 
ATOM   3908 C  CD2 . TYR C 1 137 ? 114.854 57.810  54.445  1.00 25.87 ? 134 TYR C CD2 1 
ATOM   3909 C  CE1 . TYR C 1 137 ? 112.958 57.653  52.401  1.00 27.54 ? 134 TYR C CE1 1 
ATOM   3910 C  CE2 . TYR C 1 137 ? 115.052 58.528  53.260  1.00 26.56 ? 134 TYR C CE2 1 
ATOM   3911 C  CZ  . TYR C 1 137 ? 114.104 58.444  52.240  1.00 27.86 ? 134 TYR C CZ  1 
ATOM   3912 O  OH  . TYR C 1 137 ? 114.340 59.162  51.071  1.00 28.23 ? 134 TYR C OH  1 
ATOM   3913 N  N   . GLY C 1 138 ? 114.622 52.863  56.932  1.00 27.07 ? 135 GLY C N   1 
ATOM   3914 C  CA  . GLY C 1 138 ? 114.451 51.860  57.967  1.00 26.17 ? 135 GLY C CA  1 
ATOM   3915 C  C   . GLY C 1 138 ? 113.395 50.857  57.528  1.00 25.94 ? 135 GLY C C   1 
ATOM   3916 O  O   . GLY C 1 138 ? 112.613 51.103  56.579  1.00 25.93 ? 135 GLY C O   1 
ATOM   3917 N  N   . ALA C 1 139 ? 113.362 49.726  58.220  1.00 25.31 ? 136 ALA C N   1 
ATOM   3918 C  CA  . ALA C 1 139 ? 112.345 48.712  57.995  1.00 25.38 ? 136 ALA C CA  1 
ATOM   3919 C  C   . ALA C 1 139 ? 111.029 49.244  58.566  1.00 25.54 ? 136 ALA C C   1 
ATOM   3920 O  O   . ALA C 1 139 ? 110.998 49.728  59.719  1.00 25.88 ? 136 ALA C O   1 
ATOM   3921 C  CB  . ALA C 1 139 ? 112.740 47.362  58.672  1.00 24.42 ? 136 ALA C CB  1 
ATOM   3922 N  N   . VAL C 1 140 ? 109.950 49.163  57.781  1.00 25.33 ? 137 VAL C N   1 
ATOM   3923 C  CA  . VAL C 1 140 ? 108.632 49.571  58.263  1.00 25.32 ? 137 VAL C CA  1 
ATOM   3924 C  C   . VAL C 1 140 ? 107.564 48.531  57.936  1.00 25.80 ? 137 VAL C C   1 
ATOM   3925 O  O   . VAL C 1 140 ? 107.586 47.912  56.862  1.00 26.00 ? 137 VAL C O   1 
ATOM   3926 C  CB  . VAL C 1 140 ? 108.216 50.970  57.715  1.00 25.85 ? 137 VAL C CB  1 
ATOM   3927 C  CG1 . VAL C 1 140 ? 109.109 52.049  58.269  1.00 25.23 ? 137 VAL C CG1 1 
ATOM   3928 C  CG2 . VAL C 1 140 ? 108.220 51.007  56.193  1.00 24.13 ? 137 VAL C CG2 1 
ATOM   3929 N  N   . VAL C 1 141 ? 106.626 48.342  58.855  1.00 26.11 ? 138 VAL C N   1 
ATOM   3930 C  CA  . VAL C 1 141 ? 105.535 47.368  58.682  1.00 26.53 ? 138 VAL C CA  1 
ATOM   3931 C  C   . VAL C 1 141 ? 104.262 47.980  59.244  1.00 26.77 ? 138 VAL C C   1 
ATOM   3932 O  O   . VAL C 1 141 ? 104.334 48.816  60.145  1.00 26.84 ? 138 VAL C O   1 
ATOM   3933 C  CB  . VAL C 1 141 ? 105.826 46.033  59.449  1.00 26.76 ? 138 VAL C CB  1 
ATOM   3934 C  CG1 . VAL C 1 141 ? 104.607 45.091  59.407  1.00 26.67 ? 138 VAL C CG1 1 
ATOM   3935 C  CG2 . VAL C 1 141 ? 107.056 45.314  58.876  1.00 27.09 ? 138 VAL C CG2 1 
ATOM   3936 N  N   . ALA C 1 142 ? 103.101 47.580  58.721  1.00 27.14 ? 139 ALA C N   1 
ATOM   3937 C  CA  . ALA C 1 142 ? 101.821 47.884  59.378  1.00 27.47 ? 139 ALA C CA  1 
ATOM   3938 C  C   . ALA C 1 142 ? 101.437 46.699  60.236  1.00 27.81 ? 139 ALA C C   1 
ATOM   3939 O  O   . ALA C 1 142 ? 101.206 45.617  59.713  1.00 29.17 ? 139 ALA C O   1 
ATOM   3940 C  CB  . ALA C 1 142 ? 100.733 48.186  58.366  1.00 27.05 ? 139 ALA C CB  1 
ATOM   3941 N  N   . GLY C 1 143 ? 101.393 46.883  61.551  1.00 28.21 ? 140 GLY C N   1 
ATOM   3942 C  CA  . GLY C 1 143 ? 101.126 45.774  62.480  1.00 28.29 ? 140 GLY C CA  1 
ATOM   3943 C  C   . GLY C 1 143 ? 102.282 44.800  62.610  1.00 28.69 ? 140 GLY C C   1 
ATOM   3944 O  O   . GLY C 1 143 ? 103.438 45.189  62.576  1.00 29.05 ? 140 GLY C O   1 
ATOM   3945 N  N   . GLU C 1 144 ? 101.977 43.518  62.773  1.00 29.83 ? 141 GLU C N   1 
ATOM   3946 C  CA  . GLU C 1 144 ? 103.011 42.482  62.927  1.00 30.49 ? 141 GLU C CA  1 
ATOM   3947 C  C   . GLU C 1 144 ? 103.615 42.061  61.575  1.00 30.26 ? 141 GLU C C   1 
ATOM   3948 O  O   . GLU C 1 144 ? 102.868 41.889  60.599  1.00 30.19 ? 141 GLU C O   1 
ATOM   3949 C  CB  . GLU C 1 144 ? 102.421 41.253  63.613  1.00 30.77 ? 141 GLU C CB  1 
ATOM   3950 C  CG  . GLU C 1 144 ? 103.483 40.357  64.208  1.00 33.48 ? 141 GLU C CG  1 
ATOM   3951 C  CD  . GLU C 1 144 ? 103.005 38.940  64.466  1.00 36.06 ? 141 GLU C CD  1 
ATOM   3952 O  OE1 . GLU C 1 144 ? 101.969 38.772  65.153  1.00 37.18 ? 141 GLU C OE1 1 
ATOM   3953 O  OE2 . GLU C 1 144 ? 103.684 37.994  63.992  1.00 36.76 ? 141 GLU C OE2 1 
ATOM   3954 N  N   . PRO C 1 145 ? 104.960 41.900  61.507  1.00 29.97 ? 142 PRO C N   1 
ATOM   3955 C  CA  . PRO C 1 145 ? 105.541 41.385  60.262  1.00 30.05 ? 142 PRO C CA  1 
ATOM   3956 C  C   . PRO C 1 145 ? 105.178 39.909  60.021  1.00 30.50 ? 142 PRO C C   1 
ATOM   3957 O  O   . PRO C 1 145 ? 105.735 39.002  60.652  1.00 30.60 ? 142 PRO C O   1 
ATOM   3958 C  CB  . PRO C 1 145 ? 107.057 41.598  60.454  1.00 29.74 ? 142 PRO C CB  1 
ATOM   3959 C  CG  . PRO C 1 145 ? 107.257 41.662  61.917  1.00 28.62 ? 142 PRO C CG  1 
ATOM   3960 C  CD  . PRO C 1 145 ? 105.994 42.203  62.519  1.00 29.69 ? 142 PRO C CD  1 
ATOM   3961 N  N   . ARG C 1 146 ? 104.230 39.677  59.116  1.00 31.10 ? 143 ARG C N   1 
ATOM   3962 C  CA  . ARG C 1 146 ? 103.752 38.321  58.860  1.00 31.85 ? 143 ARG C CA  1 
ATOM   3963 C  C   . ARG C 1 146 ? 104.194 37.795  57.503  1.00 31.35 ? 143 ARG C C   1 
ATOM   3964 O  O   . ARG C 1 146 ? 104.666 36.665  57.407  1.00 31.57 ? 143 ARG C O   1 
ATOM   3965 C  CB  . ARG C 1 146 ? 102.236 38.238  59.009  1.00 32.42 ? 143 ARG C CB  1 
ATOM   3966 C  CG  . ARG C 1 146 ? 101.727 38.949  60.244  1.00 35.31 ? 143 ARG C CG  1 
ATOM   3967 C  CD  . ARG C 1 146 ? 100.452 38.333  60.773  1.00 41.10 ? 143 ARG C CD  1 
ATOM   3968 N  NE  . ARG C 1 146 ? 99.967  39.072  61.939  1.00 44.86 ? 143 ARG C NE  1 
ATOM   3969 C  CZ  . ARG C 1 146 ? 99.297  38.539  62.961  1.00 45.74 ? 143 ARG C CZ  1 
ATOM   3970 N  NH1 . ARG C 1 146 ? 99.022  37.232  62.988  1.00 47.20 ? 143 ARG C NH1 1 
ATOM   3971 N  NH2 . ARG C 1 146 ? 98.905  39.321  63.963  1.00 44.82 ? 143 ARG C NH2 1 
ATOM   3972 N  N   . SER C 1 147 ? 104.055 38.617  56.466  1.00 30.75 ? 144 SER C N   1 
ATOM   3973 C  CA  . SER C 1 147 ? 104.470 38.229  55.114  1.00 30.28 ? 144 SER C CA  1 
ATOM   3974 C  C   . SER C 1 147 ? 105.980 38.015  54.981  1.00 30.34 ? 144 SER C C   1 
ATOM   3975 O  O   . SER C 1 147 ? 106.782 38.525  55.776  1.00 30.95 ? 144 SER C O   1 
ATOM   3976 C  CB  . SER C 1 147 ? 103.984 39.263  54.083  1.00 30.35 ? 144 SER C CB  1 
ATOM   3977 O  OG  . SER C 1 147 ? 104.889 40.350  53.937  1.00 29.01 ? 144 SER C OG  1 
ATOM   3978 N  N   . GLU C 1 148 ? 106.361 37.285  53.945  1.00 30.38 ? 145 GLU C N   1 
ATOM   3979 C  CA  . GLU C 1 148 ? 107.761 37.001  53.669  1.00 30.50 ? 145 GLU C CA  1 
ATOM   3980 C  C   . GLU C 1 148 ? 108.596 38.259  53.362  1.00 30.18 ? 145 GLU C C   1 
ATOM   3981 O  O   . GLU C 1 148 ? 109.762 38.331  53.758  1.00 30.06 ? 145 GLU C O   1 
ATOM   3982 C  CB  . GLU C 1 148 ? 107.857 35.987  52.542  1.00 30.53 ? 145 GLU C CB  1 
ATOM   3983 C  CG  . GLU C 1 148 ? 108.819 34.845  52.842  1.00 32.92 ? 145 GLU C CG  1 
ATOM   3984 C  CD  . GLU C 1 148 ? 108.246 33.784  53.812  1.00 34.72 ? 145 GLU C CD  1 
ATOM   3985 O  OE1 . GLU C 1 148 ? 108.034 32.627  53.355  1.00 36.06 ? 145 GLU C OE1 1 
ATOM   3986 O  OE2 . GLU C 1 148 ? 108.020 34.094  55.015  1.00 33.02 ? 145 GLU C OE2 1 
ATOM   3987 N  N   . GLU C 1 149 ? 107.986 39.230  52.665  1.00 29.63 ? 146 GLU C N   1 
ATOM   3988 C  CA  . GLU C 1 149 ? 108.570 40.561  52.390  1.00 29.07 ? 146 GLU C CA  1 
ATOM   3989 C  C   . GLU C 1 149 ? 108.895 41.303  53.683  1.00 28.46 ? 146 GLU C C   1 
ATOM   3990 O  O   . GLU C 1 149 ? 109.990 41.834  53.866  1.00 27.99 ? 146 GLU C O   1 
ATOM   3991 C  CB  . GLU C 1 149 ? 107.568 41.431  51.618  1.00 28.95 ? 146 GLU C CB  1 
ATOM   3992 C  CG  . GLU C 1 149 ? 107.575 41.325  50.094  1.00 29.51 ? 146 GLU C CG  1 
ATOM   3993 C  CD  . GLU C 1 149 ? 106.387 42.072  49.451  1.00 29.92 ? 146 GLU C CD  1 
ATOM   3994 O  OE1 . GLU C 1 149 ? 105.406 42.363  50.187  1.00 28.75 ? 146 GLU C OE1 1 
ATOM   3995 O  OE2 . GLU C 1 149 ? 106.442 42.374  48.217  1.00 31.27 ? 146 GLU C OE2 1 
ATOM   3996 N  N   . GLU C 1 150 ? 107.900 41.352  54.562  1.00 28.31 ? 147 GLU C N   1 
ATOM   3997 C  CA  . GLU C 1 150 ? 107.995 42.028  55.851  1.00 27.68 ? 147 GLU C CA  1 
ATOM   3998 C  C   . GLU C 1 150 ? 109.108 41.452  56.717  1.00 27.39 ? 147 GLU C C   1 
ATOM   3999 O  O   . GLU C 1 150 ? 109.961 42.188  57.188  1.00 27.72 ? 147 GLU C O   1 
ATOM   4000 C  CB  . GLU C 1 150 ? 106.649 41.966  56.577  1.00 27.41 ? 147 GLU C CB  1 
ATOM   4001 C  CG  . GLU C 1 150 ? 105.632 42.841  55.922  1.00 27.58 ? 147 GLU C CG  1 
ATOM   4002 C  CD  . GLU C 1 150 ? 104.205 42.570  56.336  1.00 29.48 ? 147 GLU C CD  1 
ATOM   4003 O  OE1 . GLU C 1 150 ? 103.894 41.522  56.954  1.00 29.71 ? 147 GLU C OE1 1 
ATOM   4004 O  OE2 . GLU C 1 150 ? 103.368 43.429  55.994  1.00 31.77 ? 147 GLU C OE2 1 
ATOM   4005 N  N   . LYS C 1 151 ? 109.110 40.134  56.905  1.00 27.30 ? 148 LYS C N   1 
ATOM   4006 C  CA  . LYS C 1 151 ? 110.116 39.509  57.758  1.00 27.00 ? 148 LYS C CA  1 
ATOM   4007 C  C   . LYS C 1 151 ? 111.542 39.730  57.204  1.00 26.82 ? 148 LYS C C   1 
ATOM   4008 O  O   . LYS C 1 151 ? 112.486 39.923  57.968  1.00 26.25 ? 148 LYS C O   1 
ATOM   4009 C  CB  . LYS C 1 151 ? 109.800 38.019  57.980  1.00 27.13 ? 148 LYS C CB  1 
ATOM   4010 C  CG  . LYS C 1 151 ? 108.580 37.744  58.884  1.00 26.96 ? 148 LYS C CG  1 
ATOM   4011 C  CD  . LYS C 1 151 ? 108.472 36.259  59.213  1.00 26.63 ? 148 LYS C CD  1 
ATOM   4012 C  CE  . LYS C 1 151 ? 107.050 35.825  59.586  1.00 27.89 ? 148 LYS C CE  1 
ATOM   4013 N  NZ  . LYS C 1 151 ? 106.871 34.314  59.705  1.00 26.47 ? 148 LYS C NZ  1 
ATOM   4014 N  N   . GLU C 1 152 ? 111.669 39.732  55.876  1.00 26.75 ? 149 GLU C N   1 
ATOM   4015 C  CA  . GLU C 1 152 ? 112.949 39.890  55.200  1.00 26.67 ? 149 GLU C CA  1 
ATOM   4016 C  C   . GLU C 1 152 ? 113.418 41.356  55.216  1.00 27.45 ? 149 GLU C C   1 
ATOM   4017 O  O   . GLU C 1 152 ? 114.637 41.632  55.275  1.00 27.92 ? 149 GLU C O   1 
ATOM   4018 C  CB  . GLU C 1 152 ? 112.845 39.348  53.769  1.00 26.42 ? 149 GLU C CB  1 
ATOM   4019 C  CG  . GLU C 1 152 ? 114.156 39.296  52.971  1.00 26.38 ? 149 GLU C CG  1 
ATOM   4020 C  CD  . GLU C 1 152 ? 115.291 38.503  53.651  1.00 27.06 ? 149 GLU C CD  1 
ATOM   4021 O  OE1 . GLU C 1 152 ? 116.463 38.858  53.393  1.00 25.91 ? 149 GLU C OE1 1 
ATOM   4022 O  OE2 . GLU C 1 152 ? 115.032 37.536  54.422  1.00 27.71 ? 149 GLU C OE2 1 
ATOM   4023 N  N   . ALA C 1 153 ? 112.458 42.289  55.140  1.00 27.09 ? 150 ALA C N   1 
ATOM   4024 C  CA  . ALA C 1 153 ? 112.747 43.711  55.300  1.00 26.62 ? 150 ALA C CA  1 
ATOM   4025 C  C   . ALA C 1 153 ? 113.490 43.911  56.621  1.00 26.48 ? 150 ALA C C   1 
ATOM   4026 O  O   . ALA C 1 153 ? 114.536 44.541  56.649  1.00 26.63 ? 150 ALA C O   1 
ATOM   4027 C  CB  . ALA C 1 153 ? 111.473 44.533  55.263  1.00 25.91 ? 150 ALA C CB  1 
ATOM   4028 N  N   . CYS C 1 154 ? 112.957 43.339  57.697  1.00 26.15 ? 151 CYS C N   1 
ATOM   4029 C  CA  . CYS C 1 154 ? 113.600 43.398  59.009  1.00 26.23 ? 151 CYS C CA  1 
ATOM   4030 C  C   . CYS C 1 154 ? 114.961 42.729  59.029  1.00 25.68 ? 151 CYS C C   1 
ATOM   4031 O  O   . CYS C 1 154 ? 115.919 43.311  59.518  1.00 26.10 ? 151 CYS C O   1 
ATOM   4032 C  CB  . CYS C 1 154 ? 112.718 42.755  60.062  1.00 25.80 ? 151 CYS C CB  1 
ATOM   4033 S  SG  . CYS C 1 154 ? 111.161 43.560  60.200  1.00 27.09 ? 151 CYS C SG  1 
ATOM   4034 N  N   . ARG C 1 155 ? 115.041 41.506  58.507  1.00 25.58 ? 152 ARG C N   1 
ATOM   4035 C  CA  . ARG C 1 155 ? 116.310 40.802  58.437  1.00 24.94 ? 152 ARG C CA  1 
ATOM   4036 C  C   . ARG C 1 155 ? 117.357 41.676  57.753  1.00 24.97 ? 152 ARG C C   1 
ATOM   4037 O  O   . ARG C 1 155 ? 118.462 41.840  58.271  1.00 24.85 ? 152 ARG C O   1 
ATOM   4038 C  CB  . ARG C 1 155 ? 116.156 39.484  57.693  1.00 25.05 ? 152 ARG C CB  1 
ATOM   4039 C  CG  . ARG C 1 155 ? 115.521 38.364  58.503  1.00 24.79 ? 152 ARG C CG  1 
ATOM   4040 C  CD  . ARG C 1 155 ? 115.485 37.073  57.694  1.00 25.63 ? 152 ARG C CD  1 
ATOM   4041 N  NE  . ARG C 1 155 ? 114.485 36.159  58.240  1.00 26.67 ? 152 ARG C NE  1 
ATOM   4042 C  CZ  . ARG C 1 155 ? 113.302 35.915  57.680  1.00 25.43 ? 152 ARG C CZ  1 
ATOM   4043 N  NH1 . ARG C 1 155 ? 112.968 36.488  56.516  1.00 25.22 ? 152 ARG C NH1 1 
ATOM   4044 N  NH2 . ARG C 1 155 ? 112.455 35.093  58.286  1.00 21.46 ? 152 ARG C NH2 1 
ATOM   4045 N  N   . ARG C 1 156 ? 116.984 42.262  56.609  1.00 24.77 ? 153 ARG C N   1 
ATOM   4046 C  CA  . ARG C 1 156 ? 117.919 42.982  55.744  1.00 24.57 ? 153 ARG C CA  1 
ATOM   4047 C  C   . ARG C 1 156 ? 118.562 44.223  56.377  1.00 24.69 ? 153 ARG C C   1 
ATOM   4048 O  O   . ARG C 1 156 ? 119.747 44.488  56.148  1.00 24.35 ? 153 ARG C O   1 
ATOM   4049 C  CB  . ARG C 1 156 ? 117.266 43.336  54.404  1.00 24.62 ? 153 ARG C CB  1 
ATOM   4050 C  CG  . ARG C 1 156 ? 118.255 43.903  53.372  1.00 23.93 ? 153 ARG C CG  1 
ATOM   4051 C  CD  . ARG C 1 156 ? 119.289 42.869  52.952  1.00 22.35 ? 153 ARG C CD  1 
ATOM   4052 N  NE  . ARG C 1 156 ? 118.613 41.613  52.632  1.00 23.46 ? 153 ARG C NE  1 
ATOM   4053 C  CZ  . ARG C 1 156 ? 118.031 41.353  51.464  1.00 23.08 ? 153 ARG C CZ  1 
ATOM   4054 N  NH1 . ARG C 1 156 ? 117.416 40.196  51.276  1.00 22.37 ? 153 ARG C NH1 1 
ATOM   4055 N  NH2 . ARG C 1 156 ? 118.061 42.250  50.483  1.00 22.69 ? 153 ARG C NH2 1 
ATOM   4056 N  N   . LEU C 1 157 ? 117.764 44.970  57.145  1.00 24.83 ? 154 LEU C N   1 
ATOM   4057 C  CA  . LEU C 1 157 ? 118.233 46.057  57.997  1.00 25.22 ? 154 LEU C CA  1 
ATOM   4058 C  C   . LEU C 1 157 ? 119.346 45.557  58.937  1.00 26.25 ? 154 LEU C C   1 
ATOM   4059 O  O   . LEU C 1 157 ? 120.467 46.126  58.972  1.00 26.38 ? 154 LEU C O   1 
ATOM   4060 C  CB  . LEU C 1 157 ? 117.062 46.649  58.817  1.00 24.77 ? 154 LEU C CB  1 
ATOM   4061 C  CG  . LEU C 1 157 ? 117.361 47.974  59.532  1.00 23.31 ? 154 LEU C CG  1 
ATOM   4062 C  CD1 . LEU C 1 157 ? 117.205 49.144  58.557  1.00 24.12 ? 154 LEU C CD1 1 
ATOM   4063 C  CD2 . LEU C 1 157 ? 116.471 48.187  60.720  1.00 21.63 ? 154 LEU C CD2 1 
ATOM   4064 N  N   . GLY C 1 158 ? 119.035 44.494  59.682  1.00 26.10 ? 155 GLY C N   1 
ATOM   4065 C  CA  . GLY C 1 158 ? 120.011 43.871  60.566  1.00 27.08 ? 155 GLY C CA  1 
ATOM   4066 C  C   . GLY C 1 158 ? 121.255 43.469  59.798  1.00 27.50 ? 155 GLY C C   1 
ATOM   4067 O  O   . GLY C 1 158 ? 122.381 43.706  60.249  1.00 27.56 ? 155 GLY C O   1 
ATOM   4068 N  N   . ARG C 1 159 ? 121.030 42.886  58.619  1.00 27.46 ? 156 ARG C N   1 
ATOM   4069 C  CA  . ARG C 1 159 ? 122.100 42.397  57.750  1.00 27.71 ? 156 ARG C CA  1 
ATOM   4070 C  C   . ARG C 1 159 ? 122.949 43.551  57.205  1.00 27.58 ? 156 ARG C C   1 
ATOM   4071 O  O   . ARG C 1 159 ? 124.177 43.453  57.211  1.00 28.25 ? 156 ARG C O   1 
ATOM   4072 C  CB  . ARG C 1 159 ? 121.531 41.449  56.645  1.00 27.10 ? 156 ARG C CB  1 
ATOM   4073 C  CG  . ARG C 1 159 ? 122.409 41.120  55.412  1.00 27.07 ? 156 ARG C CG  1 
ATOM   4074 C  CD  . ARG C 1 159 ? 123.861 40.707  55.718  1.00 26.03 ? 156 ARG C CD  1 
ATOM   4075 N  NE  . ARG C 1 159 ? 124.023 39.319  56.124  1.00 27.64 ? 156 ARG C NE  1 
ATOM   4076 C  CZ  . ARG C 1 159 ? 124.849 38.424  55.564  1.00 25.71 ? 156 ARG C CZ  1 
ATOM   4077 N  NH1 . ARG C 1 159 ? 125.645 38.719  54.542  1.00 24.22 ? 156 ARG C NH1 1 
ATOM   4078 N  NH2 . ARG C 1 159 ? 124.875 37.206  56.051  1.00 25.13 ? 156 ARG C NH2 1 
ATOM   4079 N  N   . ARG C 1 160 ? 122.318 44.638  56.764  1.00 27.03 ? 157 ARG C N   1 
ATOM   4080 C  CA  . ARG C 1 160 ? 123.084 45.770  56.261  1.00 26.96 ? 157 ARG C CA  1 
ATOM   4081 C  C   . ARG C 1 160 ? 123.907 46.508  57.350  1.00 26.87 ? 157 ARG C C   1 
ATOM   4082 O  O   . ARG C 1 160 ? 125.011 46.953  57.080  1.00 26.72 ? 157 ARG C O   1 
ATOM   4083 C  CB  . ARG C 1 160 ? 122.192 46.707  55.450  1.00 26.66 ? 157 ARG C CB  1 
ATOM   4084 C  CG  . ARG C 1 160 ? 122.926 47.832  54.668  1.00 27.94 ? 157 ARG C CG  1 
ATOM   4085 C  CD  . ARG C 1 160 ? 124.050 47.360  53.671  1.00 28.85 ? 157 ARG C CD  1 
ATOM   4086 N  NE  . ARG C 1 160 ? 123.746 46.149  52.900  1.00 30.62 ? 157 ARG C NE  1 
ATOM   4087 C  CZ  . ARG C 1 160 ? 122.796 46.032  51.966  1.00 31.11 ? 157 ARG C CZ  1 
ATOM   4088 N  NH1 . ARG C 1 160 ? 122.002 47.054  51.650  1.00 30.76 ? 157 ARG C NH1 1 
ATOM   4089 N  NH2 . ARG C 1 160 ? 122.627 44.867  51.357  1.00 30.92 ? 157 ARG C NH2 1 
ATOM   4090 N  N   . LEU C 1 161 ? 123.367 46.625  58.568  1.00 27.25 ? 158 LEU C N   1 
ATOM   4091 C  CA  . LEU C 1 161 ? 124.086 47.190  59.738  1.00 26.71 ? 158 LEU C CA  1 
ATOM   4092 C  C   . LEU C 1 161 ? 125.347 46.406  60.016  1.00 26.88 ? 158 LEU C C   1 
ATOM   4093 O  O   . LEU C 1 161 ? 126.434 46.984  60.168  1.00 27.32 ? 158 LEU C O   1 
ATOM   4094 C  CB  . LEU C 1 161 ? 123.228 47.093  61.007  1.00 26.14 ? 158 LEU C CB  1 
ATOM   4095 C  CG  . LEU C 1 161 ? 123.125 48.214  62.061  1.00 26.46 ? 158 LEU C CG  1 
ATOM   4096 C  CD1 . LEU C 1 161 ? 122.813 47.624  63.422  1.00 22.46 ? 158 LEU C CD1 1 
ATOM   4097 C  CD2 . LEU C 1 161 ? 124.294 49.224  62.139  1.00 24.52 ? 158 LEU C CD2 1 
ATOM   4098 N  N   . ALA C 1 162 ? 125.181 45.084  60.129  1.00 26.20 ? 159 ALA C N   1 
ATOM   4099 C  CA  . ALA C 1 162 ? 126.286 44.180  60.366  1.00 25.65 ? 159 ALA C CA  1 
ATOM   4100 C  C   . ALA C 1 162 ? 127.365 44.402  59.291  1.00 25.68 ? 159 ALA C C   1 
ATOM   4101 O  O   . ALA C 1 162 ? 128.549 44.523  59.611  1.00 25.48 ? 159 ALA C O   1 
ATOM   4102 C  CB  . ALA C 1 162 ? 125.793 42.753  60.386  1.00 25.02 ? 159 ALA C CB  1 
ATOM   4103 N  N   . GLU C 1 163 ? 126.935 44.504  58.033  1.00 25.54 ? 160 GLU C N   1 
ATOM   4104 C  CA  . GLU C 1 163 ? 127.822 44.789  56.911  1.00 25.74 ? 160 GLU C CA  1 
ATOM   4105 C  C   . GLU C 1 163 ? 128.504 46.161  56.956  1.00 26.15 ? 160 GLU C C   1 
ATOM   4106 O  O   . GLU C 1 163 ? 129.707 46.262  56.671  1.00 25.86 ? 160 GLU C O   1 
ATOM   4107 C  CB  . GLU C 1 163 ? 127.081 44.607  55.595  1.00 25.11 ? 160 GLU C CB  1 
ATOM   4108 C  CG  . GLU C 1 163 ? 126.704 43.186  55.349  1.00 25.72 ? 160 GLU C CG  1 
ATOM   4109 C  CD  . GLU C 1 163 ? 125.821 43.001  54.123  1.00 27.43 ? 160 GLU C CD  1 
ATOM   4110 O  OE1 . GLU C 1 163 ? 125.098 43.946  53.725  1.00 26.78 ? 160 GLU C OE1 1 
ATOM   4111 O  OE2 . GLU C 1 163 ? 125.830 41.880  53.568  1.00 27.30 ? 160 GLU C OE2 1 
ATOM   4112 N  N   . TRP C 1 164 ? 127.754 47.217  57.288  1.00 26.54 ? 161 TRP C N   1 
ATOM   4113 C  CA  . TRP C 1 164 ? 128.379 48.529  57.449  1.00 27.23 ? 161 TRP C CA  1 
ATOM   4114 C  C   . TRP C 1 164 ? 129.437 48.483  58.562  1.00 27.58 ? 161 TRP C C   1 
ATOM   4115 O  O   . TRP C 1 164 ? 130.529 49.008  58.397  1.00 28.54 ? 161 TRP C O   1 
ATOM   4116 C  CB  . TRP C 1 164 ? 127.359 49.650  57.686  1.00 27.65 ? 161 TRP C CB  1 
ATOM   4117 C  CG  . TRP C 1 164 ? 126.543 50.034  56.500  1.00 27.41 ? 161 TRP C CG  1 
ATOM   4118 C  CD1 . TRP C 1 164 ? 125.318 50.611  56.521  1.00 27.86 ? 161 TRP C CD1 1 
ATOM   4119 C  CD2 . TRP C 1 164 ? 126.872 49.846  55.103  1.00 29.51 ? 161 TRP C CD2 1 
ATOM   4120 N  NE1 . TRP C 1 164 ? 124.861 50.825  55.234  1.00 27.68 ? 161 TRP C NE1 1 
ATOM   4121 C  CE2 . TRP C 1 164 ? 125.793 50.359  54.348  1.00 29.09 ? 161 TRP C CE2 1 
ATOM   4122 C  CE3 . TRP C 1 164 ? 127.981 49.305  54.419  1.00 28.70 ? 161 TRP C CE3 1 
ATOM   4123 C  CZ2 . TRP C 1 164 ? 125.784 50.344  52.943  1.00 30.09 ? 161 TRP C CZ2 1 
ATOM   4124 C  CZ3 . TRP C 1 164 ? 127.966 49.291  53.026  1.00 28.75 ? 161 TRP C CZ3 1 
ATOM   4125 C  CH2 . TRP C 1 164 ? 126.872 49.808  52.305  1.00 28.58 ? 161 TRP C CH2 1 
ATOM   4126 N  N   . VAL C 1 165 ? 129.131 47.811  59.667  1.00 27.13 ? 162 VAL C N   1 
ATOM   4127 C  CA  . VAL C 1 165 ? 130.096 47.635  60.741  1.00 26.97 ? 162 VAL C CA  1 
ATOM   4128 C  C   . VAL C 1 165 ? 131.303 46.792  60.307  1.00 26.99 ? 162 VAL C C   1 
ATOM   4129 O  O   . VAL C 1 165 ? 132.438 47.077  60.713  1.00 26.77 ? 162 VAL C O   1 
ATOM   4130 C  CB  . VAL C 1 165 ? 129.434 47.034  62.013  1.00 27.29 ? 162 VAL C CB  1 
ATOM   4131 C  CG1 . VAL C 1 165 ? 130.492 46.545  63.010  1.00 26.53 ? 162 VAL C CG1 1 
ATOM   4132 C  CG2 . VAL C 1 165 ? 128.507 48.068  62.668  1.00 26.49 ? 162 VAL C CG2 1 
ATOM   4133 N  N   . ALA C 1 166 ? 131.061 45.772  59.481  1.00 26.89 ? 163 ALA C N   1 
ATOM   4134 C  CA  . ALA C 1 166 ? 132.154 44.897  59.012  1.00 26.78 ? 163 ALA C CA  1 
ATOM   4135 C  C   . ALA C 1 166 ? 133.069 45.639  58.042  1.00 26.50 ? 163 ALA C C   1 
ATOM   4136 O  O   . ALA C 1 166 ? 134.285 45.448  58.068  1.00 27.01 ? 163 ALA C O   1 
ATOM   4137 C  CB  . ALA C 1 166 ? 131.628 43.587  58.395  1.00 26.17 ? 163 ALA C CB  1 
ATOM   4138 N  N   . ILE C 1 167 ? 132.497 46.516  57.224  1.00 26.17 ? 164 ILE C N   1 
ATOM   4139 C  CA  . ILE C 1 167 ? 133.285 47.279  56.260  1.00 25.54 ? 164 ILE C CA  1 
ATOM   4140 C  C   . ILE C 1 167 ? 133.993 48.453  56.912  1.00 26.30 ? 164 ILE C C   1 
ATOM   4141 O  O   . ILE C 1 167 ? 135.179 48.677  56.650  1.00 26.47 ? 164 ILE C O   1 
ATOM   4142 C  CB  . ILE C 1 167 ? 132.426 47.779  55.094  1.00 24.95 ? 164 ILE C CB  1 
ATOM   4143 C  CG1 . ILE C 1 167 ? 131.970 46.606  54.235  1.00 22.89 ? 164 ILE C CG1 1 
ATOM   4144 C  CG2 . ILE C 1 167 ? 133.196 48.771  54.245  1.00 25.24 ? 164 ILE C CG2 1 
ATOM   4145 C  CD1 . ILE C 1 167 ? 130.679 46.856  53.509  1.00 20.42 ? 164 ILE C CD1 1 
ATOM   4146 N  N   . PHE C 1 168 ? 133.274 49.187  57.765  1.00 26.99 ? 165 PHE C N   1 
ATOM   4147 C  CA  . PHE C 1 168 ? 133.741 50.494  58.259  1.00 28.03 ? 165 PHE C CA  1 
ATOM   4148 C  C   . PHE C 1 168 ? 134.462 50.467  59.614  1.00 28.51 ? 165 PHE C C   1 
ATOM   4149 O  O   . PHE C 1 168 ? 135.339 51.304  59.863  1.00 28.53 ? 165 PHE C O   1 
ATOM   4150 C  CB  . PHE C 1 168 ? 132.599 51.540  58.268  1.00 28.45 ? 165 PHE C CB  1 
ATOM   4151 C  CG  . PHE C 1 168 ? 132.034 51.845  56.890  1.00 29.11 ? 165 PHE C CG  1 
ATOM   4152 C  CD1 . PHE C 1 168 ? 130.758 51.423  56.538  1.00 29.01 ? 165 PHE C CD1 1 
ATOM   4153 C  CD2 . PHE C 1 168 ? 132.796 52.532  55.941  1.00 30.83 ? 165 PHE C CD2 1 
ATOM   4154 C  CE1 . PHE C 1 168 ? 130.237 51.680  55.267  1.00 30.90 ? 165 PHE C CE1 1 
ATOM   4155 C  CE2 . PHE C 1 168 ? 132.291 52.792  54.671  1.00 32.61 ? 165 PHE C CE2 1 
ATOM   4156 C  CZ  . PHE C 1 168 ? 130.995 52.362  54.328  1.00 30.49 ? 165 PHE C CZ  1 
ATOM   4157 N  N   . VAL C 1 169 ? 134.102 49.519  60.480  1.00 28.89 ? 166 VAL C N   1 
ATOM   4158 C  CA  . VAL C 1 169 ? 134.772 49.389  61.771  1.00 29.62 ? 166 VAL C CA  1 
ATOM   4159 C  C   . VAL C 1 169 ? 135.856 48.308  61.678  1.00 30.65 ? 166 VAL C C   1 
ATOM   4160 O  O   . VAL C 1 169 ? 137.011 48.527  62.054  1.00 30.24 ? 166 VAL C O   1 
ATOM   4161 C  CB  . VAL C 1 169 ? 133.779 49.114  62.924  1.00 29.72 ? 166 VAL C CB  1 
ATOM   4162 C  CG1 . VAL C 1 169 ? 134.516 49.057  64.270  1.00 29.66 ? 166 VAL C CG1 1 
ATOM   4163 C  CG2 . VAL C 1 169 ? 132.690 50.202  62.969  1.00 28.44 ? 166 VAL C CG2 1 
ATOM   4164 N  N   . ASP C 1 170 ? 135.466 47.169  61.115  1.00 31.36 ? 167 ASP C N   1 
ATOM   4165 C  CA  . ASP C 1 170 ? 136.302 45.999  61.018  1.00 32.13 ? 167 ASP C CA  1 
ATOM   4166 C  C   . ASP C 1 170 ? 137.173 46.018  59.739  1.00 32.64 ? 167 ASP C C   1 
ATOM   4167 O  O   . ASP C 1 170 ? 138.082 45.216  59.594  1.00 31.96 ? 167 ASP C O   1 
ATOM   4168 C  CB  . ASP C 1 170 ? 135.409 44.760  61.096  1.00 32.31 ? 167 ASP C CB  1 
ATOM   4169 C  CG  . ASP C 1 170 ? 136.190 43.469  61.310  1.00 33.41 ? 167 ASP C CG  1 
ATOM   4170 O  OD1 . ASP C 1 170 ? 137.229 43.471  62.027  1.00 34.34 ? 167 ASP C OD1 1 
ATOM   4171 O  OD2 . ASP C 1 170 ? 135.736 42.433  60.759  1.00 34.53 ? 167 ASP C OD2 1 
ATOM   4172 N  N   . GLY C 1 171 ? 136.906 46.949  58.826  1.00 33.32 ? 168 GLY C N   1 
ATOM   4173 C  CA  . GLY C 1 171 ? 137.822 47.195  57.715  1.00 33.98 ? 168 GLY C CA  1 
ATOM   4174 C  C   . GLY C 1 171 ? 137.808 46.153  56.616  1.00 34.63 ? 168 GLY C C   1 
ATOM   4175 O  O   . GLY C 1 171 ? 138.795 45.994  55.913  1.00 34.28 ? 168 GLY C O   1 
ATOM   4176 N  N   . ARG C 1 172 ? 136.682 45.462  56.450  1.00 35.66 ? 169 ARG C N   1 
ATOM   4177 C  CA  . ARG C 1 172 ? 136.534 44.454  55.389  1.00 36.45 ? 169 ARG C CA  1 
ATOM   4178 C  C   . ARG C 1 172 ? 136.070 45.093  54.080  1.00 37.07 ? 169 ARG C C   1 
ATOM   4179 O  O   . ARG C 1 172 ? 134.987 44.797  53.573  1.00 36.70 ? 169 ARG C O   1 
ATOM   4180 C  CB  . ARG C 1 172 ? 135.578 43.342  55.818  1.00 36.24 ? 169 ARG C CB  1 
ATOM   4181 C  CG  . ARG C 1 172 ? 135.841 42.854  57.237  1.00 36.10 ? 169 ARG C CG  1 
ATOM   4182 C  CD  . ARG C 1 172 ? 135.945 41.348  57.245  1.00 36.69 ? 169 ARG C CD  1 
ATOM   4183 N  NE  . ARG C 1 172 ? 134.627 40.707  56.970  1.00 35.55 ? 169 ARG C NE  1 
ATOM   4184 C  CZ  . ARG C 1 172 ? 133.845 40.287  58.143  1.00 33.72 ? 169 ARG C CZ  1 
ATOM   4185 N  NH1 . ARG C 1 172 ? 132.661 39.705  57.708  1.00 33.36 ? 169 ARG C NH1 1 
ATOM   4186 N  NH2 . ARG C 1 172 ? 134.055 40.692  59.571  1.00 31.28 ? 169 ARG C NH2 1 
ATOM   4187 N  N   . LYS C 1 173 ? 136.936 45.949  53.536  1.00 38.27 ? 170 LYS C N   1 
ATOM   4188 C  CA  . LYS C 1 173 ? 136.653 46.782  52.361  1.00 39.30 ? 170 LYS C CA  1 
ATOM   4189 C  C   . LYS C 1 173 ? 136.157 45.975  51.167  1.00 39.41 ? 170 LYS C C   1 
ATOM   4190 O  O   . LYS C 1 173 ? 135.390 46.498  50.364  1.00 39.49 ? 170 LYS C O   1 
ATOM   4191 C  CB  . LYS C 1 173 ? 137.905 47.573  51.928  1.00 39.67 ? 170 LYS C CB  1 
ATOM   4192 C  CG  . LYS C 1 173 ? 138.797 48.116  53.058  1.00 40.08 ? 170 LYS C CG  1 
ATOM   4193 C  CD  . LYS C 1 173 ? 139.899 49.018  52.494  1.00 40.26 ? 170 LYS C CD  1 
ATOM   4194 C  CE  . LYS C 1 173 ? 141.198 48.927  53.301  1.00 41.79 ? 170 LYS C CE  1 
ATOM   4195 N  NZ  . LYS C 1 173 ? 141.039 49.487  54.681  1.00 41.92 ? 170 LYS C NZ  1 
ATOM   4196 N  N   . GLU C 1 174 ? 136.625 44.725  51.048  1.00 39.27 ? 171 GLU C N   1 
ATOM   4197 C  CA  . GLU C 1 174 ? 136.219 43.793  49.980  1.00 39.21 ? 171 GLU C CA  1 
ATOM   4198 C  C   . GLU C 1 174 ? 134.701 43.597  49.872  1.00 38.60 ? 171 GLU C C   1 
ATOM   4199 O  O   . GLU C 1 174 ? 134.162 43.555  48.765  1.00 38.49 ? 171 GLU C O   1 
ATOM   4200 C  CB  . GLU C 1 174 ? 136.882 42.417  50.157  1.00 39.60 ? 171 GLU C CB  1 
ATOM   4201 C  CG  . GLU C 1 174 ? 138.256 42.413  50.852  1.00 41.78 ? 171 GLU C CG  1 
ATOM   4202 C  CD  . GLU C 1 174 ? 138.154 42.521  52.384  1.00 43.51 ? 171 GLU C CD  1 
ATOM   4203 O  OE1 . GLU C 1 174 ? 139.181 42.846  53.042  1.00 43.98 ? 171 GLU C OE1 1 
ATOM   4204 O  OE2 . GLU C 1 174 ? 137.049 42.272  52.920  1.00 42.53 ? 171 GLU C OE2 1 
ATOM   4205 N  N   . LEU C 1 175 ? 134.025 43.460  51.017  1.00 37.97 ? 172 LEU C N   1 
ATOM   4206 C  CA  . LEU C 1 175 ? 132.552 43.369  51.067  1.00 37.38 ? 172 LEU C CA  1 
ATOM   4207 C  C   . LEU C 1 175 ? 131.816 44.479  50.309  1.00 36.08 ? 172 LEU C C   1 
ATOM   4208 O  O   . LEU C 1 175 ? 130.874 44.197  49.587  1.00 35.92 ? 172 LEU C O   1 
ATOM   4209 C  CB  . LEU C 1 175 ? 132.045 43.339  52.516  1.00 37.94 ? 172 LEU C CB  1 
ATOM   4210 C  CG  . LEU C 1 175 ? 131.429 42.078  53.129  1.00 38.86 ? 172 LEU C CG  1 
ATOM   4211 C  CD1 . LEU C 1 175 ? 131.223 42.333  54.610  1.00 38.19 ? 172 LEU C CD1 1 
ATOM   4212 C  CD2 . LEU C 1 175 ? 130.091 41.711  52.462  1.00 39.59 ? 172 LEU C CD2 1 
ATOM   4213 N  N   . LEU C 1 176 ? 132.255 45.725  50.480  1.00 34.85 ? 173 LEU C N   1 
ATOM   4214 C  CA  . LEU C 1 176 ? 131.628 46.905  49.863  1.00 34.17 ? 173 LEU C CA  1 
ATOM   4215 C  C   . LEU C 1 176 ? 131.199 46.689  48.406  1.00 33.93 ? 173 LEU C C   1 
ATOM   4216 O  O   . LEU C 1 176 ? 130.024 46.848  48.063  1.00 34.02 ? 173 LEU C O   1 
ATOM   4217 C  CB  . LEU C 1 176 ? 132.567 48.119  49.964  1.00 34.14 ? 173 LEU C CB  1 
ATOM   4218 C  CG  . LEU C 1 176 ? 132.066 49.513  49.566  1.00 34.32 ? 173 LEU C CG  1 
ATOM   4219 C  CD1 . LEU C 1 176 ? 130.861 49.905  50.404  1.00 33.98 ? 173 LEU C CD1 1 
ATOM   4220 C  CD2 . LEU C 1 176 ? 133.172 50.567  49.665  1.00 33.39 ? 173 LEU C CD2 1 
ATOM   4221 N  N   . GLU C 1 177 ? 132.161 46.319  47.564  1.00 33.37 ? 174 GLU C N   1 
ATOM   4222 C  CA  . GLU C 1 177 ? 131.926 46.092  46.144  1.00 32.48 ? 174 GLU C CA  1 
ATOM   4223 C  C   . GLU C 1 177 ? 131.067 44.855  45.891  1.00 31.77 ? 174 GLU C C   1 
ATOM   4224 O  O   . GLU C 1 177 ? 130.256 44.831  44.962  1.00 31.64 ? 174 GLU C O   1 
ATOM   4225 C  CB  . GLU C 1 177 ? 133.257 45.993  45.404  1.00 32.37 ? 174 GLU C CB  1 
ATOM   4226 C  CG  . GLU C 1 177 ? 133.152 45.715  43.895  1.00 33.39 ? 174 GLU C CG  1 
ATOM   4227 C  CD  . GLU C 1 177 ? 132.537 46.863  43.094  1.00 34.48 ? 174 GLU C CD  1 
ATOM   4228 O  OE1 . GLU C 1 177 ? 132.235 47.946  43.680  1.00 33.00 ? 174 GLU C OE1 1 
ATOM   4229 O  OE2 . GLU C 1 177 ? 132.364 46.658  41.864  1.00 34.88 ? 174 GLU C OE2 1 
ATOM   4230 N  N   . LYS C 1 178 ? 131.237 43.834  46.720  1.00 30.82 ? 175 LYS C N   1 
ATOM   4231 C  CA  . LYS C 1 178 ? 130.404 42.652  46.632  1.00 30.32 ? 175 LYS C CA  1 
ATOM   4232 C  C   . LYS C 1 178 ? 128.912 43.014  46.797  1.00 30.02 ? 175 LYS C C   1 
ATOM   4233 O  O   . LYS C 1 178 ? 128.078 42.599  45.971  1.00 30.16 ? 175 LYS C O   1 
ATOM   4234 C  CB  . LYS C 1 178 ? 130.862 41.612  47.657  1.00 30.42 ? 175 LYS C CB  1 
ATOM   4235 C  CG  . LYS C 1 178 ? 130.547 40.183  47.273  1.00 31.63 ? 175 LYS C CG  1 
ATOM   4236 C  CD  . LYS C 1 178 ? 131.206 39.205  48.233  1.00 34.37 ? 175 LYS C CD  1 
ATOM   4237 C  CE  . LYS C 1 178 ? 130.477 39.173  49.619  1.00 33.24 ? 175 LYS C CE  1 
ATOM   4238 N  NZ  . LYS C 1 178 ? 131.172 38.033  50.452  1.00 31.79 ? 175 LYS C NZ  1 
ATOM   4239 N  N   . ILE C 1 179 ? 128.600 43.802  47.835  1.00 28.93 ? 176 ILE C N   1 
ATOM   4240 C  CA  . ILE C 1 179 ? 127.242 44.321  48.100  1.00 28.59 ? 176 ILE C CA  1 
ATOM   4241 C  C   . ILE C 1 179 ? 126.728 45.217  46.957  1.00 28.11 ? 176 ILE C C   1 
ATOM   4242 O  O   . ILE C 1 179 ? 125.625 45.037  46.464  1.00 27.76 ? 176 ILE C O   1 
ATOM   4243 C  CB  . ILE C 1 179 ? 127.175 45.116  49.459  1.00 28.54 ? 176 ILE C CB  1 
ATOM   4244 C  CG1 . ILE C 1 179 ? 127.568 44.229  50.640  1.00 28.21 ? 176 ILE C CG1 1 
ATOM   4245 C  CG2 . ILE C 1 179 ? 125.807 45.712  49.693  1.00 28.01 ? 176 ILE C CG2 1 
ATOM   4246 C  CD1 . ILE C 1 179 ? 127.926 45.001  51.901  1.00 28.62 ? 176 ILE C CD1 1 
ATOM   4247 N  N   . ARG C 1 180 ? 127.546 46.176  46.548  1.00 27.87 ? 177 ARG C N   1 
ATOM   4248 C  CA  . ARG C 1 180 ? 127.193 47.113  45.496  1.00 28.16 ? 177 ARG C CA  1 
ATOM   4249 C  C   . ARG C 1 180 ? 126.766 46.450  44.166  1.00 28.35 ? 177 ARG C C   1 
ATOM   4250 O  O   . ARG C 1 180 ? 125.921 46.982  43.421  1.00 27.98 ? 177 ARG C O   1 
ATOM   4251 C  CB  . ARG C 1 180 ? 128.366 48.062  45.273  1.00 28.13 ? 177 ARG C CB  1 
ATOM   4252 C  CG  . ARG C 1 180 ? 128.423 49.190  46.280  1.00 28.60 ? 177 ARG C CG  1 
ATOM   4253 C  CD  . ARG C 1 180 ? 129.698 49.962  46.115  1.00 28.14 ? 177 ARG C CD  1 
ATOM   4254 N  NE  . ARG C 1 180 ? 129.760 51.092  47.040  1.00 28.83 ? 177 ARG C NE  1 
ATOM   4255 C  CZ  . ARG C 1 180 ? 130.656 52.075  46.952  1.00 29.18 ? 177 ARG C CZ  1 
ATOM   4256 N  NH1 . ARG C 1 180 ? 131.567 52.070  45.978  1.00 28.94 ? 177 ARG C NH1 1 
ATOM   4257 N  NH2 . ARG C 1 180 ? 130.644 53.065  47.829  1.00 26.56 ? 177 ARG C NH2 1 
ATOM   4258 N  N   . LYS C 1 181 ? 127.348 45.283  43.890  1.00 28.37 ? 178 LYS C N   1 
ATOM   4259 C  CA  . LYS C 1 181 ? 127.098 44.567  42.654  1.00 28.40 ? 178 LYS C CA  1 
ATOM   4260 C  C   . LYS C 1 181 ? 126.171 43.375  42.842  1.00 28.19 ? 178 LYS C C   1 
ATOM   4261 O  O   . LYS C 1 181 ? 125.860 42.715  41.869  1.00 28.08 ? 178 LYS C O   1 
ATOM   4262 C  CB  . LYS C 1 181 ? 128.412 44.122  42.016  1.00 28.69 ? 178 LYS C CB  1 
ATOM   4263 C  CG  . LYS C 1 181 ? 129.365 45.254  41.638  1.00 29.53 ? 178 LYS C CG  1 
ATOM   4264 C  CD  . LYS C 1 181 ? 128.928 46.026  40.377  1.00 31.80 ? 178 LYS C CD  1 
ATOM   4265 C  CE  . LYS C 1 181 ? 129.836 47.251  40.121  1.00 31.65 ? 178 LYS C CE  1 
ATOM   4266 N  NZ  . LYS C 1 181 ? 129.622 48.335  41.157  1.00 31.82 ? 178 LYS C NZ  1 
ATOM   4267 N  N   . ASP C 1 182 ? 125.709 43.117  44.070  1.00 28.15 ? 179 ASP C N   1 
ATOM   4268 C  CA  . ASP C 1 182 ? 124.862 41.944  44.334  1.00 28.05 ? 179 ASP C CA  1 
ATOM   4269 C  C   . ASP C 1 182 ? 123.456 42.023  43.724  1.00 28.16 ? 179 ASP C C   1 
ATOM   4270 O  O   . ASP C 1 182 ? 122.653 42.865  44.126  1.00 27.98 ? 179 ASP C O   1 
ATOM   4271 C  CB  . ASP C 1 182 ? 124.762 41.637  45.828  1.00 27.80 ? 179 ASP C CB  1 
ATOM   4272 C  CG  . ASP C 1 182 ? 123.943 40.364  46.117  1.00 28.79 ? 179 ASP C CG  1 
ATOM   4273 O  OD1 . ASP C 1 182 ? 123.482 40.180  47.259  1.00 30.47 ? 179 ASP C OD1 1 
ATOM   4274 O  OD2 . ASP C 1 182 ? 123.755 39.526  45.210  1.00 31.00 ? 179 ASP C OD2 1 
ATOM   4275 N  N   . PRO C 1 183 ? 123.149 41.120  42.765  1.00 28.16 ? 180 PRO C N   1 
ATOM   4276 C  CA  . PRO C 1 183 ? 121.840 41.147  42.108  1.00 28.14 ? 180 PRO C CA  1 
ATOM   4277 C  C   . PRO C 1 183 ? 120.698 40.651  43.007  1.00 28.04 ? 180 PRO C C   1 
ATOM   4278 O  O   . PRO C 1 183 ? 119.536 41.004  42.777  1.00 27.50 ? 180 PRO C O   1 
ATOM   4279 C  CB  . PRO C 1 183 ? 122.029 40.218  40.899  1.00 28.00 ? 180 PRO C CB  1 
ATOM   4280 C  CG  . PRO C 1 183 ? 123.515 39.944  40.824  1.00 28.00 ? 180 PRO C CG  1 
ATOM   4281 C  CD  . PRO C 1 183 ? 123.990 40.039  42.224  1.00 28.20 ? 180 PRO C CD  1 
ATOM   4282 N  N   . ALA C 1 184 ? 121.033 39.849  44.016  1.00 27.93 ? 181 ALA C N   1 
ATOM   4283 C  CA  . ALA C 1 184 ? 120.046 39.350  44.971  1.00 28.15 ? 181 ALA C CA  1 
ATOM   4284 C  C   . ALA C 1 184 ? 119.380 40.485  45.758  1.00 28.37 ? 181 ALA C C   1 
ATOM   4285 O  O   . ALA C 1 184 ? 118.300 40.307  46.302  1.00 28.56 ? 181 ALA C O   1 
ATOM   4286 C  CB  . ALA C 1 184 ? 120.686 38.334  45.923  1.00 28.02 ? 181 ALA C CB  1 
ATOM   4287 N  N   . ARG C 1 185 ? 120.027 41.647  45.792  1.00 28.48 ? 182 ARG C N   1 
ATOM   4288 C  CA  . ARG C 1 185 ? 119.518 42.824  46.502  1.00 29.11 ? 182 ARG C CA  1 
ATOM   4289 C  C   . ARG C 1 185 ? 118.188 43.384  45.958  1.00 29.77 ? 182 ARG C C   1 
ATOM   4290 O  O   . ARG C 1 185 ? 117.426 44.032  46.699  1.00 29.19 ? 182 ARG C O   1 
ATOM   4291 C  CB  . ARG C 1 185 ? 120.578 43.929  46.531  1.00 28.44 ? 182 ARG C CB  1 
ATOM   4292 C  CG  . ARG C 1 185 ? 121.798 43.562  47.312  1.00 28.73 ? 182 ARG C CG  1 
ATOM   4293 C  CD  . ARG C 1 185 ? 122.394 44.772  48.003  1.00 31.62 ? 182 ARG C CD  1 
ATOM   4294 N  NE  . ARG C 1 185 ? 123.139 45.641  47.100  1.00 30.87 ? 182 ARG C NE  1 
ATOM   4295 C  CZ  . ARG C 1 185 ? 122.922 46.940  46.926  1.00 30.00 ? 182 ARG C CZ  1 
ATOM   4296 N  NH1 . ARG C 1 185 ? 121.960 47.577  47.587  1.00 28.19 ? 182 ARG C NH1 1 
ATOM   4297 N  NH2 . ARG C 1 185 ? 123.686 47.600  46.065  1.00 30.63 ? 182 ARG C NH2 1 
ATOM   4298 N  N   . PHE C 1 186 ? 117.925 43.140  44.672  1.00 30.36 ? 183 PHE C N   1 
ATOM   4299 C  CA  . PHE C 1 186 ? 116.744 43.670  44.015  1.00 31.33 ? 183 PHE C CA  1 
ATOM   4300 C  C   . PHE C 1 186 ? 115.891 42.557  43.437  1.00 32.67 ? 183 PHE C C   1 
ATOM   4301 O  O   . PHE C 1 186 ? 116.225 41.978  42.417  1.00 33.35 ? 183 PHE C O   1 
ATOM   4302 C  CB  . PHE C 1 186 ? 117.144 44.742  42.993  1.00 30.72 ? 183 PHE C CB  1 
ATOM   4303 C  CG  . PHE C 1 186 ? 117.895 45.862  43.618  1.00 30.60 ? 183 PHE C CG  1 
ATOM   4304 C  CD1 . PHE C 1 186 ? 119.290 45.866  43.617  1.00 30.37 ? 183 PHE C CD1 1 
ATOM   4305 C  CD2 . PHE C 1 186 ? 117.218 46.862  44.317  1.00 29.86 ? 183 PHE C CD2 1 
ATOM   4306 C  CE1 . PHE C 1 186 ? 120.004 46.884  44.267  1.00 30.48 ? 183 PHE C CE1 1 
ATOM   4307 C  CE2 . PHE C 1 186 ? 117.919 47.878  44.972  1.00 30.35 ? 183 PHE C CE2 1 
ATOM   4308 C  CZ  . PHE C 1 186 ? 119.319 47.883  44.948  1.00 29.64 ? 183 PHE C CZ  1 
ATOM   4309 N  N   . VAL C 1 187 ? 114.790 42.270  44.126  1.00 34.62 ? 184 VAL C N   1 
ATOM   4310 C  CA  . VAL C 1 187 ? 113.903 41.153  43.823  1.00 36.38 ? 184 VAL C CA  1 
ATOM   4311 C  C   . VAL C 1 187 ? 113.309 41.275  42.430  1.00 38.07 ? 184 VAL C C   1 
ATOM   4312 O  O   . VAL C 1 187 ? 112.716 42.303  42.089  1.00 38.99 ? 184 VAL C O   1 
ATOM   4313 C  CB  . VAL C 1 187 ? 112.819 40.997  44.919  1.00 36.16 ? 184 VAL C CB  1 
ATOM   4314 C  CG1 . VAL C 1 187 ? 111.483 40.547  44.358  1.00 36.20 ? 184 VAL C CG1 1 
ATOM   4315 C  CG2 . VAL C 1 187 ? 113.309 40.025  45.976  1.00 36.06 ? 184 VAL C CG2 1 
ATOM   4316 N  N   . ASP C 1 188 ? 113.521 40.222  41.636  1.00 39.58 ? 185 ASP C N   1 
ATOM   4317 C  CA  . ASP C 1 188 ? 113.070 40.101  40.240  1.00 41.11 ? 185 ASP C CA  1 
ATOM   4318 C  C   . ASP C 1 188 ? 114.194 40.135  39.208  1.00 41.01 ? 185 ASP C C   1 
ATOM   4319 O  O   . ASP C 1 188 ? 114.332 39.202  38.418  1.00 41.29 ? 185 ASP C O   1 
ATOM   4320 C  CB  . ASP C 1 188 ? 111.939 41.083  39.890  1.00 41.76 ? 185 ASP C CB  1 
ATOM   4321 C  CG  . ASP C 1 188 ? 110.555 40.472  40.114  1.00 43.97 ? 185 ASP C CG  1 
ATOM   4322 O  OD1 . ASP C 1 188 ? 110.164 40.288  41.298  1.00 45.56 ? 185 ASP C OD1 1 
ATOM   4323 O  OD2 . ASP C 1 188 ? 109.876 40.160  39.103  1.00 44.64 ? 185 ASP C OD2 1 
ATOM   4324 N  N   . SER D 1 1   ? 151.152 50.452  50.052  1.00 50.80 ? -2  SER D N   1 
ATOM   4325 C  CA  . SER D 1 1   ? 149.501 50.537  50.015  1.00 51.07 ? -2  SER D CA  1 
ATOM   4326 C  C   . SER D 1 1   ? 149.149 51.834  50.808  1.00 51.19 ? -2  SER D C   1 
ATOM   4327 O  O   . SER D 1 1   ? 149.163 51.889  52.089  1.00 51.23 ? -2  SER D O   1 
ATOM   4328 C  CB  . SER D 1 1   ? 148.852 49.196  50.825  1.00 51.17 ? -2  SER D CB  1 
ATOM   4329 O  OG  . SER D 1 1   ? 149.404 48.073  49.560  1.00 50.56 ? -2  SER D OG  1 
ATOM   4330 N  N   . ASN D 1 2   ? 148.843 52.878  50.026  1.00 51.12 ? -1  ASN D N   1 
ATOM   4331 C  CA  . ASN D 1 2   ? 148.847 54.246  50.555  1.00 51.21 ? -1  ASN D CA  1 
ATOM   4332 C  C   . ASN D 1 2   ? 147.648 55.099  50.140  1.00 51.35 ? -1  ASN D C   1 
ATOM   4333 O  O   . ASN D 1 2   ? 147.784 56.304  49.903  1.00 51.28 ? -1  ASN D O   1 
ATOM   4334 C  CB  . ASN D 1 2   ? 150.183 54.964  50.248  1.00 51.21 ? -1  ASN D CB  1 
ATOM   4335 C  CG  . ASN D 1 2   ? 150.951 54.348  49.054  1.00 51.31 ? -1  ASN D CG  1 
ATOM   4336 O  OD1 . ASN D 1 2   ? 152.056 53.821  49.227  1.00 49.64 ? -1  ASN D OD1 1 
ATOM   4337 N  ND2 . ASN D 1 2   ? 150.370 54.424  47.852  1.00 50.75 ? -1  ASN D ND2 1 
ATOM   4338 N  N   . ALA D 1 3   ? 146.476 54.462  50.081  1.00 51.35 ? 0   ALA D N   1 
ATOM   4339 C  CA  . ALA D 1 3   ? 145.228 55.131  49.722  1.00 51.41 ? 0   ALA D CA  1 
ATOM   4340 C  C   . ALA D 1 3   ? 144.881 56.219  50.745  1.00 51.47 ? 0   ALA D C   1 
ATOM   4341 O  O   . ALA D 1 3   ? 145.296 56.146  51.907  1.00 51.40 ? 0   ALA D O   1 
ATOM   4342 C  CB  . ALA D 1 3   ? 144.080 54.107  49.569  1.00 51.23 ? 0   ALA D CB  1 
HETATM 4343 N  N   . MSE D 1 4   ? 144.152 57.243  50.302  1.00 51.23 ? 1   MSE D N   1 
HETATM 4344 C  CA  . MSE D 1 4   ? 143.750 58.323  51.200  1.00 51.89 ? 1   MSE D CA  1 
HETATM 4345 C  C   . MSE D 1 4   ? 142.325 58.847  50.955  1.00 48.64 ? 1   MSE D C   1 
HETATM 4346 O  O   . MSE D 1 4   ? 141.560 58.280  50.153  1.00 48.09 ? 1   MSE D O   1 
HETATM 4347 C  CB  . MSE D 1 4   ? 144.781 59.452  51.169  1.00 51.37 ? 1   MSE D CB  1 
HETATM 4348 C  CG  . MSE D 1 4   ? 144.670 60.399  49.994  1.00 53.40 ? 1   MSE D CG  1 
HETATM 4349 SE SE  . MSE D 1 4   ? 146.443 60.959  49.375  1.00 60.87 ? 1   MSE D SE  1 
HETATM 4350 C  CE  . MSE D 1 4   ? 147.638 60.764  51.032  1.00 58.95 ? 1   MSE D CE  1 
ATOM   4351 N  N   . GLY D 1 5   ? 141.997 59.932  51.657  1.00 45.90 ? 2   GLY D N   1 
ATOM   4352 C  CA  . GLY D 1 5   ? 140.654 60.477  51.668  1.00 42.68 ? 2   GLY D CA  1 
ATOM   4353 C  C   . GLY D 1 5   ? 140.263 61.205  50.408  1.00 40.30 ? 2   GLY D C   1 
ATOM   4354 O  O   . GLY D 1 5   ? 140.977 62.107  49.959  1.00 40.48 ? 2   GLY D O   1 
ATOM   4355 N  N   . LYS D 1 6   ? 139.133 60.792  49.840  1.00 37.47 ? 3   LYS D N   1 
ATOM   4356 C  CA  . LYS D 1 6   ? 138.557 61.446  48.679  1.00 35.27 ? 3   LYS D CA  1 
ATOM   4357 C  C   . LYS D 1 6   ? 137.222 62.067  49.094  1.00 33.83 ? 3   LYS D C   1 
ATOM   4358 O  O   . LYS D 1 6   ? 136.267 61.371  49.444  1.00 32.88 ? 3   LYS D O   1 
ATOM   4359 C  CB  . LYS D 1 6   ? 138.413 60.468  47.492  1.00 35.46 ? 3   LYS D CB  1 
ATOM   4360 C  CG  . LYS D 1 6   ? 139.770 60.006  46.857  1.00 35.53 ? 3   LYS D CG  1 
ATOM   4361 C  CD  . LYS D 1 6   ? 139.638 59.027  45.667  1.00 35.40 ? 3   LYS D CD  1 
ATOM   4362 C  CE  . LYS D 1 6   ? 139.576 57.557  46.108  1.00 36.16 ? 3   LYS D CE  1 
ATOM   4363 N  NZ  . LYS D 1 6   ? 140.168 56.620  45.092  1.00 34.48 ? 3   LYS D NZ  1 
ATOM   4364 N  N   . VAL D 1 7   ? 137.200 63.394  49.092  1.00 32.13 ? 4   VAL D N   1 
ATOM   4365 C  CA  . VAL D 1 7   ? 136.050 64.160  49.493  1.00 30.33 ? 4   VAL D CA  1 
ATOM   4366 C  C   . VAL D 1 7   ? 135.611 65.046  48.346  1.00 29.90 ? 4   VAL D C   1 
ATOM   4367 O  O   . VAL D 1 7   ? 136.422 65.789  47.773  1.00 30.09 ? 4   VAL D O   1 
ATOM   4368 C  CB  . VAL D 1 7   ? 136.369 65.009  50.743  1.00 30.59 ? 4   VAL D CB  1 
ATOM   4369 C  CG1 . VAL D 1 7   ? 135.304 66.124  50.965  1.00 30.49 ? 4   VAL D CG1 1 
ATOM   4370 C  CG2 . VAL D 1 7   ? 136.477 64.102  51.975  1.00 29.40 ? 4   VAL D CG2 1 
ATOM   4371 N  N   . LEU D 1 8   ? 134.331 64.948  47.995  1.00 29.23 ? 5   LEU D N   1 
ATOM   4372 C  CA  . LEU D 1 8   ? 133.718 65.850  47.026  1.00 28.50 ? 5   LEU D CA  1 
ATOM   4373 C  C   . LEU D 1 8   ? 132.797 66.847  47.743  1.00 28.67 ? 5   LEU D C   1 
ATOM   4374 O  O   . LEU D 1 8   ? 131.959 66.461  48.575  1.00 28.33 ? 5   LEU D O   1 
ATOM   4375 C  CB  . LEU D 1 8   ? 132.955 65.036  46.005  1.00 28.30 ? 5   LEU D CB  1 
ATOM   4376 C  CG  . LEU D 1 8   ? 132.373 65.505  44.658  1.00 29.45 ? 5   LEU D CG  1 
ATOM   4377 C  CD1 . LEU D 1 8   ? 130.886 65.227  44.603  1.00 28.81 ? 5   LEU D CD1 1 
ATOM   4378 C  CD2 . LEU D 1 8   ? 132.716 66.927  44.207  1.00 29.72 ? 5   LEU D CD2 1 
ATOM   4379 N  N   . VAL D 1 9   ? 132.985 68.136  47.454  1.00 28.64 ? 6   VAL D N   1 
ATOM   4380 C  CA  . VAL D 1 9   ? 132.054 69.163  47.916  1.00 28.53 ? 6   VAL D CA  1 
ATOM   4381 C  C   . VAL D 1 9   ? 131.282 69.696  46.723  1.00 28.96 ? 6   VAL D C   1 
ATOM   4382 O  O   . VAL D 1 9   ? 131.828 70.370  45.846  1.00 29.14 ? 6   VAL D O   1 
ATOM   4383 C  CB  . VAL D 1 9   ? 132.734 70.307  48.709  1.00 28.83 ? 6   VAL D CB  1 
ATOM   4384 C  CG1 . VAL D 1 9   ? 131.678 71.298  49.226  1.00 26.25 ? 6   VAL D CG1 1 
ATOM   4385 C  CG2 . VAL D 1 9   ? 133.545 69.720  49.868  1.00 28.65 ? 6   VAL D CG2 1 
ATOM   4386 N  N   . ILE D 1 10  ? 130.004 69.364  46.696  1.00 29.24 ? 7   ILE D N   1 
ATOM   4387 C  CA  . ILE D 1 10  ? 129.155 69.721  45.582  1.00 29.75 ? 7   ILE D CA  1 
ATOM   4388 C  C   . ILE D 1 10  ? 128.104 70.733  46.064  1.00 29.35 ? 7   ILE D C   1 
ATOM   4389 O  O   . ILE D 1 10  ? 127.488 70.553  47.094  1.00 30.20 ? 7   ILE D O   1 
ATOM   4390 C  CB  . ILE D 1 10  ? 128.553 68.442  44.906  1.00 29.93 ? 7   ILE D CB  1 
ATOM   4391 C  CG1 . ILE D 1 10  ? 127.507 68.817  43.858  1.00 30.97 ? 7   ILE D CG1 1 
ATOM   4392 C  CG2 . ILE D 1 10  ? 128.001 67.474  45.946  1.00 29.05 ? 7   ILE D CG2 1 
ATOM   4393 C  CD1 . ILE D 1 10  ? 127.054 67.658  43.028  1.00 34.08 ? 7   ILE D CD1 1 
ATOM   4394 N  N   . TYR D 1 11  ? 127.914 71.818  45.335  1.00 29.16 ? 8   TYR D N   1 
ATOM   4395 C  CA  . TYR D 1 11  ? 127.005 72.853  45.812  1.00 28.59 ? 8   TYR D CA  1 
ATOM   4396 C  C   . TYR D 1 11  ? 126.226 73.454  44.643  1.00 28.34 ? 8   TYR D C   1 
ATOM   4397 O  O   . TYR D 1 11  ? 126.637 73.361  43.485  1.00 27.84 ? 8   TYR D O   1 
ATOM   4398 C  CB  . TYR D 1 11  ? 127.777 73.944  46.580  1.00 28.13 ? 8   TYR D CB  1 
ATOM   4399 C  CG  . TYR D 1 11  ? 128.662 74.752  45.659  1.00 27.71 ? 8   TYR D CG  1 
ATOM   4400 C  CD1 . TYR D 1 11  ? 128.188 75.924  45.059  1.00 28.13 ? 8   TYR D CD1 1 
ATOM   4401 C  CD2 . TYR D 1 11  ? 129.940 74.310  45.324  1.00 26.84 ? 8   TYR D CD2 1 
ATOM   4402 C  CE1 . TYR D 1 11  ? 128.971 76.649  44.192  1.00 28.38 ? 8   TYR D CE1 1 
ATOM   4403 C  CE2 . TYR D 1 11  ? 130.741 75.031  44.459  1.00 27.48 ? 8   TYR D CE2 1 
ATOM   4404 C  CZ  . TYR D 1 11  ? 130.255 76.199  43.889  1.00 28.65 ? 8   TYR D CZ  1 
ATOM   4405 O  OH  . TYR D 1 11  ? 131.041 76.918  43.010  1.00 28.00 ? 8   TYR D OH  1 
ATOM   4406 N  N   . ASP D 1 12  ? 125.079 74.030  44.976  1.00 28.63 ? 9   ASP D N   1 
ATOM   4407 C  CA  . ASP D 1 12  ? 124.360 74.947  44.121  1.00 28.75 ? 9   ASP D CA  1 
ATOM   4408 C  C   . ASP D 1 12  ? 124.374 76.306  44.835  1.00 29.68 ? 9   ASP D C   1 
ATOM   4409 O  O   . ASP D 1 12  ? 124.573 76.390  46.063  1.00 30.16 ? 9   ASP D O   1 
ATOM   4410 C  CB  . ASP D 1 12  ? 122.922 74.467  43.897  1.00 27.69 ? 9   ASP D CB  1 
ATOM   4411 C  CG  . ASP D 1 12  ? 122.187 75.291  42.838  1.00 29.23 ? 9   ASP D CG  1 
ATOM   4412 O  OD1 . ASP D 1 12  ? 122.846 75.760  41.864  1.00 32.16 ? 9   ASP D OD1 1 
ATOM   4413 O  OD2 . ASP D 1 12  ? 120.959 75.485  42.947  1.00 24.81 ? 9   ASP D OD2 1 
ATOM   4414 N  N   . THR D 1 13  ? 124.165 77.368  44.074  1.00 30.28 ? 10  THR D N   1 
ATOM   4415 C  CA  . THR D 1 13  ? 124.061 78.689  44.640  1.00 31.33 ? 10  THR D CA  1 
ATOM   4416 C  C   . THR D 1 13  ? 123.374 79.560  43.624  1.00 32.62 ? 10  THR D C   1 
ATOM   4417 O  O   . THR D 1 13  ? 123.482 79.318  42.419  1.00 32.36 ? 10  THR D O   1 
ATOM   4418 C  CB  . THR D 1 13  ? 125.451 79.305  44.999  1.00 31.50 ? 10  THR D CB  1 
ATOM   4419 O  OG1 . THR D 1 13  ? 125.267 80.544  45.703  1.00 31.77 ? 10  THR D OG1 1 
ATOM   4420 C  CG2 . THR D 1 13  ? 126.307 79.574  43.752  1.00 29.90 ? 10  THR D CG2 1 
ATOM   4421 N  N   . ARG D 1 14  ? 122.684 80.585  44.117  1.00 34.20 ? 11  ARG D N   1 
ATOM   4422 C  CA  . ARG D 1 14  ? 122.012 81.545  43.256  1.00 35.87 ? 11  ARG D CA  1 
ATOM   4423 C  C   . ARG D 1 14  ? 122.622 82.934  43.419  1.00 35.77 ? 11  ARG D C   1 
ATOM   4424 O  O   . ARG D 1 14  ? 122.683 83.682  42.468  1.00 36.08 ? 11  ARG D O   1 
ATOM   4425 C  CB  . ARG D 1 14  ? 120.515 81.545  43.545  1.00 36.84 ? 11  ARG D CB  1 
ATOM   4426 C  CG  . ARG D 1 14  ? 119.619 82.315  42.552  1.00 40.82 ? 11  ARG D CG  1 
ATOM   4427 C  CD  . ARG D 1 14  ? 119.219 83.716  43.111  1.00 47.06 ? 11  ARG D CD  1 
ATOM   4428 N  NE  . ARG D 1 14  ? 119.001 83.738  44.572  1.00 48.89 ? 11  ARG D NE  1 
ATOM   4429 C  CZ  . ARG D 1 14  ? 118.436 84.748  45.246  1.00 51.68 ? 11  ARG D CZ  1 
ATOM   4430 N  NH1 . ARG D 1 14  ? 118.016 85.839  44.603  1.00 52.55 ? 11  ARG D NH1 1 
ATOM   4431 N  NH2 . ARG D 1 14  ? 118.292 84.676  46.573  1.00 52.40 ? 11  ARG D NH2 1 
ATOM   4432 N  N   . THR D 1 15  ? 123.083 83.292  44.610  1.00 35.64 ? 12  THR D N   1 
ATOM   4433 C  CA  . THR D 1 15  ? 123.755 84.586  44.742  1.00 35.23 ? 12  THR D CA  1 
ATOM   4434 C  C   . THR D 1 15  ? 125.196 84.496  45.228  1.00 34.47 ? 12  THR D C   1 
ATOM   4435 O  O   . THR D 1 15  ? 125.841 85.523  45.457  1.00 34.52 ? 12  THR D O   1 
ATOM   4436 C  CB  . THR D 1 15  ? 122.983 85.583  45.651  1.00 35.86 ? 12  THR D CB  1 
ATOM   4437 O  OG1 . THR D 1 15  ? 122.884 85.058  46.981  1.00 36.43 ? 12  THR D OG1 1 
ATOM   4438 C  CG2 . THR D 1 15  ? 121.599 85.918  45.080  1.00 35.41 ? 12  THR D CG2 1 
ATOM   4439 N  N   . GLY D 1 16  ? 125.697 83.278  45.396  1.00 33.66 ? 13  GLY D N   1 
ATOM   4440 C  CA  . GLY D 1 16  ? 127.047 83.097  45.902  1.00 32.19 ? 13  GLY D CA  1 
ATOM   4441 C  C   . GLY D 1 16  ? 127.166 82.705  47.359  1.00 31.15 ? 13  GLY D C   1 
ATOM   4442 O  O   . GLY D 1 16  ? 128.212 82.229  47.764  1.00 32.10 ? 13  GLY D O   1 
ATOM   4443 N  N   . ASN D 1 17  ? 126.124 82.889  48.163  1.00 30.05 ? 14  ASN D N   1 
ATOM   4444 C  CA  . ASN D 1 17  ? 126.220 82.577  49.625  1.00 29.29 ? 14  ASN D CA  1 
ATOM   4445 C  C   . ASN D 1 17  ? 126.677 81.153  49.999  1.00 28.55 ? 14  ASN D C   1 
ATOM   4446 O  O   . ASN D 1 17  ? 127.583 80.997  50.823  1.00 28.58 ? 14  ASN D O   1 
ATOM   4447 C  CB  . ASN D 1 17  ? 124.941 82.959  50.395  1.00 28.58 ? 14  ASN D CB  1 
ATOM   4448 C  CG  . ASN D 1 17  ? 124.609 84.461  50.310  1.00 29.08 ? 14  ASN D CG  1 
ATOM   4449 O  OD1 . ASN D 1 17  ? 125.490 85.314  50.108  1.00 27.93 ? 14  ASN D OD1 1 
ATOM   4450 N  ND2 . ASN D 1 17  ? 123.322 84.785  50.476  1.00 28.44 ? 14  ASN D ND2 1 
ATOM   4451 N  N   . THR D 1 18  ? 126.042 80.145  49.389  1.00 28.08 ? 15  THR D N   1 
ATOM   4452 C  CA  . THR D 1 18  ? 126.328 78.718  49.574  1.00 27.68 ? 15  THR D CA  1 
ATOM   4453 C  C   . THR D 1 18  ? 127.673 78.322  48.955  1.00 28.46 ? 15  THR D C   1 
ATOM   4454 O  O   . THR D 1 18  ? 128.332 77.382  49.438  1.00 28.24 ? 15  THR D O   1 
ATOM   4455 C  CB  . THR D 1 18  ? 125.207 77.859  48.960  1.00 27.64 ? 15  THR D CB  1 
ATOM   4456 O  OG1 . THR D 1 18  ? 123.947 78.294  49.480  1.00 28.71 ? 15  THR D OG1 1 
ATOM   4457 C  CG2 . THR D 1 18  ? 125.375 76.389  49.286  1.00 26.53 ? 15  THR D CG2 1 
ATOM   4458 N  N   . LYS D 1 19  ? 128.071 79.022  47.886  1.00 28.68 ? 16  LYS D N   1 
ATOM   4459 C  CA  . LYS D 1 19  ? 129.406 78.870  47.333  1.00 29.22 ? 16  LYS D CA  1 
ATOM   4460 C  C   . LYS D 1 19  ? 130.463 79.289  48.375  1.00 30.11 ? 16  LYS D C   1 
ATOM   4461 O  O   . LYS D 1 19  ? 131.432 78.572  48.586  1.00 30.25 ? 16  LYS D O   1 
ATOM   4462 C  CB  . LYS D 1 19  ? 129.566 79.673  46.027  1.00 29.82 ? 16  LYS D CB  1 
ATOM   4463 C  CG  . LYS D 1 19  ? 130.968 79.555  45.358  1.00 28.87 ? 16  LYS D CG  1 
ATOM   4464 C  CD  . LYS D 1 19  ? 131.082 80.377  44.096  1.00 27.54 ? 16  LYS D CD  1 
ATOM   4465 C  CE  . LYS D 1 19  ? 132.429 80.130  43.433  1.00 26.72 ? 16  LYS D CE  1 
ATOM   4466 N  NZ  . LYS D 1 19  ? 132.705 81.014  42.230  1.00 25.13 ? 16  LYS D NZ  1 
ATOM   4467 N  N   . LYS D 1 20  ? 130.282 80.438  49.024  1.00 31.12 ? 17  LYS D N   1 
ATOM   4468 C  CA  . LYS D 1 20  ? 131.214 80.857  50.086  1.00 32.35 ? 17  LYS D CA  1 
ATOM   4469 C  C   . LYS D 1 20  ? 131.311 79.812  51.206  1.00 33.03 ? 17  LYS D C   1 
ATOM   4470 O  O   . LYS D 1 20  ? 132.398 79.560  51.722  1.00 32.71 ? 17  LYS D O   1 
ATOM   4471 C  CB  . LYS D 1 20  ? 130.830 82.214  50.674  1.00 32.31 ? 17  LYS D CB  1 
ATOM   4472 C  CG  . LYS D 1 20  ? 131.448 83.426  49.988  1.00 34.87 ? 17  LYS D CG  1 
ATOM   4473 C  CD  . LYS D 1 20  ? 130.573 83.916  48.855  1.00 39.36 ? 17  LYS D CD  1 
ATOM   4474 C  CE  . LYS D 1 20  ? 130.641 85.441  48.669  1.00 42.80 ? 17  LYS D CE  1 
ATOM   4475 N  NZ  . LYS D 1 20  ? 131.884 85.950  47.974  1.00 43.57 ? 17  LYS D NZ  1 
HETATM 4476 N  N   . MSE D 1 21  ? 130.168 79.205  51.560  1.00 34.12 ? 18  MSE D N   1 
HETATM 4477 C  CA  . MSE D 1 21  ? 130.116 78.117  52.537  1.00 35.64 ? 18  MSE D CA  1 
HETATM 4478 C  C   . MSE D 1 21  ? 130.910 76.923  52.034  1.00 33.30 ? 18  MSE D C   1 
HETATM 4479 O  O   . MSE D 1 21  ? 131.727 76.352  52.767  1.00 32.60 ? 18  MSE D O   1 
HETATM 4480 C  CB  . MSE D 1 21  ? 128.672 77.682  52.780  1.00 35.34 ? 18  MSE D CB  1 
HETATM 4481 C  CG  . MSE D 1 21  ? 127.770 78.732  53.368  1.00 37.06 ? 18  MSE D CG  1 
HETATM 4482 SE SE  . MSE D 1 21  ? 126.035 77.936  53.909  1.00 44.48 ? 18  MSE D SE  1 
HETATM 4483 C  CE  . MSE D 1 21  ? 126.539 76.849  55.581  1.00 38.41 ? 18  MSE D CE  1 
ATOM   4484 N  N   . ALA D 1 22  ? 130.664 76.584  50.764  1.00 32.09 ? 19  ALA D N   1 
ATOM   4485 C  CA  . ALA D 1 22  ? 131.245 75.418  50.091  1.00 30.61 ? 19  ALA D CA  1 
ATOM   4486 C  C   . ALA D 1 22  ? 132.745 75.472  50.083  1.00 29.99 ? 19  ALA D C   1 
ATOM   4487 O  O   . ALA D 1 22  ? 133.394 74.443  50.298  1.00 29.30 ? 19  ALA D O   1 
ATOM   4488 C  CB  . ALA D 1 22  ? 130.714 75.296  48.653  1.00 30.40 ? 19  ALA D CB  1 
ATOM   4489 N  N   . GLU D 1 23  ? 133.277 76.674  49.835  1.00 29.57 ? 20  GLU D N   1 
ATOM   4490 C  CA  . GLU D 1 23  ? 134.719 76.933  49.818  1.00 30.44 ? 20  GLU D CA  1 
ATOM   4491 C  C   . GLU D 1 23  ? 135.342 76.697  51.189  1.00 29.73 ? 20  GLU D C   1 
ATOM   4492 O  O   . GLU D 1 23  ? 136.420 76.111  51.308  1.00 29.74 ? 20  GLU D O   1 
ATOM   4493 C  CB  . GLU D 1 23  ? 135.005 78.374  49.384  1.00 30.58 ? 20  GLU D CB  1 
ATOM   4494 C  CG  . GLU D 1 23  ? 134.745 78.699  47.901  1.00 31.69 ? 20  GLU D CG  1 
ATOM   4495 C  CD  . GLU D 1 23  ? 134.804 80.202  47.623  1.00 32.45 ? 20  GLU D CD  1 
ATOM   4496 O  OE1 . GLU D 1 23  ? 134.732 80.983  48.609  1.00 35.69 ? 20  GLU D OE1 1 
ATOM   4497 O  OE2 . GLU D 1 23  ? 134.925 80.603  46.432  1.00 33.27 ? 20  GLU D OE2 1 
ATOM   4498 N  N   . LEU D 1 24  ? 134.655 77.177  52.218  1.00 29.39 ? 21  LEU D N   1 
ATOM   4499 C  CA  . LEU D 1 24  ? 135.045 76.940  53.600  1.00 28.80 ? 21  LEU D CA  1 
ATOM   4500 C  C   . LEU D 1 24  ? 134.861 75.464  54.002  1.00 28.67 ? 21  LEU D C   1 
ATOM   4501 O  O   . LEU D 1 24  ? 135.726 74.908  54.672  1.00 28.22 ? 21  LEU D O   1 
ATOM   4502 C  CB  . LEU D 1 24  ? 134.254 77.860  54.522  1.00 28.88 ? 21  LEU D CB  1 
ATOM   4503 C  CG  . LEU D 1 24  ? 134.551 79.353  54.451  1.00 28.17 ? 21  LEU D CG  1 
ATOM   4504 C  CD1 . LEU D 1 24  ? 133.339 80.160  54.958  1.00 27.14 ? 21  LEU D CD1 1 
ATOM   4505 C  CD2 . LEU D 1 24  ? 135.822 79.671  55.259  1.00 26.23 ? 21  LEU D CD2 1 
ATOM   4506 N  N   . VAL D 1 25  ? 133.762 74.826  53.584  1.00 28.43 ? 22  VAL D N   1 
ATOM   4507 C  CA  . VAL D 1 25  ? 133.624 73.370  53.766  1.00 28.79 ? 22  VAL D CA  1 
ATOM   4508 C  C   . VAL D 1 25  ? 134.850 72.627  53.183  1.00 29.57 ? 22  VAL D C   1 
ATOM   4509 O  O   . VAL D 1 25  ? 135.443 71.768  53.848  1.00 29.22 ? 22  VAL D O   1 
ATOM   4510 C  CB  . VAL D 1 25  ? 132.267 72.799  53.229  1.00 28.87 ? 22  VAL D CB  1 
ATOM   4511 C  CG1 . VAL D 1 25  ? 132.227 71.277  53.326  1.00 27.66 ? 22  VAL D CG1 1 
ATOM   4512 C  CG2 . VAL D 1 25  ? 131.083 73.363  54.021  1.00 28.33 ? 22  VAL D CG2 1 
ATOM   4513 N  N   . ALA D 1 26  ? 135.261 73.002  51.966  1.00 30.57 ? 23  ALA D N   1 
ATOM   4514 C  CA  . ALA D 1 26  ? 136.427 72.404  51.304  1.00 30.55 ? 23  ALA D CA  1 
ATOM   4515 C  C   . ALA D 1 26  ? 137.752 72.730  52.010  1.00 31.12 ? 23  ALA D C   1 
ATOM   4516 O  O   . ALA D 1 26  ? 138.631 71.872  52.149  1.00 31.46 ? 23  ALA D O   1 
ATOM   4517 C  CB  . ALA D 1 26  ? 136.466 72.811  49.835  1.00 30.48 ? 23  ALA D CB  1 
ATOM   4518 N  N   . GLU D 1 27  ? 137.902 73.971  52.452  1.00 31.45 ? 24  GLU D N   1 
ATOM   4519 C  CA  . GLU D 1 27  ? 139.058 74.354  53.250  1.00 31.86 ? 24  GLU D CA  1 
ATOM   4520 C  C   . GLU D 1 27  ? 139.158 73.432  54.476  1.00 31.35 ? 24  GLU D C   1 
ATOM   4521 O  O   . GLU D 1 27  ? 140.208 72.862  54.761  1.00 31.12 ? 24  GLU D O   1 
ATOM   4522 C  CB  . GLU D 1 27  ? 138.911 75.815  53.693  1.00 32.49 ? 24  GLU D CB  1 
ATOM   4523 C  CG  . GLU D 1 27  ? 140.188 76.460  54.223  1.00 35.53 ? 24  GLU D CG  1 
ATOM   4524 C  CD  . GLU D 1 27  ? 139.906 77.558  55.221  1.00 38.22 ? 24  GLU D CD  1 
ATOM   4525 O  OE1 . GLU D 1 27  ? 139.304 78.589  54.863  1.00 40.55 ? 24  GLU D OE1 1 
ATOM   4526 O  OE2 . GLU D 1 27  ? 140.289 77.387  56.383  1.00 40.66 ? 24  GLU D OE2 1 
ATOM   4527 N  N   . GLY D 1 28  ? 138.045 73.284  55.190  1.00 31.26 ? 25  GLY D N   1 
ATOM   4528 C  CA  . GLY D 1 28  ? 137.984 72.425  56.376  1.00 31.34 ? 25  GLY D CA  1 
ATOM   4529 C  C   . GLY D 1 28  ? 138.397 70.987  56.102  1.00 31.27 ? 25  GLY D C   1 
ATOM   4530 O  O   . GLY D 1 28  ? 139.146 70.388  56.878  1.00 31.10 ? 25  GLY D O   1 
ATOM   4531 N  N   . ALA D 1 29  ? 137.908 70.444  54.985  1.00 31.48 ? 26  ALA D N   1 
ATOM   4532 C  CA  . ALA D 1 29  ? 138.219 69.076  54.580  1.00 31.78 ? 26  ALA D CA  1 
ATOM   4533 C  C   . ALA D 1 29  ? 139.710 68.899  54.253  1.00 32.19 ? 26  ALA D C   1 
ATOM   4534 O  O   . ALA D 1 29  ? 140.325 67.904  54.651  1.00 32.18 ? 26  ALA D O   1 
ATOM   4535 C  CB  . ALA D 1 29  ? 137.349 68.672  53.410  1.00 31.38 ? 26  ALA D CB  1 
ATOM   4536 N  N   . ARG D 1 30  ? 140.276 69.883  53.545  1.00 32.44 ? 27  ARG D N   1 
ATOM   4537 C  CA  . ARG D 1 30  ? 141.687 69.875  53.151  1.00 32.92 ? 27  ARG D CA  1 
ATOM   4538 C  C   . ARG D 1 30  ? 142.607 70.000  54.351  1.00 32.39 ? 27  ARG D C   1 
ATOM   4539 O  O   . ARG D 1 30  ? 143.777 69.667  54.239  1.00 33.40 ? 27  ARG D O   1 
ATOM   4540 C  CB  . ARG D 1 30  ? 142.005 70.989  52.139  1.00 32.19 ? 27  ARG D CB  1 
ATOM   4541 C  CG  . ARG D 1 30  ? 141.719 70.626  50.701  1.00 33.60 ? 27  ARG D CG  1 
ATOM   4542 C  CD  . ARG D 1 30  ? 142.151 71.746  49.745  1.00 34.55 ? 27  ARG D CD  1 
ATOM   4543 N  NE  . ARG D 1 30  ? 141.301 72.926  49.907  1.00 38.55 ? 27  ARG D NE  1 
ATOM   4544 C  CZ  . ARG D 1 30  ? 140.397 73.334  49.015  1.00 39.64 ? 27  ARG D CZ  1 
ATOM   4545 N  NH1 . ARG D 1 30  ? 140.234 72.678  47.861  1.00 37.78 ? 27  ARG D NH1 1 
ATOM   4546 N  NH2 . ARG D 1 30  ? 139.658 74.413  49.276  1.00 40.80 ? 27  ARG D NH2 1 
ATOM   4547 N  N   . SER D 1 31  ? 142.099 70.470  55.490  1.00 32.09 ? 28  SER D N   1 
ATOM   4548 C  CA  . SER D 1 31  ? 142.946 70.641  56.688  1.00 31.94 ? 28  SER D CA  1 
ATOM   4549 C  C   . SER D 1 31  ? 143.495 69.325  57.280  1.00 32.07 ? 28  SER D C   1 
ATOM   4550 O  O   . SER D 1 31  ? 144.551 69.327  57.935  1.00 31.79 ? 28  SER D O   1 
ATOM   4551 C  CB  . SER D 1 31  ? 142.243 71.484  57.763  1.00 31.69 ? 28  SER D CB  1 
ATOM   4552 O  OG  . SER D 1 31  ? 141.150 70.793  58.337  1.00 31.41 ? 28  SER D OG  1 
ATOM   4553 N  N   . LEU D 1 32  ? 142.797 68.213  57.026  1.00 32.19 ? 29  LEU D N   1 
ATOM   4554 C  CA  . LEU D 1 32  ? 143.210 66.892  57.517  1.00 32.91 ? 29  LEU D CA  1 
ATOM   4555 C  C   . LEU D 1 32  ? 144.216 66.219  56.564  1.00 33.99 ? 29  LEU D C   1 
ATOM   4556 O  O   . LEU D 1 32  ? 143.938 66.068  55.371  1.00 34.31 ? 29  LEU D O   1 
ATOM   4557 C  CB  . LEU D 1 32  ? 141.980 66.013  57.752  1.00 32.27 ? 29  LEU D CB  1 
ATOM   4558 C  CG  . LEU D 1 32  ? 141.905 64.802  58.702  1.00 31.87 ? 29  LEU D CG  1 
ATOM   4559 C  CD1 . LEU D 1 32  ? 141.543 63.515  57.979  1.00 31.33 ? 29  LEU D CD1 1 
ATOM   4560 C  CD2 . LEU D 1 32  ? 143.130 64.582  59.585  1.00 29.90 ? 29  LEU D CD2 1 
ATOM   4561 N  N   . GLU D 1 33  ? 145.375 65.820  57.099  1.00 34.84 ? 30  GLU D N   1 
ATOM   4562 C  CA  . GLU D 1 33  ? 146.480 65.266  56.305  1.00 36.00 ? 30  GLU D CA  1 
ATOM   4563 C  C   . GLU D 1 33  ? 146.015 64.165  55.366  1.00 36.01 ? 30  GLU D C   1 
ATOM   4564 O  O   . GLU D 1 33  ? 145.257 63.282  55.776  1.00 36.01 ? 30  GLU D O   1 
ATOM   4565 C  CB  . GLU D 1 33  ? 147.571 64.691  57.221  1.00 36.60 ? 30  GLU D CB  1 
ATOM   4566 C  CG  . GLU D 1 33  ? 148.806 65.550  57.397  1.00 38.40 ? 30  GLU D CG  1 
ATOM   4567 C  CD  . GLU D 1 33  ? 149.848 65.296  56.318  1.00 40.88 ? 30  GLU D CD  1 
ATOM   4568 O  OE1 . GLU D 1 33  ? 149.555 65.575  55.129  1.00 41.19 ? 30  GLU D OE1 1 
ATOM   4569 O  OE2 . GLU D 1 33  ? 150.966 64.830  56.664  1.00 41.29 ? 30  GLU D OE2 1 
ATOM   4570 N  N   . GLY D 1 34  ? 146.490 64.209  54.121  1.00 36.17 ? 31  GLY D N   1 
ATOM   4571 C  CA  . GLY D 1 34  ? 146.136 63.200  53.131  1.00 36.37 ? 31  GLY D CA  1 
ATOM   4572 C  C   . GLY D 1 34  ? 144.645 63.148  52.834  1.00 36.64 ? 31  GLY D C   1 
ATOM   4573 O  O   . GLY D 1 34  ? 144.046 62.065  52.772  1.00 37.10 ? 31  GLY D O   1 
ATOM   4574 N  N   . THR D 1 35  ? 144.031 64.321  52.699  1.00 36.38 ? 32  THR D N   1 
ATOM   4575 C  CA  . THR D 1 35  ? 142.659 64.406  52.210  1.00 35.70 ? 32  THR D CA  1 
ATOM   4576 C  C   . THR D 1 35  ? 142.746 65.185  50.919  1.00 35.73 ? 32  THR D C   1 
ATOM   4577 O  O   . THR D 1 35  ? 143.225 66.332  50.894  1.00 35.89 ? 32  THR D O   1 
ATOM   4578 C  CB  . THR D 1 35  ? 141.694 65.118  53.199  1.00 35.64 ? 32  THR D CB  1 
ATOM   4579 O  OG1 . THR D 1 35  ? 141.724 64.449  54.465  1.00 35.35 ? 32  THR D OG1 1 
ATOM   4580 C  CG2 . THR D 1 35  ? 140.253 65.136  52.663  1.00 34.42 ? 32  THR D CG2 1 
ATOM   4581 N  N   . GLU D 1 36  ? 142.323 64.532  49.845  1.00 35.14 ? 33  GLU D N   1 
ATOM   4582 C  CA  . GLU D 1 36  ? 142.186 65.166  48.550  1.00 34.50 ? 33  GLU D CA  1 
ATOM   4583 C  C   . GLU D 1 36  ? 140.716 65.591  48.342  1.00 33.92 ? 33  GLU D C   1 
ATOM   4584 O  O   . GLU D 1 36  ? 139.782 64.825  48.614  1.00 33.56 ? 33  GLU D O   1 
ATOM   4585 C  CB  . GLU D 1 36  ? 142.631 64.198  47.477  1.00 34.42 ? 33  GLU D CB  1 
ATOM   4586 C  CG  . GLU D 1 36  ? 142.358 64.687  46.090  1.00 35.45 ? 33  GLU D CG  1 
ATOM   4587 C  CD  . GLU D 1 36  ? 143.412 64.240  45.149  1.00 37.01 ? 33  GLU D CD  1 
ATOM   4588 O  OE1 . GLU D 1 36  ? 144.598 64.593  45.400  1.00 38.53 ? 33  GLU D OE1 1 
ATOM   4589 O  OE2 . GLU D 1 36  ? 143.057 63.537  44.174  1.00 36.45 ? 33  GLU D OE2 1 
ATOM   4590 N  N   . VAL D 1 37  ? 140.528 66.817  47.863  1.00 33.16 ? 34  VAL D N   1 
ATOM   4591 C  CA  . VAL D 1 37  ? 139.215 67.430  47.846  1.00 33.01 ? 34  VAL D CA  1 
ATOM   4592 C  C   . VAL D 1 37  ? 138.901 68.058  46.509  1.00 32.44 ? 34  VAL D C   1 
ATOM   4593 O  O   . VAL D 1 37  ? 139.679 68.852  45.998  1.00 32.84 ? 34  VAL D O   1 
ATOM   4594 C  CB  . VAL D 1 37  ? 139.047 68.460  48.998  1.00 33.17 ? 34  VAL D CB  1 
ATOM   4595 C  CG1 . VAL D 1 37  ? 137.751 69.288  48.849  1.00 32.91 ? 34  VAL D CG1 1 
ATOM   4596 C  CG2 . VAL D 1 37  ? 139.043 67.734  50.340  1.00 33.56 ? 34  VAL D CG2 1 
ATOM   4597 N  N   . ARG D 1 38  ? 137.759 67.671  45.946  1.00 31.70 ? 35  ARG D N   1 
ATOM   4598 C  CA  . ARG D 1 38  ? 137.202 68.329  44.769  1.00 31.00 ? 35  ARG D CA  1 
ATOM   4599 C  C   . ARG D 1 38  ? 136.082 69.257  45.201  1.00 30.54 ? 35  ARG D C   1 
ATOM   4600 O  O   . ARG D 1 38  ? 135.254 68.885  46.026  1.00 30.15 ? 35  ARG D O   1 
ATOM   4601 C  CB  . ARG D 1 38  ? 136.651 67.311  43.779  1.00 30.87 ? 35  ARG D CB  1 
ATOM   4602 C  CG  . ARG D 1 38  ? 137.701 66.551  43.045  1.00 31.06 ? 35  ARG D CG  1 
ATOM   4603 C  CD  . ARG D 1 38  ? 137.127 65.727  41.928  1.00 31.57 ? 35  ARG D CD  1 
ATOM   4604 N  NE  . ARG D 1 38  ? 138.152 64.829  41.388  1.00 31.77 ? 35  ARG D NE  1 
ATOM   4605 C  CZ  . ARG D 1 38  ? 137.898 63.754  40.649  1.00 31.52 ? 35  ARG D CZ  1 
ATOM   4606 N  NH1 . ARG D 1 38  ? 138.904 63.010  40.223  1.00 30.39 ? 35  ARG D NH1 1 
ATOM   4607 N  NH2 . ARG D 1 38  ? 136.643 63.417  40.339  1.00 30.92 ? 35  ARG D NH2 1 
ATOM   4608 N  N   . LEU D 1 39  ? 136.081 70.460  44.631  1.00 30.36 ? 36  LEU D N   1 
ATOM   4609 C  CA  . LEU D 1 39  ? 135.041 71.469  44.839  1.00 30.33 ? 36  LEU D CA  1 
ATOM   4610 C  C   . LEU D 1 39  ? 134.358 71.800  43.497  1.00 30.76 ? 36  LEU D C   1 
ATOM   4611 O  O   . LEU D 1 39  ? 135.015 72.192  42.524  1.00 30.50 ? 36  LEU D O   1 
ATOM   4612 C  CB  . LEU D 1 39  ? 135.617 72.729  45.507  1.00 29.63 ? 36  LEU D CB  1 
ATOM   4613 C  CG  . LEU D 1 39  ? 134.713 73.970  45.584  1.00 30.04 ? 36  LEU D CG  1 
ATOM   4614 C  CD1 . LEU D 1 39  ? 133.450 73.747  46.452  1.00 26.21 ? 36  LEU D CD1 1 
ATOM   4615 C  CD2 . LEU D 1 39  ? 135.497 75.176  46.081  1.00 29.28 ? 36  LEU D CD2 1 
ATOM   4616 N  N   . LYS D 1 40  ? 133.041 71.613  43.448  1.00 31.16 ? 37  LYS D N   1 
ATOM   4617 C  CA  . LYS D 1 40  ? 132.310 71.662  42.180  1.00 31.78 ? 37  LYS D CA  1 
ATOM   4618 C  C   . LYS D 1 40  ? 130.900 72.227  42.323  1.00 31.57 ? 37  LYS D C   1 
ATOM   4619 O  O   . LYS D 1 40  ? 130.119 71.732  43.121  1.00 31.42 ? 37  LYS D O   1 
ATOM   4620 C  CB  . LYS D 1 40  ? 132.216 70.250  41.562  1.00 32.17 ? 37  LYS D CB  1 
ATOM   4621 C  CG  . LYS D 1 40  ? 133.567 69.568  41.143  1.00 32.49 ? 37  LYS D CG  1 
ATOM   4622 C  CD  . LYS D 1 40  ? 134.183 70.173  39.903  1.00 32.17 ? 37  LYS D CD  1 
ATOM   4623 C  CE  . LYS D 1 40  ? 135.617 69.671  39.686  1.00 33.42 ? 37  LYS D CE  1 
ATOM   4624 N  NZ  . LYS D 1 40  ? 136.415 70.490  38.699  1.00 32.02 ? 37  LYS D NZ  1 
ATOM   4625 N  N   . HIS D 1 41  ? 130.588 73.260  41.542  1.00 32.10 ? 38  HIS D N   1 
ATOM   4626 C  CA  . HIS D 1 41  ? 129.194 73.662  41.274  1.00 32.78 ? 38  HIS D CA  1 
ATOM   4627 C  C   . HIS D 1 41  ? 128.435 72.454  40.691  1.00 32.31 ? 38  HIS D C   1 
ATOM   4628 O  O   . HIS D 1 41  ? 129.068 71.597  40.062  1.00 32.55 ? 38  HIS D O   1 
ATOM   4629 C  CB  . HIS D 1 41  ? 129.154 74.860  40.291  1.00 32.73 ? 38  HIS D CB  1 
ATOM   4630 C  CG  . HIS D 1 41  ? 127.839 75.590  40.273  1.00 33.93 ? 38  HIS D CG  1 
ATOM   4631 N  ND1 . HIS D 1 41  ? 126.700 75.069  39.689  1.00 35.00 ? 38  HIS D ND1 1 
ATOM   4632 C  CD2 . HIS D 1 41  ? 127.482 76.800  40.770  1.00 34.29 ? 38  HIS D CD2 1 
ATOM   4633 C  CE1 . HIS D 1 41  ? 125.700 75.923  39.832  1.00 34.93 ? 38  HIS D CE1 1 
ATOM   4634 N  NE2 . HIS D 1 41  ? 126.146 76.978  40.492  1.00 34.25 ? 38  HIS D NE2 1 
ATOM   4635 N  N   . VAL D 1 42  ? 127.112 72.365  40.891  1.00 32.09 ? 39  VAL D N   1 
ATOM   4636 C  CA  . VAL D 1 42  ? 126.309 71.277  40.235  1.00 32.41 ? 39  VAL D CA  1 
ATOM   4637 C  C   . VAL D 1 42  ? 126.403 71.251  38.724  1.00 32.14 ? 39  VAL D C   1 
ATOM   4638 O  O   . VAL D 1 42  ? 126.377 70.178  38.125  1.00 32.04 ? 39  VAL D O   1 
ATOM   4639 C  CB  . VAL D 1 42  ? 124.772 71.317  40.477  1.00 32.08 ? 39  VAL D CB  1 
ATOM   4640 C  CG1 . VAL D 1 42  ? 124.391 70.263  41.407  1.00 32.86 ? 39  VAL D CG1 1 
ATOM   4641 C  CG2 . VAL D 1 42  ? 124.274 72.703  40.866  1.00 32.36 ? 39  VAL D CG2 1 
ATOM   4642 N  N   . ASP D 1 43  ? 126.454 72.447  38.136  1.00 32.46 ? 40  ASP D N   1 
ATOM   4643 C  CA  . ASP D 1 43  ? 126.533 72.640  36.695  1.00 33.07 ? 40  ASP D CA  1 
ATOM   4644 C  C   . ASP D 1 43  ? 127.803 72.055  36.089  1.00 32.99 ? 40  ASP D C   1 
ATOM   4645 O  O   . ASP D 1 43  ? 127.854 71.820  34.889  1.00 34.00 ? 40  ASP D O   1 
ATOM   4646 C  CB  . ASP D 1 43  ? 126.431 74.132  36.360  1.00 33.46 ? 40  ASP D CB  1 
ATOM   4647 C  CG  . ASP D 1 43  ? 125.026 74.706  36.585  1.00 35.32 ? 40  ASP D CG  1 
ATOM   4648 O  OD1 . ASP D 1 43  ? 124.899 75.941  36.507  1.00 37.70 ? 40  ASP D OD1 1 
ATOM   4649 O  OD2 . ASP D 1 43  ? 124.047 73.959  36.838  1.00 37.66 ? 40  ASP D OD2 1 
ATOM   4650 N  N   . GLU D 1 44  ? 128.827 71.819  36.901  1.00 32.73 ? 41  GLU D N   1 
ATOM   4651 C  CA  . GLU D 1 44  ? 130.060 71.226  36.388  1.00 32.41 ? 41  GLU D CA  1 
ATOM   4652 C  C   . GLU D 1 44  ? 130.433 69.842  36.984  1.00 31.79 ? 41  GLU D C   1 
ATOM   4653 O  O   . GLU D 1 44  ? 131.441 69.248  36.594  1.00 32.19 ? 41  GLU D O   1 
ATOM   4654 C  CB  . GLU D 1 44  ? 131.216 72.230  36.532  1.00 32.50 ? 41  GLU D CB  1 
ATOM   4655 C  CG  . GLU D 1 44  ? 131.743 72.362  37.944  1.00 34.12 ? 41  GLU D CG  1 
ATOM   4656 C  CD  . GLU D 1 44  ? 132.573 73.618  38.162  1.00 37.10 ? 41  GLU D CD  1 
ATOM   4657 O  OE1 . GLU D 1 44  ? 133.259 74.053  37.204  1.00 38.67 ? 41  GLU D OE1 1 
ATOM   4658 O  OE2 . GLU D 1 44  ? 132.555 74.156  39.304  1.00 37.27 ? 41  GLU D OE2 1 
ATOM   4659 N  N   . ALA D 1 45  ? 129.637 69.341  37.923  1.00 30.87 ? 42  ALA D N   1 
ATOM   4660 C  CA  . ALA D 1 45  ? 129.915 68.063  38.581  1.00 30.26 ? 42  ALA D CA  1 
ATOM   4661 C  C   . ALA D 1 45  ? 129.479 66.929  37.674  1.00 30.07 ? 42  ALA D C   1 
ATOM   4662 O  O   . ALA D 1 45  ? 128.609 67.110  36.834  1.00 30.45 ? 42  ALA D O   1 
ATOM   4663 C  CB  . ALA D 1 45  ? 129.196 67.978  39.918  1.00 30.12 ? 42  ALA D CB  1 
ATOM   4664 N  N   . THR D 1 46  ? 130.091 65.763  37.825  1.00 29.63 ? 43  THR D N   1 
ATOM   4665 C  CA  . THR D 1 46  ? 129.783 64.636  36.954  1.00 29.68 ? 43  THR D CA  1 
ATOM   4666 C  C   . THR D 1 46  ? 129.442 63.436  37.820  1.00 29.53 ? 43  THR D C   1 
ATOM   4667 O  O   . THR D 1 46  ? 129.585 63.500  39.034  1.00 29.24 ? 43  THR D O   1 
ATOM   4668 C  CB  . THR D 1 46  ? 130.967 64.273  35.965  1.00 29.62 ? 43  THR D CB  1 
ATOM   4669 O  OG1 . THR D 1 46  ? 132.043 63.677  36.692  1.00 30.30 ? 43  THR D OG1 1 
ATOM   4670 C  CG2 . THR D 1 46  ? 131.485 65.495  35.179  1.00 28.60 ? 43  THR D CG2 1 
ATOM   4671 N  N   . LYS D 1 47  ? 128.995 62.342  37.209  1.00 29.74 ? 44  LYS D N   1 
ATOM   4672 C  CA  . LYS D 1 47  ? 128.762 61.131  37.992  1.00 30.12 ? 44  LYS D CA  1 
ATOM   4673 C  C   . LYS D 1 47  ? 130.085 60.482  38.360  1.00 29.98 ? 44  LYS D C   1 
ATOM   4674 O  O   . LYS D 1 47  ? 130.183 59.803  39.384  1.00 29.76 ? 44  LYS D O   1 
ATOM   4675 C  CB  . LYS D 1 47  ? 127.804 60.140  37.309  1.00 30.08 ? 44  LYS D CB  1 
ATOM   4676 C  CG  . LYS D 1 47  ? 127.937 60.011  35.817  1.00 31.01 ? 44  LYS D CG  1 
ATOM   4677 C  CD  . LYS D 1 47  ? 127.168 58.783  35.340  1.00 31.34 ? 44  LYS D CD  1 
ATOM   4678 C  CE  . LYS D 1 47  ? 126.838 58.896  33.883  1.00 31.30 ? 44  LYS D CE  1 
ATOM   4679 N  NZ  . LYS D 1 47  ? 127.078 57.603  33.173  1.00 32.10 ? 44  LYS D NZ  1 
ATOM   4680 N  N   . GLU D 1 48  ? 131.106 60.718  37.536  1.00 30.22 ? 45  GLU D N   1 
ATOM   4681 C  CA  . GLU D 1 48  ? 132.458 60.249  37.854  1.00 30.28 ? 45  GLU D CA  1 
ATOM   4682 C  C   . GLU D 1 48  ? 132.971 60.848  39.165  1.00 29.42 ? 45  GLU D C   1 
ATOM   4683 O  O   . GLU D 1 48  ? 133.672 60.164  39.910  1.00 29.04 ? 45  GLU D O   1 
ATOM   4684 C  CB  . GLU D 1 48  ? 133.437 60.519  36.705  1.00 30.67 ? 45  GLU D CB  1 
ATOM   4685 C  CG  . GLU D 1 48  ? 133.165 59.696  35.447  1.00 33.54 ? 45  GLU D CG  1 
ATOM   4686 C  CD  . GLU D 1 48  ? 131.968 60.214  34.655  1.00 37.50 ? 45  GLU D CD  1 
ATOM   4687 O  OE1 . GLU D 1 48  ? 131.962 61.411  34.285  1.00 38.42 ? 45  GLU D OE1 1 
ATOM   4688 O  OE2 . GLU D 1 48  ? 131.031 59.420  34.403  1.00 39.29 ? 45  GLU D OE2 1 
ATOM   4689 N  N   . ASP D 1 49  ? 132.606 62.104  39.449  1.00 28.68 ? 46  ASP D N   1 
ATOM   4690 C  CA  . ASP D 1 49  ? 132.982 62.742  40.711  1.00 28.55 ? 46  ASP D CA  1 
ATOM   4691 C  C   . ASP D 1 49  ? 132.420 61.996  41.900  1.00 28.04 ? 46  ASP D C   1 
ATOM   4692 O  O   . ASP D 1 49  ? 133.108 61.786  42.896  1.00 28.33 ? 46  ASP D O   1 
ATOM   4693 C  CB  . ASP D 1 49  ? 132.527 64.195  40.769  1.00 28.39 ? 46  ASP D CB  1 
ATOM   4694 C  CG  . ASP D 1 49  ? 133.357 65.106  39.896  1.00 30.43 ? 46  ASP D CG  1 
ATOM   4695 O  OD1 . ASP D 1 49  ? 134.604 64.948  39.849  1.00 33.19 ? 46  ASP D OD1 1 
ATOM   4696 O  OD2 . ASP D 1 49  ? 132.764 66.000  39.259  1.00 32.26 ? 46  ASP D OD2 1 
ATOM   4697 N  N   . VAL D 1 50  ? 131.166 61.579  41.781  1.00 28.09 ? 47  VAL D N   1 
ATOM   4698 C  CA  . VAL D 1 50  ? 130.462 60.897  42.870  1.00 27.78 ? 47  VAL D CA  1 
ATOM   4699 C  C   . VAL D 1 50  ? 131.065 59.506  43.054  1.00 27.73 ? 47  VAL D C   1 
ATOM   4700 O  O   . VAL D 1 50  ? 131.267 59.067  44.178  1.00 28.66 ? 47  VAL D O   1 
ATOM   4701 C  CB  . VAL D 1 50  ? 128.926 60.845  42.605  1.00 27.41 ? 47  VAL D CB  1 
ATOM   4702 C  CG1 . VAL D 1 50  ? 128.201 60.026  43.653  1.00 26.71 ? 47  VAL D CG1 1 
ATOM   4703 C  CG2 . VAL D 1 50  ? 128.372 62.226  42.565  1.00 27.16 ? 47  VAL D CG2 1 
ATOM   4704 N  N   . LEU D 1 51  ? 131.375 58.838  41.946  1.00 27.24 ? 48  LEU D N   1 
ATOM   4705 C  CA  . LEU D 1 51  ? 132.047 57.537  41.967  1.00 27.11 ? 48  LEU D CA  1 
ATOM   4706 C  C   . LEU D 1 51  ? 133.455 57.610  42.580  1.00 26.97 ? 48  LEU D C   1 
ATOM   4707 O  O   . LEU D 1 51  ? 133.869 56.695  43.282  1.00 26.85 ? 48  LEU D O   1 
ATOM   4708 C  CB  . LEU D 1 51  ? 132.125 56.960  40.549  1.00 26.72 ? 48  LEU D CB  1 
ATOM   4709 C  CG  . LEU D 1 51  ? 130.881 56.267  39.982  1.00 26.77 ? 48  LEU D CG  1 
ATOM   4710 C  CD1 . LEU D 1 51  ? 130.895 56.222  38.439  1.00 25.40 ? 48  LEU D CD1 1 
ATOM   4711 C  CD2 . LEU D 1 51  ? 130.738 54.861  40.555  1.00 26.66 ? 48  LEU D CD2 1 
ATOM   4712 N  N   . TRP D 1 52  ? 134.170 58.700  42.287  1.00 26.81 ? 49  TRP D N   1 
ATOM   4713 C  CA  . TRP D 1 52  ? 135.506 58.986  42.823  1.00 26.55 ? 49  TRP D CA  1 
ATOM   4714 C  C   . TRP D 1 52  ? 135.511 59.181  44.352  1.00 27.29 ? 49  TRP D C   1 
ATOM   4715 O  O   . TRP D 1 52  ? 136.470 58.759  45.026  1.00 27.05 ? 49  TRP D O   1 
ATOM   4716 C  CB  . TRP D 1 52  ? 136.090 60.224  42.116  1.00 26.11 ? 49  TRP D CB  1 
ATOM   4717 C  CG  . TRP D 1 52  ? 137.347 60.793  42.742  1.00 26.32 ? 49  TRP D CG  1 
ATOM   4718 C  CD1 . TRP D 1 52  ? 138.644 60.393  42.512  1.00 25.31 ? 49  TRP D CD1 1 
ATOM   4719 C  CD2 . TRP D 1 52  ? 137.425 61.862  43.703  1.00 26.66 ? 49  TRP D CD2 1 
ATOM   4720 N  NE1 . TRP D 1 52  ? 139.519 61.144  43.271  1.00 24.54 ? 49  TRP D NE1 1 
ATOM   4721 C  CE2 . TRP D 1 52  ? 138.803 62.055  44.005  1.00 27.41 ? 49  TRP D CE2 1 
ATOM   4722 C  CE3 . TRP D 1 52  ? 136.471 62.680  44.336  1.00 26.07 ? 49  TRP D CE3 1 
ATOM   4723 C  CZ2 . TRP D 1 52  ? 139.242 63.028  44.919  1.00 26.06 ? 49  TRP D CZ2 1 
ATOM   4724 C  CZ3 . TRP D 1 52  ? 136.911 63.648  45.239  1.00 25.39 ? 49  TRP D CZ3 1 
ATOM   4725 C  CH2 . TRP D 1 52  ? 138.289 63.811  45.516  1.00 25.73 ? 49  TRP D CH2 1 
ATOM   4726 N  N   . ALA D 1 53  ? 134.435 59.794  44.877  1.00 27.21 ? 50  ALA D N   1 
ATOM   4727 C  CA  . ALA D 1 53  ? 134.338 60.244  46.285  1.00 27.55 ? 50  ALA D CA  1 
ATOM   4728 C  C   . ALA D 1 53  ? 134.109 59.132  47.318  1.00 27.84 ? 50  ALA D C   1 
ATOM   4729 O  O   . ALA D 1 53  ? 133.286 58.227  47.107  1.00 28.05 ? 50  ALA D O   1 
ATOM   4730 C  CB  . ALA D 1 53  ? 133.224 61.311  46.429  1.00 27.21 ? 50  ALA D CB  1 
ATOM   4731 N  N   . ASP D 1 54  ? 134.826 59.218  48.441  1.00 28.01 ? 51  ASP D N   1 
ATOM   4732 C  CA  . ASP D 1 54  ? 134.547 58.393  49.624  1.00 28.13 ? 51  ASP D CA  1 
ATOM   4733 C  C   . ASP D 1 54  ? 133.491 59.128  50.449  1.00 27.99 ? 51  ASP D C   1 
ATOM   4734 O  O   . ASP D 1 54  ? 132.589 58.515  51.041  1.00 26.94 ? 51  ASP D O   1 
ATOM   4735 C  CB  . ASP D 1 54  ? 135.799 58.242  50.495  1.00 28.49 ? 51  ASP D CB  1 
ATOM   4736 C  CG  . ASP D 1 54  ? 136.950 57.583  49.773  1.00 29.47 ? 51  ASP D CG  1 
ATOM   4737 O  OD1 . ASP D 1 54  ? 136.704 56.573  49.075  1.00 31.13 ? 51  ASP D OD1 1 
ATOM   4738 O  OD2 . ASP D 1 54  ? 138.101 58.072  49.923  1.00 27.91 ? 51  ASP D OD2 1 
ATOM   4739 N  N   . GLY D 1 55  ? 133.650 60.453  50.489  1.00 28.09 ? 52  GLY D N   1 
ATOM   4740 C  CA  . GLY D 1 55  ? 132.804 61.344  51.262  1.00 27.97 ? 52  GLY D CA  1 
ATOM   4741 C  C   . GLY D 1 55  ? 132.304 62.492  50.419  1.00 28.12 ? 52  GLY D C   1 
ATOM   4742 O  O   . GLY D 1 55  ? 133.017 62.978  49.513  1.00 27.54 ? 52  GLY D O   1 
ATOM   4743 N  N   . LEU D 1 56  ? 131.065 62.905  50.704  1.00 27.88 ? 53  LEU D N   1 
ATOM   4744 C  CA  . LEU D 1 56  ? 130.440 64.047  50.038  1.00 28.01 ? 53  LEU D CA  1 
ATOM   4745 C  C   . LEU D 1 56  ? 129.903 65.031  51.032  1.00 27.75 ? 53  LEU D C   1 
ATOM   4746 O  O   . LEU D 1 56  ? 129.364 64.645  52.086  1.00 28.13 ? 53  LEU D O   1 
ATOM   4747 C  CB  . LEU D 1 56  ? 129.274 63.630  49.157  1.00 27.63 ? 53  LEU D CB  1 
ATOM   4748 C  CG  . LEU D 1 56  ? 129.483 62.889  47.855  1.00 29.57 ? 53  LEU D CG  1 
ATOM   4749 C  CD1 . LEU D 1 56  ? 129.693 61.381  48.122  1.00 30.11 ? 53  LEU D CD1 1 
ATOM   4750 C  CD2 . LEU D 1 56  ? 128.242 63.095  47.029  1.00 30.07 ? 53  LEU D CD2 1 
ATOM   4751 N  N   . ALA D 1 57  ? 130.036 66.307  50.672  1.00 27.63 ? 54  ALA D N   1 
ATOM   4752 C  CA  . ALA D 1 57  ? 129.352 67.395  51.353  1.00 27.68 ? 54  ALA D CA  1 
ATOM   4753 C  C   . ALA D 1 57  ? 128.497 68.095  50.300  1.00 27.72 ? 54  ALA D C   1 
ATOM   4754 O  O   . ALA D 1 57  ? 129.010 68.519  49.246  1.00 28.66 ? 54  ALA D O   1 
ATOM   4755 C  CB  . ALA D 1 57  ? 130.348 68.341  51.987  1.00 27.21 ? 54  ALA D CB  1 
ATOM   4756 N  N   . VAL D 1 58  ? 127.194 68.180  50.550  1.00 26.78 ? 55  VAL D N   1 
ATOM   4757 C  CA  . VAL D 1 58  ? 126.264 68.622  49.510  1.00 26.00 ? 55  VAL D CA  1 
ATOM   4758 C  C   . VAL D 1 58  ? 125.620 69.894  50.014  1.00 25.76 ? 55  VAL D C   1 
ATOM   4759 O  O   . VAL D 1 58  ? 125.025 69.900  51.075  1.00 25.33 ? 55  VAL D O   1 
ATOM   4760 C  CB  . VAL D 1 58  ? 125.187 67.487  49.169  1.00 26.10 ? 55  VAL D CB  1 
ATOM   4761 C  CG1 . VAL D 1 58  ? 124.182 67.933  48.117  1.00 24.04 ? 55  VAL D CG1 1 
ATOM   4762 C  CG2 . VAL D 1 58  ? 125.890 66.188  48.725  1.00 24.73 ? 55  VAL D CG2 1 
ATOM   4763 N  N   . GLY D 1 59  ? 125.750 70.988  49.281  1.00 25.34 ? 56  GLY D N   1 
ATOM   4764 C  CA  . GLY D 1 59  ? 125.172 72.243  49.778  1.00 25.32 ? 56  GLY D CA  1 
ATOM   4765 C  C   . GLY D 1 59  ? 124.245 72.923  48.793  1.00 24.87 ? 56  GLY D C   1 
ATOM   4766 O  O   . GLY D 1 59  ? 124.466 72.848  47.609  1.00 24.74 ? 56  GLY D O   1 
ATOM   4767 N  N   . SER D 1 60  ? 123.231 73.623  49.298  1.00 24.96 ? 57  SER D N   1 
ATOM   4768 C  CA  . SER D 1 60  ? 122.204 74.268  48.480  1.00 25.03 ? 57  SER D CA  1 
ATOM   4769 C  C   . SER D 1 60  ? 121.637 75.495  49.194  1.00 25.43 ? 57  SER D C   1 
ATOM   4770 O  O   . SER D 1 60  ? 121.556 75.512  50.426  1.00 25.74 ? 57  SER D O   1 
ATOM   4771 C  CB  . SER D 1 60  ? 121.090 73.237  48.198  1.00 25.43 ? 57  SER D CB  1 
ATOM   4772 O  OG  . SER D 1 60  ? 119.910 73.808  47.671  1.00 26.03 ? 57  SER D OG  1 
ATOM   4773 N  N   . PRO D 1 61  ? 121.210 76.528  48.440  1.00 25.87 ? 58  PRO D N   1 
ATOM   4774 C  CA  . PRO D 1 61  ? 120.370 77.554  49.113  1.00 25.95 ? 58  PRO D CA  1 
ATOM   4775 C  C   . PRO D 1 61  ? 119.115 76.909  49.677  1.00 25.89 ? 58  PRO D C   1 
ATOM   4776 O  O   . PRO D 1 61  ? 118.611 75.962  49.084  1.00 26.63 ? 58  PRO D O   1 
ATOM   4777 C  CB  . PRO D 1 61  ? 119.949 78.488  47.969  1.00 26.21 ? 58  PRO D CB  1 
ATOM   4778 C  CG  . PRO D 1 61  ? 120.261 77.733  46.707  1.00 26.24 ? 58  PRO D CG  1 
ATOM   4779 C  CD  . PRO D 1 61  ? 121.420 76.828  47.014  1.00 25.62 ? 58  PRO D CD  1 
ATOM   4780 N  N   . THR D 1 62  ? 118.629 77.382  50.817  1.00 25.57 ? 59  THR D N   1 
ATOM   4781 C  CA  . THR D 1 62  ? 117.314 76.977  51.285  1.00 25.49 ? 59  THR D CA  1 
ATOM   4782 C  C   . THR D 1 62  ? 116.289 77.616  50.358  1.00 25.71 ? 59  THR D C   1 
ATOM   4783 O  O   . THR D 1 62  ? 116.172 78.844  50.307  1.00 25.87 ? 59  THR D O   1 
ATOM   4784 C  CB  . THR D 1 62  ? 117.071 77.439  52.728  1.00 25.69 ? 59  THR D CB  1 
ATOM   4785 O  OG1 . THR D 1 62  ? 118.044 76.815  53.582  1.00 25.42 ? 59  THR D OG1 1 
ATOM   4786 C  CG2 . THR D 1 62  ? 115.634 77.129  53.175  1.00 21.93 ? 59  THR D CG2 1 
ATOM   4787 N  N   . ASN D 1 63  ? 115.569 76.788  49.613  1.00 25.42 ? 60  ASN D N   1 
ATOM   4788 C  CA  . ASN D 1 63  ? 114.572 77.278  48.674  1.00 25.40 ? 60  ASN D CA  1 
ATOM   4789 C  C   . ASN D 1 63  ? 113.225 76.674  49.020  1.00 25.73 ? 60  ASN D C   1 
ATOM   4790 O  O   . ASN D 1 63  ? 112.984 75.508  48.744  1.00 25.69 ? 60  ASN D O   1 
ATOM   4791 C  CB  . ASN D 1 63  ? 114.965 76.897  47.226  1.00 25.65 ? 60  ASN D CB  1 
ATOM   4792 C  CG  . ASN D 1 63  ? 116.143 77.732  46.679  1.00 25.67 ? 60  ASN D CG  1 
ATOM   4793 O  OD1 . ASN D 1 63  ? 116.685 77.430  45.624  1.00 28.20 ? 60  ASN D OD1 1 
ATOM   4794 N  ND2 . ASN D 1 63  ? 116.522 78.781  47.387  1.00 26.48 ? 60  ASN D ND2 1 
HETATM 4795 N  N   . MSE D 1 64  ? 112.343 77.461  49.619  1.00 26.49 ? 61  MSE D N   1 
HETATM 4796 C  CA  . MSE D 1 64  ? 111.049 76.955  50.086  1.00 27.63 ? 61  MSE D CA  1 
HETATM 4797 C  C   . MSE D 1 64  ? 111.201 75.840  51.122  1.00 26.37 ? 61  MSE D C   1 
HETATM 4798 O  O   . MSE D 1 64  ? 110.364 74.954  51.183  1.00 26.27 ? 61  MSE D O   1 
HETATM 4799 C  CB  . MSE D 1 64  ? 110.146 76.450  48.937  1.00 29.58 ? 61  MSE D CB  1 
HETATM 4800 C  CG  . MSE D 1 64  ? 109.770 77.463  47.851  1.00 34.29 ? 61  MSE D CG  1 
HETATM 4801 SE SE  . MSE D 1 64  ? 109.370 79.269  48.595  1.00 50.98 ? 61  MSE D SE  1 
HETATM 4802 C  CE  . MSE D 1 64  ? 109.505 80.468  46.781  1.00 38.63 ? 61  MSE D CE  1 
ATOM   4803 N  N   . GLY D 1 65  ? 112.271 75.878  51.912  1.00 25.01 ? 62  GLY D N   1 
ATOM   4804 C  CA  . GLY D 1 65  ? 112.513 74.882  52.945  1.00 23.51 ? 62  GLY D CA  1 
ATOM   4805 C  C   . GLY D 1 65  ? 113.286 73.661  52.507  1.00 23.64 ? 62  GLY D C   1 
ATOM   4806 O  O   . GLY D 1 65  ? 113.472 72.759  53.315  1.00 24.49 ? 62  GLY D O   1 
ATOM   4807 N  N   . LEU D 1 66  ? 113.736 73.625  51.242  1.00 22.95 ? 63  LEU D N   1 
ATOM   4808 C  CA  . LEU D 1 66  ? 114.271 72.420  50.607  1.00 23.16 ? 63  LEU D CA  1 
ATOM   4809 C  C   . LEU D 1 66  ? 115.493 72.691  49.710  1.00 23.30 ? 63  LEU D C   1 
ATOM   4810 O  O   . LEU D 1 66  ? 115.784 73.842  49.398  1.00 22.71 ? 63  LEU D O   1 
ATOM   4811 C  CB  . LEU D 1 66  ? 113.178 71.754  49.767  1.00 22.80 ? 63  LEU D CB  1 
ATOM   4812 C  CG  . LEU D 1 66  ? 111.873 71.250  50.408  1.00 25.14 ? 63  LEU D CG  1 
ATOM   4813 C  CD1 . LEU D 1 66  ? 110.801 70.866  49.358  1.00 22.51 ? 63  LEU D CD1 1 
ATOM   4814 C  CD2 . LEU D 1 66  ? 112.076 70.096  51.423  1.00 22.68 ? 63  LEU D CD2 1 
ATOM   4815 N  N   . VAL D 1 67  ? 116.207 71.620  49.329  1.00 24.33 ? 64  VAL D N   1 
ATOM   4816 C  CA  . VAL D 1 67  ? 117.202 71.635  48.263  1.00 24.12 ? 64  VAL D CA  1 
ATOM   4817 C  C   . VAL D 1 67  ? 116.644 72.381  47.072  1.00 24.46 ? 64  VAL D C   1 
ATOM   4818 O  O   . VAL D 1 67  ? 115.456 72.288  46.748  1.00 24.39 ? 64  VAL D O   1 
ATOM   4819 C  CB  . VAL D 1 67  ? 117.469 70.244  47.589  1.00 25.31 ? 64  VAL D CB  1 
ATOM   4820 C  CG1 . VAL D 1 67  ? 118.923 69.819  47.594  1.00 24.65 ? 64  VAL D CG1 1 
ATOM   4821 C  CG2 . VAL D 1 67  ? 116.435 69.182  47.910  1.00 24.53 ? 64  VAL D CG2 1 
ATOM   4822 N  N   . SER D 1 68  ? 117.540 73.116  46.442  1.00 23.75 ? 65  SER D N   1 
ATOM   4823 C  CA  . SER D 1 68  ? 117.437 73.664  45.100  1.00 23.66 ? 65  SER D CA  1 
ATOM   4824 C  C   . SER D 1 68  ? 116.744 72.709  44.123  1.00 23.35 ? 65  SER D C   1 
ATOM   4825 O  O   . SER D 1 68  ? 117.012 71.499  44.148  1.00 23.32 ? 65  SER D O   1 
ATOM   4826 C  CB  . SER D 1 68  ? 118.886 73.720  44.665  1.00 22.85 ? 65  SER D CB  1 
ATOM   4827 O  OG  . SER D 1 68  ? 119.067 74.583  43.641  1.00 27.16 ? 65  SER D OG  1 
ATOM   4828 N  N   . TRP D 1 69  ? 115.911 73.232  43.226  1.00 22.51 ? 66  TRP D N   1 
ATOM   4829 C  CA  . TRP D 1 69  ? 115.423 72.410  42.134  1.00 22.11 ? 66  TRP D CA  1 
ATOM   4830 C  C   . TRP D 1 69  ? 116.572 71.967  41.196  1.00 23.23 ? 66  TRP D C   1 
ATOM   4831 O  O   . TRP D 1 69  ? 116.522 70.861  40.631  1.00 22.80 ? 66  TRP D O   1 
ATOM   4832 C  CB  . TRP D 1 69  ? 114.237 73.051  41.361  1.00 20.97 ? 66  TRP D CB  1 
ATOM   4833 C  CG  . TRP D 1 69  ? 114.533 74.185  40.411  1.00 19.50 ? 66  TRP D CG  1 
ATOM   4834 C  CD1 . TRP D 1 69  ? 114.287 75.519  40.620  1.00 19.27 ? 66  TRP D CD1 1 
ATOM   4835 C  CD2 . TRP D 1 69  ? 115.095 74.089  39.086  1.00 17.49 ? 66  TRP D CD2 1 
ATOM   4836 N  NE1 . TRP D 1 69  ? 114.685 76.256  39.522  1.00 16.62 ? 66  TRP D NE1 1 
ATOM   4837 C  CE2 . TRP D 1 69  ? 115.181 75.403  38.570  1.00 16.95 ? 66  TRP D CE2 1 
ATOM   4838 C  CE3 . TRP D 1 69  ? 115.530 73.024  38.291  1.00 17.08 ? 66  TRP D CE3 1 
ATOM   4839 C  CZ2 . TRP D 1 69  ? 115.672 75.676  37.284  1.00 17.44 ? 66  TRP D CZ2 1 
ATOM   4840 C  CZ3 . TRP D 1 69  ? 116.029 73.301  37.010  1.00 18.16 ? 66  TRP D CZ3 1 
ATOM   4841 C  CH2 . TRP D 1 69  ? 116.091 74.615  36.526  1.00 17.83 ? 66  TRP D CH2 1 
ATOM   4842 N  N   . LYS D 1 70  ? 117.589 72.823  41.031  1.00 23.65 ? 67  LYS D N   1 
ATOM   4843 C  CA  . LYS D 1 70  ? 118.780 72.446  40.266  1.00 24.64 ? 67  LYS D CA  1 
ATOM   4844 C  C   . LYS D 1 70  ? 119.579 71.320  40.901  1.00 24.99 ? 67  LYS D C   1 
ATOM   4845 O  O   . LYS D 1 70  ? 120.095 70.471  40.200  1.00 25.29 ? 67  LYS D O   1 
ATOM   4846 C  CB  . LYS D 1 70  ? 119.675 73.650  39.980  1.00 25.05 ? 67  LYS D CB  1 
ATOM   4847 C  CG  . LYS D 1 70  ? 119.557 74.104  38.540  1.00 26.91 ? 67  LYS D CG  1 
ATOM   4848 C  CD  . LYS D 1 70  ? 119.707 75.599  38.338  1.00 28.54 ? 67  LYS D CD  1 
ATOM   4849 C  CE  . LYS D 1 70  ? 119.428 75.992  36.841  1.00 29.57 ? 67  LYS D CE  1 
ATOM   4850 N  NZ  . LYS D 1 70  ? 120.125 75.191  35.736  1.00 31.39 ? 67  LYS D NZ  1 
HETATM 4851 N  N   . MSE D 1 71  ? 119.685 71.310  42.227  1.00 26.05 ? 68  MSE D N   1 
HETATM 4852 C  CA  . MSE D 1 71  ? 120.421 70.251  42.905  1.00 26.27 ? 68  MSE D CA  1 
HETATM 4853 C  C   . MSE D 1 71  ? 119.630 68.948  42.823  1.00 24.65 ? 68  MSE D C   1 
HETATM 4854 O  O   . MSE D 1 71  ? 120.201 67.902  42.525  1.00 24.40 ? 68  MSE D O   1 
HETATM 4855 C  CB  . MSE D 1 71  ? 120.743 70.621  44.351  1.00 27.50 ? 68  MSE D CB  1 
HETATM 4856 C  CG  . MSE D 1 71  ? 121.483 69.521  45.120  1.00 34.45 ? 68  MSE D CG  1 
HETATM 4857 SE SE  . MSE D 1 71  ? 123.325 69.265  44.387  1.00 56.78 ? 68  MSE D SE  1 
HETATM 4858 C  CE  . MSE D 1 71  ? 124.168 70.700  45.506  1.00 48.52 ? 68  MSE D CE  1 
ATOM   4859 N  N   . LYS D 1 72  ? 118.323 69.036  43.057  1.00 22.89 ? 69  LYS D N   1 
ATOM   4860 C  CA  . LYS D 1 72  ? 117.402 67.918  42.900  1.00 22.43 ? 69  LYS D CA  1 
ATOM   4861 C  C   . LYS D 1 72  ? 117.456 67.309  41.470  1.00 21.81 ? 69  LYS D C   1 
ATOM   4862 O  O   . LYS D 1 72  ? 117.577 66.092  41.296  1.00 21.82 ? 69  LYS D O   1 
ATOM   4863 C  CB  . LYS D 1 72  ? 115.975 68.379  43.267  1.00 22.43 ? 69  LYS D CB  1 
ATOM   4864 C  CG  . LYS D 1 72  ? 114.955 67.255  43.399  1.00 23.89 ? 69  LYS D CG  1 
ATOM   4865 C  CD  . LYS D 1 72  ? 115.151 66.435  44.696  1.00 23.66 ? 69  LYS D CD  1 
ATOM   4866 C  CE  . LYS D 1 72  ? 114.750 64.972  44.517  1.00 21.34 ? 69  LYS D CE  1 
ATOM   4867 N  NZ  . LYS D 1 72  ? 113.439 64.821  43.793  1.00 21.53 ? 69  LYS D NZ  1 
ATOM   4868 N  N   . ARG D 1 73  ? 117.385 68.165  40.459  1.00 20.94 ? 70  ARG D N   1 
ATOM   4869 C  CA  . ARG D 1 73  ? 117.483 67.750  39.057  1.00 20.12 ? 70  ARG D CA  1 
ATOM   4870 C  C   . ARG D 1 73  ? 118.746 66.944  38.757  1.00 21.00 ? 70  ARG D C   1 
ATOM   4871 O  O   . ARG D 1 73  ? 118.690 65.945  38.018  1.00 20.88 ? 70  ARG D O   1 
ATOM   4872 C  CB  . ARG D 1 73  ? 117.429 68.965  38.147  1.00 18.63 ? 70  ARG D CB  1 
ATOM   4873 C  CG  . ARG D 1 73  ? 117.508 68.677  36.681  1.00 15.21 ? 70  ARG D CG  1 
ATOM   4874 C  CD  . ARG D 1 73  ? 117.347 69.972  36.002  1.00 9.33  ? 70  ARG D CD  1 
ATOM   4875 N  NE  . ARG D 1 73  ? 117.373 69.838  34.571  1.00 7.00  ? 70  ARG D NE  1 
ATOM   4876 C  CZ  . ARG D 1 73  ? 118.371 70.263  33.795  1.00 5.98  ? 70  ARG D CZ  1 
ATOM   4877 N  NH1 . ARG D 1 73  ? 118.303 70.071  32.493  1.00 2.00  ? 70  ARG D NH1 1 
ATOM   4878 N  NH2 . ARG D 1 73  ? 119.442 70.848  34.327  1.00 5.03  ? 70  ARG D NH2 1 
ATOM   4879 N  N   . PHE D 1 74  ? 119.868 67.371  39.332  1.00 21.96 ? 71  PHE D N   1 
ATOM   4880 C  CA  . PHE D 1 74  ? 121.145 66.655  39.187  1.00 23.32 ? 71  PHE D CA  1 
ATOM   4881 C  C   . PHE D 1 74  ? 121.166 65.218  39.789  1.00 23.55 ? 71  PHE D C   1 
ATOM   4882 O  O   . PHE D 1 74  ? 121.664 64.290  39.155  1.00 24.06 ? 71  PHE D O   1 
ATOM   4883 C  CB  . PHE D 1 74  ? 122.296 67.508  39.729  1.00 23.50 ? 71  PHE D CB  1 
ATOM   4884 C  CG  . PHE D 1 74  ? 123.617 66.816  39.693  1.00 25.33 ? 71  PHE D CG  1 
ATOM   4885 C  CD1 . PHE D 1 74  ? 124.300 66.653  38.488  1.00 25.63 ? 71  PHE D CD1 1 
ATOM   4886 C  CD2 . PHE D 1 74  ? 124.187 66.308  40.861  1.00 25.47 ? 71  PHE D CD2 1 
ATOM   4887 C  CE1 . PHE D 1 74  ? 125.539 65.990  38.447  1.00 25.45 ? 71  PHE D CE1 1 
ATOM   4888 C  CE2 . PHE D 1 74  ? 125.406 65.652  40.816  1.00 25.61 ? 71  PHE D CE2 1 
ATOM   4889 C  CZ  . PHE D 1 74  ? 126.078 65.484  39.599  1.00 23.65 ? 71  PHE D CZ  1 
ATOM   4890 N  N   . PHE D 1 75  ? 120.613 65.042  40.982  1.00 23.88 ? 72  PHE D N   1 
ATOM   4891 C  CA  . PHE D 1 75  ? 120.445 63.723  41.593  1.00 24.59 ? 72  PHE D CA  1 
ATOM   4892 C  C   . PHE D 1 75  ? 119.451 62.814  40.855  1.00 24.96 ? 72  PHE D C   1 
ATOM   4893 O  O   . PHE D 1 75  ? 119.755 61.643  40.618  1.00 25.40 ? 72  PHE D O   1 
ATOM   4894 C  CB  . PHE D 1 75  ? 120.071 63.857  43.087  1.00 25.06 ? 72  PHE D CB  1 
ATOM   4895 C  CG  . PHE D 1 75  ? 121.255 64.145  43.976  1.00 25.51 ? 72  PHE D CG  1 
ATOM   4896 C  CD1 . PHE D 1 75  ? 121.868 65.400  43.961  1.00 24.90 ? 72  PHE D CD1 1 
ATOM   4897 C  CD2 . PHE D 1 75  ? 121.772 63.158  44.815  1.00 27.10 ? 72  PHE D CD2 1 
ATOM   4898 C  CE1 . PHE D 1 75  ? 122.975 65.674  44.742  1.00 25.25 ? 72  PHE D CE1 1 
ATOM   4899 C  CE2 . PHE D 1 75  ? 122.895 63.427  45.619  1.00 28.08 ? 72  PHE D CE2 1 
ATOM   4900 C  CZ  . PHE D 1 75  ? 123.495 64.694  45.578  1.00 26.55 ? 72  PHE D CZ  1 
ATOM   4901 N  N   . ASP D 1 76  ? 118.281 63.342  40.494  1.00 24.95 ? 73  ASP D N   1 
ATOM   4902 C  CA  . ASP D 1 76  ? 117.257 62.555  39.817  1.00 25.80 ? 73  ASP D CA  1 
ATOM   4903 C  C   . ASP D 1 76  ? 117.766 62.170  38.441  1.00 25.86 ? 73  ASP D C   1 
ATOM   4904 O  O   . ASP D 1 76  ? 117.658 61.000  38.048  1.00 25.88 ? 73  ASP D O   1 
ATOM   4905 C  CB  . ASP D 1 76  ? 115.905 63.317  39.657  1.00 25.96 ? 73  ASP D CB  1 
ATOM   4906 C  CG  . ASP D 1 76  ? 115.173 63.609  41.005  1.00 29.80 ? 73  ASP D CG  1 
ATOM   4907 O  OD1 . ASP D 1 76  ? 115.509 62.968  42.038  1.00 35.93 ? 73  ASP D OD1 1 
ATOM   4908 O  OD2 . ASP D 1 76  ? 114.234 64.473  41.046  1.00 29.16 ? 73  ASP D OD2 1 
ATOM   4909 N  N   . ASP D 1 77  ? 118.325 63.141  37.710  1.00 26.08 ? 74  ASP D N   1 
ATOM   4910 C  CA  . ASP D 1 77  ? 118.528 62.963  36.259  1.00 26.66 ? 74  ASP D CA  1 
ATOM   4911 C  C   . ASP D 1 77  ? 119.936 62.574  35.844  1.00 26.99 ? 74  ASP D C   1 
ATOM   4912 O  O   . ASP D 1 77  ? 120.104 61.882  34.852  1.00 27.18 ? 74  ASP D O   1 
ATOM   4913 C  CB  . ASP D 1 77  ? 117.939 64.124  35.406  1.00 26.44 ? 74  ASP D CB  1 
ATOM   4914 C  CG  . ASP D 1 77  ? 116.380 64.122  35.381  1.00 27.58 ? 74  ASP D CG  1 
ATOM   4915 O  OD1 . ASP D 1 77  ? 115.743 63.218  35.976  1.00 26.86 ? 74  ASP D OD1 1 
ATOM   4916 O  OD2 . ASP D 1 77  ? 115.771 65.027  34.767  1.00 28.11 ? 74  ASP D OD2 1 
ATOM   4917 N  N   . VAL D 1 78  ? 120.956 63.000  36.579  1.00 27.70 ? 75  VAL D N   1 
ATOM   4918 C  CA  . VAL D 1 78  ? 122.299 62.525  36.235  1.00 28.35 ? 75  VAL D CA  1 
ATOM   4919 C  C   . VAL D 1 78  ? 122.857 61.440  37.156  1.00 28.50 ? 75  VAL D C   1 
ATOM   4920 O  O   . VAL D 1 78  ? 123.496 60.512  36.676  1.00 30.08 ? 75  VAL D O   1 
ATOM   4921 C  CB  . VAL D 1 78  ? 123.308 63.662  35.858  1.00 28.43 ? 75  VAL D CB  1 
ATOM   4922 C  CG1 . VAL D 1 78  ? 122.726 65.020  36.136  1.00 29.64 ? 75  VAL D CG1 1 
ATOM   4923 C  CG2 . VAL D 1 78  ? 124.696 63.449  36.478  1.00 27.42 ? 75  VAL D CG2 1 
ATOM   4924 N  N   . LEU D 1 79  ? 122.570 61.510  38.445  1.00 28.29 ? 76  LEU D N   1 
ATOM   4925 C  CA  . LEU D 1 79  ? 123.025 60.474  39.371  1.00 27.93 ? 76  LEU D CA  1 
ATOM   4926 C  C   . LEU D 1 79  ? 122.114 59.261  39.488  1.00 27.95 ? 76  LEU D C   1 
ATOM   4927 O  O   . LEU D 1 79  ? 122.529 58.233  40.008  1.00 27.54 ? 76  LEU D O   1 
ATOM   4928 C  CB  . LEU D 1 79  ? 123.249 61.040  40.761  1.00 27.23 ? 76  LEU D CB  1 
ATOM   4929 C  CG  . LEU D 1 79  ? 124.331 62.089  40.957  1.00 27.38 ? 76  LEU D CG  1 
ATOM   4930 C  CD1 . LEU D 1 79  ? 124.534 62.219  42.456  1.00 25.14 ? 76  LEU D CD1 1 
ATOM   4931 C  CD2 . LEU D 1 79  ? 125.657 61.769  40.209  1.00 24.06 ? 76  LEU D CD2 1 
ATOM   4932 N  N   . GLY D 1 80  ? 120.878 59.381  39.020  1.00 28.22 ? 77  GLY D N   1 
ATOM   4933 C  CA  . GLY D 1 80  ? 119.909 58.311  39.170  1.00 28.25 ? 77  GLY D CA  1 
ATOM   4934 C  C   . GLY D 1 80  ? 120.342 56.949  38.651  1.00 28.91 ? 77  GLY D C   1 
ATOM   4935 O  O   . GLY D 1 80  ? 119.942 55.926  39.216  1.00 28.55 ? 77  GLY D O   1 
ATOM   4936 N  N   . ASP D 1 81  ? 121.139 56.926  37.571  1.00 29.40 ? 78  ASP D N   1 
ATOM   4937 C  CA  . ASP D 1 81  ? 121.579 55.673  36.952  1.00 29.77 ? 78  ASP D CA  1 
ATOM   4938 C  C   . ASP D 1 81  ? 122.542 54.889  37.888  1.00 28.82 ? 78  ASP D C   1 
ATOM   4939 O  O   . ASP D 1 81  ? 122.813 53.700  37.676  1.00 28.93 ? 78  ASP D O   1 
ATOM   4940 C  CB  . ASP D 1 81  ? 122.193 55.913  35.555  1.00 30.62 ? 78  ASP D CB  1 
ATOM   4941 C  CG  . ASP D 1 81  ? 121.113 56.150  34.414  1.00 35.21 ? 78  ASP D CG  1 
ATOM   4942 O  OD1 . ASP D 1 81  ? 120.034 55.482  34.391  1.00 39.42 ? 78  ASP D OD1 1 
ATOM   4943 O  OD2 . ASP D 1 81  ? 121.362 56.989  33.493  1.00 36.07 ? 78  ASP D OD2 1 
ATOM   4944 N  N   . LEU D 1 82  ? 123.027 55.554  38.937  1.00 27.62 ? 79  LEU D N   1 
ATOM   4945 C  CA  . LEU D 1 82  ? 123.949 54.937  39.910  1.00 26.51 ? 79  LEU D CA  1 
ATOM   4946 C  C   . LEU D 1 82  ? 123.213 54.400  41.128  1.00 25.69 ? 79  LEU D C   1 
ATOM   4947 O  O   . LEU D 1 82  ? 123.801 53.708  41.970  1.00 24.99 ? 79  LEU D O   1 
ATOM   4948 C  CB  . LEU D 1 82  ? 125.030 55.924  40.358  1.00 26.31 ? 79  LEU D CB  1 
ATOM   4949 C  CG  . LEU D 1 82  ? 125.781 56.731  39.301  1.00 27.09 ? 79  LEU D CG  1 
ATOM   4950 C  CD1 . LEU D 1 82  ? 126.728 57.697  40.007  1.00 30.15 ? 79  LEU D CD1 1 
ATOM   4951 C  CD2 . LEU D 1 82  ? 126.538 55.844  38.300  1.00 27.13 ? 79  LEU D CD2 1 
ATOM   4952 N  N   . TRP D 1 83  ? 121.926 54.733  41.212  1.00 24.65 ? 80  TRP D N   1 
ATOM   4953 C  CA  . TRP D 1 83  ? 121.098 54.267  42.292  1.00 24.43 ? 80  TRP D CA  1 
ATOM   4954 C  C   . TRP D 1 83  ? 121.175 52.728  42.426  1.00 24.13 ? 80  TRP D C   1 
ATOM   4955 O  O   . TRP D 1 83  ? 121.027 51.978  41.453  1.00 23.62 ? 80  TRP D O   1 
ATOM   4956 C  CB  . TRP D 1 83  ? 119.646 54.803  42.180  1.00 24.53 ? 80  TRP D CB  1 
ATOM   4957 C  CG  . TRP D 1 83  ? 118.864 54.517  43.426  1.00 24.73 ? 80  TRP D CG  1 
ATOM   4958 C  CD1 . TRP D 1 83  ? 118.767 55.307  44.540  1.00 24.31 ? 80  TRP D CD1 1 
ATOM   4959 C  CD2 . TRP D 1 83  ? 118.155 53.303  43.726  1.00 24.63 ? 80  TRP D CD2 1 
ATOM   4960 N  NE1 . TRP D 1 83  ? 117.990 54.681  45.491  1.00 25.31 ? 80  TRP D NE1 1 
ATOM   4961 C  CE2 . TRP D 1 83  ? 117.618 53.442  45.019  1.00 22.91 ? 80  TRP D CE2 1 
ATOM   4962 C  CE3 . TRP D 1 83  ? 117.915 52.114  43.011  1.00 25.35 ? 80  TRP D CE3 1 
ATOM   4963 C  CZ2 . TRP D 1 83  ? 116.859 52.450  45.619  1.00 21.99 ? 80  TRP D CZ2 1 
ATOM   4964 C  CZ3 . TRP D 1 83  ? 117.154 51.127  43.608  1.00 24.87 ? 80  TRP D CZ3 1 
ATOM   4965 C  CH2 . TRP D 1 83  ? 116.633 51.307  44.909  1.00 24.62 ? 80  TRP D CH2 1 
ATOM   4966 N  N   . GLY D 1 84  ? 121.467 52.279  43.642  1.00 23.77 ? 81  GLY D N   1 
ATOM   4967 C  CA  . GLY D 1 84  ? 121.491 50.871  43.929  1.00 23.72 ? 81  GLY D CA  1 
ATOM   4968 C  C   . GLY D 1 84  ? 122.864 50.260  43.879  1.00 24.19 ? 81  GLY D C   1 
ATOM   4969 O  O   . GLY D 1 84  ? 123.011 49.083  44.203  1.00 23.72 ? 81  GLY D O   1 
ATOM   4970 N  N   . GLU D 1 85  ? 123.870 51.044  43.480  1.00 25.01 ? 82  GLU D N   1 
ATOM   4971 C  CA  . GLU D 1 85  ? 125.234 50.512  43.345  1.00 26.46 ? 82  GLU D CA  1 
ATOM   4972 C  C   . GLU D 1 85  ? 126.330 51.421  43.895  1.00 26.40 ? 82  GLU D C   1 
ATOM   4973 O  O   . GLU D 1 85  ? 127.509 51.142  43.710  1.00 27.61 ? 82  GLU D O   1 
ATOM   4974 C  CB  . GLU D 1 85  ? 125.536 50.079  41.895  1.00 26.19 ? 82  GLU D CB  1 
ATOM   4975 C  CG  . GLU D 1 85  ? 125.675 51.230  40.879  1.00 28.14 ? 82  GLU D CG  1 
ATOM   4976 C  CD  . GLU D 1 85  ? 125.844 50.741  39.421  1.00 28.77 ? 82  GLU D CD  1 
ATOM   4977 O  OE1 . GLU D 1 85  ? 125.127 51.236  38.519  1.00 31.99 ? 82  GLU D OE1 1 
ATOM   4978 O  OE2 . GLU D 1 85  ? 126.689 49.855  39.175  1.00 30.86 ? 82  GLU D OE2 1 
ATOM   4979 N  N   . ILE D 1 86  ? 125.954 52.481  44.598  1.00 26.19 ? 83  ILE D N   1 
ATOM   4980 C  CA  . ILE D 1 86  ? 126.934 53.337  45.288  1.00 25.94 ? 83  ILE D CA  1 
ATOM   4981 C  C   . ILE D 1 86  ? 126.698 53.444  46.808  1.00 25.70 ? 83  ILE D C   1 
ATOM   4982 O  O   . ILE D 1 86  ? 127.154 54.361  47.468  1.00 25.87 ? 83  ILE D O   1 
ATOM   4983 C  CB  . ILE D 1 86  ? 127.054 54.746  44.630  1.00 26.35 ? 83  ILE D CB  1 
ATOM   4984 C  CG1 . ILE D 1 86  ? 125.677 55.403  44.472  1.00 25.27 ? 83  ILE D CG1 1 
ATOM   4985 C  CG2 . ILE D 1 86  ? 127.782 54.628  43.277  1.00 25.40 ? 83  ILE D CG2 1 
ATOM   4986 C  CD1 . ILE D 1 86  ? 125.722 56.893  44.213  1.00 25.88 ? 83  ILE D CD1 1 
ATOM   4987 N  N   . ASP D 1 87  ? 126.005 52.464  47.354  1.00 25.60 ? 84  ASP D N   1 
ATOM   4988 C  CA  . ASP D 1 87  ? 125.765 52.383  48.776  1.00 26.16 ? 84  ASP D CA  1 
ATOM   4989 C  C   . ASP D 1 87  ? 127.040 52.423  49.593  1.00 26.49 ? 84  ASP D C   1 
ATOM   4990 O  O   . ASP D 1 87  ? 128.035 51.792  49.244  1.00 27.39 ? 84  ASP D O   1 
ATOM   4991 C  CB  . ASP D 1 87  ? 125.028 51.088  49.084  1.00 26.25 ? 84  ASP D CB  1 
ATOM   4992 C  CG  . ASP D 1 87  ? 123.690 50.992  48.368  1.00 27.54 ? 84  ASP D CG  1 
ATOM   4993 O  OD1 . ASP D 1 87  ? 123.654 50.944  47.110  1.00 27.49 ? 84  ASP D OD1 1 
ATOM   4994 O  OD2 . ASP D 1 87  ? 122.670 50.964  49.084  1.00 28.67 ? 84  ASP D OD2 1 
ATOM   4995 N  N   . GLY D 1 88  ? 127.013 53.143  50.703  1.00 26.73 ? 85  GLY D N   1 
ATOM   4996 C  CA  . GLY D 1 88  ? 128.136 53.106  51.615  1.00 26.69 ? 85  GLY D CA  1 
ATOM   4997 C  C   . GLY D 1 88  ? 129.039 54.308  51.518  1.00 26.94 ? 85  GLY D C   1 
ATOM   4998 O  O   . GLY D 1 88  ? 130.029 54.392  52.236  1.00 27.69 ? 85  GLY D O   1 
ATOM   4999 N  N   . LYS D 1 89  ? 128.724 55.241  50.629  1.00 26.93 ? 86  LYS D N   1 
ATOM   5000 C  CA  . LYS D 1 89  ? 129.365 56.555  50.707  1.00 26.92 ? 86  LYS D CA  1 
ATOM   5001 C  C   . LYS D 1 89  ? 128.921 57.298  51.988  1.00 26.86 ? 86  LYS D C   1 
ATOM   5002 O  O   . LYS D 1 89  ? 127.871 56.997  52.566  1.00 27.15 ? 86  LYS D O   1 
ATOM   5003 C  CB  . LYS D 1 89  ? 129.155 57.383  49.426  1.00 27.26 ? 86  LYS D CB  1 
ATOM   5004 C  CG  . LYS D 1 89  ? 129.695 56.670  48.175  1.00 26.69 ? 86  LYS D CG  1 
ATOM   5005 C  CD  . LYS D 1 89  ? 129.541 57.501  46.902  1.00 26.18 ? 86  LYS D CD  1 
ATOM   5006 C  CE  . LYS D 1 89  ? 130.110 56.741  45.702  1.00 26.04 ? 86  LYS D CE  1 
ATOM   5007 N  NZ  . LYS D 1 89  ? 131.624 56.507  45.670  1.00 23.79 ? 86  LYS D NZ  1 
ATOM   5008 N  N   . ILE D 1 90  ? 129.768 58.217  52.443  1.00 26.59 ? 87  ILE D N   1 
ATOM   5009 C  CA  . ILE D 1 90  ? 129.601 58.959  53.679  1.00 26.18 ? 87  ILE D CA  1 
ATOM   5010 C  C   . ILE D 1 90  ? 129.304 60.393  53.251  1.00 26.06 ? 87  ILE D C   1 
ATOM   5011 O  O   . ILE D 1 90  ? 130.024 60.937  52.425  1.00 26.94 ? 87  ILE D O   1 
ATOM   5012 C  CB  . ILE D 1 90  ? 130.873 58.836  54.545  1.00 26.04 ? 87  ILE D CB  1 
ATOM   5013 C  CG1 . ILE D 1 90  ? 130.914 57.429  55.169  1.00 26.35 ? 87  ILE D CG1 1 
ATOM   5014 C  CG2 . ILE D 1 90  ? 130.927 59.921  55.623  1.00 26.69 ? 87  ILE D CG2 1 
ATOM   5015 C  CD1 . ILE D 1 90  ? 132.270 56.948  55.649  1.00 24.18 ? 87  ILE D CD1 1 
ATOM   5016 N  N   . ALA D 1 91  ? 128.230 60.983  53.767  1.00 24.95 ? 88  ALA D N   1 
ATOM   5017 C  CA  . ALA D 1 91  ? 127.757 62.260  53.244  1.00 24.57 ? 88  ALA D CA  1 
ATOM   5018 C  C   . ALA D 1 91  ? 127.063 63.147  54.284  1.00 24.41 ? 88  ALA D C   1 
ATOM   5019 O  O   . ALA D 1 91  ? 126.513 62.683  55.292  1.00 23.24 ? 88  ALA D O   1 
ATOM   5020 C  CB  . ALA D 1 91  ? 126.825 62.034  52.011  1.00 24.31 ? 88  ALA D CB  1 
ATOM   5021 N  N   . CYS D 1 92  ? 127.101 64.446  54.016  1.00 25.13 ? 89  CYS D N   1 
ATOM   5022 C  CA  . CYS D 1 92  ? 126.504 65.446  54.921  1.00 25.18 ? 89  CYS D CA  1 
ATOM   5023 C  C   . CYS D 1 92  ? 126.024 66.608  54.069  1.00 25.00 ? 89  CYS D C   1 
ATOM   5024 O  O   . CYS D 1 92  ? 126.236 66.606  52.859  1.00 25.69 ? 89  CYS D O   1 
ATOM   5025 C  CB  . CYS D 1 92  ? 127.518 65.891  55.984  1.00 24.41 ? 89  CYS D CB  1 
ATOM   5026 S  SG  . CYS D 1 92  ? 129.042 66.566  55.283  1.00 24.54 ? 89  CYS D SG  1 
ATOM   5027 N  N   . ALA D 1 93  ? 125.398 67.591  54.709  1.00 25.71 ? 90  ALA D N   1 
ATOM   5028 C  CA  . ALA D 1 93  ? 124.603 68.623  54.034  1.00 25.73 ? 90  ALA D CA  1 
ATOM   5029 C  C   . ALA D 1 93  ? 124.942 69.990  54.563  1.00 26.01 ? 90  ALA D C   1 
ATOM   5030 O  O   . ALA D 1 93  ? 125.387 70.128  55.708  1.00 26.74 ? 90  ALA D O   1 
ATOM   5031 C  CB  . ALA D 1 93  ? 123.168 68.370  54.258  1.00 25.73 ? 90  ALA D CB  1 
ATOM   5032 N  N   . PHE D 1 94  ? 124.745 71.015  53.744  1.00 25.84 ? 91  PHE D N   1 
ATOM   5033 C  CA  . PHE D 1 94  ? 124.896 72.394  54.240  1.00 26.16 ? 91  PHE D CA  1 
ATOM   5034 C  C   . PHE D 1 94  ? 124.023 73.322  53.444  1.00 26.11 ? 91  PHE D C   1 
ATOM   5035 O  O   . PHE D 1 94  ? 123.699 73.041  52.295  1.00 27.09 ? 91  PHE D O   1 
ATOM   5036 C  CB  . PHE D 1 94  ? 126.375 72.872  54.335  1.00 25.29 ? 91  PHE D CB  1 
ATOM   5037 C  CG  . PHE D 1 94  ? 127.089 72.999  53.012  1.00 25.12 ? 91  PHE D CG  1 
ATOM   5038 C  CD1 . PHE D 1 94  ? 127.761 71.900  52.455  1.00 25.44 ? 91  PHE D CD1 1 
ATOM   5039 C  CD2 . PHE D 1 94  ? 127.129 74.223  52.334  1.00 24.97 ? 91  PHE D CD2 1 
ATOM   5040 C  CE1 . PHE D 1 94  ? 128.456 72.000  51.231  1.00 24.86 ? 91  PHE D CE1 1 
ATOM   5041 C  CE2 . PHE D 1 94  ? 127.810 74.346  51.101  1.00 25.64 ? 91  PHE D CE2 1 
ATOM   5042 C  CZ  . PHE D 1 94  ? 128.484 73.224  50.551  1.00 25.25 ? 91  PHE D CZ  1 
ATOM   5043 N  N   . SER D 1 95  ? 123.617 74.420  54.058  1.00 26.49 ? 92  SER D N   1 
ATOM   5044 C  CA  . SER D 1 95  ? 122.661 75.305  53.415  1.00 26.09 ? 92  SER D CA  1 
ATOM   5045 C  C   . SER D 1 95  ? 122.708 76.724  53.944  1.00 25.65 ? 92  SER D C   1 
ATOM   5046 O  O   . SER D 1 95  ? 122.936 76.951  55.114  1.00 25.45 ? 92  SER D O   1 
ATOM   5047 C  CB  . SER D 1 95  ? 121.244 74.729  53.562  1.00 25.85 ? 92  SER D CB  1 
ATOM   5048 O  OG  . SER D 1 95  ? 120.342 75.415  52.723  1.00 26.76 ? 92  SER D OG  1 
ATOM   5049 N  N   . SER D 1 96  ? 122.464 77.672  53.055  1.00 25.89 ? 93  SER D N   1 
ATOM   5050 C  CA  . SER D 1 96  ? 122.349 79.074  53.403  1.00 25.96 ? 93  SER D CA  1 
ATOM   5051 C  C   . SER D 1 96  ? 120.921 79.533  53.149  1.00 26.01 ? 93  SER D C   1 
ATOM   5052 O  O   . SER D 1 96  ? 120.378 79.266  52.090  1.00 26.35 ? 93  SER D O   1 
ATOM   5053 C  CB  . SER D 1 96  ? 123.305 79.894  52.548  1.00 25.65 ? 93  SER D CB  1 
ATOM   5054 O  OG  . SER D 1 96  ? 123.075 81.277  52.736  1.00 27.14 ? 93  SER D OG  1 
ATOM   5055 N  N   . SER D 1 97  ? 120.316 80.227  54.111  1.00 25.91 ? 94  SER D N   1 
ATOM   5056 C  CA  . SER D 1 97  ? 118.949 80.732  53.968  1.00 25.79 ? 94  SER D CA  1 
ATOM   5057 C  C   . SER D 1 97  ? 118.858 82.259  54.078  1.00 25.77 ? 94  SER D C   1 
ATOM   5058 O  O   . SER D 1 97  ? 119.836 82.942  54.420  1.00 26.98 ? 94  SER D O   1 
ATOM   5059 C  CB  . SER D 1 97  ? 118.031 80.071  54.989  1.00 25.86 ? 94  SER D CB  1 
ATOM   5060 O  OG  . SER D 1 97  ? 118.480 80.296  56.311  1.00 27.18 ? 94  SER D OG  1 
ATOM   5061 N  N   . GLY D 1 98  ? 117.693 82.807  53.762  1.00 25.63 ? 95  GLY D N   1 
ATOM   5062 C  CA  . GLY D 1 98  ? 117.486 84.255  53.824  1.00 24.66 ? 95  GLY D CA  1 
ATOM   5063 C  C   . GLY D 1 98  ? 117.365 84.781  55.247  1.00 24.60 ? 95  GLY D C   1 
ATOM   5064 O  O   . GLY D 1 98  ? 117.492 85.979  55.479  1.00 25.12 ? 95  GLY D O   1 
ATOM   5065 N  N   . GLY D 1 99  ? 117.078 83.892  56.193  1.00 23.97 ? 96  GLY D N   1 
ATOM   5066 C  CA  . GLY D 1 99  ? 116.831 84.285  57.564  1.00 23.16 ? 96  GLY D CA  1 
ATOM   5067 C  C   . GLY D 1 99  ? 116.948 83.110  58.511  1.00 22.72 ? 96  GLY D C   1 
ATOM   5068 O  O   . GLY D 1 99  ? 116.655 81.981  58.165  1.00 22.39 ? 96  GLY D O   1 
ATOM   5069 N  N   . TRP D 1 100 ? 117.438 83.383  59.703  1.00 22.81 ? 97  TRP D N   1 
ATOM   5070 C  CA  . TRP D 1 100 ? 117.295 82.472  60.817  1.00 22.78 ? 97  TRP D CA  1 
ATOM   5071 C  C   . TRP D 1 100 ? 115.798 82.188  61.082  1.00 22.68 ? 97  TRP D C   1 
ATOM   5072 O  O   . TRP D 1 100 ? 114.962 83.091  61.006  1.00 21.74 ? 97  TRP D O   1 
ATOM   5073 C  CB  . TRP D 1 100 ? 118.013 83.050  62.027  1.00 22.74 ? 97  TRP D CB  1 
ATOM   5074 C  CG  . TRP D 1 100 ? 119.486 83.098  61.796  1.00 23.23 ? 97  TRP D CG  1 
ATOM   5075 C  CD1 . TRP D 1 100 ? 120.255 84.222  61.622  1.00 24.47 ? 97  TRP D CD1 1 
ATOM   5076 C  CD2 . TRP D 1 100 ? 120.385 81.972  61.699  1.00 23.98 ? 97  TRP D CD2 1 
ATOM   5077 N  NE1 . TRP D 1 100 ? 121.576 83.860  61.417  1.00 25.47 ? 97  TRP D NE1 1 
ATOM   5078 C  CE2 . TRP D 1 100 ? 121.683 82.489  61.467  1.00 24.74 ? 97  TRP D CE2 1 
ATOM   5079 C  CE3 . TRP D 1 100 ? 120.217 80.574  61.780  1.00 25.18 ? 97  TRP D CE3 1 
ATOM   5080 C  CZ2 . TRP D 1 100 ? 122.818 81.656  61.317  1.00 24.09 ? 97  TRP D CZ2 1 
ATOM   5081 C  CZ3 . TRP D 1 100 ? 121.356 79.736  61.623  1.00 24.48 ? 97  TRP D CZ3 1 
ATOM   5082 C  CH2 . TRP D 1 100 ? 122.637 80.294  61.399  1.00 24.17 ? 97  TRP D CH2 1 
ATOM   5083 N  N   . GLY D 1 101 ? 115.486 80.918  61.343  1.00 22.68 ? 98  GLY D N   1 
ATOM   5084 C  CA  . GLY D 1 101 ? 114.107 80.441  61.437  1.00 23.12 ? 98  GLY D CA  1 
ATOM   5085 C  C   . GLY D 1 101 ? 113.448 80.321  60.071  1.00 23.50 ? 98  GLY D C   1 
ATOM   5086 O  O   . GLY D 1 101 ? 112.215 80.245  59.956  1.00 22.98 ? 98  GLY D O   1 
ATOM   5087 N  N   . GLY D 1 102 ? 114.291 80.315  59.042  1.00 23.59 ? 99  GLY D N   1 
ATOM   5088 C  CA  . GLY D 1 102 ? 113.859 80.371  57.663  1.00 24.35 ? 99  GLY D CA  1 
ATOM   5089 C  C   . GLY D 1 102 ? 113.885 79.039  56.963  1.00 25.43 ? 99  GLY D C   1 
ATOM   5090 O  O   . GLY D 1 102 ? 113.549 78.966  55.788  1.00 26.60 ? 99  GLY D O   1 
ATOM   5091 N  N   . GLY D 1 103 ? 114.296 77.985  57.661  1.00 25.17 ? 100 GLY D N   1 
ATOM   5092 C  CA  . GLY D 1 103 ? 114.209 76.652  57.110  1.00 25.58 ? 100 GLY D CA  1 
ATOM   5093 C  C   . GLY D 1 103 ? 115.507 75.988  56.705  1.00 25.68 ? 100 GLY D C   1 
ATOM   5094 O  O   . GLY D 1 103 ? 115.480 75.010  55.933  1.00 24.58 ? 100 GLY D O   1 
ATOM   5095 N  N   . ASN D 1 104 ? 116.636 76.492  57.203  1.00 25.94 ? 101 ASN D N   1 
ATOM   5096 C  CA  . ASN D 1 104 ? 117.923 75.971  56.747  1.00 27.29 ? 101 ASN D CA  1 
ATOM   5097 C  C   . ASN D 1 104 ? 118.224 74.567  57.261  1.00 27.76 ? 101 ASN D C   1 
ATOM   5098 O  O   . ASN D 1 104 ? 118.872 73.777  56.553  1.00 28.24 ? 101 ASN D O   1 
ATOM   5099 C  CB  . ASN D 1 104 ? 119.110 76.936  56.968  1.00 27.17 ? 101 ASN D CB  1 
ATOM   5100 C  CG  . ASN D 1 104 ? 119.104 77.590  58.338  1.00 30.06 ? 101 ASN D CG  1 
ATOM   5101 O  OD1 . ASN D 1 104 ? 119.334 78.800  58.445  1.00 34.95 ? 101 ASN D OD1 1 
ATOM   5102 N  ND2 . ASN D 1 104 ? 118.854 76.812  59.392  1.00 29.10 ? 101 ASN D ND2 1 
ATOM   5103 N  N   . GLU D 1 105 ? 117.763 74.258  58.474  1.00 27.47 ? 102 GLU D N   1 
ATOM   5104 C  CA  . GLU D 1 105 ? 117.941 72.910  59.035  1.00 27.89 ? 102 GLU D CA  1 
ATOM   5105 C  C   . GLU D 1 105 ? 117.037 71.959  58.288  1.00 27.04 ? 102 GLU D C   1 
ATOM   5106 O  O   . GLU D 1 105 ? 117.412 70.829  58.055  1.00 27.70 ? 102 GLU D O   1 
ATOM   5107 C  CB  . GLU D 1 105 ? 117.599 72.846  60.534  1.00 28.00 ? 102 GLU D CB  1 
ATOM   5108 C  CG  . GLU D 1 105 ? 118.638 73.492  61.435  1.00 30.24 ? 102 GLU D CG  1 
ATOM   5109 C  CD  . GLU D 1 105 ? 118.131 73.728  62.840  1.00 32.15 ? 102 GLU D CD  1 
ATOM   5110 O  OE1 . GLU D 1 105 ? 116.937 73.479  63.098  1.00 34.32 ? 102 GLU D OE1 1 
ATOM   5111 O  OE2 . GLU D 1 105 ? 118.917 74.196  63.686  1.00 33.55 ? 102 GLU D OE2 1 
ATOM   5112 N  N   . VAL D 1 106 ? 115.837 72.416  57.943  1.00 25.92 ? 103 VAL D N   1 
ATOM   5113 C  CA  . VAL D 1 106 ? 114.919 71.615  57.170  1.00 25.48 ? 103 VAL D CA  1 
ATOM   5114 C  C   . VAL D 1 106 ? 115.491 71.355  55.761  1.00 25.59 ? 103 VAL D C   1 
ATOM   5115 O  O   . VAL D 1 106 ? 115.441 70.210  55.263  1.00 25.67 ? 103 VAL D O   1 
ATOM   5116 C  CB  . VAL D 1 106 ? 113.472 72.217  57.140  1.00 26.21 ? 103 VAL D CB  1 
ATOM   5117 C  CG1 . VAL D 1 106 ? 112.545 71.327  56.321  1.00 23.05 ? 103 VAL D CG1 1 
ATOM   5118 C  CG2 . VAL D 1 106 ? 112.917 72.409  58.554  1.00 23.97 ? 103 VAL D CG2 1 
ATOM   5119 N  N   . ALA D 1 107 ? 116.089 72.383  55.147  1.00 25.62 ? 104 ALA D N   1 
ATOM   5120 C  CA  . ALA D 1 107 ? 116.712 72.223  53.831  1.00 25.50 ? 104 ALA D CA  1 
ATOM   5121 C  C   . ALA D 1 107 ? 117.795 71.164  53.892  1.00 26.31 ? 104 ALA D C   1 
ATOM   5122 O  O   . ALA D 1 107 ? 117.905 70.323  52.997  1.00 27.29 ? 104 ALA D O   1 
ATOM   5123 C  CB  . ALA D 1 107 ? 117.267 73.554  53.296  1.00 24.70 ? 104 ALA D CB  1 
ATOM   5124 N  N   . CYS D 1 108 ? 118.600 71.215  54.943  1.00 26.93 ? 105 CYS D N   1 
ATOM   5125 C  CA  . CYS D 1 108 ? 119.606 70.204  55.226  1.00 27.92 ? 105 CYS D CA  1 
ATOM   5126 C  C   . CYS D 1 108 ? 119.036 68.798  55.362  1.00 28.19 ? 105 CYS D C   1 
ATOM   5127 O  O   . CYS D 1 108 ? 119.598 67.861  54.784  1.00 28.55 ? 105 CYS D O   1 
ATOM   5128 C  CB  . CYS D 1 108 ? 120.374 70.557  56.512  1.00 28.48 ? 105 CYS D CB  1 
ATOM   5129 S  SG  . CYS D 1 108 ? 121.611 71.809  56.271  1.00 27.66 ? 105 CYS D SG  1 
HETATM 5130 N  N   . MSE D 1 109 ? 117.978 68.653  56.161  1.00 28.37 ? 106 MSE D N   1 
HETATM 5131 C  CA  . MSE D 1 109 ? 117.215 67.398  56.283  1.00 29.83 ? 106 MSE D CA  1 
HETATM 5132 C  C   . MSE D 1 109 ? 116.796 66.859  54.937  1.00 28.58 ? 106 MSE D C   1 
HETATM 5133 O  O   . MSE D 1 109 ? 116.883 65.661  54.692  1.00 28.48 ? 106 MSE D O   1 
HETATM 5134 C  CB  . MSE D 1 109 ? 115.940 67.580  57.114  1.00 31.13 ? 106 MSE D CB  1 
HETATM 5135 C  CG  . MSE D 1 109 ? 116.104 67.476  58.615  1.00 41.56 ? 106 MSE D CG  1 
HETATM 5136 SE SE  . MSE D 1 109 ? 117.139 65.855  59.311  1.00 63.15 ? 106 MSE D SE  1 
HETATM 5137 C  CE  . MSE D 1 109 ? 116.545 64.491  58.118  1.00 48.46 ? 106 MSE D CE  1 
ATOM   5138 N  N   . SER D 1 110 ? 116.327 67.741  54.057  1.00 27.37 ? 107 SER D N   1 
ATOM   5139 C  CA  . SER D 1 110 ? 115.894 67.306  52.720  1.00 25.50 ? 107 SER D CA  1 
ATOM   5140 C  C   . SER D 1 110 ? 117.069 66.784  51.872  1.00 25.01 ? 107 SER D C   1 
ATOM   5141 O  O   . SER D 1 110 ? 116.927 65.822  51.127  1.00 24.99 ? 107 SER D O   1 
ATOM   5142 C  CB  . SER D 1 110 ? 115.094 68.409  52.021  1.00 24.67 ? 107 SER D CB  1 
ATOM   5143 O  OG  . SER D 1 110 ? 115.934 69.411  51.463  1.00 22.93 ? 107 SER D OG  1 
ATOM   5144 N  N   . ILE D 1 111 ? 118.231 67.413  52.008  1.00 25.08 ? 108 ILE D N   1 
ATOM   5145 C  CA  . ILE D 1 111 ? 119.475 66.923  51.398  1.00 24.73 ? 108 ILE D CA  1 
ATOM   5146 C  C   . ILE D 1 111 ? 119.889 65.531  51.933  1.00 24.96 ? 108 ILE D C   1 
ATOM   5147 O  O   . ILE D 1 111 ? 120.255 64.652  51.176  1.00 24.27 ? 108 ILE D O   1 
ATOM   5148 C  CB  . ILE D 1 111 ? 120.646 67.945  51.554  1.00 24.38 ? 108 ILE D CB  1 
ATOM   5149 C  CG1 . ILE D 1 111 ? 120.335 69.254  50.813  1.00 24.94 ? 108 ILE D CG1 1 
ATOM   5150 C  CG2 . ILE D 1 111 ? 121.943 67.399  50.968  1.00 22.85 ? 108 ILE D CG2 1 
ATOM   5151 C  CD1 . ILE D 1 111 ? 121.108 70.529  51.353  1.00 25.25 ? 108 ILE D CD1 1 
ATOM   5152 N  N   . LEU D 1 112 ? 119.825 65.357  53.246  1.00 25.67 ? 109 LEU D N   1 
ATOM   5153 C  CA  . LEU D 1 112 ? 120.168 64.095  53.909  1.00 25.50 ? 109 LEU D CA  1 
ATOM   5154 C  C   . LEU D 1 112 ? 119.195 62.988  53.480  1.00 25.33 ? 109 LEU D C   1 
ATOM   5155 O  O   . LEU D 1 112 ? 119.577 61.836  53.287  1.00 24.60 ? 109 LEU D O   1 
ATOM   5156 C  CB  . LEU D 1 112 ? 120.174 64.276  55.445  1.00 24.68 ? 109 LEU D CB  1 
ATOM   5157 C  CG  . LEU D 1 112 ? 121.305 65.182  56.000  1.00 25.31 ? 109 LEU D CG  1 
ATOM   5158 C  CD1 . LEU D 1 112 ? 121.175 65.454  57.504  1.00 21.59 ? 109 LEU D CD1 1 
ATOM   5159 C  CD2 . LEU D 1 112 ? 122.724 64.687  55.689  1.00 22.71 ? 109 LEU D CD2 1 
ATOM   5160 N  N   . THR D 1 113 ? 117.937 63.355  53.330  1.00 25.65 ? 110 THR D N   1 
ATOM   5161 C  CA  . THR D 1 113 ? 116.923 62.437  52.870  1.00 26.74 ? 110 THR D CA  1 
ATOM   5162 C  C   . THR D 1 113 ? 117.260 61.843  51.501  1.00 27.89 ? 110 THR D C   1 
ATOM   5163 O  O   . THR D 1 113 ? 117.182 60.617  51.305  1.00 28.05 ? 110 THR D O   1 
ATOM   5164 C  CB  . THR D 1 113 ? 115.583 63.151  52.857  1.00 26.09 ? 110 THR D CB  1 
ATOM   5165 O  OG1 . THR D 1 113 ? 115.168 63.236  54.209  1.00 27.54 ? 110 THR D OG1 1 
ATOM   5166 C  CG2 . THR D 1 113 ? 114.529 62.365  52.063  1.00 26.69 ? 110 THR D CG2 1 
HETATM 5167 N  N   . MSE D 1 114 ? 117.648 62.733  50.594  1.00 28.51 ? 111 MSE D N   1 
HETATM 5168 C  CA  . MSE D 1 114 ? 118.052 62.429  49.257  1.00 31.91 ? 111 MSE D CA  1 
HETATM 5169 C  C   . MSE D 1 114 ? 119.280 61.546  49.239  1.00 30.23 ? 111 MSE D C   1 
HETATM 5170 O  O   . MSE D 1 114 ? 119.296 60.543  48.548  1.00 30.18 ? 111 MSE D O   1 
HETATM 5171 C  CB  . MSE D 1 114 ? 118.381 63.744  48.575  1.00 31.25 ? 111 MSE D CB  1 
HETATM 5172 C  CG  . MSE D 1 114 ? 118.421 63.708  47.094  1.00 33.72 ? 111 MSE D CG  1 
HETATM 5173 SE SE  . MSE D 1 114 ? 118.570 65.573  46.398  1.00 41.76 ? 111 MSE D SE  1 
HETATM 5174 C  CE  . MSE D 1 114 ? 120.375 66.127  47.239  1.00 32.32 ? 111 MSE D CE  1 
ATOM   5175 N  N   . LEU D 1 115 ? 120.304 61.937  49.999  1.00 30.20 ? 112 LEU D N   1 
ATOM   5176 C  CA  . LEU D 1 115 ? 121.533 61.152  50.175  1.00 29.88 ? 112 LEU D CA  1 
ATOM   5177 C  C   . LEU D 1 115 ? 121.293 59.767  50.793  1.00 30.12 ? 112 LEU D C   1 
ATOM   5178 O  O   . LEU D 1 115 ? 121.862 58.784  50.339  1.00 29.47 ? 112 LEU D O   1 
ATOM   5179 C  CB  . LEU D 1 115 ? 122.568 61.932  50.986  1.00 29.01 ? 112 LEU D CB  1 
ATOM   5180 C  CG  . LEU D 1 115 ? 123.043 63.250  50.357  1.00 28.96 ? 112 LEU D CG  1 
ATOM   5181 C  CD1 . LEU D 1 115 ? 123.735 64.099  51.431  1.00 24.55 ? 112 LEU D CD1 1 
ATOM   5182 C  CD2 . LEU D 1 115 ? 123.957 63.022  49.118  1.00 26.41 ? 112 LEU D CD2 1 
HETATM 5183 N  N   . MSE D 1 116 ? 120.427 59.685  51.795  1.00 29.99 ? 113 MSE D N   1 
HETATM 5184 C  CA  . MSE D 1 116 ? 120.079 58.395  52.363  1.00 32.85 ? 113 MSE D CA  1 
HETATM 5185 C  C   . MSE D 1 116 ? 119.419 57.477  51.370  1.00 29.96 ? 113 MSE D C   1 
HETATM 5186 O  O   . MSE D 1 116 ? 119.606 56.273  51.413  1.00 30.11 ? 113 MSE D O   1 
HETATM 5187 C  CB  . MSE D 1 116 ? 119.152 58.550  53.543  1.00 31.01 ? 113 MSE D CB  1 
HETATM 5188 C  CG  . MSE D 1 116 ? 119.893 58.810  54.792  1.00 35.76 ? 113 MSE D CG  1 
HETATM 5189 SE SE  . MSE D 1 116 ? 118.721 58.879  56.361  1.00 45.77 ? 113 MSE D SE  1 
HETATM 5190 C  CE  . MSE D 1 116 ? 117.700 60.510  55.990  1.00 39.16 ? 113 MSE D CE  1 
ATOM   5191 N  N   . ASN D 1 117 ? 118.616 58.048  50.491  1.00 28.72 ? 114 ASN D N   1 
ATOM   5192 C  CA  . ASN D 1 117 ? 117.958 57.270  49.474  1.00 27.41 ? 114 ASN D CA  1 
ATOM   5193 C  C   . ASN D 1 117 ? 118.962 56.574  48.562  1.00 26.34 ? 114 ASN D C   1 
ATOM   5194 O  O   . ASN D 1 117 ? 118.668 55.517  48.061  1.00 26.19 ? 114 ASN D O   1 
ATOM   5195 C  CB  . ASN D 1 117 ? 117.004 58.151  48.681  1.00 27.52 ? 114 ASN D CB  1 
ATOM   5196 C  CG  . ASN D 1 117 ? 115.805 57.412  48.239  1.00 28.31 ? 114 ASN D CG  1 
ATOM   5197 O  OD1 . ASN D 1 117 ? 115.801 56.780  47.174  1.00 33.54 ? 114 ASN D OD1 1 
ATOM   5198 N  ND2 . ASN D 1 117 ? 114.748 57.472  49.045  1.00 31.11 ? 114 ASN D ND2 1 
ATOM   5199 N  N   . PHE D 1 118 ? 120.151 57.158  48.383  1.00 26.00 ? 115 PHE D N   1 
ATOM   5200 C  CA  . PHE D 1 118 ? 121.273 56.486  47.673  1.00 26.01 ? 115 PHE D CA  1 
ATOM   5201 C  C   . PHE D 1 118 ? 122.071 55.432  48.470  1.00 25.43 ? 115 PHE D C   1 
ATOM   5202 O  O   . PHE D 1 118 ? 123.018 54.832  47.940  1.00 24.33 ? 115 PHE D O   1 
ATOM   5203 C  CB  . PHE D 1 118 ? 122.234 57.519  47.069  1.00 26.21 ? 115 PHE D CB  1 
ATOM   5204 C  CG  . PHE D 1 118 ? 121.772 58.055  45.754  1.00 27.42 ? 115 PHE D CG  1 
ATOM   5205 C  CD1 . PHE D 1 118 ? 120.977 59.207  45.697  1.00 28.71 ? 115 PHE D CD1 1 
ATOM   5206 C  CD2 . PHE D 1 118 ? 122.091 57.378  44.559  1.00 25.24 ? 115 PHE D CD2 1 
ATOM   5207 C  CE1 . PHE D 1 118 ? 120.511 59.689  44.458  1.00 30.03 ? 115 PHE D CE1 1 
ATOM   5208 C  CE2 . PHE D 1 118 ? 121.657 57.857  43.333  1.00 23.72 ? 115 PHE D CE2 1 
ATOM   5209 C  CZ  . PHE D 1 118 ? 120.878 59.014  43.270  1.00 26.14 ? 115 PHE D CZ  1 
ATOM   5210 N  N   . GLY D 1 119 ? 121.690 55.229  49.735  1.00 24.80 ? 116 GLY D N   1 
ATOM   5211 C  CA  . GLY D 1 119 ? 122.291 54.213  50.584  1.00 25.16 ? 116 GLY D CA  1 
ATOM   5212 C  C   . GLY D 1 119 ? 123.526 54.731  51.305  1.00 25.76 ? 116 GLY D C   1 
ATOM   5213 O  O   . GLY D 1 119 ? 124.297 53.944  51.900  1.00 26.50 ? 116 GLY D O   1 
ATOM   5214 N  N   . PHE D 1 120 ? 123.737 56.045  51.230  1.00 25.16 ? 117 PHE D N   1 
ATOM   5215 C  CA  . PHE D 1 120 ? 124.838 56.689  51.931  1.00 25.27 ? 117 PHE D CA  1 
ATOM   5216 C  C   . PHE D 1 120 ? 124.642 56.669  53.436  1.00 25.47 ? 117 PHE D C   1 
ATOM   5217 O  O   . PHE D 1 120 ? 123.498 56.624  53.940  1.00 24.98 ? 117 PHE D O   1 
ATOM   5218 C  CB  . PHE D 1 120 ? 125.023 58.135  51.476  1.00 25.35 ? 117 PHE D CB  1 
ATOM   5219 C  CG  . PHE D 1 120 ? 125.317 58.286  50.023  1.00 25.79 ? 117 PHE D CG  1 
ATOM   5220 C  CD1 . PHE D 1 120 ? 125.547 57.163  49.206  1.00 27.27 ? 117 PHE D CD1 1 
ATOM   5221 C  CD2 . PHE D 1 120 ? 125.419 59.556  49.462  1.00 26.41 ? 117 PHE D CD2 1 
ATOM   5222 C  CE1 . PHE D 1 120 ? 125.861 57.313  47.852  1.00 26.65 ? 117 PHE D CE1 1 
ATOM   5223 C  CE2 . PHE D 1 120 ? 125.742 59.729  48.101  1.00 25.96 ? 117 PHE D CE2 1 
ATOM   5224 C  CZ  . PHE D 1 120 ? 125.949 58.606  47.298  1.00 26.60 ? 117 PHE D CZ  1 
ATOM   5225 N  N   . LEU D 1 121 ? 125.780 56.658  54.137  1.00 25.94 ? 118 LEU D N   1 
ATOM   5226 C  CA  . LEU D 1 121 ? 125.826 56.863  55.576  1.00 26.23 ? 118 LEU D CA  1 
ATOM   5227 C  C   . LEU D 1 121 ? 125.979 58.378  55.756  1.00 26.54 ? 118 LEU D C   1 
ATOM   5228 O  O   . LEU D 1 121 ? 126.882 59.032  55.179  1.00 25.99 ? 118 LEU D O   1 
ATOM   5229 C  CB  . LEU D 1 121 ? 127.001 56.130  56.229  1.00 26.11 ? 118 LEU D CB  1 
ATOM   5230 C  CG  . LEU D 1 121 ? 127.350 54.635  56.190  1.00 27.68 ? 118 LEU D CG  1 
ATOM   5231 C  CD1 . LEU D 1 121 ? 127.197 53.975  57.551  1.00 27.81 ? 118 LEU D CD1 1 
ATOM   5232 C  CD2 . LEU D 1 121 ? 126.652 53.809  55.070  1.00 26.80 ? 118 LEU D CD2 1 
ATOM   5233 N  N   . VAL D 1 122 ? 125.102 58.907  56.597  1.00 26.39 ? 119 VAL D N   1 
ATOM   5234 C  CA  . VAL D 1 122 ? 124.777 60.315  56.643  1.00 26.08 ? 119 VAL D CA  1 
ATOM   5235 C  C   . VAL D 1 122 ? 124.981 60.822  58.104  1.00 25.70 ? 119 VAL D C   1 
ATOM   5236 O  O   . VAL D 1 122 ? 124.741 60.094  59.056  1.00 25.07 ? 119 VAL D O   1 
ATOM   5237 C  CB  . VAL D 1 122 ? 123.325 60.443  56.009  1.00 26.83 ? 119 VAL D CB  1 
ATOM   5238 C  CG1 . VAL D 1 122 ? 122.213 60.986  56.941  1.00 24.17 ? 119 VAL D CG1 1 
ATOM   5239 C  CG2 . VAL D 1 122 ? 123.357 61.033  54.597  1.00 27.42 ? 119 VAL D CG2 1 
ATOM   5240 N  N   . PHE D 1 123 ? 125.459 62.049  58.271  1.00 25.03 ? 120 PHE D N   1 
ATOM   5241 C  CA  . PHE D 1 123 ? 125.688 62.586  59.617  1.00 25.03 ? 120 PHE D CA  1 
ATOM   5242 C  C   . PHE D 1 123 ? 125.506 64.125  59.754  1.00 25.19 ? 120 PHE D C   1 
ATOM   5243 O  O   . PHE D 1 123 ? 125.455 64.863  58.768  1.00 24.56 ? 120 PHE D O   1 
ATOM   5244 C  CB  . PHE D 1 123 ? 127.102 62.190  60.107  1.00 24.05 ? 120 PHE D CB  1 
ATOM   5245 C  CG  . PHE D 1 123 ? 128.189 62.858  59.341  1.00 23.14 ? 120 PHE D CG  1 
ATOM   5246 C  CD1 . PHE D 1 123 ? 128.549 62.401  58.064  1.00 21.67 ? 120 PHE D CD1 1 
ATOM   5247 C  CD2 . PHE D 1 123 ? 128.832 63.977  59.862  1.00 21.07 ? 120 PHE D CD2 1 
ATOM   5248 C  CE1 . PHE D 1 123 ? 129.524 63.064  57.332  1.00 18.87 ? 120 PHE D CE1 1 
ATOM   5249 C  CE2 . PHE D 1 123 ? 129.807 64.623  59.131  1.00 19.50 ? 120 PHE D CE2 1 
ATOM   5250 C  CZ  . PHE D 1 123 ? 130.152 64.159  57.870  1.00 18.74 ? 120 PHE D CZ  1 
ATOM   5251 N  N   . GLY D 1 124 ? 125.384 64.574  61.005  1.00 25.81 ? 121 GLY D N   1 
ATOM   5252 C  CA  . GLY D 1 124 ? 125.671 65.965  61.382  1.00 25.99 ? 121 GLY D CA  1 
ATOM   5253 C  C   . GLY D 1 124 ? 126.780 66.063  62.436  1.00 26.35 ? 121 GLY D C   1 
ATOM   5254 O  O   . GLY D 1 124 ? 127.426 65.067  62.781  1.00 26.69 ? 121 GLY D O   1 
ATOM   5255 N  N   . VAL D 1 125 ? 127.017 67.270  62.949  1.00 26.43 ? 122 VAL D N   1 
ATOM   5256 C  CA  . VAL D 1 125 ? 128.137 67.494  63.836  1.00 26.29 ? 122 VAL D CA  1 
ATOM   5257 C  C   . VAL D 1 125 ? 127.631 68.040  65.159  1.00 27.03 ? 122 VAL D C   1 
ATOM   5258 O  O   . VAL D 1 125 ? 126.826 68.972  65.194  1.00 27.30 ? 122 VAL D O   1 
ATOM   5259 C  CB  . VAL D 1 125 ? 129.208 68.413  63.185  1.00 26.75 ? 122 VAL D CB  1 
ATOM   5260 C  CG1 . VAL D 1 125 ? 130.321 68.726  64.171  1.00 25.56 ? 122 VAL D CG1 1 
ATOM   5261 C  CG2 . VAL D 1 125 ? 129.785 67.766  61.901  1.00 23.25 ? 122 VAL D CG2 1 
ATOM   5262 N  N   . THR D 1 126 ? 128.068 67.412  66.248  1.00 27.54 ? 123 THR D N   1 
ATOM   5263 C  CA  . THR D 1 126 ? 127.708 67.848  67.610  1.00 27.61 ? 123 THR D CA  1 
ATOM   5264 C  C   . THR D 1 126 ? 128.473 69.112  68.071  1.00 27.72 ? 123 THR D C   1 
ATOM   5265 O  O   . THR D 1 126 ? 127.920 69.947  68.816  1.00 27.39 ? 123 THR D O   1 
ATOM   5266 C  CB  . THR D 1 126 ? 127.960 66.732  68.611  1.00 27.07 ? 123 THR D CB  1 
ATOM   5267 O  OG1 . THR D 1 126 ? 129.294 66.259  68.437  1.00 29.38 ? 123 THR D OG1 1 
ATOM   5268 C  CG2 . THR D 1 126 ? 127.041 65.594  68.378  1.00 26.52 ? 123 THR D CG2 1 
ATOM   5269 N  N   . ASP D 1 127 ? 129.739 69.219  67.636  1.00 27.47 ? 124 ASP D N   1 
ATOM   5270 C  CA  . ASP D 1 127 ? 130.643 70.333  67.969  1.00 27.84 ? 124 ASP D CA  1 
ATOM   5271 C  C   . ASP D 1 127 ? 129.937 71.662  68.107  1.00 28.08 ? 124 ASP D C   1 
ATOM   5272 O  O   . ASP D 1 127 ? 129.126 72.040  67.235  1.00 28.86 ? 124 ASP D O   1 
ATOM   5273 C  CB  . ASP D 1 127 ? 131.734 70.514  66.898  1.00 27.72 ? 124 ASP D CB  1 
ATOM   5274 C  CG  . ASP D 1 127 ? 132.642 69.294  66.762  1.00 28.28 ? 124 ASP D CG  1 
ATOM   5275 O  OD1 . ASP D 1 127 ? 132.159 68.149  67.028  1.00 23.25 ? 124 ASP D OD1 1 
ATOM   5276 O  OD2 . ASP D 1 127 ? 133.835 69.513  66.390  1.00 27.37 ? 124 ASP D OD2 1 
ATOM   5277 N  N   . TYR D 1 128 ? 130.226 72.357  69.201  1.00 27.22 ? 125 TYR D N   1 
ATOM   5278 C  CA  . TYR D 1 128 ? 129.867 73.749  69.312  1.00 27.45 ? 125 TYR D CA  1 
ATOM   5279 C  C   . TYR D 1 128 ? 131.066 74.627  68.930  1.00 28.08 ? 125 TYR D C   1 
ATOM   5280 O  O   . TYR D 1 128 ? 132.173 74.517  69.462  1.00 28.16 ? 125 TYR D O   1 
ATOM   5281 C  CB  . TYR D 1 128 ? 129.363 74.086  70.709  1.00 27.35 ? 125 TYR D CB  1 
ATOM   5282 C  CG  . TYR D 1 128 ? 127.875 73.927  70.876  1.00 26.57 ? 125 TYR D CG  1 
ATOM   5283 C  CD1 . TYR D 1 128 ? 127.251 72.688  70.683  1.00 25.17 ? 125 TYR D CD1 1 
ATOM   5284 C  CD2 . TYR D 1 128 ? 127.082 75.018  71.244  1.00 26.14 ? 125 TYR D CD2 1 
ATOM   5285 C  CE1 . TYR D 1 128 ? 125.878 72.544  70.851  1.00 24.26 ? 125 TYR D CE1 1 
ATOM   5286 C  CE2 . TYR D 1 128 ? 125.706 74.880  71.407  1.00 25.61 ? 125 TYR D CE2 1 
ATOM   5287 C  CZ  . TYR D 1 128 ? 125.118 73.643  71.213  1.00 25.55 ? 125 TYR D CZ  1 
ATOM   5288 O  OH  . TYR D 1 128 ? 123.767 73.516  71.379  1.00 26.60 ? 125 TYR D OH  1 
ATOM   5289 N  N   . VAL D 1 129 ? 130.787 75.527  68.011  1.00 28.67 ? 126 VAL D N   1 
ATOM   5290 C  CA  . VAL D 1 129 ? 131.768 76.282  67.291  1.00 28.86 ? 126 VAL D CA  1 
ATOM   5291 C  C   . VAL D 1 129 ? 131.720 77.775  67.745  1.00 29.55 ? 126 VAL D C   1 
ATOM   5292 O  O   . VAL D 1 129 ? 132.673 78.533  67.545  1.00 30.30 ? 126 VAL D O   1 
ATOM   5293 C  CB  . VAL D 1 129 ? 131.553 75.928  65.793  1.00 28.95 ? 126 VAL D CB  1 
ATOM   5294 C  CG1 . VAL D 1 129 ? 131.049 77.061  64.927  1.00 28.31 ? 126 VAL D CG1 1 
ATOM   5295 C  CG2 . VAL D 1 129 ? 132.725 75.105  65.253  1.00 27.84 ? 126 VAL D CG2 1 
ATOM   5296 N  N   . GLY D 1 130 ? 130.617 78.141  68.402  1.00 29.98 ? 127 GLY D N   1 
ATOM   5297 C  CA  . GLY D 1 130 ? 130.477 79.334  69.223  1.00 30.02 ? 127 GLY D CA  1 
ATOM   5298 C  C   . GLY D 1 130 ? 129.588 78.948  70.408  1.00 31.37 ? 127 GLY D C   1 
ATOM   5299 O  O   . GLY D 1 130 ? 129.120 77.798  70.512  1.00 31.55 ? 127 GLY D O   1 
ATOM   5300 N  N   . LYS D 1 131 ? 129.338 79.902  71.299  1.00 32.13 ? 128 LYS D N   1 
ATOM   5301 C  CA  . LYS D 1 131 ? 128.537 79.655  72.500  1.00 33.22 ? 128 LYS D CA  1 
ATOM   5302 C  C   . LYS D 1 131 ? 127.166 79.069  72.161  1.00 33.05 ? 128 LYS D C   1 
ATOM   5303 O  O   . LYS D 1 131 ? 126.740 78.093  72.783  1.00 33.98 ? 128 LYS D O   1 
ATOM   5304 C  CB  . LYS D 1 131 ? 128.359 80.937  73.326  1.00 33.16 ? 128 LYS D CB  1 
ATOM   5305 C  CG  . LYS D 1 131 ? 129.409 81.159  74.405  1.00 36.51 ? 128 LYS D CG  1 
ATOM   5306 C  CD  . LYS D 1 131 ? 129.060 80.394  75.703  1.00 42.07 ? 128 LYS D CD  1 
ATOM   5307 C  CE  . LYS D 1 131 ? 127.921 81.069  76.519  1.00 43.82 ? 128 LYS D CE  1 
ATOM   5308 N  NZ  . LYS D 1 131 ? 128.368 82.290  77.285  1.00 45.51 ? 128 LYS D NZ  1 
ATOM   5309 N  N   . LYS D 1 132 ? 126.465 79.685  71.210  1.00 32.05 ? 129 LYS D N   1 
ATOM   5310 C  CA  . LYS D 1 132 ? 125.138 79.206  70.796  1.00 31.03 ? 129 LYS D CA  1 
ATOM   5311 C  C   . LYS D 1 132 ? 125.179 78.931  69.288  1.00 29.33 ? 129 LYS D C   1 
ATOM   5312 O  O   . LYS D 1 132 ? 124.306 79.350  68.539  1.00 29.09 ? 129 LYS D O   1 
ATOM   5313 C  CB  . LYS D 1 132 ? 124.004 80.193  71.186  1.00 31.69 ? 129 LYS D CB  1 
ATOM   5314 C  CG  . LYS D 1 132 ? 124.014 80.693  72.635  1.00 32.52 ? 129 LYS D CG  1 
ATOM   5315 C  CD  . LYS D 1 132 ? 122.630 80.521  73.340  1.00 36.49 ? 129 LYS D CD  1 
ATOM   5316 C  CE  . LYS D 1 132 ? 122.460 81.323  74.684  1.00 36.46 ? 129 LYS D CE  1 
ATOM   5317 N  NZ  . LYS D 1 132 ? 123.640 81.382  75.659  1.00 37.54 ? 129 LYS D NZ  1 
ATOM   5318 N  N   . PHE D 1 133 ? 126.212 78.220  68.854  1.00 27.64 ? 130 PHE D N   1 
ATOM   5319 C  CA  . PHE D 1 133 ? 126.368 77.948  67.449  1.00 26.80 ? 130 PHE D CA  1 
ATOM   5320 C  C   . PHE D 1 133 ? 126.878 76.547  67.097  1.00 26.67 ? 130 PHE D C   1 
ATOM   5321 O  O   . PHE D 1 133 ? 127.976 76.138  67.460  1.00 26.78 ? 130 PHE D O   1 
ATOM   5322 C  CB  . PHE D 1 133 ? 127.201 79.028  66.767  1.00 26.28 ? 130 PHE D CB  1 
ATOM   5323 C  CG  . PHE D 1 133 ? 126.867 79.195  65.316  1.00 26.17 ? 130 PHE D CG  1 
ATOM   5324 C  CD1 . PHE D 1 133 ? 127.529 78.428  64.337  1.00 25.09 ? 130 PHE D CD1 1 
ATOM   5325 C  CD2 . PHE D 1 133 ? 125.874 80.086  64.921  1.00 24.92 ? 130 PHE D CD2 1 
ATOM   5326 C  CE1 . PHE D 1 133 ? 127.253 78.580  62.970  1.00 24.02 ? 130 PHE D CE1 1 
ATOM   5327 C  CE2 . PHE D 1 133 ? 125.557 80.233  63.560  1.00 26.78 ? 130 PHE D CE2 1 
ATOM   5328 C  CZ  . PHE D 1 133 ? 126.254 79.471  62.571  1.00 26.50 ? 130 PHE D CZ  1 
ATOM   5329 N  N   . THR D 1 134 ? 126.068 75.817  66.349  1.00 26.74 ? 131 THR D N   1 
ATOM   5330 C  CA  . THR D 1 134 ? 126.385 74.423  66.070  1.00 26.14 ? 131 THR D CA  1 
ATOM   5331 C  C   . THR D 1 134 ? 125.906 73.978  64.681  1.00 26.21 ? 131 THR D C   1 
ATOM   5332 O  O   . THR D 1 134 ? 125.497 74.820  63.875  1.00 26.25 ? 131 THR D O   1 
ATOM   5333 C  CB  . THR D 1 134 ? 125.913 73.509  67.251  1.00 25.76 ? 131 THR D CB  1 
ATOM   5334 O  OG1 . THR D 1 134 ? 126.444 72.198  67.069  1.00 26.12 ? 131 THR D OG1 1 
ATOM   5335 C  CG2 . THR D 1 134 ? 124.389 73.485  67.395  1.00 23.78 ? 131 THR D CG2 1 
ATOM   5336 N  N   . LEU D 1 135 ? 125.958 72.675  64.399  1.00 26.30 ? 132 LEU D N   1 
ATOM   5337 C  CA  . LEU D 1 135 ? 125.724 72.170  63.043  1.00 26.26 ? 132 LEU D CA  1 
ATOM   5338 C  C   . LEU D 1 135 ? 125.279 70.700  63.021  1.00 26.91 ? 132 LEU D C   1 
ATOM   5339 O  O   . LEU D 1 135 ? 125.830 69.845  62.295  1.00 26.87 ? 132 LEU D O   1 
ATOM   5340 C  CB  . LEU D 1 135 ? 126.917 72.466  62.113  1.00 26.03 ? 132 LEU D CB  1 
ATOM   5341 C  CG  . LEU D 1 135 ? 128.453 72.472  62.355  1.00 27.54 ? 132 LEU D CG  1 
ATOM   5342 C  CD1 . LEU D 1 135 ? 128.950 72.521  63.815  1.00 26.87 ? 132 LEU D CD1 1 
ATOM   5343 C  CD2 . LEU D 1 135 ? 129.164 71.364  61.573  1.00 25.74 ? 132 LEU D CD2 1 
ATOM   5344 N  N   . HIS D 1 136 ? 124.240 70.448  63.811  1.00 26.78 ? 133 HIS D N   1 
ATOM   5345 C  CA  . HIS D 1 136 ? 123.775 69.130  64.160  1.00 26.81 ? 133 HIS D CA  1 
ATOM   5346 C  C   . HIS D 1 136 ? 123.218 68.356  62.959  1.00 27.72 ? 133 HIS D C   1 
ATOM   5347 O  O   . HIS D 1 136 ? 123.364 67.145  62.920  1.00 28.20 ? 133 HIS D O   1 
ATOM   5348 C  CB  . HIS D 1 136 ? 122.704 69.216  65.279  1.00 26.24 ? 133 HIS D CB  1 
ATOM   5349 C  CG  . HIS D 1 136 ? 123.228 69.572  66.652  1.00 25.10 ? 133 HIS D CG  1 
ATOM   5350 N  ND1 . HIS D 1 136 ? 124.570 69.544  66.993  1.00 25.02 ? 133 HIS D ND1 1 
ATOM   5351 C  CD2 . HIS D 1 136 ? 122.567 69.922  67.784  1.00 22.08 ? 133 HIS D CD2 1 
ATOM   5352 C  CE1 . HIS D 1 136 ? 124.709 69.891  68.260  1.00 22.73 ? 133 HIS D CE1 1 
ATOM   5353 N  NE2 . HIS D 1 136 ? 123.506 70.110  68.766  1.00 22.77 ? 133 HIS D NE2 1 
ATOM   5354 N  N   . TYR D 1 137 ? 122.569 69.039  62.005  1.00 27.66 ? 134 TYR D N   1 
ATOM   5355 C  CA  . TYR D 1 137 ? 122.076 68.402  60.768  1.00 27.58 ? 134 TYR D CA  1 
ATOM   5356 C  C   . TYR D 1 137 ? 122.874 68.859  59.552  1.00 27.62 ? 134 TYR D C   1 
ATOM   5357 O  O   . TYR D 1 137 ? 122.545 68.510  58.424  1.00 28.54 ? 134 TYR D O   1 
ATOM   5358 C  CB  . TYR D 1 137 ? 120.519 68.579  60.593  1.00 28.29 ? 134 TYR D CB  1 
ATOM   5359 C  CG  . TYR D 1 137 ? 119.863 68.105  61.859  1.00 27.81 ? 134 TYR D CG  1 
ATOM   5360 C  CD1 . TYR D 1 137 ? 119.428 69.002  62.837  1.00 29.24 ? 134 TYR D CD1 1 
ATOM   5361 C  CD2 . TYR D 1 137 ? 119.834 66.759  62.148  1.00 27.70 ? 134 TYR D CD2 1 
ATOM   5362 C  CE1 . TYR D 1 137 ? 118.949 68.528  64.070  1.00 30.13 ? 134 TYR D CE1 1 
ATOM   5363 C  CE2 . TYR D 1 137 ? 119.348 66.281  63.338  1.00 29.12 ? 134 TYR D CE2 1 
ATOM   5364 C  CZ  . TYR D 1 137 ? 118.908 67.155  64.293  1.00 29.72 ? 134 TYR D CZ  1 
ATOM   5365 O  OH  . TYR D 1 137 ? 118.445 66.612  65.461  1.00 30.71 ? 134 TYR D OH  1 
ATOM   5366 N  N   . GLY D 1 138 ? 123.940 69.621  59.783  1.00 26.89 ? 135 GLY D N   1 
ATOM   5367 C  CA  . GLY D 1 138 ? 124.753 70.161  58.699  1.00 25.43 ? 135 GLY D CA  1 
ATOM   5368 C  C   . GLY D 1 138 ? 125.048 71.620  58.980  1.00 24.73 ? 135 GLY D C   1 
ATOM   5369 O  O   . GLY D 1 138 ? 124.513 72.187  59.905  1.00 24.03 ? 135 GLY D O   1 
ATOM   5370 N  N   . ALA D 1 139 ? 125.891 72.244  58.179  1.00 24.80 ? 136 ALA D N   1 
ATOM   5371 C  CA  . ALA D 1 139 ? 126.236 73.629  58.449  1.00 24.67 ? 136 ALA D CA  1 
ATOM   5372 C  C   . ALA D 1 139 ? 125.127 74.494  57.895  1.00 24.80 ? 136 ALA D C   1 
ATOM   5373 O  O   . ALA D 1 139 ? 124.655 74.279  56.754  1.00 24.86 ? 136 ALA D O   1 
ATOM   5374 C  CB  . ALA D 1 139 ? 127.603 73.992  57.866  1.00 23.86 ? 136 ALA D CB  1 
ATOM   5375 N  N   . VAL D 1 140 ? 124.670 75.435  58.722  1.00 24.82 ? 137 VAL D N   1 
ATOM   5376 C  CA  . VAL D 1 140 ? 123.619 76.352  58.321  1.00 25.02 ? 137 VAL D CA  1 
ATOM   5377 C  C   . VAL D 1 140 ? 124.023 77.789  58.601  1.00 26.39 ? 137 VAL D C   1 
ATOM   5378 O  O   . VAL D 1 140 ? 124.724 78.064  59.584  1.00 27.16 ? 137 VAL D O   1 
ATOM   5379 C  CB  . VAL D 1 140 ? 122.228 75.983  58.933  1.00 25.15 ? 137 VAL D CB  1 
ATOM   5380 C  CG1 . VAL D 1 140 ? 121.754 74.707  58.364  1.00 21.95 ? 137 VAL D CG1 1 
ATOM   5381 C  CG2 . VAL D 1 140 ? 122.252 75.903  60.475  1.00 24.46 ? 137 VAL D CG2 1 
ATOM   5382 N  N   . VAL D 1 141 ? 123.634 78.687  57.691  1.00 27.33 ? 138 VAL D N   1 
ATOM   5383 C  CA  . VAL D 1 141 ? 123.847 80.138  57.833  1.00 27.85 ? 138 VAL D CA  1 
ATOM   5384 C  C   . VAL D 1 141 ? 122.677 80.911  57.181  1.00 27.78 ? 138 VAL D C   1 
ATOM   5385 O  O   . VAL D 1 141 ? 122.143 80.508  56.153  1.00 26.66 ? 138 VAL D O   1 
ATOM   5386 C  CB  . VAL D 1 141 ? 125.218 80.642  57.213  1.00 28.46 ? 138 VAL D CB  1 
ATOM   5387 C  CG1 . VAL D 1 141 ? 125.478 82.139  57.598  1.00 28.73 ? 138 VAL D CG1 1 
ATOM   5388 C  CG2 . VAL D 1 141 ? 126.409 79.802  57.692  1.00 29.65 ? 138 VAL D CG2 1 
ATOM   5389 N  N   . ALA D 1 142 ? 122.284 82.031  57.779  1.00 28.29 ? 139 ALA D N   1 
ATOM   5390 C  CA  . ALA D 1 142 ? 121.431 82.975  57.060  1.00 28.99 ? 139 ALA D CA  1 
ATOM   5391 C  C   . ALA D 1 142 ? 122.317 83.968  56.275  1.00 29.38 ? 139 ALA D C   1 
ATOM   5392 O  O   . ALA D 1 142 ? 122.962 84.819  56.871  1.00 29.58 ? 139 ALA D O   1 
ATOM   5393 C  CB  . ALA D 1 142 ? 120.509 83.703  58.002  1.00 28.94 ? 139 ALA D CB  1 
ATOM   5394 N  N   . GLY D 1 143 ? 122.349 83.848  54.951  1.00 29.06 ? 140 GLY D N   1 
ATOM   5395 C  CA  . GLY D 1 143 ? 123.230 84.676  54.134  1.00 29.89 ? 140 GLY D CA  1 
ATOM   5396 C  C   . GLY D 1 143 ? 124.651 84.149  53.922  1.00 30.76 ? 140 GLY D C   1 
ATOM   5397 O  O   . GLY D 1 143 ? 124.908 82.941  53.881  1.00 30.26 ? 140 GLY D O   1 
ATOM   5398 N  N   . GLU D 1 144 ? 125.586 85.081  53.772  1.00 31.69 ? 141 GLU D N   1 
ATOM   5399 C  CA  . GLU D 1 144 ? 126.982 84.728  53.604  1.00 32.82 ? 141 GLU D CA  1 
ATOM   5400 C  C   . GLU D 1 144 ? 127.557 84.389  54.963  1.00 32.71 ? 141 GLU D C   1 
ATOM   5401 O  O   . GLU D 1 144 ? 127.239 85.062  55.939  1.00 33.48 ? 141 GLU D O   1 
ATOM   5402 C  CB  . GLU D 1 144 ? 127.763 85.893  53.002  1.00 33.06 ? 141 GLU D CB  1 
ATOM   5403 C  CG  . GLU D 1 144 ? 129.025 85.460  52.276  1.00 35.71 ? 141 GLU D CG  1 
ATOM   5404 C  CD  . GLU D 1 144 ? 130.082 86.545  52.258  1.00 39.90 ? 141 GLU D CD  1 
ATOM   5405 O  OE1 . GLU D 1 144 ? 130.097 87.343  51.298  1.00 39.73 ? 141 GLU D OE1 1 
ATOM   5406 O  OE2 . GLU D 1 144 ? 130.888 86.603  53.217  1.00 42.92 ? 141 GLU D OE2 1 
ATOM   5407 N  N   . PRO D 1 145 ? 128.392 83.341  55.042  1.00 32.61 ? 142 PRO D N   1 
ATOM   5408 C  CA  . PRO D 1 145 ? 129.116 83.148  56.299  1.00 33.13 ? 142 PRO D CA  1 
ATOM   5409 C  C   . PRO D 1 145 ? 130.097 84.308  56.529  1.00 33.76 ? 142 PRO D C   1 
ATOM   5410 O  O   . PRO D 1 145 ? 131.022 84.513  55.739  1.00 34.48 ? 142 PRO D O   1 
ATOM   5411 C  CB  . PRO D 1 145 ? 129.824 81.804  56.104  1.00 33.05 ? 142 PRO D CB  1 
ATOM   5412 C  CG  . PRO D 1 145 ? 129.870 81.599  54.609  1.00 32.56 ? 142 PRO D CG  1 
ATOM   5413 C  CD  . PRO D 1 145 ? 128.697 82.308  54.039  1.00 32.08 ? 142 PRO D CD  1 
ATOM   5414 N  N   . ARG D 1 146 ? 129.854 85.088  57.580  1.00 34.55 ? 143 ARG D N   1 
ATOM   5415 C  CA  . ARG D 1 146 ? 130.612 86.305  57.840  1.00 35.57 ? 143 ARG D CA  1 
ATOM   5416 C  C   . ARG D 1 146 ? 131.278 86.368  59.217  1.00 35.06 ? 143 ARG D C   1 
ATOM   5417 O  O   . ARG D 1 146 ? 132.414 86.853  59.338  1.00 34.81 ? 143 ARG D O   1 
ATOM   5418 C  CB  . ARG D 1 146 ? 129.737 87.538  57.622  1.00 36.34 ? 143 ARG D CB  1 
ATOM   5419 C  CG  . ARG D 1 146 ? 129.970 88.229  56.276  1.00 40.89 ? 143 ARG D CG  1 
ATOM   5420 C  CD  . ARG D 1 146 ? 128.630 88.628  55.640  1.00 48.05 ? 143 ARG D CD  1 
ATOM   5421 N  NE  . ARG D 1 146 ? 127.728 89.240  56.623  1.00 52.09 ? 143 ARG D NE  1 
ATOM   5422 C  CZ  . ARG D 1 146 ? 127.720 90.539  56.936  1.00 55.10 ? 143 ARG D CZ  1 
ATOM   5423 N  NH1 . ARG D 1 146 ? 126.869 90.989  57.851  1.00 55.50 ? 143 ARG D NH1 1 
ATOM   5424 N  NH2 . ARG D 1 146 ? 128.561 91.394  56.342  1.00 55.93 ? 143 ARG D NH2 1 
ATOM   5425 N  N   . SER D 1 147 ? 130.568 85.915  60.251  1.00 34.15 ? 144 SER D N   1 
ATOM   5426 C  CA  . SER D 1 147 ? 131.141 85.851  61.584  1.00 33.14 ? 144 SER D CA  1 
ATOM   5427 C  C   . SER D 1 147 ? 132.077 84.653  61.661  1.00 33.30 ? 144 SER D C   1 
ATOM   5428 O  O   . SER D 1 147 ? 131.991 83.737  60.829  1.00 34.10 ? 144 SER D O   1 
ATOM   5429 C  CB  . SER D 1 147 ? 130.052 85.775  62.644  1.00 32.88 ? 144 SER D CB  1 
ATOM   5430 O  OG  . SER D 1 147 ? 129.391 84.522  62.629  1.00 31.92 ? 144 SER D OG  1 
ATOM   5431 N  N   . GLU D 1 148 ? 132.957 84.668  62.656  1.00 32.90 ? 145 GLU D N   1 
ATOM   5432 C  CA  . GLU D 1 148 ? 133.974 83.650  62.876  1.00 33.55 ? 145 GLU D CA  1 
ATOM   5433 C  C   . GLU D 1 148 ? 133.358 82.268  63.079  1.00 32.45 ? 145 GLU D C   1 
ATOM   5434 O  O   . GLU D 1 148 ? 133.857 81.280  62.541  1.00 31.87 ? 145 GLU D O   1 
ATOM   5435 C  CB  . GLU D 1 148 ? 134.802 84.041  64.113  1.00 33.72 ? 145 GLU D CB  1 
ATOM   5436 C  CG  . GLU D 1 148 ? 136.308 83.776  64.036  1.00 36.20 ? 145 GLU D CG  1 
ATOM   5437 C  CD  . GLU D 1 148 ? 137.045 84.147  65.351  1.00 37.40 ? 145 GLU D CD  1 
ATOM   5438 O  OE1 . GLU D 1 148 ? 136.531 83.792  66.454  1.00 41.29 ? 145 GLU D OE1 1 
ATOM   5439 O  OE2 . GLU D 1 148 ? 138.149 84.783  65.283  1.00 41.43 ? 145 GLU D OE2 1 
ATOM   5440 N  N   . GLU D 1 149 ? 132.276 82.216  63.863  1.00 31.96 ? 146 GLU D N   1 
ATOM   5441 C  CA  . GLU D 1 149 ? 131.558 80.967  64.168  1.00 31.68 ? 146 GLU D CA  1 
ATOM   5442 C  C   . GLU D 1 149 ? 130.855 80.389  62.927  1.00 30.79 ? 146 GLU D C   1 
ATOM   5443 O  O   . GLU D 1 149 ? 130.833 79.172  62.716  1.00 29.69 ? 146 GLU D O   1 
ATOM   5444 C  CB  . GLU D 1 149 ? 130.562 81.160  65.332  1.00 31.49 ? 146 GLU D CB  1 
ATOM   5445 C  CG  . GLU D 1 149 ? 129.661 82.376  65.190  1.00 32.11 ? 146 GLU D CG  1 
ATOM   5446 C  CD  . GLU D 1 149 ? 128.616 82.551  66.302  1.00 32.98 ? 146 GLU D CD  1 
ATOM   5447 O  OE1 . GLU D 1 149 ? 127.572 83.166  65.973  1.00 34.82 ? 146 GLU D OE1 1 
ATOM   5448 O  OE2 . GLU D 1 149 ? 128.815 82.114  67.479  1.00 33.08 ? 146 GLU D OE2 1 
ATOM   5449 N  N   . GLU D 1 150 ? 130.301 81.277  62.106  1.00 30.23 ? 147 GLU D N   1 
ATOM   5450 C  CA  . GLU D 1 150 ? 129.654 80.864  60.875  1.00 29.95 ? 147 GLU D CA  1 
ATOM   5451 C  C   . GLU D 1 150 ? 130.689 80.254  59.934  1.00 29.53 ? 147 GLU D C   1 
ATOM   5452 O  O   . GLU D 1 150 ? 130.461 79.174  59.397  1.00 28.92 ? 147 GLU D O   1 
ATOM   5453 C  CB  . GLU D 1 150 ? 128.922 82.038  60.241  1.00 30.58 ? 147 GLU D CB  1 
ATOM   5454 C  CG  . GLU D 1 150 ? 127.689 82.437  61.035  1.00 31.04 ? 147 GLU D CG  1 
ATOM   5455 C  CD  . GLU D 1 150 ? 127.114 83.773  60.613  1.00 34.01 ? 147 GLU D CD  1 
ATOM   5456 O  OE1 . GLU D 1 150 ? 127.792 84.553  59.891  1.00 33.90 ? 147 GLU D OE1 1 
ATOM   5457 O  OE2 . GLU D 1 150 ? 125.959 84.042  61.008  1.00 35.61 ? 147 GLU D OE2 1 
ATOM   5458 N  N   . LYS D 1 151 ? 131.853 80.911  59.801  1.00 29.02 ? 148 LYS D N   1 
ATOM   5459 C  CA  . LYS D 1 151 ? 132.951 80.374  58.987  1.00 27.91 ? 148 LYS D CA  1 
ATOM   5460 C  C   . LYS D 1 151 ? 133.515 79.045  59.538  1.00 27.13 ? 148 LYS D C   1 
ATOM   5461 O  O   . LYS D 1 151 ? 133.830 78.110  58.765  1.00 26.43 ? 148 LYS D O   1 
ATOM   5462 C  CB  . LYS D 1 151 ? 134.049 81.419  58.789  1.00 27.85 ? 148 LYS D CB  1 
ATOM   5463 C  CG  . LYS D 1 151 ? 133.623 82.568  57.887  1.00 28.75 ? 148 LYS D CG  1 
ATOM   5464 C  CD  . LYS D 1 151 ? 134.581 83.773  57.960  1.00 28.15 ? 148 LYS D CD  1 
ATOM   5465 C  CE  . LYS D 1 151 ? 134.250 84.795  56.860  1.00 30.20 ? 148 LYS D CE  1 
ATOM   5466 N  NZ  . LYS D 1 151 ? 135.362 85.800  56.587  1.00 32.52 ? 148 LYS D NZ  1 
ATOM   5467 N  N   . GLU D 1 152 ? 133.599 78.944  60.862  1.00 26.27 ? 149 GLU D N   1 
ATOM   5468 C  CA  . GLU D 1 152 ? 134.130 77.738  61.503  1.00 26.44 ? 149 GLU D CA  1 
ATOM   5469 C  C   . GLU D 1 152 ? 133.145 76.560  61.488  1.00 27.02 ? 149 GLU D C   1 
ATOM   5470 O  O   . GLU D 1 152 ? 133.591 75.404  61.474  1.00 27.50 ? 149 GLU D O   1 
ATOM   5471 C  CB  . GLU D 1 152 ? 134.624 78.029  62.927  1.00 26.84 ? 149 GLU D CB  1 
ATOM   5472 C  CG  . GLU D 1 152 ? 135.386 76.875  63.616  1.00 27.79 ? 149 GLU D CG  1 
ATOM   5473 C  CD  . GLU D 1 152 ? 136.621 76.357  62.831  1.00 29.29 ? 149 GLU D CD  1 
ATOM   5474 O  OE1 . GLU D 1 152 ? 136.832 75.120  62.819  1.00 27.13 ? 149 GLU D OE1 1 
ATOM   5475 O  OE2 . GLU D 1 152 ? 137.368 77.179  62.236  1.00 29.20 ? 149 GLU D OE2 1 
ATOM   5476 N  N   . ALA D 1 153 ? 131.831 76.831  61.491  1.00 26.55 ? 150 ALA D N   1 
ATOM   5477 C  CA  . ALA D 1 153 ? 130.841 75.753  61.288  1.00 27.37 ? 150 ALA D CA  1 
ATOM   5478 C  C   . ALA D 1 153 ? 131.043 75.092  59.918  1.00 27.55 ? 150 ALA D C   1 
ATOM   5479 O  O   . ALA D 1 153 ? 131.089 73.859  59.812  1.00 27.90 ? 150 ALA D O   1 
ATOM   5480 C  CB  . ALA D 1 153 ? 129.391 76.258  61.451  1.00 26.23 ? 150 ALA D CB  1 
ATOM   5481 N  N   . CYS D 1 154 ? 131.192 75.920  58.881  1.00 27.90 ? 151 CYS D N   1 
ATOM   5482 C  CA  . CYS D 1 154 ? 131.479 75.441  57.522  1.00 27.72 ? 151 CYS D CA  1 
ATOM   5483 C  C   . CYS D 1 154 ? 132.738 74.588  57.468  1.00 27.61 ? 151 CYS D C   1 
ATOM   5484 O  O   . CYS D 1 154 ? 132.685 73.481  56.943  1.00 27.82 ? 151 CYS D O   1 
ATOM   5485 C  CB  . CYS D 1 154 ? 131.596 76.604  56.553  1.00 27.54 ? 151 CYS D CB  1 
ATOM   5486 S  SG  . CYS D 1 154 ? 130.044 77.492  56.311  1.00 28.96 ? 151 CYS D SG  1 
ATOM   5487 N  N   . ARG D 1 155 ? 133.845 75.092  58.033  1.00 27.61 ? 152 ARG D N   1 
ATOM   5488 C  CA  . ARG D 1 155 ? 135.107 74.352  58.096  1.00 27.22 ? 152 ARG D CA  1 
ATOM   5489 C  C   . ARG D 1 155 ? 134.980 73.027  58.872  1.00 27.28 ? 152 ARG D C   1 
ATOM   5490 O  O   . ARG D 1 155 ? 135.525 72.001  58.463  1.00 27.33 ? 152 ARG D O   1 
ATOM   5491 C  CB  . ARG D 1 155 ? 136.214 75.205  58.722  1.00 27.32 ? 152 ARG D CB  1 
ATOM   5492 C  CG  . ARG D 1 155 ? 136.689 76.418  57.915  1.00 26.69 ? 152 ARG D CG  1 
ATOM   5493 C  CD  . ARG D 1 155 ? 137.911 77.111  58.594  1.00 27.35 ? 152 ARG D CD  1 
ATOM   5494 N  NE  . ARG D 1 155 ? 138.141 78.480  58.104  1.00 26.88 ? 152 ARG D NE  1 
ATOM   5495 C  CZ  . ARG D 1 155 ? 137.803 79.588  58.770  1.00 27.57 ? 152 ARG D CZ  1 
ATOM   5496 N  NH1 . ARG D 1 155 ? 137.242 79.512  59.971  1.00 29.78 ? 152 ARG D NH1 1 
ATOM   5497 N  NH2 . ARG D 1 155 ? 138.030 80.786  58.251  1.00 27.38 ? 152 ARG D NH2 1 
ATOM   5498 N  N   . ARG D 1 156 ? 134.251 73.059  59.981  1.00 27.01 ? 153 ARG D N   1 
ATOM   5499 C  CA  . ARG D 1 156 ? 134.126 71.911  60.863  1.00 27.10 ? 153 ARG D CA  1 
ATOM   5500 C  C   . ARG D 1 156 ? 133.382 70.758  60.209  1.00 27.46 ? 153 ARG D C   1 
ATOM   5501 O  O   . ARG D 1 156 ? 133.717 69.582  60.444  1.00 27.24 ? 153 ARG D O   1 
ATOM   5502 C  CB  . ARG D 1 156 ? 133.440 72.305  62.179  1.00 26.88 ? 153 ARG D CB  1 
ATOM   5503 C  CG  . ARG D 1 156 ? 133.413 71.198  63.237  1.00 26.59 ? 153 ARG D CG  1 
ATOM   5504 C  CD  . ARG D 1 156 ? 134.802 70.824  63.729  1.00 26.95 ? 153 ARG D CD  1 
ATOM   5505 N  NE  . ARG D 1 156 ? 135.599 72.032  63.932  1.00 29.90 ? 153 ARG D NE  1 
ATOM   5506 C  CZ  . ARG D 1 156 ? 135.577 72.761  65.048  1.00 29.58 ? 153 ARG D CZ  1 
ATOM   5507 N  NH1 . ARG D 1 156 ? 136.306 73.866  65.142  1.00 24.53 ? 153 ARG D NH1 1 
ATOM   5508 N  NH2 . ARG D 1 156 ? 134.820 72.381  66.071  1.00 29.78 ? 153 ARG D NH2 1 
ATOM   5509 N  N   . LEU D 1 157 ? 132.370 71.107  59.407  1.00 27.87 ? 154 LEU D N   1 
ATOM   5510 C  CA  . LEU D 1 157 ? 131.634 70.148  58.596  1.00 27.74 ? 154 LEU D CA  1 
ATOM   5511 C  C   . LEU D 1 157 ? 132.602 69.377  57.682  1.00 28.13 ? 154 LEU D C   1 
ATOM   5512 O  O   . LEU D 1 157 ? 132.555 68.137  57.610  1.00 29.30 ? 154 LEU D O   1 
ATOM   5513 C  CB  . LEU D 1 157 ? 130.535 70.843  57.776  1.00 27.00 ? 154 LEU D CB  1 
ATOM   5514 C  CG  . LEU D 1 157 ? 129.590 69.867  57.057  1.00 26.53 ? 154 LEU D CG  1 
ATOM   5515 C  CD1 . LEU D 1 157 ? 128.553 69.280  58.006  1.00 25.93 ? 154 LEU D CD1 1 
ATOM   5516 C  CD2 . LEU D 1 157 ? 128.897 70.481  55.865  1.00 24.37 ? 154 LEU D CD2 1 
ATOM   5517 N  N   . GLY D 1 158 ? 133.489 70.101  57.009  1.00 27.77 ? 155 GLY D N   1 
ATOM   5518 C  CA  . GLY D 1 158 ? 134.428 69.480  56.102  1.00 27.53 ? 155 GLY D CA  1 
ATOM   5519 C  C   . GLY D 1 158 ? 135.449 68.662  56.857  1.00 27.99 ? 155 GLY D C   1 
ATOM   5520 O  O   . GLY D 1 158 ? 135.905 67.614  56.370  1.00 27.91 ? 155 GLY D O   1 
ATOM   5521 N  N   . ARG D 1 159 ? 135.798 69.145  58.053  1.00 27.96 ? 156 ARG D N   1 
ATOM   5522 C  CA  . ARG D 1 159 ? 136.776 68.503  58.909  1.00 28.34 ? 156 ARG D CA  1 
ATOM   5523 C  C   . ARG D 1 159 ? 136.283 67.137  59.340  1.00 28.12 ? 156 ARG D C   1 
ATOM   5524 O  O   . ARG D 1 159 ? 136.986 66.148  59.152  1.00 28.77 ? 156 ARG D O   1 
ATOM   5525 C  CB  . ARG D 1 159 ? 137.045 69.351  60.154  1.00 29.08 ? 156 ARG D CB  1 
ATOM   5526 C  CG  . ARG D 1 159 ? 138.479 69.548  60.502  1.00 29.51 ? 156 ARG D CG  1 
ATOM   5527 C  CD  . ARG D 1 159 ? 139.188 68.339  61.057  1.00 30.50 ? 156 ARG D CD  1 
ATOM   5528 N  NE  . ARG D 1 159 ? 140.531 68.408  60.515  1.00 33.90 ? 156 ARG D NE  1 
ATOM   5529 C  CZ  . ARG D 1 159 ? 141.682 68.141  61.134  1.00 32.08 ? 156 ARG D CZ  1 
ATOM   5530 N  NH1 . ARG D 1 159 ? 141.757 67.713  62.385  1.00 30.74 ? 156 ARG D NH1 1 
ATOM   5531 N  NH2 . ARG D 1 159 ? 142.788 68.301  60.443  1.00 31.82 ? 156 ARG D NH2 1 
ATOM   5532 N  N   . ARG D 1 160 ? 135.087 67.090  59.924  1.00 27.84 ? 157 ARG D N   1 
ATOM   5533 C  CA  . ARG D 1 160 ? 134.493 65.848  60.412  1.00 27.39 ? 157 ARG D CA  1 
ATOM   5534 C  C   . ARG D 1 160 ? 134.267 64.793  59.305  1.00 27.42 ? 157 ARG D C   1 
ATOM   5535 O  O   . ARG D 1 160 ? 134.443 63.594  59.559  1.00 27.20 ? 157 ARG D O   1 
ATOM   5536 C  CB  . ARG D 1 160 ? 133.182 66.159  61.148  1.00 27.71 ? 157 ARG D CB  1 
ATOM   5537 C  CG  . ARG D 1 160 ? 132.606 65.006  61.986  1.00 27.46 ? 157 ARG D CG  1 
ATOM   5538 C  CD  . ARG D 1 160 ? 133.633 64.440  63.032  1.00 26.54 ? 157 ARG D CD  1 
ATOM   5539 N  NE  . ARG D 1 160 ? 134.475 65.463  63.665  1.00 26.11 ? 157 ARG D NE  1 
ATOM   5540 C  CZ  . ARG D 1 160 ? 134.065 66.333  64.594  1.00 26.85 ? 157 ARG D CZ  1 
ATOM   5541 N  NH1 . ARG D 1 160 ? 132.805 66.345  65.018  1.00 27.78 ? 157 ARG D NH1 1 
ATOM   5542 N  NH2 . ARG D 1 160 ? 134.917 67.216  65.089  1.00 26.57 ? 157 ARG D NH2 1 
ATOM   5543 N  N   . LEU D 1 161 ? 133.874 65.243  58.102  1.00 27.12 ? 158 LEU D N   1 
ATOM   5544 C  CA  . LEU D 1 161 ? 133.690 64.372  56.932  1.00 26.92 ? 158 LEU D CA  1 
ATOM   5545 C  C   . LEU D 1 161 ? 134.996 63.670  56.619  1.00 27.53 ? 158 LEU D C   1 
ATOM   5546 O  O   . LEU D 1 161 ? 135.044 62.433  56.523  1.00 28.00 ? 158 LEU D O   1 
ATOM   5547 C  CB  . LEU D 1 161 ? 133.324 65.190  55.695  1.00 26.64 ? 158 LEU D CB  1 
ATOM   5548 C  CG  . LEU D 1 161 ? 132.436 64.698  54.529  1.00 26.47 ? 158 LEU D CG  1 
ATOM   5549 C  CD1 . LEU D 1 161 ? 132.837 65.423  53.263  1.00 25.97 ? 158 LEU D CD1 1 
ATOM   5550 C  CD2 . LEU D 1 161 ? 132.377 63.193  54.269  1.00 23.13 ? 158 LEU D CD2 1 
ATOM   5551 N  N   . ALA D 1 162 ? 136.051 64.479  56.460  1.00 27.59 ? 159 ALA D N   1 
ATOM   5552 C  CA  . ALA D 1 162 ? 137.398 63.998  56.160  1.00 27.54 ? 159 ALA D CA  1 
ATOM   5553 C  C   . ALA D 1 162 ? 137.836 63.036  57.246  1.00 27.69 ? 159 ALA D C   1 
ATOM   5554 O  O   . ALA D 1 162 ? 138.484 62.025  56.966  1.00 27.74 ? 159 ALA D O   1 
ATOM   5555 C  CB  . ALA D 1 162 ? 138.392 65.167  56.022  1.00 26.96 ? 159 ALA D CB  1 
ATOM   5556 N  N   . GLU D 1 163 ? 137.445 63.354  58.480  1.00 27.80 ? 160 GLU D N   1 
ATOM   5557 C  CA  . GLU D 1 163 ? 137.752 62.542  59.641  1.00 27.65 ? 160 GLU D CA  1 
ATOM   5558 C  C   . GLU D 1 163 ? 137.017 61.212  59.596  1.00 27.38 ? 160 GLU D C   1 
ATOM   5559 O  O   . GLU D 1 163 ? 137.621 60.174  59.871  1.00 27.55 ? 160 GLU D O   1 
ATOM   5560 C  CB  . GLU D 1 163 ? 137.473 63.312  60.934  1.00 27.61 ? 160 GLU D CB  1 
ATOM   5561 C  CG  . GLU D 1 163 ? 138.570 64.322  61.272  1.00 27.38 ? 160 GLU D CG  1 
ATOM   5562 C  CD  . GLU D 1 163 ? 138.174 65.325  62.358  1.00 27.73 ? 160 GLU D CD  1 
ATOM   5563 O  OE1 . GLU D 1 163 ? 136.981 65.410  62.708  1.00 27.72 ? 160 GLU D OE1 1 
ATOM   5564 O  OE2 . GLU D 1 163 ? 139.063 66.051  62.863  1.00 27.26 ? 160 GLU D OE2 1 
ATOM   5565 N  N   . TRP D 1 164 ? 135.736 61.236  59.229  1.00 27.19 ? 161 TRP D N   1 
ATOM   5566 C  CA  . TRP D 1 164 ? 134.961 59.995  59.072  1.00 27.15 ? 161 TRP D CA  1 
ATOM   5567 C  C   . TRP D 1 164 ? 135.497 59.151  57.900  1.00 27.48 ? 161 TRP D C   1 
ATOM   5568 O  O   . TRP D 1 164 ? 135.631 57.938  58.001  1.00 27.67 ? 161 TRP D O   1 
ATOM   5569 C  CB  . TRP D 1 164 ? 133.459 60.277  58.904  1.00 26.81 ? 161 TRP D CB  1 
ATOM   5570 C  CG  . TRP D 1 164 ? 132.703 60.792  60.117  1.00 26.05 ? 161 TRP D CG  1 
ATOM   5571 C  CD1 . TRP D 1 164 ? 131.505 61.466  60.102  1.00 26.76 ? 161 TRP D CD1 1 
ATOM   5572 C  CD2 . TRP D 1 164 ? 133.065 60.670  61.511  1.00 26.64 ? 161 TRP D CD2 1 
ATOM   5573 N  NE1 . TRP D 1 164 ? 131.097 61.755  61.392  1.00 23.95 ? 161 TRP D NE1 1 
ATOM   5574 C  CE2 . TRP D 1 164 ? 132.040 61.292  62.270  1.00 25.55 ? 161 TRP D CE2 1 
ATOM   5575 C  CE3 . TRP D 1 164 ? 134.157 60.106  62.193  1.00 26.90 ? 161 TRP D CE3 1 
ATOM   5576 C  CZ2 . TRP D 1 164 ? 132.075 61.359  63.673  1.00 25.95 ? 161 TRP D CZ2 1 
ATOM   5577 C  CZ3 . TRP D 1 164 ? 134.191 60.186  63.595  1.00 26.73 ? 161 TRP D CZ3 1 
ATOM   5578 C  CH2 . TRP D 1 164 ? 133.147 60.797  64.313  1.00 26.53 ? 161 TRP D CH2 1 
ATOM   5579 N  N   . VAL D 1 165 ? 135.834 59.804  56.797  1.00 27.83 ? 162 VAL D N   1 
ATOM   5580 C  CA  . VAL D 1 165 ? 136.510 59.132  55.692  1.00 27.66 ? 162 VAL D CA  1 
ATOM   5581 C  C   . VAL D 1 165 ? 137.823 58.478  56.126  1.00 28.08 ? 162 VAL D C   1 
ATOM   5582 O  O   . VAL D 1 165 ? 138.117 57.354  55.716  1.00 27.61 ? 162 VAL D O   1 
ATOM   5583 C  CB  . VAL D 1 165 ? 136.752 60.084  54.507  1.00 27.84 ? 162 VAL D CB  1 
ATOM   5584 C  CG1 . VAL D 1 165 ? 137.858 59.551  53.603  1.00 25.86 ? 162 VAL D CG1 1 
ATOM   5585 C  CG2 . VAL D 1 165 ? 135.441 60.306  53.736  1.00 27.36 ? 162 VAL D CG2 1 
ATOM   5586 N  N   . ALA D 1 166 ? 138.589 59.173  56.967  1.00 28.57 ? 163 ALA D N   1 
ATOM   5587 C  CA  . ALA D 1 166 ? 139.864 58.663  57.465  1.00 29.27 ? 163 ALA D CA  1 
ATOM   5588 C  C   . ALA D 1 166 ? 139.672 57.461  58.398  1.00 29.79 ? 163 ALA D C   1 
ATOM   5589 O  O   . ALA D 1 166 ? 140.328 56.422  58.222  1.00 30.12 ? 163 ALA D O   1 
ATOM   5590 C  CB  . ALA D 1 166 ? 140.675 59.775  58.159  1.00 28.93 ? 163 ALA D CB  1 
ATOM   5591 N  N   . ILE D 1 167 ? 138.780 57.596  59.376  1.00 30.16 ? 164 ILE D N   1 
ATOM   5592 C  CA  . ILE D 1 167 ? 138.498 56.502  60.313  1.00 30.90 ? 164 ILE D CA  1 
ATOM   5593 C  C   . ILE D 1 167 ? 137.765 55.314  59.667  1.00 31.78 ? 164 ILE D C   1 
ATOM   5594 O  O   . ILE D 1 167 ? 138.118 54.153  59.932  1.00 31.67 ? 164 ILE D O   1 
ATOM   5595 C  CB  . ILE D 1 167 ? 137.711 56.989  61.565  1.00 30.96 ? 164 ILE D CB  1 
ATOM   5596 C  CG1 . ILE D 1 167 ? 138.507 58.066  62.297  1.00 30.69 ? 164 ILE D CG1 1 
ATOM   5597 C  CG2 . ILE D 1 167 ? 137.354 55.815  62.516  1.00 29.60 ? 164 ILE D CG2 1 
ATOM   5598 C  CD1 . ILE D 1 167 ? 137.638 59.056  63.033  1.00 30.61 ? 164 ILE D CD1 1 
ATOM   5599 N  N   . PHE D 1 168 ? 136.751 55.592  58.841  1.00 32.35 ? 165 PHE D N   1 
ATOM   5600 C  CA  . PHE D 1 168 ? 135.901 54.509  58.339  1.00 33.33 ? 165 PHE D CA  1 
ATOM   5601 C  C   . PHE D 1 168 ? 136.309 53.877  57.005  1.00 34.34 ? 165 PHE D C   1 
ATOM   5602 O  O   . PHE D 1 168 ? 136.000 52.711  56.769  1.00 34.24 ? 165 PHE D O   1 
ATOM   5603 C  CB  . PHE D 1 168 ? 134.423 54.880  58.369  1.00 33.03 ? 165 PHE D CB  1 
ATOM   5604 C  CG  . PHE D 1 168 ? 133.910 55.188  59.750  1.00 33.04 ? 165 PHE D CG  1 
ATOM   5605 C  CD1 . PHE D 1 168 ? 133.417 56.452  60.054  1.00 32.84 ? 165 PHE D CD1 1 
ATOM   5606 C  CD2 . PHE D 1 168 ? 133.954 54.217  60.759  1.00 33.29 ? 165 PHE D CD2 1 
ATOM   5607 C  CE1 . PHE D 1 168 ? 132.955 56.746  61.329  1.00 33.98 ? 165 PHE D CE1 1 
ATOM   5608 C  CE2 . PHE D 1 168 ? 133.505 54.491  62.033  1.00 33.32 ? 165 PHE D CE2 1 
ATOM   5609 C  CZ  . PHE D 1 168 ? 133.002 55.765  62.324  1.00 34.50 ? 165 PHE D CZ  1 
ATOM   5610 N  N   . VAL D 1 169 ? 137.016 54.630  56.162  1.00 35.55 ? 166 VAL D N   1 
ATOM   5611 C  CA  . VAL D 1 169 ? 137.479 54.114  54.861  1.00 36.44 ? 166 VAL D CA  1 
ATOM   5612 C  C   . VAL D 1 169 ? 138.974 53.776  54.889  1.00 37.35 ? 166 VAL D C   1 
ATOM   5613 O  O   . VAL D 1 169 ? 139.391 52.684  54.496  1.00 37.61 ? 166 VAL D O   1 
ATOM   5614 C  CB  . VAL D 1 169 ? 137.142 55.092  53.688  1.00 36.54 ? 166 VAL D CB  1 
ATOM   5615 C  CG1 . VAL D 1 169 ? 137.567 54.500  52.346  1.00 36.26 ? 166 VAL D CG1 1 
ATOM   5616 C  CG2 . VAL D 1 169 ? 135.643 55.436  53.676  1.00 35.45 ? 166 VAL D CG2 1 
ATOM   5617 N  N   . ASP D 1 170 ? 139.769 54.706  55.407  1.00 38.30 ? 167 ASP D N   1 
ATOM   5618 C  CA  . ASP D 1 170 ? 141.216 54.598  55.359  1.00 39.05 ? 167 ASP D CA  1 
ATOM   5619 C  C   . ASP D 1 170 ? 141.830 54.079  56.657  1.00 38.93 ? 167 ASP D C   1 
ATOM   5620 O  O   . ASP D 1 170 ? 143.026 54.277  56.921  1.00 38.60 ? 167 ASP D O   1 
ATOM   5621 C  CB  . ASP D 1 170 ? 141.815 55.938  54.930  1.00 39.73 ? 167 ASP D CB  1 
ATOM   5622 C  CG  . ASP D 1 170 ? 141.228 56.437  53.602  1.00 41.30 ? 167 ASP D CG  1 
ATOM   5623 O  OD1 . ASP D 1 170 ? 140.799 57.613  53.569  1.00 42.73 ? 167 ASP D OD1 1 
ATOM   5624 O  OD2 . ASP D 1 170 ? 141.184 55.658  52.603  1.00 42.82 ? 167 ASP D OD2 1 
ATOM   5625 N  N   . GLY D 1 171 ? 140.993 53.416  57.452  1.00 38.63 ? 168 GLY D N   1 
ATOM   5626 C  CA  . GLY D 1 171 ? 141.435 52.656  58.606  1.00 38.73 ? 168 GLY D CA  1 
ATOM   5627 C  C   . GLY D 1 171 ? 142.006 53.376  59.816  1.00 38.91 ? 168 GLY D C   1 
ATOM   5628 O  O   . GLY D 1 171 ? 142.149 52.756  60.868  1.00 39.06 ? 168 GLY D O   1 
ATOM   5629 N  N   . ARG D 1 172 ? 142.337 54.662  59.706  1.00 39.09 ? 169 ARG D N   1 
ATOM   5630 C  CA  . ARG D 1 172 ? 143.000 55.348  60.837  1.00 39.51 ? 169 ARG D CA  1 
ATOM   5631 C  C   . ARG D 1 172 ? 142.120 55.531  62.085  1.00 39.23 ? 169 ARG D C   1 
ATOM   5632 O  O   . ARG D 1 172 ? 141.698 56.638  62.417  1.00 38.80 ? 169 ARG D O   1 
ATOM   5633 C  CB  . ARG D 1 172 ? 143.743 56.643  60.422  1.00 39.73 ? 169 ARG D CB  1 
ATOM   5634 C  CG  . ARG D 1 172 ? 143.117 57.431  59.282  1.00 40.82 ? 169 ARG D CG  1 
ATOM   5635 C  CD  . ARG D 1 172 ? 144.184 57.922  58.297  1.00 41.82 ? 169 ARG D CD  1 
ATOM   5636 N  NE  . ARG D 1 172 ? 144.279 59.383  58.144  1.00 42.33 ? 169 ARG D NE  1 
ATOM   5637 C  CZ  . ARG D 1 172 ? 144.744 60.235  59.070  1.00 42.64 ? 169 ARG D CZ  1 
ATOM   5638 N  NH1 . ARG D 1 172 ? 145.136 59.810  60.285  1.00 41.86 ? 169 ARG D NH1 1 
ATOM   5639 N  NH2 . ARG D 1 172 ? 144.808 61.532  58.778  1.00 42.76 ? 169 ARG D NH2 1 
ATOM   5640 N  N   . LYS D 1 173 ? 141.913 54.413  62.783  1.00 39.62 ? 170 LYS D N   1 
ATOM   5641 C  CA  . LYS D 1 173 ? 140.985 54.296  63.921  1.00 40.35 ? 170 LYS D CA  1 
ATOM   5642 C  C   . LYS D 1 173 ? 141.436 54.895  65.275  1.00 40.18 ? 170 LYS D C   1 
ATOM   5643 O  O   . LYS D 1 173 ? 140.606 55.054  66.192  1.00 40.33 ? 170 LYS D O   1 
ATOM   5644 C  CB  . LYS D 1 173 ? 140.540 52.831  64.108  1.00 40.78 ? 170 LYS D CB  1 
ATOM   5645 C  CG  . LYS D 1 173 ? 141.644 51.771  64.009  1.00 41.79 ? 170 LYS D CG  1 
ATOM   5646 C  CD  . LYS D 1 173 ? 141.386 50.575  64.952  1.00 43.71 ? 170 LYS D CD  1 
ATOM   5647 C  CE  . LYS D 1 173 ? 140.159 49.726  64.537  1.00 44.48 ? 170 LYS D CE  1 
ATOM   5648 N  NZ  . LYS D 1 173 ? 140.419 48.740  63.412  1.00 43.36 ? 170 LYS D NZ  1 
ATOM   5649 N  N   . GLU D 1 174 ? 142.723 55.241  65.396  1.00 39.54 ? 171 GLU D N   1 
ATOM   5650 C  CA  . GLU D 1 174 ? 143.232 55.983  66.570  1.00 39.17 ? 171 GLU D CA  1 
ATOM   5651 C  C   . GLU D 1 174 ? 142.504 57.322  66.752  1.00 38.38 ? 171 GLU D C   1 
ATOM   5652 O  O   . GLU D 1 174 ? 142.382 57.834  67.874  1.00 38.32 ? 171 GLU D O   1 
ATOM   5653 C  CB  . GLU D 1 174 ? 144.745 56.228  66.467  1.00 39.32 ? 171 GLU D CB  1 
ATOM   5654 C  CG  . GLU D 1 174 ? 145.163 57.249  65.382  1.00 40.78 ? 171 GLU D CG  1 
ATOM   5655 C  CD  . GLU D 1 174 ? 145.423 56.619  63.995  1.00 43.54 ? 171 GLU D CD  1 
ATOM   5656 O  OE1 . GLU D 1 174 ? 146.297 57.146  63.269  1.00 44.65 ? 171 GLU D OE1 1 
ATOM   5657 O  OE2 . GLU D 1 174 ? 144.783 55.602  63.624  1.00 43.76 ? 171 GLU D OE2 1 
ATOM   5658 N  N   . LEU D 1 175 ? 142.017 57.857  65.634  1.00 37.42 ? 172 LEU D N   1 
ATOM   5659 C  CA  . LEU D 1 175 ? 141.411 59.185  65.553  1.00 36.54 ? 172 LEU D CA  1 
ATOM   5660 C  C   . LEU D 1 175 ? 140.029 59.295  66.202  1.00 35.38 ? 172 LEU D C   1 
ATOM   5661 O  O   . LEU D 1 175 ? 139.627 60.378  66.635  1.00 35.33 ? 172 LEU D O   1 
ATOM   5662 C  CB  . LEU D 1 175 ? 141.330 59.607  64.085  1.00 36.65 ? 172 LEU D CB  1 
ATOM   5663 C  CG  . LEU D 1 175 ? 141.387 61.093  63.736  1.00 37.35 ? 172 LEU D CG  1 
ATOM   5664 C  CD1 . LEU D 1 175 ? 142.497 61.821  64.513  1.00 38.38 ? 172 LEU D CD1 1 
ATOM   5665 C  CD2 . LEU D 1 175 ? 141.585 61.245  62.227  1.00 36.85 ? 172 LEU D CD2 1 
ATOM   5666 N  N   . LEU D 1 176 ? 139.312 58.177  66.265  1.00 34.02 ? 173 LEU D N   1 
ATOM   5667 C  CA  . LEU D 1 176 ? 137.959 58.148  66.792  1.00 32.72 ? 173 LEU D CA  1 
ATOM   5668 C  C   . LEU D 1 176 ? 137.966 58.723  68.190  1.00 32.45 ? 173 LEU D C   1 
ATOM   5669 O  O   . LEU D 1 176 ? 137.259 59.677  68.489  1.00 32.73 ? 173 LEU D O   1 
ATOM   5670 C  CB  . LEU D 1 176 ? 137.453 56.706  66.858  1.00 32.17 ? 173 LEU D CB  1 
ATOM   5671 C  CG  . LEU D 1 176 ? 136.033 56.336  66.402  1.00 32.19 ? 173 LEU D CG  1 
ATOM   5672 C  CD1 . LEU D 1 176 ? 135.496 55.153  67.213  1.00 30.31 ? 173 LEU D CD1 1 
ATOM   5673 C  CD2 . LEU D 1 176 ? 135.060 57.511  66.415  1.00 29.63 ? 173 LEU D CD2 1 
ATOM   5674 N  N   . GLU D 1 177 ? 138.788 58.118  69.031  1.00 32.00 ? 174 GLU D N   1 
ATOM   5675 C  CA  . GLU D 1 177 ? 138.891 58.420  70.438  1.00 31.84 ? 174 GLU D CA  1 
ATOM   5676 C  C   . GLU D 1 177 ? 139.473 59.812  70.699  1.00 31.11 ? 174 GLU D C   1 
ATOM   5677 O  O   . GLU D 1 177 ? 139.053 60.508  71.624  1.00 30.69 ? 174 GLU D O   1 
ATOM   5678 C  CB  . GLU D 1 177 ? 139.740 57.330  71.098  1.00 31.99 ? 174 GLU D CB  1 
ATOM   5679 C  CG  . GLU D 1 177 ? 139.766 57.388  72.614  1.00 34.59 ? 174 GLU D CG  1 
ATOM   5680 C  CD  . GLU D 1 177 ? 138.370 57.310  73.262  1.00 37.48 ? 174 GLU D CD  1 
ATOM   5681 O  OE1 . GLU D 1 177 ? 138.342 57.330  74.518  1.00 38.34 ? 174 GLU D OE1 1 
ATOM   5682 O  OE2 . GLU D 1 177 ? 137.325 57.234  72.542  1.00 36.28 ? 174 GLU D OE2 1 
ATOM   5683 N  N   . LYS D 1 178 ? 140.441 60.206  69.880  1.00 30.70 ? 175 LYS D N   1 
ATOM   5684 C  CA  . LYS D 1 178 ? 140.986 61.550  69.921  1.00 30.86 ? 175 LYS D CA  1 
ATOM   5685 C  C   . LYS D 1 178 ? 139.921 62.620  69.640  1.00 30.36 ? 175 LYS D C   1 
ATOM   5686 O  O   . LYS D 1 178 ? 139.855 63.615  70.354  1.00 30.36 ? 175 LYS D O   1 
ATOM   5687 C  CB  . LYS D 1 178 ? 142.213 61.675  69.004  1.00 30.86 ? 175 LYS D CB  1 
ATOM   5688 C  CG  . LYS D 1 178 ? 143.520 61.572  69.796  1.00 34.25 ? 175 LYS D CG  1 
ATOM   5689 C  CD  . LYS D 1 178 ? 144.693 60.988  69.007  1.00 37.58 ? 175 LYS D CD  1 
ATOM   5690 C  CE  . LYS D 1 178 ? 145.930 60.954  69.892  1.00 40.28 ? 175 LYS D CE  1 
ATOM   5691 N  NZ  . LYS D 1 178 ? 147.074 60.217  69.272  1.00 41.81 ? 175 LYS D NZ  1 
ATOM   5692 N  N   . ILE D 1 179 ? 139.087 62.401  68.619  1.00 30.00 ? 176 ILE D N   1 
ATOM   5693 C  CA  . ILE D 1 179 ? 137.945 63.275  68.322  1.00 29.58 ? 176 ILE D CA  1 
ATOM   5694 C  C   . ILE D 1 179 ? 136.924 63.188  69.477  1.00 29.75 ? 176 ILE D C   1 
ATOM   5695 O  O   . ILE D 1 179 ? 136.577 64.202  70.081  1.00 29.67 ? 176 ILE D O   1 
ATOM   5696 C  CB  . ILE D 1 179 ? 137.282 62.897  66.958  1.00 30.13 ? 176 ILE D CB  1 
ATOM   5697 C  CG1 . ILE D 1 179 ? 138.239 63.153  65.783  1.00 29.67 ? 176 ILE D CG1 1 
ATOM   5698 C  CG2 . ILE D 1 179 ? 135.959 63.628  66.734  1.00 27.95 ? 176 ILE D CG2 1 
ATOM   5699 C  CD1 . ILE D 1 179 ? 137.735 62.526  64.476  1.00 29.64 ? 176 ILE D CD1 1 
ATOM   5700 N  N   . ARG D 1 180 ? 136.478 61.970  69.792  1.00 29.46 ? 177 ARG D N   1 
ATOM   5701 C  CA  . ARG D 1 180 ? 135.571 61.701  70.909  1.00 29.21 ? 177 ARG D CA  1 
ATOM   5702 C  C   . ARG D 1 180 ? 135.894 62.397  72.241  1.00 29.17 ? 177 ARG D C   1 
ATOM   5703 O  O   . ARG D 1 180 ? 134.967 62.811  72.944  1.00 29.68 ? 177 ARG D O   1 
ATOM   5704 C  CB  . ARG D 1 180 ? 135.382 60.189  71.100  1.00 28.88 ? 177 ARG D CB  1 
ATOM   5705 C  CG  . ARG D 1 180 ? 134.062 59.718  70.547  1.00 31.52 ? 177 ARG D CG  1 
ATOM   5706 C  CD  . ARG D 1 180 ? 134.163 58.571  69.543  1.00 34.83 ? 177 ARG D CD  1 
ATOM   5707 N  NE  . ARG D 1 180 ? 133.956 57.254  70.142  1.00 35.52 ? 177 ARG D NE  1 
ATOM   5708 C  CZ  . ARG D 1 180 ? 133.099 56.323  69.711  1.00 36.02 ? 177 ARG D CZ  1 
ATOM   5709 N  NH1 . ARG D 1 180 ? 133.023 55.175  70.368  1.00 37.92 ? 177 ARG D NH1 1 
ATOM   5710 N  NH2 . ARG D 1 180 ? 132.324 56.502  68.647  1.00 34.43 ? 177 ARG D NH2 1 
ATOM   5711 N  N   . LYS D 1 181 ? 137.175 62.552  72.581  1.00 28.72 ? 178 LYS D N   1 
ATOM   5712 C  CA  . LYS D 1 181 ? 137.565 63.187  73.859  1.00 28.75 ? 178 LYS D CA  1 
ATOM   5713 C  C   . LYS D 1 181 ? 138.121 64.630  73.711  1.00 28.18 ? 178 LYS D C   1 
ATOM   5714 O  O   . LYS D 1 181 ? 138.553 65.221  74.692  1.00 27.35 ? 178 LYS D O   1 
ATOM   5715 C  CB  . LYS D 1 181 ? 138.571 62.306  74.653  1.00 28.60 ? 178 LYS D CB  1 
ATOM   5716 C  CG  . LYS D 1 181 ? 138.180 60.821  74.832  1.00 30.73 ? 178 LYS D CG  1 
ATOM   5717 C  CD  . LYS D 1 181 ? 137.441 60.499  76.167  1.00 33.03 ? 178 LYS D CD  1 
ATOM   5718 C  CE  . LYS D 1 181 ? 136.237 59.559  75.923  1.00 33.88 ? 178 LYS D CE  1 
ATOM   5719 N  NZ  . LYS D 1 181 ? 136.178 58.448  76.925  1.00 32.24 ? 178 LYS D NZ  1 
ATOM   5720 N  N   . ASP D 1 182 ? 138.095 65.191  72.498  1.00 28.08 ? 179 ASP D N   1 
ATOM   5721 C  CA  . ASP D 1 182 ? 138.720 66.502  72.232  1.00 28.05 ? 179 ASP D CA  1 
ATOM   5722 C  C   . ASP D 1 182 ? 137.924 67.682  72.813  1.00 27.34 ? 179 ASP D C   1 
ATOM   5723 O  O   . ASP D 1 182 ? 136.796 67.921  72.382  1.00 27.54 ? 179 ASP D O   1 
ATOM   5724 C  CB  . ASP D 1 182 ? 138.918 66.682  70.728  1.00 28.32 ? 179 ASP D CB  1 
ATOM   5725 C  CG  . ASP D 1 182 ? 139.489 68.063  70.345  1.00 31.29 ? 179 ASP D CG  1 
ATOM   5726 O  OD1 . ASP D 1 182 ? 139.293 68.446  69.164  1.00 34.12 ? 179 ASP D OD1 1 
ATOM   5727 O  OD2 . ASP D 1 182 ? 140.138 68.750  71.189  1.00 32.23 ? 179 ASP D OD2 1 
ATOM   5728 N  N   . PRO D 1 183 ? 138.514 68.431  73.779  1.00 26.52 ? 180 PRO D N   1 
ATOM   5729 C  CA  . PRO D 1 183 ? 137.795 69.548  74.422  1.00 26.28 ? 180 PRO D CA  1 
ATOM   5730 C  C   . PRO D 1 183 ? 137.554 70.739  73.483  1.00 26.41 ? 180 PRO D C   1 
ATOM   5731 O  O   . PRO D 1 183 ? 136.620 71.519  73.697  1.00 26.50 ? 180 PRO D O   1 
ATOM   5732 C  CB  . PRO D 1 183 ? 138.726 69.965  75.586  1.00 26.30 ? 180 PRO D CB  1 
ATOM   5733 C  CG  . PRO D 1 183 ? 139.799 68.946  75.652  1.00 25.91 ? 180 PRO D CG  1 
ATOM   5734 C  CD  . PRO D 1 183 ? 139.881 68.286  74.316  1.00 26.32 ? 180 PRO D CD  1 
ATOM   5735 N  N   . ALA D 1 184 ? 138.396 70.870  72.460  1.00 26.42 ? 181 ALA D N   1 
ATOM   5736 C  CA  . ALA D 1 184 ? 138.270 71.919  71.447  1.00 26.89 ? 181 ALA D CA  1 
ATOM   5737 C  C   . ALA D 1 184 ? 136.931 71.901  70.723  1.00 27.23 ? 181 ALA D C   1 
ATOM   5738 O  O   . ALA D 1 184 ? 136.509 72.930  70.191  1.00 27.74 ? 181 ALA D O   1 
ATOM   5739 C  CB  . ALA D 1 184 ? 139.400 71.805  70.412  1.00 26.62 ? 181 ALA D CB  1 
ATOM   5740 N  N   . ARG D 1 185 ? 136.290 70.730  70.679  1.00 26.97 ? 182 ARG D N   1 
ATOM   5741 C  CA  . ARG D 1 185 ? 135.004 70.573  70.013  1.00 27.53 ? 182 ARG D CA  1 
ATOM   5742 C  C   . ARG D 1 185 ? 133.858 71.394  70.639  1.00 27.39 ? 182 ARG D C   1 
ATOM   5743 O  O   . ARG D 1 185 ? 132.818 71.521  70.045  1.00 26.95 ? 182 ARG D O   1 
ATOM   5744 C  CB  . ARG D 1 185 ? 134.627 69.080  69.922  1.00 27.40 ? 182 ARG D CB  1 
ATOM   5745 C  CG  . ARG D 1 185 ? 135.631 68.228  69.108  1.00 28.23 ? 182 ARG D CG  1 
ATOM   5746 C  CD  . ARG D 1 185 ? 135.283 66.746  69.160  1.00 27.06 ? 182 ARG D CD  1 
ATOM   5747 N  NE  . ARG D 1 185 ? 133.865 66.574  68.867  1.00 26.59 ? 182 ARG D NE  1 
ATOM   5748 C  CZ  . ARG D 1 185 ? 133.057 65.731  69.500  1.00 25.70 ? 182 ARG D CZ  1 
ATOM   5749 N  NH1 . ARG D 1 185 ? 131.765 65.693  69.174  1.00 25.50 ? 182 ARG D NH1 1 
ATOM   5750 N  NH2 . ARG D 1 185 ? 133.526 64.960  70.474  1.00 23.61 ? 182 ARG D NH2 1 
ATOM   5751 N  N   . PHE D 1 186 ? 134.059 71.930  71.838  1.00 28.26 ? 183 PHE D N   1 
ATOM   5752 C  CA  . PHE D 1 186 ? 133.024 72.686  72.528  1.00 29.72 ? 183 PHE D CA  1 
ATOM   5753 C  C   . PHE D 1 186 ? 133.537 74.021  73.028  1.00 30.88 ? 183 PHE D C   1 
ATOM   5754 O  O   . PHE D 1 186 ? 134.214 74.113  74.052  1.00 30.93 ? 183 PHE D O   1 
ATOM   5755 C  CB  . PHE D 1 186 ? 132.356 71.815  73.610  1.00 28.82 ? 183 PHE D CB  1 
ATOM   5756 C  CG  . PHE D 1 186 ? 131.709 70.602  73.023  1.00 29.98 ? 183 PHE D CG  1 
ATOM   5757 C  CD1 . PHE D 1 186 ? 132.404 69.390  72.942  1.00 30.17 ? 183 PHE D CD1 1 
ATOM   5758 C  CD2 . PHE D 1 186 ? 130.462 70.694  72.401  1.00 28.93 ? 183 PHE D CD2 1 
ATOM   5759 C  CE1 . PHE D 1 186 ? 131.841 68.281  72.315  1.00 27.76 ? 183 PHE D CE1 1 
ATOM   5760 C  CE2 . PHE D 1 186 ? 129.897 69.573  71.774  1.00 29.40 ? 183 PHE D CE2 1 
ATOM   5761 C  CZ  . PHE D 1 186 ? 130.582 68.382  71.730  1.00 27.68 ? 183 PHE D CZ  1 
ATOM   5762 N  N   . VAL D 1 187 ? 133.245 75.048  72.232  1.00 32.70 ? 184 VAL D N   1 
ATOM   5763 C  CA  . VAL D 1 187 ? 133.468 76.441  72.597  1.00 33.83 ? 184 VAL D CA  1 
ATOM   5764 C  C   . VAL D 1 187 ? 132.311 76.849  73.488  1.00 34.25 ? 184 VAL D C   1 
ATOM   5765 O  O   . VAL D 1 187 ? 132.347 76.590  74.693  1.00 35.37 ? 184 VAL D O   1 
ATOM   5766 C  CB  . VAL D 1 187 ? 133.521 77.356  71.357  1.00 34.01 ? 184 VAL D CB  1 
ATOM   5767 C  CG1 . VAL D 1 187 ? 133.486 78.832  71.765  1.00 35.43 ? 184 VAL D CG1 1 
ATOM   5768 C  CG2 . VAL D 1 187 ? 134.779 77.064  70.518  1.00 35.32 ? 184 VAL D CG2 1 
HETATM 5769 N  N   . MSE E 1 4   ? 81.963  117.272 83.023  1.00 56.79 ? 1   MSE E N   1 
HETATM 5770 C  CA  . MSE E 1 4   ? 80.885  118.292 83.203  1.00 57.68 ? 1   MSE E CA  1 
HETATM 5771 C  C   . MSE E 1 4   ? 79.511  117.650 83.312  1.00 54.97 ? 1   MSE E C   1 
HETATM 5772 O  O   . MSE E 1 4   ? 78.824  117.813 84.322  1.00 55.17 ? 1   MSE E O   1 
HETATM 5773 C  CB  . MSE E 1 4   ? 80.883  119.301 82.059  1.00 57.15 ? 1   MSE E CB  1 
HETATM 5774 C  CG  . MSE E 1 4   ? 79.989  120.483 82.358  1.00 59.16 ? 1   MSE E CG  1 
HETATM 5775 SE SE  . MSE E 1 4   ? 80.081  121.982 81.090  1.00 65.36 ? 1   MSE E SE  1 
HETATM 5776 C  CE  . MSE E 1 4   ? 82.068  122.328 80.901  1.00 61.54 ? 1   MSE E CE  1 
ATOM   5777 N  N   . GLY E 1 5   ? 79.111  116.944 82.252  1.00 52.78 ? 2   GLY E N   1 
ATOM   5778 C  CA  . GLY E 1 5   ? 77.883  116.154 82.241  1.00 49.44 ? 2   GLY E CA  1 
ATOM   5779 C  C   . GLY E 1 5   ? 77.916  115.074 83.306  1.00 47.12 ? 2   GLY E C   1 
ATOM   5780 O  O   . GLY E 1 5   ? 78.994  114.576 83.662  1.00 47.01 ? 2   GLY E O   1 
ATOM   5781 N  N   . LYS E 1 6   ? 76.740  114.719 83.817  1.00 44.29 ? 3   LYS E N   1 
ATOM   5782 C  CA  . LYS E 1 6   ? 76.643  113.842 84.975  1.00 41.76 ? 3   LYS E CA  1 
ATOM   5783 C  C   . LYS E 1 6   ? 75.860  112.574 84.629  1.00 40.33 ? 3   LYS E C   1 
ATOM   5784 O  O   . LYS E 1 6   ? 74.636  112.592 84.426  1.00 39.35 ? 3   LYS E O   1 
ATOM   5785 C  CB  . LYS E 1 6   ? 76.047  114.595 86.173  1.00 41.94 ? 3   LYS E CB  1 
ATOM   5786 C  CG  . LYS E 1 6   ? 76.963  115.713 86.741  1.00 41.58 ? 3   LYS E CG  1 
ATOM   5787 C  CD  . LYS E 1 6   ? 76.177  116.975 87.097  1.00 41.65 ? 3   LYS E CD  1 
ATOM   5788 C  CE  . LYS E 1 6   ? 75.538  116.888 88.482  1.00 42.26 ? 3   LYS E CE  1 
ATOM   5789 N  NZ  . LYS E 1 6   ? 74.324  117.750 88.644  1.00 40.89 ? 3   LYS E NZ  1 
ATOM   5790 N  N   . VAL E 1 7   ? 76.599  111.474 84.538  1.00 38.32 ? 4   VAL E N   1 
ATOM   5791 C  CA  . VAL E 1 7   ? 76.034  110.203 84.134  1.00 36.65 ? 4   VAL E CA  1 
ATOM   5792 C  C   . VAL E 1 7   ? 76.076  109.242 85.316  1.00 35.90 ? 4   VAL E C   1 
ATOM   5793 O  O   . VAL E 1 7   ? 77.126  109.008 85.907  1.00 36.07 ? 4   VAL E O   1 
ATOM   5794 C  CB  . VAL E 1 7   ? 76.737  109.630 82.855  1.00 36.48 ? 4   VAL E CB  1 
ATOM   5795 C  CG1 . VAL E 1 7   ? 76.368  108.166 82.612  1.00 35.63 ? 4   VAL E CG1 1 
ATOM   5796 C  CG2 . VAL E 1 7   ? 76.372  110.462 81.626  1.00 35.05 ? 4   VAL E CG2 1 
ATOM   5797 N  N   . LEU E 1 8   ? 74.911  108.716 85.663  1.00 34.57 ? 5   LEU E N   1 
ATOM   5798 C  CA  . LEU E 1 8   ? 74.793  107.684 86.667  1.00 33.72 ? 5   LEU E CA  1 
ATOM   5799 C  C   . LEU E 1 8   ? 74.615  106.362 85.927  1.00 33.03 ? 5   LEU E C   1 
ATOM   5800 O  O   . LEU E 1 8   ? 73.780  106.265 85.027  1.00 32.84 ? 5   LEU E O   1 
ATOM   5801 C  CB  . LEU E 1 8   ? 73.556  107.943 87.526  1.00 33.68 ? 5   LEU E CB  1 
ATOM   5802 C  CG  . LEU E 1 8   ? 73.369  107.408 88.950  1.00 33.83 ? 5   LEU E CG  1 
ATOM   5803 C  CD1 . LEU E 1 8   ? 71.988  106.837 89.061  1.00 30.59 ? 5   LEU E CD1 1 
ATOM   5804 C  CD2 . LEU E 1 8   ? 74.421  106.368 89.416  1.00 34.82 ? 5   LEU E CD2 1 
ATOM   5805 N  N   . VAL E 1 9   ? 75.416  105.360 86.281  1.00 32.33 ? 6   VAL E N   1 
ATOM   5806 C  CA  . VAL E 1 9   ? 75.170  103.989 85.834  1.00 31.78 ? 6   VAL E CA  1 
ATOM   5807 C  C   . VAL E 1 9   ? 74.821  103.166 87.068  1.00 31.68 ? 6   VAL E C   1 
ATOM   5808 O  O   . VAL E 1 9   ? 75.648  103.011 87.975  1.00 32.56 ? 6   VAL E O   1 
ATOM   5809 C  CB  . VAL E 1 9   ? 76.366  103.362 85.063  1.00 31.30 ? 6   VAL E CB  1 
ATOM   5810 C  CG1 . VAL E 1 9   ? 75.957  102.002 84.496  1.00 31.30 ? 6   VAL E CG1 1 
ATOM   5811 C  CG2 . VAL E 1 9   ? 76.801  104.257 83.936  1.00 29.90 ? 6   VAL E CG2 1 
ATOM   5812 N  N   . ILE E 1 10  ? 73.583  102.695 87.116  1.00 30.92 ? 7   ILE E N   1 
ATOM   5813 C  CA  . ILE E 1 10  ? 73.056  101.951 88.258  1.00 30.90 ? 7   ILE E CA  1 
ATOM   5814 C  C   . ILE E 1 10  ? 72.602  100.589 87.733  1.00 30.24 ? 7   ILE E C   1 
ATOM   5815 O  O   . ILE E 1 10  ? 72.019  100.504 86.655  1.00 30.70 ? 7   ILE E O   1 
ATOM   5816 C  CB  . ILE E 1 10  ? 71.898  102.749 88.994  1.00 31.25 ? 7   ILE E CB  1 
ATOM   5817 C  CG1 . ILE E 1 10  ? 71.114  101.850 89.966  1.00 32.25 ? 7   ILE E CG1 1 
ATOM   5818 C  CG2 . ILE E 1 10  ? 70.929  103.393 87.992  1.00 30.77 ? 7   ILE E CG2 1 
ATOM   5819 C  CD1 . ILE E 1 10  ? 70.056  102.578 90.817  1.00 31.12 ? 7   ILE E CD1 1 
ATOM   5820 N  N   . TYR E 1 11  ? 72.890  99.520  88.466  1.00 29.62 ? 8   TYR E N   1 
ATOM   5821 C  CA  . TYR E 1 11  ? 72.667  98.161  87.955  1.00 28.81 ? 8   TYR E CA  1 
ATOM   5822 C  C   . TYR E 1 11  ? 72.331  97.203  89.095  1.00 28.90 ? 8   TYR E C   1 
ATOM   5823 O  O   . TYR E 1 11  ? 72.711  97.451  90.237  1.00 29.17 ? 8   TYR E O   1 
ATOM   5824 C  CB  . TYR E 1 11  ? 73.914  97.659  87.196  1.00 28.26 ? 8   TYR E CB  1 
ATOM   5825 C  CG  . TYR E 1 11  ? 75.087  97.397  88.128  1.00 27.36 ? 8   TYR E CG  1 
ATOM   5826 C  CD1 . TYR E 1 11  ? 75.216  96.164  88.774  1.00 26.28 ? 8   TYR E CD1 1 
ATOM   5827 C  CD2 . TYR E 1 11  ? 76.022  98.395  88.410  1.00 24.73 ? 8   TYR E CD2 1 
ATOM   5828 C  CE1 . TYR E 1 11  ? 76.241  95.920  89.656  1.00 27.37 ? 8   TYR E CE1 1 
ATOM   5829 C  CE2 . TYR E 1 11  ? 77.070  98.164  89.307  1.00 26.80 ? 8   TYR E CE2 1 
ATOM   5830 C  CZ  . TYR E 1 11  ? 77.172  96.921  89.925  1.00 27.36 ? 8   TYR E CZ  1 
ATOM   5831 O  OH  . TYR E 1 11  ? 78.188  96.654  90.811  1.00 27.30 ? 8   TYR E OH  1 
ATOM   5832 N  N   . ASP E 1 12  ? 71.610  96.131  88.777  1.00 29.06 ? 9   ASP E N   1 
ATOM   5833 C  CA  . ASP E 1 12  ? 71.459  94.970  89.653  1.00 29.78 ? 9   ASP E CA  1 
ATOM   5834 C  C   . ASP E 1 12  ? 72.163  93.778  88.989  1.00 30.29 ? 9   ASP E C   1 
ATOM   5835 O  O   . ASP E 1 12  ? 72.413  93.790  87.777  1.00 29.86 ? 9   ASP E O   1 
ATOM   5836 C  CB  . ASP E 1 12  ? 69.964  94.654  89.916  1.00 29.98 ? 9   ASP E CB  1 
ATOM   5837 C  CG  . ASP E 1 12  ? 69.758  93.491  90.920  1.00 31.12 ? 9   ASP E CG  1 
ATOM   5838 O  OD1 . ASP E 1 12  ? 70.607  93.298  91.833  1.00 34.02 ? 9   ASP E OD1 1 
ATOM   5839 O  OD2 . ASP E 1 12  ? 68.752  92.759  90.809  1.00 29.85 ? 9   ASP E OD2 1 
ATOM   5840 N  N   . THR E 1 13  ? 72.499  92.758  89.771  1.00 30.97 ? 10  THR E N   1 
ATOM   5841 C  CA  . THR E 1 13  ? 73.127  91.572  89.209  1.00 32.08 ? 10  THR E CA  1 
ATOM   5842 C  C   . THR E 1 13  ? 72.994  90.385  90.158  1.00 33.32 ? 10  THR E C   1 
ATOM   5843 O  O   . THR E 1 13  ? 73.127  90.554  91.375  1.00 33.40 ? 10  THR E O   1 
ATOM   5844 C  CB  . THR E 1 13  ? 74.612  91.850  88.869  1.00 32.21 ? 10  THR E CB  1 
ATOM   5845 O  OG1 . THR E 1 13  ? 75.108  90.842  87.979  1.00 31.91 ? 10  THR E OG1 1 
ATOM   5846 C  CG2 . THR E 1 13  ? 75.478  91.904  90.132  1.00 32.14 ? 10  THR E CG2 1 
ATOM   5847 N  N   . ARG E 1 14  ? 72.703  89.193  89.627  1.00 34.65 ? 11  ARG E N   1 
ATOM   5848 C  CA  . ARG E 1 14  ? 72.745  87.995  90.479  1.00 36.44 ? 11  ARG E CA  1 
ATOM   5849 C  C   . ARG E 1 14  ? 74.026  87.202  90.299  1.00 35.76 ? 11  ARG E C   1 
ATOM   5850 O  O   . ARG E 1 14  ? 74.576  86.707  91.278  1.00 36.02 ? 11  ARG E O   1 
ATOM   5851 C  CB  . ARG E 1 14  ? 71.492  87.100  90.403  1.00 36.45 ? 11  ARG E CB  1 
ATOM   5852 C  CG  . ARG E 1 14  ? 70.967  86.760  91.856  1.00 38.78 ? 11  ARG E CG  1 
ATOM   5853 C  CD  . ARG E 1 14  ? 69.807  85.713  91.960  1.00 39.65 ? 11  ARG E CD  1 
ATOM   5854 N  NE  . ARG E 1 14  ? 68.487  86.198  91.491  1.00 45.31 ? 11  ARG E NE  1 
ATOM   5855 C  CZ  . ARG E 1 14  ? 67.476  86.613  92.270  1.00 45.96 ? 11  ARG E CZ  1 
ATOM   5856 N  NH1 . ARG E 1 14  ? 66.332  87.017  91.707  1.00 44.03 ? 11  ARG E NH1 1 
ATOM   5857 N  NH2 . ARG E 1 14  ? 67.593  86.631  93.606  1.00 45.38 ? 11  ARG E NH2 1 
ATOM   5858 N  N   . THR E 1 15  ? 74.524  87.101  89.073  1.00 35.33 ? 12  THR E N   1 
ATOM   5859 C  CA  . THR E 1 15  ? 75.779  86.361  88.863  1.00 35.26 ? 12  THR E CA  1 
ATOM   5860 C  C   . THR E 1 15  ? 77.014  87.221  88.530  1.00 34.38 ? 12  THR E C   1 
ATOM   5861 O  O   . THR E 1 15  ? 78.123  86.699  88.495  1.00 34.82 ? 12  THR E O   1 
ATOM   5862 C  CB  . THR E 1 15  ? 75.625  85.216  87.820  1.00 35.54 ? 12  THR E CB  1 
ATOM   5863 O  OG1 . THR E 1 15  ? 75.212  85.759  86.560  1.00 35.38 ? 12  THR E OG1 1 
ATOM   5864 C  CG2 . THR E 1 15  ? 74.597  84.182  88.301  1.00 36.56 ? 12  THR E CG2 1 
ATOM   5865 N  N   . GLY E 1 16  ? 76.831  88.519  88.301  1.00 33.15 ? 13  GLY E N   1 
ATOM   5866 C  CA  . GLY E 1 16  ? 77.940  89.377  87.896  1.00 31.28 ? 13  GLY E CA  1 
ATOM   5867 C  C   . GLY E 1 16  ? 77.949  89.846  86.446  1.00 30.36 ? 13  GLY E C   1 
ATOM   5868 O  O   . GLY E 1 16  ? 78.707  90.752  86.109  1.00 30.22 ? 13  GLY E O   1 
ATOM   5869 N  N   . ASN E 1 17  ? 77.109  89.259  85.586  1.00 29.23 ? 14  ASN E N   1 
ATOM   5870 C  CA  . ASN E 1 17  ? 77.121  89.593  84.148  1.00 28.30 ? 14  ASN E CA  1 
ATOM   5871 C  C   . ASN E 1 17  ? 76.696  91.024  83.827  1.00 27.91 ? 14  ASN E C   1 
ATOM   5872 O  O   . ASN E 1 17  ? 77.384  91.724  83.055  1.00 27.32 ? 14  ASN E O   1 
ATOM   5873 C  CB  . ASN E 1 17  ? 76.277  88.607  83.328  1.00 28.02 ? 14  ASN E CB  1 
ATOM   5874 C  CG  . ASN E 1 17  ? 76.788  87.184  83.418  1.00 27.45 ? 14  ASN E CG  1 
ATOM   5875 O  OD1 . ASN E 1 17  ? 77.982  86.951  83.647  1.00 24.34 ? 14  ASN E OD1 1 
ATOM   5876 N  ND2 . ASN E 1 17  ? 75.873  86.215  83.264  1.00 25.91 ? 14  ASN E ND2 1 
ATOM   5877 N  N   . THR E 1 18  ? 75.568  91.437  84.417  1.00 27.20 ? 15  THR E N   1 
ATOM   5878 C  CA  . THR E 1 18  ? 75.049  92.796  84.281  1.00 27.21 ? 15  THR E CA  1 
ATOM   5879 C  C   . THR E 1 18  ? 76.039  93.798  84.877  1.00 27.58 ? 15  THR E C   1 
ATOM   5880 O  O   . THR E 1 18  ? 76.175  94.907  84.364  1.00 27.11 ? 15  THR E O   1 
ATOM   5881 C  CB  . THR E 1 18  ? 73.602  92.947  84.876  1.00 27.06 ? 15  THR E CB  1 
ATOM   5882 O  OG1 . THR E 1 18  ? 72.755  91.947  84.308  1.00 27.16 ? 15  THR E OG1 1 
ATOM   5883 C  CG2 . THR E 1 18  ? 73.001  94.298  84.572  1.00 25.93 ? 15  THR E CG2 1 
ATOM   5884 N  N   . LYS E 1 19  ? 76.750  93.392  85.936  1.00 28.35 ? 16  LYS E N   1 
ATOM   5885 C  CA  . LYS E 1 19  ? 77.834  94.210  86.483  1.00 28.66 ? 16  LYS E CA  1 
ATOM   5886 C  C   . LYS E 1 19  ? 78.928  94.418  85.432  1.00 29.35 ? 16  LYS E C   1 
ATOM   5887 O  O   . LYS E 1 19  ? 79.390  95.541  85.222  1.00 29.31 ? 16  LYS E O   1 
ATOM   5888 C  CB  . LYS E 1 19  ? 78.407  93.609  87.774  1.00 28.70 ? 16  LYS E CB  1 
ATOM   5889 C  CG  . LYS E 1 19  ? 79.456  94.501  88.453  1.00 27.87 ? 16  LYS E CG  1 
ATOM   5890 C  CD  . LYS E 1 19  ? 80.001  93.892  89.731  1.00 28.50 ? 16  LYS E CD  1 
ATOM   5891 C  CE  . LYS E 1 19  ? 81.016  94.825  90.412  1.00 28.86 ? 16  LYS E CE  1 
ATOM   5892 N  NZ  . LYS E 1 19  ? 81.775  94.159  91.518  1.00 27.63 ? 16  LYS E NZ  1 
ATOM   5893 N  N   . LYS E 1 20  ? 79.339  93.346  84.760  1.00 30.26 ? 17  LYS E N   1 
ATOM   5894 C  CA  . LYS E 1 20  ? 80.317  93.485  83.683  1.00 31.24 ? 17  LYS E CA  1 
ATOM   5895 C  C   . LYS E 1 20  ? 79.845  94.465  82.618  1.00 31.51 ? 17  LYS E C   1 
ATOM   5896 O  O   . LYS E 1 20  ? 80.613  95.317  82.201  1.00 30.92 ? 17  LYS E O   1 
ATOM   5897 C  CB  . LYS E 1 20  ? 80.688  92.131  83.080  1.00 31.53 ? 17  LYS E CB  1 
ATOM   5898 C  CG  . LYS E 1 20  ? 81.982  91.585  83.653  1.00 33.90 ? 17  LYS E CG  1 
ATOM   5899 C  CD  . LYS E 1 20  ? 81.754  90.223  84.259  1.00 36.93 ? 17  LYS E CD  1 
ATOM   5900 C  CE  . LYS E 1 20  ? 82.734  89.963  85.396  1.00 39.06 ? 17  LYS E CE  1 
ATOM   5901 N  NZ  . LYS E 1 20  ? 82.006  89.315  86.540  1.00 40.40 ? 17  LYS E NZ  1 
HETATM 5902 N  N   . MSE E 1 21  ? 78.574  94.354  82.211  1.00 32.11 ? 18  MSE E N   1 
HETATM 5903 C  CA  . MSE E 1 21  ? 77.972  95.299  81.271  1.00 34.14 ? 18  MSE E CA  1 
HETATM 5904 C  C   . MSE E 1 21  ? 78.055  96.720  81.774  1.00 31.78 ? 18  MSE E C   1 
HETATM 5905 O  O   . MSE E 1 21  ? 78.477  97.608  81.052  1.00 31.94 ? 18  MSE E O   1 
HETATM 5906 C  CB  . MSE E 1 21  ? 76.508  94.972  81.021  1.00 33.29 ? 18  MSE E CB  1 
HETATM 5907 C  CG  . MSE E 1 21  ? 76.265  93.876  80.010  1.00 36.82 ? 18  MSE E CG  1 
HETATM 5908 SE SE  . MSE E 1 21  ? 74.331  93.501  79.791  1.00 43.42 ? 18  MSE E SE  1 
HETATM 5909 C  CE  . MSE E 1 21  ? 74.168  92.504  81.380  1.00 43.33 ? 18  MSE E CE  1 
ATOM   5910 N  N   . ALA E 1 22  ? 77.644  96.914  83.020  1.00 30.74 ? 19  ALA E N   1 
ATOM   5911 C  CA  . ALA E 1 22  ? 77.596  98.216  83.650  1.00 29.89 ? 19  ALA E CA  1 
ATOM   5912 C  C   . ALA E 1 22  ? 78.979  98.905  83.707  1.00 29.69 ? 19  ALA E C   1 
ATOM   5913 O  O   . ALA E 1 22  ? 79.082  100.120 83.462  1.00 29.61 ? 19  ALA E O   1 
ATOM   5914 C  CB  . ALA E 1 22  ? 76.973  98.103  85.027  1.00 29.38 ? 19  ALA E CB  1 
ATOM   5915 N  N   . GLU E 1 23  ? 80.028  98.134  83.992  1.00 28.93 ? 20  GLU E N   1 
ATOM   5916 C  CA  . GLU E 1 23  ? 81.399  98.669  84.014  1.00 29.13 ? 20  GLU E CA  1 
ATOM   5917 C  C   . GLU E 1 23  ? 81.801  99.169  82.631  1.00 28.64 ? 20  GLU E C   1 
ATOM   5918 O  O   . GLU E 1 23  ? 82.528  100.149 82.508  1.00 28.93 ? 20  GLU E O   1 
ATOM   5919 C  CB  . GLU E 1 23  ? 82.417  97.620  84.483  1.00 28.87 ? 20  GLU E CB  1 
ATOM   5920 C  CG  . GLU E 1 23  ? 82.232  97.091  85.907  1.00 29.20 ? 20  GLU E CG  1 
ATOM   5921 C  CD  . GLU E 1 23  ? 82.980  95.752  86.144  1.00 29.74 ? 20  GLU E CD  1 
ATOM   5922 O  OE1 . GLU E 1 23  ? 83.071  95.318  87.322  1.00 29.62 ? 20  GLU E OE1 1 
ATOM   5923 O  OE2 . GLU E 1 23  ? 83.455  95.126  85.156  1.00 28.86 ? 20  GLU E OE2 1 
ATOM   5924 N  N   . LEU E 1 24  ? 81.335  98.477  81.597  1.00 28.09 ? 21  LEU E N   1 
ATOM   5925 C  CA  . LEU E 1 24  ? 81.608  98.882  80.223  1.00 27.72 ? 21  LEU E CA  1 
ATOM   5926 C  C   . LEU E 1 24  ? 80.731  100.069 79.798  1.00 27.62 ? 21  LEU E C   1 
ATOM   5927 O  O   . LEU E 1 24  ? 81.238  101.025 79.207  1.00 27.91 ? 21  LEU E O   1 
ATOM   5928 C  CB  . LEU E 1 24  ? 81.485  97.702  79.250  1.00 27.28 ? 21  LEU E CB  1 
ATOM   5929 C  CG  . LEU E 1 24  ? 82.433  96.524  79.469  1.00 26.76 ? 21  LEU E CG  1 
ATOM   5930 C  CD1 . LEU E 1 24  ? 81.823  95.270  78.884  1.00 27.41 ? 21  LEU E CD1 1 
ATOM   5931 C  CD2 . LEU E 1 24  ? 83.836  96.778  78.893  1.00 26.61 ? 21  LEU E CD2 1 
ATOM   5932 N  N   . VAL E 1 25  ? 79.437  100.030 80.112  1.00 26.86 ? 22  VAL E N   1 
ATOM   5933 C  CA  . VAL E 1 25  ? 78.588  101.210 79.906  1.00 26.91 ? 22  VAL E CA  1 
ATOM   5934 C  C   . VAL E 1 25  ? 79.272  102.491 80.472  1.00 27.41 ? 22  VAL E C   1 
ATOM   5935 O  O   . VAL E 1 25  ? 79.391  103.509 79.778  1.00 26.83 ? 22  VAL E O   1 
ATOM   5936 C  CB  . VAL E 1 25  ? 77.170  101.011 80.501  1.00 26.48 ? 22  VAL E CB  1 
ATOM   5937 C  CG1 . VAL E 1 25  ? 76.402  102.284 80.452  1.00 26.30 ? 22  VAL E CG1 1 
ATOM   5938 C  CG2 . VAL E 1 25  ? 76.408  99.926  79.733  1.00 26.44 ? 22  VAL E CG2 1 
ATOM   5939 N  N   . ALA E 1 26  ? 79.748  102.404 81.717  1.00 27.71 ? 23  ALA E N   1 
ATOM   5940 C  CA  . ALA E 1 26  ? 80.383  103.519 82.406  1.00 28.13 ? 23  ALA E CA  1 
ATOM   5941 C  C   . ALA E 1 26  ? 81.693  103.939 81.728  1.00 28.55 ? 23  ALA E C   1 
ATOM   5942 O  O   . ALA E 1 26  ? 82.022  105.124 81.665  1.00 28.31 ? 23  ALA E O   1 
ATOM   5943 C  CB  . ALA E 1 26  ? 80.620  103.162 83.868  1.00 28.22 ? 23  ALA E CB  1 
ATOM   5944 N  N   . GLU E 1 27  ? 82.424  102.952 81.218  1.00 28.92 ? 24  GLU E N   1 
ATOM   5945 C  CA  . GLU E 1 27  ? 83.625  103.182 80.434  1.00 29.45 ? 24  GLU E CA  1 
ATOM   5946 C  C   . GLU E 1 27  ? 83.294  104.012 79.193  1.00 28.78 ? 24  GLU E C   1 
ATOM   5947 O  O   . GLU E 1 27  ? 83.988  104.985 78.887  1.00 28.92 ? 24  GLU E O   1 
ATOM   5948 C  CB  . GLU E 1 27  ? 84.259  101.834 80.050  1.00 29.37 ? 24  GLU E CB  1 
ATOM   5949 C  CG  . GLU E 1 27  ? 85.603  101.905 79.298  1.00 30.67 ? 24  GLU E CG  1 
ATOM   5950 C  CD  . GLU E 1 27  ? 86.072  100.523 78.836  1.00 31.71 ? 24  GLU E CD  1 
ATOM   5951 O  OE1 . GLU E 1 27  ? 85.731  99.519  79.504  1.00 37.07 ? 24  GLU E OE1 1 
ATOM   5952 O  OE2 . GLU E 1 27  ? 86.775  100.422 77.810  1.00 33.84 ? 24  GLU E OE2 1 
ATOM   5953 N  N   . GLY E 1 28  ? 82.242  103.612 78.482  1.00 28.46 ? 25  GLY E N   1 
ATOM   5954 C  CA  . GLY E 1 28  ? 81.727  104.366 77.346  1.00 28.12 ? 25  GLY E CA  1 
ATOM   5955 C  C   . GLY E 1 28  ? 81.407  105.827 77.637  1.00 28.09 ? 25  GLY E C   1 
ATOM   5956 O  O   . GLY E 1 28  ? 81.732  106.694 76.831  1.00 27.80 ? 25  GLY E O   1 
ATOM   5957 N  N   . ALA E 1 29  ? 80.761  106.093 78.776  1.00 28.20 ? 26  ALA E N   1 
ATOM   5958 C  CA  . ALA E 1 29  ? 80.443  107.450 79.205  1.00 28.38 ? 26  ALA E CA  1 
ATOM   5959 C  C   . ALA E 1 29  ? 81.718  108.219 79.571  1.00 29.62 ? 26  ALA E C   1 
ATOM   5960 O  O   . ALA E 1 29  ? 81.815  109.437 79.369  1.00 29.88 ? 26  ALA E O   1 
ATOM   5961 C  CB  . ALA E 1 29  ? 79.497  107.408 80.375  1.00 27.73 ? 26  ALA E CB  1 
ATOM   5962 N  N   . ARG E 1 30  ? 82.704  107.513 80.112  1.00 30.32 ? 27  ARG E N   1 
ATOM   5963 C  CA  . ARG E 1 30  ? 83.960  108.149 80.447  1.00 31.37 ? 27  ARG E CA  1 
ATOM   5964 C  C   . ARG E 1 30  ? 84.770  108.544 79.202  1.00 31.59 ? 27  ARG E C   1 
ATOM   5965 O  O   . ARG E 1 30  ? 85.465  109.550 79.226  1.00 31.23 ? 27  ARG E O   1 
ATOM   5966 C  CB  . ARG E 1 30  ? 84.749  107.312 81.464  1.00 31.15 ? 27  ARG E CB  1 
ATOM   5967 C  CG  . ARG E 1 30  ? 84.171  107.436 82.887  1.00 31.43 ? 27  ARG E CG  1 
ATOM   5968 C  CD  . ARG E 1 30  ? 85.076  106.834 83.957  1.00 32.25 ? 27  ARG E CD  1 
ATOM   5969 N  NE  . ARG E 1 30  ? 84.623  105.521 84.418  1.00 34.36 ? 27  ARG E NE  1 
ATOM   5970 C  CZ  . ARG E 1 30  ? 83.965  105.307 85.562  1.00 34.82 ? 27  ARG E CZ  1 
ATOM   5971 N  NH1 . ARG E 1 30  ? 83.605  104.074 85.894  1.00 33.58 ? 27  ARG E NH1 1 
ATOM   5972 N  NH2 . ARG E 1 30  ? 83.677  106.316 86.385  1.00 34.56 ? 27  ARG E NH2 1 
ATOM   5973 N  N   . SER E 1 31  ? 84.611  107.809 78.101  1.00 32.66 ? 28  SER E N   1 
ATOM   5974 C  CA  . SER E 1 31  ? 85.378  108.083 76.869  1.00 33.66 ? 28  SER E CA  1 
ATOM   5975 C  C   . SER E 1 31  ? 85.051  109.428 76.216  1.00 34.18 ? 28  SER E C   1 
ATOM   5976 O  O   . SER E 1 31  ? 85.886  109.983 75.482  1.00 34.08 ? 28  SER E O   1 
ATOM   5977 C  CB  . SER E 1 31  ? 85.225  106.951 75.840  1.00 33.68 ? 28  SER E CB  1 
ATOM   5978 O  OG  . SER E 1 31  ? 83.946  106.976 75.228  1.00 34.04 ? 28  SER E OG  1 
ATOM   5979 N  N   . LEU E 1 32  ? 83.835  109.931 76.454  1.00 35.12 ? 29  LEU E N   1 
ATOM   5980 C  CA  . LEU E 1 32  ? 83.515  111.329 76.130  1.00 36.02 ? 29  LEU E CA  1 
ATOM   5981 C  C   . LEU E 1 32  ? 84.078  112.284 77.202  1.00 36.69 ? 29  LEU E C   1 
ATOM   5982 O  O   . LEU E 1 32  ? 83.681  112.238 78.373  1.00 37.02 ? 29  LEU E O   1 
ATOM   5983 C  CB  . LEU E 1 32  ? 82.008  111.529 75.943  1.00 35.68 ? 29  LEU E CB  1 
ATOM   5984 C  CG  . LEU E 1 32  ? 81.603  112.910 75.419  1.00 35.68 ? 29  LEU E CG  1 
ATOM   5985 C  CD1 . LEU E 1 32  ? 81.844  113.043 73.911  1.00 36.04 ? 29  LEU E CD1 1 
ATOM   5986 C  CD2 . LEU E 1 32  ? 80.162  113.191 75.753  1.00 34.60 ? 29  LEU E CD2 1 
ATOM   5987 N  N   . GLU E 1 33  ? 85.008  113.145 76.803  1.00 37.52 ? 30  GLU E N   1 
ATOM   5988 C  CA  . GLU E 1 33  ? 85.705  113.989 77.785  1.00 38.57 ? 30  GLU E CA  1 
ATOM   5989 C  C   . GLU E 1 33  ? 84.801  115.120 78.323  1.00 38.61 ? 30  GLU E C   1 
ATOM   5990 O  O   . GLU E 1 33  ? 83.610  115.415 77.591  1.00 39.32 ? 30  GLU E O   1 
ATOM   5991 C  CB  . GLU E 1 33  ? 87.019  114.521 77.216  1.00 38.77 ? 30  GLU E CB  1 
ATOM   5992 C  CG  . GLU E 1 33  ? 86.939  115.925 76.588  1.00 40.89 ? 30  GLU E CG  1 
ATOM   5993 C  CD  . GLU E 1 33  ? 86.508  115.924 75.121  1.00 42.06 ? 30  GLU E CD  1 
ATOM   5994 O  OE1 . GLU E 1 33  ? 87.309  116.665 74.328  1.00 40.47 ? 30  GLU E OE1 1 
ATOM   5995 O  OE2 . GLU E 1 33  ? 85.399  115.201 74.768  1.00 41.79 ? 30  GLU E OE2 1 
ATOM   5996 N  N   . GLY E 1 34  ? 85.064  115.733 79.592  1.00 38.06 ? 31  GLY E N   1 
ATOM   5997 C  CA  . GLY E 1 34  ? 84.055  116.570 80.339  1.00 37.26 ? 31  GLY E CA  1 
ATOM   5998 C  C   . GLY E 1 34  ? 82.792  115.784 80.499  1.00 36.53 ? 31  GLY E C   1 
ATOM   5999 O  O   . GLY E 1 34  ? 81.654  116.294 80.091  1.00 36.67 ? 31  GLY E O   1 
ATOM   6000 N  N   . THR E 1 35  ? 83.018  114.552 81.096  1.00 35.78 ? 32  THR E N   1 
ATOM   6001 C  CA  . THR E 1 35  ? 81.825  113.826 81.624  1.00 35.29 ? 32  THR E CA  1 
ATOM   6002 C  C   . THR E 1 35  ? 82.242  113.156 82.949  1.00 35.09 ? 32  THR E C   1 
ATOM   6003 O  O   . THR E 1 35  ? 83.346  112.559 83.022  1.00 34.80 ? 32  THR E O   1 
ATOM   6004 C  CB  . THR E 1 35  ? 81.281  112.694 80.632  1.00 35.14 ? 32  THR E CB  1 
ATOM   6005 O  OG1 . THR E 1 35  ? 80.736  113.274 79.349  1.00 34.57 ? 32  THR E OG1 1 
ATOM   6006 C  CG2 . THR E 1 35  ? 80.141  111.854 81.341  1.00 33.97 ? 32  THR E CG2 1 
ATOM   6007 N  N   . GLU E 1 36  ? 81.372  113.266 83.990  1.00 34.63 ? 33  GLU E N   1 
ATOM   6008 C  CA  . GLU E 1 36  ? 81.600  112.535 85.239  1.00 34.12 ? 33  GLU E CA  1 
ATOM   6009 C  C   . GLU E 1 36  ? 80.620  111.367 85.368  1.00 33.32 ? 33  GLU E C   1 
ATOM   6010 O  O   . GLU E 1 36  ? 79.458  111.495 85.020  1.00 33.36 ? 33  GLU E O   1 
ATOM   6011 C  CB  . GLU E 1 36  ? 81.478  113.453 86.443  1.00 34.23 ? 33  GLU E CB  1 
ATOM   6012 C  CG  . GLU E 1 36  ? 82.197  112.894 87.665  1.00 35.94 ? 33  GLU E CG  1 
ATOM   6013 C  CD  . GLU E 1 36  ? 81.868  113.664 88.921  1.00 37.58 ? 33  GLU E CD  1 
ATOM   6014 O  OE1 . GLU E 1 36  ? 82.406  114.819 89.070  1.00 36.36 ? 33  GLU E OE1 1 
ATOM   6015 O  OE2 . GLU E 1 36  ? 81.065  113.109 89.750  1.00 39.14 ? 33  GLU E OE2 1 
ATOM   6016 N  N   . VAL E 1 37  ? 81.095  110.238 85.879  1.00 32.53 ? 34  VAL E N   1 
ATOM   6017 C  CA  . VAL E 1 37  ? 80.312  109.013 85.893  1.00 32.14 ? 34  VAL E CA  1 
ATOM   6018 C  C   . VAL E 1 37  ? 80.291  108.325 87.266  1.00 31.96 ? 34  VAL E C   1 
ATOM   6019 O  O   . VAL E 1 37  ? 81.330  108.027 87.836  1.00 31.95 ? 34  VAL E O   1 
ATOM   6020 C  CB  . VAL E 1 37  ? 80.806  108.022 84.791  1.00 32.26 ? 34  VAL E CB  1 
ATOM   6021 C  CG1 . VAL E 1 37  ? 79.803  106.875 84.576  1.00 31.03 ? 34  VAL E CG1 1 
ATOM   6022 C  CG2 . VAL E 1 37  ? 81.053  108.767 83.478  1.00 32.17 ? 34  VAL E CG2 1 
ATOM   6023 N  N   . ARG E 1 38  ? 79.095  108.070 87.783  1.00 31.83 ? 35  ARG E N   1 
ATOM   6024 C  CA  . ARG E 1 38  ? 78.929  107.268 88.996  1.00 31.76 ? 35  ARG E CA  1 
ATOM   6025 C  C   . ARG E 1 38  ? 78.522  105.837 88.657  1.00 31.27 ? 35  ARG E C   1 
ATOM   6026 O  O   . ARG E 1 38  ? 77.541  105.619 87.958  1.00 31.47 ? 35  ARG E O   1 
ATOM   6027 C  CB  . ARG E 1 38  ? 77.862  107.889 89.886  1.00 31.88 ? 35  ARG E CB  1 
ATOM   6028 C  CG  . ARG E 1 38  ? 78.387  108.557 91.110  1.00 32.46 ? 35  ARG E CG  1 
ATOM   6029 C  CD  . ARG E 1 38  ? 77.834  109.950 91.213  1.00 33.93 ? 35  ARG E CD  1 
ATOM   6030 N  NE  . ARG E 1 38  ? 77.235  110.203 92.517  1.00 35.98 ? 35  ARG E NE  1 
ATOM   6031 C  CZ  . ARG E 1 38  ? 77.236  111.384 93.128  1.00 37.31 ? 35  ARG E CZ  1 
ATOM   6032 N  NH1 . ARG E 1 38  ? 77.830  112.431 92.570  1.00 36.74 ? 35  ARG E NH1 1 
ATOM   6033 N  NH2 . ARG E 1 38  ? 76.657  111.515 94.315  1.00 38.66 ? 35  ARG E NH2 1 
ATOM   6034 N  N   . LEU E 1 39  ? 79.260  104.858 89.162  1.00 30.68 ? 36  LEU E N   1 
ATOM   6035 C  CA  . LEU E 1 39  ? 78.865  103.475 88.964  1.00 30.43 ? 36  LEU E CA  1 
ATOM   6036 C  C   . LEU E 1 39  ? 78.398  102.868 90.283  1.00 30.68 ? 36  LEU E C   1 
ATOM   6037 O  O   . LEU E 1 39  ? 79.204  102.591 91.149  1.00 30.49 ? 36  LEU E O   1 
ATOM   6038 C  CB  . LEU E 1 39  ? 79.997  102.671 88.322  1.00 30.22 ? 36  LEU E CB  1 
ATOM   6039 C  CG  . LEU E 1 39  ? 79.824  101.159 88.145  1.00 30.59 ? 36  LEU E CG  1 
ATOM   6040 C  CD1 . LEU E 1 39  ? 78.635  100.817 87.247  1.00 29.32 ? 36  LEU E CD1 1 
ATOM   6041 C  CD2 . LEU E 1 39  ? 81.101  100.566 87.593  1.00 29.30 ? 36  LEU E CD2 1 
ATOM   6042 N  N   . LYS E 1 40  ? 77.089  102.664 90.425  1.00 31.15 ? 37  LYS E N   1 
ATOM   6043 C  CA  . LYS E 1 40  ? 76.512  102.159 91.681  1.00 31.35 ? 37  LYS E CA  1 
ATOM   6044 C  C   . LYS E 1 40  ? 75.626  100.924 91.488  1.00 31.53 ? 37  LYS E C   1 
ATOM   6045 O  O   . LYS E 1 40  ? 74.766  100.886 90.598  1.00 31.76 ? 37  LYS E O   1 
ATOM   6046 C  CB  . LYS E 1 40  ? 75.717  103.268 92.403  1.00 31.40 ? 37  LYS E CB  1 
ATOM   6047 C  CG  . LYS E 1 40  ? 76.431  103.974 93.582  1.00 30.96 ? 37  LYS E CG  1 
ATOM   6048 C  CD  . LYS E 1 40  ? 77.595  104.870 93.145  1.00 31.68 ? 37  LYS E CD  1 
ATOM   6049 C  CE  . LYS E 1 40  ? 78.459  105.326 94.347  1.00 31.97 ? 37  LYS E CE  1 
ATOM   6050 N  NZ  . LYS E 1 40  ? 79.883  105.614 93.958  1.00 30.91 ? 37  LYS E NZ  1 
ATOM   6051 N  N   . HIS E 1 41  ? 75.852  99.909  92.319  1.00 31.63 ? 38  HIS E N   1 
ATOM   6052 C  CA  . HIS E 1 41  ? 74.909  98.796  92.471  1.00 31.85 ? 38  HIS E CA  1 
ATOM   6053 C  C   . HIS E 1 41  ? 73.630  99.358  93.133  1.00 32.08 ? 38  HIS E C   1 
ATOM   6054 O  O   . HIS E 1 41  ? 73.711  100.333 93.891  1.00 32.21 ? 38  HIS E O   1 
ATOM   6055 C  CB  . HIS E 1 41  ? 75.553  97.707  93.347  1.00 31.43 ? 38  HIS E CB  1 
ATOM   6056 C  CG  . HIS E 1 41  ? 74.810  96.406  93.362  1.00 31.14 ? 38  HIS E CG  1 
ATOM   6057 N  ND1 . HIS E 1 41  ? 73.583  96.250  93.972  1.00 31.41 ? 38  HIS E ND1 1 
ATOM   6058 C  CD2 . HIS E 1 41  ? 75.137  95.191  92.865  1.00 31.48 ? 38  HIS E CD2 1 
ATOM   6059 C  CE1 . HIS E 1 41  ? 73.174  95.003  93.826  1.00 30.64 ? 38  HIS E CE1 1 
ATOM   6060 N  NE2 . HIS E 1 41  ? 74.102  94.338  93.161  1.00 31.03 ? 38  HIS E NE2 1 
ATOM   6061 N  N   . VAL E 1 42  ? 72.465  98.770  92.855  1.00 32.36 ? 39  VAL E N   1 
ATOM   6062 C  CA  . VAL E 1 42  ? 71.198  99.236  93.477  1.00 32.84 ? 39  VAL E CA  1 
ATOM   6063 C  C   . VAL E 1 42  ? 71.235  99.308  95.000  1.00 33.34 ? 39  VAL E C   1 
ATOM   6064 O  O   . VAL E 1 42  ? 70.458  100.041 95.598  1.00 33.63 ? 39  VAL E O   1 
ATOM   6065 C  CB  . VAL E 1 42  ? 69.988  98.304  93.213  1.00 32.40 ? 39  VAL E CB  1 
ATOM   6066 C  CG1 . VAL E 1 42  ? 68.827  99.101  92.723  1.00 32.38 ? 39  VAL E CG1 1 
ATOM   6067 C  CG2 . VAL E 1 42  ? 70.316  97.221  92.280  1.00 32.48 ? 39  VAL E CG2 1 
ATOM   6068 N  N   . ASP E 1 43  ? 72.078  98.490  95.621  1.00 34.22 ? 40  ASP E N   1 
ATOM   6069 C  CA  . ASP E 1 43  ? 72.144  98.397  97.072  1.00 35.01 ? 40  ASP E CA  1 
ATOM   6070 C  C   . ASP E 1 43  ? 72.920  99.567  97.666  1.00 35.20 ? 40  ASP E C   1 
ATOM   6071 O  O   . ASP E 1 43  ? 72.755  99.875  98.853  1.00 35.93 ? 40  ASP E O   1 
ATOM   6072 C  CB  . ASP E 1 43  ? 72.801  97.076  97.514  1.00 35.71 ? 40  ASP E CB  1 
ATOM   6073 C  CG  . ASP E 1 43  ? 72.004  95.824  97.090  1.00 36.74 ? 40  ASP E CG  1 
ATOM   6074 O  OD1 . ASP E 1 43  ? 72.636  94.735  97.044  1.00 38.19 ? 40  ASP E OD1 1 
ATOM   6075 O  OD2 . ASP E 1 43  ? 70.776  95.912  96.819  1.00 35.23 ? 40  ASP E OD2 1 
ATOM   6076 N  N   . GLU E 1 44  ? 73.780  100.201 96.865  1.00 35.24 ? 41  GLU E N   1 
ATOM   6077 C  CA  . GLU E 1 44  ? 74.525  101.386 97.325  1.00 35.32 ? 41  GLU E CA  1 
ATOM   6078 C  C   . GLU E 1 44  ? 73.876  102.680 96.884  1.00 35.16 ? 41  GLU E C   1 
ATOM   6079 O  O   . GLU E 1 44  ? 73.977  103.691 97.567  1.00 35.21 ? 41  GLU E O   1 
ATOM   6080 C  CB  . GLU E 1 44  ? 75.954  101.419 96.804  1.00 35.49 ? 41  GLU E CB  1 
ATOM   6081 C  CG  . GLU E 1 44  ? 76.518  100.135 96.285  1.00 36.81 ? 41  GLU E CG  1 
ATOM   6082 C  CD  . GLU E 1 44  ? 77.856  100.374 95.624  1.00 38.33 ? 41  GLU E CD  1 
ATOM   6083 O  OE1 . GLU E 1 44  ? 78.025  99.962  94.439  1.00 37.73 ? 41  GLU E OE1 1 
ATOM   6084 O  OE2 . GLU E 1 44  ? 78.723  100.999 96.298  1.00 38.08 ? 41  GLU E OE2 1 
ATOM   6085 N  N   . ALA E 1 45  ? 73.226  102.650 95.723  1.00 35.19 ? 42  ALA E N   1 
ATOM   6086 C  CA  . ALA E 1 45  ? 72.657  103.847 95.133  1.00 34.85 ? 42  ALA E CA  1 
ATOM   6087 C  C   . ALA E 1 45  ? 71.621  104.507 96.053  1.00 34.86 ? 42  ALA E C   1 
ATOM   6088 O  O   . ALA E 1 45  ? 70.969  103.825 96.854  1.00 34.97 ? 42  ALA E O   1 
ATOM   6089 C  CB  . ALA E 1 45  ? 72.067  103.511 93.810  1.00 34.66 ? 42  ALA E CB  1 
ATOM   6090 N  N   . THR E 1 46  ? 71.499  105.829 95.951  1.00 34.61 ? 43  THR E N   1 
ATOM   6091 C  CA  . THR E 1 46  ? 70.541  106.596 96.754  1.00 34.92 ? 43  THR E CA  1 
ATOM   6092 C  C   . THR E 1 46  ? 69.790  107.576 95.858  1.00 34.88 ? 43  THR E C   1 
ATOM   6093 O  O   . THR E 1 46  ? 70.148  107.739 94.695  1.00 35.20 ? 43  THR E O   1 
ATOM   6094 C  CB  . THR E 1 46  ? 71.245  107.406 97.874  1.00 35.00 ? 43  THR E CB  1 
ATOM   6095 O  OG1 . THR E 1 46  ? 72.110  108.380 97.283  1.00 34.69 ? 43  THR E OG1 1 
ATOM   6096 C  CG2 . THR E 1 46  ? 72.062  106.499 98.821  1.00 35.25 ? 43  THR E CG2 1 
ATOM   6097 N  N   . LYS E 1 47  ? 68.757  108.225 96.399  1.00 34.75 ? 44  LYS E N   1 
ATOM   6098 C  CA  . LYS E 1 47  ? 68.049  109.312 95.707  1.00 34.45 ? 44  LYS E CA  1 
ATOM   6099 C  C   . LYS E 1 47  ? 68.990  110.443 95.261  1.00 33.89 ? 44  LYS E C   1 
ATOM   6100 O  O   . LYS E 1 47  ? 68.765  111.056 94.219  1.00 33.87 ? 44  LYS E O   1 
ATOM   6101 C  CB  . LYS E 1 47  ? 66.956  109.934 96.593  1.00 34.61 ? 44  LYS E CB  1 
ATOM   6102 C  CG  . LYS E 1 47  ? 66.271  109.015 97.609  1.00 35.50 ? 44  LYS E CG  1 
ATOM   6103 C  CD  . LYS E 1 47  ? 65.789  109.808 98.860  1.00 35.09 ? 44  LYS E CD  1 
ATOM   6104 C  CE  . LYS E 1 47  ? 64.410  110.458 98.656  1.00 36.06 ? 44  LYS E CE  1 
ATOM   6105 N  NZ  . LYS E 1 47  ? 64.142  111.593 99.606  1.00 34.11 ? 44  LYS E NZ  1 
ATOM   6106 N  N   . GLU E 1 48  ? 70.020  110.735 96.063  1.00 33.50 ? 45  GLU E N   1 
ATOM   6107 C  CA  . GLU E 1 48  ? 70.982  111.819 95.758  1.00 33.02 ? 45  GLU E CA  1 
ATOM   6108 C  C   . GLU E 1 48  ? 71.717  111.553 94.445  1.00 32.10 ? 45  GLU E C   1 
ATOM   6109 O  O   . GLU E 1 48  ? 71.941  112.474 93.659  1.00 32.01 ? 45  GLU E O   1 
ATOM   6110 C  CB  . GLU E 1 48  ? 71.994  112.032 96.894  1.00 33.26 ? 45  GLU E CB  1 
ATOM   6111 C  CG  . GLU E 1 48  ? 71.447  112.717 98.146  1.00 35.24 ? 45  GLU E CG  1 
ATOM   6112 C  CD  . GLU E 1 48  ? 70.311  111.937 98.812  1.00 38.01 ? 45  GLU E CD  1 
ATOM   6113 O  OE1 . GLU E 1 48  ? 70.410  110.690 98.930  1.00 38.73 ? 45  GLU E OE1 1 
ATOM   6114 O  OE2 . GLU E 1 48  ? 69.309  112.576 99.210  1.00 38.85 ? 45  GLU E OE2 1 
ATOM   6115 N  N   . ASP E 1 49  ? 72.075  110.290 94.214  1.00 31.02 ? 46  ASP E N   1 
ATOM   6116 C  CA  . ASP E 1 49  ? 72.698  109.874 92.959  1.00 30.21 ? 46  ASP E CA  1 
ATOM   6117 C  C   . ASP E 1 49  ? 71.845  110.244 91.752  1.00 29.43 ? 46  ASP E C   1 
ATOM   6118 O  O   . ASP E 1 49  ? 72.362  110.707 90.746  1.00 29.58 ? 46  ASP E O   1 
ATOM   6119 C  CB  . ASP E 1 49  ? 73.004  108.373 92.982  1.00 30.23 ? 46  ASP E CB  1 
ATOM   6120 C  CG  . ASP E 1 49  ? 74.109  108.012 93.972  1.00 30.12 ? 46  ASP E CG  1 
ATOM   6121 O  OD1 . ASP E 1 49  ? 74.759  108.935 94.526  1.00 30.50 ? 46  ASP E OD1 1 
ATOM   6122 O  OD2 . ASP E 1 49  ? 74.334  106.802 94.191  1.00 29.32 ? 46  ASP E OD2 1 
ATOM   6123 N  N   . VAL E 1 50  ? 70.532  110.076 91.884  1.00 28.94 ? 47  VAL E N   1 
ATOM   6124 C  CA  . VAL E 1 50  ? 69.566  110.399 90.827  1.00 27.85 ? 47  VAL E CA  1 
ATOM   6125 C  C   . VAL E 1 50  ? 69.293  111.913 90.681  1.00 28.12 ? 47  VAL E C   1 
ATOM   6126 O  O   . VAL E 1 50  ? 69.193  112.434 89.563  1.00 27.87 ? 47  VAL E O   1 
ATOM   6127 C  CB  . VAL E 1 50  ? 68.281  109.592 91.042  1.00 27.78 ? 47  VAL E CB  1 
ATOM   6128 C  CG1 . VAL E 1 50  ? 67.243  109.879 89.958  1.00 26.01 ? 47  VAL E CG1 1 
ATOM   6129 C  CG2 . VAL E 1 50  ? 68.633  108.112 91.085  1.00 26.81 ? 47  VAL E CG2 1 
ATOM   6130 N  N   . LEU E 1 51  ? 69.197  112.622 91.804  1.00 27.96 ? 48  LEU E N   1 
ATOM   6131 C  CA  . LEU E 1 51  ? 69.103  114.077 91.758  1.00 28.63 ? 48  LEU E CA  1 
ATOM   6132 C  C   . LEU E 1 51  ? 70.335  114.679 91.088  1.00 29.10 ? 48  LEU E C   1 
ATOM   6133 O  O   . LEU E 1 51  ? 70.233  115.623 90.307  1.00 29.21 ? 48  LEU E O   1 
ATOM   6134 C  CB  . LEU E 1 51  ? 68.936  114.650 93.164  1.00 28.22 ? 48  LEU E CB  1 
ATOM   6135 C  CG  . LEU E 1 51  ? 67.691  114.185 93.903  1.00 28.43 ? 48  LEU E CG  1 
ATOM   6136 C  CD1 . LEU E 1 51  ? 67.779  114.527 95.383  1.00 27.18 ? 48  LEU E CD1 1 
ATOM   6137 C  CD2 . LEU E 1 51  ? 66.447  114.787 93.256  1.00 28.92 ? 48  LEU E CD2 1 
ATOM   6138 N  N   . TRP E 1 52  ? 71.493  114.111 91.405  1.00 29.74 ? 49  TRP E N   1 
ATOM   6139 C  CA  . TRP E 1 52  ? 72.764  114.492 90.812  1.00 30.51 ? 49  TRP E CA  1 
ATOM   6140 C  C   . TRP E 1 52  ? 72.761  114.359 89.289  1.00 30.75 ? 49  TRP E C   1 
ATOM   6141 O  O   . TRP E 1 52  ? 73.026  115.324 88.587  1.00 31.63 ? 49  TRP E O   1 
ATOM   6142 C  CB  . TRP E 1 52  ? 73.858  113.618 91.421  1.00 30.73 ? 49  TRP E CB  1 
ATOM   6143 C  CG  . TRP E 1 52  ? 75.222  113.787 90.864  1.00 30.73 ? 49  TRP E CG  1 
ATOM   6144 C  CD1 . TRP E 1 52  ? 76.113  114.760 91.178  1.00 31.51 ? 49  TRP E CD1 1 
ATOM   6145 C  CD2 . TRP E 1 52  ? 75.878  112.924 89.930  1.00 31.15 ? 49  TRP E CD2 1 
ATOM   6146 N  NE1 . TRP E 1 52  ? 77.277  114.579 90.480  1.00 31.73 ? 49  TRP E NE1 1 
ATOM   6147 C  CE2 . TRP E 1 52  ? 77.164  113.454 89.709  1.00 30.62 ? 49  TRP E CE2 1 
ATOM   6148 C  CE3 . TRP E 1 52  ? 75.499  111.762 89.252  1.00 30.68 ? 49  TRP E CE3 1 
ATOM   6149 C  CZ2 . TRP E 1 52  ? 78.085  112.862 88.843  1.00 30.14 ? 49  TRP E CZ2 1 
ATOM   6150 C  CZ3 . TRP E 1 52  ? 76.410  111.179 88.382  1.00 31.66 ? 49  TRP E CZ3 1 
ATOM   6151 C  CH2 . TRP E 1 52  ? 77.699  111.732 88.195  1.00 30.87 ? 49  TRP E CH2 1 
ATOM   6152 N  N   . ALA E 1 53  ? 72.434  113.170 88.795  1.00 30.72 ? 50  ALA E N   1 
ATOM   6153 C  CA  . ALA E 1 53  ? 72.596  112.810 87.381  1.00 30.76 ? 50  ALA E CA  1 
ATOM   6154 C  C   . ALA E 1 53  ? 71.715  113.553 86.370  1.00 30.87 ? 50  ALA E C   1 
ATOM   6155 O  O   . ALA E 1 53  ? 70.511  113.707 86.582  1.00 31.22 ? 50  ALA E O   1 
ATOM   6156 C  CB  . ALA E 1 53  ? 72.417  111.309 87.219  1.00 30.44 ? 50  ALA E CB  1 
ATOM   6157 N  N   . ASP E 1 54  ? 72.337  113.986 85.272  1.00 31.05 ? 51  ASP E N   1 
ATOM   6158 C  CA  . ASP E 1 54  ? 71.655  114.457 84.067  1.00 31.13 ? 51  ASP E CA  1 
ATOM   6159 C  C   . ASP E 1 54  ? 71.156  113.279 83.237  1.00 31.53 ? 51  ASP E C   1 
ATOM   6160 O  O   . ASP E 1 54  ? 70.003  113.258 82.791  1.00 32.33 ? 51  ASP E O   1 
ATOM   6161 C  CB  . ASP E 1 54  ? 72.615  115.257 83.190  1.00 31.32 ? 51  ASP E CB  1 
ATOM   6162 C  CG  . ASP E 1 54  ? 73.183  116.468 83.882  1.00 31.05 ? 51  ASP E CG  1 
ATOM   6163 O  OD1 . ASP E 1 54  ? 72.393  117.249 84.456  1.00 31.02 ? 51  ASP E OD1 1 
ATOM   6164 O  OD2 . ASP E 1 54  ? 74.424  116.651 83.834  1.00 31.02 ? 51  ASP E OD2 1 
ATOM   6165 N  N   . GLY E 1 55  ? 72.035  112.301 83.018  1.00 31.79 ? 52  GLY E N   1 
ATOM   6166 C  CA  . GLY E 1 55  ? 71.710  111.099 82.245  1.00 31.40 ? 52  GLY E CA  1 
ATOM   6167 C  C   . GLY E 1 55  ? 71.815  109.858 83.101  1.00 31.38 ? 52  GLY E C   1 
ATOM   6168 O  O   . GLY E 1 55  ? 72.532  109.857 84.091  1.00 31.58 ? 52  GLY E O   1 
ATOM   6169 N  N   . LEU E 1 56  ? 71.097  108.802 82.731  1.00 31.07 ? 53  LEU E N   1 
ATOM   6170 C  CA  . LEU E 1 56  ? 71.119  107.545 83.486  1.00 31.13 ? 53  LEU E CA  1 
ATOM   6171 C  C   . LEU E 1 56  ? 71.203  106.329 82.578  1.00 30.62 ? 53  LEU E C   1 
ATOM   6172 O  O   . LEU E 1 56  ? 70.735  106.353 81.454  1.00 31.30 ? 53  LEU E O   1 
ATOM   6173 C  CB  . LEU E 1 56  ? 69.870  107.398 84.368  1.00 31.55 ? 53  LEU E CB  1 
ATOM   6174 C  CG  . LEU E 1 56  ? 69.778  108.024 85.757  1.00 32.03 ? 53  LEU E CG  1 
ATOM   6175 C  CD1 . LEU E 1 56  ? 69.399  109.503 85.662  1.00 33.98 ? 53  LEU E CD1 1 
ATOM   6176 C  CD2 . LEU E 1 56  ? 68.741  107.265 86.564  1.00 31.18 ? 53  LEU E CD2 1 
ATOM   6177 N  N   . ALA E 1 57  ? 71.806  105.265 83.085  1.00 30.18 ? 54  ALA E N   1 
ATOM   6178 C  CA  . ALA E 1 57  ? 71.860  103.981 82.399  1.00 29.51 ? 54  ALA E CA  1 
ATOM   6179 C  C   . ALA E 1 57  ? 71.415  102.976 83.439  1.00 28.81 ? 54  ALA E C   1 
ATOM   6180 O  O   . ALA E 1 57  ? 72.001  102.889 84.520  1.00 29.60 ? 54  ALA E O   1 
ATOM   6181 C  CB  . ALA E 1 57  ? 73.270  103.696 81.940  1.00 29.33 ? 54  ALA E CB  1 
ATOM   6182 N  N   . VAL E 1 58  ? 70.335  102.270 83.173  1.00 27.85 ? 55  VAL E N   1 
ATOM   6183 C  CA  . VAL E 1 58  ? 69.803  101.361 84.191  1.00 26.80 ? 55  VAL E CA  1 
ATOM   6184 C  C   . VAL E 1 58  ? 69.891  99.911  83.709  1.00 25.99 ? 55  VAL E C   1 
ATOM   6185 O  O   . VAL E 1 58  ? 69.355  99.553  82.667  1.00 25.15 ? 55  VAL E O   1 
ATOM   6186 C  CB  . VAL E 1 58  ? 68.362  101.754 84.591  1.00 27.46 ? 55  VAL E CB  1 
ATOM   6187 C  CG1 . VAL E 1 58  ? 67.815  100.819 85.705  1.00 27.59 ? 55  VAL E CG1 1 
ATOM   6188 C  CG2 . VAL E 1 58  ? 68.295  103.242 84.991  1.00 25.94 ? 55  VAL E CG2 1 
ATOM   6189 N  N   . GLY E 1 59  ? 70.606  99.089  84.461  1.00 25.57 ? 56  GLY E N   1 
ATOM   6190 C  CA  . GLY E 1 59  ? 70.853  97.731  84.024  1.00 25.27 ? 56  GLY E CA  1 
ATOM   6191 C  C   . GLY E 1 59  ? 70.314  96.695  84.967  1.00 25.27 ? 56  GLY E C   1 
ATOM   6192 O  O   . GLY E 1 59  ? 70.404  96.845  86.177  1.00 25.30 ? 56  GLY E O   1 
ATOM   6193 N  N   . SER E 1 60  ? 69.778  95.618  84.413  1.00 25.21 ? 57  SER E N   1 
ATOM   6194 C  CA  . SER E 1 60  ? 69.225  94.545  85.226  1.00 24.99 ? 57  SER E CA  1 
ATOM   6195 C  C   . SER E 1 60  ? 69.396  93.186  84.534  1.00 25.01 ? 57  SER E C   1 
ATOM   6196 O  O   . SER E 1 60  ? 69.373  93.124  83.294  1.00 26.00 ? 57  SER E O   1 
ATOM   6197 C  CB  . SER E 1 60  ? 67.743  94.855  85.489  1.00 24.98 ? 57  SER E CB  1 
ATOM   6198 O  OG  . SER E 1 60  ? 67.054  93.739  85.957  1.00 23.91 ? 57  SER E OG  1 
ATOM   6199 N  N   . PRO E 1 61  ? 69.547  92.089  85.315  1.00 24.59 ? 58  PRO E N   1 
ATOM   6200 C  CA  . PRO E 1 61  ? 69.392  90.761  84.703  1.00 24.41 ? 58  PRO E CA  1 
ATOM   6201 C  C   . PRO E 1 61  ? 68.007  90.682  84.093  1.00 24.32 ? 58  PRO E C   1 
ATOM   6202 O  O   . PRO E 1 61  ? 67.091  91.369  84.577  1.00 24.36 ? 58  PRO E O   1 
ATOM   6203 C  CB  . PRO E 1 61  ? 69.435  89.797  85.901  1.00 24.40 ? 58  PRO E CB  1 
ATOM   6204 C  CG  . PRO E 1 61  ? 69.934  90.551  87.034  1.00 22.87 ? 58  PRO E CG  1 
ATOM   6205 C  CD  . PRO E 1 61  ? 69.830  92.010  86.759  1.00 24.30 ? 58  PRO E CD  1 
ATOM   6206 N  N   . THR E 1 62  ? 67.818  89.873  83.057  1.00 24.55 ? 59  THR E N   1 
ATOM   6207 C  CA  . THR E 1 62  ? 66.461  89.701  82.583  1.00 24.88 ? 59  THR E CA  1 
ATOM   6208 C  C   . THR E 1 62  ? 65.811  88.588  83.397  1.00 25.30 ? 59  THR E C   1 
ATOM   6209 O  O   . THR E 1 62  ? 66.283  87.460  83.422  1.00 25.83 ? 59  THR E O   1 
ATOM   6210 C  CB  . THR E 1 62  ? 66.278  89.679  80.987  1.00 24.88 ? 59  THR E CB  1 
ATOM   6211 O  OG1 . THR E 1 62  ? 65.774  88.429  80.501  1.00 27.99 ? 59  THR E OG1 1 
ATOM   6212 C  CG2 . THR E 1 62  ? 67.496  90.069  80.266  1.00 22.61 ? 59  THR E CG2 1 
ATOM   6213 N  N   . ASN E 1 63  ? 64.770  88.939  84.140  1.00 25.87 ? 60  ASN E N   1 
ATOM   6214 C  CA  . ASN E 1 63  ? 64.133  87.972  85.008  1.00 25.99 ? 60  ASN E CA  1 
ATOM   6215 C  C   . ASN E 1 63  ? 62.671  87.832  84.617  1.00 26.26 ? 60  ASN E C   1 
ATOM   6216 O  O   . ASN E 1 63  ? 61.868  88.721  84.858  1.00 26.35 ? 60  ASN E O   1 
ATOM   6217 C  CB  . ASN E 1 63  ? 64.285  88.375  86.496  1.00 26.39 ? 60  ASN E CB  1 
ATOM   6218 C  CG  . ASN E 1 63  ? 65.755  88.352  86.991  1.00 26.38 ? 60  ASN E CG  1 
ATOM   6219 O  OD1 . ASN E 1 63  ? 66.050  88.851  88.061  1.00 28.44 ? 60  ASN E OD1 1 
ATOM   6220 N  ND2 . ASN E 1 63  ? 66.652  87.765  86.225  1.00 27.53 ? 60  ASN E ND2 1 
HETATM 6221 N  N   . MSE E 1 64  ? 62.334  86.709  84.001  1.00 26.83 ? 61  MSE E N   1 
HETATM 6222 C  CA  . MSE E 1 64  ? 60.981  86.462  83.520  1.00 27.64 ? 61  MSE E CA  1 
HETATM 6223 C  C   . MSE E 1 64  ? 60.546  87.545  82.520  1.00 26.66 ? 61  MSE E C   1 
HETATM 6224 O  O   . MSE E 1 64  ? 59.379  87.963  82.529  1.00 26.80 ? 61  MSE E O   1 
HETATM 6225 C  CB  . MSE E 1 64  ? 59.961  86.327  84.685  1.00 29.14 ? 61  MSE E CB  1 
HETATM 6226 C  CG  . MSE E 1 64  ? 60.312  85.310  85.779  1.00 32.23 ? 61  MSE E CG  1 
HETATM 6227 SE SE  . MSE E 1 64  ? 60.884  83.503  85.037  1.00 49.19 ? 61  MSE E SE  1 
HETATM 6228 C  CE  . MSE E 1 64  ? 61.394  82.436  86.874  1.00 36.95 ? 61  MSE E CE  1 
ATOM   6229 N  N   . GLY E 1 65  ? 61.481  87.970  81.674  1.00 24.80 ? 62  GLY E N   1 
ATOM   6230 C  CA  . GLY E 1 65  ? 61.248  89.021  80.674  1.00 24.91 ? 62  GLY E CA  1 
ATOM   6231 C  C   . GLY E 1 65  ? 61.299  90.490  81.127  1.00 24.65 ? 62  GLY E C   1 
ATOM   6232 O  O   . GLY E 1 65  ? 61.016  91.397  80.338  1.00 24.86 ? 62  GLY E O   1 
ATOM   6233 N  N   . LEU E 1 66  ? 61.657  90.728  82.394  1.00 24.26 ? 63  LEU E N   1 
ATOM   6234 C  CA  . LEU E 1 66  ? 61.465  92.029  83.050  1.00 23.96 ? 63  LEU E CA  1 
ATOM   6235 C  C   . LEU E 1 66  ? 62.676  92.444  83.903  1.00 24.56 ? 63  LEU E C   1 
ATOM   6236 O  O   . LEU E 1 66  ? 63.537  91.594  84.201  1.00 25.12 ? 63  LEU E O   1 
ATOM   6237 C  CB  . LEU E 1 66  ? 60.212  91.947  83.937  1.00 23.53 ? 63  LEU E CB  1 
ATOM   6238 C  CG  . LEU E 1 66  ? 58.850  91.611  83.300  1.00 21.81 ? 63  LEU E CG  1 
ATOM   6239 C  CD1 . LEU E 1 66  ? 57.744  91.673  84.354  1.00 21.62 ? 63  LEU E CD1 1 
ATOM   6240 C  CD2 . LEU E 1 66  ? 58.545  92.572  82.184  1.00 19.95 ? 63  LEU E CD2 1 
ATOM   6241 N  N   . VAL E 1 67  ? 62.751  93.732  84.274  1.00 24.35 ? 64  VAL E N   1 
ATOM   6242 C  CA  . VAL E 1 67  ? 63.591  94.168  85.400  1.00 24.11 ? 64  VAL E CA  1 
ATOM   6243 C  C   . VAL E 1 67  ? 63.452  93.210  86.560  1.00 24.09 ? 64  VAL E C   1 
ATOM   6244 O  O   . VAL E 1 67  ? 62.335  92.728  86.856  1.00 24.09 ? 64  VAL E O   1 
ATOM   6245 C  CB  . VAL E 1 67  ? 63.156  95.515  86.124  1.00 24.72 ? 64  VAL E CB  1 
ATOM   6246 C  CG1 . VAL E 1 67  ? 64.249  96.567  86.123  1.00 25.43 ? 64  VAL E CG1 1 
ATOM   6247 C  CG2 . VAL E 1 67  ? 61.787  96.026  85.752  1.00 24.45 ? 64  VAL E CG2 1 
ATOM   6248 N  N   . SER E 1 68  ? 64.559  93.038  87.283  1.00 23.60 ? 65  SER E N   1 
ATOM   6249 C  CA  . SER E 1 68  ? 64.569  92.280  88.520  1.00 24.28 ? 65  SER E CA  1 
ATOM   6250 C  C   . SER E 1 68  ? 63.701  92.980  89.608  1.00 23.84 ? 65  SER E C   1 
ATOM   6251 O  O   . SER E 1 68  ? 63.526  94.210  89.597  1.00 23.47 ? 65  SER E O   1 
ATOM   6252 C  CB  . SER E 1 68  ? 66.013  92.128  89.006  1.00 24.34 ? 65  SER E CB  1 
ATOM   6253 O  OG  . SER E 1 68  ? 66.464  93.349  89.586  1.00 26.02 ? 65  SER E OG  1 
ATOM   6254 N  N   . TRP E 1 69  ? 63.175  92.196  90.539  1.00 23.09 ? 66  TRP E N   1 
ATOM   6255 C  CA  . TRP E 1 69  ? 62.362  92.752  91.582  1.00 23.36 ? 66  TRP E CA  1 
ATOM   6256 C  C   . TRP E 1 69  ? 63.197  93.642  92.503  1.00 24.91 ? 66  TRP E C   1 
ATOM   6257 O  O   . TRP E 1 69  ? 62.660  94.585  93.119  1.00 24.21 ? 66  TRP E O   1 
ATOM   6258 C  CB  . TRP E 1 69  ? 61.617  91.666  92.369  1.00 22.49 ? 66  TRP E CB  1 
ATOM   6259 C  CG  . TRP E 1 69  ? 62.474  90.744  93.193  1.00 21.42 ? 66  TRP E CG  1 
ATOM   6260 C  CD1 . TRP E 1 69  ? 62.924  89.519  92.826  1.00 20.40 ? 66  TRP E CD1 1 
ATOM   6261 C  CD2 . TRP E 1 69  ? 62.963  90.965  94.534  1.00 20.81 ? 66  TRP E CD2 1 
ATOM   6262 N  NE1 . TRP E 1 69  ? 63.665  88.959  93.838  1.00 20.55 ? 66  TRP E NE1 1 
ATOM   6263 C  CE2 . TRP E 1 69  ? 63.708  89.827  94.897  1.00 21.00 ? 66  TRP E CE2 1 
ATOM   6264 C  CE3 . TRP E 1 69  ? 62.833  92.009  95.464  1.00 21.51 ? 66  TRP E CE3 1 
ATOM   6265 C  CZ2 . TRP E 1 69  ? 64.321  89.698  96.159  1.00 21.53 ? 66  TRP E CZ2 1 
ATOM   6266 C  CZ3 . TRP E 1 69  ? 63.454  91.883  96.717  1.00 20.99 ? 66  TRP E CZ3 1 
ATOM   6267 C  CH2 . TRP E 1 69  ? 64.183  90.741  97.047  1.00 20.81 ? 66  TRP E CH2 1 
ATOM   6268 N  N   . LYS E 1 70  ? 64.500  93.370  92.593  1.00 26.10 ? 67  LYS E N   1 
ATOM   6269 C  CA  . LYS E 1 70  ? 65.348  94.244  93.403  1.00 28.73 ? 67  LYS E CA  1 
ATOM   6270 C  C   . LYS E 1 70  ? 65.469  95.674  92.827  1.00 29.83 ? 67  LYS E C   1 
ATOM   6271 O  O   . LYS E 1 70  ? 65.441  96.660  93.583  1.00 30.56 ? 67  LYS E O   1 
ATOM   6272 C  CB  . LYS E 1 70  ? 66.702  93.595  93.756  1.00 28.93 ? 67  LYS E CB  1 
ATOM   6273 C  CG  . LYS E 1 70  ? 66.724  93.111  95.223  1.00 30.28 ? 67  LYS E CG  1 
ATOM   6274 C  CD  . LYS E 1 70  ? 67.716  91.999  95.510  1.00 31.36 ? 67  LYS E CD  1 
ATOM   6275 C  CE  . LYS E 1 70  ? 67.587  91.494  96.980  1.00 33.11 ? 67  LYS E CE  1 
ATOM   6276 N  NZ  . LYS E 1 70  ? 67.744  92.524  98.101  1.00 35.05 ? 67  LYS E NZ  1 
HETATM 6277 N  N   . MSE E 1 71  ? 65.565  95.777  91.503  1.00 30.83 ? 68  MSE E N   1 
HETATM 6278 C  CA  . MSE E 1 71  ? 65.654  97.056  90.825  1.00 31.75 ? 68  MSE E CA  1 
HETATM 6279 C  C   . MSE E 1 71  ? 64.311  97.758  90.899  1.00 30.34 ? 68  MSE E C   1 
HETATM 6280 O  O   . MSE E 1 71  ? 64.248  98.959  91.044  1.00 30.09 ? 68  MSE E O   1 
HETATM 6281 C  CB  . MSE E 1 71  ? 66.094  96.851  89.358  1.00 33.34 ? 68  MSE E CB  1 
HETATM 6282 C  CG  . MSE E 1 71  ? 66.277  98.138  88.509  1.00 40.83 ? 68  MSE E CG  1 
HETATM 6283 SE SE  . MSE E 1 71  ? 67.590  99.436  89.319  1.00 63.80 ? 68  MSE E SE  1 
HETATM 6284 C  CE  . MSE E 1 71  ? 69.264  98.514  88.795  1.00 57.78 ? 68  MSE E CE  1 
ATOM   6285 N  N   . LYS E 1 72  ? 63.237  96.996  90.778  1.00 29.29 ? 69  LYS E N   1 
ATOM   6286 C  CA  . LYS E 1 72  ? 61.890  97.556  90.791  1.00 27.89 ? 69  LYS E CA  1 
ATOM   6287 C  C   . LYS E 1 72  ? 61.606  98.166  92.173  1.00 26.30 ? 69  LYS E C   1 
ATOM   6288 O  O   . LYS E 1 72  ? 61.137  99.293  92.299  1.00 26.83 ? 69  LYS E O   1 
ATOM   6289 C  CB  . LYS E 1 72  ? 60.889  96.458  90.424  1.00 27.73 ? 69  LYS E CB  1 
ATOM   6290 C  CG  . LYS E 1 72  ? 59.457  96.919  90.301  1.00 29.10 ? 69  LYS E CG  1 
ATOM   6291 C  CD  . LYS E 1 72  ? 59.183  97.649  88.999  1.00 29.56 ? 69  LYS E CD  1 
ATOM   6292 C  CE  . LYS E 1 72  ? 58.063  98.681  89.178  1.00 28.30 ? 69  LYS E CE  1 
ATOM   6293 N  NZ  . LYS E 1 72  ? 56.804  98.087  89.708  1.00 27.10 ? 69  LYS E NZ  1 
ATOM   6294 N  N   . ARG E 1 73  ? 61.962  97.416  93.197  1.00 24.66 ? 70  ARG E N   1 
ATOM   6295 C  CA  . ARG E 1 73  ? 61.786  97.783  94.577  1.00 22.88 ? 70  ARG E CA  1 
ATOM   6296 C  C   . ARG E 1 73  ? 62.481  99.085  94.876  1.00 23.63 ? 70  ARG E C   1 
ATOM   6297 O  O   . ARG E 1 73  ? 61.923  99.924  95.580  1.00 24.13 ? 70  ARG E O   1 
ATOM   6298 C  CB  . ARG E 1 73  ? 62.357  96.685  95.480  1.00 21.92 ? 70  ARG E CB  1 
ATOM   6299 C  CG  . ARG E 1 73  ? 62.189  96.902  96.946  1.00 17.45 ? 70  ARG E CG  1 
ATOM   6300 C  CD  . ARG E 1 73  ? 62.751  95.729  97.692  1.00 14.02 ? 70  ARG E CD  1 
ATOM   6301 N  NE  . ARG E 1 73  ? 62.561  95.869  99.124  1.00 12.21 ? 70  ARG E NE  1 
ATOM   6302 C  CZ  . ARG E 1 73  ? 63.548  95.939  100.010 1.00 10.78 ? 70  ARG E CZ  1 
ATOM   6303 N  NH1 . ARG E 1 73  ? 63.279  96.063  101.305 1.00 7.15  ? 70  ARG E NH1 1 
ATOM   6304 N  NH2 . ARG E 1 73  ? 64.803  95.849  99.596  1.00 9.87  ? 70  ARG E NH2 1 
ATOM   6305 N  N   . PHE E 1 74  ? 63.712  99.234  94.384  1.00 23.77 ? 71  PHE E N   1 
ATOM   6306 C  CA  . PHE E 1 74  ? 64.477  100.474 94.541  1.00 24.00 ? 71  PHE E CA  1 
ATOM   6307 C  C   . PHE E 1 74  ? 63.750  101.674 93.939  1.00 24.11 ? 71  PHE E C   1 
ATOM   6308 O  O   . PHE E 1 74  ? 63.815  102.789 94.461  1.00 23.88 ? 71  PHE E O   1 
ATOM   6309 C  CB  . PHE E 1 74  ? 65.862  100.336 93.895  1.00 23.89 ? 71  PHE E CB  1 
ATOM   6310 C  CG  . PHE E 1 74  ? 66.675  101.605 93.932  1.00 24.12 ? 71  PHE E CG  1 
ATOM   6311 C  CD1 . PHE E 1 74  ? 67.338  101.993 95.098  1.00 23.91 ? 71  PHE E CD1 1 
ATOM   6312 C  CD2 . PHE E 1 74  ? 66.793  102.408 92.800  1.00 24.50 ? 71  PHE E CD2 1 
ATOM   6313 C  CE1 . PHE E 1 74  ? 68.095  103.155 95.132  1.00 24.42 ? 71  PHE E CE1 1 
ATOM   6314 C  CE2 . PHE E 1 74  ? 67.554  103.578 92.833  1.00 24.64 ? 71  PHE E CE2 1 
ATOM   6315 C  CZ  . PHE E 1 74  ? 68.204  103.946 93.993  1.00 23.86 ? 71  PHE E CZ  1 
ATOM   6316 N  N   . PHE E 1 75  ? 63.085  101.442 92.821  1.00 24.42 ? 72  PHE E N   1 
ATOM   6317 C  CA  . PHE E 1 75  ? 62.312  102.474 92.176  1.00 25.79 ? 72  PHE E CA  1 
ATOM   6318 C  C   . PHE E 1 75  ? 60.977  102.778 92.869  1.00 25.95 ? 72  PHE E C   1 
ATOM   6319 O  O   . PHE E 1 75  ? 60.677  103.944 93.111  1.00 25.71 ? 72  PHE E O   1 
ATOM   6320 C  CB  . PHE E 1 75  ? 62.090  102.105 90.697  1.00 26.78 ? 72  PHE E CB  1 
ATOM   6321 C  CG  . PHE E 1 75  ? 63.216  102.537 89.818  1.00 28.04 ? 72  PHE E CG  1 
ATOM   6322 C  CD1 . PHE E 1 75  ? 64.400  101.804 89.773  1.00 27.62 ? 72  PHE E CD1 1 
ATOM   6323 C  CD2 . PHE E 1 75  ? 63.108  103.695 89.049  1.00 29.90 ? 72  PHE E CD2 1 
ATOM   6324 C  CE1 . PHE E 1 75  ? 65.472  102.215 88.975  1.00 28.45 ? 72  PHE E CE1 1 
ATOM   6325 C  CE2 . PHE E 1 75  ? 64.189  104.107 88.235  1.00 30.97 ? 72  PHE E CE2 1 
ATOM   6326 C  CZ  . PHE E 1 75  ? 65.362  103.367 88.209  1.00 27.97 ? 72  PHE E CZ  1 
ATOM   6327 N  N   . ASP E 1 76  ? 60.169  101.747 93.151  1.00 26.30 ? 73  ASP E N   1 
ATOM   6328 C  CA  . ASP E 1 76  ? 58.875  101.956 93.792  1.00 27.01 ? 73  ASP E CA  1 
ATOM   6329 C  C   . ASP E 1 76  ? 59.102  102.585 95.147  1.00 27.22 ? 73  ASP E C   1 
ATOM   6330 O  O   . ASP E 1 76  ? 58.377  103.516 95.516  1.00 26.99 ? 73  ASP E O   1 
ATOM   6331 C  CB  . ASP E 1 76  ? 58.057  100.670 93.965  1.00 27.42 ? 73  ASP E CB  1 
ATOM   6332 C  CG  . ASP E 1 76  ? 57.676  100.007 92.623  1.00 30.95 ? 73  ASP E CG  1 
ATOM   6333 O  OD1 . ASP E 1 76  ? 57.731  100.688 91.567  1.00 34.47 ? 73  ASP E OD1 1 
ATOM   6334 O  OD2 . ASP E 1 76  ? 57.313  98.798  92.630  1.00 31.85 ? 73  ASP E OD2 1 
ATOM   6335 N  N   . ASP E 1 77  ? 60.098  102.098 95.897  1.00 27.10 ? 74  ASP E N   1 
ATOM   6336 C  CA  . ASP E 1 77  ? 60.257  102.670 97.216  1.00 27.75 ? 74  ASP E CA  1 
ATOM   6337 C  C   . ASP E 1 77  ? 61.454  103.495 97.686  1.00 27.68 ? 74  ASP E C   1 
ATOM   6338 O  O   . ASP E 1 77  ? 61.327  104.124 98.698  1.00 28.11 ? 74  ASP E O   1 
ATOM   6339 C  CB  . ASP E 1 77  ? 59.498  101.934 98.358  1.00 27.89 ? 74  ASP E CB  1 
ATOM   6340 C  CG  . ASP E 1 77  ? 59.641  100.425 98.334  1.00 27.08 ? 74  ASP E CG  1 
ATOM   6341 O  OD1 . ASP E 1 77  ? 58.599  99.730  98.115  1.00 21.89 ? 74  ASP E OD1 1 
ATOM   6342 O  OD2 . ASP E 1 77  ? 60.774  99.959  98.629  1.00 26.31 ? 74  ASP E OD2 1 
ATOM   6343 N  N   . VAL E 1 78  ? 62.553  103.621 96.964  1.00 27.85 ? 75  VAL E N   1 
ATOM   6344 C  CA  . VAL E 1 78  ? 63.406  104.767 97.326  1.00 28.25 ? 75  VAL E CA  1 
ATOM   6345 C  C   . VAL E 1 78  ? 63.185  106.014 96.461  1.00 28.41 ? 75  VAL E C   1 
ATOM   6346 O  O   . VAL E 1 78  ? 62.940  107.110 96.988  1.00 28.14 ? 75  VAL E O   1 
ATOM   6347 C  CB  . VAL E 1 78  ? 64.908  104.422 97.685  1.00 28.26 ? 75  VAL E CB  1 
ATOM   6348 C  CG1 . VAL E 1 78  ? 65.238  102.973 97.398  1.00 28.21 ? 75  VAL E CG1 1 
ATOM   6349 C  CG2 . VAL E 1 78  ? 65.898  105.401 97.072  1.00 28.38 ? 75  VAL E CG2 1 
ATOM   6350 N  N   . LEU E 1 79  ? 63.195  105.826 95.145  1.00 28.85 ? 76  LEU E N   1 
ATOM   6351 C  CA  . LEU E 1 79  ? 63.024  106.930 94.208  1.00 28.90 ? 76  LEU E CA  1 
ATOM   6352 C  C   . LEU E 1 79  ? 61.599  107.469 94.132  1.00 29.29 ? 76  LEU E C   1 
ATOM   6353 O  O   . LEU E 1 79  ? 61.396  108.609 93.730  1.00 29.34 ? 76  LEU E O   1 
ATOM   6354 C  CB  . LEU E 1 79  ? 63.532  106.554 92.821  1.00 28.45 ? 76  LEU E CB  1 
ATOM   6355 C  CG  . LEU E 1 79  ? 65.007  106.139 92.770  1.00 29.11 ? 76  LEU E CG  1 
ATOM   6356 C  CD1 . LEU E 1 79  ? 65.433  105.867 91.344  1.00 28.73 ? 76  LEU E CD1 1 
ATOM   6357 C  CD2 . LEU E 1 79  ? 65.942  107.170 93.423  1.00 27.89 ? 76  LEU E CD2 1 
ATOM   6358 N  N   . GLY E 1 80  ? 60.630  106.646 94.531  1.00 29.55 ? 77  GLY E N   1 
ATOM   6359 C  CA  . GLY E 1 80  ? 59.207  106.976 94.459  1.00 29.77 ? 77  GLY E CA  1 
ATOM   6360 C  C   . GLY E 1 80  ? 58.814  108.328 95.014  1.00 30.06 ? 77  GLY E C   1 
ATOM   6361 O  O   . GLY E 1 80  ? 57.955  109.003 94.448  1.00 30.32 ? 77  GLY E O   1 
ATOM   6362 N  N   . ASP E 1 81  ? 59.433  108.721 96.125  1.00 30.25 ? 78  ASP E N   1 
ATOM   6363 C  CA  . ASP E 1 81  ? 59.258  110.063 96.684  1.00 30.20 ? 78  ASP E CA  1 
ATOM   6364 C  C   . ASP E 1 81  ? 59.608  111.234 95.729  1.00 29.10 ? 78  ASP E C   1 
ATOM   6365 O  O   . ASP E 1 81  ? 59.120  112.340 95.931  1.00 29.39 ? 78  ASP E O   1 
ATOM   6366 C  CB  . ASP E 1 81  ? 60.033  110.192 98.005  1.00 31.12 ? 78  ASP E CB  1 
ATOM   6367 C  CG  . ASP E 1 81  ? 59.288  109.549 99.205  1.00 33.77 ? 78  ASP E CG  1 
ATOM   6368 O  OD1 . ASP E 1 81  ? 58.052  109.279 99.108  1.00 35.97 ? 78  ASP E OD1 1 
ATOM   6369 O  OD2 . ASP E 1 81  ? 59.942  109.328 100.258 1.00 34.74 ? 78  ASP E OD2 1 
ATOM   6370 N  N   . LEU E 1 82  ? 60.424  110.986 94.701  1.00 27.48 ? 79  LEU E N   1 
ATOM   6371 C  CA  . LEU E 1 82  ? 60.822  112.024 93.733  1.00 26.34 ? 79  LEU E CA  1 
ATOM   6372 C  C   . LEU E 1 82  ? 59.886  112.166 92.522  1.00 25.55 ? 79  LEU E C   1 
ATOM   6373 O  O   . LEU E 1 82  ? 60.031  113.109 91.711  1.00 25.52 ? 79  LEU E O   1 
ATOM   6374 C  CB  . LEU E 1 82  ? 62.248  111.787 93.204  1.00 26.05 ? 79  LEU E CB  1 
ATOM   6375 C  CG  . LEU E 1 82  ? 63.438  111.475 94.105  1.00 25.87 ? 79  LEU E CG  1 
ATOM   6376 C  CD1 . LEU E 1 82  ? 64.542  110.985 93.203  1.00 27.54 ? 79  LEU E CD1 1 
ATOM   6377 C  CD2 . LEU E 1 82  ? 63.908  112.646 94.957  1.00 24.68 ? 79  LEU E CD2 1 
ATOM   6378 N  N   . TRP E 1 83  ? 58.942  111.238 92.394  1.00 24.07 ? 80  TRP E N   1 
ATOM   6379 C  CA  . TRP E 1 83  ? 58.052  111.213 91.236  1.00 23.31 ? 80  TRP E CA  1 
ATOM   6380 C  C   . TRP E 1 83  ? 57.304  112.555 91.059  1.00 23.05 ? 80  TRP E C   1 
ATOM   6381 O  O   . TRP E 1 83  ? 56.628  113.027 91.969  1.00 22.37 ? 80  TRP E O   1 
ATOM   6382 C  CB  . TRP E 1 83  ? 57.080  110.015 91.310  1.00 22.61 ? 80  TRP E CB  1 
ATOM   6383 C  CG  . TRP E 1 83  ? 56.219  109.882 90.114  1.00 21.18 ? 80  TRP E CG  1 
ATOM   6384 C  CD1 . TRP E 1 83  ? 56.491  109.161 89.019  1.00 20.61 ? 80  TRP E CD1 1 
ATOM   6385 C  CD2 . TRP E 1 83  ? 54.958  110.543 89.865  1.00 20.43 ? 80  TRP E CD2 1 
ATOM   6386 N  NE1 . TRP E 1 83  ? 55.478  109.288 88.100  1.00 20.68 ? 80  TRP E NE1 1 
ATOM   6387 C  CE2 . TRP E 1 83  ? 54.526  110.138 88.592  1.00 19.52 ? 80  TRP E CE2 1 
ATOM   6388 C  CE3 . TRP E 1 83  ? 54.161  111.425 90.596  1.00 19.31 ? 80  TRP E CE3 1 
ATOM   6389 C  CZ2 . TRP E 1 83  ? 53.326  110.581 88.022  1.00 21.09 ? 80  TRP E CZ2 1 
ATOM   6390 C  CZ3 . TRP E 1 83  ? 52.945  111.869 90.029  1.00 21.49 ? 80  TRP E CZ3 1 
ATOM   6391 C  CH2 . TRP E 1 83  ? 52.549  111.448 88.754  1.00 21.01 ? 80  TRP E CH2 1 
ATOM   6392 N  N   . GLY E 1 84  ? 57.471  113.147 89.879  1.00 23.25 ? 81  GLY E N   1 
ATOM   6393 C  CA  . GLY E 1 84  ? 56.809  114.369 89.488  1.00 23.66 ? 81  GLY E CA  1 
ATOM   6394 C  C   . GLY E 1 84  ? 57.689  115.598 89.605  1.00 24.81 ? 81  GLY E C   1 
ATOM   6395 O  O   . GLY E 1 84  ? 57.247  116.714 89.295  1.00 24.87 ? 81  GLY E O   1 
ATOM   6396 N  N   . GLU E 1 85  ? 58.923  115.407 90.071  1.00 25.42 ? 82  GLU E N   1 
ATOM   6397 C  CA  . GLU E 1 85  ? 59.825  116.526 90.312  1.00 26.65 ? 82  GLU E CA  1 
ATOM   6398 C  C   . GLU E 1 85  ? 61.240  116.271 89.783  1.00 26.53 ? 82  GLU E C   1 
ATOM   6399 O  O   . GLU E 1 85  ? 62.172  117.054 90.048  1.00 27.17 ? 82  GLU E O   1 
ATOM   6400 C  CB  . GLU E 1 85  ? 59.826  116.940 91.798  1.00 26.25 ? 82  GLU E CB  1 
ATOM   6401 C  CG  . GLU E 1 85  ? 60.173  115.834 92.800  1.00 28.27 ? 82  GLU E CG  1 
ATOM   6402 C  CD  . GLU E 1 85  ? 60.262  116.330 94.250  1.00 28.98 ? 82  GLU E CD  1 
ATOM   6403 O  OE1 . GLU E 1 85  ? 61.387  116.312 94.819  1.00 32.86 ? 82  GLU E OE1 1 
ATOM   6404 O  OE2 . GLU E 1 85  ? 59.221  116.742 94.820  1.00 30.95 ? 82  GLU E OE2 1 
ATOM   6405 N  N   . ILE E 1 86  ? 61.390  115.183 89.032  1.00 26.36 ? 83  ILE E N   1 
ATOM   6406 C  CA  . ILE E 1 86  ? 62.646  114.897 88.330  1.00 26.03 ? 83  ILE E CA  1 
ATOM   6407 C  C   . ILE E 1 86  ? 62.460  114.703 86.834  1.00 25.99 ? 83  ILE E C   1 
ATOM   6408 O  O   . ILE E 1 86  ? 63.333  114.169 86.175  1.00 25.92 ? 83  ILE E O   1 
ATOM   6409 C  CB  . ILE E 1 86  ? 63.428  113.705 88.947  1.00 25.94 ? 83  ILE E CB  1 
ATOM   6410 C  CG1 . ILE E 1 86  ? 62.636  112.396 88.845  1.00 25.28 ? 83  ILE E CG1 1 
ATOM   6411 C  CG2 . ILE E 1 86  ? 63.843  114.041 90.400  1.00 25.64 ? 83  ILE E CG2 1 
ATOM   6412 C  CD1 . ILE E 1 86  ? 63.375  111.146 89.430  1.00 25.52 ? 83  ILE E CD1 1 
ATOM   6413 N  N   . ASP E 1 87  ? 61.323  115.146 86.301  1.00 26.11 ? 84  ASP E N   1 
ATOM   6414 C  CA  . ASP E 1 87  ? 61.045  115.030 84.871  1.00 26.13 ? 84  ASP E CA  1 
ATOM   6415 C  C   . ASP E 1 87  ? 62.201  115.599 84.070  1.00 26.53 ? 84  ASP E C   1 
ATOM   6416 O  O   . ASP E 1 87  ? 62.857  116.546 84.504  1.00 26.84 ? 84  ASP E O   1 
ATOM   6417 C  CB  . ASP E 1 87  ? 59.773  115.788 84.506  1.00 25.84 ? 84  ASP E CB  1 
ATOM   6418 C  CG  . ASP E 1 87  ? 58.539  115.192 85.126  1.00 25.35 ? 84  ASP E CG  1 
ATOM   6419 O  OD1 . ASP E 1 87  ? 58.417  115.221 86.369  1.00 25.94 ? 84  ASP E OD1 1 
ATOM   6420 O  OD2 . ASP E 1 87  ? 57.671  114.726 84.365  1.00 22.29 ? 84  ASP E OD2 1 
ATOM   6421 N  N   . GLY E 1 88  ? 62.462  115.011 82.910  1.00 27.01 ? 85  GLY E N   1 
ATOM   6422 C  CA  . GLY E 1 88  ? 63.438  115.572 81.978  1.00 27.13 ? 85  GLY E CA  1 
ATOM   6423 C  C   . GLY E 1 88  ? 64.860  115.062 82.095  1.00 27.42 ? 85  GLY E C   1 
ATOM   6424 O  O   . GLY E 1 88  ? 65.734  115.521 81.370  1.00 27.69 ? 85  GLY E O   1 
ATOM   6425 N  N   . LYS E 1 89  ? 65.113  114.131 83.012  1.00 27.53 ? 86  LYS E N   1 
ATOM   6426 C  CA  . LYS E 1 89  ? 66.408  113.445 83.035  1.00 27.53 ? 86  LYS E CA  1 
ATOM   6427 C  C   . LYS E 1 89  ? 66.408  112.526 81.830  1.00 27.55 ? 86  LYS E C   1 
ATOM   6428 O  O   . LYS E 1 89  ? 65.358  112.088 81.398  1.00 28.38 ? 86  LYS E O   1 
ATOM   6429 C  CB  . LYS E 1 89  ? 66.621  112.676 84.342  1.00 27.40 ? 86  LYS E CB  1 
ATOM   6430 C  CG  . LYS E 1 89  ? 66.564  113.558 85.566  1.00 25.75 ? 86  LYS E CG  1 
ATOM   6431 C  CD  . LYS E 1 89  ? 67.190  112.940 86.782  1.00 24.52 ? 86  LYS E CD  1 
ATOM   6432 C  CE  . LYS E 1 89  ? 67.358  113.977 87.894  1.00 25.21 ? 86  LYS E CE  1 
ATOM   6433 N  NZ  . LYS E 1 89  ? 68.256  115.144 87.506  1.00 24.89 ? 86  LYS E NZ  1 
ATOM   6434 N  N   . ILE E 1 90  ? 67.571  112.284 81.251  1.00 27.88 ? 87  ILE E N   1 
ATOM   6435 C  CA  . ILE E 1 90  ? 67.698  111.455 80.051  1.00 27.94 ? 87  ILE E CA  1 
ATOM   6436 C  C   . ILE E 1 90  ? 68.134  110.086 80.515  1.00 27.74 ? 87  ILE E C   1 
ATOM   6437 O  O   . ILE E 1 90  ? 69.059  109.988 81.330  1.00 28.44 ? 87  ILE E O   1 
ATOM   6438 C  CB  . ILE E 1 90  ? 68.770  112.050 79.086  1.00 28.57 ? 87  ILE E CB  1 
ATOM   6439 C  CG1 . ILE E 1 90  ? 68.341  113.438 78.577  1.00 28.44 ? 87  ILE E CG1 1 
ATOM   6440 C  CG2 . ILE E 1 90  ? 69.079  111.102 77.926  1.00 28.51 ? 87  ILE E CG2 1 
ATOM   6441 C  CD1 . ILE E 1 90  ? 69.494  114.263 77.985  1.00 28.39 ? 87  ILE E CD1 1 
ATOM   6442 N  N   . ALA E 1 91  ? 67.496  109.024 80.011  1.00 27.60 ? 88  ALA E N   1 
ATOM   6443 C  CA  . ALA E 1 91  ? 67.839  107.660 80.449  1.00 26.77 ? 88  ALA E CA  1 
ATOM   6444 C  C   . ALA E 1 91  ? 67.790  106.570 79.361  1.00 26.46 ? 88  ALA E C   1 
ATOM   6445 O  O   . ALA E 1 91  ? 67.255  106.777 78.264  1.00 25.37 ? 88  ALA E O   1 
ATOM   6446 C  CB  . ALA E 1 91  ? 67.004  107.262 81.677  1.00 26.74 ? 88  ALA E CB  1 
ATOM   6447 N  N   . CYS E 1 92  ? 68.378  105.414 79.696  1.00 26.18 ? 89  CYS E N   1 
ATOM   6448 C  CA  . CYS E 1 92  ? 68.487  104.261 78.811  1.00 25.80 ? 89  CYS E CA  1 
ATOM   6449 C  C   . CYS E 1 92  ? 68.706  102.960 79.599  1.00 25.03 ? 89  CYS E C   1 
ATOM   6450 O  O   . CYS E 1 92  ? 68.954  102.996 80.794  1.00 24.91 ? 89  CYS E O   1 
ATOM   6451 C  CB  . CYS E 1 92  ? 69.614  104.482 77.808  1.00 25.94 ? 89  CYS E CB  1 
ATOM   6452 S  SG  . CYS E 1 92  ? 71.227  104.587 78.557  1.00 27.84 ? 89  CYS E SG  1 
ATOM   6453 N  N   . ALA E 1 93  ? 68.625  101.817 78.917  1.00 24.81 ? 90  ALA E N   1 
ATOM   6454 C  CA  . ALA E 1 93  ? 68.551  100.506 79.584  1.00 24.48 ? 90  ALA E CA  1 
ATOM   6455 C  C   . ALA E 1 93  ? 69.595  99.512  79.040  1.00 24.31 ? 90  ALA E C   1 
ATOM   6456 O  O   . ALA E 1 93  ? 70.045  99.637  77.901  1.00 25.15 ? 90  ALA E O   1 
ATOM   6457 C  CB  . ALA E 1 93  ? 67.099  99.919  79.463  1.00 22.52 ? 90  ALA E CB  1 
ATOM   6458 N  N   . PHE E 1 94  ? 69.983  98.543  79.856  1.00 24.00 ? 91  PHE E N   1 
ATOM   6459 C  CA  . PHE E 1 94  ? 70.788  97.406  79.393  1.00 24.04 ? 91  PHE E CA  1 
ATOM   6460 C  C   . PHE E 1 94  ? 70.443  96.152  80.195  1.00 24.41 ? 91  PHE E C   1 
ATOM   6461 O  O   . PHE E 1 94  ? 69.963  96.247  81.328  1.00 24.66 ? 91  PHE E O   1 
ATOM   6462 C  CB  . PHE E 1 94  ? 72.297  97.695  79.405  1.00 23.76 ? 91  PHE E CB  1 
ATOM   6463 C  CG  . PHE E 1 94  ? 72.852  98.120  80.745  1.00 22.31 ? 91  PHE E CG  1 
ATOM   6464 C  CD1 . PHE E 1 94  ? 72.733  99.438  81.181  1.00 23.22 ? 91  PHE E CD1 1 
ATOM   6465 C  CD2 . PHE E 1 94  ? 73.563  97.218  81.531  1.00 20.70 ? 91  PHE E CD2 1 
ATOM   6466 C  CE1 . PHE E 1 94  ? 73.274  99.832  82.423  1.00 24.03 ? 91  PHE E CE1 1 
ATOM   6467 C  CE2 . PHE E 1 94  ? 74.103  97.593  82.758  1.00 20.19 ? 91  PHE E CE2 1 
ATOM   6468 C  CZ  . PHE E 1 94  ? 73.971  98.897  83.200  1.00 22.42 ? 91  PHE E CZ  1 
ATOM   6469 N  N   . SER E 1 95  ? 70.649  94.983  79.607  1.00 24.28 ? 92  SER E N   1 
ATOM   6470 C  CA  . SER E 1 95  ? 70.183  93.753  80.244  1.00 24.82 ? 92  SER E CA  1 
ATOM   6471 C  C   . SER E 1 95  ? 70.927  92.490  79.792  1.00 24.88 ? 92  SER E C   1 
ATOM   6472 O  O   . SER E 1 95  ? 71.297  92.375  78.630  1.00 25.36 ? 92  SER E O   1 
ATOM   6473 C  CB  . SER E 1 95  ? 68.674  93.596  80.011  1.00 24.18 ? 92  SER E CB  1 
ATOM   6474 O  OG  . SER E 1 95  ? 68.228  92.518  80.791  1.00 25.80 ? 92  SER E OG  1 
ATOM   6475 N  N   . SER E 1 96  ? 71.144  91.552  80.710  1.00 25.21 ? 93  SER E N   1 
ATOM   6476 C  CA  . SER E 1 96  ? 71.701  90.243  80.357  1.00 25.39 ? 93  SER E CA  1 
ATOM   6477 C  C   . SER E 1 96  ? 70.697  89.127  80.616  1.00 25.36 ? 93  SER E C   1 
ATOM   6478 O  O   . SER E 1 96  ? 70.183  89.007  81.722  1.00 25.28 ? 93  SER E O   1 
ATOM   6479 C  CB  . SER E 1 96  ? 72.981  89.964  81.132  1.00 25.62 ? 93  SER E CB  1 
ATOM   6480 O  OG  . SER E 1 96  ? 73.344  88.589  81.048  1.00 27.86 ? 93  SER E OG  1 
ATOM   6481 N  N   . SER E 1 97  ? 70.416  88.327  79.582  1.00 25.54 ? 94  SER E N   1 
ATOM   6482 C  CA  . SER E 1 97  ? 69.550  87.163  79.675  1.00 25.76 ? 94  SER E CA  1 
ATOM   6483 C  C   . SER E 1 97  ? 70.365  85.873  79.604  1.00 25.68 ? 94  SER E C   1 
ATOM   6484 O  O   . SER E 1 97  ? 71.559  85.908  79.294  1.00 26.08 ? 94  SER E O   1 
ATOM   6485 C  CB  . SER E 1 97  ? 68.502  87.195  78.556  1.00 26.35 ? 94  SER E CB  1 
ATOM   6486 O  OG  . SER E 1 97  ? 69.088  87.273  77.261  1.00 28.74 ? 94  SER E OG  1 
ATOM   6487 N  N   . GLY E 1 98  ? 69.727  84.737  79.879  1.00 25.16 ? 95  GLY E N   1 
ATOM   6488 C  CA  . GLY E 1 98  ? 70.409  83.433  79.812  1.00 24.80 ? 95  GLY E CA  1 
ATOM   6489 C  C   . GLY E 1 98  ? 70.590  82.920  78.395  1.00 25.26 ? 95  GLY E C   1 
ATOM   6490 O  O   . GLY E 1 98  ? 71.305  81.929  78.144  1.00 25.35 ? 95  GLY E O   1 
ATOM   6491 N  N   . GLY E 1 99  ? 69.940  83.600  77.458  1.00 25.04 ? 96  GLY E N   1 
ATOM   6492 C  CA  . GLY E 1 99  ? 69.900  83.167  76.071  1.00 24.72 ? 96  GLY E CA  1 
ATOM   6493 C  C   . GLY E 1 99  ? 69.322  84.217  75.133  1.00 24.31 ? 96  GLY E C   1 
ATOM   6494 O  O   . GLY E 1 99  ? 68.484  85.035  75.524  1.00 24.14 ? 96  GLY E O   1 
ATOM   6495 N  N   . TRP E 1 100 ? 69.824  84.213  73.904  1.00 23.93 ? 97  TRP E N   1 
ATOM   6496 C  CA  . TRP E 1 100 ? 69.200  84.907  72.799  1.00 23.85 ? 97  TRP E CA  1 
ATOM   6497 C  C   . TRP E 1 100 ? 67.806  84.327  72.568  1.00 23.27 ? 97  TRP E C   1 
ATOM   6498 O  O   . TRP E 1 100 ? 67.597  83.102  72.647  1.00 23.59 ? 97  TRP E O   1 
ATOM   6499 C  CB  . TRP E 1 100 ? 70.092  84.806  71.565  1.00 24.58 ? 97  TRP E CB  1 
ATOM   6500 C  CG  . TRP E 1 100 ? 71.373  85.500  71.817  1.00 25.07 ? 97  TRP E CG  1 
ATOM   6501 C  CD1 . TRP E 1 100 ? 72.586  84.931  72.067  1.00 25.05 ? 97  TRP E CD1 1 
ATOM   6502 C  CD2 . TRP E 1 100 ? 71.559  86.915  71.931  1.00 25.90 ? 97  TRP E CD2 1 
ATOM   6503 N  NE1 . TRP E 1 100 ? 73.521  85.907  72.320  1.00 24.44 ? 97  TRP E NE1 1 
ATOM   6504 C  CE2 . TRP E 1 100 ? 72.919  87.133  72.235  1.00 24.46 ? 97  TRP E CE2 1 
ATOM   6505 C  CE3 . TRP E 1 100 ? 70.702  88.018  71.818  1.00 26.31 ? 97  TRP E CE3 1 
ATOM   6506 C  CZ2 . TRP E 1 100 ? 73.454  88.411  72.397  1.00 25.19 ? 97  TRP E CZ2 1 
ATOM   6507 C  CZ3 . TRP E 1 100 ? 71.238  89.298  71.996  1.00 25.81 ? 97  TRP E CZ3 1 
ATOM   6508 C  CH2 . TRP E 1 100 ? 72.595  89.477  72.285  1.00 26.27 ? 97  TRP E CH2 1 
ATOM   6509 N  N   . GLY E 1 101 ? 66.844  85.219  72.364  1.00 23.01 ? 98  GLY E N   1 
ATOM   6510 C  CA  . GLY E 1 101 ? 65.423  84.852  72.278  1.00 21.97 ? 98  GLY E CA  1 
ATOM   6511 C  C   . GLY E 1 101 ? 64.769  84.781  73.635  1.00 21.15 ? 98  GLY E C   1 
ATOM   6512 O  O   . GLY E 1 101 ? 63.581  84.456  73.752  1.00 21.52 ? 98  GLY E O   1 
ATOM   6513 N  N   . GLY E 1 102 ? 65.544  85.118  74.657  1.00 21.19 ? 99  GLY E N   1 
ATOM   6514 C  CA  . GLY E 1 102 ? 65.158  84.919  76.045  1.00 22.26 ? 99  GLY E CA  1 
ATOM   6515 C  C   . GLY E 1 102 ? 64.576  86.117  76.760  1.00 23.15 ? 99  GLY E C   1 
ATOM   6516 O  O   . GLY E 1 102 ? 64.284  86.036  77.949  1.00 23.89 ? 99  GLY E O   1 
ATOM   6517 N  N   . GLY E 1 103 ? 64.413  87.232  76.060  1.00 23.69 ? 100 GLY E N   1 
ATOM   6518 C  CA  . GLY E 1 103 ? 63.652  88.337  76.600  1.00 24.60 ? 100 GLY E CA  1 
ATOM   6519 C  C   . GLY E 1 103 ? 64.445  89.560  76.990  1.00 25.83 ? 100 GLY E C   1 
ATOM   6520 O  O   . GLY E 1 103 ? 63.920  90.446  77.687  1.00 25.35 ? 100 GLY E O   1 
ATOM   6521 N  N   . ASN E 1 104 ? 65.691  89.649  76.518  1.00 26.29 ? 101 ASN E N   1 
ATOM   6522 C  CA  . ASN E 1 104 ? 66.512  90.787  76.901  1.00 27.43 ? 101 ASN E CA  1 
ATOM   6523 C  C   . ASN E 1 104 ? 66.065  92.152  76.348  1.00 27.20 ? 101 ASN E C   1 
ATOM   6524 O  O   . ASN E 1 104 ? 66.271  93.165  77.010  1.00 26.98 ? 101 ASN E O   1 
ATOM   6525 C  CB  . ASN E 1 104 ? 68.016  90.515  76.691  1.00 28.12 ? 101 ASN E CB  1 
ATOM   6526 C  CG  . ASN E 1 104 ? 68.352  90.184  75.263  1.00 30.84 ? 101 ASN E CG  1 
ATOM   6527 O  OD1 . ASN E 1 104 ? 67.543  90.365  74.346  1.00 33.66 ? 101 ASN E OD1 1 
ATOM   6528 N  ND2 . ASN E 1 104 ? 69.549  89.678  75.063  1.00 33.61 ? 101 ASN E ND2 1 
ATOM   6529 N  N   . GLU E 1 105 ? 65.474  92.193  75.153  1.00 27.00 ? 102 GLU E N   1 
ATOM   6530 C  CA  . GLU E 1 105 ? 64.941  93.463  74.654  1.00 27.02 ? 102 GLU E CA  1 
ATOM   6531 C  C   . GLU E 1 105 ? 63.637  93.816  75.374  1.00 26.77 ? 102 GLU E C   1 
ATOM   6532 O  O   . GLU E 1 105 ? 63.389  94.975  75.644  1.00 26.31 ? 102 GLU E O   1 
ATOM   6533 C  CB  . GLU E 1 105 ? 64.694  93.440  73.146  1.00 27.66 ? 102 GLU E CB  1 
ATOM   6534 C  CG  . GLU E 1 105 ? 65.925  93.342  72.279  1.00 28.17 ? 102 GLU E CG  1 
ATOM   6535 C  CD  . GLU E 1 105 ? 65.607  92.878  70.884  1.00 31.70 ? 102 GLU E CD  1 
ATOM   6536 O  OE1 . GLU E 1 105 ? 64.441  92.564  70.570  1.00 36.57 ? 102 GLU E OE1 1 
ATOM   6537 O  OE2 . GLU E 1 105 ? 66.525  92.800  70.060  1.00 37.77 ? 102 GLU E OE2 1 
ATOM   6538 N  N   . VAL E 1 106 ? 62.807  92.810  75.666  1.00 26.76 ? 103 VAL E N   1 
ATOM   6539 C  CA  . VAL E 1 106 ? 61.576  93.013  76.413  1.00 26.39 ? 103 VAL E CA  1 
ATOM   6540 C  C   . VAL E 1 106 ? 61.928  93.540  77.821  1.00 26.39 ? 103 VAL E C   1 
ATOM   6541 O  O   . VAL E 1 106 ? 61.260  94.438  78.356  1.00 27.57 ? 103 VAL E O   1 
ATOM   6542 C  CB  . VAL E 1 106 ? 60.689  91.717  76.490  1.00 26.97 ? 103 VAL E CB  1 
ATOM   6543 C  CG1 . VAL E 1 106 ? 59.389  92.019  77.191  1.00 26.37 ? 103 VAL E CG1 1 
ATOM   6544 C  CG2 . VAL E 1 106 ? 60.403  91.145  75.096  1.00 25.56 ? 103 VAL E CG2 1 
ATOM   6545 N  N   . ALA E 1 107 ? 62.989  93.005  78.409  1.00 26.23 ? 104 ALA E N   1 
ATOM   6546 C  CA  . ALA E 1 107 ? 63.443  93.438  79.732  1.00 25.49 ? 104 ALA E CA  1 
ATOM   6547 C  C   . ALA E 1 107 ? 63.904  94.912  79.715  1.00 26.38 ? 104 ALA E C   1 
ATOM   6548 O  O   . ALA E 1 107 ? 63.572  95.679  80.633  1.00 26.74 ? 104 ALA E O   1 
ATOM   6549 C  CB  . ALA E 1 107 ? 64.530  92.529  80.256  1.00 23.88 ? 104 ALA E CB  1 
ATOM   6550 N  N   . CYS E 1 108 ? 64.634  95.303  78.670  1.00 26.27 ? 105 CYS E N   1 
ATOM   6551 C  CA  . CYS E 1 108 ? 65.013  96.689  78.448  1.00 27.47 ? 105 CYS E CA  1 
ATOM   6552 C  C   . CYS E 1 108 ? 63.788  97.574  78.313  1.00 27.85 ? 105 CYS E C   1 
ATOM   6553 O  O   . CYS E 1 108 ? 63.746  98.661  78.864  1.00 28.39 ? 105 CYS E O   1 
ATOM   6554 C  CB  . CYS E 1 108 ? 65.869  96.815  77.185  1.00 27.37 ? 105 CYS E CB  1 
ATOM   6555 S  SG  . CYS E 1 108 ? 67.576  96.285  77.440  1.00 28.77 ? 105 CYS E SG  1 
HETATM 6556 N  N   . MSE E 1 109 ? 62.786  97.086  77.590  1.00 29.05 ? 106 MSE E N   1 
HETATM 6557 C  CA  . MSE E 1 109 ? 61.528  97.761  77.400  1.00 29.29 ? 106 MSE E CA  1 
HETATM 6558 C  C   . MSE E 1 109 ? 60.850  98.078  78.744  1.00 28.66 ? 106 MSE E C   1 
HETATM 6559 O  O   . MSE E 1 109 ? 60.295  99.167  78.941  1.00 28.25 ? 106 MSE E O   1 
HETATM 6560 C  CB  . MSE E 1 109 ? 60.644  96.894  76.511  1.00 30.11 ? 106 MSE E CB  1 
HETATM 6561 C  CG  . MSE E 1 109 ? 60.814  97.180  75.022  1.00 39.53 ? 106 MSE E CG  1 
HETATM 6562 SE SE  . MSE E 1 109 ? 60.549  99.170  74.456  1.00 62.35 ? 106 MSE E SE  1 
HETATM 6563 C  CE  . MSE E 1 109 ? 59.311  99.706  75.755  1.00 49.17 ? 106 MSE E CE  1 
ATOM   6564 N  N   . SER E 1 110 ? 60.907  97.121  79.672  1.00 27.52 ? 107 SER E N   1 
ATOM   6565 C  CA  . SER E 1 110 ? 60.292  97.294  80.983  1.00 26.58 ? 107 SER E CA  1 
ATOM   6566 C  C   . SER E 1 110 ? 61.056  98.302  81.813  1.00 26.43 ? 107 SER E C   1 
ATOM   6567 O  O   . SER E 1 110 ? 60.442  99.105  82.520  1.00 26.54 ? 107 SER E O   1 
ATOM   6568 C  CB  . SER E 1 110 ? 60.173  95.966  81.729  1.00 25.83 ? 107 SER E CB  1 
ATOM   6569 O  OG  . SER E 1 110 ? 61.433  95.502  82.158  1.00 25.30 ? 107 SER E OG  1 
ATOM   6570 N  N   . ILE E 1 111 ? 62.390  98.256  81.730  1.00 26.37 ? 108 ILE E N   1 
ATOM   6571 C  CA  . ILE E 1 111 ? 63.239  99.292  82.302  1.00 25.47 ? 108 ILE E CA  1 
ATOM   6572 C  C   . ILE E 1 111 ? 62.872  100.640 81.715  1.00 25.96 ? 108 ILE E C   1 
ATOM   6573 O  O   . ILE E 1 111 ? 62.677  101.590 82.449  1.00 26.84 ? 108 ILE E O   1 
ATOM   6574 C  CB  . ILE E 1 111 ? 64.751  98.991  82.131  1.00 25.66 ? 108 ILE E CB  1 
ATOM   6575 C  CG1 . ILE E 1 111 ? 65.113  97.684  82.835  1.00 25.55 ? 108 ILE E CG1 1 
ATOM   6576 C  CG2 . ILE E 1 111 ? 65.627  100.155 82.669  1.00 24.46 ? 108 ILE E CG2 1 
ATOM   6577 C  CD1 . ILE E 1 111 ? 66.532  97.184  82.604  1.00 24.52 ? 108 ILE E CD1 1 
ATOM   6578 N  N   . LEU E 1 112 ? 62.744  100.727 80.397  1.00 26.78 ? 109 LEU E N   1 
ATOM   6579 C  CA  . LEU E 1 112 ? 62.437  102.021 79.740  1.00 26.96 ? 109 LEU E CA  1 
ATOM   6580 C  C   . LEU E 1 112 ? 61.062  102.579 80.147  1.00 26.96 ? 109 LEU E C   1 
ATOM   6581 O  O   . LEU E 1 112 ? 60.905  103.790 80.326  1.00 26.73 ? 109 LEU E O   1 
ATOM   6582 C  CB  . LEU E 1 112 ? 62.516  101.892 78.208  1.00 26.30 ? 109 LEU E CB  1 
ATOM   6583 C  CG  . LEU E 1 112 ? 63.861  101.677 77.533  1.00 25.25 ? 109 LEU E CG  1 
ATOM   6584 C  CD1 . LEU E 1 112 ? 63.673  101.434 76.026  1.00 22.72 ? 109 LEU E CD1 1 
ATOM   6585 C  CD2 . LEU E 1 112 ? 64.788  102.843 77.781  1.00 25.15 ? 109 LEU E CD2 1 
ATOM   6586 N  N   . THR E 1 113 ? 60.089  101.673 80.268  1.00 27.15 ? 110 THR E N   1 
ATOM   6587 C  CA  . THR E 1 113 ? 58.741  101.962 80.714  1.00 27.47 ? 110 THR E CA  1 
ATOM   6588 C  C   . THR E 1 113 ? 58.765  102.632 82.059  1.00 29.26 ? 110 THR E C   1 
ATOM   6589 O  O   . THR E 1 113 ? 58.056  103.631 82.298  1.00 28.91 ? 110 THR E O   1 
ATOM   6590 C  CB  . THR E 1 113 ? 57.929  100.648 80.867  1.00 27.08 ? 110 THR E CB  1 
ATOM   6591 O  OG1 . THR E 1 113 ? 57.617  100.140 79.571  1.00 27.14 ? 110 THR E OG1 1 
ATOM   6592 C  CG2 . THR E 1 113 ? 56.621  100.861 81.680  1.00 24.07 ? 110 THR E CG2 1 
HETATM 6593 N  N   . MSE E 1 114 ? 59.573  102.048 82.934  1.00 30.64 ? 111 MSE E N   1 
HETATM 6594 C  CA  . MSE E 1 114 ? 59.705  102.484 84.303  1.00 34.49 ? 111 MSE E CA  1 
HETATM 6595 C  C   . MSE E 1 114 ? 60.333  103.869 84.381  1.00 32.07 ? 111 MSE E C   1 
HETATM 6596 O  O   . MSE E 1 114 ? 59.876  104.707 85.133  1.00 31.86 ? 111 MSE E O   1 
HETATM 6597 C  CB  . MSE E 1 114 ? 60.521  101.456 85.058  1.00 33.53 ? 111 MSE E CB  1 
HETATM 6598 C  CG  . MSE E 1 114 ? 60.596  101.657 86.518  1.00 37.49 ? 111 MSE E CG  1 
HETATM 6599 SE SE  . MSE E 1 114 ? 61.607  100.127 87.282  1.00 45.21 ? 111 MSE E SE  1 
HETATM 6600 C  CE  . MSE E 1 114 ? 63.509  100.551 86.478  1.00 41.62 ? 111 MSE E CE  1 
ATOM   6601 N  N   . LEU E 1 115 ? 61.333  104.126 83.547  1.00 31.56 ? 112 LEU E N   1 
ATOM   6602 C  CA  . LEU E 1 115 ? 61.952  105.443 83.491  1.00 30.50 ? 112 LEU E CA  1 
ATOM   6603 C  C   . LEU E 1 115 ? 61.033  106.518 82.908  1.00 30.97 ? 112 LEU E C   1 
ATOM   6604 O  O   . LEU E 1 115 ? 60.993  107.651 83.400  1.00 29.60 ? 112 LEU E O   1 
ATOM   6605 C  CB  . LEU E 1 115 ? 63.270  105.381 82.722  1.00 29.52 ? 112 LEU E CB  1 
ATOM   6606 C  CG  . LEU E 1 115 ? 64.306  104.385 83.258  1.00 28.80 ? 112 LEU E CG  1 
ATOM   6607 C  CD1 . LEU E 1 115 ? 65.330  103.975 82.191  1.00 26.49 ? 112 LEU E CD1 1 
ATOM   6608 C  CD2 . LEU E 1 115 ? 64.990  104.911 84.480  1.00 26.51 ? 112 LEU E CD2 1 
HETATM 6609 N  N   . MSE E 1 116 ? 60.312  106.162 81.849  1.00 32.05 ? 113 MSE E N   1 
HETATM 6610 C  CA  . MSE E 1 116 ? 59.382  107.082 81.209  1.00 34.95 ? 113 MSE E CA  1 
HETATM 6611 C  C   . MSE E 1 116 ? 58.304  107.556 82.149  1.00 32.07 ? 113 MSE E C   1 
HETATM 6612 O  O   . MSE E 1 116 ? 57.833  108.682 82.031  1.00 32.46 ? 113 MSE E O   1 
HETATM 6613 C  CB  . MSE E 1 116 ? 58.728  106.445 80.018  1.00 33.88 ? 113 MSE E CB  1 
HETATM 6614 C  CG  . MSE E 1 116 ? 59.512  106.575 78.748  1.00 37.57 ? 113 MSE E CG  1 
HETATM 6615 SE SE  . MSE E 1 116 ? 58.351  105.916 77.290  1.00 47.72 ? 113 MSE E SE  1 
HETATM 6616 C  CE  . MSE E 1 116 ? 58.657  103.938 77.406  1.00 37.99 ? 113 MSE E CE  1 
ATOM   6617 N  N   . ASN E 1 117 ? 57.935  106.691 83.082  1.00 30.64 ? 114 ASN E N   1 
ATOM   6618 C  CA  . ASN E 1 117 ? 56.997  107.002 84.126  1.00 29.73 ? 114 ASN E CA  1 
ATOM   6619 C  C   . ASN E 1 117 ? 57.483  108.153 85.014  1.00 29.09 ? 114 ASN E C   1 
ATOM   6620 O  O   . ASN E 1 117 ? 56.666  108.904 85.552  1.00 28.89 ? 114 ASN E O   1 
ATOM   6621 C  CB  . ASN E 1 117 ? 56.721  105.763 84.967  1.00 29.60 ? 114 ASN E CB  1 
ATOM   6622 C  CG  . ASN E 1 117 ? 55.313  105.725 85.493  1.00 32.06 ? 114 ASN E CG  1 
ATOM   6623 O  OD1 . ASN E 1 117 ? 55.058  106.095 86.649  1.00 37.43 ? 114 ASN E OD1 1 
ATOM   6624 N  ND2 . ASN E 1 117 ? 54.370  105.305 84.652  1.00 32.40 ? 114 ASN E ND2 1 
ATOM   6625 N  N   . PHE E 1 118 ? 58.800  108.301 85.149  1.00 28.23 ? 115 PHE E N   1 
ATOM   6626 C  CA  . PHE E 1 118 ? 59.378  109.402 85.937  1.00 28.31 ? 115 PHE E CA  1 
ATOM   6627 C  C   . PHE E 1 118 ? 59.494  110.719 85.160  1.00 27.49 ? 115 PHE E C   1 
ATOM   6628 O  O   . PHE E 1 118 ? 60.024  111.693 85.677  1.00 27.27 ? 115 PHE E O   1 
ATOM   6629 C  CB  . PHE E 1 118 ? 60.722  109.003 86.572  1.00 28.99 ? 115 PHE E CB  1 
ATOM   6630 C  CG  . PHE E 1 118 ? 60.572  108.282 87.882  1.00 30.44 ? 115 PHE E CG  1 
ATOM   6631 C  CD1 . PHE E 1 118 ? 60.231  106.917 87.913  1.00 34.31 ? 115 PHE E CD1 1 
ATOM   6632 C  CD2 . PHE E 1 118 ? 60.706  108.969 89.084  1.00 28.86 ? 115 PHE E CD2 1 
ATOM   6633 C  CE1 . PHE E 1 118 ? 60.055  106.244 89.153  1.00 34.78 ? 115 PHE E CE1 1 
ATOM   6634 C  CE2 . PHE E 1 118 ? 60.549  108.332 90.309  1.00 28.90 ? 115 PHE E CE2 1 
ATOM   6635 C  CZ  . PHE E 1 118 ? 60.231  106.981 90.361  1.00 32.08 ? 115 PHE E CZ  1 
ATOM   6636 N  N   . GLY E 1 119 ? 58.961  110.746 83.939  1.00 26.32 ? 116 GLY E N   1 
ATOM   6637 C  CA  . GLY E 1 119 ? 59.086  111.891 83.065  1.00 25.33 ? 116 GLY E CA  1 
ATOM   6638 C  C   . GLY E 1 119 ? 60.408  111.974 82.320  1.00 25.02 ? 116 GLY E C   1 
ATOM   6639 O  O   . GLY E 1 119 ? 60.705  113.011 81.715  1.00 24.83 ? 116 GLY E O   1 
ATOM   6640 N  N   . PHE E 1 120 ? 61.209  110.901 82.359  1.00 24.78 ? 117 PHE E N   1 
ATOM   6641 C  CA  . PHE E 1 120 ? 62.498  110.875 81.651  1.00 24.39 ? 117 PHE E CA  1 
ATOM   6642 C  C   . PHE E 1 120 ? 62.344  110.763 80.138  1.00 24.29 ? 117 PHE E C   1 
ATOM   6643 O  O   . PHE E 1 120 ? 61.383  110.174 79.642  1.00 24.41 ? 117 PHE E O   1 
ATOM   6644 C  CB  . PHE E 1 120 ? 63.416  109.751 82.131  1.00 24.52 ? 117 PHE E CB  1 
ATOM   6645 C  CG  . PHE E 1 120 ? 63.754  109.796 83.592  1.00 24.38 ? 117 PHE E CG  1 
ATOM   6646 C  CD1 . PHE E 1 120 ? 63.351  110.848 84.404  1.00 24.36 ? 117 PHE E CD1 1 
ATOM   6647 C  CD2 . PHE E 1 120 ? 64.506  108.779 84.151  1.00 24.59 ? 117 PHE E CD2 1 
ATOM   6648 C  CE1 . PHE E 1 120 ? 63.681  110.877 85.757  1.00 23.19 ? 117 PHE E CE1 1 
ATOM   6649 C  CE2 . PHE E 1 120 ? 64.841  108.792 85.503  1.00 24.64 ? 117 PHE E CE2 1 
ATOM   6650 C  CZ  . PHE E 1 120 ? 64.423  109.844 86.303  1.00 25.13 ? 117 PHE E CZ  1 
ATOM   6651 N  N   . LEU E 1 121 ? 63.295  111.365 79.422  1.00 24.69 ? 118 LEU E N   1 
ATOM   6652 C  CA  . LEU E 1 121 ? 63.430  111.238 77.970  1.00 24.20 ? 118 LEU E CA  1 
ATOM   6653 C  C   . LEU E 1 121 ? 64.324  110.035 77.771  1.00 24.44 ? 118 LEU E C   1 
ATOM   6654 O  O   . LEU E 1 121 ? 65.394  109.904 78.378  1.00 23.98 ? 118 LEU E O   1 
ATOM   6655 C  CB  . LEU E 1 121 ? 64.120  112.455 77.368  1.00 23.89 ? 118 LEU E CB  1 
ATOM   6656 C  CG  . LEU E 1 121 ? 63.531  113.859 77.309  1.00 23.47 ? 118 LEU E CG  1 
ATOM   6657 C  CD1 . LEU E 1 121 ? 63.018  114.116 75.914  1.00 23.88 ? 118 LEU E CD1 1 
ATOM   6658 C  CD2 . LEU E 1 121 ? 62.486  114.115 78.344  1.00 20.10 ? 118 LEU E CD2 1 
ATOM   6659 N  N   . VAL E 1 122 ? 63.889  109.169 76.885  1.00 24.54 ? 119 VAL E N   1 
ATOM   6660 C  CA  . VAL E 1 122 ? 64.335  107.806 76.905  1.00 24.66 ? 119 VAL E CA  1 
ATOM   6661 C  C   . VAL E 1 122 ? 64.731  107.411 75.485  1.00 24.37 ? 119 VAL E C   1 
ATOM   6662 O  O   . VAL E 1 122 ? 64.132  107.885 74.498  1.00 24.17 ? 119 VAL E O   1 
ATOM   6663 C  CB  . VAL E 1 122 ? 63.230  106.972 77.597  1.00 24.84 ? 119 VAL E CB  1 
ATOM   6664 C  CG1 . VAL E 1 122 ? 62.752  105.804 76.760  1.00 24.45 ? 119 VAL E CG1 1 
ATOM   6665 C  CG2 . VAL E 1 122 ? 63.651  106.621 79.042  1.00 23.90 ? 119 VAL E CG2 1 
ATOM   6666 N  N   . PHE E 1 123 ? 65.789  106.624 75.371  1.00 23.10 ? 120 PHE E N   1 
ATOM   6667 C  CA  . PHE E 1 123 ? 66.324  106.351 74.057  1.00 22.52 ? 120 PHE E CA  1 
ATOM   6668 C  C   . PHE E 1 123 ? 66.963  104.976 73.996  1.00 22.56 ? 120 PHE E C   1 
ATOM   6669 O  O   . PHE E 1 123 ? 67.236  104.329 75.024  1.00 21.97 ? 120 PHE E O   1 
ATOM   6670 C  CB  . PHE E 1 123 ? 67.343  107.443 73.650  1.00 22.64 ? 120 PHE E CB  1 
ATOM   6671 C  CG  . PHE E 1 123 ? 68.630  107.379 74.423  1.00 21.92 ? 120 PHE E CG  1 
ATOM   6672 C  CD1 . PHE E 1 123 ? 68.769  108.059 75.630  1.00 21.70 ? 120 PHE E CD1 1 
ATOM   6673 C  CD2 . PHE E 1 123 ? 69.696  106.600 73.962  1.00 20.53 ? 120 PHE E CD2 1 
ATOM   6674 C  CE1 . PHE E 1 123 ? 69.945  107.962 76.355  1.00 20.83 ? 120 PHE E CE1 1 
ATOM   6675 C  CE2 . PHE E 1 123 ? 70.876  106.503 74.673  1.00 18.26 ? 120 PHE E CE2 1 
ATOM   6676 C  CZ  . PHE E 1 123 ? 71.003  107.174 75.866  1.00 21.34 ? 120 PHE E CZ  1 
ATOM   6677 N  N   . GLY E 1 124 ? 67.165  104.535 72.761  1.00 22.78 ? 121 GLY E N   1 
ATOM   6678 C  CA  . GLY E 1 124 ? 68.092  103.459 72.436  1.00 22.83 ? 121 GLY E CA  1 
ATOM   6679 C  C   . GLY E 1 124 ? 69.015  103.974 71.347  1.00 23.60 ? 121 GLY E C   1 
ATOM   6680 O  O   . GLY E 1 124 ? 69.086  105.201 71.070  1.00 23.52 ? 121 GLY E O   1 
ATOM   6681 N  N   . VAL E 1 125 ? 69.733  103.046 70.719  1.00 24.06 ? 122 VAL E N   1 
ATOM   6682 C  CA  . VAL E 1 125 ? 70.883  103.379 69.872  1.00 23.48 ? 122 VAL E CA  1 
ATOM   6683 C  C   . VAL E 1 125 ? 70.792  102.618 68.559  1.00 23.99 ? 122 VAL E C   1 
ATOM   6684 O  O   . VAL E 1 125 ? 70.738  101.376 68.533  1.00 24.36 ? 122 VAL E O   1 
ATOM   6685 C  CB  . VAL E 1 125 ? 72.225  103.039 70.610  1.00 23.76 ? 122 VAL E CB  1 
ATOM   6686 C  CG1 . VAL E 1 125 ? 73.401  103.038 69.662  1.00 22.74 ? 122 VAL E CG1 1 
ATOM   6687 C  CG2 . VAL E 1 125 ? 72.479  103.991 71.796  1.00 22.38 ? 122 VAL E CG2 1 
ATOM   6688 N  N   . THR E 1 126 ? 70.793  103.372 67.467  1.00 24.44 ? 123 THR E N   1 
ATOM   6689 C  CA  . THR E 1 126 ? 70.708  102.809 66.106  1.00 24.16 ? 123 THR E CA  1 
ATOM   6690 C  C   . THR E 1 126 ? 71.976  102.079 65.662  1.00 24.64 ? 123 THR E C   1 
ATOM   6691 O  O   . THR E 1 126 ? 71.901  101.176 64.843  1.00 25.30 ? 123 THR E O   1 
ATOM   6692 C  CB  . THR E 1 126 ? 70.397  103.905 65.056  1.00 23.69 ? 123 THR E CB  1 
ATOM   6693 O  OG1 . THR E 1 126 ? 71.378  104.939 65.156  1.00 23.30 ? 123 THR E OG1 1 
ATOM   6694 C  CG2 . THR E 1 126 ? 68.994  104.501 65.255  1.00 21.33 ? 123 THR E CG2 1 
ATOM   6695 N  N   . ASP E 1 127 ? 73.128  102.487 66.197  1.00 24.99 ? 124 ASP E N   1 
ATOM   6696 C  CA  . ASP E 1 127 ? 74.446  102.053 65.728  1.00 24.81 ? 124 ASP E CA  1 
ATOM   6697 C  C   . ASP E 1 127 ? 74.592  100.555 65.548  1.00 25.12 ? 124 ASP E C   1 
ATOM   6698 O  O   . ASP E 1 127 ? 74.061  99.772  66.353  1.00 25.96 ? 124 ASP E O   1 
ATOM   6699 C  CB  . ASP E 1 127 ? 75.526  102.504 66.727  1.00 25.12 ? 124 ASP E CB  1 
ATOM   6700 C  CG  . ASP E 1 127 ? 75.695  104.046 66.804  1.00 24.74 ? 124 ASP E CG  1 
ATOM   6701 O  OD1 . ASP E 1 127 ? 74.712  104.812 66.648  1.00 24.09 ? 124 ASP E OD1 1 
ATOM   6702 O  OD2 . ASP E 1 127 ? 76.833  104.482 67.056  1.00 23.50 ? 124 ASP E OD2 1 
ATOM   6703 N  N   . TYR E 1 128 ? 75.315  100.147 64.509  1.00 24.72 ? 125 TYR E N   1 
ATOM   6704 C  CA  . TYR E 1 128 ? 75.768  98.764  64.405  1.00 24.75 ? 125 TYR E CA  1 
ATOM   6705 C  C   . TYR E 1 128 ? 77.228  98.658  64.755  1.00 25.44 ? 125 TYR E C   1 
ATOM   6706 O  O   . TYR E 1 128 ? 78.128  99.248  64.151  1.00 25.21 ? 125 TYR E O   1 
ATOM   6707 C  CB  . TYR E 1 128 ? 75.523  98.149  63.037  1.00 24.63 ? 125 TYR E CB  1 
ATOM   6708 C  CG  . TYR E 1 128 ? 74.151  97.532  62.860  1.00 24.16 ? 125 TYR E CG  1 
ATOM   6709 C  CD1 . TYR E 1 128 ? 73.000  98.313  62.879  1.00 22.84 ? 125 TYR E CD1 1 
ATOM   6710 C  CD2 . TYR E 1 128 ? 74.021  96.172  62.606  1.00 24.26 ? 125 TYR E CD2 1 
ATOM   6711 C  CE1 . TYR E 1 128 ? 71.759  97.748  62.682  1.00 22.76 ? 125 TYR E CE1 1 
ATOM   6712 C  CE2 . TYR E 1 128 ? 72.795  95.604  62.414  1.00 23.92 ? 125 TYR E CE2 1 
ATOM   6713 C  CZ  . TYR E 1 128 ? 71.674  96.390  62.466  1.00 22.84 ? 125 TYR E CZ  1 
ATOM   6714 O  OH  . TYR E 1 128 ? 70.478  95.792  62.274  1.00 24.98 ? 125 TYR E OH  1 
ATOM   6715 N  N   . VAL E 1 129 ? 77.436  97.851  65.759  1.00 26.41 ? 126 VAL E N   1 
ATOM   6716 C  CA  . VAL E 1 129 ? 78.677  97.788  66.450  1.00 26.37 ? 126 VAL E CA  1 
ATOM   6717 C  C   . VAL E 1 129 ? 79.376  96.509  65.931  1.00 26.61 ? 126 VAL E C   1 
ATOM   6718 O  O   . VAL E 1 129 ? 80.592  96.366  66.029  1.00 27.71 ? 126 VAL E O   1 
ATOM   6719 C  CB  . VAL E 1 129 ? 78.290  97.820  67.936  1.00 26.54 ? 126 VAL E CB  1 
ATOM   6720 C  CG1 . VAL E 1 129 ? 78.274  96.422  68.568  1.00 26.81 ? 126 VAL E CG1 1 
ATOM   6721 C  CG2 . VAL E 1 129 ? 79.096  98.815  68.674  1.00 26.16 ? 126 VAL E CG2 1 
ATOM   6722 N  N   . GLY E 1 130 ? 78.580  95.617  65.336  1.00 26.36 ? 127 GLY E N   1 
ATOM   6723 C  CA  . GLY E 1 130 ? 79.022  94.470  64.555  1.00 25.76 ? 127 GLY E CA  1 
ATOM   6724 C  C   . GLY E 1 130 ? 78.044  94.290  63.406  1.00 25.98 ? 127 GLY E C   1 
ATOM   6725 O  O   . GLY E 1 130 ? 76.977  94.915  63.399  1.00 26.33 ? 127 GLY E O   1 
ATOM   6726 N  N   . LYS E 1 131 ? 78.400  93.456  62.428  1.00 26.09 ? 128 LYS E N   1 
ATOM   6727 C  CA  . LYS E 1 131 ? 77.563  93.228  61.229  1.00 26.12 ? 128 LYS E CA  1 
ATOM   6728 C  C   . LYS E 1 131 ? 76.103  92.854  61.558  1.00 26.00 ? 128 LYS E C   1 
ATOM   6729 O  O   . LYS E 1 131 ? 75.185  93.280  60.880  1.00 26.06 ? 128 LYS E O   1 
ATOM   6730 C  CB  . LYS E 1 131 ? 78.186  92.172  60.283  1.00 26.14 ? 128 LYS E CB  1 
ATOM   6731 C  CG  . LYS E 1 131 ? 79.593  92.502  59.780  1.00 26.79 ? 128 LYS E CG  1 
ATOM   6732 C  CD  . LYS E 1 131 ? 79.872  92.035  58.333  1.00 26.80 ? 128 LYS E CD  1 
ATOM   6733 C  CE  . LYS E 1 131 ? 81.363  92.262  57.967  1.00 27.19 ? 128 LYS E CE  1 
ATOM   6734 N  NZ  . LYS E 1 131 ? 81.689  92.327  56.501  1.00 24.94 ? 128 LYS E NZ  1 
ATOM   6735 N  N   . LYS E 1 132 ? 75.893  92.041  62.584  1.00 25.79 ? 129 LYS E N   1 
ATOM   6736 C  CA  . LYS E 1 132 ? 74.538  91.671  62.991  1.00 26.10 ? 129 LYS E CA  1 
ATOM   6737 C  C   . LYS E 1 132 ? 74.414  91.923  64.510  1.00 25.54 ? 129 LYS E C   1 
ATOM   6738 O  O   . LYS E 1 132 ? 73.870  91.122  65.262  1.00 25.26 ? 129 LYS E O   1 
ATOM   6739 C  CB  . LYS E 1 132 ? 74.198  90.218  62.582  1.00 26.09 ? 129 LYS E CB  1 
ATOM   6740 C  CG  . LYS E 1 132 ? 74.193  89.976  61.061  1.00 26.78 ? 129 LYS E CG  1 
ATOM   6741 C  CD  . LYS E 1 132 ? 73.647  88.584  60.651  1.00 27.49 ? 129 LYS E CD  1 
ATOM   6742 C  CE  . LYS E 1 132 ? 74.232  88.105  59.278  1.00 29.06 ? 129 LYS E CE  1 
ATOM   6743 N  NZ  . LYS E 1 132 ? 74.031  89.045  58.087  1.00 28.34 ? 129 LYS E NZ  1 
ATOM   6744 N  N   . PHE E 1 133 ? 74.948  93.060  64.947  1.00 25.27 ? 130 PHE E N   1 
ATOM   6745 C  CA  . PHE E 1 133 ? 74.925  93.418  66.351  1.00 24.57 ? 130 PHE E CA  1 
ATOM   6746 C  C   . PHE E 1 133 ? 74.652  94.899  66.559  1.00 24.01 ? 130 PHE E C   1 
ATOM   6747 O  O   . PHE E 1 133 ? 75.346  95.762  66.027  1.00 23.89 ? 130 PHE E O   1 
ATOM   6748 C  CB  . PHE E 1 133 ? 76.195  92.976  67.091  1.00 24.45 ? 130 PHE E CB  1 
ATOM   6749 C  CG  . PHE E 1 133 ? 75.930  92.625  68.522  1.00 25.54 ? 130 PHE E CG  1 
ATOM   6750 C  CD1 . PHE E 1 133 ? 76.188  93.541  69.539  1.00 25.94 ? 130 PHE E CD1 1 
ATOM   6751 C  CD2 . PHE E 1 133 ? 75.353  91.395  68.854  1.00 26.94 ? 130 PHE E CD2 1 
ATOM   6752 C  CE1 . PHE E 1 133 ? 75.905  93.229  70.883  1.00 26.16 ? 130 PHE E CE1 1 
ATOM   6753 C  CE2 . PHE E 1 133 ? 75.050  91.079  70.189  1.00 28.23 ? 130 PHE E CE2 1 
ATOM   6754 C  CZ  . PHE E 1 133 ? 75.325  92.003  71.206  1.00 26.26 ? 130 PHE E CZ  1 
ATOM   6755 N  N   . THR E 1 134 ? 73.625  95.167  67.350  1.00 24.01 ? 131 THR E N   1 
ATOM   6756 C  CA  . THR E 1 134 ? 73.146  96.509  67.585  1.00 24.41 ? 131 THR E CA  1 
ATOM   6757 C  C   . THR E 1 134 ? 72.493  96.591  68.977  1.00 25.17 ? 131 THR E C   1 
ATOM   6758 O  O   . THR E 1 134 ? 72.649  95.669  69.820  1.00 25.89 ? 131 THR E O   1 
ATOM   6759 C  CB  . THR E 1 134 ? 72.222  97.006  66.418  1.00 24.41 ? 131 THR E CB  1 
ATOM   6760 O  OG1 . THR E 1 134 ? 71.881  98.373  66.622  1.00 24.58 ? 131 THR E OG1 1 
ATOM   6761 C  CG2 . THR E 1 134 ? 70.941  96.161  66.269  1.00 22.33 ? 131 THR E CG2 1 
ATOM   6762 N  N   . LEU E 1 135 ? 71.787  97.686  69.240  1.00 24.70 ? 132 LEU E N   1 
ATOM   6763 C  CA  . LEU E 1 135 ? 71.290  97.930  70.587  1.00 24.57 ? 132 LEU E CA  1 
ATOM   6764 C  C   . LEU E 1 135 ? 70.130  98.940  70.578  1.00 25.08 ? 132 LEU E C   1 
ATOM   6765 O  O   . LEU E 1 135 ? 70.171  99.921  71.303  1.00 25.59 ? 132 LEU E O   1 
ATOM   6766 C  CB  . LEU E 1 135 ? 72.445  98.379  71.497  1.00 23.82 ? 132 LEU E CB  1 
ATOM   6767 C  CG  . LEU E 1 135 ? 73.332  99.569  71.085  1.00 22.71 ? 132 LEU E CG  1 
ATOM   6768 C  CD1 . LEU E 1 135 ? 73.870  100.315 72.282  1.00 18.43 ? 132 LEU E CD1 1 
ATOM   6769 C  CD2 . LEU E 1 135 ? 74.489  99.143  70.155  1.00 22.55 ? 132 LEU E CD2 1 
ATOM   6770 N  N   . HIS E 1 136 ? 69.110  98.686  69.749  1.00 24.93 ? 133 HIS E N   1 
ATOM   6771 C  CA  . HIS E 1 136 ? 68.054  99.661  69.488  1.00 24.84 ? 133 HIS E CA  1 
ATOM   6772 C  C   . HIS E 1 136 ? 67.200  100.069 70.699  1.00 26.13 ? 133 HIS E C   1 
ATOM   6773 O  O   . HIS E 1 136 ? 66.632  101.159 70.702  1.00 26.61 ? 133 HIS E O   1 
ATOM   6774 C  CB  . HIS E 1 136 ? 67.123  99.174  68.384  1.00 24.54 ? 133 HIS E CB  1 
ATOM   6775 C  CG  . HIS E 1 136 ? 67.770  99.016  67.033  1.00 22.41 ? 133 HIS E CG  1 
ATOM   6776 N  ND1 . HIS E 1 136 ? 68.961  99.614  66.694  1.00 21.26 ? 133 HIS E ND1 1 
ATOM   6777 C  CD2 . HIS E 1 136 ? 67.370  98.332  65.935  1.00 19.96 ? 133 HIS E CD2 1 
ATOM   6778 C  CE1 . HIS E 1 136 ? 69.266  99.312  65.445  1.00 21.86 ? 133 HIS E CE1 1 
ATOM   6779 N  NE2 . HIS E 1 136 ? 68.312  98.542  64.959  1.00 21.63 ? 133 HIS E NE2 1 
ATOM   6780 N  N   . TYR E 1 137 ? 67.084  99.191  71.693  1.00 26.61 ? 134 TYR E N   1 
ATOM   6781 C  CA  . TYR E 1 137 ? 66.277  99.448  72.882  1.00 27.39 ? 134 TYR E CA  1 
ATOM   6782 C  C   . TYR E 1 137 ? 67.163  99.460  74.122  1.00 27.26 ? 134 TYR E C   1 
ATOM   6783 O  O   . TYR E 1 137 ? 66.699  99.684  75.229  1.00 28.45 ? 134 TYR E O   1 
ATOM   6784 C  CB  . TYR E 1 137 ? 65.052  98.472  72.974  1.00 28.18 ? 134 TYR E CB  1 
ATOM   6785 C  CG  . TYR E 1 137 ? 64.208  98.608  71.710  1.00 28.60 ? 134 TYR E CG  1 
ATOM   6786 C  CD1 . TYR E 1 137 ? 64.351  97.717  70.654  1.00 32.46 ? 134 TYR E CD1 1 
ATOM   6787 C  CD2 . TYR E 1 137 ? 63.376  99.704  71.523  1.00 29.34 ? 134 TYR E CD2 1 
ATOM   6788 C  CE1 . TYR E 1 137 ? 63.640  97.890  69.437  1.00 31.96 ? 134 TYR E CE1 1 
ATOM   6789 C  CE2 . TYR E 1 137 ? 62.661  99.889  70.314  1.00 30.94 ? 134 TYR E CE2 1 
ATOM   6790 C  CZ  . TYR E 1 137 ? 62.796  98.969  69.284  1.00 29.98 ? 134 TYR E CZ  1 
ATOM   6791 O  OH  . TYR E 1 137 ? 62.108  99.146  68.100  1.00 29.76 ? 134 TYR E OH  1 
ATOM   6792 N  N   . GLY E 1 138 ? 68.457  99.258  73.927  1.00 27.03 ? 135 GLY E N   1 
ATOM   6793 C  CA  . GLY E 1 138 ? 69.395  99.203  75.037  1.00 25.77 ? 135 GLY E CA  1 
ATOM   6794 C  C   . GLY E 1 138 ? 70.427  98.163  74.716  1.00 25.57 ? 135 GLY E C   1 
ATOM   6795 O  O   . GLY E 1 138 ? 70.257  97.387  73.773  1.00 25.78 ? 135 GLY E O   1 
ATOM   6796 N  N   . ALA E 1 139 ? 71.502  98.135  75.493  1.00 25.16 ? 136 ALA E N   1 
ATOM   6797 C  CA  . ALA E 1 139 ? 72.541  97.153  75.273  1.00 25.61 ? 136 ALA E CA  1 
ATOM   6798 C  C   . ALA E 1 139 ? 72.037  95.779  75.778  1.00 25.54 ? 136 ALA E C   1 
ATOM   6799 O  O   . ALA E 1 139 ? 71.516  95.652  76.909  1.00 24.22 ? 136 ALA E O   1 
ATOM   6800 C  CB  . ALA E 1 139 ? 73.871  97.577  75.937  1.00 25.07 ? 136 ALA E CB  1 
ATOM   6801 N  N   . VAL E 1 140 ? 72.143  94.766  74.918  1.00 25.56 ? 137 VAL E N   1 
ATOM   6802 C  CA  . VAL E 1 140 ? 71.661  93.451  75.319  1.00 25.36 ? 137 VAL E CA  1 
ATOM   6803 C  C   . VAL E 1 140 ? 72.709  92.366  75.115  1.00 25.96 ? 137 VAL E C   1 
ATOM   6804 O  O   . VAL E 1 140 ? 73.458  92.386  74.136  1.00 26.05 ? 137 VAL E O   1 
ATOM   6805 C  CB  . VAL E 1 140 ? 70.257  93.081  74.742  1.00 25.08 ? 137 VAL E CB  1 
ATOM   6806 C  CG1 . VAL E 1 140 ? 69.134  93.941  75.380  1.00 24.07 ? 137 VAL E CG1 1 
ATOM   6807 C  CG2 . VAL E 1 140 ? 70.223  93.082  73.233  1.00 24.26 ? 137 VAL E CG2 1 
ATOM   6808 N  N   . VAL E 1 141 ? 72.779  91.436  76.066  1.00 26.20 ? 138 VAL E N   1 
ATOM   6809 C  CA  . VAL E 1 141 ? 73.733  90.312  75.959  1.00 27.12 ? 138 VAL E CA  1 
ATOM   6810 C  C   . VAL E 1 141 ? 73.091  89.026  76.476  1.00 26.60 ? 138 VAL E C   1 
ATOM   6811 O  O   . VAL E 1 141 ? 72.228  89.073  77.331  1.00 26.73 ? 138 VAL E O   1 
ATOM   6812 C  CB  . VAL E 1 141 ? 75.065  90.607  76.729  1.00 26.55 ? 138 VAL E CB  1 
ATOM   6813 C  CG1 . VAL E 1 141 ? 75.939  89.414  76.734  1.00 27.75 ? 138 VAL E CG1 1 
ATOM   6814 C  CG2 . VAL E 1 141 ? 75.811  91.749  76.059  1.00 27.96 ? 138 VAL E CG2 1 
ATOM   6815 N  N   . ALA E 1 142 ? 73.510  87.887  75.944  1.00 26.40 ? 139 ALA E N   1 
ATOM   6816 C  CA  . ALA E 1 142 ? 73.192  86.596  76.551  1.00 26.31 ? 139 ALA E CA  1 
ATOM   6817 C  C   . ALA E 1 142 ? 74.381  86.146  77.403  1.00 26.25 ? 139 ALA E C   1 
ATOM   6818 O  O   . ALA E 1 142 ? 75.447  85.788  76.878  1.00 26.10 ? 139 ALA E O   1 
ATOM   6819 C  CB  . ALA E 1 142 ? 72.826  85.544  75.490  1.00 25.62 ? 139 ALA E CB  1 
ATOM   6820 N  N   . GLY E 1 143 ? 74.187  86.196  78.718  1.00 26.24 ? 140 GLY E N   1 
ATOM   6821 C  CA  . GLY E 1 143 ? 75.253  85.946  79.682  1.00 26.50 ? 140 GLY E CA  1 
ATOM   6822 C  C   . GLY E 1 143 ? 76.177  87.142  79.868  1.00 26.67 ? 140 GLY E C   1 
ATOM   6823 O  O   . GLY E 1 143 ? 75.740  88.294  79.883  1.00 26.49 ? 140 GLY E O   1 
ATOM   6824 N  N   . GLU E 1 144 ? 77.462  86.850  80.005  1.00 27.16 ? 141 GLU E N   1 
ATOM   6825 C  CA  . GLU E 1 144 ? 78.508  87.850  80.122  1.00 28.16 ? 141 GLU E CA  1 
ATOM   6826 C  C   . GLU E 1 144 ? 78.991  88.436  78.767  1.00 28.40 ? 141 GLU E C   1 
ATOM   6827 O  O   . GLU E 1 144 ? 79.158  87.695  77.770  1.00 27.66 ? 141 GLU E O   1 
ATOM   6828 C  CB  . GLU E 1 144 ? 79.688  87.210  80.828  1.00 28.46 ? 141 GLU E CB  1 
ATOM   6829 C  CG  . GLU E 1 144 ? 80.665  88.203  81.411  1.00 30.92 ? 141 GLU E CG  1 
ATOM   6830 C  CD  . GLU E 1 144 ? 82.013  87.578  81.646  1.00 34.06 ? 141 GLU E CD  1 
ATOM   6831 O  OE1 . GLU E 1 144 ? 82.994  88.090  81.059  1.00 36.15 ? 141 GLU E OE1 1 
ATOM   6832 O  OE2 . GLU E 1 144 ? 82.079  86.569  82.394  1.00 33.37 ? 141 GLU E OE2 1 
ATOM   6833 N  N   . PRO E 1 145 ? 79.248  89.765  78.739  1.00 28.62 ? 142 PRO E N   1 
ATOM   6834 C  CA  . PRO E 1 145 ? 79.805  90.368  77.534  1.00 28.95 ? 142 PRO E CA  1 
ATOM   6835 C  C   . PRO E 1 145 ? 81.288  89.945  77.376  1.00 29.64 ? 142 PRO E C   1 
ATOM   6836 O  O   . PRO E 1 145 ? 82.146  90.254  78.222  1.00 29.45 ? 142 PRO E O   1 
ATOM   6837 C  CB  . PRO E 1 145 ? 79.634  91.868  77.778  1.00 28.73 ? 142 PRO E CB  1 
ATOM   6838 C  CG  . PRO E 1 145 ? 79.667  92.010  79.244  1.00 28.12 ? 142 PRO E CG  1 
ATOM   6839 C  CD  . PRO E 1 145 ? 79.077  90.755  79.819  1.00 28.52 ? 142 PRO E CD  1 
ATOM   6840 N  N   . ARG E 1 146 ? 81.550  89.205  76.302  1.00 30.26 ? 143 ARG E N   1 
ATOM   6841 C  CA  . ARG E 1 146 ? 82.826  88.567  76.079  1.00 31.00 ? 143 ARG E CA  1 
ATOM   6842 C  C   . ARG E 1 146 ? 83.381  88.974  74.718  1.00 31.42 ? 143 ARG E C   1 
ATOM   6843 O  O   . ARG E 1 146 ? 84.559  89.328  74.615  1.00 31.38 ? 143 ARG E O   1 
ATOM   6844 C  CB  . ARG E 1 146 ? 82.680  87.040  76.189  1.00 31.09 ? 143 ARG E CB  1 
ATOM   6845 C  CG  . ARG E 1 146 ? 82.618  86.523  77.626  1.00 32.62 ? 143 ARG E CG  1 
ATOM   6846 C  CD  . ARG E 1 146 ? 84.024  86.473  78.264  1.00 37.06 ? 143 ARG E CD  1 
ATOM   6847 N  NE  . ARG E 1 146 ? 84.547  85.112  78.480  1.00 39.10 ? 143 ARG E NE  1 
ATOM   6848 C  CZ  . ARG E 1 146 ? 84.745  84.175  77.539  1.00 39.76 ? 143 ARG E CZ  1 
ATOM   6849 N  NH1 . ARG E 1 146 ? 84.454  84.386  76.258  1.00 39.61 ? 143 ARG E NH1 1 
ATOM   6850 N  NH2 . ARG E 1 146 ? 85.221  82.989  77.893  1.00 40.43 ? 143 ARG E NH2 1 
ATOM   6851 N  N   . SER E 1 147 ? 82.533  88.919  73.684  1.00 31.58 ? 144 SER E N   1 
ATOM   6852 C  CA  . SER E 1 147 ? 82.929  89.297  72.324  1.00 31.66 ? 144 SER E CA  1 
ATOM   6853 C  C   . SER E 1 147 ? 83.074  90.807  72.207  1.00 31.83 ? 144 SER E C   1 
ATOM   6854 O  O   . SER E 1 147 ? 82.511  91.556  73.010  1.00 32.36 ? 144 SER E O   1 
ATOM   6855 C  CB  . SER E 1 147 ? 81.955  88.734  71.261  1.00 31.67 ? 144 SER E CB  1 
ATOM   6856 O  OG  . SER E 1 147 ? 80.889  89.616  70.947  1.00 30.98 ? 144 SER E OG  1 
ATOM   6857 N  N   . GLU E 1 148 ? 83.829  91.248  71.206  1.00 31.87 ? 145 GLU E N   1 
ATOM   6858 C  CA  . GLU E 1 148 ? 84.073  92.661  71.004  1.00 31.88 ? 145 GLU E CA  1 
ATOM   6859 C  C   . GLU E 1 148 ? 82.798  93.430  70.679  1.00 31.78 ? 145 GLU E C   1 
ATOM   6860 O  O   . GLU E 1 148 ? 82.583  94.520  71.213  1.00 32.07 ? 145 GLU E O   1 
ATOM   6861 C  CB  . GLU E 1 148 ? 85.161  92.890  69.948  1.00 32.25 ? 145 GLU E CB  1 
ATOM   6862 C  CG  . GLU E 1 148 ? 86.579  92.488  70.404  1.00 34.26 ? 145 GLU E CG  1 
ATOM   6863 C  CD  . GLU E 1 148 ? 86.832  92.727  71.911  1.00 37.21 ? 145 GLU E CD  1 
ATOM   6864 O  OE1 . GLU E 1 148 ? 86.973  93.906  72.315  1.00 37.77 ? 145 GLU E OE1 1 
ATOM   6865 O  OE2 . GLU E 1 148 ? 86.886  91.732  72.690  1.00 37.57 ? 145 GLU E OE2 1 
ATOM   6866 N  N   . GLU E 1 149 ? 81.946  92.868  69.821  1.00 31.26 ? 146 GLU E N   1 
ATOM   6867 C  CA  . GLU E 1 149 ? 80.657  93.501  69.523  1.00 30.41 ? 146 GLU E CA  1 
ATOM   6868 C  C   . GLU E 1 149 ? 79.802  93.568  70.791  1.00 30.14 ? 146 GLU E C   1 
ATOM   6869 O  O   . GLU E 1 149 ? 79.211  94.613  71.078  1.00 29.84 ? 146 GLU E O   1 
ATOM   6870 C  CB  . GLU E 1 149 ? 79.929  92.830  68.346  1.00 30.19 ? 146 GLU E CB  1 
ATOM   6871 C  CG  . GLU E 1 149 ? 79.470  91.389  68.569  1.00 30.04 ? 146 GLU E CG  1 
ATOM   6872 C  CD  . GLU E 1 149 ? 78.984  90.693  67.289  1.00 30.68 ? 146 GLU E CD  1 
ATOM   6873 O  OE1 . GLU E 1 149 ? 78.498  89.533  67.380  1.00 30.96 ? 146 GLU E OE1 1 
ATOM   6874 O  OE2 . GLU E 1 149 ? 79.083  91.293  66.193  1.00 30.10 ? 146 GLU E OE2 1 
ATOM   6875 N  N   . GLU E 1 150 ? 79.787  92.479  71.570  1.00 29.68 ? 147 GLU E N   1 
ATOM   6876 C  CA  . GLU E 1 150 ? 79.112  92.457  72.878  1.00 28.90 ? 147 GLU E CA  1 
ATOM   6877 C  C   . GLU E 1 150 ? 79.706  93.497  73.813  1.00 28.12 ? 147 GLU E C   1 
ATOM   6878 O  O   . GLU E 1 150 ? 78.987  94.219  74.452  1.00 27.75 ? 147 GLU E O   1 
ATOM   6879 C  CB  . GLU E 1 150 ? 79.181  91.070  73.516  1.00 28.72 ? 147 GLU E CB  1 
ATOM   6880 C  CG  . GLU E 1 150 ? 78.206  90.053  72.912  1.00 28.98 ? 147 GLU E CG  1 
ATOM   6881 C  CD  . GLU E 1 150 ? 78.428  88.606  73.398  1.00 30.25 ? 147 GLU E CD  1 
ATOM   6882 O  OE1 . GLU E 1 150 ? 79.442  88.308  74.103  1.00 29.21 ? 147 GLU E OE1 1 
ATOM   6883 O  OE2 . GLU E 1 150 ? 77.559  87.762  73.061  1.00 31.50 ? 147 GLU E OE2 1 
ATOM   6884 N  N   . LYS E 1 151 ? 81.031  93.603  73.865  1.00 27.99 ? 148 LYS E N   1 
ATOM   6885 C  CA  . LYS E 1 151 ? 81.653  94.618  74.727  1.00 27.27 ? 148 LYS E CA  1 
ATOM   6886 C  C   . LYS E 1 151 ? 81.427  96.052  74.204  1.00 27.26 ? 148 LYS E C   1 
ATOM   6887 O  O   . LYS E 1 151 ? 81.136  96.966  74.977  1.00 26.91 ? 148 LYS E O   1 
ATOM   6888 C  CB  . LYS E 1 151 ? 83.133  94.314  74.951  1.00 27.02 ? 148 LYS E CB  1 
ATOM   6889 C  CG  . LYS E 1 151 ? 83.415  93.121  75.870  1.00 27.49 ? 148 LYS E CG  1 
ATOM   6890 C  CD  . LYS E 1 151 ? 84.932  92.808  75.944  1.00 26.53 ? 148 LYS E CD  1 
ATOM   6891 C  CE  . LYS E 1 151 ? 85.275  91.680  76.939  1.00 27.32 ? 148 LYS E CE  1 
ATOM   6892 N  NZ  . LYS E 1 151 ? 86.765  91.328  77.026  1.00 25.59 ? 148 LYS E NZ  1 
ATOM   6893 N  N   . GLU E 1 152 ? 81.519  96.234  72.892  1.00 27.46 ? 149 GLU E N   1 
ATOM   6894 C  CA  . GLU E 1 152 ? 81.386  97.560  72.291  1.00 28.32 ? 149 GLU E CA  1 
ATOM   6895 C  C   . GLU E 1 152 ? 79.953  98.088  72.217  1.00 28.31 ? 149 GLU E C   1 
ATOM   6896 O  O   . GLU E 1 152 ? 79.752  99.296  72.034  1.00 29.17 ? 149 GLU E O   1 
ATOM   6897 C  CB  . GLU E 1 152 ? 82.074  97.623  70.914  1.00 28.39 ? 149 GLU E CB  1 
ATOM   6898 C  CG  . GLU E 1 152 ? 82.003  98.978  70.197  1.00 29.54 ? 149 GLU E CG  1 
ATOM   6899 C  CD  . GLU E 1 152 ? 82.793  100.084 70.878  1.00 32.50 ? 149 GLU E CD  1 
ATOM   6900 O  OE1 . GLU E 1 152 ? 82.468  101.269 70.654  1.00 33.16 ? 149 GLU E OE1 1 
ATOM   6901 O  OE2 . GLU E 1 152 ? 83.748  99.778  71.627  1.00 34.44 ? 149 GLU E OE2 1 
ATOM   6902 N  N   . ALA E 1 153 ? 78.967  97.207  72.358  1.00 27.92 ? 150 ALA E N   1 
ATOM   6903 C  CA  . ALA E 1 153 ? 77.577  97.653  72.471  1.00 27.65 ? 150 ALA E CA  1 
ATOM   6904 C  C   . ALA E 1 153 ? 77.377  98.337  73.803  1.00 27.79 ? 150 ALA E C   1 
ATOM   6905 O  O   . ALA E 1 153 ? 76.741  99.384  73.875  1.00 27.87 ? 150 ALA E O   1 
ATOM   6906 C  CB  . ALA E 1 153 ? 76.609  96.496  72.335  1.00 27.02 ? 150 ALA E CB  1 
ATOM   6907 N  N   . CYS E 1 154 ? 77.916  97.733  74.853  1.00 28.12 ? 151 CYS E N   1 
ATOM   6908 C  CA  . CYS E 1 154 ? 77.830  98.294  76.195  1.00 29.01 ? 151 CYS E CA  1 
ATOM   6909 C  C   . CYS E 1 154 ? 78.513  99.655  76.240  1.00 29.04 ? 151 CYS E C   1 
ATOM   6910 O  O   . CYS E 1 154 ? 77.917  100.647 76.713  1.00 29.59 ? 151 CYS E O   1 
ATOM   6911 C  CB  . CYS E 1 154 ? 78.492  97.358  77.212  1.00 29.34 ? 151 CYS E CB  1 
ATOM   6912 S  SG  . CYS E 1 154 ? 77.662  95.762  77.459  1.00 30.67 ? 151 CYS E SG  1 
ATOM   6913 N  N   . ARG E 1 155 ? 79.763  99.681  75.758  1.00 28.59 ? 152 ARG E N   1 
ATOM   6914 C  CA  . ARG E 1 155 ? 80.523  100.904 75.567  1.00 28.03 ? 152 ARG E CA  1 
ATOM   6915 C  C   . ARG E 1 155 ? 79.737  101.982 74.828  1.00 28.00 ? 152 ARG E C   1 
ATOM   6916 O  O   . ARG E 1 155 ? 79.698  103.127 75.271  1.00 28.38 ? 152 ARG E O   1 
ATOM   6917 C  CB  . ARG E 1 155 ? 81.811  100.610 74.819  1.00 28.04 ? 152 ARG E CB  1 
ATOM   6918 C  CG  . ARG E 1 155 ? 82.938  100.174 75.726  1.00 27.92 ? 152 ARG E CG  1 
ATOM   6919 C  CD  . ARG E 1 155 ? 84.267  100.190 75.007  1.00 28.72 ? 152 ARG E CD  1 
ATOM   6920 N  NE  . ARG E 1 155 ? 85.143  99.175  75.574  1.00 28.96 ? 152 ARG E NE  1 
ATOM   6921 C  CZ  . ARG E 1 155 ? 85.332  97.969  75.049  1.00 28.58 ? 152 ARG E CZ  1 
ATOM   6922 N  NH1 . ARG E 1 155 ? 84.737  97.626  73.913  1.00 27.06 ? 152 ARG E NH1 1 
ATOM   6923 N  NH2 . ARG E 1 155 ? 86.139  97.110  75.658  1.00 28.44 ? 152 ARG E NH2 1 
ATOM   6924 N  N   . ARG E 1 156 ? 79.102  101.614 73.718  1.00 27.23 ? 153 ARG E N   1 
ATOM   6925 C  CA  . ARG E 1 156 ? 78.362  102.568 72.914  1.00 27.34 ? 153 ARG E CA  1 
ATOM   6926 C  C   . ARG E 1 156 ? 77.100  103.180 73.552  1.00 27.90 ? 153 ARG E C   1 
ATOM   6927 O  O   . ARG E 1 156 ? 76.785  104.359 73.304  1.00 27.53 ? 153 ARG E O   1 
ATOM   6928 C  CB  . ARG E 1 156 ? 77.983  101.957 71.573  1.00 27.67 ? 153 ARG E CB  1 
ATOM   6929 C  CG  . ARG E 1 156 ? 77.396  103.004 70.644  1.00 28.30 ? 153 ARG E CG  1 
ATOM   6930 C  CD  . ARG E 1 156 ? 78.498  103.972 70.114  1.00 28.75 ? 153 ARG E CD  1 
ATOM   6931 N  NE  . ARG E 1 156 ? 78.759  103.590 68.739  1.00 28.37 ? 153 ARG E NE  1 
ATOM   6932 C  CZ  . ARG E 1 156 ? 79.714  102.771 68.358  1.00 27.03 ? 153 ARG E CZ  1 
ATOM   6933 N  NH1 . ARG E 1 156 ? 80.569  102.300 69.252  1.00 25.99 ? 153 ARG E NH1 1 
ATOM   6934 N  NH2 . ARG E 1 156 ? 79.811  102.449 67.073  1.00 28.38 ? 153 ARG E NH2 1 
ATOM   6935 N  N   . LEU E 1 157 ? 76.356  102.371 74.316  1.00 27.81 ? 154 LEU E N   1 
ATOM   6936 C  CA  . LEU E 1 157 ? 75.212  102.869 75.061  1.00 28.00 ? 154 LEU E CA  1 
ATOM   6937 C  C   . LEU E 1 157 ? 75.657  104.027 75.941  1.00 28.50 ? 154 LEU E C   1 
ATOM   6938 O  O   . LEU E 1 157 ? 75.056  105.111 75.900  1.00 28.60 ? 154 LEU E O   1 
ATOM   6939 C  CB  . LEU E 1 157 ? 74.577  101.763 75.924  1.00 28.43 ? 154 LEU E CB  1 
ATOM   6940 C  CG  . LEU E 1 157 ? 73.299  102.102 76.700  1.00 26.48 ? 154 LEU E CG  1 
ATOM   6941 C  CD1 . LEU E 1 157 ? 72.103  101.931 75.822  1.00 24.70 ? 154 LEU E CD1 1 
ATOM   6942 C  CD2 . LEU E 1 157 ? 73.193  101.185 77.890  1.00 27.87 ? 154 LEU E CD2 1 
ATOM   6943 N  N   . GLY E 1 158 ? 76.723  103.796 76.713  1.00 28.38 ? 155 GLY E N   1 
ATOM   6944 C  CA  . GLY E 1 158 ? 77.243  104.804 77.621  1.00 28.39 ? 155 GLY E CA  1 
ATOM   6945 C  C   . GLY E 1 158 ? 77.805  106.012 76.900  1.00 27.90 ? 155 GLY E C   1 
ATOM   6946 O  O   . GLY E 1 158 ? 77.727  107.136 77.402  1.00 27.41 ? 155 GLY E O   1 
ATOM   6947 N  N   . ARG E 1 159 ? 78.369  105.768 75.718  1.00 27.87 ? 156 ARG E N   1 
ATOM   6948 C  CA  . ARG E 1 159 ? 78.915  106.833 74.870  1.00 27.71 ? 156 ARG E CA  1 
ATOM   6949 C  C   . ARG E 1 159 ? 77.794  107.791 74.466  1.00 27.92 ? 156 ARG E C   1 
ATOM   6950 O  O   . ARG E 1 159 ? 77.882  109.001 74.694  1.00 28.63 ? 156 ARG E O   1 
ATOM   6951 C  CB  . ARG E 1 159 ? 79.548  106.243 73.612  1.00 26.84 ? 156 ARG E CB  1 
ATOM   6952 C  CG  . ARG E 1 159 ? 80.886  106.837 73.251  1.00 27.85 ? 156 ARG E CG  1 
ATOM   6953 C  CD  . ARG E 1 159 ? 80.826  108.226 72.635  1.00 25.34 ? 156 ARG E CD  1 
ATOM   6954 N  NE  . ARG E 1 159 ? 81.901  109.009 73.205  1.00 24.98 ? 156 ARG E NE  1 
ATOM   6955 C  CZ  . ARG E 1 159 ? 82.910  109.584 72.543  1.00 24.42 ? 156 ARG E CZ  1 
ATOM   6956 N  NH1 . ARG E 1 159 ? 83.028  109.562 71.217  1.00 22.46 ? 156 ARG E NH1 1 
ATOM   6957 N  NH2 . ARG E 1 159 ? 83.799  110.236 73.247  1.00 23.59 ? 156 ARG E NH2 1 
ATOM   6958 N  N   . ARG E 1 160 ? 76.742  107.232 73.878  1.00 27.30 ? 157 ARG E N   1 
ATOM   6959 C  CA  . ARG E 1 160 ? 75.624  107.986 73.374  1.00 27.08 ? 157 ARG E CA  1 
ATOM   6960 C  C   . ARG E 1 160 ? 74.847  108.684 74.489  1.00 27.08 ? 157 ARG E C   1 
ATOM   6961 O  O   . ARG E 1 160 ? 74.341  109.774 74.283  1.00 27.19 ? 157 ARG E O   1 
ATOM   6962 C  CB  . ARG E 1 160 ? 74.716  107.035 72.580  1.00 27.29 ? 157 ARG E CB  1 
ATOM   6963 C  CG  . ARG E 1 160 ? 73.613  107.692 71.729  1.00 27.46 ? 157 ARG E CG  1 
ATOM   6964 C  CD  . ARG E 1 160 ? 74.143  108.681 70.667  1.00 28.26 ? 157 ARG E CD  1 
ATOM   6965 N  NE  . ARG E 1 160 ? 75.391  108.245 70.025  1.00 27.02 ? 157 ARG E NE  1 
ATOM   6966 C  CZ  . ARG E 1 160 ? 75.491  107.288 69.107  1.00 27.99 ? 157 ARG E CZ  1 
ATOM   6967 N  NH1 . ARG E 1 160 ? 74.409  106.608 68.705  1.00 29.25 ? 157 ARG E NH1 1 
ATOM   6968 N  NH2 . ARG E 1 160 ? 76.687  106.997 68.596  1.00 28.09 ? 157 ARG E NH2 1 
ATOM   6969 N  N   . LEU E 1 161 ? 74.729  108.043 75.655  1.00 27.12 ? 158 LEU E N   1 
ATOM   6970 C  CA  . LEU E 1 161 ? 74.154  108.667 76.846  1.00 26.57 ? 158 LEU E CA  1 
ATOM   6971 C  C   . LEU E 1 161 ? 74.900  109.951 77.142  1.00 26.76 ? 158 LEU E C   1 
ATOM   6972 O  O   . LEU E 1 161 ? 74.270  110.991 77.319  1.00 27.39 ? 158 LEU E O   1 
ATOM   6973 C  CB  . LEU E 1 161 ? 74.275  107.758 78.075  1.00 26.49 ? 158 LEU E CB  1 
ATOM   6974 C  CG  . LEU E 1 161 ? 73.227  107.858 79.208  1.00 26.87 ? 158 LEU E CG  1 
ATOM   6975 C  CD1 . LEU E 1 161 ? 73.803  107.386 80.515  1.00 25.30 ? 158 LEU E CD1 1 
ATOM   6976 C  CD2 . LEU E 1 161 ? 72.635  109.234 79.395  1.00 25.63 ? 158 LEU E CD2 1 
ATOM   6977 N  N   . ALA E 1 162 ? 76.237  109.871 77.200  1.00 26.45 ? 159 ALA E N   1 
ATOM   6978 C  CA  . ALA E 1 162 ? 77.088  111.025 77.492  1.00 26.15 ? 159 ALA E CA  1 
ATOM   6979 C  C   . ALA E 1 162 ? 77.014  112.072 76.387  1.00 25.88 ? 159 ALA E C   1 
ATOM   6980 O  O   . ALA E 1 162 ? 76.996  113.280 76.684  1.00 26.50 ? 159 ALA E O   1 
ATOM   6981 C  CB  . ALA E 1 162 ? 78.562  110.596 77.767  1.00 25.64 ? 159 ALA E CB  1 
ATOM   6982 N  N   . GLU E 1 163 ? 76.984  111.614 75.128  1.00 25.69 ? 160 GLU E N   1 
ATOM   6983 C  CA  . GLU E 1 163 ? 76.838  112.502 73.967  1.00 25.77 ? 160 GLU E CA  1 
ATOM   6984 C  C   . GLU E 1 163 ? 75.500  113.237 74.014  1.00 25.51 ? 160 GLU E C   1 
ATOM   6985 O  O   . GLU E 1 163 ? 75.412  114.415 73.653  1.00 25.54 ? 160 GLU E O   1 
ATOM   6986 C  CB  . GLU E 1 163 ? 76.960  111.726 72.646  1.00 25.76 ? 160 GLU E CB  1 
ATOM   6987 C  CG  . GLU E 1 163 ? 78.378  111.202 72.290  1.00 26.20 ? 160 GLU E CG  1 
ATOM   6988 C  CD  . GLU E 1 163 ? 78.383  110.194 71.116  1.00 26.45 ? 160 GLU E CD  1 
ATOM   6989 O  OE1 . GLU E 1 163 ? 77.356  109.529 70.875  1.00 26.91 ? 160 GLU E OE1 1 
ATOM   6990 O  OE2 . GLU E 1 163 ? 79.419  110.042 70.433  1.00 27.02 ? 160 GLU E OE2 1 
ATOM   6991 N  N   . TRP E 1 164 ? 74.463  112.541 74.479  1.00 25.20 ? 161 TRP E N   1 
ATOM   6992 C  CA  . TRP E 1 164 ? 73.120  113.125 74.593  1.00 24.98 ? 161 TRP E CA  1 
ATOM   6993 C  C   . TRP E 1 164 ? 73.059  114.170 75.708  1.00 25.02 ? 161 TRP E C   1 
ATOM   6994 O  O   . TRP E 1 164 ? 72.464  115.226 75.530  1.00 24.58 ? 161 TRP E O   1 
ATOM   6995 C  CB  . TRP E 1 164 ? 72.035  112.045 74.782  1.00 24.43 ? 161 TRP E CB  1 
ATOM   6996 C  CG  . TRP E 1 164 ? 71.587  111.313 73.525  1.00 23.61 ? 161 TRP E CG  1 
ATOM   6997 C  CD1 . TRP E 1 164 ? 70.862  110.160 73.483  1.00 22.76 ? 161 TRP E CD1 1 
ATOM   6998 C  CD2 . TRP E 1 164 ? 71.815  111.687 72.145  1.00 23.51 ? 161 TRP E CD2 1 
ATOM   6999 N  NE1 . TRP E 1 164 ? 70.621  109.785 72.174  1.00 21.55 ? 161 TRP E NE1 1 
ATOM   7000 C  CE2 . TRP E 1 164 ? 71.192  110.701 71.335  1.00 23.15 ? 161 TRP E CE2 1 
ATOM   7001 C  CE3 . TRP E 1 164 ? 72.466  112.760 71.517  1.00 23.33 ? 161 TRP E CE3 1 
ATOM   7002 C  CZ2 . TRP E 1 164 ? 71.215  110.750 69.930  1.00 23.41 ? 161 TRP E CZ2 1 
ATOM   7003 C  CZ3 . TRP E 1 164 ? 72.497  112.804 70.109  1.00 23.15 ? 161 TRP E CZ3 1 
ATOM   7004 C  CH2 . TRP E 1 164 ? 71.867  111.807 69.338  1.00 23.82 ? 161 TRP E CH2 1 
ATOM   7005 N  N   . VAL E 1 165 ? 73.685  113.863 76.845  1.00 25.46 ? 162 VAL E N   1 
ATOM   7006 C  CA  . VAL E 1 165 ? 73.849  114.823 77.940  1.00 25.90 ? 162 VAL E CA  1 
ATOM   7007 C  C   . VAL E 1 165 ? 74.678  116.045 77.492  1.00 26.09 ? 162 VAL E C   1 
ATOM   7008 O  O   . VAL E 1 165 ? 74.309  117.180 77.817  1.00 26.10 ? 162 VAL E O   1 
ATOM   7009 C  CB  . VAL E 1 165 ? 74.470  114.161 79.210  1.00 25.95 ? 162 VAL E CB  1 
ATOM   7010 C  CG1 . VAL E 1 165 ? 74.701  115.195 80.340  1.00 26.23 ? 162 VAL E CG1 1 
ATOM   7011 C  CG2 . VAL E 1 165 ? 73.602  113.032 79.707  1.00 27.02 ? 162 VAL E CG2 1 
ATOM   7012 N  N   . ALA E 1 166 ? 75.757  115.828 76.732  1.00 25.95 ? 163 ALA E N   1 
ATOM   7013 C  CA  . ALA E 1 166 ? 76.556  116.963 76.240  1.00 26.81 ? 163 ALA E CA  1 
ATOM   7014 C  C   . ALA E 1 166 ? 75.755  117.886 75.314  1.00 26.80 ? 163 ALA E C   1 
ATOM   7015 O  O   . ALA E 1 166 ? 75.784  119.112 75.481  1.00 27.26 ? 163 ALA E O   1 
ATOM   7016 C  CB  . ALA E 1 166 ? 77.910  116.497 75.554  1.00 27.09 ? 163 ALA E CB  1 
ATOM   7017 N  N   . ILE E 1 167 ? 75.057  117.293 74.350  1.00 26.92 ? 164 ILE E N   1 
ATOM   7018 C  CA  . ILE E 1 167 ? 74.297  118.034 73.341  1.00 27.14 ? 164 ILE E CA  1 
ATOM   7019 C  C   . ILE E 1 167 ? 73.094  118.788 73.935  1.00 27.93 ? 164 ILE E C   1 
ATOM   7020 O  O   . ILE E 1 167 ? 72.876  119.977 73.639  1.00 28.01 ? 164 ILE E O   1 
ATOM   7021 C  CB  . ILE E 1 167 ? 73.862  117.098 72.171  1.00 26.99 ? 164 ILE E CB  1 
ATOM   7022 C  CG1 . ILE E 1 167 ? 75.071  116.733 71.307  1.00 26.51 ? 164 ILE E CG1 1 
ATOM   7023 C  CG2 . ILE E 1 167 ? 72.783  117.743 71.297  1.00 26.58 ? 164 ILE E CG2 1 
ATOM   7024 C  CD1 . ILE E 1 167 ? 74.854  115.512 70.407  1.00 26.43 ? 164 ILE E CD1 1 
ATOM   7025 N  N   . PHE E 1 168 ? 72.338  118.099 74.788  1.00 28.81 ? 165 PHE E N   1 
ATOM   7026 C  CA  . PHE E 1 168 ? 71.041  118.585 75.259  1.00 29.48 ? 165 PHE E CA  1 
ATOM   7027 C  C   . PHE E 1 168 ? 71.050  119.318 76.587  1.00 30.48 ? 165 PHE E C   1 
ATOM   7028 O  O   . PHE E 1 168 ? 70.204  120.181 76.805  1.00 30.92 ? 165 PHE E O   1 
ATOM   7029 C  CB  . PHE E 1 168 ? 70.013  117.448 75.282  1.00 29.32 ? 165 PHE E CB  1 
ATOM   7030 C  CG  . PHE E 1 168 ? 69.716  116.900 73.929  1.00 28.24 ? 165 PHE E CG  1 
ATOM   7031 C  CD1 . PHE E 1 168 ? 69.874  115.563 73.667  1.00 26.50 ? 165 PHE E CD1 1 
ATOM   7032 C  CD2 . PHE E 1 168 ? 69.348  117.757 72.886  1.00 29.12 ? 165 PHE E CD2 1 
ATOM   7033 C  CE1 . PHE E 1 168 ? 69.638  115.064 72.400  1.00 28.08 ? 165 PHE E CE1 1 
ATOM   7034 C  CE2 . PHE E 1 168 ? 69.103  117.269 71.613  1.00 28.53 ? 165 PHE E CE2 1 
ATOM   7035 C  CZ  . PHE E 1 168 ? 69.248  115.910 71.371  1.00 28.23 ? 165 PHE E CZ  1 
ATOM   7036 N  N   . VAL E 1 169 ? 71.986  118.982 77.471  1.00 31.41 ? 166 VAL E N   1 
ATOM   7037 C  CA  . VAL E 1 169 ? 72.061  119.655 78.769  1.00 32.33 ? 166 VAL E CA  1 
ATOM   7038 C  C   . VAL E 1 169 ? 73.217  120.671 78.823  1.00 33.19 ? 166 VAL E C   1 
ATOM   7039 O  O   . VAL E 1 169 ? 73.052  121.807 79.281  1.00 33.44 ? 166 VAL E O   1 
ATOM   7040 C  CB  . VAL E 1 169 ? 72.174  118.646 79.935  1.00 32.27 ? 166 VAL E CB  1 
ATOM   7041 C  CG1 . VAL E 1 169 ? 71.649  119.269 81.218  1.00 32.65 ? 166 VAL E CG1 1 
ATOM   7042 C  CG2 . VAL E 1 169 ? 71.404  117.398 79.627  1.00 31.49 ? 166 VAL E CG2 1 
ATOM   7043 N  N   . ASP E 1 170 ? 74.383  120.257 78.340  1.00 33.92 ? 167 ASP E N   1 
ATOM   7044 C  CA  . ASP E 1 170 ? 75.556  121.107 78.337  1.00 34.35 ? 167 ASP E CA  1 
ATOM   7045 C  C   . ASP E 1 170 ? 75.694  121.837 77.010  1.00 34.58 ? 167 ASP E C   1 
ATOM   7046 O  O   . ASP E 1 170 ? 76.654  122.577 76.798  1.00 34.57 ? 167 ASP E O   1 
ATOM   7047 C  CB  . ASP E 1 170 ? 76.790  120.275 78.671  1.00 34.63 ? 167 ASP E CB  1 
ATOM   7048 C  CG  . ASP E 1 170 ? 76.650  119.545 80.008  1.00 35.28 ? 167 ASP E CG  1 
ATOM   7049 O  OD1 . ASP E 1 170 ? 76.062  120.123 80.953  1.00 35.80 ? 167 ASP E OD1 1 
ATOM   7050 O  OD2 . ASP E 1 170 ? 77.129  118.394 80.115  1.00 35.68 ? 167 ASP E OD2 1 
ATOM   7051 N  N   . GLY E 1 171 ? 74.733  121.595 76.120  1.00 34.76 ? 168 GLY E N   1 
ATOM   7052 C  CA  . GLY E 1 171 ? 74.463  122.457 74.969  1.00 35.21 ? 168 GLY E CA  1 
ATOM   7053 C  C   . GLY E 1 171 ? 75.423  122.470 73.792  1.00 35.61 ? 168 GLY E C   1 
ATOM   7054 O  O   . GLY E 1 171 ? 75.279  123.312 72.889  1.00 35.78 ? 168 GLY E O   1 
ATOM   7055 N  N   . ARG E 1 172 ? 76.400  121.561 73.773  1.00 35.68 ? 169 ARG E N   1 
ATOM   7056 C  CA  . ARG E 1 172 ? 77.359  121.587 72.673  1.00 35.45 ? 169 ARG E CA  1 
ATOM   7057 C  C   . ARG E 1 172 ? 76.837  120.876 71.421  1.00 35.62 ? 169 ARG E C   1 
ATOM   7058 O  O   . ARG E 1 172 ? 77.201  119.703 71.139  1.00 35.40 ? 169 ARG E O   1 
ATOM   7059 C  CB  . ARG E 1 172 ? 78.789  121.170 73.079  1.00 35.49 ? 169 ARG E CB  1 
ATOM   7060 C  CG  . ARG E 1 172 ? 78.975  119.743 73.785  1.00 34.93 ? 169 ARG E CG  1 
ATOM   7061 C  CD  . ARG E 1 172 ? 80.683  119.912 74.287  1.00 34.83 ? 169 ARG E CD  1 
ATOM   7062 N  NE  . ARG E 1 172 ? 81.036  118.589 74.879  1.00 35.28 ? 169 ARG E NE  1 
ATOM   7063 C  CZ  . ARG E 1 172 ? 80.926  118.418 76.204  1.00 35.32 ? 169 ARG E CZ  1 
ATOM   7064 N  NH1 . ARG E 1 172 ? 81.363  117.235 76.676  1.00 37.54 ? 169 ARG E NH1 1 
ATOM   7065 N  NH2 . ARG E 1 172 ? 80.027  119.295 77.260  1.00 33.86 ? 169 ARG E NH2 1 
ATOM   7066 N  N   . LYS E 1 173 ? 75.990  121.610 70.665  1.00 36.07 ? 170 LYS E N   1 
ATOM   7067 C  CA  . LYS E 1 173 ? 75.119  120.981 69.648  1.00 36.73 ? 170 LYS E CA  1 
ATOM   7068 C  C   . LYS E 1 173 ? 75.794  120.643 68.311  1.00 36.40 ? 170 LYS E C   1 
ATOM   7069 O  O   . LYS E 1 173 ? 75.210  119.965 67.445  1.00 35.96 ? 170 LYS E O   1 
ATOM   7070 C  CB  . LYS E 1 173 ? 73.852  121.826 69.428  1.00 37.04 ? 170 LYS E CB  1 
ATOM   7071 C  CG  . LYS E 1 173 ? 72.537  120.989 69.328  1.00 38.15 ? 170 LYS E CG  1 
ATOM   7072 C  CD  . LYS E 1 173 ? 71.321  121.713 69.972  1.00 38.31 ? 170 LYS E CD  1 
ATOM   7073 C  CE  . LYS E 1 173 ? 71.053  123.108 69.343  1.00 38.15 ? 170 LYS E CE  1 
ATOM   7074 N  NZ  . LYS E 1 173 ? 72.214  124.079 69.368  1.00 36.90 ? 170 LYS E NZ  1 
ATOM   7075 N  N   . GLU E 1 174 ? 77.020  121.130 68.156  1.00 36.09 ? 171 GLU E N   1 
ATOM   7076 C  CA  . GLU E 1 174 ? 77.842  120.805 66.996  1.00 35.83 ? 171 GLU E CA  1 
ATOM   7077 C  C   . GLU E 1 174 ? 78.135  119.299 66.826  1.00 35.36 ? 171 GLU E C   1 
ATOM   7078 O  O   . GLU E 1 174 ? 78.335  118.846 65.694  1.00 35.40 ? 171 GLU E O   1 
ATOM   7079 C  CB  . GLU E 1 174 ? 79.133  121.630 67.006  1.00 35.79 ? 171 GLU E CB  1 
ATOM   7080 C  CG  . GLU E 1 174 ? 79.525  122.180 68.394  1.00 36.48 ? 171 GLU E CG  1 
ATOM   7081 C  CD  . GLU E 1 174 ? 80.162  121.129 69.319  1.00 36.70 ? 171 GLU E CD  1 
ATOM   7082 O  OE1 . GLU E 1 174 ? 80.275  121.564 70.763  1.00 37.74 ? 171 GLU E OE1 1 
ATOM   7083 O  OE2 . GLU E 1 174 ? 80.933  120.084 68.496  1.00 36.04 ? 171 GLU E OE2 1 
ATOM   7084 N  N   . LEU E 1 175 ? 78.147  118.524 67.918  1.00 34.66 ? 172 LEU E N   1 
ATOM   7085 C  CA  . LEU E 1 175 ? 78.365  117.070 67.776  1.00 34.24 ? 172 LEU E CA  1 
ATOM   7086 C  C   . LEU E 1 175 ? 77.135  116.278 67.354  1.00 33.90 ? 172 LEU E C   1 
ATOM   7087 O  O   . LEU E 1 175 ? 77.249  115.099 67.036  1.00 33.96 ? 172 LEU E O   1 
ATOM   7088 C  CB  . LEU E 1 175 ? 79.091  116.402 68.962  1.00 34.19 ? 172 LEU E CB  1 
ATOM   7089 C  CG  . LEU E 1 175 ? 78.670  116.468 70.424  1.00 33.70 ? 172 LEU E CG  1 
ATOM   7090 C  CD1 . LEU E 1 175 ? 79.081  115.203 71.123  1.00 33.12 ? 172 LEU E CD1 1 
ATOM   7091 C  CD2 . LEU E 1 175 ? 79.367  117.639 71.064  1.00 34.03 ? 172 LEU E CD2 1 
ATOM   7092 N  N   . LEU E 1 176 ? 75.974  116.929 67.331  1.00 33.52 ? 173 LEU E N   1 
ATOM   7093 C  CA  . LEU E 1 176 ? 74.794  116.336 66.735  1.00 33.08 ? 173 LEU E CA  1 
ATOM   7094 C  C   . LEU E 1 176 ? 75.069  115.949 65.279  1.00 32.98 ? 173 LEU E C   1 
ATOM   7095 O  O   . LEU E 1 176 ? 74.887  114.792 64.917  1.00 33.28 ? 173 LEU E O   1 
ATOM   7096 C  CB  . LEU E 1 176 ? 73.573  117.257 66.854  1.00 33.22 ? 173 LEU E CB  1 
ATOM   7097 C  CG  . LEU E 1 176 ? 72.207  116.658 66.489  1.00 32.73 ? 173 LEU E CG  1 
ATOM   7098 C  CD1 . LEU E 1 176 ? 71.853  115.479 67.392  1.00 32.32 ? 173 LEU E CD1 1 
ATOM   7099 C  CD2 . LEU E 1 176 ? 71.106  117.708 66.521  1.00 32.70 ? 173 LEU E CD2 1 
ATOM   7100 N  N   . GLU E 1 177 ? 75.528  116.894 64.456  1.00 32.89 ? 174 GLU E N   1 
ATOM   7101 C  CA  . GLU E 1 177 ? 75.906  116.568 63.064  1.00 32.71 ? 174 GLU E CA  1 
ATOM   7102 C  C   . GLU E 1 177 ? 77.166  115.686 62.968  1.00 31.98 ? 174 GLU E C   1 
ATOM   7103 O  O   . GLU E 1 177 ? 77.335  114.932 61.963  1.00 31.80 ? 174 GLU E O   1 
ATOM   7104 C  CB  . GLU E 1 177 ? 76.043  117.818 62.166  1.00 32.94 ? 174 GLU E CB  1 
ATOM   7105 C  CG  . GLU E 1 177 ? 74.719  118.318 61.518  1.00 35.16 ? 174 GLU E CG  1 
ATOM   7106 C  CD  . GLU E 1 177 ? 73.767  117.176 61.042  1.00 39.01 ? 174 GLU E CD  1 
ATOM   7107 O  OE1 . GLU E 1 177 ? 74.179  116.357 60.171  1.00 39.79 ? 174 GLU E OE1 1 
ATOM   7108 O  OE2 . GLU E 1 177 ? 72.597  117.113 61.530  1.00 38.55 ? 174 GLU E OE2 1 
ATOM   7109 N  N   . LYS E 1 178 ? 78.039  115.774 63.996  1.00 31.38 ? 175 LYS E N   1 
ATOM   7110 C  CA  . LYS E 1 178 ? 79.216  114.892 64.038  1.00 31.05 ? 175 LYS E CA  1 
ATOM   7111 C  C   . LYS E 1 178 ? 78.769  113.427 64.126  1.00 30.27 ? 175 LYS E C   1 
ATOM   7112 O  O   . LYS E 1 178 ? 79.171  112.588 63.312  1.00 30.13 ? 175 LYS E O   1 
ATOM   7113 C  CB  . LYS E 1 178 ? 80.169  115.257 65.185  1.00 30.88 ? 175 LYS E CB  1 
ATOM   7114 C  CG  . LYS E 1 178 ? 81.001  116.504 64.918  1.00 31.77 ? 175 LYS E CG  1 
ATOM   7115 C  CD  . LYS E 1 178 ? 81.933  116.844 66.088  1.00 31.78 ? 175 LYS E CD  1 
ATOM   7116 C  CE  . LYS E 1 178 ? 82.267  118.339 66.137  1.00 32.31 ? 175 LYS E CE  1 
ATOM   7117 N  NZ  . LYS E 1 178 ? 83.588  118.691 65.519  1.00 33.57 ? 175 LYS E NZ  1 
ATOM   7118 N  N   . ILE E 1 179 ? 77.907  113.144 65.101  1.00 29.69 ? 176 ILE E N   1 
ATOM   7119 C  CA  . ILE E 1 179 ? 77.323  111.824 65.279  1.00 28.33 ? 176 ILE E CA  1 
ATOM   7120 C  C   . ILE E 1 179 ? 76.457  111.409 64.083  1.00 28.02 ? 176 ILE E C   1 
ATOM   7121 O  O   . ILE E 1 179 ? 76.664  110.339 63.525  1.00 28.05 ? 176 ILE E O   1 
ATOM   7122 C  CB  . ILE E 1 179 ? 76.509  111.749 66.592  1.00 28.69 ? 176 ILE E CB  1 
ATOM   7123 C  CG1 . ILE E 1 179 ? 77.410  112.049 67.803  1.00 27.65 ? 176 ILE E CG1 1 
ATOM   7124 C  CG2 . ILE E 1 179 ? 75.853  110.373 66.732  1.00 27.82 ? 176 ILE E CG2 1 
ATOM   7125 C  CD1 . ILE E 1 179 ? 76.649  112.362 69.079  1.00 27.86 ? 176 ILE E CD1 1 
ATOM   7126 N  N   . ARG E 1 180 ? 75.514  112.258 63.675  1.00 27.55 ? 177 ARG E N   1 
ATOM   7127 C  CA  . ARG E 1 180 ? 74.545  111.910 62.609  1.00 27.61 ? 177 ARG E CA  1 
ATOM   7128 C  C   . ARG E 1 180 ? 75.107  111.380 61.278  1.00 27.67 ? 177 ARG E C   1 
ATOM   7129 O  O   . ARG E 1 180 ? 74.461  110.560 60.609  1.00 27.31 ? 177 ARG E O   1 
ATOM   7130 C  CB  . ARG E 1 180 ? 73.600  113.079 62.325  1.00 27.49 ? 177 ARG E CB  1 
ATOM   7131 C  CG  . ARG E 1 180 ? 72.553  113.277 63.398  1.00 27.11 ? 177 ARG E CG  1 
ATOM   7132 C  CD  . ARG E 1 180 ? 71.495  114.259 62.978  1.00 24.80 ? 177 ARG E CD  1 
ATOM   7133 N  NE  . ARG E 1 180 ? 70.438  114.329 63.987  1.00 24.67 ? 177 ARG E NE  1 
ATOM   7134 C  CZ  . ARG E 1 180 ? 69.487  115.260 64.025  1.00 23.82 ? 177 ARG E CZ  1 
ATOM   7135 N  NH1 . ARG E 1 180 ? 69.449  116.219 63.117  1.00 22.89 ? 177 ARG E NH1 1 
ATOM   7136 N  NH2 . ARG E 1 180 ? 68.574  115.234 64.981  1.00 23.93 ? 177 ARG E NH2 1 
ATOM   7137 N  N   . LYS E 1 181 ? 76.296  111.868 60.910  1.00 27.93 ? 178 LYS E N   1 
ATOM   7138 C  CA  . LYS E 1 181 ? 76.928  111.634 59.605  1.00 27.91 ? 178 LYS E CA  1 
ATOM   7139 C  C   . LYS E 1 181 ? 78.167  110.727 59.696  1.00 27.89 ? 178 LYS E C   1 
ATOM   7140 O  O   . LYS E 1 181 ? 78.795  110.415 58.680  1.00 27.72 ? 178 LYS E O   1 
ATOM   7141 C  CB  . LYS E 1 181 ? 77.302  112.983 58.966  1.00 28.16 ? 178 LYS E CB  1 
ATOM   7142 C  CG  . LYS E 1 181 ? 76.467  113.417 57.730  1.00 29.07 ? 178 LYS E CG  1 
ATOM   7143 C  CD  . LYS E 1 181 ? 75.061  113.952 58.053  1.00 30.62 ? 178 LYS E CD  1 
ATOM   7144 C  CE  . LYS E 1 181 ? 74.628  115.011 57.006  1.00 30.22 ? 178 LYS E CE  1 
ATOM   7145 N  NZ  . LYS E 1 181 ? 73.207  115.473 57.174  1.00 27.59 ? 178 LYS E NZ  1 
ATOM   7146 N  N   . ASP E 1 182 ? 78.488  110.304 60.919  1.00 27.94 ? 179 ASP E N   1 
ATOM   7147 C  CA  . ASP E 1 182 ? 79.630  109.439 61.240  1.00 27.99 ? 179 ASP E CA  1 
ATOM   7148 C  C   . ASP E 1 182 ? 79.503  108.027 60.640  1.00 28.00 ? 179 ASP E C   1 
ATOM   7149 O  O   . ASP E 1 182 ? 78.612  107.256 61.057  1.00 28.53 ? 179 ASP E O   1 
ATOM   7150 C  CB  . ASP E 1 182 ? 79.768  109.356 62.773  1.00 28.07 ? 179 ASP E CB  1 
ATOM   7151 C  CG  . ASP E 1 182 ? 80.920  108.458 63.234  1.00 28.95 ? 179 ASP E CG  1 
ATOM   7152 O  OD1 . ASP E 1 182 ? 81.052  108.275 64.462  1.00 29.18 ? 179 ASP E OD1 1 
ATOM   7153 O  OD2 . ASP E 1 182 ? 81.692  107.941 62.393  1.00 29.28 ? 179 ASP E OD2 1 
ATOM   7154 N  N   . PRO E 1 183 ? 80.395  107.679 59.679  1.00 27.86 ? 180 PRO E N   1 
ATOM   7155 C  CA  . PRO E 1 183 ? 80.388  106.356 59.014  1.00 27.80 ? 180 PRO E CA  1 
ATOM   7156 C  C   . PRO E 1 183 ? 80.664  105.160 59.951  1.00 27.97 ? 180 PRO E C   1 
ATOM   7157 O  O   . PRO E 1 183 ? 80.114  104.063 59.745  1.00 27.65 ? 180 PRO E O   1 
ATOM   7158 C  CB  . PRO E 1 183 ? 81.500  106.484 57.958  1.00 27.78 ? 180 PRO E CB  1 
ATOM   7159 C  CG  . PRO E 1 183 ? 82.379  107.600 58.441  1.00 27.22 ? 180 PRO E CG  1 
ATOM   7160 C  CD  . PRO E 1 183 ? 81.466  108.552 59.144  1.00 27.86 ? 180 PRO E CD  1 
ATOM   7161 N  N   . ALA E 1 184 ? 81.491  105.394 60.972  1.00 27.68 ? 181 ALA E N   1 
ATOM   7162 C  CA  . ALA E 1 184 ? 81.911  104.374 61.928  1.00 27.60 ? 181 ALA E CA  1 
ATOM   7163 C  C   . ALA E 1 184 ? 80.783  103.894 62.837  1.00 27.96 ? 181 ALA E C   1 
ATOM   7164 O  O   . ALA E 1 184 ? 80.980  102.969 63.617  1.00 28.45 ? 181 ALA E O   1 
ATOM   7165 C  CB  . ALA E 1 184 ? 83.068  104.896 62.773  1.00 27.31 ? 181 ALA E CB  1 
ATOM   7166 N  N   . ARG E 1 185 ? 79.615  104.525 62.757  1.00 27.76 ? 182 ARG E N   1 
ATOM   7167 C  CA  . ARG E 1 185 ? 78.488  104.116 63.569  1.00 27.86 ? 182 ARG E CA  1 
ATOM   7168 C  C   . ARG E 1 185 ? 77.854  102.840 63.023  1.00 28.17 ? 182 ARG E C   1 
ATOM   7169 O  O   . ARG E 1 185 ? 77.094  102.167 63.713  1.00 27.94 ? 182 ARG E O   1 
ATOM   7170 C  CB  . ARG E 1 185 ? 77.455  105.236 63.664  1.00 27.71 ? 182 ARG E CB  1 
ATOM   7171 C  CG  . ARG E 1 185 ? 77.821  106.311 64.665  1.00 27.07 ? 182 ARG E CG  1 
ATOM   7172 C  CD  . ARG E 1 185 ? 76.816  107.451 64.616  1.00 27.51 ? 182 ARG E CD  1 
ATOM   7173 N  NE  . ARG E 1 185 ? 75.449  106.973 64.815  1.00 27.02 ? 182 ARG E NE  1 
ATOM   7174 C  CZ  . ARG E 1 185 ? 74.378  107.413 64.158  1.00 25.53 ? 182 ARG E CZ  1 
ATOM   7175 N  NH1 . ARG E 1 185 ? 73.200  106.890 64.435  1.00 25.88 ? 182 ARG E NH1 1 
ATOM   7176 N  NH2 . ARG E 1 185 ? 74.469  108.355 63.229  1.00 23.18 ? 182 ARG E NH2 1 
ATOM   7177 N  N   . PHE E 1 186 ? 78.183  102.510 61.780  1.00 28.64 ? 183 PHE E N   1 
ATOM   7178 C  CA  . PHE E 1 186 ? 77.666  101.320 61.121  1.00 29.13 ? 183 PHE E CA  1 
ATOM   7179 C  C   . PHE E 1 186 ? 78.825  100.550 60.505  1.00 30.20 ? 183 PHE E C   1 
ATOM   7180 O  O   . PHE E 1 186 ? 79.385  100.952 59.475  1.00 30.97 ? 183 PHE E O   1 
ATOM   7181 C  CB  . PHE E 1 186 ? 76.599  101.727 60.103  1.00 28.33 ? 183 PHE E CB  1 
ATOM   7182 C  CG  . PHE E 1 186 ? 75.504  102.545 60.717  1.00 27.84 ? 183 PHE E CG  1 
ATOM   7183 C  CD1 . PHE E 1 186 ? 75.537  103.943 60.654  1.00 25.37 ? 183 PHE E CD1 1 
ATOM   7184 C  CD2 . PHE E 1 186 ? 74.486  101.923 61.451  1.00 25.39 ? 183 PHE E CD2 1 
ATOM   7185 C  CE1 . PHE E 1 186 ? 74.554  104.701 61.275  1.00 24.74 ? 183 PHE E CE1 1 
ATOM   7186 C  CE2 . PHE E 1 186 ? 73.499  102.675 62.073  1.00 23.34 ? 183 PHE E CE2 1 
ATOM   7187 C  CZ  . PHE E 1 186 ? 73.523  104.050 61.987  1.00 25.19 ? 183 PHE E CZ  1 
ATOM   7188 N  N   . VAL E 1 187 ? 79.226  99.466  61.165  1.00 30.99 ? 184 VAL E N   1 
ATOM   7189 C  CA  . VAL E 1 187 ? 80.430  98.749  60.744  1.00 31.77 ? 184 VAL E CA  1 
ATOM   7190 C  C   . VAL E 1 187 ? 80.273  98.102  59.352  1.00 33.09 ? 184 VAL E C   1 
ATOM   7191 O  O   . VAL E 1 187 ? 79.148  97.782  58.937  1.00 33.28 ? 184 VAL E O   1 
ATOM   7192 C  CB  . VAL E 1 187 ? 80.847  97.678  61.771  1.00 31.49 ? 184 VAL E CB  1 
ATOM   7193 C  CG1 . VAL E 1 187 ? 81.165  98.321  63.131  1.00 30.56 ? 184 VAL E CG1 1 
ATOM   7194 C  CG2 . VAL E 1 187 ? 79.792  96.613  61.859  1.00 30.06 ? 184 VAL E CG2 1 
ATOM   7195 N  N   . ASP E 1 188 ? 81.399  97.920  58.645  1.00 34.21 ? 185 ASP E N   1 
ATOM   7196 C  CA  . ASP E 1 188 ? 81.443  97.191  57.367  1.00 35.20 ? 185 ASP E CA  1 
ATOM   7197 C  C   . ASP E 1 188 ? 81.076  95.722  57.521  1.00 35.53 ? 185 ASP E C   1 
ATOM   7198 O  O   . ASP E 1 188 ? 80.015  95.288  57.069  1.00 36.37 ? 185 ASP E O   1 
ATOM   7199 C  CB  . ASP E 1 188 ? 82.836  97.285  56.747  1.00 35.55 ? 185 ASP E CB  1 
ATOM   7200 C  CG  . ASP E 1 188 ? 83.021  98.538  55.920  1.00 37.01 ? 185 ASP E CG  1 
ATOM   7201 O  OD1 . ASP E 1 188 ? 82.162  99.455  56.033  1.00 38.49 ? 185 ASP E OD1 1 
ATOM   7202 O  OD2 . ASP E 1 188 ? 84.017  98.601  55.156  1.00 36.63 ? 185 ASP E OD2 1 
ATOM   7203 N  N   . ALA F 1 3   ? 45.688  65.495  59.794  1.00 51.91 ? 0   ALA F N   1 
ATOM   7204 C  CA  . ALA F 1 3   ? 44.278  65.185  60.183  1.00 52.00 ? 0   ALA F CA  1 
ATOM   7205 C  C   . ALA F 1 3   ? 43.629  66.229  61.136  1.00 51.99 ? 0   ALA F C   1 
ATOM   7206 O  O   . ALA F 1 3   ? 43.155  67.283  60.686  1.00 51.54 ? 0   ALA F O   1 
ATOM   7207 C  CB  . ALA F 1 3   ? 44.166  63.725  60.748  1.00 51.82 ? 0   ALA F CB  1 
HETATM 7208 N  N   . MSE F 1 4   ? 43.634  65.933  62.438  1.00 51.98 ? 1   MSE F N   1 
HETATM 7209 C  CA  . MSE F 1 4   ? 42.831  66.644  63.435  1.00 53.15 ? 1   MSE F CA  1 
HETATM 7210 C  C   . MSE F 1 4   ? 43.294  68.091  63.743  1.00 49.86 ? 1   MSE F C   1 
HETATM 7211 O  O   . MSE F 1 4   ? 42.514  69.037  63.597  1.00 50.26 ? 1   MSE F O   1 
HETATM 7212 C  CB  . MSE F 1 4   ? 42.744  65.793  64.703  1.00 52.67 ? 1   MSE F CB  1 
HETATM 7213 C  CG  . MSE F 1 4   ? 41.309  65.605  65.221  1.00 56.34 ? 1   MSE F CG  1 
HETATM 7214 SE SE  . MSE F 1 4   ? 40.822  63.723  65.822  1.00 62.85 ? 1   MSE F SE  1 
HETATM 7215 C  CE  . MSE F 1 4   ? 42.017  63.468  67.584  1.00 62.51 ? 1   MSE F CE  1 
ATOM   7216 N  N   . GLY F 1 5   ? 44.545  68.277  64.158  1.00 46.62 ? 2   GLY F N   1 
ATOM   7217 C  CA  . GLY F 1 5   ? 45.064  69.632  64.369  1.00 42.52 ? 2   GLY F CA  1 
ATOM   7218 C  C   . GLY F 1 5   ? 45.199  70.457  63.100  1.00 39.50 ? 2   GLY F C   1 
ATOM   7219 O  O   . GLY F 1 5   ? 45.767  69.979  62.119  1.00 39.18 ? 2   GLY F O   1 
ATOM   7220 N  N   . LYS F 1 6   ? 44.665  71.681  63.120  1.00 36.38 ? 3   LYS F N   1 
ATOM   7221 C  CA  . LYS F 1 6   ? 44.727  72.609  61.973  1.00 34.00 ? 3   LYS F CA  1 
ATOM   7222 C  C   . LYS F 1 6   ? 45.548  73.845  62.324  1.00 32.40 ? 3   LYS F C   1 
ATOM   7223 O  O   . LYS F 1 6   ? 45.250  74.554  63.287  1.00 31.79 ? 3   LYS F O   1 
ATOM   7224 C  CB  . LYS F 1 6   ? 43.326  73.040  61.514  1.00 34.14 ? 3   LYS F CB  1 
ATOM   7225 C  CG  . LYS F 1 6   ? 42.406  71.906  61.080  1.00 33.96 ? 3   LYS F CG  1 
ATOM   7226 C  CD  . LYS F 1 6   ? 41.087  72.430  60.554  1.00 34.20 ? 3   LYS F CD  1 
ATOM   7227 C  CE  . LYS F 1 6   ? 39.911  71.664  61.154  1.00 35.17 ? 3   LYS F CE  1 
ATOM   7228 N  NZ  . LYS F 1 6   ? 39.039  71.049  60.104  1.00 35.01 ? 3   LYS F NZ  1 
ATOM   7229 N  N   . VAL F 1 7   ? 46.597  74.084  61.550  1.00 30.71 ? 4   VAL F N   1 
ATOM   7230 C  CA  . VAL F 1 7   ? 47.595  75.102  61.861  1.00 28.59 ? 4   VAL F CA  1 
ATOM   7231 C  C   . VAL F 1 7   ? 47.914  75.947  60.638  1.00 27.90 ? 4   VAL F C   1 
ATOM   7232 O  O   . VAL F 1 7   ? 48.279  75.416  59.587  1.00 28.01 ? 4   VAL F O   1 
ATOM   7233 C  CB  . VAL F 1 7   ? 48.894  74.460  62.401  1.00 28.61 ? 4   VAL F CB  1 
ATOM   7234 C  CG1 . VAL F 1 7   ? 50.009  75.501  62.552  1.00 28.20 ? 4   VAL F CG1 1 
ATOM   7235 C  CG2 . VAL F 1 7   ? 48.630  73.773  63.706  1.00 27.50 ? 4   VAL F CG2 1 
ATOM   7236 N  N   . LEU F 1 8   ? 47.741  77.257  60.784  1.00 26.72 ? 5   LEU F N   1 
ATOM   7237 C  CA  . LEU F 1 8   ? 48.076  78.241  59.763  1.00 26.19 ? 5   LEU F CA  1 
ATOM   7238 C  C   . LEU F 1 8   ? 49.400  78.914  60.102  1.00 26.19 ? 5   LEU F C   1 
ATOM   7239 O  O   . LEU F 1 8   ? 49.549  79.482  61.183  1.00 26.82 ? 5   LEU F O   1 
ATOM   7240 C  CB  . LEU F 1 8   ? 47.024  79.349  59.766  1.00 25.67 ? 5   LEU F CB  1 
ATOM   7241 C  CG  . LEU F 1 8   ? 46.599  80.125  58.519  1.00 26.01 ? 5   LEU F CG  1 
ATOM   7242 C  CD1 . LEU F 1 8   ? 46.363  81.527  58.934  1.00 23.83 ? 5   LEU F CD1 1 
ATOM   7243 C  CD2 . LEU F 1 8   ? 47.539  79.996  57.256  1.00 23.92 ? 5   LEU F CD2 1 
ATOM   7244 N  N   . VAL F 1 9   ? 50.355  78.855  59.190  1.00 25.84 ? 6   VAL F N   1 
ATOM   7245 C  CA  . VAL F 1 9   ? 51.574  79.643  59.312  1.00 25.00 ? 6   VAL F CA  1 
ATOM   7246 C  C   . VAL F 1 9   ? 51.437  80.747  58.259  1.00 25.04 ? 6   VAL F C   1 
ATOM   7247 O  O   . VAL F 1 9   ? 51.339  80.488  57.069  1.00 24.20 ? 6   VAL F O   1 
ATOM   7248 C  CB  . VAL F 1 9   ? 52.859  78.780  59.107  1.00 24.58 ? 6   VAL F CB  1 
ATOM   7249 C  CG1 . VAL F 1 9   ? 54.084  79.608  59.270  1.00 23.76 ? 6   VAL F CG1 1 
ATOM   7250 C  CG2 . VAL F 1 9   ? 52.896  77.604  60.094  1.00 23.16 ? 6   VAL F CG2 1 
ATOM   7251 N  N   . ILE F 1 10  ? 51.373  81.983  58.725  1.00 25.74 ? 7   ILE F N   1 
ATOM   7252 C  CA  . ILE F 1 10  ? 51.188  83.110  57.834  1.00 26.31 ? 7   ILE F CA  1 
ATOM   7253 C  C   . ILE F 1 10  ? 52.331  84.074  58.060  1.00 26.02 ? 7   ILE F C   1 
ATOM   7254 O  O   . ILE F 1 10  ? 52.734  84.274  59.191  1.00 25.52 ? 7   ILE F O   1 
ATOM   7255 C  CB  . ILE F 1 10  ? 49.793  83.763  58.020  1.00 26.94 ? 7   ILE F CB  1 
ATOM   7256 C  CG1 . ILE F 1 10  ? 49.552  84.843  56.967  1.00 27.14 ? 7   ILE F CG1 1 
ATOM   7257 C  CG2 . ILE F 1 10  ? 49.592  84.272  59.431  1.00 26.59 ? 7   ILE F CG2 1 
ATOM   7258 C  CD1 . ILE F 1 10  ? 48.528  85.818  57.410  1.00 27.94 ? 7   ILE F CD1 1 
ATOM   7259 N  N   . TYR F 1 11  ? 52.869  84.633  56.978  1.00 25.72 ? 8   TYR F N   1 
ATOM   7260 C  CA  . TYR F 1 11  ? 54.108  85.387  57.066  1.00 26.76 ? 8   TYR F CA  1 
ATOM   7261 C  C   . TYR F 1 11  ? 54.174  86.544  56.088  1.00 27.03 ? 8   TYR F C   1 
ATOM   7262 O  O   . TYR F 1 11  ? 53.566  86.541  55.022  1.00 26.61 ? 8   TYR F O   1 
ATOM   7263 C  CB  . TYR F 1 11  ? 55.356  84.472  56.903  1.00 27.59 ? 8   TYR F CB  1 
ATOM   7264 C  CG  . TYR F 1 11  ? 55.548  83.880  55.501  1.00 27.07 ? 8   TYR F CG  1 
ATOM   7265 C  CD1 . TYR F 1 11  ? 56.247  84.574  54.505  1.00 25.46 ? 8   TYR F CD1 1 
ATOM   7266 C  CD2 . TYR F 1 11  ? 55.016  82.628  55.176  1.00 27.70 ? 8   TYR F CD2 1 
ATOM   7267 C  CE1 . TYR F 1 11  ? 56.396  84.033  53.193  1.00 24.92 ? 8   TYR F CE1 1 
ATOM   7268 C  CE2 . TYR F 1 11  ? 55.174  82.075  53.884  1.00 26.96 ? 8   TYR F CE2 1 
ATOM   7269 C  CZ  . TYR F 1 11  ? 55.867  82.780  52.908  1.00 26.61 ? 8   TYR F CZ  1 
ATOM   7270 O  OH  . TYR F 1 11  ? 55.994  82.210  51.644  1.00 29.67 ? 8   TYR F OH  1 
ATOM   7271 N  N   . ASP F 1 12  ? 54.913  87.558  56.485  1.00 27.51 ? 9   ASP F N   1 
ATOM   7272 C  CA  . ASP F 1 12  ? 55.327  88.560  55.549  1.00 28.17 ? 9   ASP F CA  1 
ATOM   7273 C  C   . ASP F 1 12  ? 56.864  88.477  55.490  1.00 28.85 ? 9   ASP F C   1 
ATOM   7274 O  O   . ASP F 1 12  ? 57.507  87.819  56.313  1.00 28.48 ? 9   ASP F O   1 
ATOM   7275 C  CB  . ASP F 1 12  ? 54.827  89.945  55.962  1.00 27.26 ? 9   ASP F CB  1 
ATOM   7276 C  CG  . ASP F 1 12  ? 55.029  90.991  54.851  1.00 28.30 ? 9   ASP F CG  1 
ATOM   7277 O  OD1 . ASP F 1 12  ? 55.403  90.603  53.719  1.00 29.01 ? 9   ASP F OD1 1 
ATOM   7278 O  OD2 . ASP F 1 12  ? 54.813  92.197  55.084  1.00 26.66 ? 9   ASP F OD2 1 
ATOM   7279 N  N   . THR F 1 13  ? 57.447  89.118  54.494  1.00 29.97 ? 10  THR F N   1 
ATOM   7280 C  CA  . THR F 1 13  ? 58.886  89.110  54.338  1.00 30.97 ? 10  THR F CA  1 
ATOM   7281 C  C   . THR F 1 13  ? 59.306  90.310  53.514  1.00 31.49 ? 10  THR F C   1 
ATOM   7282 O  O   . THR F 1 13  ? 58.483  90.941  52.847  1.00 31.97 ? 10  THR F O   1 
ATOM   7283 C  CB  . THR F 1 13  ? 59.374  87.755  53.722  1.00 31.61 ? 10  THR F CB  1 
ATOM   7284 O  OG1 . THR F 1 13  ? 60.783  87.586  53.953  1.00 30.60 ? 10  THR F OG1 1 
ATOM   7285 C  CG2 . THR F 1 13  ? 59.026  87.662  52.238  1.00 30.77 ? 10  THR F CG2 1 
ATOM   7286 N  N   . ARG F 1 14  ? 60.585  90.631  53.583  1.00 31.79 ? 11  ARG F N   1 
ATOM   7287 C  CA  . ARG F 1 14  ? 61.146  91.778  52.899  1.00 32.36 ? 11  ARG F CA  1 
ATOM   7288 C  C   . ARG F 1 14  ? 62.223  91.283  51.965  1.00 31.31 ? 11  ARG F C   1 
ATOM   7289 O  O   . ARG F 1 14  ? 62.355  91.794  50.867  1.00 32.24 ? 11  ARG F O   1 
ATOM   7290 C  CB  . ARG F 1 14  ? 61.711  92.769  53.936  1.00 33.55 ? 11  ARG F CB  1 
ATOM   7291 C  CG  . ARG F 1 14  ? 61.747  94.250  53.508  1.00 38.27 ? 11  ARG F CG  1 
ATOM   7292 C  CD  . ARG F 1 14  ? 63.160  94.726  53.134  1.00 44.94 ? 11  ARG F CD  1 
ATOM   7293 N  NE  . ARG F 1 14  ? 64.168  94.322  54.135  1.00 50.77 ? 11  ARG F NE  1 
ATOM   7294 C  CZ  . ARG F 1 14  ? 65.421  94.799  54.213  1.00 52.59 ? 11  ARG F CZ  1 
ATOM   7295 N  NH1 . ARG F 1 14  ? 65.855  95.741  53.371  1.00 51.48 ? 11  ARG F NH1 1 
ATOM   7296 N  NH2 . ARG F 1 14  ? 66.247  94.339  55.157  1.00 53.04 ? 11  ARG F NH2 1 
ATOM   7297 N  N   . THR F 1 15  ? 62.978  90.268  52.385  1.00 30.20 ? 12  THR F N   1 
ATOM   7298 C  CA  . THR F 1 15  ? 64.075  89.718  51.572  1.00 29.15 ? 12  THR F CA  1 
ATOM   7299 C  C   . THR F 1 15  ? 64.071  88.202  51.486  1.00 28.12 ? 12  THR F C   1 
ATOM   7300 O  O   . THR F 1 15  ? 64.913  87.616  50.773  1.00 27.84 ? 12  THR F O   1 
ATOM   7301 C  CB  . THR F 1 15  ? 65.479  90.098  52.112  1.00 29.40 ? 12  THR F CB  1 
ATOM   7302 O  OG1 . THR F 1 15  ? 65.616  89.589  53.445  1.00 29.94 ? 12  THR F OG1 1 
ATOM   7303 C  CG2 . THR F 1 15  ? 65.704  91.602  52.110  1.00 28.82 ? 12  THR F CG2 1 
ATOM   7304 N  N   . GLY F 1 16  ? 63.167  87.573  52.236  1.00 26.65 ? 13  GLY F N   1 
ATOM   7305 C  CA  . GLY F 1 16  ? 63.053  86.118  52.255  1.00 25.10 ? 13  GLY F CA  1 
ATOM   7306 C  C   . GLY F 1 16  ? 63.382  85.429  53.565  1.00 24.35 ? 13  GLY F C   1 
ATOM   7307 O  O   . GLY F 1 16  ? 63.000  84.287  53.767  1.00 24.62 ? 13  GLY F O   1 
ATOM   7308 N  N   . ASN F 1 17  ? 64.062  86.116  54.480  1.00 23.75 ? 14  ASN F N   1 
ATOM   7309 C  CA  . ASN F 1 17  ? 64.499  85.498  55.746  1.00 22.29 ? 14  ASN F CA  1 
ATOM   7310 C  C   . ASN F 1 17  ? 63.389  84.908  56.612  1.00 22.28 ? 14  ASN F C   1 
ATOM   7311 O  O   . ASN F 1 17  ? 63.545  83.807  57.174  1.00 22.70 ? 14  ASN F O   1 
ATOM   7312 C  CB  . ASN F 1 17  ? 65.341  86.486  56.556  1.00 21.61 ? 14  ASN F CB  1 
ATOM   7313 C  CG  . ASN F 1 17  ? 66.672  86.786  55.895  1.00 20.90 ? 14  ASN F CG  1 
ATOM   7314 O  OD1 . ASN F 1 17  ? 67.196  85.968  55.149  1.00 18.58 ? 14  ASN F OD1 1 
ATOM   7315 N  ND2 . ASN F 1 17  ? 67.223  87.963  56.162  1.00 19.41 ? 14  ASN F ND2 1 
ATOM   7316 N  N   . THR F 1 18  ? 62.298  85.658  56.742  1.00 21.42 ? 15  THR F N   1 
ATOM   7317 C  CA  . THR F 1 18  ? 61.109  85.257  57.490  1.00 21.50 ? 15  THR F CA  1 
ATOM   7318 C  C   . THR F 1 18  ? 60.318  84.156  56.759  1.00 21.83 ? 15  THR F C   1 
ATOM   7319 O  O   . THR F 1 18  ? 59.688  83.302  57.413  1.00 21.30 ? 15  THR F O   1 
ATOM   7320 C  CB  . THR F 1 18  ? 60.198  86.483  57.790  1.00 20.93 ? 15  THR F CB  1 
ATOM   7321 O  OG1 . THR F 1 18  ? 60.975  87.485  58.443  1.00 22.29 ? 15  THR F OG1 1 
ATOM   7322 C  CG2 . THR F 1 18  ? 59.061  86.129  58.707  1.00 19.83 ? 15  THR F CG2 1 
ATOM   7323 N  N   . LYS F 1 19  ? 60.350  84.185  55.423  1.00 22.21 ? 16  LYS F N   1 
ATOM   7324 C  CA  . LYS F 1 19  ? 59.876  83.060  54.628  1.00 23.64 ? 16  LYS F CA  1 
ATOM   7325 C  C   . LYS F 1 19  ? 60.658  81.789  55.021  1.00 24.95 ? 16  LYS F C   1 
ATOM   7326 O  O   . LYS F 1 19  ? 60.057  80.764  55.279  1.00 25.58 ? 16  LYS F O   1 
ATOM   7327 C  CB  . LYS F 1 19  ? 59.943  83.354  53.112  1.00 22.60 ? 16  LYS F CB  1 
ATOM   7328 C  CG  . LYS F 1 19  ? 59.786  82.123  52.199  1.00 21.63 ? 16  LYS F CG  1 
ATOM   7329 C  CD  . LYS F 1 19  ? 59.192  82.473  50.842  1.00 18.48 ? 16  LYS F CD  1 
ATOM   7330 C  CE  . LYS F 1 19  ? 58.992  81.261  49.948  1.00 19.48 ? 16  LYS F CE  1 
ATOM   7331 N  NZ  . LYS F 1 19  ? 58.754  81.612  48.448  1.00 15.41 ? 16  LYS F NZ  1 
ATOM   7332 N  N   . LYS F 1 20  ? 61.983  81.868  55.089  1.00 26.62 ? 17  LYS F N   1 
ATOM   7333 C  CA  . LYS F 1 20  ? 62.804  80.735  55.497  1.00 28.57 ? 17  LYS F CA  1 
ATOM   7334 C  C   . LYS F 1 20  ? 62.417  80.227  56.879  1.00 29.42 ? 17  LYS F C   1 
ATOM   7335 O  O   . LYS F 1 20  ? 62.356  79.010  57.096  1.00 29.84 ? 17  LYS F O   1 
ATOM   7336 C  CB  . LYS F 1 20  ? 64.299  81.071  55.451  1.00 28.47 ? 17  LYS F CB  1 
ATOM   7337 C  CG  . LYS F 1 20  ? 65.033  80.451  54.286  1.00 32.21 ? 17  LYS F CG  1 
ATOM   7338 C  CD  . LYS F 1 20  ? 64.931  81.295  53.020  1.00 37.10 ? 17  LYS F CD  1 
ATOM   7339 C  CE  . LYS F 1 20  ? 63.857  80.806  52.044  1.00 38.84 ? 17  LYS F CE  1 
ATOM   7340 N  NZ  . LYS F 1 20  ? 63.465  81.924  51.112  1.00 37.51 ? 17  LYS F NZ  1 
HETATM 7341 N  N   . MSE F 1 21  ? 62.159  81.157  57.802  1.00 29.52 ? 18  MSE F N   1 
HETATM 7342 C  CA  . MSE F 1 21  ? 61.627  80.829  59.114  1.00 30.73 ? 18  MSE F CA  1 
HETATM 7343 C  C   . MSE F 1 21  ? 60.262  80.166  59.062  1.00 29.24 ? 18  MSE F C   1 
HETATM 7344 O  O   . MSE F 1 21  ? 60.027  79.193  59.777  1.00 28.84 ? 18  MSE F O   1 
HETATM 7345 C  CB  . MSE F 1 21  ? 61.515  82.073  59.987  1.00 30.32 ? 18  MSE F CB  1 
HETATM 7346 C  CG  . MSE F 1 21  ? 62.849  82.719  60.357  1.00 32.24 ? 18  MSE F CG  1 
HETATM 7347 SE SE  . MSE F 1 21  ? 62.605  84.275  61.549  1.00 38.18 ? 18  MSE F SE  1 
HETATM 7348 C  CE  . MSE F 1 21  ? 62.320  83.311  63.313  1.00 32.47 ? 18  MSE F CE  1 
ATOM   7349 N  N   . ALA F 1 22  ? 59.356  80.701  58.244  1.00 28.60 ? 19  ALA F N   1 
ATOM   7350 C  CA  . ALA F 1 22  ? 57.995  80.184  58.183  1.00 28.12 ? 19  ALA F CA  1 
ATOM   7351 C  C   . ALA F 1 22  ? 57.977  78.745  57.705  1.00 28.86 ? 19  ALA F C   1 
ATOM   7352 O  O   . ALA F 1 22  ? 57.131  77.952  58.144  1.00 29.35 ? 19  ALA F O   1 
ATOM   7353 C  CB  . ALA F 1 22  ? 57.168  81.016  57.286  1.00 28.30 ? 19  ALA F CB  1 
ATOM   7354 N  N   . GLU F 1 23  ? 58.909  78.417  56.805  1.00 28.07 ? 20  GLU F N   1 
ATOM   7355 C  CA  . GLU F 1 23  ? 59.031  77.077  56.262  1.00 28.28 ? 20  GLU F CA  1 
ATOM   7356 C  C   . GLU F 1 23  ? 59.483  76.104  57.350  1.00 27.56 ? 20  GLU F C   1 
ATOM   7357 O  O   . GLU F 1 23  ? 58.974  74.987  57.432  1.00 27.25 ? 20  GLU F O   1 
ATOM   7358 C  CB  . GLU F 1 23  ? 59.962  77.049  55.024  1.00 27.84 ? 20  GLU F CB  1 
ATOM   7359 C  CG  . GLU F 1 23  ? 59.332  77.699  53.812  1.00 27.61 ? 20  GLU F CG  1 
ATOM   7360 C  CD  . GLU F 1 23  ? 60.316  78.053  52.698  1.00 30.10 ? 20  GLU F CD  1 
ATOM   7361 O  OE1 . GLU F 1 23  ? 61.532  78.263  52.971  1.00 33.49 ? 20  GLU F OE1 1 
ATOM   7362 O  OE2 . GLU F 1 23  ? 59.864  78.133  51.524  1.00 30.99 ? 20  GLU F OE2 1 
ATOM   7363 N  N   . LEU F 1 24  ? 60.409  76.538  58.200  1.00 27.04 ? 21  LEU F N   1 
ATOM   7364 C  CA  . LEU F 1 24  ? 60.825  75.712  59.326  1.00 26.57 ? 21  LEU F CA  1 
ATOM   7365 C  C   . LEU F 1 24  ? 59.742  75.589  60.411  1.00 26.85 ? 21  LEU F C   1 
ATOM   7366 O  O   . LEU F 1 24  ? 59.573  74.515  61.002  1.00 27.66 ? 21  LEU F O   1 
ATOM   7367 C  CB  . LEU F 1 24  ? 62.175  76.166  59.880  1.00 26.20 ? 21  LEU F CB  1 
ATOM   7368 C  CG  . LEU F 1 24  ? 63.378  76.013  58.929  1.00 25.96 ? 21  LEU F CG  1 
ATOM   7369 C  CD1 . LEU F 1 24  ? 64.431  77.105  59.188  1.00 24.82 ? 21  LEU F CD1 1 
ATOM   7370 C  CD2 . LEU F 1 24  ? 63.986  74.628  58.977  1.00 22.78 ? 21  LEU F CD2 1 
ATOM   7371 N  N   . VAL F 1 25  ? 58.982  76.657  60.640  1.00 26.79 ? 22  VAL F N   1 
ATOM   7372 C  CA  . VAL F 1 25  ? 57.834  76.615  61.557  1.00 26.85 ? 22  VAL F CA  1 
ATOM   7373 C  C   . VAL F 1 25  ? 56.782  75.590  61.055  1.00 27.83 ? 22  VAL F C   1 
ATOM   7374 O  O   . VAL F 1 25  ? 56.279  74.757  61.838  1.00 28.42 ? 22  VAL F O   1 
ATOM   7375 C  CB  . VAL F 1 25  ? 57.171  78.007  61.752  1.00 26.15 ? 22  VAL F CB  1 
ATOM   7376 C  CG1 . VAL F 1 25  ? 55.925  77.896  62.611  1.00 26.55 ? 22  VAL F CG1 1 
ATOM   7377 C  CG2 . VAL F 1 25  ? 58.117  78.968  62.396  1.00 24.45 ? 22  VAL F CG2 1 
ATOM   7378 N  N   . ALA F 1 26  ? 56.463  75.656  59.767  1.00 27.49 ? 23  ALA F N   1 
ATOM   7379 C  CA  . ALA F 1 26  ? 55.530  74.701  59.149  1.00 28.56 ? 23  ALA F CA  1 
ATOM   7380 C  C   . ALA F 1 26  ? 56.020  73.272  59.312  1.00 28.75 ? 23  ALA F C   1 
ATOM   7381 O  O   . ALA F 1 26  ? 55.254  72.408  59.664  1.00 28.59 ? 23  ALA F O   1 
ATOM   7382 C  CB  . ALA F 1 26  ? 55.293  75.022  57.653  1.00 27.73 ? 23  ALA F CB  1 
ATOM   7383 N  N   . GLU F 1 27  ? 57.310  73.051  59.076  1.00 30.00 ? 24  GLU F N   1 
ATOM   7384 C  CA  . GLU F 1 27  ? 57.921  71.736  59.163  1.00 30.96 ? 24  GLU F CA  1 
ATOM   7385 C  C   . GLU F 1 27  ? 57.759  71.215  60.576  1.00 30.95 ? 24  GLU F C   1 
ATOM   7386 O  O   . GLU F 1 27  ? 57.440  70.051  60.792  1.00 31.03 ? 24  GLU F O   1 
ATOM   7387 C  CB  . GLU F 1 27  ? 59.406  71.811  58.780  1.00 30.70 ? 24  GLU F CB  1 
ATOM   7388 C  CG  . GLU F 1 27  ? 60.186  70.537  59.098  1.00 32.35 ? 24  GLU F CG  1 
ATOM   7389 C  CD  . GLU F 1 27  ? 61.657  70.600  58.712  1.00 32.89 ? 24  GLU F CD  1 
ATOM   7390 O  OE1 . GLU F 1 27  ? 62.480  69.955  59.405  1.00 35.80 ? 24  GLU F OE1 1 
ATOM   7391 O  OE2 . GLU F 1 27  ? 61.987  71.261  57.703  1.00 36.44 ? 24  GLU F OE2 1 
ATOM   7392 N  N   . GLY F 1 28  ? 57.964  72.100  61.540  1.00 31.50 ? 25  GLY F N   1 
ATOM   7393 C  CA  . GLY F 1 28  ? 57.868  71.723  62.943  1.00 31.03 ? 25  GLY F CA  1 
ATOM   7394 C  C   . GLY F 1 28  ? 56.468  71.326  63.341  1.00 30.76 ? 25  GLY F C   1 
ATOM   7395 O  O   . GLY F 1 28  ? 56.292  70.434  64.157  1.00 31.12 ? 25  GLY F O   1 
ATOM   7396 N  N   . ALA F 1 29  ? 55.468  71.995  62.776  1.00 30.77 ? 26  ALA F N   1 
ATOM   7397 C  CA  . ALA F 1 29  ? 54.079  71.738  63.146  1.00 30.53 ? 26  ALA F CA  1 
ATOM   7398 C  C   . ALA F 1 29  ? 53.641  70.427  62.504  1.00 30.95 ? 26  ALA F C   1 
ATOM   7399 O  O   . ALA F 1 29  ? 52.983  69.606  63.142  1.00 32.07 ? 26  ALA F O   1 
ATOM   7400 C  CB  . ALA F 1 29  ? 53.180  72.901  62.734  1.00 29.60 ? 26  ALA F CB  1 
ATOM   7401 N  N   . ARG F 1 30  ? 54.052  70.215  61.259  1.00 30.80 ? 27  ARG F N   1 
ATOM   7402 C  CA  . ARG F 1 30  ? 53.785  68.975  60.527  1.00 30.83 ? 27  ARG F CA  1 
ATOM   7403 C  C   . ARG F 1 30  ? 54.373  67.734  61.206  1.00 30.80 ? 27  ARG F C   1 
ATOM   7404 O  O   . ARG F 1 30  ? 53.863  66.636  61.019  1.00 30.46 ? 27  ARG F O   1 
ATOM   7405 C  CB  . ARG F 1 30  ? 54.334  69.072  59.108  1.00 30.77 ? 27  ARG F CB  1 
ATOM   7406 C  CG  . ARG F 1 30  ? 53.446  69.802  58.147  1.00 31.69 ? 27  ARG F CG  1 
ATOM   7407 C  CD  . ARG F 1 30  ? 53.890  69.564  56.694  1.00 34.20 ? 27  ARG F CD  1 
ATOM   7408 N  NE  . ARG F 1 30  ? 54.883  70.553  56.271  1.00 34.26 ? 27  ARG F NE  1 
ATOM   7409 C  CZ  . ARG F 1 30  ? 54.599  71.647  55.570  1.00 34.80 ? 27  ARG F CZ  1 
ATOM   7410 N  NH1 . ARG F 1 30  ? 55.573  72.488  55.242  1.00 35.87 ? 27  ARG F NH1 1 
ATOM   7411 N  NH2 . ARG F 1 30  ? 53.350  71.900  55.185  1.00 34.56 ? 27  ARG F NH2 1 
ATOM   7412 N  N   . SER F 1 31  ? 55.436  67.911  61.995  1.00 30.88 ? 28  SER F N   1 
ATOM   7413 C  CA  . SER F 1 31  ? 56.091  66.788  62.671  1.00 30.45 ? 28  SER F CA  1 
ATOM   7414 C  C   . SER F 1 31  ? 55.211  66.128  63.737  1.00 30.37 ? 28  SER F C   1 
ATOM   7415 O  O   . SER F 1 31  ? 55.456  64.988  64.111  1.00 31.10 ? 28  SER F O   1 
ATOM   7416 C  CB  . SER F 1 31  ? 57.438  67.219  63.263  1.00 30.39 ? 28  SER F CB  1 
ATOM   7417 O  OG  . SER F 1 31  ? 57.284  67.970  64.463  1.00 30.44 ? 28  SER F OG  1 
ATOM   7418 N  N   . LEU F 1 32  ? 54.203  66.838  64.232  1.00 30.22 ? 29  LEU F N   1 
ATOM   7419 C  CA  . LEU F 1 32  ? 53.237  66.248  65.147  1.00 30.35 ? 29  LEU F CA  1 
ATOM   7420 C  C   . LEU F 1 32  ? 52.155  65.524  64.362  1.00 30.81 ? 29  LEU F C   1 
ATOM   7421 O  O   . LEU F 1 32  ? 51.458  66.159  63.560  1.00 31.11 ? 29  LEU F O   1 
ATOM   7422 C  CB  . LEU F 1 32  ? 52.564  67.309  66.022  1.00 29.90 ? 29  LEU F CB  1 
ATOM   7423 C  CG  . LEU F 1 32  ? 52.255  66.999  67.496  1.00 29.65 ? 29  LEU F CG  1 
ATOM   7424 C  CD1 . LEU F 1 32  ? 50.871  67.529  67.882  1.00 27.83 ? 29  LEU F CD1 1 
ATOM   7425 C  CD2 . LEU F 1 32  ? 52.388  65.536  67.878  1.00 26.35 ? 29  LEU F CD2 1 
ATOM   7426 N  N   . GLU F 1 33  ? 52.007  64.217  64.623  1.00 30.94 ? 30  GLU F N   1 
ATOM   7427 C  CA  . GLU F 1 33  ? 50.946  63.381  64.068  1.00 31.11 ? 30  GLU F CA  1 
ATOM   7428 C  C   . GLU F 1 33  ? 49.576  64.034  64.019  1.00 31.00 ? 30  GLU F C   1 
ATOM   7429 O  O   . GLU F 1 33  ? 49.104  64.600  65.005  1.00 31.14 ? 30  GLU F O   1 
ATOM   7430 C  CB  . GLU F 1 33  ? 50.805  62.113  64.890  1.00 31.40 ? 30  GLU F CB  1 
ATOM   7431 C  CG  . GLU F 1 33  ? 49.950  61.040  64.177  1.00 32.92 ? 30  GLU F CG  1 
ATOM   7432 C  CD  . GLU F 1 33  ? 48.949  60.342  65.094  1.00 34.45 ? 30  GLU F CD  1 
ATOM   7433 O  OE1 . GLU F 1 33  ? 49.057  60.446  66.340  1.00 34.98 ? 30  GLU F OE1 1 
ATOM   7434 O  OE2 . GLU F 1 33  ? 48.039  59.683  64.555  1.00 35.57 ? 30  GLU F OE2 1 
ATOM   7435 N  N   . GLY F 1 34  ? 48.930  63.924  62.868  1.00 31.46 ? 31  GLY F N   1 
ATOM   7436 C  CA  . GLY F 1 34  ? 47.590  64.458  62.676  1.00 32.06 ? 31  GLY F CA  1 
ATOM   7437 C  C   . GLY F 1 34  ? 47.499  65.974  62.654  1.00 32.80 ? 31  GLY F C   1 
ATOM   7438 O  O   . GLY F 1 34  ? 46.468  66.524  63.024  1.00 33.96 ? 31  GLY F O   1 
ATOM   7439 N  N   . THR F 1 35  ? 48.577  66.655  62.264  1.00 32.76 ? 32  THR F N   1 
ATOM   7440 C  CA  . THR F 1 35  ? 48.557  68.112  62.097  1.00 32.58 ? 32  THR F CA  1 
ATOM   7441 C  C   . THR F 1 35  ? 48.518  68.447  60.601  1.00 32.52 ? 32  THR F C   1 
ATOM   7442 O  O   . THR F 1 35  ? 49.413  68.083  59.842  1.00 32.36 ? 32  THR F O   1 
ATOM   7443 C  CB  . THR F 1 35  ? 49.757  68.811  62.803  1.00 32.77 ? 32  THR F CB  1 
ATOM   7444 O  OG1 . THR F 1 35  ? 49.883  68.322  64.146  1.00 33.42 ? 32  THR F OG1 1 
ATOM   7445 C  CG2 . THR F 1 35  ? 49.583  70.320  62.854  1.00 31.19 ? 32  THR F CG2 1 
ATOM   7446 N  N   . GLU F 1 36  ? 47.433  69.087  60.188  1.00 32.31 ? 33  GLU F N   1 
ATOM   7447 C  CA  . GLU F 1 36  ? 47.285  69.615  58.848  1.00 32.21 ? 33  GLU F CA  1 
ATOM   7448 C  C   . GLU F 1 36  ? 47.807  71.047  58.907  1.00 31.70 ? 33  GLU F C   1 
ATOM   7449 O  O   . GLU F 1 36  ? 47.279  71.879  59.658  1.00 31.23 ? 33  GLU F O   1 
ATOM   7450 C  CB  . GLU F 1 36  ? 45.808  69.596  58.458  1.00 32.17 ? 33  GLU F CB  1 
ATOM   7451 C  CG  . GLU F 1 36  ? 45.491  69.832  56.987  1.00 32.93 ? 33  GLU F CG  1 
ATOM   7452 C  CD  . GLU F 1 36  ? 44.015  69.577  56.671  1.00 33.39 ? 33  GLU F CD  1 
ATOM   7453 O  OE1 . GLU F 1 36  ? 43.609  69.783  55.510  1.00 34.39 ? 33  GLU F OE1 1 
ATOM   7454 O  OE2 . GLU F 1 36  ? 43.253  69.164  57.583  1.00 35.89 ? 33  GLU F OE2 1 
ATOM   7455 N  N   . VAL F 1 37  ? 48.866  71.315  58.142  1.00 31.26 ? 34  VAL F N   1 
ATOM   7456 C  CA  . VAL F 1 37  ? 49.467  72.651  58.087  1.00 30.60 ? 34  VAL F CA  1 
ATOM   7457 C  C   . VAL F 1 37  ? 49.180  73.362  56.767  1.00 30.30 ? 34  VAL F C   1 
ATOM   7458 O  O   . VAL F 1 37  ? 49.321  72.797  55.680  1.00 30.35 ? 34  VAL F O   1 
ATOM   7459 C  CB  . VAL F 1 37  ? 50.989  72.620  58.384  1.00 30.45 ? 34  VAL F CB  1 
ATOM   7460 C  CG1 . VAL F 1 37  ? 51.582  73.988  58.250  1.00 29.51 ? 34  VAL F CG1 1 
ATOM   7461 C  CG2 . VAL F 1 37  ? 51.233  72.093  59.790  1.00 30.20 ? 34  VAL F CG2 1 
ATOM   7462 N  N   . ARG F 1 38  ? 48.755  74.604  56.887  1.00 29.86 ? 35  ARG F N   1 
ATOM   7463 C  CA  . ARG F 1 38  ? 48.612  75.486  55.761  1.00 29.65 ? 35  ARG F CA  1 
ATOM   7464 C  C   . ARG F 1 38  ? 49.696  76.536  55.932  1.00 29.45 ? 35  ARG F C   1 
ATOM   7465 O  O   . ARG F 1 38  ? 49.894  77.026  57.040  1.00 30.58 ? 35  ARG F O   1 
ATOM   7466 C  CB  . ARG F 1 38  ? 47.279  76.180  55.865  1.00 29.48 ? 35  ARG F CB  1 
ATOM   7467 C  CG  . ARG F 1 38  ? 46.480  76.232  54.628  1.00 29.42 ? 35  ARG F CG  1 
ATOM   7468 C  CD  . ARG F 1 38  ? 45.222  75.441  54.851  1.00 28.24 ? 35  ARG F CD  1 
ATOM   7469 N  NE  . ARG F 1 38  ? 44.031  76.243  54.597  1.00 28.42 ? 35  ARG F NE  1 
ATOM   7470 C  CZ  . ARG F 1 38  ? 42.814  75.734  54.397  1.00 28.68 ? 35  ARG F CZ  1 
ATOM   7471 N  NH1 . ARG F 1 38  ? 42.625  74.421  54.409  1.00 26.00 ? 35  ARG F NH1 1 
ATOM   7472 N  NH2 . ARG F 1 38  ? 41.785  76.544  54.180  1.00 28.62 ? 35  ARG F NH2 1 
ATOM   7473 N  N   . LEU F 1 39  ? 50.398  76.874  54.858  1.00 29.41 ? 36  LEU F N   1 
ATOM   7474 C  CA  . LEU F 1 39  ? 51.480  77.861  54.885  1.00 29.46 ? 36  LEU F CA  1 
ATOM   7475 C  C   . LEU F 1 39  ? 51.229  78.916  53.817  1.00 29.88 ? 36  LEU F C   1 
ATOM   7476 O  O   . LEU F 1 39  ? 51.256  78.603  52.617  1.00 29.75 ? 36  LEU F O   1 
ATOM   7477 C  CB  . LEU F 1 39  ? 52.836  77.183  54.615  1.00 29.55 ? 36  LEU F CB  1 
ATOM   7478 C  CG  . LEU F 1 39  ? 53.979  78.149  54.279  1.00 28.24 ? 36  LEU F CG  1 
ATOM   7479 C  CD1 . LEU F 1 39  ? 54.301  78.934  55.520  1.00 27.97 ? 36  LEU F CD1 1 
ATOM   7480 C  CD2 . LEU F 1 39  ? 55.203  77.431  53.782  1.00 26.25 ? 36  LEU F CD2 1 
ATOM   7481 N  N   . LYS F 1 40  ? 51.004  80.158  54.240  1.00 29.83 ? 37  LYS F N   1 
ATOM   7482 C  CA  . LYS F 1 40  ? 50.602  81.211  53.311  1.00 30.40 ? 37  LYS F CA  1 
ATOM   7483 C  C   . LYS F 1 40  ? 51.287  82.531  53.572  1.00 31.03 ? 37  LYS F C   1 
ATOM   7484 O  O   . LYS F 1 40  ? 51.284  83.015  54.685  1.00 31.98 ? 37  LYS F O   1 
ATOM   7485 C  CB  . LYS F 1 40  ? 49.070  81.378  53.291  1.00 30.42 ? 37  LYS F CB  1 
ATOM   7486 C  CG  . LYS F 1 40  ? 48.356  80.305  52.425  1.00 30.33 ? 37  LYS F CG  1 
ATOM   7487 C  CD  . LYS F 1 40  ? 47.091  80.841  51.773  1.00 32.50 ? 37  LYS F CD  1 
ATOM   7488 C  CE  . LYS F 1 40  ? 46.250  79.766  51.040  1.00 33.65 ? 37  LYS F CE  1 
ATOM   7489 N  NZ  . LYS F 1 40  ? 44.824  80.246  50.811  1.00 32.91 ? 37  LYS F NZ  1 
ATOM   7490 N  N   . HIS F 1 41  ? 51.912  83.093  52.542  1.00 31.87 ? 38  HIS F N   1 
ATOM   7491 C  CA  . HIS F 1 41  ? 52.354  84.485  52.555  1.00 32.42 ? 38  HIS F CA  1 
ATOM   7492 C  C   . HIS F 1 41  ? 51.129  85.394  52.738  1.00 32.57 ? 38  HIS F C   1 
ATOM   7493 O  O   . HIS F 1 41  ? 50.043  85.093  52.247  1.00 32.83 ? 38  HIS F O   1 
ATOM   7494 C  CB  . HIS F 1 41  ? 53.053  84.807  51.219  1.00 32.20 ? 38  HIS F CB  1 
ATOM   7495 C  CG  . HIS F 1 41  ? 53.705  86.161  51.169  1.00 33.43 ? 38  HIS F CG  1 
ATOM   7496 N  ND1 . HIS F 1 41  ? 53.094  87.266  50.620  1.00 36.17 ? 38  HIS F ND1 1 
ATOM   7497 C  CD2 . HIS F 1 41  ? 54.922  86.581  51.587  1.00 34.43 ? 38  HIS F CD2 1 
ATOM   7498 C  CE1 . HIS F 1 41  ? 53.900  88.309  50.708  1.00 35.72 ? 38  HIS F CE1 1 
ATOM   7499 N  NE2 . HIS F 1 41  ? 55.021  87.918  51.282  1.00 35.23 ? 38  HIS F NE2 1 
ATOM   7500 N  N   . VAL F 1 42  ? 51.319  86.506  53.431  1.00 32.96 ? 39  VAL F N   1 
ATOM   7501 C  CA  . VAL F 1 42  ? 50.277  87.500  53.692  1.00 33.46 ? 39  VAL F CA  1 
ATOM   7502 C  C   . VAL F 1 42  ? 49.422  87.889  52.445  1.00 34.42 ? 39  VAL F C   1 
ATOM   7503 O  O   . VAL F 1 42  ? 48.173  87.879  52.503  1.00 34.12 ? 39  VAL F O   1 
ATOM   7504 C  CB  . VAL F 1 42  ? 50.893  88.751  54.421  1.00 33.14 ? 39  VAL F CB  1 
ATOM   7505 C  CG1 . VAL F 1 42  ? 51.736  89.599  53.484  1.00 32.60 ? 39  VAL F CG1 1 
ATOM   7506 C  CG2 . VAL F 1 42  ? 49.824  89.591  55.062  1.00 33.63 ? 39  VAL F CG2 1 
ATOM   7507 N  N   . ASP F 1 43  ? 50.095  88.203  51.334  1.00 34.79 ? 40  ASP F N   1 
ATOM   7508 C  CA  . ASP F 1 43  ? 49.436  88.571  50.070  1.00 35.85 ? 40  ASP F CA  1 
ATOM   7509 C  C   . ASP F 1 43  ? 48.434  87.537  49.504  1.00 35.73 ? 40  ASP F C   1 
ATOM   7510 O  O   . ASP F 1 43  ? 47.542  87.909  48.737  1.00 35.29 ? 40  ASP F O   1 
ATOM   7511 C  CB  . ASP F 1 43  ? 50.481  88.915  48.982  1.00 36.09 ? 40  ASP F CB  1 
ATOM   7512 C  CG  . ASP F 1 43  ? 51.207  90.258  49.235  1.00 38.43 ? 40  ASP F CG  1 
ATOM   7513 O  OD1 . ASP F 1 43  ? 52.090  90.611  48.424  1.00 40.85 ? 40  ASP F OD1 1 
ATOM   7514 O  OD2 . ASP F 1 43  ? 50.916  90.967  50.230  1.00 40.29 ? 40  ASP F OD2 1 
ATOM   7515 N  N   . GLU F 1 44  ? 48.580  86.265  49.887  1.00 35.56 ? 41  GLU F N   1 
ATOM   7516 C  CA  . GLU F 1 44  ? 47.757  85.182  49.359  1.00 35.78 ? 41  GLU F CA  1 
ATOM   7517 C  C   . GLU F 1 44  ? 46.828  84.556  50.411  1.00 35.06 ? 41  GLU F C   1 
ATOM   7518 O  O   . GLU F 1 44  ? 46.035  83.662  50.101  1.00 35.51 ? 41  GLU F O   1 
ATOM   7519 C  CB  . GLU F 1 44  ? 48.662  84.108  48.757  1.00 36.00 ? 41  GLU F CB  1 
ATOM   7520 C  CG  . GLU F 1 44  ? 49.467  83.311  49.804  1.00 37.82 ? 41  GLU F CG  1 
ATOM   7521 C  CD  . GLU F 1 44  ? 50.259  82.128  49.217  1.00 38.37 ? 41  GLU F CD  1 
ATOM   7522 O  OE1 . GLU F 1 44  ? 49.684  81.362  48.390  1.00 41.20 ? 41  GLU F OE1 1 
ATOM   7523 O  OE2 . GLU F 1 44  ? 51.453  81.958  49.605  1.00 40.54 ? 41  GLU F OE2 1 
ATOM   7524 N  N   . ALA F 1 45  ? 46.928  85.026  51.651  1.00 34.26 ? 42  ALA F N   1 
ATOM   7525 C  CA  . ALA F 1 45  ? 46.148  84.500  52.777  1.00 33.27 ? 42  ALA F CA  1 
ATOM   7526 C  C   . ALA F 1 45  ? 44.734  85.062  52.793  1.00 32.62 ? 42  ALA F C   1 
ATOM   7527 O  O   . ALA F 1 45  ? 44.517  86.190  52.353  1.00 32.53 ? 42  ALA F O   1 
ATOM   7528 C  CB  . ALA F 1 45  ? 46.851  84.829  54.092  1.00 33.16 ? 42  ALA F CB  1 
ATOM   7529 N  N   . THR F 1 46  ? 43.781  84.294  53.316  1.00 31.80 ? 43  THR F N   1 
ATOM   7530 C  CA  . THR F 1 46  ? 42.382  84.742  53.375  1.00 31.66 ? 43  THR F CA  1 
ATOM   7531 C  C   . THR F 1 46  ? 41.763  84.653  54.775  1.00 31.37 ? 43  THR F C   1 
ATOM   7532 O  O   . THR F 1 46  ? 42.311  84.001  55.652  1.00 31.07 ? 43  THR F O   1 
ATOM   7533 C  CB  . THR F 1 46  ? 41.470  83.948  52.403  1.00 31.93 ? 43  THR F CB  1 
ATOM   7534 O  OG1 . THR F 1 46  ? 41.550  82.552  52.711  1.00 32.36 ? 43  THR F OG1 1 
ATOM   7535 C  CG2 . THR F 1 46  ? 41.868  84.175  50.948  1.00 31.24 ? 43  THR F CG2 1 
ATOM   7536 N  N   . LYS F 1 47  ? 40.638  85.356  54.956  1.00 31.23 ? 44  LYS F N   1 
ATOM   7537 C  CA  . LYS F 1 47  ? 39.711  85.213  56.094  1.00 30.92 ? 44  LYS F CA  1 
ATOM   7538 C  C   . LYS F 1 47  ? 39.583  83.753  56.449  1.00 30.60 ? 44  LYS F C   1 
ATOM   7539 O  O   . LYS F 1 47  ? 39.671  83.374  57.606  1.00 30.25 ? 44  LYS F O   1 
ATOM   7540 C  CB  . LYS F 1 47  ? 38.299  85.642  55.663  1.00 31.37 ? 44  LYS F CB  1 
ATOM   7541 C  CG  . LYS F 1 47  ? 37.850  87.032  56.010  1.00 30.71 ? 44  LYS F CG  1 
ATOM   7542 C  CD  . LYS F 1 47  ? 36.325  87.105  55.882  1.00 32.59 ? 44  LYS F CD  1 
ATOM   7543 C  CE  . LYS F 1 47  ? 35.881  87.456  54.462  1.00 34.11 ? 44  LYS F CE  1 
ATOM   7544 N  NZ  . LYS F 1 47  ? 34.594  86.820  54.124  1.00 32.82 ? 44  LYS F NZ  1 
ATOM   7545 N  N   . GLU F 1 48  ? 39.345  82.957  55.410  1.00 30.83 ? 45  GLU F N   1 
ATOM   7546 C  CA  . GLU F 1 48  ? 38.967  81.563  55.529  1.00 30.78 ? 45  GLU F CA  1 
ATOM   7547 C  C   . GLU F 1 48  ? 40.123  80.698  56.014  1.00 30.20 ? 45  GLU F C   1 
ATOM   7548 O  O   . GLU F 1 48  ? 39.905  79.717  56.711  1.00 30.40 ? 45  GLU F O   1 
ATOM   7549 C  CB  . GLU F 1 48  ? 38.382  81.058  54.211  1.00 30.70 ? 45  GLU F CB  1 
ATOM   7550 C  CG  . GLU F 1 48  ? 36.984  81.631  53.897  1.00 32.94 ? 45  GLU F CG  1 
ATOM   7551 C  CD  . GLU F 1 48  ? 36.994  82.987  53.141  1.00 35.65 ? 45  GLU F CD  1 
ATOM   7552 O  OE1 . GLU F 1 48  ? 37.959  83.271  52.395  1.00 36.08 ? 45  GLU F OE1 1 
ATOM   7553 O  OE2 . GLU F 1 48  ? 36.013  83.765  53.269  1.00 35.82 ? 45  GLU F OE2 1 
ATOM   7554 N  N   . ASP F 1 49  ? 41.351  81.085  55.686  1.00 30.13 ? 46  ASP F N   1 
ATOM   7555 C  CA  . ASP F 1 49  ? 42.548  80.438  56.252  1.00 29.65 ? 46  ASP F CA  1 
ATOM   7556 C  C   . ASP F 1 49  ? 42.518  80.498  57.767  1.00 29.46 ? 46  ASP F C   1 
ATOM   7557 O  O   . ASP F 1 49  ? 42.828  79.512  58.450  1.00 29.99 ? 46  ASP F O   1 
ATOM   7558 C  CB  . ASP F 1 49  ? 43.824  81.105  55.744  1.00 29.61 ? 46  ASP F CB  1 
ATOM   7559 C  CG  . ASP F 1 49  ? 44.135  80.771  54.272  1.00 31.54 ? 46  ASP F CG  1 
ATOM   7560 O  OD1 . ASP F 1 49  ? 43.850  79.644  53.814  1.00 31.86 ? 46  ASP F OD1 1 
ATOM   7561 O  OD2 . ASP F 1 49  ? 44.680  81.648  53.573  1.00 33.55 ? 46  ASP F OD2 1 
ATOM   7562 N  N   . VAL F 1 50  ? 42.127  81.665  58.281  1.00 28.54 ? 47  VAL F N   1 
ATOM   7563 C  CA  . VAL F 1 50  ? 42.063  81.924  59.711  1.00 27.82 ? 47  VAL F CA  1 
ATOM   7564 C  C   . VAL F 1 50  ? 40.878  81.230  60.386  1.00 27.34 ? 47  VAL F C   1 
ATOM   7565 O  O   . VAL F 1 50  ? 41.036  80.655  61.462  1.00 27.05 ? 47  VAL F O   1 
ATOM   7566 C  CB  . VAL F 1 50  ? 42.024  83.456  60.004  1.00 28.36 ? 47  VAL F CB  1 
ATOM   7567 C  CG1 . VAL F 1 50  ? 41.821  83.710  61.466  1.00 26.28 ? 47  VAL F CG1 1 
ATOM   7568 C  CG2 . VAL F 1 50  ? 43.301  84.120  59.513  1.00 26.86 ? 47  VAL F CG2 1 
ATOM   7569 N  N   . LEU F 1 51  ? 39.701  81.302  59.761  1.00 26.43 ? 48  LEU F N   1 
ATOM   7570 C  CA  . LEU F 1 51  ? 38.528  80.588  60.237  1.00 26.22 ? 48  LEU F CA  1 
ATOM   7571 C  C   . LEU F 1 51  ? 38.824  79.086  60.293  1.00 26.46 ? 48  LEU F C   1 
ATOM   7572 O  O   . LEU F 1 51  ? 38.443  78.395  61.243  1.00 26.82 ? 48  LEU F O   1 
ATOM   7573 C  CB  . LEU F 1 51  ? 37.330  80.827  59.309  1.00 25.91 ? 48  LEU F CB  1 
ATOM   7574 C  CG  . LEU F 1 51  ? 36.580  82.162  59.303  1.00 25.48 ? 48  LEU F CG  1 
ATOM   7575 C  CD1 . LEU F 1 51  ? 35.474  82.132  58.258  1.00 23.42 ? 48  LEU F CD1 1 
ATOM   7576 C  CD2 . LEU F 1 51  ? 35.973  82.487  60.663  1.00 25.31 ? 48  LEU F CD2 1 
ATOM   7577 N  N   . TRP F 1 52  ? 39.513  78.594  59.267  1.00 26.16 ? 49  TRP F N   1 
ATOM   7578 C  CA  . TRP F 1 52  ? 39.913  77.199  59.199  1.00 25.98 ? 49  TRP F CA  1 
ATOM   7579 C  C   . TRP F 1 52  ? 40.796  76.800  60.395  1.00 25.88 ? 49  TRP F C   1 
ATOM   7580 O  O   . TRP F 1 52  ? 40.557  75.764  61.029  1.00 25.99 ? 49  TRP F O   1 
ATOM   7581 C  CB  . TRP F 1 52  ? 40.589  76.920  57.841  1.00 25.93 ? 49  TRP F CB  1 
ATOM   7582 C  CG  . TRP F 1 52  ? 41.240  75.578  57.712  1.00 25.58 ? 49  TRP F CG  1 
ATOM   7583 C  CD1 . TRP F 1 52  ? 40.643  74.400  57.331  1.00 25.50 ? 49  TRP F CD1 1 
ATOM   7584 C  CD2 . TRP F 1 52  ? 42.608  75.272  57.966  1.00 24.42 ? 49  TRP F CD2 1 
ATOM   7585 N  NE1 . TRP F 1 52  ? 41.570  73.382  57.328  1.00 24.90 ? 49  TRP F NE1 1 
ATOM   7586 C  CE2 . TRP F 1 52  ? 42.784  73.892  57.713  1.00 26.31 ? 49  TRP F CE2 1 
ATOM   7587 C  CE3 . TRP F 1 52  ? 43.714  76.034  58.363  1.00 25.57 ? 49  TRP F CE3 1 
ATOM   7588 C  CZ2 . TRP F 1 52  ? 44.023  73.253  57.865  1.00 26.34 ? 49  TRP F CZ2 1 
ATOM   7589 C  CZ3 . TRP F 1 52  ? 44.940  75.401  58.517  1.00 25.66 ? 49  TRP F CZ3 1 
ATOM   7590 C  CH2 . TRP F 1 52  ? 45.082  74.021  58.271  1.00 25.69 ? 49  TRP F CH2 1 
ATOM   7591 N  N   . ALA F 1 53  ? 41.787  77.637  60.697  1.00 25.45 ? 50  ALA F N   1 
ATOM   7592 C  CA  . ALA F 1 53  ? 42.807  77.347  61.702  1.00 25.87 ? 50  ALA F CA  1 
ATOM   7593 C  C   . ALA F 1 53  ? 42.365  77.216  63.195  1.00 26.29 ? 50  ALA F C   1 
ATOM   7594 O  O   . ALA F 1 53  ? 41.519  77.982  63.701  1.00 25.44 ? 50  ALA F O   1 
ATOM   7595 C  CB  . ALA F 1 53  ? 43.917  78.389  61.596  1.00 26.21 ? 50  ALA F CB  1 
ATOM   7596 N  N   . ASP F 1 54  ? 42.984  76.252  63.881  1.00 26.31 ? 51  ASP F N   1 
ATOM   7597 C  CA  . ASP F 1 54  ? 42.941  76.158  65.333  1.00 26.87 ? 51  ASP F CA  1 
ATOM   7598 C  C   . ASP F 1 54  ? 44.082  76.940  65.966  1.00 26.98 ? 51  ASP F C   1 
ATOM   7599 O  O   . ASP F 1 54  ? 43.947  77.452  67.072  1.00 27.26 ? 51  ASP F O   1 
ATOM   7600 C  CB  . ASP F 1 54  ? 43.051  74.708  65.782  1.00 26.85 ? 51  ASP F CB  1 
ATOM   7601 C  CG  . ASP F 1 54  ? 41.895  73.874  65.323  1.00 27.21 ? 51  ASP F CG  1 
ATOM   7602 O  OD1 . ASP F 1 54  ? 40.741  74.325  65.493  1.00 25.37 ? 51  ASP F OD1 1 
ATOM   7603 O  OD2 . ASP F 1 54  ? 42.156  72.767  64.805  1.00 26.55 ? 51  ASP F OD2 1 
ATOM   7604 N  N   . GLY F 1 55  ? 45.204  76.993  65.260  1.00 26.74 ? 52  GLY F N   1 
ATOM   7605 C  CA  . GLY F 1 55  ? 46.401  77.667  65.714  1.00 27.46 ? 52  GLY F CA  1 
ATOM   7606 C  C   . GLY F 1 55  ? 47.034  78.436  64.571  1.00 28.11 ? 52  GLY F C   1 
ATOM   7607 O  O   . GLY F 1 55  ? 46.968  78.006  63.408  1.00 28.52 ? 52  GLY F O   1 
ATOM   7608 N  N   . LEU F 1 56  ? 47.643  79.565  64.902  1.00 27.87 ? 53  LEU F N   1 
ATOM   7609 C  CA  . LEU F 1 56  ? 48.341  80.421  63.940  1.00 29.08 ? 53  LEU F CA  1 
ATOM   7610 C  C   . LEU F 1 56  ? 49.743  80.711  64.422  1.00 28.69 ? 53  LEU F C   1 
ATOM   7611 O  O   . LEU F 1 56  ? 49.937  81.049  65.592  1.00 29.20 ? 53  LEU F O   1 
ATOM   7612 C  CB  . LEU F 1 56  ? 47.672  81.804  63.820  1.00 29.35 ? 53  LEU F CB  1 
ATOM   7613 C  CG  . LEU F 1 56  ? 46.283  81.909  63.225  1.00 31.12 ? 53  LEU F CG  1 
ATOM   7614 C  CD1 . LEU F 1 56  ? 45.240  81.613  64.327  1.00 34.15 ? 53  LEU F CD1 1 
ATOM   7615 C  CD2 . LEU F 1 56  ? 46.109  83.292  62.657  1.00 31.70 ? 53  LEU F CD2 1 
ATOM   7616 N  N   . ALA F 1 57  ? 50.702  80.631  63.504  1.00 27.91 ? 54  ALA F N   1 
ATOM   7617 C  CA  . ALA F 1 57  ? 52.034  81.173  63.714  1.00 26.98 ? 54  ALA F CA  1 
ATOM   7618 C  C   . ALA F 1 57  ? 52.143  82.352  62.746  1.00 27.03 ? 54  ALA F C   1 
ATOM   7619 O  O   . ALA F 1 57  ? 52.059  82.170  61.521  1.00 27.21 ? 54  ALA F O   1 
ATOM   7620 C  CB  . ALA F 1 57  ? 53.106  80.113  63.440  1.00 25.97 ? 54  ALA F CB  1 
ATOM   7621 N  N   . VAL F 1 58  ? 52.285  83.555  63.297  1.00 26.35 ? 55  VAL F N   1 
ATOM   7622 C  CA  . VAL F 1 58  ? 52.326  84.766  62.499  1.00 25.75 ? 55  VAL F CA  1 
ATOM   7623 C  C   . VAL F 1 58  ? 53.748  85.299  62.514  1.00 26.12 ? 55  VAL F C   1 
ATOM   7624 O  O   . VAL F 1 58  ? 54.309  85.541  63.598  1.00 26.75 ? 55  VAL F O   1 
ATOM   7625 C  CB  . VAL F 1 58  ? 51.338  85.848  63.075  1.00 26.23 ? 55  VAL F CB  1 
ATOM   7626 C  CG1 . VAL F 1 58  ? 51.448  87.187  62.295  1.00 23.27 ? 55  VAL F CG1 1 
ATOM   7627 C  CG2 . VAL F 1 58  ? 49.905  85.284  63.132  1.00 22.30 ? 55  VAL F CG2 1 
ATOM   7628 N  N   . GLY F 1 59  ? 54.326  85.447  61.323  1.00 25.73 ? 56  GLY F N   1 
ATOM   7629 C  CA  . GLY F 1 59  ? 55.711  85.874  61.153  1.00 25.43 ? 56  GLY F CA  1 
ATOM   7630 C  C   . GLY F 1 59  ? 55.876  87.171  60.406  1.00 25.52 ? 56  GLY F C   1 
ATOM   7631 O  O   . GLY F 1 59  ? 55.099  87.504  59.524  1.00 25.72 ? 56  GLY F O   1 
ATOM   7632 N  N   . SER F 1 60  ? 56.881  87.935  60.774  1.00 25.72 ? 57  SER F N   1 
ATOM   7633 C  CA  . SER F 1 60  ? 57.106  89.216  60.129  1.00 25.97 ? 57  SER F CA  1 
ATOM   7634 C  C   . SER F 1 60  ? 58.552  89.605  60.255  1.00 25.45 ? 57  SER F C   1 
ATOM   7635 O  O   . SER F 1 60  ? 59.179  89.295  61.275  1.00 25.62 ? 57  SER F O   1 
ATOM   7636 C  CB  . SER F 1 60  ? 56.248  90.323  60.750  1.00 26.56 ? 57  SER F CB  1 
ATOM   7637 O  OG  . SER F 1 60  ? 56.535  91.587  60.150  1.00 28.75 ? 57  SER F OG  1 
ATOM   7638 N  N   . PRO F 1 61  ? 59.082  90.310  59.238  1.00 25.01 ? 58  PRO F N   1 
ATOM   7639 C  CA  . PRO F 1 61  ? 60.367  90.922  59.489  1.00 25.09 ? 58  PRO F CA  1 
ATOM   7640 C  C   . PRO F 1 61  ? 60.161  91.965  60.591  1.00 25.91 ? 58  PRO F C   1 
ATOM   7641 O  O   . PRO F 1 61  ? 59.047  92.482  60.764  1.00 26.15 ? 58  PRO F O   1 
ATOM   7642 C  CB  . PRO F 1 61  ? 60.723  91.587  58.137  1.00 24.47 ? 58  PRO F CB  1 
ATOM   7643 C  CG  . PRO F 1 61  ? 59.441  91.789  57.455  1.00 24.15 ? 58  PRO F CG  1 
ATOM   7644 C  CD  . PRO F 1 61  ? 58.568  90.620  57.890  1.00 24.60 ? 58  PRO F CD  1 
ATOM   7645 N  N   . THR F 1 62  ? 61.228  92.247  61.336  1.00 26.92 ? 59  THR F N   1 
ATOM   7646 C  CA  . THR F 1 62  ? 61.259  93.306  62.336  1.00 26.99 ? 59  THR F CA  1 
ATOM   7647 C  C   . THR F 1 62  ? 61.411  94.587  61.565  1.00 27.40 ? 59  THR F C   1 
ATOM   7648 O  O   . THR F 1 62  ? 62.484  94.857  61.041  1.00 27.65 ? 59  THR F O   1 
ATOM   7649 C  CB  . THR F 1 62  ? 62.482  93.124  63.257  1.00 26.90 ? 59  THR F CB  1 
ATOM   7650 O  OG1 . THR F 1 62  ? 62.386  91.852  63.914  1.00 28.36 ? 59  THR F OG1 1 
ATOM   7651 C  CG2 . THR F 1 62  ? 62.623  94.259  64.278  1.00 24.84 ? 59  THR F CG2 1 
ATOM   7652 N  N   . ASN F 1 63  ? 60.341  95.364  61.466  1.00 28.17 ? 60  ASN F N   1 
ATOM   7653 C  CA  . ASN F 1 63  ? 60.394  96.625  60.717  1.00 28.69 ? 60  ASN F CA  1 
ATOM   7654 C  C   . ASN F 1 63  ? 60.186  97.822  61.617  1.00 29.57 ? 60  ASN F C   1 
ATOM   7655 O  O   . ASN F 1 63  ? 59.067  98.089  62.040  1.00 30.79 ? 60  ASN F O   1 
ATOM   7656 C  CB  . ASN F 1 63  ? 59.352  96.624  59.602  1.00 28.37 ? 60  ASN F CB  1 
ATOM   7657 C  CG  . ASN F 1 63  ? 59.742  95.725  58.415  1.00 29.61 ? 60  ASN F CG  1 
ATOM   7658 O  OD1 . ASN F 1 63  ? 58.921  95.480  57.524  1.00 31.32 ? 60  ASN F OD1 1 
ATOM   7659 N  ND2 . ASN F 1 63  ? 60.989  95.236  58.399  1.00 27.63 ? 60  ASN F ND2 1 
HETATM 7660 N  N   . MSE F 1 64  ? 61.254  98.543  61.917  1.00 30.66 ? 61  MSE F N   1 
HETATM 7661 C  CA  . MSE F 1 64  ? 61.213  99.662  62.889  1.00 32.34 ? 61  MSE F CA  1 
HETATM 7662 C  C   . MSE F 1 64  ? 60.723  99.186  64.249  1.00 30.46 ? 61  MSE F C   1 
HETATM 7663 O  O   . MSE F 1 64  ? 60.071  99.937  64.958  1.00 30.90 ? 61  MSE F O   1 
HETATM 7664 C  CB  . MSE F 1 64  ? 60.341  100.844 62.422  1.00 33.48 ? 61  MSE F CB  1 
HETATM 7665 C  CG  . MSE F 1 64  ? 60.637  101.354 61.043  1.00 42.35 ? 61  MSE F CG  1 
HETATM 7666 SE SE  . MSE F 1 64  ? 62.487  102.069 60.868  1.00 68.29 ? 61  MSE F SE  1 
HETATM 7667 C  CE  . MSE F 1 64  ? 63.720  100.373 60.832  1.00 59.66 ? 61  MSE F CE  1 
ATOM   7668 N  N   . GLY F 1 65  ? 61.003  97.934  64.571  1.00 28.62 ? 62  GLY F N   1 
ATOM   7669 C  CA  . GLY F 1 65  ? 60.663  97.343  65.860  1.00 27.55 ? 62  GLY F CA  1 
ATOM   7670 C  C   . GLY F 1 65  ? 59.371  96.549  65.915  1.00 26.47 ? 62  GLY F C   1 
ATOM   7671 O  O   . GLY F 1 65  ? 59.094  95.917  66.923  1.00 25.80 ? 62  GLY F O   1 
ATOM   7672 N  N   . LEU F 1 66  ? 58.584  96.585  64.837  1.00 26.02 ? 63  LEU F N   1 
ATOM   7673 C  CA  . LEU F 1 66  ? 57.177  96.149  64.868  1.00 25.28 ? 63  LEU F CA  1 
ATOM   7674 C  C   . LEU F 1 66  ? 56.803  95.236  63.685  1.00 25.63 ? 63  LEU F C   1 
ATOM   7675 O  O   . LEU F 1 66  ? 57.563  95.164  62.708  1.00 26.08 ? 63  LEU F O   1 
ATOM   7676 C  CB  . LEU F 1 66  ? 56.278  97.402  64.867  1.00 24.98 ? 63  LEU F CB  1 
ATOM   7677 C  CG  . LEU F 1 66  ? 56.335  98.452  66.003  1.00 23.16 ? 63  LEU F CG  1 
ATOM   7678 C  CD1 . LEU F 1 66  ? 55.565  99.728  65.612  1.00 19.01 ? 63  LEU F CD1 1 
ATOM   7679 C  CD2 . LEU F 1 66  ? 55.792  97.861  67.347  1.00 21.37 ? 63  LEU F CD2 1 
ATOM   7680 N  N   . VAL F 1 67  ? 55.659  94.529  63.757  1.00 25.86 ? 64  VAL F N   1 
ATOM   7681 C  CA  . VAL F 1 67  ? 55.071  93.919  62.548  1.00 25.24 ? 64  VAL F CA  1 
ATOM   7682 C  C   . VAL F 1 67  ? 55.217  94.881  61.359  1.00 24.50 ? 64  VAL F C   1 
ATOM   7683 O  O   . VAL F 1 67  ? 55.142  96.109  61.532  1.00 23.48 ? 64  VAL F O   1 
ATOM   7684 C  CB  . VAL F 1 67  ? 53.514  93.807  62.614  1.00 25.84 ? 64  VAL F CB  1 
ATOM   7685 C  CG1 . VAL F 1 67  ? 53.013  92.375  62.465  1.00 26.87 ? 64  VAL F CG1 1 
ATOM   7686 C  CG2 . VAL F 1 67  ? 52.950  94.560  63.764  1.00 25.27 ? 64  VAL F CG2 1 
ATOM   7687 N  N   . SER F 1 68  ? 55.301  94.297  60.163  1.00 22.99 ? 65  SER F N   1 
ATOM   7688 C  CA  . SER F 1 68  ? 55.253  95.021  58.926  1.00 22.29 ? 65  SER F CA  1 
ATOM   7689 C  C   . SER F 1 68  ? 53.888  95.671  58.688  1.00 22.81 ? 65  SER F C   1 
ATOM   7690 O  O   . SER F 1 68  ? 52.853  95.269  59.289  1.00 22.38 ? 65  SER F O   1 
ATOM   7691 C  CB  . SER F 1 68  ? 55.577  94.065  57.770  1.00 22.46 ? 65  SER F CB  1 
ATOM   7692 O  OG  . SER F 1 68  ? 54.462  93.252  57.459  1.00 21.55 ? 65  SER F OG  1 
ATOM   7693 N  N   . TRP F 1 69  ? 53.865  96.656  57.788  1.00 22.10 ? 66  TRP F N   1 
ATOM   7694 C  CA  . TRP F 1 69  ? 52.627  97.357  57.565  1.00 22.67 ? 66  TRP F CA  1 
ATOM   7695 C  C   . TRP F 1 69  ? 51.612  96.482  56.828  1.00 23.69 ? 66  TRP F C   1 
ATOM   7696 O  O   . TRP F 1 69  ? 50.405  96.610  57.071  1.00 24.48 ? 66  TRP F O   1 
ATOM   7697 C  CB  . TRP F 1 69  ? 52.826  98.737  56.928  1.00 21.37 ? 66  TRP F CB  1 
ATOM   7698 C  CG  . TRP F 1 69  ? 53.234  98.750  55.476  1.00 21.67 ? 66  TRP F CG  1 
ATOM   7699 C  CD1 . TRP F 1 69  ? 54.496  98.933  54.979  1.00 20.58 ? 66  TRP F CD1 1 
ATOM   7700 C  CD2 . TRP F 1 69  ? 52.374  98.603  54.334  1.00 20.36 ? 66  TRP F CD2 1 
ATOM   7701 N  NE1 . TRP F 1 69  ? 54.478  98.897  53.616  1.00 19.44 ? 66  TRP F NE1 1 
ATOM   7702 C  CE2 . TRP F 1 69  ? 53.192  98.693  53.188  1.00 20.68 ? 66  TRP F CE2 1 
ATOM   7703 C  CE3 . TRP F 1 69  ? 50.994  98.409  54.170  1.00 19.16 ? 66  TRP F CE3 1 
ATOM   7704 C  CZ2 . TRP F 1 69  ? 52.673  98.604  51.884  1.00 20.12 ? 66  TRP F CZ2 1 
ATOM   7705 C  CZ3 . TRP F 1 69  ? 50.484  98.300  52.886  1.00 19.50 ? 66  TRP F CZ3 1 
ATOM   7706 C  CH2 . TRP F 1 69  ? 51.322  98.412  51.757  1.00 20.52 ? 66  TRP F CH2 1 
ATOM   7707 N  N   . LYS F 1 70  ? 52.108  95.583  55.973  1.00 24.47 ? 67  LYS F N   1 
ATOM   7708 C  CA  . LYS F 1 70  ? 51.275  94.671  55.194  1.00 25.05 ? 67  LYS F CA  1 
ATOM   7709 C  C   . LYS F 1 70  ? 50.677  93.560  56.073  1.00 26.33 ? 67  LYS F C   1 
ATOM   7710 O  O   . LYS F 1 70  ? 49.522  93.190  55.908  1.00 26.79 ? 67  LYS F O   1 
ATOM   7711 C  CB  . LYS F 1 70  ? 52.060  94.091  54.008  1.00 25.19 ? 67  LYS F CB  1 
ATOM   7712 C  CG  . LYS F 1 70  ? 52.111  94.972  52.730  1.00 23.78 ? 67  LYS F CG  1 
ATOM   7713 C  CD  . LYS F 1 70  ? 52.844  94.268  51.539  1.00 24.04 ? 67  LYS F CD  1 
ATOM   7714 C  CE  . LYS F 1 70  ? 52.372  94.792  50.173  1.00 25.12 ? 67  LYS F CE  1 
ATOM   7715 N  NZ  . LYS F 1 70  ? 52.918  94.062  48.937  1.00 24.70 ? 67  LYS F NZ  1 
HETATM 7716 N  N   . MSE F 1 71  ? 51.434  93.066  57.049  1.00 27.44 ? 68  MSE F N   1 
HETATM 7717 C  CA  . MSE F 1 71  ? 50.851  92.133  58.024  1.00 27.95 ? 68  MSE F CA  1 
HETATM 7718 C  C   . MSE F 1 71  ? 49.776  92.790  58.909  1.00 27.21 ? 68  MSE F C   1 
HETATM 7719 O  O   . MSE F 1 71  ? 48.707  92.223  59.132  1.00 28.15 ? 68  MSE F O   1 
HETATM 7720 C  CB  . MSE F 1 71  ? 51.932  91.469  58.876  1.00 28.22 ? 68  MSE F CB  1 
HETATM 7721 C  CG  . MSE F 1 71  ? 51.342  90.423  59.838  1.00 33.00 ? 68  MSE F CG  1 
HETATM 7722 SE SE  . MSE F 1 71  ? 50.401  88.900  58.917  1.00 45.55 ? 68  MSE F SE  1 
HETATM 7723 C  CE  . MSE F 1 71  ? 51.986  87.854  58.438  1.00 35.37 ? 68  MSE F CE  1 
ATOM   7724 N  N   . LYS F 1 72  ? 50.082  93.978  59.409  1.00 26.11 ? 69  LYS F N   1 
ATOM   7725 C  CA  . LYS F 1 72  ? 49.135  94.832  60.126  1.00 25.40 ? 69  LYS F CA  1 
ATOM   7726 C  C   . LYS F 1 72  ? 47.846  95.055  59.354  1.00 24.77 ? 69  LYS F C   1 
ATOM   7727 O  O   . LYS F 1 72  ? 46.771  94.973  59.899  1.00 25.19 ? 69  LYS F O   1 
ATOM   7728 C  CB  . LYS F 1 72  ? 49.787  96.198  60.418  1.00 24.99 ? 69  LYS F CB  1 
ATOM   7729 C  CG  . LYS F 1 72  ? 48.998  97.099  61.321  1.00 24.55 ? 69  LYS F CG  1 
ATOM   7730 C  CD  . LYS F 1 72  ? 49.115  96.642  62.784  1.00 24.95 ? 69  LYS F CD  1 
ATOM   7731 C  CE  . LYS F 1 72  ? 47.782  96.692  63.512  1.00 18.29 ? 69  LYS F CE  1 
ATOM   7732 N  NZ  . LYS F 1 72  ? 47.170  98.014  63.400  1.00 19.87 ? 69  LYS F NZ  1 
ATOM   7733 N  N   . ARG F 1 73  ? 47.970  95.338  58.069  1.00 24.88 ? 70  ARG F N   1 
ATOM   7734 C  CA  . ARG F 1 73  ? 46.832  95.688  57.229  1.00 24.25 ? 70  ARG F CA  1 
ATOM   7735 C  C   . ARG F 1 73  ? 45.946  94.463  56.965  1.00 24.87 ? 70  ARG F C   1 
ATOM   7736 O  O   . ARG F 1 73  ? 44.719  94.567  56.822  1.00 24.87 ? 70  ARG F O   1 
ATOM   7737 C  CB  . ARG F 1 73  ? 47.381  96.284  55.952  1.00 23.13 ? 70  ARG F CB  1 
ATOM   7738 C  CG  . ARG F 1 73  ? 46.407  96.603  54.856  1.00 22.16 ? 70  ARG F CG  1 
ATOM   7739 C  CD  . ARG F 1 73  ? 47.058  96.150  53.586  1.00 20.91 ? 70  ARG F CD  1 
ATOM   7740 N  NE  . ARG F 1 73  ? 46.909  97.139  52.563  1.00 22.59 ? 70  ARG F NE  1 
ATOM   7741 C  CZ  . ARG F 1 73  ? 47.468  97.071  51.360  1.00 19.21 ? 70  ARG F CZ  1 
ATOM   7742 N  NH1 . ARG F 1 73  ? 47.243  98.055  50.528  1.00 14.48 ? 70  ARG F NH1 1 
ATOM   7743 N  NH2 . ARG F 1 73  ? 48.228  96.038  51.004  1.00 18.27 ? 70  ARG F NH2 1 
ATOM   7744 N  N   . PHE F 1 74  ? 46.574  93.298  56.917  1.00 25.34 ? 71  PHE F N   1 
ATOM   7745 C  CA  . PHE F 1 74  ? 45.838  92.065  56.811  1.00 26.31 ? 71  PHE F CA  1 
ATOM   7746 C  C   . PHE F 1 74  ? 44.885  91.930  58.013  1.00 27.37 ? 71  PHE F C   1 
ATOM   7747 O  O   . PHE F 1 74  ? 43.695  91.631  57.846  1.00 27.76 ? 71  PHE F O   1 
ATOM   7748 C  CB  . PHE F 1 74  ? 46.808  90.881  56.748  1.00 26.07 ? 71  PHE F CB  1 
ATOM   7749 C  CG  . PHE F 1 74  ? 46.123  89.564  56.592  1.00 26.08 ? 71  PHE F CG  1 
ATOM   7750 C  CD1 . PHE F 1 74  ? 45.590  89.183  55.357  1.00 26.85 ? 71  PHE F CD1 1 
ATOM   7751 C  CD2 . PHE F 1 74  ? 45.978  88.708  57.679  1.00 25.02 ? 71  PHE F CD2 1 
ATOM   7752 C  CE1 . PHE F 1 74  ? 44.934  87.940  55.200  1.00 26.96 ? 71  PHE F CE1 1 
ATOM   7753 C  CE2 . PHE F 1 74  ? 45.322  87.475  57.531  1.00 27.30 ? 71  PHE F CE2 1 
ATOM   7754 C  CZ  . PHE F 1 74  ? 44.802  87.094  56.279  1.00 25.60 ? 71  PHE F CZ  1 
ATOM   7755 N  N   . PHE F 1 75  ? 45.426  92.154  59.214  1.00 27.97 ? 72  PHE F N   1 
ATOM   7756 C  CA  . PHE F 1 75  ? 44.676  92.080  60.440  1.00 28.22 ? 72  PHE F CA  1 
ATOM   7757 C  C   . PHE F 1 75  ? 43.636  93.195  60.556  1.00 29.04 ? 72  PHE F C   1 
ATOM   7758 O  O   . PHE F 1 75  ? 42.465  92.890  60.806  1.00 29.69 ? 72  PHE F O   1 
ATOM   7759 C  CB  . PHE F 1 75  ? 45.638  92.007  61.647  1.00 28.68 ? 72  PHE F CB  1 
ATOM   7760 C  CG  . PHE F 1 75  ? 46.143  90.601  61.924  1.00 30.34 ? 72  PHE F CG  1 
ATOM   7761 C  CD1 . PHE F 1 75  ? 47.195  90.065  61.190  1.00 26.87 ? 72  PHE F CD1 1 
ATOM   7762 C  CD2 . PHE F 1 75  ? 45.509  89.783  62.882  1.00 32.26 ? 72  PHE F CD2 1 
ATOM   7763 C  CE1 . PHE F 1 75  ? 47.631  88.749  61.415  1.00 28.55 ? 72  PHE F CE1 1 
ATOM   7764 C  CE2 . PHE F 1 75  ? 45.943  88.448  63.110  1.00 30.45 ? 72  PHE F CE2 1 
ATOM   7765 C  CZ  . PHE F 1 75  ? 47.005  87.941  62.378  1.00 29.85 ? 72  PHE F CZ  1 
ATOM   7766 N  N   . ASP F 1 76  ? 44.029  94.459  60.336  1.00 28.99 ? 73  ASP F N   1 
ATOM   7767 C  CA  . ASP F 1 76  ? 43.095  95.585  60.429  1.00 30.06 ? 73  ASP F CA  1 
ATOM   7768 C  C   . ASP F 1 76  ? 41.942  95.447  59.445  1.00 30.62 ? 73  ASP F C   1 
ATOM   7769 O  O   . ASP F 1 76  ? 40.785  95.710  59.802  1.00 30.58 ? 73  ASP F O   1 
ATOM   7770 C  CB  . ASP F 1 76  ? 43.771  96.960  60.206  1.00 30.31 ? 73  ASP F CB  1 
ATOM   7771 C  CG  . ASP F 1 76  ? 44.763  97.359  61.326  1.00 32.44 ? 73  ASP F CG  1 
ATOM   7772 O  OD1 . ASP F 1 76  ? 44.585  96.933  62.496  1.00 34.47 ? 73  ASP F OD1 1 
ATOM   7773 O  OD2 . ASP F 1 76  ? 45.733  98.119  61.032  1.00 32.34 ? 73  ASP F OD2 1 
ATOM   7774 N  N   . ASP F 1 77  ? 42.256  95.020  58.217  1.00 31.26 ? 74  ASP F N   1 
ATOM   7775 C  CA  . ASP F 1 77  ? 41.322  95.154  57.097  1.00 31.68 ? 74  ASP F CA  1 
ATOM   7776 C  C   . ASP F 1 77  ? 40.737  93.877  56.468  1.00 32.26 ? 74  ASP F C   1 
ATOM   7777 O  O   . ASP F 1 77  ? 39.679  93.945  55.851  1.00 32.91 ? 74  ASP F O   1 
ATOM   7778 C  CB  . ASP F 1 77  ? 41.939  96.023  55.993  1.00 31.35 ? 74  ASP F CB  1 
ATOM   7779 C  CG  . ASP F 1 77  ? 42.112  97.465  56.413  1.00 30.98 ? 74  ASP F CG  1 
ATOM   7780 O  OD1 . ASP F 1 77  ? 41.877  97.804  57.581  1.00 30.92 ? 74  ASP F OD1 1 
ATOM   7781 O  OD2 . ASP F 1 77  ? 42.494  98.279  55.571  1.00 31.18 ? 74  ASP F OD2 1 
ATOM   7782 N  N   . VAL F 1 78  ? 41.426  92.745  56.554  1.00 32.38 ? 75  VAL F N   1 
ATOM   7783 C  CA  . VAL F 1 78  ? 40.882  91.506  56.015  1.00 32.07 ? 75  VAL F CA  1 
ATOM   7784 C  C   . VAL F 1 78  ? 40.188  90.747  57.134  1.00 33.04 ? 75  VAL F C   1 
ATOM   7785 O  O   . VAL F 1 78  ? 39.086  90.244  56.935  1.00 33.63 ? 75  VAL F O   1 
ATOM   7786 C  CB  . VAL F 1 78  ? 41.961  90.622  55.356  1.00 32.26 ? 75  VAL F CB  1 
ATOM   7787 C  CG1 . VAL F 1 78  ? 41.465  89.179  55.195  1.00 30.73 ? 75  VAL F CG1 1 
ATOM   7788 C  CG2 . VAL F 1 78  ? 42.368  91.206  54.020  1.00 30.44 ? 75  VAL F CG2 1 
ATOM   7789 N  N   . LEU F 1 79  ? 40.828  90.686  58.307  1.00 33.00 ? 76  LEU F N   1 
ATOM   7790 C  CA  . LEU F 1 79  ? 40.272  89.987  59.457  1.00 33.07 ? 76  LEU F CA  1 
ATOM   7791 C  C   . LEU F 1 79  ? 39.387  90.857  60.347  1.00 32.92 ? 76  LEU F C   1 
ATOM   7792 O  O   . LEU F 1 79  ? 38.785  90.353  61.276  1.00 32.64 ? 76  LEU F O   1 
ATOM   7793 C  CB  . LEU F 1 79  ? 41.388  89.366  60.288  1.00 33.48 ? 76  LEU F CB  1 
ATOM   7794 C  CG  . LEU F 1 79  ? 42.302  88.408  59.531  1.00 35.04 ? 76  LEU F CG  1 
ATOM   7795 C  CD1 . LEU F 1 79  ? 43.465  88.052  60.450  1.00 38.77 ? 76  LEU F CD1 1 
ATOM   7796 C  CD2 . LEU F 1 79  ? 41.541  87.150  59.104  1.00 35.45 ? 76  LEU F CD2 1 
ATOM   7797 N  N   . GLY F 1 80  ? 39.297  92.152  60.046  1.00 32.84 ? 77  GLY F N   1 
ATOM   7798 C  CA  . GLY F 1 80  ? 38.476  93.079  60.814  1.00 32.58 ? 77  GLY F CA  1 
ATOM   7799 C  C   . GLY F 1 80  ? 37.041  92.626  60.987  1.00 32.79 ? 77  GLY F C   1 
ATOM   7800 O  O   . GLY F 1 80  ? 36.463  92.756  62.063  1.00 33.22 ? 77  GLY F O   1 
ATOM   7801 N  N   . ASP F 1 81  ? 36.461  92.071  59.933  1.00 32.76 ? 78  ASP F N   1 
ATOM   7802 C  CA  . ASP F 1 81  ? 35.084  91.564  59.990  1.00 32.51 ? 78  ASP F CA  1 
ATOM   7803 C  C   . ASP F 1 81  ? 34.849  90.362  60.909  1.00 31.04 ? 78  ASP F C   1 
ATOM   7804 O  O   . ASP F 1 81  ? 33.717  90.089  61.322  1.00 30.86 ? 78  ASP F O   1 
ATOM   7805 C  CB  . ASP F 1 81  ? 34.598  91.236  58.586  1.00 33.16 ? 78  ASP F CB  1 
ATOM   7806 C  CG  . ASP F 1 81  ? 33.746  92.337  58.017  1.00 36.48 ? 78  ASP F CG  1 
ATOM   7807 O  OD1 . ASP F 1 81  ? 32.544  92.427  58.401  1.00 38.47 ? 78  ASP F OD1 1 
ATOM   7808 O  OD2 . ASP F 1 81  ? 34.291  93.119  57.200  1.00 39.90 ? 78  ASP F OD2 1 
ATOM   7809 N  N   . LEU F 1 82  ? 35.917  89.639  61.199  1.00 29.57 ? 79  LEU F N   1 
ATOM   7810 C  CA  . LEU F 1 82  ? 35.834  88.480  62.067  1.00 28.58 ? 79  LEU F CA  1 
ATOM   7811 C  C   . LEU F 1 82  ? 36.083  88.860  63.536  1.00 27.59 ? 79  LEU F C   1 
ATOM   7812 O  O   . LEU F 1 82  ? 35.914  88.028  64.448  1.00 26.82 ? 79  LEU F O   1 
ATOM   7813 C  CB  . LEU F 1 82  ? 36.840  87.413  61.617  1.00 28.48 ? 79  LEU F CB  1 
ATOM   7814 C  CG  . LEU F 1 82  ? 36.740  86.809  60.221  1.00 27.79 ? 79  LEU F CG  1 
ATOM   7815 C  CD1 . LEU F 1 82  ? 37.612  85.582  60.199  1.00 26.00 ? 79  LEU F CD1 1 
ATOM   7816 C  CD2 . LEU F 1 82  ? 35.313  86.462  59.872  1.00 27.31 ? 79  LEU F CD2 1 
ATOM   7817 N  N   . TRP F 1 83  ? 36.511  90.106  63.755  1.00 26.27 ? 80  TRP F N   1 
ATOM   7818 C  CA  . TRP F 1 83  ? 36.875  90.532  65.089  1.00 25.32 ? 80  TRP F CA  1 
ATOM   7819 C  C   . TRP F 1 83  ? 35.677  90.370  66.024  1.00 25.28 ? 80  TRP F C   1 
ATOM   7820 O  O   . TRP F 1 83  ? 34.585  90.857  65.748  1.00 25.45 ? 80  TRP F O   1 
ATOM   7821 C  CB  . TRP F 1 83  ? 37.402  91.965  65.097  1.00 24.88 ? 80  TRP F CB  1 
ATOM   7822 C  CG  . TRP F 1 83  ? 37.941  92.356  66.413  1.00 23.77 ? 80  TRP F CG  1 
ATOM   7823 C  CD1 . TRP F 1 83  ? 39.218  92.247  66.821  1.00 23.39 ? 80  TRP F CD1 1 
ATOM   7824 C  CD2 . TRP F 1 83  ? 37.203  92.889  67.525  1.00 23.87 ? 80  TRP F CD2 1 
ATOM   7825 N  NE1 . TRP F 1 83  ? 39.347  92.683  68.116  1.00 23.00 ? 80  TRP F NE1 1 
ATOM   7826 C  CE2 . TRP F 1 83  ? 38.121  93.089  68.571  1.00 22.95 ? 80  TRP F CE2 1 
ATOM   7827 C  CE3 . TRP F 1 83  ? 35.854  93.223  67.732  1.00 23.91 ? 80  TRP F CE3 1 
ATOM   7828 C  CZ2 . TRP F 1 83  ? 37.744  93.605  69.810  1.00 22.96 ? 80  TRP F CZ2 1 
ATOM   7829 C  CZ3 . TRP F 1 83  ? 35.479  93.737  68.963  1.00 23.42 ? 80  TRP F CZ3 1 
ATOM   7830 C  CH2 . TRP F 1 83  ? 36.422  93.915  69.991  1.00 23.95 ? 80  TRP F CH2 1 
ATOM   7831 N  N   . GLY F 1 84  ? 35.890  89.657  67.123  1.00 24.90 ? 81  GLY F N   1 
ATOM   7832 C  CA  . GLY F 1 84  ? 34.837  89.436  68.081  1.00 24.56 ? 81  GLY F CA  1 
ATOM   7833 C  C   . GLY F 1 84  ? 34.116  88.107  67.941  1.00 24.46 ? 81  GLY F C   1 
ATOM   7834 O  O   . GLY F 1 84  ? 33.313  87.756  68.795  1.00 23.84 ? 81  GLY F O   1 
ATOM   7835 N  N   . GLU F 1 85  ? 34.400  87.359  66.879  1.00 24.82 ? 82  GLU F N   1 
ATOM   7836 C  CA  . GLU F 1 85  ? 33.716  86.087  66.683  1.00 25.38 ? 82  GLU F CA  1 
ATOM   7837 C  C   . GLU F 1 85  ? 34.635  84.901  66.418  1.00 24.77 ? 82  GLU F C   1 
ATOM   7838 O  O   . GLU F 1 85  ? 34.181  83.830  66.055  1.00 25.62 ? 82  GLU F O   1 
ATOM   7839 C  CB  . GLU F 1 85  ? 32.620  86.205  65.624  1.00 25.54 ? 82  GLU F CB  1 
ATOM   7840 C  CG  . GLU F 1 85  ? 32.870  87.215  64.559  1.00 27.97 ? 82  GLU F CG  1 
ATOM   7841 C  CD  . GLU F 1 85  ? 31.975  86.986  63.358  1.00 33.21 ? 82  GLU F CD  1 
ATOM   7842 O  OE1 . GLU F 1 85  ? 32.191  85.980  62.621  1.00 32.98 ? 82  GLU F OE1 1 
ATOM   7843 O  OE2 . GLU F 1 85  ? 31.043  87.809  63.168  1.00 35.05 ? 82  GLU F OE2 1 
ATOM   7844 N  N   . ILE F 1 86  ? 35.921  85.091  66.646  1.00 24.22 ? 83  ILE F N   1 
ATOM   7845 C  CA  . ILE F 1 86  ? 36.923  84.036  66.483  1.00 23.85 ? 83  ILE F CA  1 
ATOM   7846 C  C   . ILE F 1 86  ? 37.853  83.915  67.711  1.00 24.50 ? 83  ILE F C   1 
ATOM   7847 O  O   . ILE F 1 86  ? 38.925  83.323  67.642  1.00 25.57 ? 83  ILE F O   1 
ATOM   7848 C  CB  . ILE F 1 86  ? 37.733  84.216  65.168  1.00 23.63 ? 83  ILE F CB  1 
ATOM   7849 C  CG1 . ILE F 1 86  ? 38.296  85.641  65.046  1.00 22.85 ? 83  ILE F CG1 1 
ATOM   7850 C  CG2 . ILE F 1 86  ? 36.851  83.883  63.942  1.00 22.53 ? 83  ILE F CG2 1 
ATOM   7851 C  CD1 . ILE F 1 86  ? 39.460  85.790  64.012  1.00 23.73 ? 83  ILE F CD1 1 
ATOM   7852 N  N   . ASP F 1 87  ? 37.433  84.481  68.834  1.00 24.46 ? 84  ASP F N   1 
ATOM   7853 C  CA  . ASP F 1 87  ? 38.117  84.299  70.103  1.00 24.76 ? 84  ASP F CA  1 
ATOM   7854 C  C   . ASP F 1 87  ? 38.536  82.863  70.379  1.00 25.11 ? 84  ASP F C   1 
ATOM   7855 O  O   . ASP F 1 87  ? 37.818  81.913  70.051  1.00 26.25 ? 84  ASP F O   1 
ATOM   7856 C  CB  . ASP F 1 87  ? 37.194  84.751  71.243  1.00 24.78 ? 84  ASP F CB  1 
ATOM   7857 C  CG  . ASP F 1 87  ? 36.807  86.231  71.152  1.00 24.66 ? 84  ASP F CG  1 
ATOM   7858 O  OD1 . ASP F 1 87  ? 36.129  86.619  70.166  1.00 22.33 ? 84  ASP F OD1 1 
ATOM   7859 O  OD2 . ASP F 1 87  ? 37.172  86.985  72.091  1.00 22.42 ? 84  ASP F OD2 1 
ATOM   7860 N  N   . GLY F 1 88  ? 39.678  82.688  71.016  1.00 25.38 ? 85  GLY F N   1 
ATOM   7861 C  CA  . GLY F 1 88  ? 40.021  81.372  71.534  1.00 26.11 ? 85  GLY F CA  1 
ATOM   7862 C  C   . GLY F 1 88  ? 40.852  80.520  70.590  1.00 26.95 ? 85  GLY F C   1 
ATOM   7863 O  O   . GLY F 1 88  ? 41.146  79.361  70.882  1.00 28.09 ? 85  GLY F O   1 
ATOM   7864 N  N   . LYS F 1 89  ? 41.224  81.077  69.452  1.00 26.80 ? 86  LYS F N   1 
ATOM   7865 C  CA  . LYS F 1 89  ? 42.233  80.444  68.618  1.00 27.44 ? 86  LYS F CA  1 
ATOM   7866 C  C   . LYS F 1 89  ? 43.551  80.578  69.345  1.00 27.60 ? 86  LYS F C   1 
ATOM   7867 O  O   . LYS F 1 89  ? 43.710  81.482  70.161  1.00 27.75 ? 86  LYS F O   1 
ATOM   7868 C  CB  . LYS F 1 89  ? 42.281  81.093  67.224  1.00 27.39 ? 86  LYS F CB  1 
ATOM   7869 C  CG  . LYS F 1 89  ? 41.034  80.747  66.384  1.00 26.48 ? 86  LYS F CG  1 
ATOM   7870 C  CD  . LYS F 1 89  ? 41.092  81.356  64.996  1.00 27.56 ? 86  LYS F CD  1 
ATOM   7871 C  CE  . LYS F 1 89  ? 39.746  81.207  64.296  1.00 28.44 ? 86  LYS F CE  1 
ATOM   7872 N  NZ  . LYS F 1 89  ? 39.281  79.786  64.098  1.00 28.94 ? 86  LYS F NZ  1 
ATOM   7873 N  N   . ILE F 1 90  ? 44.484  79.672  69.073  1.00 27.62 ? 87  ILE F N   1 
ATOM   7874 C  CA  . ILE F 1 90  ? 45.786  79.687  69.735  1.00 27.42 ? 87  ILE F CA  1 
ATOM   7875 C  C   . ILE F 1 90  ? 46.783  80.308  68.753  1.00 28.05 ? 87  ILE F C   1 
ATOM   7876 O  O   . ILE F 1 90  ? 46.681  80.085  67.552  1.00 28.49 ? 87  ILE F O   1 
ATOM   7877 C  CB  . ILE F 1 90  ? 46.167  78.255  70.167  1.00 27.78 ? 87  ILE F CB  1 
ATOM   7878 C  CG1 . ILE F 1 90  ? 45.047  77.675  71.060  1.00 28.37 ? 87  ILE F CG1 1 
ATOM   7879 C  CG2 . ILE F 1 90  ? 47.530  78.238  70.863  1.00 28.62 ? 87  ILE F CG2 1 
ATOM   7880 C  CD1 . ILE F 1 90  ? 45.155  76.205  71.428  1.00 27.10 ? 87  ILE F CD1 1 
ATOM   7881 N  N   . ALA F 1 91  ? 47.726  81.110  69.226  1.00 27.83 ? 88  ALA F N   1 
ATOM   7882 C  CA  . ALA F 1 91  ? 48.623  81.792  68.292  1.00 27.96 ? 88  ALA F CA  1 
ATOM   7883 C  C   . ALA F 1 91  ? 49.983  82.154  68.899  1.00 28.12 ? 88  ALA F C   1 
ATOM   7884 O  O   . ALA F 1 91  ? 50.134  82.273  70.105  1.00 27.99 ? 88  ALA F O   1 
ATOM   7885 C  CB  . ALA F 1 91  ? 47.944  83.044  67.713  1.00 27.68 ? 88  ALA F CB  1 
ATOM   7886 N  N   . CYS F 1 92  ? 50.971  82.320  68.032  1.00 27.78 ? 89  CYS F N   1 
ATOM   7887 C  CA  . CYS F 1 92  ? 52.328  82.627  68.441  1.00 27.43 ? 89  CYS F CA  1 
ATOM   7888 C  C   . CYS F 1 92  ? 52.981  83.458  67.320  1.00 26.86 ? 89  CYS F C   1 
ATOM   7889 O  O   . CYS F 1 92  ? 52.382  83.639  66.266  1.00 27.06 ? 89  CYS F O   1 
ATOM   7890 C  CB  . CYS F 1 92  ? 53.098  81.339  68.770  1.00 26.34 ? 89  CYS F CB  1 
ATOM   7891 S  SG  . CYS F 1 92  ? 53.242  80.167  67.419  1.00 27.52 ? 89  CYS F SG  1 
ATOM   7892 N  N   . ALA F 1 93  ? 54.175  83.986  67.569  1.00 26.47 ? 90  ALA F N   1 
ATOM   7893 C  CA  . ALA F 1 93  ? 54.813  84.944  66.661  1.00 26.25 ? 90  ALA F CA  1 
ATOM   7894 C  C   . ALA F 1 93  ? 56.243  84.532  66.291  1.00 25.49 ? 90  ALA F C   1 
ATOM   7895 O  O   . ALA F 1 93  ? 56.860  83.728  66.988  1.00 25.62 ? 90  ALA F O   1 
ATOM   7896 C  CB  . ALA F 1 93  ? 54.807  86.326  67.291  1.00 25.99 ? 90  ALA F CB  1 
ATOM   7897 N  N   . PHE F 1 94  ? 56.754  85.038  65.172  1.00 25.26 ? 91  PHE F N   1 
ATOM   7898 C  CA  . PHE F 1 94  ? 58.194  84.923  64.879  1.00 24.81 ? 91  PHE F CA  1 
ATOM   7899 C  C   . PHE F 1 94  ? 58.693  86.078  64.047  1.00 25.15 ? 91  PHE F C   1 
ATOM   7900 O  O   . PHE F 1 94  ? 57.906  86.719  63.350  1.00 24.46 ? 91  PHE F O   1 
ATOM   7901 C  CB  . PHE F 1 94  ? 58.563  83.589  64.242  1.00 25.07 ? 91  PHE F CB  1 
ATOM   7902 C  CG  . PHE F 1 94  ? 57.792  83.252  62.987  1.00 24.28 ? 91  PHE F CG  1 
ATOM   7903 C  CD1 . PHE F 1 94  ? 56.515  82.712  63.057  1.00 25.68 ? 91  PHE F CD1 1 
ATOM   7904 C  CD2 . PHE F 1 94  ? 58.376  83.404  61.738  1.00 24.02 ? 91  PHE F CD2 1 
ATOM   7905 C  CE1 . PHE F 1 94  ? 55.820  82.347  61.877  1.00 26.71 ? 91  PHE F CE1 1 
ATOM   7906 C  CE2 . PHE F 1 94  ? 57.694  83.038  60.576  1.00 23.26 ? 91  PHE F CE2 1 
ATOM   7907 C  CZ  . PHE F 1 94  ? 56.422  82.510  60.644  1.00 23.76 ? 91  PHE F CZ  1 
ATOM   7908 N  N   . SER F 1 95  ? 59.998  86.358  64.120  1.00 24.99 ? 92  SER F N   1 
ATOM   7909 C  CA  . SER F 1 95  ? 60.489  87.552  63.469  1.00 25.44 ? 92  SER F CA  1 
ATOM   7910 C  C   . SER F 1 95  ? 61.944  87.456  63.172  1.00 25.15 ? 92  SER F C   1 
ATOM   7911 O  O   . SER F 1 95  ? 62.708  86.954  63.980  1.00 25.03 ? 92  SER F O   1 
ATOM   7912 C  CB  . SER F 1 95  ? 60.227  88.791  64.354  1.00 25.97 ? 92  SER F CB  1 
ATOM   7913 O  OG  . SER F 1 95  ? 60.488  90.004  63.643  1.00 28.38 ? 92  SER F OG  1 
ATOM   7914 N  N   . SER F 1 96  ? 62.326  87.940  61.999  1.00 25.27 ? 93  SER F N   1 
ATOM   7915 C  CA  . SER F 1 96  ? 63.742  88.119  61.673  1.00 25.89 ? 93  SER F CA  1 
ATOM   7916 C  C   . SER F 1 96  ? 64.072  89.609  61.655  1.00 25.93 ? 93  SER F C   1 
ATOM   7917 O  O   . SER F 1 96  ? 63.325  90.389  61.073  1.00 26.65 ? 93  SER F O   1 
ATOM   7918 C  CB  . SER F 1 96  ? 64.064  87.511  60.317  1.00 25.74 ? 93  SER F CB  1 
ATOM   7919 O  OG  . SER F 1 96  ? 65.423  87.718  59.989  1.00 26.92 ? 93  SER F OG  1 
ATOM   7920 N  N   . SER F 1 97  ? 65.180  89.994  62.290  1.00 26.20 ? 94  SER F N   1 
ATOM   7921 C  CA  . SER F 1 97  ? 65.672  91.358  62.245  1.00 26.89 ? 94  SER F CA  1 
ATOM   7922 C  C   . SER F 1 97  ? 67.029  91.430  61.564  1.00 27.06 ? 94  SER F C   1 
ATOM   7923 O  O   . SER F 1 97  ? 67.615  90.403  61.191  1.00 27.04 ? 94  SER F O   1 
ATOM   7924 C  CB  . SER F 1 97  ? 65.746  91.968  63.652  1.00 27.32 ? 94  SER F CB  1 
ATOM   7925 O  OG  . SER F 1 97  ? 66.583  91.221  64.520  1.00 29.64 ? 94  SER F OG  1 
ATOM   7926 N  N   . GLY F 1 98  ? 67.529  92.655  61.417  1.00 26.88 ? 95  GLY F N   1 
ATOM   7927 C  CA  . GLY F 1 98  ? 68.816  92.904  60.792  1.00 25.68 ? 95  GLY F CA  1 
ATOM   7928 C  C   . GLY F 1 98  ? 69.987  92.554  61.682  1.00 25.31 ? 95  GLY F C   1 
ATOM   7929 O  O   . GLY F 1 98  ? 71.080  92.295  61.199  1.00 25.67 ? 95  GLY F O   1 
ATOM   7930 N  N   . GLY F 1 99  ? 69.764  92.537  62.986  1.00 24.87 ? 96  GLY F N   1 
ATOM   7931 C  CA  . GLY F 1 99  ? 70.842  92.317  63.933  1.00 24.32 ? 96  GLY F CA  1 
ATOM   7932 C  C   . GLY F 1 99  ? 70.319  91.895  65.284  1.00 24.32 ? 96  GLY F C   1 
ATOM   7933 O  O   . GLY F 1 99  ? 69.142  92.071  65.587  1.00 24.29 ? 96  GLY F O   1 
ATOM   7934 N  N   . TRP F 1 100 ? 71.196  91.293  66.077  1.00 24.40 ? 97  TRP F N   1 
ATOM   7935 C  CA  . TRP F 1 100 ? 70.918  91.003  67.472  1.00 24.07 ? 97  TRP F CA  1 
ATOM   7936 C  C   . TRP F 1 100 ? 70.923  92.343  68.197  1.00 23.35 ? 97  TRP F C   1 
ATOM   7937 O  O   . TRP F 1 100 ? 71.816  93.193  67.955  1.00 23.25 ? 97  TRP F O   1 
ATOM   7938 C  CB  . TRP F 1 100 ? 71.943  89.997  68.030  1.00 24.29 ? 97  TRP F CB  1 
ATOM   7939 C  CG  . TRP F 1 100 ? 71.783  88.636  67.352  1.00 25.42 ? 97  TRP F CG  1 
ATOM   7940 C  CD1 . TRP F 1 100 ? 72.598  88.089  66.384  1.00 25.37 ? 97  TRP F CD1 1 
ATOM   7941 C  CD2 . TRP F 1 100 ? 70.712  87.689  67.546  1.00 25.38 ? 97  TRP F CD2 1 
ATOM   7942 N  NE1 . TRP F 1 100 ? 72.109  86.865  65.983  1.00 25.33 ? 97  TRP F NE1 1 
ATOM   7943 C  CE2 . TRP F 1 100 ? 70.956  86.593  66.680  1.00 26.46 ? 97  TRP F CE2 1 
ATOM   7944 C  CE3 . TRP F 1 100 ? 69.579  87.660  68.363  1.00 26.79 ? 97  TRP F CE3 1 
ATOM   7945 C  CZ2 . TRP F 1 100 ? 70.104  85.475  66.613  1.00 25.32 ? 97  TRP F CZ2 1 
ATOM   7946 C  CZ3 . TRP F 1 100 ? 68.727  86.544  68.292  1.00 26.76 ? 97  TRP F CZ3 1 
ATOM   7947 C  CH2 . TRP F 1 100 ? 69.005  85.468  67.423  1.00 25.97 ? 97  TRP F CH2 1 
ATOM   7948 N  N   . GLY F 1 101 ? 69.905  92.540  69.038  1.00 22.58 ? 98  GLY F N   1 
ATOM   7949 C  CA  . GLY F 1 101 ? 69.647  93.816  69.717  1.00 22.38 ? 98  GLY F CA  1 
ATOM   7950 C  C   . GLY F 1 101 ? 68.827  94.740  68.837  1.00 22.30 ? 98  GLY F C   1 
ATOM   7951 O  O   . GLY F 1 101 ? 68.670  95.919  69.138  1.00 21.88 ? 98  GLY F O   1 
ATOM   7952 N  N   . GLY F 1 102 ? 68.338  94.190  67.728  1.00 22.83 ? 99  GLY F N   1 
ATOM   7953 C  CA  . GLY F 1 102 ? 67.644  94.942  66.681  1.00 23.74 ? 99  GLY F CA  1 
ATOM   7954 C  C   . GLY F 1 102 ? 66.132  94.975  66.836  1.00 24.47 ? 99  GLY F C   1 
ATOM   7955 O  O   . GLY F 1 102 ? 65.441  95.566  66.024  1.00 24.83 ? 99  GLY F O   1 
ATOM   7956 N  N   . GLY F 1 103 ? 65.618  94.313  67.865  1.00 24.73 ? 100 GLY F N   1 
ATOM   7957 C  CA  . GLY F 1 103 ? 64.222  94.408  68.197  1.00 25.18 ? 100 GLY F CA  1 
ATOM   7958 C  C   . GLY F 1 103 ? 63.335  93.281  67.728  1.00 25.97 ? 100 GLY F C   1 
ATOM   7959 O  O   . GLY F 1 103 ? 62.134  93.494  67.584  1.00 26.05 ? 100 GLY F O   1 
ATOM   7960 N  N   . ASN F 1 104 ? 63.889  92.081  67.507  1.00 26.52 ? 101 ASN F N   1 
ATOM   7961 C  CA  . ASN F 1 104 ? 63.055  90.956  67.087  1.00 26.61 ? 101 ASN F CA  1 
ATOM   7962 C  C   . ASN F 1 104 ? 62.054  90.488  68.131  1.00 26.90 ? 101 ASN F C   1 
ATOM   7963 O  O   . ASN F 1 104 ? 60.924  90.085  67.796  1.00 26.03 ? 101 ASN F O   1 
ATOM   7964 C  CB  . ASN F 1 104 ? 63.830  89.782  66.454  1.00 27.39 ? 101 ASN F CB  1 
ATOM   7965 C  CG  . ASN F 1 104 ? 65.183  89.502  67.096  1.00 29.69 ? 101 ASN F CG  1 
ATOM   7966 O  OD1 . ASN F 1 104 ? 66.143  89.183  66.378  1.00 33.71 ? 101 ASN F OD1 1 
ATOM   7967 N  ND2 . ASN F 1 104 ? 65.264  89.542  68.432  1.00 32.11 ? 101 ASN F ND2 1 
ATOM   7968 N  N   . GLU F 1 105 ? 62.460  90.575  69.395  1.00 27.53 ? 102 GLU F N   1 
ATOM   7969 C  CA  . GLU F 1 105 ? 61.558  90.269  70.503  1.00 28.30 ? 102 GLU F CA  1 
ATOM   7970 C  C   . GLU F 1 105 ? 60.464  91.332  70.627  1.00 27.61 ? 102 GLU F C   1 
ATOM   7971 O  O   . GLU F 1 105 ? 59.313  90.999  70.845  1.00 28.02 ? 102 GLU F O   1 
ATOM   7972 C  CB  . GLU F 1 105 ? 62.338  90.182  71.799  1.00 28.94 ? 102 GLU F CB  1 
ATOM   7973 C  CG  . GLU F 1 105 ? 63.414  89.096  71.835  1.00 31.47 ? 102 GLU F CG  1 
ATOM   7974 C  CD  . GLU F 1 105 ? 64.110  89.067  73.173  1.00 33.68 ? 102 GLU F CD  1 
ATOM   7975 O  OE1 . GLU F 1 105 ? 63.861  89.961  74.008  1.00 37.89 ? 102 GLU F OE1 1 
ATOM   7976 O  OE2 . GLU F 1 105 ? 64.898  88.157  73.411  1.00 34.70 ? 102 GLU F OE2 1 
ATOM   7977 N  N   . VAL F 1 106 ? 60.828  92.607  70.460  1.00 27.12 ? 103 VAL F N   1 
ATOM   7978 C  CA  . VAL F 1 106 ? 59.861  93.690  70.493  1.00 26.32 ? 103 VAL F CA  1 
ATOM   7979 C  C   . VAL F 1 106 ? 58.877  93.502  69.324  1.00 26.63 ? 103 VAL F C   1 
ATOM   7980 O  O   . VAL F 1 106 ? 57.671  93.577  69.539  1.00 27.48 ? 103 VAL F O   1 
ATOM   7981 C  CB  . VAL F 1 106 ? 60.554  95.067  70.578  1.00 26.79 ? 103 VAL F CB  1 
ATOM   7982 C  CG1 . VAL F 1 106 ? 59.560  96.210  70.570  1.00 24.93 ? 103 VAL F CG1 1 
ATOM   7983 C  CG2 . VAL F 1 106 ? 61.405  95.133  71.859  1.00 26.38 ? 103 VAL F CG2 1 
ATOM   7984 N  N   . ALA F 1 107 ? 59.370  93.151  68.136  1.00 25.51 ? 104 ALA F N   1 
ATOM   7985 C  CA  . ALA F 1 107 ? 58.498  92.862  67.015  1.00 25.55 ? 104 ALA F CA  1 
ATOM   7986 C  C   . ALA F 1 107 ? 57.539  91.715  67.312  1.00 26.09 ? 104 ALA F C   1 
ATOM   7987 O  O   . ALA F 1 107 ? 56.347  91.841  67.059  1.00 26.58 ? 104 ALA F O   1 
ATOM   7988 C  CB  . ALA F 1 107 ? 59.307  92.609  65.717  1.00 25.17 ? 104 ALA F CB  1 
ATOM   7989 N  N   . CYS F 1 108 ? 58.064  90.603  67.846  1.00 26.30 ? 105 CYS F N   1 
ATOM   7990 C  CA  . CYS F 1 108 ? 57.255  89.523  68.407  1.00 25.88 ? 105 CYS F CA  1 
ATOM   7991 C  C   . CYS F 1 108 ? 56.206  90.015  69.394  1.00 26.27 ? 105 CYS F C   1 
ATOM   7992 O  O   . CYS F 1 108 ? 55.037  89.769  69.182  1.00 26.90 ? 105 CYS F O   1 
ATOM   7993 C  CB  . CYS F 1 108 ? 58.132  88.433  69.031  1.00 25.49 ? 105 CYS F CB  1 
ATOM   7994 S  SG  . CYS F 1 108 ? 58.893  87.460  67.743  1.00 24.28 ? 105 CYS F SG  1 
HETATM 7995 N  N   . MSE F 1 109 ? 56.584  90.747  70.429  1.00 27.14 ? 106 MSE F N   1 
HETATM 7996 C  CA  . MSE F 1 109 ? 55.560  91.426  71.266  1.00 28.88 ? 106 MSE F CA  1 
HETATM 7997 C  C   . MSE F 1 109 ? 54.442  92.134  70.502  1.00 27.90 ? 106 MSE F C   1 
HETATM 7998 O  O   . MSE F 1 109 ? 53.280  92.009  70.869  1.00 27.66 ? 106 MSE F O   1 
HETATM 7999 C  CB  . MSE F 1 109 ? 56.169  92.432  72.226  1.00 29.94 ? 106 MSE F CB  1 
HETATM 8000 C  CG  . MSE F 1 109 ? 56.882  91.807  73.402  1.00 39.18 ? 106 MSE F CG  1 
HETATM 8001 SE SE  . MSE F 1 109 ? 55.861  90.495  74.518  1.00 57.97 ? 106 MSE F SE  1 
HETATM 8002 C  CE  . MSE F 1 109 ? 54.227  91.393  74.563  1.00 45.16 ? 106 MSE F CE  1 
ATOM   8003 N  N   . SER F 1 110 ? 54.794  92.877  69.454  1.00 27.05 ? 107 SER F N   1 
ATOM   8004 C  CA  . SER F 1 110 ? 53.795  93.632  68.682  1.00 26.05 ? 107 SER F CA  1 
ATOM   8005 C  C   . SER F 1 110 ? 52.836  92.722  67.908  1.00 26.17 ? 107 SER F C   1 
ATOM   8006 O  O   . SER F 1 110 ? 51.633  92.988  67.840  1.00 25.82 ? 107 SER F O   1 
ATOM   8007 C  CB  . SER F 1 110 ? 54.458  94.664  67.769  1.00 25.37 ? 107 SER F CB  1 
ATOM   8008 O  OG  . SER F 1 110 ? 54.853  94.096  66.552  1.00 21.20 ? 107 SER F OG  1 
ATOM   8009 N  N   . ILE F 1 111 ? 53.370  91.640  67.344  1.00 26.53 ? 108 ILE F N   1 
ATOM   8010 C  CA  . ILE F 1 111 ? 52.521  90.572  66.802  1.00 26.73 ? 108 ILE F CA  1 
ATOM   8011 C  C   . ILE F 1 111 ? 51.565  89.937  67.879  1.00 27.34 ? 108 ILE F C   1 
ATOM   8012 O  O   . ILE F 1 111 ? 50.356  89.830  67.664  1.00 27.41 ? 108 ILE F O   1 
ATOM   8013 C  CB  . ILE F 1 111 ? 53.348  89.489  66.077  1.00 26.78 ? 108 ILE F CB  1 
ATOM   8014 C  CG1 . ILE F 1 111 ? 54.086  90.099  64.857  1.00 25.93 ? 108 ILE F CG1 1 
ATOM   8015 C  CG2 . ILE F 1 111 ? 52.416  88.374  65.642  1.00 26.54 ? 108 ILE F CG2 1 
ATOM   8016 C  CD1 . ILE F 1 111 ? 55.421  89.412  64.470  1.00 24.82 ? 108 ILE F CD1 1 
ATOM   8017 N  N   . LEU F 1 112 ? 52.113  89.557  69.028  1.00 27.05 ? 109 LEU F N   1 
ATOM   8018 C  CA  . LEU F 1 112 ? 51.317  89.013  70.122  1.00 27.97 ? 109 LEU F CA  1 
ATOM   8019 C  C   . LEU F 1 112 ? 50.222  89.964  70.640  1.00 27.31 ? 109 LEU F C   1 
ATOM   8020 O  O   . LEU F 1 112 ? 49.178  89.528  71.042  1.00 27.48 ? 109 LEU F O   1 
ATOM   8021 C  CB  . LEU F 1 112 ? 52.220  88.537  71.275  1.00 27.43 ? 109 LEU F CB  1 
ATOM   8022 C  CG  . LEU F 1 112 ? 53.163  87.365  70.930  1.00 28.00 ? 109 LEU F CG  1 
ATOM   8023 C  CD1 . LEU F 1 112 ? 54.241  87.201  72.008  1.00 25.47 ? 109 LEU F CD1 1 
ATOM   8024 C  CD2 . LEU F 1 112 ? 52.418  86.049  70.755  1.00 26.05 ? 109 LEU F CD2 1 
ATOM   8025 N  N   . THR F 1 113 ? 50.480  91.257  70.593  1.00 26.82 ? 110 THR F N   1 
ATOM   8026 C  CA  . THR F 1 113 ? 49.525  92.280  70.965  1.00 26.43 ? 110 THR F CA  1 
ATOM   8027 C  C   . THR F 1 113 ? 48.339  92.307  70.026  1.00 27.20 ? 110 THR F C   1 
ATOM   8028 O  O   . THR F 1 113 ? 47.203  92.459  70.451  1.00 26.16 ? 110 THR F O   1 
ATOM   8029 C  CB  . THR F 1 113 ? 50.228  93.641  70.941  1.00 25.02 ? 110 THR F CB  1 
ATOM   8030 O  OG1 . THR F 1 113 ? 51.156  93.640  72.002  1.00 26.10 ? 110 THR F OG1 1 
ATOM   8031 C  CG2 . THR F 1 113 ? 49.298  94.768  71.155  1.00 23.73 ? 110 THR F CG2 1 
HETATM 8032 N  N   . MSE F 1 114 ? 48.648  92.230  68.741  1.00 28.42 ? 111 MSE F N   1 
HETATM 8033 C  CA  . MSE F 1 114 ? 47.672  92.152  67.693  1.00 31.85 ? 111 MSE F CA  1 
HETATM 8034 C  C   . MSE F 1 114 ? 46.763  90.906  67.827  1.00 29.37 ? 111 MSE F C   1 
HETATM 8035 O  O   . MSE F 1 114 ? 45.536  91.026  67.766  1.00 29.81 ? 111 MSE F O   1 
HETATM 8036 C  CB  . MSE F 1 114 ? 48.418  92.160  66.367  1.00 30.67 ? 111 MSE F CB  1 
HETATM 8037 C  CG  . MSE F 1 114 ? 47.627  92.609  65.187  1.00 33.91 ? 111 MSE F CG  1 
HETATM 8038 SE SE  . MSE F 1 114 ? 48.811  92.687  63.588  1.00 44.03 ? 111 MSE F SE  1 
HETATM 8039 C  CE  . MSE F 1 114 ? 49.565  90.767  63.580  1.00 34.62 ? 111 MSE F CE  1 
ATOM   8040 N  N   . LEU F 1 115 ? 47.366  89.734  68.011  1.00 27.85 ? 112 LEU F N   1 
ATOM   8041 C  CA  . LEU F 1 115 ? 46.644  88.482  68.178  1.00 27.19 ? 112 LEU F CA  1 
ATOM   8042 C  C   . LEU F 1 115 ? 45.788  88.491  69.415  1.00 28.50 ? 112 LEU F C   1 
ATOM   8043 O  O   . LEU F 1 115 ? 44.616  88.084  69.394  1.00 29.36 ? 112 LEU F O   1 
ATOM   8044 C  CB  . LEU F 1 115 ? 47.620  87.297  68.252  1.00 25.12 ? 112 LEU F CB  1 
ATOM   8045 C  CG  . LEU F 1 115 ? 48.489  87.124  67.007  1.00 24.03 ? 112 LEU F CG  1 
ATOM   8046 C  CD1 . LEU F 1 115 ? 49.786  86.285  67.264  1.00 18.12 ? 112 LEU F CD1 1 
ATOM   8047 C  CD2 . LEU F 1 115 ? 47.668  86.580  65.865  1.00 20.43 ? 112 LEU F CD2 1 
HETATM 8048 N  N   . MSE F 1 116 ? 46.362  88.927  70.521  1.00 29.48 ? 113 MSE F N   1 
HETATM 8049 C  CA  . MSE F 1 116 ? 45.587  89.049  71.732  1.00 33.05 ? 113 MSE F CA  1 
HETATM 8050 C  C   . MSE F 1 116 ? 44.347  89.909  71.581  1.00 29.94 ? 113 MSE F C   1 
HETATM 8051 O  O   . MSE F 1 116 ? 43.346  89.650  72.250  1.00 30.27 ? 113 MSE F O   1 
HETATM 8052 C  CB  . MSE F 1 116 ? 46.431  89.583  72.866  1.00 31.53 ? 113 MSE F CB  1 
HETATM 8053 C  CG  . MSE F 1 116 ? 47.219  88.495  73.532  1.00 35.31 ? 113 MSE F CG  1 
HETATM 8054 SE SE  . MSE F 1 116 ? 48.040  89.203  75.178  1.00 47.16 ? 113 MSE F SE  1 
HETATM 8055 C  CE  . MSE F 1 116 ? 49.480  90.394  74.370  1.00 34.32 ? 113 MSE F CE  1 
ATOM   8056 N  N   . ASN F 1 117 ? 44.413  90.919  70.720  1.00 28.09 ? 114 ASN F N   1 
ATOM   8057 C  CA  . ASN F 1 117 ? 43.297  91.820  70.502  1.00 27.55 ? 114 ASN F CA  1 
ATOM   8058 C  C   . ASN F 1 117 ? 42.072  91.111  69.942  1.00 26.76 ? 114 ASN F C   1 
ATOM   8059 O  O   . ASN F 1 117 ? 40.943  91.548  70.196  1.00 26.80 ? 114 ASN F O   1 
ATOM   8060 C  CB  . ASN F 1 117 ? 43.694  92.977  69.568  1.00 28.03 ? 114 ASN F CB  1 
ATOM   8061 C  CG  . ASN F 1 117 ? 42.878  94.230  69.811  1.00 27.95 ? 114 ASN F CG  1 
ATOM   8062 O  OD1 . ASN F 1 117 ? 41.805  94.435  69.221  1.00 30.08 ? 114 ASN F OD1 1 
ATOM   8063 N  ND2 . ASN F 1 117 ? 43.388  95.090  70.671  1.00 28.12 ? 114 ASN F ND2 1 
ATOM   8064 N  N   . PHE F 1 118 ? 42.309  90.035  69.186  1.00 25.06 ? 115 PHE F N   1 
ATOM   8065 C  CA  . PHE F 1 118 ? 41.247  89.249  68.581  1.00 24.50 ? 115 PHE F CA  1 
ATOM   8066 C  C   . PHE F 1 118 ? 40.739  88.180  69.544  1.00 24.13 ? 115 PHE F C   1 
ATOM   8067 O  O   . PHE F 1 118 ? 39.967  87.306  69.144  1.00 24.29 ? 115 PHE F O   1 
ATOM   8068 C  CB  . PHE F 1 118 ? 41.762  88.557  67.306  1.00 24.00 ? 115 PHE F CB  1 
ATOM   8069 C  CG  . PHE F 1 118 ? 41.659  89.401  66.070  1.00 24.32 ? 115 PHE F CG  1 
ATOM   8070 C  CD1 . PHE F 1 118 ? 42.695  90.284  65.720  1.00 23.31 ? 115 PHE F CD1 1 
ATOM   8071 C  CD2 . PHE F 1 118 ? 40.530  89.312  65.248  1.00 22.18 ? 115 PHE F CD2 1 
ATOM   8072 C  CE1 . PHE F 1 118 ? 42.605  91.076  64.581  1.00 20.50 ? 115 PHE F CE1 1 
ATOM   8073 C  CE2 . PHE F 1 118 ? 40.430  90.091  64.120  1.00 21.49 ? 115 PHE F CE2 1 
ATOM   8074 C  CZ  . PHE F 1 118 ? 41.478  90.976  63.778  1.00 21.63 ? 115 PHE F CZ  1 
ATOM   8075 N  N   . GLY F 1 119 ? 41.221  88.214  70.784  1.00 23.58 ? 116 GLY F N   1 
ATOM   8076 C  CA  . GLY F 1 119 ? 40.850  87.248  71.808  1.00 23.56 ? 116 GLY F CA  1 
ATOM   8077 C  C   . GLY F 1 119 ? 41.553  85.900  71.728  1.00 23.99 ? 116 GLY F C   1 
ATOM   8078 O  O   . GLY F 1 119 ? 41.080  84.910  72.325  1.00 23.93 ? 116 GLY F O   1 
ATOM   8079 N  N   . PHE F 1 120 ? 42.670  85.837  71.003  1.00 23.80 ? 117 PHE F N   1 
ATOM   8080 C  CA  . PHE F 1 120 ? 43.431  84.587  70.892  1.00 24.19 ? 117 PHE F CA  1 
ATOM   8081 C  C   . PHE F 1 120 ? 44.218  84.274  72.166  1.00 23.90 ? 117 PHE F C   1 
ATOM   8082 O  O   . PHE F 1 120 ? 44.538  85.151  72.961  1.00 23.49 ? 117 PHE F O   1 
ATOM   8083 C  CB  . PHE F 1 120 ? 44.402  84.609  69.701  1.00 24.75 ? 117 PHE F CB  1 
ATOM   8084 C  CG  . PHE F 1 120 ? 43.745  84.750  68.344  1.00 25.83 ? 117 PHE F CG  1 
ATOM   8085 C  CD1 . PHE F 1 120 ? 42.372  84.631  68.177  1.00 26.71 ? 117 PHE F CD1 1 
ATOM   8086 C  CD2 . PHE F 1 120 ? 44.530  84.962  67.211  1.00 27.80 ? 117 PHE F CD2 1 
ATOM   8087 C  CE1 . PHE F 1 120 ? 41.784  84.758  66.909  1.00 27.26 ? 117 PHE F CE1 1 
ATOM   8088 C  CE2 . PHE F 1 120 ? 43.949  85.075  65.938  1.00 26.60 ? 117 PHE F CE2 1 
ATOM   8089 C  CZ  . PHE F 1 120 ? 42.581  84.981  65.796  1.00 25.93 ? 117 PHE F CZ  1 
ATOM   8090 N  N   . LEU F 1 121 ? 44.480  82.998  72.370  1.00 24.59 ? 118 LEU F N   1 
ATOM   8091 C  CA  . LEU F 1 121 ? 45.327  82.540  73.452  1.00 25.62 ? 118 LEU F CA  1 
ATOM   8092 C  C   . LEU F 1 121 ? 46.707  82.459  72.827  1.00 25.70 ? 118 LEU F C   1 
ATOM   8093 O  O   . LEU F 1 121 ? 46.902  81.815  71.812  1.00 25.80 ? 118 LEU F O   1 
ATOM   8094 C  CB  . LEU F 1 121 ? 44.898  81.173  73.975  1.00 25.12 ? 118 LEU F CB  1 
ATOM   8095 C  CG  . LEU F 1 121 ? 43.602  80.914  74.772  1.00 26.45 ? 118 LEU F CG  1 
ATOM   8096 C  CD1 . LEU F 1 121 ? 43.911  80.825  76.231  1.00 26.86 ? 118 LEU F CD1 1 
ATOM   8097 C  CD2 . LEU F 1 121 ? 42.442  81.889  74.520  1.00 23.38 ? 118 LEU F CD2 1 
ATOM   8098 N  N   . VAL F 1 122 ? 47.664  83.108  73.468  1.00 25.97 ? 119 VAL F N   1 
ATOM   8099 C  CA  . VAL F 1 122 ? 48.898  83.478  72.827  1.00 25.29 ? 119 VAL F CA  1 
ATOM   8100 C  C   . VAL F 1 122 ? 50.014  82.994  73.738  1.00 25.57 ? 119 VAL F C   1 
ATOM   8101 O  O   . VAL F 1 122 ? 49.877  83.019  74.976  1.00 25.89 ? 119 VAL F O   1 
ATOM   8102 C  CB  . VAL F 1 122 ? 48.797  85.005  72.638  1.00 26.20 ? 119 VAL F CB  1 
ATOM   8103 C  CG1 . VAL F 1 122 ? 49.913  85.843  73.371  1.00 24.57 ? 119 VAL F CG1 1 
ATOM   8104 C  CG2 . VAL F 1 122 ? 48.443  85.370  71.192  1.00 20.56 ? 119 VAL F CG2 1 
ATOM   8105 N  N   . PHE F 1 123 ? 51.096  82.518  73.147  1.00 25.04 ? 120 PHE F N   1 
ATOM   8106 C  CA  . PHE F 1 123 ? 52.144  81.901  73.951  1.00 25.43 ? 120 PHE F CA  1 
ATOM   8107 C  C   . PHE F 1 123 ? 53.546  82.123  73.363  1.00 25.32 ? 120 PHE F C   1 
ATOM   8108 O  O   . PHE F 1 123 ? 53.706  82.431  72.184  1.00 24.89 ? 120 PHE F O   1 
ATOM   8109 C  CB  . PHE F 1 123 ? 51.863  80.384  74.102  1.00 25.08 ? 120 PHE F CB  1 
ATOM   8110 C  CG  . PHE F 1 123 ? 52.099  79.618  72.840  1.00 24.54 ? 120 PHE F CG  1 
ATOM   8111 C  CD1 . PHE F 1 123 ? 51.098  79.497  71.896  1.00 24.01 ? 120 PHE F CD1 1 
ATOM   8112 C  CD2 . PHE F 1 123 ? 53.355  79.065  72.567  1.00 26.39 ? 120 PHE F CD2 1 
ATOM   8113 C  CE1 . PHE F 1 123 ? 51.323  78.835  70.720  1.00 23.58 ? 120 PHE F CE1 1 
ATOM   8114 C  CE2 . PHE F 1 123 ? 53.611  78.382  71.363  1.00 23.70 ? 120 PHE F CE2 1 
ATOM   8115 C  CZ  . PHE F 1 123 ? 52.590  78.278  70.445  1.00 25.15 ? 120 PHE F CZ  1 
ATOM   8116 N  N   . GLY F 1 124 ? 54.559  81.933  74.201  1.00 25.68 ? 121 GLY F N   1 
ATOM   8117 C  CA  . GLY F 1 124 ? 55.943  81.760  73.723  1.00 26.07 ? 121 GLY F CA  1 
ATOM   8118 C  C   . GLY F 1 124 ? 56.453  80.401  74.179  1.00 26.55 ? 121 GLY F C   1 
ATOM   8119 O  O   . GLY F 1 124 ? 55.703  79.639  74.794  1.00 27.03 ? 121 GLY F O   1 
ATOM   8120 N  N   . VAL F 1 125 ? 57.719  80.099  73.908  1.00 27.02 ? 122 VAL F N   1 
ATOM   8121 C  CA  . VAL F 1 125 ? 58.287  78.765  74.179  1.00 27.11 ? 122 VAL F CA  1 
ATOM   8122 C  C   . VAL F 1 125 ? 59.475  78.819  75.174  1.00 27.01 ? 122 VAL F C   1 
ATOM   8123 O  O   . VAL F 1 125 ? 60.428  79.583  74.974  1.00 26.45 ? 122 VAL F O   1 
ATOM   8124 C  CB  . VAL F 1 125 ? 58.680  78.071  72.843  1.00 27.36 ? 122 VAL F CB  1 
ATOM   8125 C  CG1 . VAL F 1 125 ? 59.368  76.743  73.085  1.00 29.24 ? 122 VAL F CG1 1 
ATOM   8126 C  CG2 . VAL F 1 125 ? 57.447  77.810  71.980  1.00 26.95 ? 122 VAL F CG2 1 
ATOM   8127 N  N   . THR F 1 126 ? 59.409  78.023  76.247  1.00 26.66 ? 123 THR F N   1 
ATOM   8128 C  CA  . THR F 1 126 ? 60.488  77.999  77.260  1.00 26.18 ? 123 THR F CA  1 
ATOM   8129 C  C   . THR F 1 126 ? 61.734  77.211  76.800  1.00 26.53 ? 123 THR F C   1 
ATOM   8130 O  O   . THR F 1 126 ? 62.842  77.429  77.315  1.00 26.22 ? 123 THR F O   1 
ATOM   8131 C  CB  . THR F 1 126 ? 60.041  77.339  78.565  1.00 25.90 ? 123 THR F CB  1 
ATOM   8132 O  OG1 . THR F 1 126 ? 59.343  76.137  78.238  1.00 27.69 ? 123 THR F OG1 1 
ATOM   8133 C  CG2 . THR F 1 126 ? 59.146  78.236  79.413  1.00 23.24 ? 123 THR F CG2 1 
ATOM   8134 N  N   . ASP F 1 127 ? 61.553  76.297  75.850  1.00 26.16 ? 124 ASP F N   1 
ATOM   8135 C  CA  . ASP F 1 127 ? 62.619  75.369  75.474  1.00 27.12 ? 124 ASP F CA  1 
ATOM   8136 C  C   . ASP F 1 127 ? 63.908  76.097  75.094  1.00 27.16 ? 124 ASP F C   1 
ATOM   8137 O  O   . ASP F 1 127 ? 63.872  77.052  74.325  1.00 26.69 ? 124 ASP F O   1 
ATOM   8138 C  CB  . ASP F 1 127 ? 62.212  74.505  74.265  1.00 27.36 ? 124 ASP F CB  1 
ATOM   8139 C  CG  . ASP F 1 127 ? 60.935  73.722  74.489  1.00 27.95 ? 124 ASP F CG  1 
ATOM   8140 O  OD1 . ASP F 1 127 ? 60.171  74.033  75.426  1.00 28.17 ? 124 ASP F OD1 1 
ATOM   8141 O  OD2 . ASP F 1 127 ? 60.702  72.779  73.706  1.00 29.07 ? 124 ASP F OD2 1 
ATOM   8142 N  N   . TYR F 1 128 ? 65.036  75.630  75.632  1.00 27.12 ? 125 TYR F N   1 
ATOM   8143 C  CA  . TYR F 1 128 ? 66.341  76.011  75.111  1.00 27.13 ? 125 TYR F CA  1 
ATOM   8144 C  C   . TYR F 1 128 ? 66.770  74.999  74.071  1.00 27.47 ? 125 TYR F C   1 
ATOM   8145 O  O   . TYR F 1 128 ? 67.045  73.830  74.342  1.00 27.78 ? 125 TYR F O   1 
ATOM   8146 C  CB  . TYR F 1 128 ? 67.406  76.129  76.192  1.00 26.53 ? 125 TYR F CB  1 
ATOM   8147 C  CG  . TYR F 1 128 ? 67.431  77.465  76.898  1.00 26.80 ? 125 TYR F CG  1 
ATOM   8148 C  CD1 . TYR F 1 128 ? 66.293  77.948  77.568  1.00 26.44 ? 125 TYR F CD1 1 
ATOM   8149 C  CD2 . TYR F 1 128 ? 68.588  78.228  76.932  1.00 24.99 ? 125 TYR F CD2 1 
ATOM   8150 C  CE1 . TYR F 1 128 ? 66.318  79.142  78.236  1.00 25.98 ? 125 TYR F CE1 1 
ATOM   8151 C  CE2 . TYR F 1 128 ? 68.617  79.440  77.595  1.00 25.38 ? 125 TYR F CE2 1 
ATOM   8152 C  CZ  . TYR F 1 128 ? 67.481  79.889  78.251  1.00 25.61 ? 125 TYR F CZ  1 
ATOM   8153 O  OH  . TYR F 1 128 ? 67.500  81.088  78.922  1.00 25.55 ? 125 TYR F OH  1 
ATOM   8154 N  N   . VAL F 1 129 ? 66.830  75.504  72.867  1.00 28.11 ? 126 VAL F N   1 
ATOM   8155 C  CA  . VAL F 1 129 ? 67.109  74.740  71.698  1.00 29.10 ? 126 VAL F CA  1 
ATOM   8156 C  C   . VAL F 1 129 ? 68.640  74.749  71.483  1.00 29.94 ? 126 VAL F C   1 
ATOM   8157 O  O   . VAL F 1 129 ? 69.162  73.964  70.697  1.00 30.60 ? 126 VAL F O   1 
ATOM   8158 C  CB  . VAL F 1 129 ? 66.262  75.403  70.586  1.00 29.38 ? 126 VAL F CB  1 
ATOM   8159 C  CG1 . VAL F 1 129 ? 67.090  76.041  69.506  1.00 27.70 ? 126 VAL F CG1 1 
ATOM   8160 C  CG2 . VAL F 1 129 ? 65.127  74.491  70.129  1.00 28.92 ? 126 VAL F CG2 1 
ATOM   8161 N  N   . GLY F 1 130 ? 69.329  75.633  72.221  1.00 30.61 ? 127 GLY F N   1 
ATOM   8162 C  CA  . GLY F 1 130 ? 70.793  75.761  72.268  1.00 31.48 ? 127 GLY F CA  1 
ATOM   8163 C  C   . GLY F 1 130 ? 71.259  76.116  73.685  1.00 32.37 ? 127 GLY F C   1 
ATOM   8164 O  O   . GLY F 1 130 ? 70.435  76.391  74.554  1.00 32.42 ? 127 GLY F O   1 
ATOM   8165 N  N   . LYS F 1 131 ? 72.570  76.111  73.941  1.00 32.86 ? 128 LYS F N   1 
ATOM   8166 C  CA  . LYS F 1 131 ? 73.090  76.518  75.264  1.00 33.49 ? 128 LYS F CA  1 
ATOM   8167 C  C   . LYS F 1 131 ? 72.649  77.948  75.682  1.00 33.35 ? 128 LYS F C   1 
ATOM   8168 O  O   . LYS F 1 131 ? 72.468  78.249  76.879  1.00 33.64 ? 128 LYS F O   1 
ATOM   8169 C  CB  . LYS F 1 131 ? 74.617  76.421  75.301  1.00 33.75 ? 128 LYS F CB  1 
ATOM   8170 C  CG  . LYS F 1 131 ? 75.180  76.102  76.681  1.00 35.81 ? 128 LYS F CG  1 
ATOM   8171 C  CD  . LYS F 1 131 ? 76.502  76.824  76.934  1.00 38.85 ? 128 LYS F CD  1 
ATOM   8172 C  CE  . LYS F 1 131 ? 77.331  76.125  78.028  1.00 40.84 ? 128 LYS F CE  1 
ATOM   8173 N  NZ  . LYS F 1 131 ? 78.086  74.918  77.532  1.00 39.83 ? 128 LYS F NZ  1 
ATOM   8174 N  N   . LYS F 1 132 ? 72.496  78.818  74.690  1.00 32.52 ? 129 LYS F N   1 
ATOM   8175 C  CA  . LYS F 1 132 ? 72.203  80.221  74.917  1.00 32.39 ? 129 LYS F CA  1 
ATOM   8176 C  C   . LYS F 1 132 ? 71.201  80.696  73.874  1.00 31.11 ? 129 LYS F C   1 
ATOM   8177 O  O   . LYS F 1 132 ? 71.278  81.824  73.409  1.00 30.78 ? 129 LYS F O   1 
ATOM   8178 C  CB  . LYS F 1 132 ? 73.490  81.054  74.842  1.00 31.99 ? 129 LYS F CB  1 
ATOM   8179 C  CG  . LYS F 1 132 ? 74.266  81.125  76.146  1.00 33.60 ? 129 LYS F CG  1 
ATOM   8180 C  CD  . LYS F 1 132 ? 75.440  82.120  76.039  1.00 34.60 ? 129 LYS F CD  1 
ATOM   8181 C  CE  . LYS F 1 132 ? 76.654  81.712  76.896  1.00 38.34 ? 129 LYS F CE  1 
ATOM   8182 N  NZ  . LYS F 1 132 ? 76.350  81.571  78.354  1.00 39.67 ? 129 LYS F NZ  1 
ATOM   8183 N  N   . PHE F 1 133 ? 70.267  79.822  73.507  1.00 29.96 ? 130 PHE F N   1 
ATOM   8184 C  CA  . PHE F 1 133 ? 69.327  80.127  72.452  1.00 29.03 ? 130 PHE F CA  1 
ATOM   8185 C  C   . PHE F 1 133 ? 67.951  79.568  72.791  1.00 29.13 ? 130 PHE F C   1 
ATOM   8186 O  O   . PHE F 1 133 ? 67.769  78.359  72.934  1.00 28.45 ? 130 PHE F O   1 
ATOM   8187 C  CB  . PHE F 1 133 ? 69.819  79.589  71.100  1.00 28.75 ? 130 PHE F CB  1 
ATOM   8188 C  CG  . PHE F 1 133 ? 69.295  80.346  69.928  1.00 27.56 ? 130 PHE F CG  1 
ATOM   8189 C  CD1 . PHE F 1 133 ? 68.114  79.954  69.303  1.00 25.73 ? 130 PHE F CD1 1 
ATOM   8190 C  CD2 . PHE F 1 133 ? 69.967  81.474  69.458  1.00 28.02 ? 130 PHE F CD2 1 
ATOM   8191 C  CE1 . PHE F 1 133 ? 67.594  80.674  68.236  1.00 26.23 ? 130 PHE F CE1 1 
ATOM   8192 C  CE2 . PHE F 1 133 ? 69.467  82.197  68.375  1.00 27.72 ? 130 PHE F CE2 1 
ATOM   8193 C  CZ  . PHE F 1 133 ? 68.267  81.792  67.765  1.00 28.24 ? 130 PHE F CZ  1 
ATOM   8194 N  N   . THR F 1 134 ? 66.987  80.478  72.915  1.00 28.96 ? 131 THR F N   1 
ATOM   8195 C  CA  . THR F 1 134 ? 65.607  80.121  73.225  1.00 28.60 ? 131 THR F CA  1 
ATOM   8196 C  C   . THR F 1 134 ? 64.624  80.966  72.376  1.00 28.39 ? 131 THR F C   1 
ATOM   8197 O  O   . THR F 1 134 ? 65.005  81.505  71.331  1.00 28.49 ? 131 THR F O   1 
ATOM   8198 C  CB  . THR F 1 134 ? 65.337  80.174  74.748  1.00 28.51 ? 131 THR F CB  1 
ATOM   8199 O  OG1 . THR F 1 134 ? 63.991  79.796  75.017  1.00 28.80 ? 131 THR F OG1 1 
ATOM   8200 C  CG2 . THR F 1 134 ? 65.597  81.550  75.324  1.00 27.82 ? 131 THR F CG2 1 
ATOM   8201 N  N   . LEU F 1 135 ? 63.370  81.048  72.796  1.00 27.60 ? 132 LEU F N   1 
ATOM   8202 C  CA  . LEU F 1 135 ? 62.310  81.618  71.974  1.00 27.13 ? 132 LEU F CA  1 
ATOM   8203 C  C   . LEU F 1 135 ? 61.103  81.968  72.848  1.00 27.75 ? 132 LEU F C   1 
ATOM   8204 O  O   . LEU F 1 135 ? 59.951  81.640  72.503  1.00 28.21 ? 132 LEU F O   1 
ATOM   8205 C  CB  . LEU F 1 135 ? 61.920  80.660  70.834  1.00 26.57 ? 132 LEU F CB  1 
ATOM   8206 C  CG  . LEU F 1 135 ? 61.585  79.168  71.048  1.00 26.24 ? 132 LEU F CG  1 
ATOM   8207 C  CD1 . LEU F 1 135 ? 60.551  78.731  70.028  1.00 25.03 ? 132 LEU F CD1 1 
ATOM   8208 C  CD2 . LEU F 1 135 ? 62.801  78.231  70.983  1.00 22.69 ? 132 LEU F CD2 1 
ATOM   8209 N  N   . HIS F 1 136 ? 61.371  82.651  73.972  1.00 27.30 ? 133 HIS F N   1 
ATOM   8210 C  CA  . HIS F 1 136 ? 60.349  82.911  74.971  1.00 27.23 ? 133 HIS F CA  1 
ATOM   8211 C  C   . HIS F 1 136 ? 59.090  83.662  74.505  1.00 27.41 ? 133 HIS F C   1 
ATOM   8212 O  O   . HIS F 1 136 ? 58.021  83.432  75.051  1.00 27.44 ? 133 HIS F O   1 
ATOM   8213 C  CB  . HIS F 1 136 ? 60.939  83.588  76.214  1.00 26.91 ? 133 HIS F CB  1 
ATOM   8214 C  CG  . HIS F 1 136 ? 61.930  82.746  76.973  1.00 26.47 ? 133 HIS F CG  1 
ATOM   8215 N  ND1 . HIS F 1 136 ? 62.113  81.392  76.748  1.00 24.80 ? 133 HIS F ND1 1 
ATOM   8216 C  CD2 . HIS F 1 136 ? 62.792  83.082  77.970  1.00 23.49 ? 133 HIS F CD2 1 
ATOM   8217 C  CE1 . HIS F 1 136 ? 63.046  80.940  77.571  1.00 24.00 ? 133 HIS F CE1 1 
ATOM   8218 N  NE2 . HIS F 1 136 ? 63.474  81.947  78.320  1.00 20.90 ? 133 HIS F NE2 1 
ATOM   8219 N  N   . TYR F 1 137 ? 59.234  84.549  73.515  1.00 27.62 ? 134 TYR F N   1 
ATOM   8220 C  CA  . TYR F 1 137 ? 58.169  85.455  73.038  1.00 27.02 ? 134 TYR F CA  1 
ATOM   8221 C  C   . TYR F 1 137 ? 57.864  85.142  71.585  1.00 26.63 ? 134 TYR F C   1 
ATOM   8222 O  O   . TYR F 1 137 ? 56.997  85.746  70.968  1.00 26.76 ? 134 TYR F O   1 
ATOM   8223 C  CB  . TYR F 1 137 ? 58.579  86.934  73.274  1.00 26.52 ? 134 TYR F CB  1 
ATOM   8224 C  CG  . TYR F 1 137 ? 58.711  87.107  74.756  1.00 26.94 ? 134 TYR F CG  1 
ATOM   8225 C  CD1 . TYR F 1 137 ? 59.953  87.195  75.376  1.00 27.93 ? 134 TYR F CD1 1 
ATOM   8226 C  CD2 . TYR F 1 137 ? 57.587  87.035  75.555  1.00 26.46 ? 134 TYR F CD2 1 
ATOM   8227 C  CE1 . TYR F 1 137 ? 60.049  87.265  76.791  1.00 28.31 ? 134 TYR F CE1 1 
ATOM   8228 C  CE2 . TYR F 1 137 ? 57.668  87.085  76.945  1.00 27.91 ? 134 TYR F CE2 1 
ATOM   8229 C  CZ  . TYR F 1 137 ? 58.893  87.204  77.558  1.00 27.39 ? 134 TYR F CZ  1 
ATOM   8230 O  OH  . TYR F 1 137 ? 58.921  87.239  78.949  1.00 29.17 ? 134 TYR F OH  1 
ATOM   8231 N  N   . GLY F 1 138 ? 58.595  84.168  71.051  1.00 26.49 ? 135 GLY F N   1 
ATOM   8232 C  CA  . GLY F 1 138 ? 58.469  83.763  69.652  1.00 25.71 ? 135 GLY F CA  1 
ATOM   8233 C  C   . GLY F 1 138 ? 59.828  83.393  69.140  1.00 25.55 ? 135 GLY F C   1 
ATOM   8234 O  O   . GLY F 1 138 ? 60.837  83.700  69.768  1.00 25.89 ? 135 GLY F O   1 
ATOM   8235 N  N   . ALA F 1 139 ? 59.870  82.699  68.010  1.00 26.03 ? 136 ALA F N   1 
ATOM   8236 C  CA  . ALA F 1 139 ? 61.141  82.450  67.327  1.00 25.38 ? 136 ALA F CA  1 
ATOM   8237 C  C   . ALA F 1 139 ? 61.728  83.743  66.769  1.00 25.32 ? 136 ALA F C   1 
ATOM   8238 O  O   . ALA F 1 139 ? 61.037  84.528  66.103  1.00 25.24 ? 136 ALA F O   1 
ATOM   8239 C  CB  . ALA F 1 139 ? 60.978  81.396  66.251  1.00 25.14 ? 136 ALA F CB  1 
ATOM   8240 N  N   . VAL F 1 140 ? 63.003  83.979  67.075  1.00 26.01 ? 137 VAL F N   1 
ATOM   8241 C  CA  . VAL F 1 140 ? 63.699  85.196  66.629  1.00 26.38 ? 137 VAL F CA  1 
ATOM   8242 C  C   . VAL F 1 140 ? 65.083  84.830  66.087  1.00 27.66 ? 137 VAL F C   1 
ATOM   8243 O  O   . VAL F 1 140 ? 65.735  83.895  66.580  1.00 28.69 ? 137 VAL F O   1 
ATOM   8244 C  CB  . VAL F 1 140 ? 63.807  86.247  67.750  1.00 26.02 ? 137 VAL F CB  1 
ATOM   8245 C  CG1 . VAL F 1 140 ? 62.440  86.811  68.063  1.00 25.10 ? 137 VAL F CG1 1 
ATOM   8246 C  CG2 . VAL F 1 140 ? 64.446  85.642  69.003  1.00 25.68 ? 137 VAL F CG2 1 
ATOM   8247 N  N   . VAL F 1 141 ? 65.500  85.530  65.044  1.00 27.67 ? 138 VAL F N   1 
ATOM   8248 C  CA  . VAL F 1 141 ? 66.742  85.239  64.346  1.00 28.48 ? 138 VAL F CA  1 
ATOM   8249 C  C   . VAL F 1 141 ? 67.241  86.571  63.801  1.00 28.22 ? 138 VAL F C   1 
ATOM   8250 O  O   . VAL F 1 141 ? 66.426  87.443  63.514  1.00 28.70 ? 138 VAL F O   1 
ATOM   8251 C  CB  . VAL F 1 141 ? 66.515  84.211  63.191  1.00 28.91 ? 138 VAL F CB  1 
ATOM   8252 C  CG1 . VAL F 1 141 ? 67.789  84.016  62.366  1.00 29.52 ? 138 VAL F CG1 1 
ATOM   8253 C  CG2 . VAL F 1 141 ? 66.073  82.854  63.748  1.00 28.83 ? 138 VAL F CG2 1 
ATOM   8254 N  N   . ALA F 1 142 ? 68.556  86.765  63.716  1.00 27.69 ? 139 ALA F N   1 
ATOM   8255 C  CA  . ALA F 1 142 ? 69.079  87.909  62.974  1.00 28.08 ? 139 ALA F CA  1 
ATOM   8256 C  C   . ALA F 1 142 ? 69.470  87.414  61.585  1.00 28.59 ? 139 ALA F C   1 
ATOM   8257 O  O   . ALA F 1 142 ? 70.223  86.459  61.453  1.00 29.18 ? 139 ALA F O   1 
ATOM   8258 C  CB  . ALA F 1 142 ? 70.253  88.551  63.675  1.00 27.36 ? 139 ALA F CB  1 
ATOM   8259 N  N   . GLY F 1 143 ? 68.939  88.045  60.554  1.00 28.83 ? 140 GLY F N   1 
ATOM   8260 C  CA  . GLY F 1 143 ? 69.088  87.535  59.207  1.00 29.79 ? 140 GLY F CA  1 
ATOM   8261 C  C   . GLY F 1 143 ? 68.370  86.216  58.978  1.00 30.49 ? 140 GLY F C   1 
ATOM   8262 O  O   . GLY F 1 143 ? 67.281  85.973  59.484  1.00 30.13 ? 140 GLY F O   1 
ATOM   8263 N  N   . GLU F 1 144 ? 69.016  85.366  58.197  1.00 31.88 ? 141 GLU F N   1 
ATOM   8264 C  CA  . GLU F 1 144 ? 68.505  84.067  57.787  1.00 33.49 ? 141 GLU F CA  1 
ATOM   8265 C  C   . GLU F 1 144 ? 68.757  83.016  58.883  1.00 33.19 ? 141 GLU F C   1 
ATOM   8266 O  O   . GLU F 1 144 ? 69.814  83.030  59.509  1.00 32.98 ? 141 GLU F O   1 
ATOM   8267 C  CB  . GLU F 1 144 ? 69.233  83.694  56.484  1.00 33.59 ? 141 GLU F CB  1 
ATOM   8268 C  CG  . GLU F 1 144 ? 68.759  82.451  55.751  1.00 35.04 ? 141 GLU F CG  1 
ATOM   8269 C  CD  . GLU F 1 144 ? 69.806  81.950  54.762  1.00 36.19 ? 141 GLU F CD  1 
ATOM   8270 O  OE1 . GLU F 1 144 ? 70.277  80.800  54.928  1.00 40.87 ? 141 GLU F OE1 1 
ATOM   8271 O  OE2 . GLU F 1 144 ? 70.180  82.709  53.827  1.00 39.36 ? 141 GLU F OE2 1 
ATOM   8272 N  N   . PRO F 1 145 ? 67.786  82.111  59.129  1.00 33.80 ? 142 PRO F N   1 
ATOM   8273 C  CA  . PRO F 1 145 ? 68.063  80.976  60.023  1.00 34.33 ? 142 PRO F CA  1 
ATOM   8274 C  C   . PRO F 1 145 ? 69.071  80.019  59.389  1.00 35.31 ? 142 PRO F C   1 
ATOM   8275 O  O   . PRO F 1 145 ? 68.788  79.371  58.378  1.00 35.23 ? 142 PRO F O   1 
ATOM   8276 C  CB  . PRO F 1 145 ? 66.692  80.315  60.233  1.00 34.02 ? 142 PRO F CB  1 
ATOM   8277 C  CG  . PRO F 1 145 ? 65.803  80.879  59.269  1.00 33.14 ? 142 PRO F CG  1 
ATOM   8278 C  CD  . PRO F 1 145 ? 66.409  82.089  58.610  1.00 33.70 ? 142 PRO F CD  1 
ATOM   8279 N  N   . ARG F 1 146 ? 70.260  79.967  59.979  1.00 36.59 ? 143 ARG F N   1 
ATOM   8280 C  CA  . ARG F 1 146 ? 71.404  79.341  59.341  1.00 37.54 ? 143 ARG F CA  1 
ATOM   8281 C  C   . ARG F 1 146 ? 72.069  78.308  60.223  1.00 36.85 ? 143 ARG F C   1 
ATOM   8282 O  O   . ARG F 1 146 ? 72.375  77.208  59.744  1.00 36.75 ? 143 ARG F O   1 
ATOM   8283 C  CB  . ARG F 1 146 ? 72.411  80.396  58.889  1.00 37.56 ? 143 ARG F CB  1 
ATOM   8284 C  CG  . ARG F 1 146 ? 72.036  81.033  57.553  1.00 40.23 ? 143 ARG F CG  1 
ATOM   8285 C  CD  . ARG F 1 146 ? 73.106  82.013  57.051  1.00 40.50 ? 143 ARG F CD  1 
ATOM   8286 N  NE  . ARG F 1 146 ? 73.306  81.922  55.599  1.00 45.87 ? 143 ARG F NE  1 
ATOM   8287 C  CZ  . ARG F 1 146 ? 73.861  80.876  54.976  1.00 47.50 ? 143 ARG F CZ  1 
ATOM   8288 N  NH1 . ARG F 1 146 ? 74.015  80.882  53.647  1.00 46.72 ? 143 ARG F NH1 1 
ATOM   8289 N  NH2 . ARG F 1 146 ? 74.251  79.813  55.680  1.00 48.10 ? 143 ARG F NH2 1 
ATOM   8290 N  N   . SER F 1 147 ? 72.302  78.651  61.497  1.00 36.31 ? 144 SER F N   1 
ATOM   8291 C  CA  . SER F 1 147 ? 72.837  77.661  62.446  1.00 35.58 ? 144 SER F CA  1 
ATOM   8292 C  C   . SER F 1 147 ? 71.757  76.636  62.752  1.00 35.27 ? 144 SER F C   1 
ATOM   8293 O  O   . SER F 1 147 ? 70.578  76.853  62.456  1.00 35.20 ? 144 SER F O   1 
ATOM   8294 C  CB  . SER F 1 147 ? 73.396  78.297  63.721  1.00 35.18 ? 144 SER F CB  1 
ATOM   8295 O  OG  . SER F 1 147 ? 72.387  78.943  64.472  1.00 35.62 ? 144 SER F OG  1 
ATOM   8296 N  N   . GLU F 1 148 ? 72.153  75.499  63.307  1.00 35.50 ? 145 GLU F N   1 
ATOM   8297 C  CA  . GLU F 1 148 ? 71.168  74.496  63.673  1.00 36.01 ? 145 GLU F CA  1 
ATOM   8298 C  C   . GLU F 1 148 ? 70.268  74.956  64.837  1.00 35.49 ? 145 GLU F C   1 
ATOM   8299 O  O   . GLU F 1 148 ? 69.069  74.705  64.796  1.00 35.61 ? 145 GLU F O   1 
ATOM   8300 C  CB  . GLU F 1 148 ? 71.801  73.102  63.820  1.00 36.59 ? 145 GLU F CB  1 
ATOM   8301 C  CG  . GLU F 1 148 ? 71.909  72.363  62.419  1.00 39.89 ? 145 GLU F CG  1 
ATOM   8302 C  CD  . GLU F 1 148 ? 73.191  71.503  62.235  1.00 44.36 ? 145 GLU F CD  1 
ATOM   8303 O  OE1 . GLU F 1 148 ? 73.342  70.843  61.167  1.00 44.08 ? 145 GLU F OE1 1 
ATOM   8304 O  OE2 . GLU F 1 148 ? 74.052  71.486  63.154  1.00 46.71 ? 145 GLU F OE2 1 
ATOM   8305 N  N   . GLU F 1 149 ? 70.832  75.695  65.802  1.00 34.85 ? 146 GLU F N   1 
ATOM   8306 C  CA  . GLU F 1 149 ? 70.065  76.435  66.841  1.00 34.87 ? 146 GLU F CA  1 
ATOM   8307 C  C   . GLU F 1 149 ? 68.881  77.213  66.270  1.00 33.77 ? 146 GLU F C   1 
ATOM   8308 O  O   . GLU F 1 149 ? 67.763  77.042  66.715  1.00 33.17 ? 146 GLU F O   1 
ATOM   8309 C  CB  . GLU F 1 149 ? 70.948  77.468  67.533  1.00 34.37 ? 146 GLU F CB  1 
ATOM   8310 C  CG  . GLU F 1 149 ? 71.828  76.980  68.633  1.00 36.17 ? 146 GLU F CG  1 
ATOM   8311 C  CD  . GLU F 1 149 ? 72.514  78.140  69.362  1.00 37.10 ? 146 GLU F CD  1 
ATOM   8312 O  OE1 . GLU F 1 149 ? 72.911  79.143  68.714  1.00 39.47 ? 146 GLU F OE1 1 
ATOM   8313 O  OE2 . GLU F 1 149 ? 72.648  78.054  70.601  1.00 41.23 ? 146 GLU F OE2 1 
ATOM   8314 N  N   . GLU F 1 150 ? 69.158  78.083  65.291  1.00 33.07 ? 147 GLU F N   1 
ATOM   8315 C  CA  . GLU F 1 150 ? 68.153  78.940  64.657  1.00 31.98 ? 147 GLU F CA  1 
ATOM   8316 C  C   . GLU F 1 150 ? 67.092  78.139  63.910  1.00 31.07 ? 147 GLU F C   1 
ATOM   8317 O  O   . GLU F 1 150 ? 65.889  78.407  64.018  1.00 30.88 ? 147 GLU F O   1 
ATOM   8318 C  CB  . GLU F 1 150 ? 68.836  79.908  63.699  1.00 31.93 ? 147 GLU F CB  1 
ATOM   8319 C  CG  . GLU F 1 150 ? 69.437  81.096  64.413  1.00 32.83 ? 147 GLU F CG  1 
ATOM   8320 C  CD  . GLU F 1 150 ? 70.695  81.659  63.742  1.00 34.79 ? 147 GLU F CD  1 
ATOM   8321 O  OE1 . GLU F 1 150 ? 70.993  81.316  62.569  1.00 35.64 ? 147 GLU F OE1 1 
ATOM   8322 O  OE2 . GLU F 1 150 ? 71.387  82.458  64.412  1.00 34.71 ? 147 GLU F OE2 1 
ATOM   8323 N  N   . LYS F 1 151 ? 67.541  77.140  63.168  1.00 30.08 ? 148 LYS F N   1 
ATOM   8324 C  CA  . LYS F 1 151 ? 66.623  76.274  62.450  1.00 29.01 ? 148 LYS F CA  1 
ATOM   8325 C  C   . LYS F 1 151 ? 65.710  75.541  63.443  1.00 28.46 ? 148 LYS F C   1 
ATOM   8326 O  O   . LYS F 1 151 ? 64.495  75.465  63.250  1.00 28.62 ? 148 LYS F O   1 
ATOM   8327 C  CB  . LYS F 1 151 ? 67.404  75.321  61.539  1.00 29.10 ? 148 LYS F CB  1 
ATOM   8328 C  CG  . LYS F 1 151 ? 68.024  76.023  60.315  1.00 29.46 ? 148 LYS F CG  1 
ATOM   8329 C  CD  . LYS F 1 151 ? 68.905  75.101  59.479  1.00 28.55 ? 148 LYS F CD  1 
ATOM   8330 C  CE  . LYS F 1 151 ? 69.013  75.637  58.051  1.00 29.73 ? 148 LYS F CE  1 
ATOM   8331 N  NZ  . LYS F 1 151 ? 69.509  74.625  57.036  1.00 29.54 ? 148 LYS F NZ  1 
ATOM   8332 N  N   . GLU F 1 152 ? 66.278  75.048  64.535  1.00 27.74 ? 149 GLU F N   1 
ATOM   8333 C  CA  . GLU F 1 152 ? 65.496  74.271  65.479  1.00 27.68 ? 149 GLU F CA  1 
ATOM   8334 C  C   . GLU F 1 152 ? 64.520  75.109  66.296  1.00 27.62 ? 149 GLU F C   1 
ATOM   8335 O  O   . GLU F 1 152 ? 63.478  74.603  66.743  1.00 28.34 ? 149 GLU F O   1 
ATOM   8336 C  CB  . GLU F 1 152 ? 66.403  73.483  66.406  1.00 27.40 ? 149 GLU F CB  1 
ATOM   8337 C  CG  . GLU F 1 152 ? 65.675  72.483  67.286  1.00 29.66 ? 149 GLU F CG  1 
ATOM   8338 C  CD  . GLU F 1 152 ? 64.920  71.399  66.519  1.00 31.72 ? 149 GLU F CD  1 
ATOM   8339 O  OE1 . GLU F 1 152 ? 63.929  70.870  67.074  1.00 30.93 ? 149 GLU F OE1 1 
ATOM   8340 O  OE2 . GLU F 1 152 ? 65.307  71.081  65.366  1.00 34.87 ? 149 GLU F OE2 1 
ATOM   8341 N  N   . ALA F 1 153 ? 64.867  76.372  66.515  1.00 26.97 ? 150 ALA F N   1 
ATOM   8342 C  CA  . ALA F 1 153 ? 63.997  77.287  67.237  1.00 26.91 ? 150 ALA F CA  1 
ATOM   8343 C  C   . ALA F 1 153 ? 62.728  77.585  66.465  1.00 26.28 ? 150 ALA F C   1 
ATOM   8344 O  O   . ALA F 1 153 ? 61.662  77.702  67.057  1.00 27.08 ? 150 ALA F O   1 
ATOM   8345 C  CB  . ALA F 1 153 ? 64.728  78.560  67.567  1.00 26.98 ? 150 ALA F CB  1 
ATOM   8346 N  N   . CYS F 1 154 ? 62.856  77.709  65.152  1.00 26.20 ? 151 CYS F N   1 
ATOM   8347 C  CA  . CYS F 1 154 ? 61.721  77.813  64.244  1.00 26.84 ? 151 CYS F CA  1 
ATOM   8348 C  C   . CYS F 1 154 ? 60.839  76.573  64.263  1.00 26.74 ? 151 CYS F C   1 
ATOM   8349 O  O   . CYS F 1 154 ? 59.627  76.651  64.420  1.00 27.15 ? 151 CYS F O   1 
ATOM   8350 C  CB  . CYS F 1 154 ? 62.237  77.991  62.823  1.00 26.86 ? 151 CYS F CB  1 
ATOM   8351 S  SG  . CYS F 1 154 ? 62.978  79.570  62.564  1.00 28.14 ? 151 CYS F SG  1 
ATOM   8352 N  N   . ARG F 1 155 ? 61.462  75.422  64.052  1.00 27.44 ? 152 ARG F N   1 
ATOM   8353 C  CA  . ARG F 1 155 ? 60.770  74.156  64.083  1.00 26.95 ? 152 ARG F CA  1 
ATOM   8354 C  C   . ARG F 1 155 ? 60.070  73.959  65.433  1.00 27.12 ? 152 ARG F C   1 
ATOM   8355 O  O   . ARG F 1 155 ? 58.930  73.471  65.474  1.00 27.56 ? 152 ARG F O   1 
ATOM   8356 C  CB  . ARG F 1 155 ? 61.752  73.032  63.845  1.00 27.15 ? 152 ARG F CB  1 
ATOM   8357 C  CG  . ARG F 1 155 ? 62.426  72.989  62.496  1.00 26.54 ? 152 ARG F CG  1 
ATOM   8358 C  CD  . ARG F 1 155 ? 63.149  71.655  62.413  1.00 25.46 ? 152 ARG F CD  1 
ATOM   8359 N  NE  . ARG F 1 155 ? 64.023  71.550  61.260  1.00 25.72 ? 152 ARG F NE  1 
ATOM   8360 C  CZ  . ARG F 1 155 ? 65.351  71.698  61.281  1.00 23.98 ? 152 ARG F CZ  1 
ATOM   8361 N  NH1 . ARG F 1 155 ? 66.005  71.968  62.417  1.00 20.13 ? 152 ARG F NH1 1 
ATOM   8362 N  NH2 . ARG F 1 155 ? 66.022  71.574  60.140  1.00 21.93 ? 152 ARG F NH2 1 
ATOM   8363 N  N   . ARG F 1 156 ? 60.736  74.331  66.531  1.00 26.57 ? 153 ARG F N   1 
ATOM   8364 C  CA  . ARG F 1 156 ? 60.148  74.147  67.863  1.00 26.63 ? 153 ARG F CA  1 
ATOM   8365 C  C   . ARG F 1 156 ? 58.901  74.992  68.123  1.00 27.03 ? 153 ARG F C   1 
ATOM   8366 O  O   . ARG F 1 156 ? 57.977  74.530  68.806  1.00 27.90 ? 153 ARG F O   1 
ATOM   8367 C  CB  . ARG F 1 156 ? 61.173  74.350  68.988  1.00 26.57 ? 153 ARG F CB  1 
ATOM   8368 C  CG  . ARG F 1 156 ? 60.687  73.876  70.368  1.00 24.79 ? 153 ARG F CG  1 
ATOM   8369 C  CD  . ARG F 1 156 ? 60.591  72.351  70.482  1.00 24.19 ? 153 ARG F CD  1 
ATOM   8370 N  NE  . ARG F 1 156 ? 61.794  71.697  69.952  1.00 24.68 ? 153 ARG F NE  1 
ATOM   8371 C  CZ  . ARG F 1 156 ? 62.900  71.449  70.656  1.00 22.85 ? 153 ARG F CZ  1 
ATOM   8372 N  NH1 . ARG F 1 156 ? 63.947  70.901  70.065  1.00 21.89 ? 153 ARG F NH1 1 
ATOM   8373 N  NH2 . ARG F 1 156 ? 62.976  71.768  71.938  1.00 21.15 ? 153 ARG F NH2 1 
ATOM   8374 N  N   . LEU F 1 157 ? 58.880  76.224  67.613  1.00 27.09 ? 154 LEU F N   1 
ATOM   8375 C  CA  . LEU F 1 157 ? 57.663  77.044  67.643  1.00 27.22 ? 154 LEU F CA  1 
ATOM   8376 C  C   . LEU F 1 157 ? 56.453  76.328  66.992  1.00 27.83 ? 154 LEU F C   1 
ATOM   8377 O  O   . LEU F 1 157 ? 55.385  76.239  67.589  1.00 28.08 ? 154 LEU F O   1 
ATOM   8378 C  CB  . LEU F 1 157 ? 57.919  78.415  66.994  1.00 27.02 ? 154 LEU F CB  1 
ATOM   8379 C  CG  . LEU F 1 157 ? 56.835  79.502  67.143  1.00 24.70 ? 154 LEU F CG  1 
ATOM   8380 C  CD1 . LEU F 1 157 ? 56.748  80.108  68.513  1.00 21.32 ? 154 LEU F CD1 1 
ATOM   8381 C  CD2 . LEU F 1 157 ? 57.050  80.571  66.117  1.00 24.57 ? 154 LEU F CD2 1 
ATOM   8382 N  N   . GLY F 1 158 ? 56.643  75.788  65.791  1.00 28.13 ? 155 GLY F N   1 
ATOM   8383 C  CA  . GLY F 1 158 ? 55.591  75.052  65.078  1.00 28.10 ? 155 GLY F CA  1 
ATOM   8384 C  C   . GLY F 1 158 ? 55.197  73.808  65.842  1.00 29.05 ? 155 GLY F C   1 
ATOM   8385 O  O   . GLY F 1 158 ? 54.002  73.531  66.022  1.00 29.25 ? 155 GLY F O   1 
ATOM   8386 N  N   . ARG F 1 159 ? 56.201  73.074  66.331  1.00 28.75 ? 156 ARG F N   1 
ATOM   8387 C  CA  . ARG F 1 159 ? 55.952  71.917  67.153  1.00 28.63 ? 156 ARG F CA  1 
ATOM   8388 C  C   . ARG F 1 159 ? 55.067  72.264  68.319  1.00 28.29 ? 156 ARG F C   1 
ATOM   8389 O  O   . ARG F 1 159 ? 54.041  71.633  68.520  1.00 28.12 ? 156 ARG F O   1 
ATOM   8390 C  CB  . ARG F 1 159 ? 57.256  71.327  67.689  1.00 29.27 ? 156 ARG F CB  1 
ATOM   8391 C  CG  . ARG F 1 159 ? 57.344  69.821  67.584  1.00 29.29 ? 156 ARG F CG  1 
ATOM   8392 C  CD  . ARG F 1 159 ? 56.320  69.037  68.372  1.00 30.40 ? 156 ARG F CD  1 
ATOM   8393 N  NE  . ARG F 1 159 ? 55.995  67.848  67.603  1.00 35.96 ? 156 ARG F NE  1 
ATOM   8394 C  CZ  . ARG F 1 159 ? 56.078  66.576  67.993  1.00 35.18 ? 156 ARG F CZ  1 
ATOM   8395 N  NH1 . ARG F 1 159 ? 56.428  66.221  69.219  1.00 36.66 ? 156 ARG F NH1 1 
ATOM   8396 N  NH2 . ARG F 1 159 ? 55.757  65.649  67.125  1.00 35.90 ? 156 ARG F NH2 1 
ATOM   8397 N  N   . ARG F 1 160 ? 55.471  73.269  69.089  1.00 28.52 ? 157 ARG F N   1 
ATOM   8398 C  CA  . ARG F 1 160 ? 54.729  73.620  70.306  1.00 28.40 ? 157 ARG F CA  1 
ATOM   8399 C  C   . ARG F 1 160 ? 53.300  74.088  70.010  1.00 27.73 ? 157 ARG F C   1 
ATOM   8400 O  O   . ARG F 1 160 ? 52.367  73.735  70.739  1.00 28.19 ? 157 ARG F O   1 
ATOM   8401 C  CB  . ARG F 1 160 ? 55.501  74.617  71.166  1.00 28.38 ? 157 ARG F CB  1 
ATOM   8402 C  CG  . ARG F 1 160 ? 54.870  74.891  72.541  1.00 28.77 ? 157 ARG F CG  1 
ATOM   8403 C  CD  . ARG F 1 160 ? 54.711  73.625  73.418  1.00 32.11 ? 157 ARG F CD  1 
ATOM   8404 N  NE  . ARG F 1 160 ? 55.801  72.639  73.291  1.00 30.58 ? 157 ARG F NE  1 
ATOM   8405 C  CZ  . ARG F 1 160 ? 57.034  72.789  73.779  1.00 29.66 ? 157 ARG F CZ  1 
ATOM   8406 N  NH1 . ARG F 1 160 ? 57.402  73.896  74.424  1.00 27.74 ? 157 ARG F NH1 1 
ATOM   8407 N  NH2 . ARG F 1 160 ? 57.915  71.824  73.598  1.00 29.51 ? 157 ARG F NH2 1 
ATOM   8408 N  N   . LEU F 1 161 ? 53.150  74.847  68.927  1.00 26.90 ? 158 LEU F N   1 
ATOM   8409 C  CA  . LEU F 1 161 ? 51.856  75.267  68.404  1.00 26.38 ? 158 LEU F CA  1 
ATOM   8410 C  C   . LEU F 1 161 ? 50.965  74.080  68.149  1.00 26.07 ? 158 LEU F C   1 
ATOM   8411 O  O   . LEU F 1 161 ? 49.824  74.037  68.603  1.00 27.05 ? 158 LEU F O   1 
ATOM   8412 C  CB  . LEU F 1 161 ? 52.034  75.993  67.062  1.00 26.19 ? 158 LEU F CB  1 
ATOM   8413 C  CG  . LEU F 1 161 ? 51.090  77.135  66.648  1.00 25.24 ? 158 LEU F CG  1 
ATOM   8414 C  CD1 . LEU F 1 161 ? 50.964  77.187  65.131  1.00 21.81 ? 158 LEU F CD1 1 
ATOM   8415 C  CD2 . LEU F 1 161 ? 49.734  77.119  67.305  1.00 21.87 ? 158 LEU F CD2 1 
ATOM   8416 N  N   . ALA F 1 162 ? 51.490  73.122  67.408  1.00 25.27 ? 159 ALA F N   1 
ATOM   8417 C  CA  . ALA F 1 162 ? 50.740  71.936  67.070  1.00 25.25 ? 159 ALA F CA  1 
ATOM   8418 C  C   . ALA F 1 162 ? 50.367  71.136  68.319  1.00 25.14 ? 159 ALA F C   1 
ATOM   8419 O  O   . ALA F 1 162 ? 49.246  70.617  68.418  1.00 24.85 ? 159 ALA F O   1 
ATOM   8420 C  CB  . ALA F 1 162 ? 51.516  71.079  66.050  1.00 24.40 ? 159 ALA F CB  1 
ATOM   8421 N  N   . GLU F 1 163 ? 51.305  71.045  69.267  1.00 25.15 ? 160 GLU F N   1 
ATOM   8422 C  CA  . GLU F 1 163 ? 51.080  70.346  70.545  1.00 25.22 ? 160 GLU F CA  1 
ATOM   8423 C  C   . GLU F 1 163 ? 50.003  71.015  71.377  1.00 25.13 ? 160 GLU F C   1 
ATOM   8424 O  O   . GLU F 1 163 ? 49.188  70.342  71.975  1.00 24.85 ? 160 GLU F O   1 
ATOM   8425 C  CB  . GLU F 1 163 ? 52.373  70.227  71.356  1.00 25.14 ? 160 GLU F CB  1 
ATOM   8426 C  CG  . GLU F 1 163 ? 53.356  69.164  70.801  1.00 25.56 ? 160 GLU F CG  1 
ATOM   8427 C  CD  . GLU F 1 163 ? 54.782  69.366  71.309  1.00 25.85 ? 160 GLU F CD  1 
ATOM   8428 O  OE1 . GLU F 1 163 ? 55.113  70.496  71.750  1.00 28.28 ? 160 GLU F OE1 1 
ATOM   8429 O  OE2 . GLU F 1 163 ? 55.583  68.411  71.264  1.00 23.95 ? 160 GLU F OE2 1 
ATOM   8430 N  N   . TRP F 1 164 ? 49.991  72.343  71.413  1.00 25.49 ? 161 TRP F N   1 
ATOM   8431 C  CA  . TRP F 1 164 ? 48.932  73.048  72.135  1.00 26.05 ? 161 TRP F CA  1 
ATOM   8432 C  C   . TRP F 1 164 ? 47.569  72.812  71.469  1.00 25.70 ? 161 TRP F C   1 
ATOM   8433 O  O   . TRP F 1 164 ? 46.562  72.584  72.141  1.00 25.92 ? 161 TRP F O   1 
ATOM   8434 C  CB  . TRP F 1 164 ? 49.231  74.550  72.206  1.00 26.38 ? 161 TRP F CB  1 
ATOM   8435 C  CG  . TRP F 1 164 ? 50.362  74.985  73.095  1.00 25.81 ? 161 TRP F CG  1 
ATOM   8436 C  CD1 . TRP F 1 164 ? 51.098  76.115  72.957  1.00 25.64 ? 161 TRP F CD1 1 
ATOM   8437 C  CD2 . TRP F 1 164 ? 50.880  74.313  74.256  1.00 26.89 ? 161 TRP F CD2 1 
ATOM   8438 N  NE1 . TRP F 1 164 ? 52.021  76.210  73.964  1.00 25.06 ? 161 TRP F NE1 1 
ATOM   8439 C  CE2 . TRP F 1 164 ? 51.919  75.112  74.769  1.00 25.20 ? 161 TRP F CE2 1 
ATOM   8440 C  CE3 . TRP F 1 164 ? 50.562  73.118  74.917  1.00 27.69 ? 161 TRP F CE3 1 
ATOM   8441 C  CZ2 . TRP F 1 164 ? 52.635  74.768  75.909  1.00 25.60 ? 161 TRP F CZ2 1 
ATOM   8442 C  CZ3 . TRP F 1 164 ? 51.286  72.775  76.058  1.00 26.18 ? 161 TRP F CZ3 1 
ATOM   8443 C  CH2 . TRP F 1 164 ? 52.309  73.598  76.535  1.00 25.22 ? 161 TRP F CH2 1 
ATOM   8444 N  N   . VAL F 1 165 ? 47.541  72.868  70.141  1.00 25.68 ? 162 VAL F N   1 
ATOM   8445 C  CA  . VAL F 1 165 ? 46.334  72.495  69.394  1.00 25.01 ? 162 VAL F CA  1 
ATOM   8446 C  C   . VAL F 1 165 ? 45.901  71.045  69.715  1.00 24.24 ? 162 VAL F C   1 
ATOM   8447 O  O   . VAL F 1 165 ? 44.721  70.800  69.982  1.00 24.26 ? 162 VAL F O   1 
ATOM   8448 C  CB  . VAL F 1 165 ? 46.492  72.735  67.873  1.00 24.34 ? 162 VAL F CB  1 
ATOM   8449 C  CG1 . VAL F 1 165 ? 45.331  72.126  67.089  1.00 25.02 ? 162 VAL F CG1 1 
ATOM   8450 C  CG2 . VAL F 1 165 ? 46.592  74.216  67.589  1.00 25.97 ? 162 VAL F CG2 1 
ATOM   8451 N  N   . ALA F 1 166 ? 46.854  70.107  69.713  1.00 23.51 ? 163 ALA F N   1 
ATOM   8452 C  CA  . ALA F 1 166 ? 46.557  68.702  69.995  1.00 22.69 ? 163 ALA F CA  1 
ATOM   8453 C  C   . ALA F 1 166 ? 45.984  68.530  71.394  1.00 22.66 ? 163 ALA F C   1 
ATOM   8454 O  O   . ALA F 1 166 ? 44.958  67.851  71.574  1.00 22.18 ? 163 ALA F O   1 
ATOM   8455 C  CB  . ALA F 1 166 ? 47.784  67.840  69.810  1.00 22.50 ? 163 ALA F CB  1 
ATOM   8456 N  N   . ILE F 1 167 ? 46.638  69.153  72.374  1.00 22.41 ? 164 ILE F N   1 
ATOM   8457 C  CA  . ILE F 1 167 ? 46.236  69.045  73.773  1.00 23.21 ? 164 ILE F CA  1 
ATOM   8458 C  C   . ILE F 1 167 ? 44.884  69.700  74.034  1.00 23.69 ? 164 ILE F C   1 
ATOM   8459 O  O   . ILE F 1 167 ? 43.976  69.047  74.536  1.00 23.30 ? 164 ILE F O   1 
ATOM   8460 C  CB  . ILE F 1 167 ? 47.312  69.613  74.715  1.00 23.12 ? 164 ILE F CB  1 
ATOM   8461 C  CG1 . ILE F 1 167 ? 48.535  68.709  74.688  1.00 24.24 ? 164 ILE F CG1 1 
ATOM   8462 C  CG2 . ILE F 1 167 ? 46.810  69.702  76.147  1.00 22.77 ? 164 ILE F CG2 1 
ATOM   8463 C  CD1 . ILE F 1 167 ? 49.829  69.451  74.999  1.00 25.80 ? 164 ILE F CD1 1 
ATOM   8464 N  N   . PHE F 1 168 ? 44.755  70.974  73.655  1.00 24.93 ? 165 PHE F N   1 
ATOM   8465 C  CA  . PHE F 1 168 ? 43.602  71.803  74.036  1.00 25.97 ? 165 PHE F CA  1 
ATOM   8466 C  C   . PHE F 1 168 ? 42.412  71.808  73.107  1.00 26.28 ? 165 PHE F C   1 
ATOM   8467 O  O   . PHE F 1 168 ? 41.282  71.915  73.566  1.00 27.13 ? 165 PHE F O   1 
ATOM   8468 C  CB  . PHE F 1 168 ? 44.040  73.237  74.251  1.00 26.78 ? 165 PHE F CB  1 
ATOM   8469 C  CG  . PHE F 1 168 ? 45.045  73.383  75.335  1.00 28.22 ? 165 PHE F CG  1 
ATOM   8470 C  CD1 . PHE F 1 168 ? 46.335  73.833  75.047  1.00 28.15 ? 165 PHE F CD1 1 
ATOM   8471 C  CD2 . PHE F 1 168 ? 44.715  73.014  76.649  1.00 29.43 ? 165 PHE F CD2 1 
ATOM   8472 C  CE1 . PHE F 1 168 ? 47.292  73.953  76.068  1.00 29.34 ? 165 PHE F CE1 1 
ATOM   8473 C  CE2 . PHE F 1 168 ? 45.654  73.125  77.677  1.00 30.43 ? 165 PHE F CE2 1 
ATOM   8474 C  CZ  . PHE F 1 168 ? 46.944  73.595  77.392  1.00 29.96 ? 165 PHE F CZ  1 
ATOM   8475 N  N   . VAL F 1 169 ? 42.646  71.711  71.807  1.00 25.99 ? 166 VAL F N   1 
ATOM   8476 C  CA  . VAL F 1 169 ? 41.547  71.720  70.877  1.00 25.46 ? 166 VAL F CA  1 
ATOM   8477 C  C   . VAL F 1 169 ? 41.134  70.273  70.685  1.00 26.40 ? 166 VAL F C   1 
ATOM   8478 O  O   . VAL F 1 169 ? 39.949  69.922  70.652  1.00 25.75 ? 166 VAL F O   1 
ATOM   8479 C  CB  . VAL F 1 169 ? 41.959  72.348  69.550  1.00 25.07 ? 166 VAL F CB  1 
ATOM   8480 C  CG1 . VAL F 1 169 ? 40.789  72.350  68.581  1.00 22.93 ? 166 VAL F CG1 1 
ATOM   8481 C  CG2 . VAL F 1 169 ? 42.480  73.755  69.790  1.00 23.71 ? 166 VAL F CG2 1 
ATOM   8482 N  N   . ASP F 1 170 ? 42.151  69.433  70.618  1.00 27.11 ? 167 ASP F N   1 
ATOM   8483 C  CA  . ASP F 1 170 ? 41.985  68.088  70.187  1.00 28.03 ? 167 ASP F CA  1 
ATOM   8484 C  C   . ASP F 1 170 ? 41.867  67.056  71.298  1.00 28.07 ? 167 ASP F C   1 
ATOM   8485 O  O   . ASP F 1 170 ? 41.458  65.933  71.047  1.00 27.93 ? 167 ASP F O   1 
ATOM   8486 C  CB  . ASP F 1 170 ? 43.112  67.770  69.245  1.00 28.64 ? 167 ASP F CB  1 
ATOM   8487 C  CG  . ASP F 1 170 ? 42.637  67.675  67.838  1.00 32.24 ? 167 ASP F CG  1 
ATOM   8488 O  OD1 . ASP F 1 170 ? 42.043  66.579  67.538  1.00 35.13 ? 167 ASP F OD1 1 
ATOM   8489 O  OD2 . ASP F 1 170 ? 42.821  68.669  67.070  1.00 29.75 ? 167 ASP F OD2 1 
ATOM   8490 N  N   . GLY F 1 171 ? 42.207  67.442  72.526  1.00 28.38 ? 168 GLY F N   1 
ATOM   8491 C  CA  . GLY F 1 171 ? 41.983  66.585  73.683  1.00 28.29 ? 168 GLY F CA  1 
ATOM   8492 C  C   . GLY F 1 171 ? 43.026  65.501  73.872  1.00 28.62 ? 168 GLY F C   1 
ATOM   8493 O  O   . GLY F 1 171 ? 42.831  64.615  74.687  1.00 28.63 ? 168 GLY F O   1 
ATOM   8494 N  N   . ARG F 1 172 ? 44.135  65.575  73.134  1.00 28.98 ? 169 ARG F N   1 
ATOM   8495 C  CA  . ARG F 1 172 ? 45.268  64.677  73.332  1.00 29.27 ? 169 ARG F CA  1 
ATOM   8496 C  C   . ARG F 1 172 ? 46.016  65.004  74.627  1.00 30.02 ? 169 ARG F C   1 
ATOM   8497 O  O   . ARG F 1 172 ? 47.198  65.357  74.623  1.00 29.88 ? 169 ARG F O   1 
ATOM   8498 C  CB  . ARG F 1 172 ? 46.183  64.679  72.110  1.00 29.24 ? 169 ARG F CB  1 
ATOM   8499 C  CG  . ARG F 1 172 ? 45.598  63.868  70.952  1.00 28.85 ? 169 ARG F CG  1 
ATOM   8500 C  CD  . ARG F 1 172 ? 45.897  64.505  69.611  1.00 29.16 ? 169 ARG F CD  1 
ATOM   8501 N  NE  . ARG F 1 172 ? 47.213  64.113  69.125  1.00 30.55 ? 169 ARG F NE  1 
ATOM   8502 C  CZ  . ARG F 1 172 ? 47.810  64.626  68.048  1.00 32.25 ? 169 ARG F CZ  1 
ATOM   8503 N  NH1 . ARG F 1 172 ? 47.220  65.568  67.316  1.00 33.26 ? 169 ARG F NH1 1 
ATOM   8504 N  NH2 . ARG F 1 172 ? 49.015  64.192  67.695  1.00 32.24 ? 169 ARG F NH2 1 
ATOM   8505 N  N   . LYS F 1 173 ? 45.288  64.825  75.732  1.00 31.00 ? 170 LYS F N   1 
ATOM   8506 C  CA  . LYS F 1 173 ? 45.672  65.233  77.086  1.00 32.09 ? 170 LYS F CA  1 
ATOM   8507 C  C   . LYS F 1 173 ? 47.005  64.705  77.600  1.00 32.18 ? 170 LYS F C   1 
ATOM   8508 O  O   . LYS F 1 173 ? 47.671  65.380  78.393  1.00 33.00 ? 170 LYS F O   1 
ATOM   8509 C  CB  . LYS F 1 173 ? 44.559  64.866  78.078  1.00 31.95 ? 170 LYS F CB  1 
ATOM   8510 C  CG  . LYS F 1 173 ? 43.398  65.860  78.090  1.00 32.78 ? 170 LYS F CG  1 
ATOM   8511 C  CD  . LYS F 1 173 ? 42.101  65.226  78.624  1.00 33.30 ? 170 LYS F CD  1 
ATOM   8512 C  CE  . LYS F 1 173 ? 41.033  66.388  78.908  1.00 34.21 ? 170 LYS F CE  1 
ATOM   8513 N  NZ  . LYS F 1 173 ? 39.827  65.608  79.625  1.00 34.50 ? 170 LYS F NZ  1 
ATOM   8514 N  N   . GLU F 1 174 ? 47.391  63.515  77.154  1.00 31.83 ? 171 GLU F N   1 
ATOM   8515 C  CA  . GLU F 1 174 ? 48.611  62.865  77.612  1.00 31.75 ? 171 GLU F CA  1 
ATOM   8516 C  C   . GLU F 1 174 ? 49.884  63.550  77.154  1.00 31.72 ? 171 GLU F C   1 
ATOM   8517 O  O   . GLU F 1 174 ? 50.955  63.286  77.708  1.00 31.69 ? 171 GLU F O   1 
ATOM   8518 C  CB  . GLU F 1 174 ? 48.662  61.431  77.117  1.00 31.96 ? 171 GLU F CB  1 
ATOM   8519 C  CG  . GLU F 1 174 ? 47.427  61.009  76.354  1.00 33.19 ? 171 GLU F CG  1 
ATOM   8520 C  CD  . GLU F 1 174 ? 47.551  61.277  74.870  1.00 33.20 ? 171 GLU F CD  1 
ATOM   8521 O  OE1 . GLU F 1 174 ? 48.643  61.053  74.307  1.00 33.17 ? 171 GLU F OE1 1 
ATOM   8522 O  OE2 . GLU F 1 174 ? 46.547  61.693  74.266  1.00 33.97 ? 171 GLU F OE2 1 
ATOM   8523 N  N   . LEU F 1 175 ? 49.787  64.406  76.133  1.00 31.47 ? 172 LEU F N   1 
ATOM   8524 C  CA  . LEU F 1 175 ? 50.964  65.109  75.631  1.00 31.24 ? 172 LEU F CA  1 
ATOM   8525 C  C   . LEU F 1 175 ? 51.461  66.136  76.636  1.00 30.70 ? 172 LEU F C   1 
ATOM   8526 O  O   . LEU F 1 175 ? 52.633  66.501  76.631  1.00 30.23 ? 172 LEU F O   1 
ATOM   8527 C  CB  . LEU F 1 175 ? 50.679  65.792  74.285  1.00 31.71 ? 172 LEU F CB  1 
ATOM   8528 C  CG  . LEU F 1 175 ? 50.386  64.950  73.032  1.00 33.12 ? 172 LEU F CG  1 
ATOM   8529 C  CD1 . LEU F 1 175 ? 50.185  65.884  71.828  1.00 32.09 ? 172 LEU F CD1 1 
ATOM   8530 C  CD2 . LEU F 1 175 ? 51.484  63.931  72.757  1.00 33.21 ? 172 LEU F CD2 1 
ATOM   8531 N  N   . LEU F 1 176 ? 50.563  66.593  77.502  1.00 30.54 ? 173 LEU F N   1 
ATOM   8532 C  CA  . LEU F 1 176 ? 50.888  67.657  78.452  1.00 30.63 ? 173 LEU F CA  1 
ATOM   8533 C  C   . LEU F 1 176 ? 52.046  67.299  79.386  1.00 30.74 ? 173 LEU F C   1 
ATOM   8534 O  O   . LEU F 1 176 ? 53.027  68.041  79.428  1.00 30.41 ? 173 LEU F O   1 
ATOM   8535 C  CB  . LEU F 1 176 ? 49.662  68.061  79.265  1.00 30.27 ? 173 LEU F CB  1 
ATOM   8536 C  CG  . LEU F 1 176 ? 49.443  69.522  79.644  1.00 29.74 ? 173 LEU F CG  1 
ATOM   8537 C  CD1 . LEU F 1 176 ? 49.036  69.554  81.096  1.00 27.38 ? 173 LEU F CD1 1 
ATOM   8538 C  CD2 . LEU F 1 176 ? 50.633  70.446  79.365  1.00 27.61 ? 173 LEU F CD2 1 
ATOM   8539 N  N   . GLU F 1 177 ? 51.930  66.182  80.119  1.00 30.84 ? 174 GLU F N   1 
ATOM   8540 C  CA  . GLU F 1 177 ? 52.994  65.740  81.029  1.00 31.38 ? 174 GLU F CA  1 
ATOM   8541 C  C   . GLU F 1 177 ? 54.230  65.327  80.271  1.00 30.86 ? 174 GLU F C   1 
ATOM   8542 O  O   . GLU F 1 177 ? 55.346  65.548  80.732  1.00 30.26 ? 174 GLU F O   1 
ATOM   8543 C  CB  . GLU F 1 177 ? 52.559  64.563  81.910  1.00 31.79 ? 174 GLU F CB  1 
ATOM   8544 C  CG  . GLU F 1 177 ? 52.305  64.912  83.375  1.00 34.84 ? 174 GLU F CG  1 
ATOM   8545 C  CD  . GLU F 1 177 ? 53.539  65.417  84.128  1.00 37.53 ? 174 GLU F CD  1 
ATOM   8546 O  OE1 . GLU F 1 177 ? 54.250  64.581  84.741  1.00 37.66 ? 174 GLU F OE1 1 
ATOM   8547 O  OE2 . GLU F 1 177 ? 53.784  66.652  84.115  1.00 39.40 ? 174 GLU F OE2 1 
ATOM   8548 N  N   . LYS F 1 178 ? 54.015  64.707  79.117  1.00 30.94 ? 175 LYS F N   1 
ATOM   8549 C  CA  . LYS F 1 178 ? 55.106  64.266  78.276  1.00 31.68 ? 175 LYS F CA  1 
ATOM   8550 C  C   . LYS F 1 178 ? 55.991  65.463  77.968  1.00 31.31 ? 175 LYS F C   1 
ATOM   8551 O  O   . LYS F 1 178 ? 57.199  65.378  78.164  1.00 31.64 ? 175 LYS F O   1 
ATOM   8552 C  CB  . LYS F 1 178 ? 54.588  63.591  76.996  1.00 32.52 ? 175 LYS F CB  1 
ATOM   8553 C  CG  . LYS F 1 178 ? 55.651  62.828  76.179  1.00 34.54 ? 175 LYS F CG  1 
ATOM   8554 C  CD  . LYS F 1 178 ? 56.420  63.749  75.183  1.00 38.58 ? 175 LYS F CD  1 
ATOM   8555 C  CE  . LYS F 1 178 ? 57.411  62.956  74.301  1.00 37.60 ? 175 LYS F CE  1 
ATOM   8556 N  NZ  . LYS F 1 178 ? 58.613  62.501  75.065  1.00 38.82 ? 175 LYS F NZ  1 
ATOM   8557 N  N   . ILE F 1 179 ? 55.378  66.564  77.524  1.00 30.41 ? 176 ILE F N   1 
ATOM   8558 C  CA  . ILE F 1 179 ? 56.080  67.818  77.227  1.00 30.50 ? 176 ILE F CA  1 
ATOM   8559 C  C   . ILE F 1 179 ? 56.723  68.404  78.483  1.00 30.47 ? 176 ILE F C   1 
ATOM   8560 O  O   . ILE F 1 179 ? 57.922  68.671  78.508  1.00 30.92 ? 176 ILE F O   1 
ATOM   8561 C  CB  . ILE F 1 179 ? 55.122  68.889  76.591  1.00 30.63 ? 176 ILE F CB  1 
ATOM   8562 C  CG1 . ILE F 1 179 ? 54.759  68.497  75.155  1.00 30.26 ? 176 ILE F CG1 1 
ATOM   8563 C  CG2 . ILE F 1 179 ? 55.706  70.297  76.666  1.00 28.51 ? 176 ILE F CG2 1 
ATOM   8564 C  CD1 . ILE F 1 179 ? 53.570  69.255  74.632  1.00 29.76 ? 176 ILE F CD1 1 
ATOM   8565 N  N   . ARG F 1 180 ? 55.921  68.582  79.523  1.00 30.20 ? 177 ARG F N   1 
ATOM   8566 C  CA  . ARG F 1 180 ? 56.382  69.160  80.773  1.00 30.27 ? 177 ARG F CA  1 
ATOM   8567 C  C   . ARG F 1 180 ? 57.598  68.473  81.366  1.00 30.72 ? 177 ARG F C   1 
ATOM   8568 O  O   . ARG F 1 180 ? 58.507  69.140  81.872  1.00 31.13 ? 177 ARG F O   1 
ATOM   8569 C  CB  . ARG F 1 180 ? 55.248  69.191  81.781  1.00 29.96 ? 177 ARG F CB  1 
ATOM   8570 C  CG  . ARG F 1 180 ? 54.252  70.279  81.475  1.00 29.96 ? 177 ARG F CG  1 
ATOM   8571 C  CD  . ARG F 1 180 ? 53.166  70.235  82.469  1.00 30.65 ? 177 ARG F CD  1 
ATOM   8572 N  NE  . ARG F 1 180 ? 52.299  71.402  82.417  1.00 29.67 ? 177 ARG F NE  1 
ATOM   8573 C  CZ  . ARG F 1 180 ? 51.179  71.497  83.122  1.00 29.38 ? 177 ARG F CZ  1 
ATOM   8574 N  NH1 . ARG F 1 180 ? 50.796  70.492  83.898  1.00 29.75 ? 177 ARG F NH1 1 
ATOM   8575 N  NH2 . ARG F 1 180 ? 50.427  72.572  83.030  1.00 28.98 ? 177 ARG F NH2 1 
ATOM   8576 N  N   . LYS F 1 181 ? 57.643  67.147  81.272  1.00 31.01 ? 178 LYS F N   1 
ATOM   8577 C  CA  . LYS F 1 181 ? 58.743  66.408  81.867  1.00 31.16 ? 178 LYS F CA  1 
ATOM   8578 C  C   . LYS F 1 181 ? 59.884  66.085  80.894  1.00 30.88 ? 178 LYS F C   1 
ATOM   8579 O  O   . LYS F 1 181 ? 60.879  65.505  81.306  1.00 31.68 ? 178 LYS F O   1 
ATOM   8580 C  CB  . LYS F 1 181 ? 58.227  65.139  82.554  1.00 31.37 ? 178 LYS F CB  1 
ATOM   8581 C  CG  . LYS F 1 181 ? 57.136  65.379  83.611  1.00 33.59 ? 178 LYS F CG  1 
ATOM   8582 C  CD  . LYS F 1 181 ? 57.636  65.394  85.091  1.00 36.55 ? 178 LYS F CD  1 
ATOM   8583 C  CE  . LYS F 1 181 ? 57.742  66.823  85.691  1.00 38.77 ? 178 LYS F CE  1 
ATOM   8584 N  NZ  . LYS F 1 181 ? 56.427  67.552  85.789  1.00 37.37 ? 178 LYS F NZ  1 
ATOM   8585 N  N   . ASP F 1 182 ? 59.762  66.476  79.626  1.00 30.47 ? 179 ASP F N   1 
ATOM   8586 C  CA  . ASP F 1 182 ? 60.727  66.080  78.580  1.00 30.06 ? 179 ASP F CA  1 
ATOM   8587 C  C   . ASP F 1 182 ? 62.114  66.715  78.757  1.00 30.01 ? 179 ASP F C   1 
ATOM   8588 O  O   . ASP F 1 182 ? 62.260  67.925  78.651  1.00 30.52 ? 179 ASP F O   1 
ATOM   8589 C  CB  . ASP F 1 182 ? 60.157  66.408  77.195  1.00 30.06 ? 179 ASP F CB  1 
ATOM   8590 C  CG  . ASP F 1 182 ? 60.994  65.848  76.042  1.00 30.33 ? 179 ASP F CG  1 
ATOM   8591 O  OD1 . ASP F 1 182 ? 60.713  66.230  74.888  1.00 30.28 ? 179 ASP F OD1 1 
ATOM   8592 O  OD2 . ASP F 1 182 ? 61.912  65.031  76.265  1.00 31.34 ? 179 ASP F OD2 1 
ATOM   8593 N  N   . PRO F 1 183 ? 63.150  65.896  79.036  1.00 30.30 ? 180 PRO F N   1 
ATOM   8594 C  CA  . PRO F 1 183 ? 64.475  66.505  79.275  1.00 30.03 ? 180 PRO F CA  1 
ATOM   8595 C  C   . PRO F 1 183 ? 65.152  67.110  78.031  1.00 29.82 ? 180 PRO F C   1 
ATOM   8596 O  O   . PRO F 1 183 ? 66.033  67.954  78.171  1.00 30.32 ? 180 PRO F O   1 
ATOM   8597 C  CB  . PRO F 1 183 ? 65.289  65.349  79.845  1.00 30.08 ? 180 PRO F CB  1 
ATOM   8598 C  CG  . PRO F 1 183 ? 64.627  64.131  79.301  1.00 30.07 ? 180 PRO F CG  1 
ATOM   8599 C  CD  . PRO F 1 183 ? 63.175  64.430  79.195  1.00 29.36 ? 180 PRO F CD  1 
ATOM   8600 N  N   . ALA F 1 184 ? 64.713  66.707  76.842  1.00 29.22 ? 181 ALA F N   1 
ATOM   8601 C  CA  . ALA F 1 184 ? 65.281  67.168  75.578  1.00 28.97 ? 181 ALA F CA  1 
ATOM   8602 C  C   . ALA F 1 184 ? 64.948  68.633  75.286  1.00 28.97 ? 181 ALA F C   1 
ATOM   8603 O  O   . ALA F 1 184 ? 65.589  69.266  74.446  1.00 28.61 ? 181 ALA F O   1 
ATOM   8604 C  CB  . ALA F 1 184 ? 64.793  66.279  74.425  1.00 28.65 ? 181 ALA F CB  1 
ATOM   8605 N  N   . ARG F 1 185 ? 63.938  69.158  75.981  1.00 28.79 ? 182 ARG F N   1 
ATOM   8606 C  CA  . ARG F 1 185 ? 63.489  70.530  75.796  1.00 28.35 ? 182 ARG F CA  1 
ATOM   8607 C  C   . ARG F 1 185 ? 64.535  71.554  76.215  1.00 28.71 ? 182 ARG F C   1 
ATOM   8608 O  O   . ARG F 1 185 ? 64.420  72.725  75.877  1.00 28.94 ? 182 ARG F O   1 
ATOM   8609 C  CB  . ARG F 1 185 ? 62.196  70.762  76.547  1.00 27.75 ? 182 ARG F CB  1 
ATOM   8610 C  CG  . ARG F 1 185 ? 60.991  70.088  75.947  1.00 26.84 ? 182 ARG F CG  1 
ATOM   8611 C  CD  . ARG F 1 185 ? 59.838  70.232  76.899  1.00 25.28 ? 182 ARG F CD  1 
ATOM   8612 N  NE  . ARG F 1 185 ? 59.655  71.633  77.259  1.00 24.03 ? 182 ARG F NE  1 
ATOM   8613 C  CZ  . ARG F 1 185 ? 59.296  72.070  78.461  1.00 24.74 ? 182 ARG F CZ  1 
ATOM   8614 N  NH1 . ARG F 1 185 ? 59.176  73.371  78.654  1.00 27.39 ? 182 ARG F NH1 1 
ATOM   8615 N  NH2 . ARG F 1 185 ? 59.062  71.229  79.468  1.00 23.31 ? 182 ARG F NH2 1 
ATOM   8616 N  N   . PHE F 1 186 ? 65.564  71.107  76.932  1.00 29.13 ? 183 PHE F N   1 
ATOM   8617 C  CA  . PHE F 1 186 ? 66.643  71.996  77.379  1.00 29.56 ? 183 PHE F CA  1 
ATOM   8618 C  C   . PHE F 1 186 ? 68.040  71.420  77.068  1.00 30.71 ? 183 PHE F C   1 
ATOM   8619 O  O   . PHE F 1 186 ? 68.544  70.579  77.803  1.00 30.88 ? 183 PHE F O   1 
ATOM   8620 C  CB  . PHE F 1 186 ? 66.444  72.347  78.867  1.00 28.66 ? 183 PHE F CB  1 
ATOM   8621 C  CG  . PHE F 1 186 ? 65.131  73.023  79.133  1.00 26.87 ? 183 PHE F CG  1 
ATOM   8622 C  CD1 . PHE F 1 186 ? 64.021  72.285  79.549  1.00 25.85 ? 183 PHE F CD1 1 
ATOM   8623 C  CD2 . PHE F 1 186 ? 64.985  74.396  78.911  1.00 24.56 ? 183 PHE F CD2 1 
ATOM   8624 C  CE1 . PHE F 1 186 ? 62.765  72.913  79.737  1.00 27.56 ? 183 PHE F CE1 1 
ATOM   8625 C  CE2 . PHE F 1 186 ? 63.760  75.021  79.110  1.00 23.98 ? 183 PHE F CE2 1 
ATOM   8626 C  CZ  . PHE F 1 186 ? 62.644  74.288  79.524  1.00 25.52 ? 183 PHE F CZ  1 
ATOM   8627 N  N   . VAL F 1 187 ? 68.650  71.879  75.969  1.00 31.95 ? 184 VAL F N   1 
ATOM   8628 C  CA  . VAL F 1 187 ? 69.933  71.324  75.469  1.00 33.19 ? 184 VAL F CA  1 
ATOM   8629 C  C   . VAL F 1 187 ? 71.054  71.202  76.524  1.00 33.99 ? 184 VAL F C   1 
ATOM   8630 O  O   . VAL F 1 187 ? 71.574  72.201  77.033  1.00 35.11 ? 184 VAL F O   1 
ATOM   8631 C  CB  . VAL F 1 187 ? 70.436  72.089  74.238  1.00 32.96 ? 184 VAL F CB  1 
ATOM   8632 C  CG1 . VAL F 1 187 ? 71.954  72.016  74.127  1.00 32.46 ? 184 VAL F CG1 1 
ATOM   8633 C  CG2 . VAL F 1 187 ? 69.757  71.547  72.999  1.00 33.61 ? 184 VAL F CG2 1 
HETATM 8634 P  P   . PO4 G 2 .   ? 113.669 75.330  77.806  0.60 18.17 ? 501 PO4 A P   1 
HETATM 8635 O  O1  . PO4 G 2 .   ? 114.595 75.349  76.613  0.60 23.64 ? 501 PO4 A O1  1 
HETATM 8636 O  O2  . PO4 G 2 .   ? 113.975 74.148  78.634  0.60 24.83 ? 501 PO4 A O2  1 
HETATM 8637 O  O3  . PO4 G 2 .   ? 113.908 76.487  78.705  0.60 25.54 ? 501 PO4 A O3  1 
HETATM 8638 O  O4  . PO4 G 2 .   ? 112.253 75.238  77.403  0.60 23.55 ? 501 PO4 A O4  1 
HETATM 8639 C  C1  . GOL H 3 .   ? 101.657 92.512  64.202  1.00 49.33 ? 509 GOL A C1  1 
HETATM 8640 O  O1  . GOL H 3 .   ? 101.026 92.851  65.434  1.00 49.61 ? 509 GOL A O1  1 
HETATM 8641 C  C2  . GOL H 3 .   ? 100.787 92.794  62.966  1.00 47.20 ? 509 GOL A C2  1 
HETATM 8642 O  O2  . GOL H 3 .   ? 101.613 93.051  61.849  1.00 46.54 ? 509 GOL A O2  1 
HETATM 8643 C  C3  . GOL H 3 .   ? 99.774  91.662  62.705  1.00 46.19 ? 509 GOL A C3  1 
HETATM 8644 O  O3  . GOL H 3 .   ? 100.072 90.796  61.618  1.00 43.19 ? 509 GOL A O3  1 
HETATM 8645 C  C1  . GOL I 3 .   ? 111.619 67.337  58.510  1.00 64.78 ? 512 GOL A C1  1 
HETATM 8646 O  O1  . GOL I 3 .   ? 110.671 67.522  57.469  1.00 63.38 ? 512 GOL A O1  1 
HETATM 8647 C  C2  . GOL I 3 .   ? 111.993 65.856  58.702  1.00 64.98 ? 512 GOL A C2  1 
HETATM 8648 O  O2  . GOL I 3 .   ? 112.766 65.703  59.880  1.00 61.75 ? 512 GOL A O2  1 
HETATM 8649 C  C3  . GOL I 3 .   ? 110.759 64.938  58.727  1.00 64.95 ? 512 GOL A C3  1 
HETATM 8650 O  O3  . GOL I 3 .   ? 110.717 64.106  57.579  1.00 65.43 ? 512 GOL A O3  1 
HETATM 8651 P  P   . PO4 J 2 .   ? 104.530 58.447  38.776  0.80 34.64 ? 502 PO4 B P   1 
HETATM 8652 O  O1  . PO4 J 2 .   ? 105.645 59.163  38.126  0.80 39.21 ? 502 PO4 B O1  1 
HETATM 8653 O  O2  . PO4 J 2 .   ? 104.993 57.889  40.104  0.80 38.87 ? 502 PO4 B O2  1 
HETATM 8654 O  O3  . PO4 J 2 .   ? 103.442 59.451  38.936  0.80 36.99 ? 502 PO4 B O3  1 
HETATM 8655 O  O4  . PO4 J 2 .   ? 104.142 57.311  37.859  0.80 40.90 ? 502 PO4 B O4  1 
HETATM 8656 C  C1  . GOL K 3 .   ? 113.995 51.677  37.348  1.00 75.23 ? 510 GOL B C1  1 
HETATM 8657 O  O1  . GOL K 3 .   ? 113.648 53.037  37.548  1.00 73.03 ? 510 GOL B O1  1 
HETATM 8658 C  C2  . GOL K 3 .   ? 115.374 51.339  37.944  1.00 76.10 ? 510 GOL B C2  1 
HETATM 8659 O  O2  . GOL K 3 .   ? 116.263 52.444  37.985  1.00 76.10 ? 510 GOL B O2  1 
HETATM 8660 C  C3  . GOL K 3 .   ? 116.004 50.126  37.248  1.00 76.16 ? 510 GOL B C3  1 
HETATM 8661 O  O3  . GOL K 3 .   ? 117.349 50.376  36.880  1.00 75.16 ? 510 GOL B O3  1 
HETATM 8662 P  P   . PO4 L 2 .   ? 104.008 47.850  68.801  1.00 51.20 ? 503 PO4 C P   1 
HETATM 8663 O  O1  . PO4 L 2 .   ? 105.478 47.570  68.622  1.00 48.36 ? 503 PO4 C O1  1 
HETATM 8664 O  O2  . PO4 L 2 .   ? 103.378 48.548  67.590  1.00 50.40 ? 503 PO4 C O2  1 
HETATM 8665 O  O3  . PO4 L 2 .   ? 103.337 46.526  69.074  1.00 52.54 ? 503 PO4 C O3  1 
HETATM 8666 O  O4  . PO4 L 2 .   ? 103.813 48.703  70.034  1.00 53.54 ? 503 PO4 C O4  1 
HETATM 8667 C  C1  . GOL M 3 .   ? 110.486 63.226  62.069  1.00 38.05 ? 508 GOL C C1  1 
HETATM 8668 O  O1  . GOL M 3 .   ? 109.767 62.646  61.002  1.00 38.26 ? 508 GOL C O1  1 
HETATM 8669 C  C2  . GOL M 3 .   ? 109.990 64.636  62.401  1.00 38.38 ? 508 GOL C C2  1 
HETATM 8670 O  O2  . GOL M 3 .   ? 109.044 65.069  61.427  1.00 38.48 ? 508 GOL C O2  1 
HETATM 8671 C  C3  . GOL M 3 .   ? 111.205 65.578  62.495  1.00 36.76 ? 508 GOL C C3  1 
HETATM 8672 O  O3  . GOL M 3 .   ? 112.387 64.785  62.412  1.00 35.31 ? 508 GOL C O3  1 
HETATM 8673 C  C1  . GOL N 3 .   ? 112.282 50.186  41.730  1.00 61.71 ? 511 GOL C C1  1 
HETATM 8674 O  O1  . GOL N 3 .   ? 110.968 49.965  41.254  1.00 60.79 ? 511 GOL C O1  1 
HETATM 8675 C  C2  . GOL N 3 .   ? 113.306 49.195  41.161  1.00 61.37 ? 511 GOL C C2  1 
HETATM 8676 O  O2  . GOL N 3 .   ? 113.397 48.020  41.951  1.00 59.73 ? 511 GOL C O2  1 
HETATM 8677 C  C3  . GOL N 3 .   ? 114.666 49.892  41.132  1.00 61.86 ? 511 GOL C C3  1 
HETATM 8678 O  O3  . GOL N 3 .   ? 115.717 49.000  40.806  1.00 62.27 ? 511 GOL C O3  1 
HETATM 8679 P  P   . PO4 O 2 .   ? 122.690 81.465  47.775  1.00 50.17 ? 504 PO4 D P   1 
HETATM 8680 O  O1  . PO4 O 2 .   ? 123.359 82.811  47.723  1.00 52.12 ? 504 PO4 D O1  1 
HETATM 8681 O  O2  . PO4 O 2 .   ? 121.968 81.329  46.456  1.00 51.02 ? 504 PO4 D O2  1 
HETATM 8682 O  O3  . PO4 O 2 .   ? 123.739 80.391  47.929  1.00 48.69 ? 504 PO4 D O3  1 
HETATM 8683 O  O4  . PO4 O 2 .   ? 121.712 81.425  48.950  1.00 51.44 ? 504 PO4 D O4  1 
HETATM 8684 C  C1  . GOL P 3 .   ? 110.942 67.187  54.105  1.00 38.71 ? 507 GOL D C1  1 
HETATM 8685 O  O1  . GOL P 3 .   ? 110.817 68.339  54.899  1.00 35.88 ? 507 GOL D O1  1 
HETATM 8686 C  C2  . GOL P 3 .   ? 112.411 66.812  54.045  1.00 40.62 ? 507 GOL D C2  1 
HETATM 8687 O  O2  . GOL P 3 .   ? 113.122 67.579  55.024  1.00 41.13 ? 507 GOL D O2  1 
HETATM 8688 C  C3  . GOL P 3 .   ? 112.535 65.292  54.192  1.00 39.18 ? 507 GOL D C3  1 
HETATM 8689 O  O3  . GOL P 3 .   ? 112.856 64.916  55.527  1.00 42.14 ? 507 GOL D O3  1 
HETATM 8690 P  P   . PO4 Q 2 .   ? 73.353  88.727  86.056  0.90 35.69 ? 505 PO4 E P   1 
HETATM 8691 O  O1  . PO4 Q 2 .   ? 74.735  88.106  86.101  0.90 36.40 ? 505 PO4 E O1  1 
HETATM 8692 O  O2  . PO4 Q 2 .   ? 73.468  90.217  85.824  0.90 32.03 ? 505 PO4 E O2  1 
HETATM 8693 O  O3  . PO4 Q 2 .   ? 72.495  88.075  84.970  0.90 36.70 ? 505 PO4 E O3  1 
HETATM 8694 O  O4  . PO4 Q 2 .   ? 72.713  88.453  87.401  0.90 37.83 ? 505 PO4 E O4  1 
HETATM 8695 P  P   . PO4 R 2 .   ? 62.754  89.140  55.835  0.70 33.98 ? 506 PO4 F P   1 
HETATM 8696 O  O1  . PO4 R 2 .   ? 61.908  90.180  55.208  0.70 38.70 ? 506 PO4 F O1  1 
HETATM 8697 O  O2  . PO4 R 2 .   ? 63.814  88.671  54.865  0.70 37.59 ? 506 PO4 F O2  1 
HETATM 8698 O  O3  . PO4 R 2 .   ? 63.434  89.715  57.048  0.70 37.44 ? 506 PO4 F O3  1 
HETATM 8699 O  O4  . PO4 R 2 .   ? 61.775  88.068  56.155  0.70 35.77 ? 506 PO4 F O4  1 
HETATM 8700 O  O   . HOH S 4 .   ? 116.777 76.141  75.621  1.00 28.00 ? 513 HOH A O   1 
HETATM 8701 O  O   . HOH S 4 .   ? 102.491 77.762  57.003  1.00 7.90  ? 514 HOH A O   1 
HETATM 8702 O  O   . HOH S 4 .   ? 91.319  63.723  65.458  1.00 16.59 ? 515 HOH A O   1 
HETATM 8703 O  O   . HOH S 4 .   ? 96.424  66.949  59.691  1.00 4.81  ? 516 HOH A O   1 
HETATM 8704 O  O   . HOH S 4 .   ? 104.521 76.402  63.480  1.00 16.83 ? 517 HOH A O   1 
HETATM 8705 O  O   . HOH S 4 .   ? 91.117  64.424  58.841  1.00 9.50  ? 518 HOH A O   1 
HETATM 8706 O  O   . HOH S 4 .   ? 110.193 66.104  78.898  1.00 17.45 ? 519 HOH A O   1 
HETATM 8707 O  O   . HOH S 4 .   ? 103.261 64.239  80.164  1.00 19.37 ? 520 HOH A O   1 
HETATM 8708 O  O   . HOH S 4 .   ? 107.183 91.905  60.521  1.00 24.44 ? 521 HOH A O   1 
HETATM 8709 O  O   . HOH S 4 .   ? 99.061  91.866  59.159  1.00 28.09 ? 522 HOH A O   1 
HETATM 8710 O  O   . HOH S 4 .   ? 119.205 69.185  69.796  1.00 34.10 ? 523 HOH A O   1 
HETATM 8711 O  O   . HOH S 4 .   ? 103.779 94.875  62.749  1.00 52.18 ? 524 HOH A O   1 
HETATM 8712 O  O   . HOH S 4 .   ? 89.229  80.229  79.341  1.00 38.02 ? 525 HOH A O   1 
HETATM 8713 O  O   . HOH S 4 .   ? 86.302  82.380  66.515  1.00 37.04 ? 526 HOH A O   1 
HETATM 8714 O  O   . HOH S 4 .   ? 87.791  57.741  66.607  1.00 23.13 ? 527 HOH A O   1 
HETATM 8715 O  O   . HOH S 4 .   ? 110.807 78.138  61.781  1.00 16.36 ? 528 HOH A O   1 
HETATM 8716 O  O   . HOH S 4 .   ? 106.403 91.785  76.006  1.00 27.96 ? 529 HOH A O   1 
HETATM 8717 O  O   . HOH S 4 .   ? 95.434  80.435  81.395  1.00 33.70 ? 530 HOH A O   1 
HETATM 8718 O  O   . HOH S 4 .   ? 117.798 93.674  70.261  1.00 30.81 ? 531 HOH A O   1 
HETATM 8719 O  O   . HOH S 4 .   ? 98.999  66.700  81.979  1.00 38.48 ? 532 HOH A O   1 
HETATM 8720 O  O   . HOH S 4 .   ? 89.781  75.311  64.560  1.00 25.59 ? 533 HOH A O   1 
HETATM 8721 O  O   . HOH S 4 .   ? 116.601 92.501  67.175  1.00 31.46 ? 534 HOH A O   1 
HETATM 8722 O  O   . HOH S 4 .   ? 117.799 90.018  61.584  1.00 30.76 ? 535 HOH A O   1 
HETATM 8723 O  O   . HOH S 4 .   ? 95.673  91.750  61.871  1.00 39.92 ? 536 HOH A O   1 
HETATM 8724 O  O   . HOH S 4 .   ? 85.362  66.742  78.544  1.00 36.80 ? 537 HOH A O   1 
HETATM 8725 O  O   . HOH S 4 .   ? 89.238  55.645  65.850  1.00 39.54 ? 538 HOH A O   1 
HETATM 8726 O  O   . HOH S 4 .   ? 94.354  73.112  82.764  1.00 30.20 ? 539 HOH A O   1 
HETATM 8727 O  O   . HOH S 4 .   ? 103.612 82.960  82.854  1.00 29.10 ? 540 HOH A O   1 
HETATM 8728 O  O   . HOH S 4 .   ? 86.470  59.652  70.069  1.00 26.79 ? 541 HOH A O   1 
HETATM 8729 O  O   . HOH S 4 .   ? 96.207  62.499  60.116  1.00 18.81 ? 542 HOH A O   1 
HETATM 8730 O  O   . HOH S 4 .   ? 86.449  71.667  77.235  1.00 38.97 ? 543 HOH A O   1 
HETATM 8731 O  O   . HOH S 4 .   ? 93.006  85.662  77.363  1.00 29.91 ? 544 HOH A O   1 
HETATM 8732 O  O   . HOH S 4 .   ? 120.707 72.499  70.591  1.00 27.23 ? 545 HOH A O   1 
HETATM 8733 O  O   . HOH S 4 .   ? 86.023  80.468  77.085  1.00 35.64 ? 546 HOH A O   1 
HETATM 8734 O  O   . HOH S 4 .   ? 104.493 56.899  72.979  1.00 28.25 ? 547 HOH A O   1 
HETATM 8735 O  O   . HOH S 4 .   ? 87.630  72.705  67.574  1.00 37.02 ? 548 HOH A O   1 
HETATM 8736 O  O   . HOH S 4 .   ? 103.210 90.330  66.416  1.00 17.77 ? 549 HOH A O   1 
HETATM 8737 O  O   . HOH S 4 .   ? 111.792 82.377  65.037  1.00 14.84 ? 550 HOH A O   1 
HETATM 8738 O  O   . HOH S 4 .   ? 90.245  72.037  82.005  1.00 28.99 ? 551 HOH A O   1 
HETATM 8739 O  O   . HOH S 4 .   ? 114.782 96.298  57.642  1.00 44.23 ? 552 HOH A O   1 
HETATM 8740 O  O   . HOH S 4 .   ? 92.687  60.029  76.004  1.00 40.94 ? 553 HOH A O   1 
HETATM 8741 O  O   . HOH S 4 .   ? 90.972  84.706  67.229  1.00 26.16 ? 554 HOH A O   1 
HETATM 8742 O  O   . HOH S 4 .   ? 85.522  66.878  69.440  1.00 27.93 ? 555 HOH A O   1 
HETATM 8743 O  O   . HOH S 4 .   ? 93.301  93.894  67.296  1.00 28.68 ? 556 HOH A O   1 
HETATM 8744 O  O   . HOH S 4 .   ? 97.902  67.122  84.863  1.00 40.42 ? 557 HOH A O   1 
HETATM 8745 O  O   . HOH S 4 .   ? 113.169 97.564  55.153  1.00 42.80 ? 558 HOH A O   1 
HETATM 8746 O  O   . HOH S 4 .   ? 95.602  77.454  83.981  1.00 42.19 ? 559 HOH A O   1 
HETATM 8747 O  O   . HOH S 4 .   ? 93.271  65.374  80.895  1.00 30.22 ? 560 HOH A O   1 
HETATM 8748 O  O   . HOH S 4 .   ? 100.588 95.058  49.694  1.00 51.60 ? 561 HOH A O   1 
HETATM 8749 O  O   . HOH S 4 .   ? 109.515 93.383  63.682  1.00 32.78 ? 562 HOH A O   1 
HETATM 8750 O  O   . HOH S 4 .   ? 104.520 93.719  69.640  1.00 29.68 ? 563 HOH A O   1 
HETATM 8751 O  O   . HOH S 4 .   ? 82.481  78.934  64.718  1.00 42.56 ? 564 HOH A O   1 
HETATM 8752 O  O   . HOH S 4 .   ? 102.012 86.497  78.360  1.00 25.03 ? 565 HOH A O   1 
HETATM 8753 O  O   . HOH S 4 .   ? 95.537  95.331  66.304  1.00 32.22 ? 566 HOH A O   1 
HETATM 8754 O  O   . HOH S 4 .   ? 109.275 94.979  53.216  1.00 45.11 ? 567 HOH A O   1 
HETATM 8755 O  O   . HOH S 4 .   ? 82.533  82.979  56.258  1.00 53.51 ? 568 HOH A O   1 
HETATM 8756 O  O   . HOH S 4 .   ? 86.927  86.475  67.858  1.00 39.51 ? 569 HOH A O   1 
HETATM 8757 O  O   . HOH S 4 .   ? 88.260  84.415  66.452  1.00 41.01 ? 570 HOH A O   1 
HETATM 8758 O  O   . HOH S 4 .   ? 96.989  93.081  59.851  1.00 47.32 ? 571 HOH A O   1 
HETATM 8759 O  O   . HOH S 4 .   ? 111.256 97.544  58.463  1.00 50.81 ? 572 HOH A O   1 
HETATM 8760 O  O   . HOH S 4 .   ? 85.827  80.445  69.242  1.00 41.20 ? 573 HOH A O   1 
HETATM 8761 O  O   . HOH S 4 .   ? 98.615  90.931  73.939  1.00 32.07 ? 574 HOH A O   1 
HETATM 8762 O  O   . HOH S 4 .   ? 83.277  78.980  73.188  1.00 47.44 ? 575 HOH A O   1 
HETATM 8763 O  O   . HOH S 4 .   ? 116.930 74.171  77.165  1.00 36.04 ? 576 HOH A O   1 
HETATM 8764 O  O   . HOH S 4 .   ? 90.053  93.087  53.288  1.00 39.85 ? 577 HOH A O   1 
HETATM 8765 O  O   . HOH S 4 .   ? 95.314  70.586  85.790  1.00 28.30 ? 578 HOH A O   1 
HETATM 8766 O  O   . HOH S 4 .   ? 88.097  57.564  71.263  1.00 40.32 ? 579 HOH A O   1 
HETATM 8767 O  O   . HOH S 4 .   ? 110.304 93.734  73.768  1.00 30.82 ? 580 HOH A O   1 
HETATM 8768 O  O   . HOH S 4 .   ? 102.298 79.194  82.445  1.00 34.02 ? 581 HOH A O   1 
HETATM 8769 O  O   . HOH T 4 .   ? 97.278  56.496  51.475  1.00 12.95 ? 511 HOH B O   1 
HETATM 8770 O  O   . HOH T 4 .   ? 100.422 80.622  57.833  1.00 15.34 ? 512 HOH B O   1 
HETATM 8771 O  O   . HOH T 4 .   ? 102.503 83.611  50.944  1.00 23.92 ? 513 HOH B O   1 
HETATM 8772 O  O   . HOH T 4 .   ? 77.486  67.581  49.258  1.00 26.71 ? 514 HOH B O   1 
HETATM 8773 O  O   . HOH T 4 .   ? 92.789  66.944  58.571  1.00 16.90 ? 515 HOH B O   1 
HETATM 8774 O  O   . HOH T 4 .   ? 100.404 59.621  54.901  1.00 9.33  ? 516 HOH B O   1 
HETATM 8775 O  O   . HOH T 4 .   ? 112.555 78.772  52.846  1.00 23.67 ? 517 HOH B O   1 
HETATM 8776 O  O   . HOH T 4 .   ? 85.921  59.878  49.863  1.00 14.14 ? 518 HOH B O   1 
HETATM 8777 O  O   . HOH T 4 .   ? 98.644  65.802  53.205  1.00 13.52 ? 519 HOH B O   1 
HETATM 8778 O  O   . HOH T 4 .   ? 110.415 54.468  45.963  1.00 25.08 ? 520 HOH B O   1 
HETATM 8779 O  O   . HOH T 4 .   ? 77.852  63.993  49.991  1.00 22.40 ? 521 HOH B O   1 
HETATM 8780 O  O   . HOH T 4 .   ? 110.753 66.337  37.651  1.00 25.12 ? 522 HOH B O   1 
HETATM 8781 O  O   . HOH T 4 .   ? 106.248 80.076  56.441  1.00 20.56 ? 523 HOH B O   1 
HETATM 8782 O  O   . HOH T 4 .   ? 96.618  55.672  63.022  1.00 20.76 ? 524 HOH B O   1 
HETATM 8783 O  O   . HOH T 4 .   ? 83.495  79.505  49.563  1.00 42.45 ? 525 HOH B O   1 
HETATM 8784 O  O   . HOH T 4 .   ? 79.978  71.273  63.730  1.00 33.47 ? 526 HOH B O   1 
HETATM 8785 O  O   . HOH T 4 .   ? 101.549 83.102  57.618  1.00 16.73 ? 527 HOH B O   1 
HETATM 8786 O  O   . HOH T 4 .   ? 96.981  87.206  46.810  1.00 36.51 ? 528 HOH B O   1 
HETATM 8787 O  O   . HOH T 4 .   ? 102.110 46.424  51.394  1.00 34.21 ? 529 HOH B O   1 
HETATM 8788 O  O   . HOH T 4 .   ? 80.813  73.893  40.891  1.00 33.89 ? 530 HOH B O   1 
HETATM 8789 O  O   . HOH T 4 .   ? 86.819  68.923  37.743  1.00 39.21 ? 531 HOH B O   1 
HETATM 8790 O  O   . HOH T 4 .   ? 84.076  62.815  55.029  1.00 26.64 ? 532 HOH B O   1 
HETATM 8791 O  O   . HOH T 4 .   ? 83.172  60.601  53.907  1.00 26.12 ? 533 HOH B O   1 
HETATM 8792 O  O   . HOH T 4 .   ? 86.715  55.114  56.078  1.00 17.03 ? 534 HOH B O   1 
HETATM 8793 O  O   . HOH T 4 .   ? 92.345  81.984  36.571  1.00 36.08 ? 535 HOH B O   1 
HETATM 8794 O  O   . HOH T 4 .   ? 95.336  47.908  49.112  1.00 27.79 ? 536 HOH B O   1 
HETATM 8795 O  O   . HOH T 4 .   ? 92.015  79.335  51.962  1.00 26.04 ? 537 HOH B O   1 
HETATM 8796 O  O   . HOH T 4 .   ? 119.119 52.886  38.753  1.00 38.59 ? 538 HOH B O   1 
HETATM 8797 O  O   . HOH T 4 .   ? 88.183  59.678  38.571  1.00 37.81 ? 539 HOH B O   1 
HETATM 8798 O  O   . HOH T 4 .   ? 104.378 75.528  34.653  1.00 30.17 ? 540 HOH B O   1 
HETATM 8799 O  O   . HOH T 4 .   ? 105.359 55.505  40.970  1.00 33.56 ? 541 HOH B O   1 
HETATM 8800 O  O   . HOH T 4 .   ? 110.988 65.489  35.064  1.00 34.37 ? 542 HOH B O   1 
HETATM 8801 O  O   . HOH T 4 .   ? 83.908  61.090  48.883  1.00 27.99 ? 543 HOH B O   1 
HETATM 8802 O  O   . HOH T 4 .   ? 100.075 87.954  40.160  1.00 46.42 ? 544 HOH B O   1 
HETATM 8803 O  O   . HOH T 4 .   ? 108.174 56.715  41.852  1.00 49.67 ? 545 HOH B O   1 
HETATM 8804 O  O   . HOH T 4 .   ? 110.135 56.315  43.985  1.00 36.81 ? 546 HOH B O   1 
HETATM 8805 O  O   . HOH T 4 .   ? 78.091  67.034  53.590  1.00 29.37 ? 547 HOH B O   1 
HETATM 8806 O  O   . HOH T 4 .   ? 84.654  70.711  38.900  1.00 36.71 ? 548 HOH B O   1 
HETATM 8807 O  O   . HOH T 4 .   ? 90.309  46.132  46.113  1.00 28.60 ? 549 HOH B O   1 
HETATM 8808 O  O   . HOH T 4 .   ? 93.921  48.554  37.891  1.00 47.43 ? 550 HOH B O   1 
HETATM 8809 O  O   . HOH T 4 .   ? 107.886 75.450  36.214  1.00 29.09 ? 551 HOH B O   1 
HETATM 8810 O  O   . HOH T 4 .   ? 78.160  65.533  48.262  1.00 39.21 ? 552 HOH B O   1 
HETATM 8811 O  O   . HOH T 4 .   ? 91.522  49.716  61.209  1.00 31.71 ? 553 HOH B O   1 
HETATM 8812 O  O   . HOH T 4 .   ? 86.918  52.247  42.722  1.00 35.05 ? 554 HOH B O   1 
HETATM 8813 O  O   . HOH T 4 .   ? 113.719 76.300  34.050  1.00 33.55 ? 555 HOH B O   1 
HETATM 8814 O  O   . HOH T 4 .   ? 92.887  82.035  49.018  1.00 32.47 ? 556 HOH B O   1 
HETATM 8815 O  O   . HOH T 4 .   ? 113.010 57.529  43.432  1.00 30.31 ? 557 HOH B O   1 
HETATM 8816 O  O   . HOH T 4 .   ? 108.662 73.066  36.475  1.00 21.67 ? 558 HOH B O   1 
HETATM 8817 O  O   . HOH T 4 .   ? 113.028 79.676  46.271  1.00 50.49 ? 559 HOH B O   1 
HETATM 8818 O  O   . HOH T 4 .   ? 112.144 64.293  39.561  1.00 24.68 ? 560 HOH B O   1 
HETATM 8819 O  O   . HOH T 4 .   ? 85.524  80.337  47.457  1.00 43.89 ? 561 HOH B O   1 
HETATM 8820 O  O   . HOH T 4 .   ? 82.940  63.205  42.273  1.00 25.50 ? 562 HOH B O   1 
HETATM 8821 O  O   . HOH T 4 .   ? 92.778  83.611  39.032  1.00 42.85 ? 563 HOH B O   1 
HETATM 8822 O  O   . HOH T 4 .   ? 107.196 56.418  39.352  1.00 46.52 ? 564 HOH B O   1 
HETATM 8823 O  O   . HOH T 4 .   ? 84.416  58.127  63.753  1.00 27.35 ? 565 HOH B O   1 
HETATM 8824 O  O   . HOH T 4 .   ? 87.831  82.525  44.694  1.00 42.55 ? 566 HOH B O   1 
HETATM 8825 O  O   . HOH T 4 .   ? 82.444  62.638  57.212  1.00 33.20 ? 567 HOH B O   1 
HETATM 8826 O  O   . HOH T 4 .   ? 84.915  72.916  49.017  1.00 38.56 ? 568 HOH B O   1 
HETATM 8827 O  O   . HOH T 4 .   ? 110.422 68.971  31.093  1.00 28.48 ? 569 HOH B O   1 
HETATM 8828 O  O   . HOH T 4 .   ? 92.911  72.204  32.730  1.00 36.45 ? 570 HOH B O   1 
HETATM 8829 O  O   . HOH T 4 .   ? 100.256 49.402  42.572  1.00 47.57 ? 571 HOH B O   1 
HETATM 8830 O  O   . HOH T 4 .   ? 90.639  81.211  50.292  1.00 36.03 ? 572 HOH B O   1 
HETATM 8831 O  O   . HOH T 4 .   ? 104.621 83.895  37.571  1.00 53.15 ? 573 HOH B O   1 
HETATM 8832 O  O   . HOH T 4 .   ? 98.481  65.044  32.071  1.00 45.49 ? 574 HOH B O   1 
HETATM 8833 O  O   . HOH T 4 .   ? 108.904 63.248  37.483  1.00 35.01 ? 575 HOH B O   1 
HETATM 8834 O  O   . HOH T 4 .   ? 81.592  69.279  42.820  1.00 31.44 ? 576 HOH B O   1 
HETATM 8835 O  O   . HOH T 4 .   ? 78.980  66.080  43.205  1.00 36.61 ? 577 HOH B O   1 
HETATM 8836 O  O   . HOH T 4 .   ? 99.757  49.203  37.226  1.00 27.17 ? 578 HOH B O   1 
HETATM 8837 O  O   . HOH T 4 .   ? 79.184  80.471  49.366  1.00 34.41 ? 579 HOH B O   1 
HETATM 8838 O  O   . HOH T 4 .   ? 112.767 57.346  46.532  1.00 45.58 ? 580 HOH B O   1 
HETATM 8839 O  O   . HOH T 4 .   ? 87.470  46.967  60.908  1.00 39.17 ? 581 HOH B O   1 
HETATM 8840 O  O   . HOH T 4 .   ? 77.186  78.022  51.784  1.00 32.82 ? 582 HOH B O   1 
HETATM 8841 O  O   . HOH T 4 .   ? 97.327  58.545  30.666  1.00 40.92 ? 583 HOH B O   1 
HETATM 8842 O  O   . HOH T 4 .   ? 89.895  70.340  35.426  1.00 28.28 ? 584 HOH B O   1 
HETATM 8843 O  O   . HOH T 4 .   ? 105.558 51.481  38.698  1.00 35.87 ? 585 HOH B O   1 
HETATM 8844 O  O   . HOH T 4 .   ? 109.467 52.342  35.927  1.00 37.78 ? 586 HOH B O   1 
HETATM 8845 O  O   . HOH T 4 .   ? 112.376 78.166  36.158  1.00 35.85 ? 587 HOH B O   1 
HETATM 8846 O  O   . HOH T 4 .   ? 106.727 65.625  33.862  1.00 45.32 ? 588 HOH B O   1 
HETATM 8847 O  O   . HOH T 4 .   ? 86.633  56.202  40.579  1.00 28.94 ? 589 HOH B O   1 
HETATM 8848 O  O   . HOH T 4 .   ? 89.909  81.658  46.092  1.00 35.87 ? 590 HOH B O   1 
HETATM 8849 O  O   . HOH T 4 .   ? 76.525  69.089  63.469  1.00 39.52 ? 591 HOH B O   1 
HETATM 8850 O  O   . HOH T 4 .   ? 83.696  63.136  39.646  1.00 37.20 ? 592 HOH B O   1 
HETATM 8851 O  O   . HOH T 4 .   ? 83.577  59.182  55.607  1.00 47.28 ? 593 HOH B O   1 
HETATM 8852 O  O   . HOH T 4 .   ? 94.919  84.471  46.281  1.00 38.86 ? 594 HOH B O   1 
HETATM 8853 O  O   . HOH T 4 .   ? 115.457 76.285  43.611  1.00 23.59 ? 595 HOH B O   1 
HETATM 8854 O  O   . HOH T 4 .   ? 83.026  74.483  49.974  1.00 42.95 ? 596 HOH B O   1 
HETATM 8855 O  O   . HOH T 4 .   ? 91.395  46.997  49.024  1.00 31.53 ? 597 HOH B O   1 
HETATM 8856 O  O   . HOH T 4 .   ? 78.987  70.723  42.504  1.00 39.56 ? 598 HOH B O   1 
HETATM 8857 O  O   . HOH T 4 .   ? 98.400  57.752  33.121  1.00 39.15 ? 599 HOH B O   1 
HETATM 8858 O  O   . HOH T 4 .   ? 104.538 68.485  29.011  1.00 56.82 ? 600 HOH B O   1 
HETATM 8859 O  O   . HOH T 4 .   ? 97.197  87.353  38.258  1.00 35.82 ? 601 HOH B O   1 
HETATM 8860 O  O   . HOH T 4 .   ? 100.691 83.723  34.507  1.00 27.30 ? 602 HOH B O   1 
HETATM 8861 O  O   . HOH T 4 .   ? 106.025 53.238  52.346  1.00 30.95 ? 603 HOH B O   1 
HETATM 8862 O  O   . HOH T 4 .   ? 83.953  59.696  46.935  1.00 28.07 ? 604 HOH B O   1 
HETATM 8863 O  O   . HOH T 4 .   ? 96.008  76.410  33.826  1.00 40.63 ? 605 HOH B O   1 
HETATM 8864 O  O   . HOH U 4 .   ? 128.072 62.162  70.934  1.00 17.81 ? 512 HOH C O   1 
HETATM 8865 O  O   . HOH U 4 .   ? 99.713  54.697  62.348  1.00 27.55 ? 513 HOH C O   1 
HETATM 8866 O  O   . HOH U 4 .   ? 111.524 53.286  54.989  1.00 8.11  ? 514 HOH C O   1 
HETATM 8867 O  O   . HOH U 4 .   ? 117.054 53.466  59.036  1.00 17.17 ? 515 HOH C O   1 
HETATM 8868 O  O   . HOH U 4 .   ? 112.733 65.623  76.901  1.00 33.33 ? 516 HOH C O   1 
HETATM 8869 O  O   . HOH U 4 .   ? 121.007 55.201  53.521  1.00 14.38 ? 517 HOH C O   1 
HETATM 8870 O  O   . HOH U 4 .   ? 122.236 53.087  82.383  1.00 27.84 ? 518 HOH C O   1 
HETATM 8871 O  O   . HOH U 4 .   ? 105.716 54.999  75.063  1.00 21.44 ? 519 HOH C O   1 
HETATM 8872 O  O   . HOH U 4 .   ? 122.896 52.205  53.333  1.00 27.59 ? 520 HOH C O   1 
HETATM 8873 O  O   . HOH U 4 .   ? 100.819 57.381  63.661  1.00 21.21 ? 521 HOH C O   1 
HETATM 8874 O  O   . HOH U 4 .   ? 101.874 48.613  65.730  1.00 30.36 ? 522 HOH C O   1 
HETATM 8875 O  O   . HOH U 4 .   ? 112.980 53.243  45.397  1.00 21.27 ? 523 HOH C O   1 
HETATM 8876 O  O   . HOH U 4 .   ? 111.206 56.212  86.234  1.00 22.60 ? 524 HOH C O   1 
HETATM 8877 O  O   . HOH U 4 .   ? 130.251 64.745  64.995  1.00 13.09 ? 525 HOH C O   1 
HETATM 8878 O  O   . HOH U 4 .   ? 99.929  56.188  67.178  1.00 32.60 ? 526 HOH C O   1 
HETATM 8879 O  O   . HOH U 4 .   ? 110.164 47.813  55.314  1.00 20.68 ? 527 HOH C O   1 
HETATM 8880 O  O   . HOH U 4 .   ? 132.456 48.404  70.350  1.00 44.09 ? 528 HOH C O   1 
HETATM 8881 O  O   . HOH U 4 .   ? 121.336 48.542  40.752  1.00 33.97 ? 529 HOH C O   1 
HETATM 8882 O  O   . HOH U 4 .   ? 105.728 52.578  74.454  1.00 30.56 ? 530 HOH C O   1 
HETATM 8883 O  O   . HOH U 4 .   ? 124.759 66.421  65.554  1.00 29.95 ? 531 HOH C O   1 
HETATM 8884 O  O   . HOH U 4 .   ? 117.705 53.907  51.121  1.00 24.49 ? 532 HOH C O   1 
HETATM 8885 O  O   . HOH U 4 .   ? 118.668 48.263  40.599  1.00 33.51 ? 533 HOH C O   1 
HETATM 8886 O  O   . HOH U 4 .   ? 130.231 49.137  77.850  1.00 39.14 ? 534 HOH C O   1 
HETATM 8887 O  O   . HOH U 4 .   ? 121.688 45.389  79.163  1.00 43.18 ? 535 HOH C O   1 
HETATM 8888 O  O   . HOH U 4 .   ? 130.314 67.330  75.733  1.00 29.80 ? 536 HOH C O   1 
HETATM 8889 O  O   . HOH U 4 .   ? 118.747 39.716  54.702  1.00 32.20 ? 537 HOH C O   1 
HETATM 8890 O  O   . HOH U 4 .   ? 99.587  48.126  51.634  1.00 41.31 ? 538 HOH C O   1 
HETATM 8891 O  O   . HOH U 4 .   ? 100.045 53.787  64.668  1.00 36.24 ? 539 HOH C O   1 
HETATM 8892 O  O   . HOH U 4 .   ? 117.713 66.008  75.505  1.00 32.06 ? 540 HOH C O   1 
HETATM 8893 O  O   . HOH U 4 .   ? 124.969 61.732  85.637  1.00 32.37 ? 541 HOH C O   1 
HETATM 8894 O  O   . HOH U 4 .   ? 113.601 63.842  81.821  1.00 21.66 ? 542 HOH C O   1 
HETATM 8895 O  O   . HOH U 4 .   ? 120.685 62.780  80.706  1.00 29.54 ? 543 HOH C O   1 
HETATM 8896 O  O   . HOH U 4 .   ? 99.943  45.997  51.282  1.00 35.20 ? 544 HOH C O   1 
HETATM 8897 O  O   . HOH U 4 .   ? 107.782 40.332  45.101  1.00 34.50 ? 545 HOH C O   1 
HETATM 8898 O  O   . HOH U 4 .   ? 129.125 64.079  77.990  1.00 44.31 ? 546 HOH C O   1 
HETATM 8899 O  O   . HOH U 4 .   ? 121.905 49.885  51.673  1.00 28.79 ? 547 HOH C O   1 
HETATM 8900 O  O   . HOH U 4 .   ? 112.618 61.022  83.515  1.00 18.70 ? 548 HOH C O   1 
HETATM 8901 O  O   . HOH U 4 .   ? 125.170 47.029  80.525  1.00 33.09 ? 549 HOH C O   1 
HETATM 8902 O  O   . HOH U 4 .   ? 107.105 39.645  70.523  1.00 45.64 ? 550 HOH C O   1 
HETATM 8903 O  O   . HOH U 4 .   ? 101.262 41.720  57.767  1.00 43.90 ? 551 HOH C O   1 
HETATM 8904 O  O   . HOH U 4 .   ? 131.481 38.156  54.949  1.00 49.33 ? 552 HOH C O   1 
HETATM 8905 O  O   . HOH U 4 .   ? 116.438 41.638  48.035  1.00 32.59 ? 553 HOH C O   1 
HETATM 8906 O  O   . HOH U 4 .   ? 122.637 40.429  51.689  1.00 39.34 ? 554 HOH C O   1 
HETATM 8907 O  O   . HOH U 4 .   ? 102.529 36.567  61.999  1.00 45.68 ? 555 HOH C O   1 
HETATM 8908 O  O   . HOH U 4 .   ? 127.789 64.585  80.542  1.00 36.04 ? 556 HOH C O   1 
HETATM 8909 O  O   . HOH U 4 .   ? 112.409 64.878  83.731  1.00 23.63 ? 557 HOH C O   1 
HETATM 8910 O  O   . HOH U 4 .   ? 122.476 45.057  42.165  1.00 37.69 ? 558 HOH C O   1 
HETATM 8911 O  O   . HOH U 4 .   ? 116.369 42.543  39.616  1.00 45.50 ? 559 HOH C O   1 
HETATM 8912 O  O   . HOH U 4 .   ? 112.494 44.968  42.652  1.00 51.00 ? 560 HOH C O   1 
HETATM 8913 O  O   . HOH U 4 .   ? 134.912 47.105  47.641  1.00 38.25 ? 561 HOH C O   1 
HETATM 8914 O  O   . HOH U 4 .   ? 116.026 39.285  49.132  1.00 39.80 ? 562 HOH C O   1 
HETATM 8915 O  O   . HOH U 4 .   ? 99.849  49.901  66.142  1.00 18.97 ? 563 HOH C O   1 
HETATM 8916 O  O   . HOH U 4 .   ? 123.904 36.491  45.209  1.00 29.70 ? 564 HOH C O   1 
HETATM 8917 O  O   . HOH U 4 .   ? 115.686 37.900  42.428  1.00 41.30 ? 565 HOH C O   1 
HETATM 8918 O  O   . HOH U 4 .   ? 101.413 51.834  66.024  1.00 27.64 ? 566 HOH C O   1 
HETATM 8919 O  O   . HOH V 4 .   ? 125.190 62.933  62.930  1.00 13.09 ? 508 HOH D O   1 
HETATM 8920 O  O   . HOH V 4 .   ? 124.786 67.042  57.466  1.00 19.13 ? 509 HOH D O   1 
HETATM 8921 O  O   . HOH V 4 .   ? 117.505 78.862  61.131  1.00 25.32 ? 510 HOH D O   1 
HETATM 8922 O  O   . HOH V 4 .   ? 125.753 76.099  61.382  1.00 14.28 ? 511 HOH D O   1 
HETATM 8923 O  O   . HOH V 4 .   ? 122.904 70.595  71.291  1.00 16.92 ? 512 HOH D O   1 
HETATM 8924 O  O   . HOH V 4 .   ? 129.092 62.961  63.178  1.00 18.59 ? 513 HOH D O   1 
HETATM 8925 O  O   . HOH V 4 .   ? 122.277 71.823  61.506  1.00 22.19 ? 514 HOH D O   1 
HETATM 8926 O  O   . HOH V 4 .   ? 137.832 67.635  65.012  1.00 26.64 ? 515 HOH D O   1 
HETATM 8927 O  O   . HOH V 4 .   ? 114.359 55.263  44.494  1.00 36.85 ? 516 HOH D O   1 
HETATM 8928 O  O   . HOH V 4 .   ? 137.336 72.883  61.648  1.00 24.70 ? 517 HOH D O   1 
HETATM 8929 O  O   . HOH V 4 .   ? 114.955 81.454  54.442  1.00 31.02 ? 518 HOH D O   1 
HETATM 8930 O  O   . HOH V 4 .   ? 134.037 85.366  48.972  1.00 41.04 ? 519 HOH D O   1 
HETATM 8931 O  O   . HOH V 4 .   ? 120.481 52.774  35.421  1.00 35.46 ? 520 HOH D O   1 
HETATM 8932 O  O   . HOH V 4 .   ? 117.348 75.705  41.506  1.00 28.11 ? 521 HOH D O   1 
HETATM 8933 O  O   . HOH V 4 .   ? 120.346 83.067  50.536  1.00 30.02 ? 522 HOH D O   1 
HETATM 8934 O  O   . HOH V 4 .   ? 138.934 70.053  65.531  1.00 32.84 ? 523 HOH D O   1 
HETATM 8935 O  O   . HOH V 4 .   ? 122.830 69.175  73.535  1.00 36.82 ? 524 HOH D O   1 
HETATM 8936 O  O   . HOH V 4 .   ? 113.382 80.307  49.699  1.00 44.99 ? 525 HOH D O   1 
HETATM 8937 O  O   . HOH V 4 .   ? 140.520 61.920  54.696  1.00 33.71 ? 526 HOH D O   1 
HETATM 8938 O  O   . HOH V 4 .   ? 132.348 79.378  75.680  1.00 47.98 ? 527 HOH D O   1 
HETATM 8939 O  O   . HOH V 4 .   ? 118.135 82.103  50.413  1.00 29.02 ? 528 HOH D O   1 
HETATM 8940 O  O   . HOH V 4 .   ? 118.416 59.378  35.888  1.00 20.77 ? 529 HOH D O   1 
HETATM 8941 O  O   . HOH V 4 .   ? 131.121 56.480  35.094  1.00 49.95 ? 530 HOH D O   1 
HETATM 8942 O  O   . HOH V 4 .   ? 142.642 74.370  54.665  1.00 36.72 ? 531 HOH D O   1 
HETATM 8943 O  O   . HOH V 4 .   ? 146.281 65.751  59.588  1.00 33.03 ? 532 HOH D O   1 
HETATM 8944 O  O   . HOH V 4 .   ? 123.147 53.153  45.762  1.00 24.49 ? 533 HOH D O   1 
HETATM 8945 O  O   . HOH V 4 .   ? 138.229 72.049  42.870  1.00 35.88 ? 534 HOH D O   1 
HETATM 8946 O  O   . HOH V 4 .   ? 121.078 50.976  36.813  1.00 42.70 ? 535 HOH D O   1 
HETATM 8947 O  O   . HOH V 4 .   ? 112.767 63.655  37.218  1.00 18.81 ? 536 HOH D O   1 
HETATM 8948 O  O   . HOH V 4 .   ? 147.130 59.925  53.916  1.00 50.78 ? 537 HOH D O   1 
HETATM 8949 O  O   . HOH V 4 .   ? 138.838 66.428  67.328  1.00 27.06 ? 538 HOH D O   1 
HETATM 8950 O  O   . HOH V 4 .   ? 142.431 68.541  47.692  1.00 36.41 ? 539 HOH D O   1 
HETATM 8951 O  O   . HOH V 4 .   ? 141.086 65.322  67.314  1.00 44.72 ? 540 HOH D O   1 
HETATM 8952 O  O   . HOH V 4 .   ? 131.410 82.742  76.618  1.00 48.17 ? 541 HOH D O   1 
HETATM 8953 O  O   . HOH V 4 .   ? 135.084 71.582  75.832  1.00 34.76 ? 542 HOH D O   1 
HETATM 8954 O  O   . HOH V 4 .   ? 136.397 85.310  61.263  1.00 47.48 ? 543 HOH D O   1 
HETATM 8955 O  O   . HOH V 4 .   ? 128.971 76.599  36.969  1.00 41.28 ? 544 HOH D O   1 
HETATM 8956 O  O   . HOH V 4 .   ? 114.469 53.802  42.071  1.00 36.90 ? 545 HOH D O   1 
HETATM 8957 O  O   . HOH V 4 .   ? 132.583 55.947  51.320  1.00 37.32 ? 546 HOH D O   1 
HETATM 8958 O  O   . HOH V 4 .   ? 114.218 59.998  41.045  1.00 27.59 ? 547 HOH D O   1 
HETATM 8959 O  O   . HOH V 4 .   ? 129.583 51.360  41.960  1.00 44.46 ? 548 HOH D O   1 
HETATM 8960 O  O   . HOH V 4 .   ? 125.008 83.202  67.431  1.00 35.97 ? 549 HOH D O   1 
HETATM 8961 O  O   . HOH V 4 .   ? 134.188 67.316  37.536  1.00 49.10 ? 550 HOH D O   1 
HETATM 8962 O  O   . HOH V 4 .   ? 144.421 69.282  65.010  1.00 45.69 ? 551 HOH D O   1 
HETATM 8963 O  O   . HOH V 4 .   ? 140.092 72.567  60.242  1.00 40.29 ? 552 HOH D O   1 
HETATM 8964 O  O   . HOH V 4 .   ? 123.843 84.276  59.691  1.00 50.82 ? 553 HOH D O   1 
HETATM 8965 O  O   . HOH V 4 .   ? 121.636 77.464  36.724  1.00 39.33 ? 554 HOH D O   1 
HETATM 8966 O  O   . HOH V 4 .   ? 127.913 63.089  34.434  1.00 43.18 ? 555 HOH D O   1 
HETATM 8967 O  O   . HOH V 4 .   ? 122.539 56.070  31.476  1.00 35.50 ? 556 HOH D O   1 
HETATM 8968 O  O   . HOH V 4 .   ? 118.696 81.086  45.957  1.00 38.18 ? 557 HOH D O   1 
HETATM 8969 O  O   . HOH V 4 .   ? 117.821 55.844  35.964  1.00 41.42 ? 558 HOH D O   1 
HETATM 8970 O  O   . HOH V 4 .   ? 129.342 58.891  32.077  1.00 45.35 ? 559 HOH D O   1 
HETATM 8971 O  O   . HOH V 4 .   ? 119.992 71.008  30.426  1.00 21.51 ? 560 HOH D O   1 
HETATM 8972 O  O   . HOH V 4 .   ? 131.984 54.585  43.682  1.00 36.40 ? 561 HOH D O   1 
HETATM 8973 O  O   . HOH V 4 .   ? 118.381 79.108  43.908  1.00 27.34 ? 562 HOH D O   1 
HETATM 8974 O  O   . HOH V 4 .   ? 132.546 54.974  47.592  1.00 33.77 ? 563 HOH D O   1 
HETATM 8975 O  O   . HOH V 4 .   ? 122.508 50.428  38.919  1.00 34.03 ? 564 HOH D O   1 
HETATM 8976 O  O   . HOH V 4 .   ? 122.123 77.389  39.356  1.00 38.17 ? 565 HOH D O   1 
HETATM 8977 O  O   . HOH V 4 .   ? 122.154 71.384  33.389  1.00 24.32 ? 566 HOH D O   1 
HETATM 8978 O  O   . HOH V 4 .   ? 120.536 70.559  37.228  1.00 35.04 ? 567 HOH D O   1 
HETATM 8979 O  O   . HOH V 4 .   ? 135.720 58.038  38.885  1.00 43.38 ? 568 HOH D O   1 
HETATM 8980 O  O   . HOH V 4 .   ? 114.853 81.695  48.094  1.00 38.49 ? 569 HOH D O   1 
HETATM 8981 O  O   . HOH V 4 .   ? 120.973 58.914  35.858  1.00 43.73 ? 570 HOH D O   1 
HETATM 8982 O  O   . HOH V 4 .   ? 124.706 56.752  34.343  1.00 48.60 ? 571 HOH D O   1 
HETATM 8983 O  O   . HOH V 4 .   ? 140.904 65.038  42.930  1.00 47.23 ? 572 HOH D O   1 
HETATM 8984 O  O   . HOH V 4 .   ? 133.501 76.212  42.657  1.00 36.77 ? 573 HOH D O   1 
HETATM 8985 O  O   . HOH V 4 .   ? 117.435 77.940  39.639  1.00 24.66 ? 574 HOH D O   1 
HETATM 8986 O  O   . HOH V 4 .   ? 112.705 59.780  38.208  1.00 30.39 ? 575 HOH D O   1 
HETATM 8987 O  O   . HOH V 4 .   ? 132.142 82.854  46.009  1.00 46.07 ? 576 HOH D O   1 
HETATM 8988 O  O   . HOH V 4 .   ? 115.723 81.484  45.672  1.00 40.08 ? 577 HOH D O   1 
HETATM 8989 O  O   . HOH V 4 .   ? 124.464 52.647  35.564  1.00 47.07 ? 578 HOH D O   1 
HETATM 8990 O  O   . HOH V 4 .   ? 134.808 54.449  49.697  1.00 37.11 ? 579 HOH D O   1 
HETATM 8991 O  O   . HOH V 4 .   ? 136.623 74.649  41.981  1.00 38.81 ? 580 HOH D O   1 
HETATM 8992 O  O   . HOH V 4 .   ? 122.985 83.839  65.000  1.00 29.48 ? 581 HOH D O   1 
HETATM 8993 O  O   . HOH V 4 .   ? 120.709 84.963  65.127  1.00 33.05 ? 582 HOH D O   1 
HETATM 8994 O  O   . HOH W 4 .   ? 59.283  112.869 87.858  1.00 24.47 ? 506 HOH E O   1 
HETATM 8995 O  O   . HOH W 4 .   ? 68.118  97.417  62.352  1.00 20.30 ? 507 HOH E O   1 
HETATM 8996 O  O   . HOH W 4 .   ? 68.162  107.220 99.252  1.00 43.04 ? 508 HOH E O   1 
HETATM 8997 O  O   . HOH W 4 .   ? 73.355  94.787  72.208  1.00 22.51 ? 509 HOH E O   1 
HETATM 8998 O  O   . HOH W 4 .   ? 61.564  85.393  72.036  1.00 13.57 ? 510 HOH E O   1 
HETATM 8999 O  O   . HOH W 4 .   ? 76.558  107.070 59.689  1.00 31.57 ? 511 HOH E O   1 
HETATM 9000 O  O   . HOH W 4 .   ? 67.877  90.640  69.562  1.00 27.01 ? 512 HOH E O   1 
HETATM 9001 O  O   . HOH W 4 .   ? 56.666  115.239 81.862  1.00 18.87 ? 513 HOH E O   1 
HETATM 9002 O  O   . HOH W 4 .   ? 65.719  90.729  92.057  1.00 19.02 ? 514 HOH E O   1 
HETATM 9003 O  O   . HOH W 4 .   ? 83.807  116.829 85.399  1.00 39.52 ? 515 HOH E O   1 
HETATM 9004 O  O   . HOH W 4 .   ? 58.630  110.198 79.994  1.00 21.30 ? 516 HOH E O   1 
HETATM 9005 O  O   . HOH W 4 .   ? 66.603  84.457  79.505  1.00 24.53 ? 517 HOH E O   1 
HETATM 9006 O  O   . HOH W 4 .   ? 67.649  102.522 68.130  1.00 35.82 ? 518 HOH E O   1 
HETATM 9007 O  O   . HOH W 4 .   ? 65.748  106.484 100.899 1.00 38.87 ? 519 HOH E O   1 
HETATM 9008 O  O   . HOH W 4 .   ? 63.963  85.494  81.106  1.00 29.45 ? 520 HOH E O   1 
HETATM 9009 O  O   . HOH W 4 .   ? 72.454  86.709  83.070  1.00 29.15 ? 521 HOH E O   1 
HETATM 9010 O  O   . HOH W 4 .   ? 71.469  84.615  83.342  1.00 28.90 ? 522 HOH E O   1 
HETATM 9011 O  O   . HOH W 4 .   ? 55.561  111.888 94.478  1.00 50.22 ? 523 HOH E O   1 
HETATM 9012 O  O   . HOH W 4 .   ? 67.972  98.277  60.001  1.00 31.62 ? 524 HOH E O   1 
HETATM 9013 O  O   . HOH W 4 .   ? 67.093  84.788  82.011  1.00 29.79 ? 525 HOH E O   1 
HETATM 9014 O  O   . HOH W 4 .   ? 65.813  96.710  96.331  1.00 26.69 ? 526 HOH E O   1 
HETATM 9015 O  O   . HOH W 4 .   ? 85.127  89.061  69.402  1.00 44.98 ? 527 HOH E O   1 
HETATM 9016 O  O   . HOH W 4 .   ? 69.353  86.464  83.181  1.00 32.27 ? 528 HOH E O   1 
HETATM 9017 O  O   . HOH W 4 .   ? 68.661  115.446 81.730  1.00 47.89 ? 529 HOH E O   1 
HETATM 9018 O  O   . HOH W 4 .   ? 77.637  90.793  64.101  1.00 28.31 ? 530 HOH E O   1 
HETATM 9019 O  O   . HOH W 4 .   ? 68.296  96.267  72.495  1.00 28.72 ? 531 HOH E O   1 
HETATM 9020 O  O   . HOH W 4 .   ? 60.399  97.104  100.644 0.50 11.21 ? 532 HOH E O   1 
HETATM 9021 O  O   . HOH W 4 .   ? 67.982  101.881 76.103  1.00 21.97 ? 533 HOH E O   1 
HETATM 9022 O  O   . HOH W 4 .   ? 78.527  124.595 70.847  1.00 48.78 ? 534 HOH E O   1 
HETATM 9023 O  O   . HOH W 4 .   ? 80.281  107.501 68.627  1.00 31.08 ? 535 HOH E O   1 
HETATM 9024 O  O   . HOH W 4 .   ? 57.079  97.099  79.306  1.00 24.90 ? 536 HOH E O   1 
HETATM 9025 O  O   . HOH W 4 .   ? 64.439  89.194  90.160  1.00 28.64 ? 537 HOH E O   1 
HETATM 9026 O  O   . HOH W 4 .   ? 75.530  98.187  101.045 0.50 26.74 ? 538 HOH E O   1 
HETATM 9027 O  O   . HOH W 4 .   ? 64.691  84.738  83.869  1.00 33.08 ? 539 HOH E O   1 
HETATM 9028 O  O   . HOH W 4 .   ? 68.310  88.501  89.735  1.00 29.60 ? 540 HOH E O   1 
HETATM 9029 O  O   . HOH W 4 .   ? 78.384  83.969  79.709  1.00 47.09 ? 541 HOH E O   1 
HETATM 9030 O  O   . HOH W 4 .   ? 84.823  95.880  71.736  1.00 34.59 ? 542 HOH E O   1 
HETATM 9031 O  O   . HOH W 4 .   ? 70.488  91.985  96.845  1.00 41.47 ? 543 HOH E O   1 
HETATM 9032 O  O   . HOH W 4 .   ? 67.241  96.480  100.677 1.00 28.09 ? 544 HOH E O   1 
HETATM 9033 O  O   . HOH W 4 .   ? 58.161  95.091  78.340  1.00 34.01 ? 545 HOH E O   1 
HETATM 9034 O  O   . HOH W 4 .   ? 82.582  90.261  68.205  1.00 43.77 ? 546 HOH E O   1 
HETATM 9035 O  O   . HOH W 4 .   ? 58.572  113.932 80.263  1.00 24.27 ? 547 HOH E O   1 
HETATM 9036 O  O   . HOH X 4 .   ? 37.450  87.801  68.046  1.00 22.72 ? 507 HOH F O   1 
HETATM 9037 O  O   . HOH X 4 .   ? 43.389  87.629  73.825  1.00 10.80 ? 508 HOH F O   1 
HETATM 9038 O  O   . HOH X 4 .   ? 41.246  91.405  73.376  1.00 25.03 ? 509 HOH F O   1 
HETATM 9039 O  O   . HOH X 4 .   ? 58.147  69.173  72.220  1.00 20.72 ? 510 HOH F O   1 
HETATM 9040 O  O   . HOH X 4 .   ? 40.339  85.601  74.889  1.00 23.30 ? 511 HOH F O   1 
HETATM 9041 O  O   . HOH X 4 .   ? 54.901  95.183  54.883  1.00 20.29 ? 512 HOH F O   1 
HETATM 9042 O  O   . HOH X 4 .   ? 38.055  86.792  74.829  1.00 14.14 ? 513 HOH F O   1 
HETATM 9043 O  O   . HOH X 4 .   ? 54.986  83.531  70.264  1.00 21.02 ? 514 HOH F O   1 
HETATM 9044 O  O   . HOH X 4 .   ? 45.705  58.519  65.776  1.00 41.00 ? 515 HOH F O   1 
HETATM 9045 O  O   . HOH X 4 .   ? 65.300  81.937  80.026  1.00 20.10 ? 516 HOH F O   1 
HETATM 9046 O  O   . HOH X 4 .   ? 48.031  93.344  53.724  1.00 28.28 ? 517 HOH F O   1 
HETATM 9047 O  O   . HOH X 4 .   ? 61.042  70.979  66.983  1.00 28.59 ? 518 HOH F O   1 
HETATM 9048 O  O   . HOH X 4 .   ? 65.493  90.461  57.699  1.00 33.01 ? 519 HOH F O   1 
HETATM 9049 O  O   . HOH X 4 .   ? 53.313  95.554  71.790  1.00 23.83 ? 520 HOH F O   1 
HETATM 9050 O  O   . HOH X 4 .   ? 64.606  82.210  68.626  1.00 21.35 ? 521 HOH F O   1 
HETATM 9051 O  O   . HOH X 4 .   ? 67.098  95.167  63.433  1.00 31.63 ? 522 HOH F O   1 
HETATM 9052 O  O   . HOH X 4 .   ? 55.991  95.763  71.151  1.00 28.27 ? 523 HOH F O   1 
HETATM 9053 O  O   . HOH X 4 .   ? 49.298  65.144  80.517  1.00 44.64 ? 524 HOH F O   1 
HETATM 9054 O  O   . HOH X 4 .   ? 47.959  69.350  66.318  1.00 28.72 ? 525 HOH F O   1 
HETATM 9055 O  O   . HOH X 4 .   ? 39.792  87.211  53.025  1.00 38.92 ? 526 HOH F O   1 
HETATM 9056 O  O   . HOH X 4 .   ? 59.421  68.837  65.770  1.00 36.12 ? 527 HOH F O   1 
HETATM 9057 O  O   . HOH X 4 .   ? 67.093  88.072  72.181  1.00 35.89 ? 528 HOH F O   1 
HETATM 9058 O  O   . HOH X 4 .   ? 62.309  69.425  81.051  1.00 43.74 ? 529 HOH F O   1 
HETATM 9059 O  O   . HOH X 4 .   ? 65.454  71.786  72.828  1.00 28.72 ? 530 HOH F O   1 
HETATM 9060 O  O   . HOH X 4 .   ? 41.752  98.075  63.126  1.00 35.05 ? 531 HOH F O   1 
HETATM 9061 O  O   . HOH X 4 .   ? 55.287  65.783  71.907  1.00 34.75 ? 532 HOH F O   1 
HETATM 9062 O  O   . HOH X 4 .   ? 46.939  61.621  80.792  1.00 30.65 ? 533 HOH F O   1 
HETATM 9063 O  O   . HOH X 4 .   ? 51.161  67.732  83.749  1.00 44.11 ? 534 HOH F O   1 
HETATM 9064 O  O   . HOH X 4 .   ? 73.503  81.425  70.724  1.00 47.08 ? 535 HOH F O   1 
HETATM 9065 O  O   . HOH X 4 .   ? 31.339  92.607  67.349  1.00 31.34 ? 536 HOH F O   1 
HETATM 9066 O  O   . HOH X 4 .   ? 64.850  71.286  57.589  1.00 22.07 ? 537 HOH F O   1 
HETATM 9067 O  O   . HOH X 4 .   ? 69.824  89.953  55.741  1.00 35.18 ? 538 HOH F O   1 
HETATM 9068 O  O   . HOH X 4 .   ? 36.228  80.094  63.490  1.00 34.94 ? 539 HOH F O   1 
HETATM 9069 O  O   . HOH X 4 .   ? 74.217  72.111  77.160  1.00 38.66 ? 540 HOH F O   1 
HETATM 9070 O  O   . HOH X 4 .   ? 54.160  62.902  66.067  1.00 35.62 ? 541 HOH F O   1 
HETATM 9071 O  O   . HOH X 4 .   ? 62.324  65.718  83.663  1.00 43.39 ? 542 HOH F O   1 
HETATM 9072 O  O   . HOH X 4 .   ? 62.204  67.617  71.949  1.00 47.91 ? 543 HOH F O   1 
HETATM 9073 O  O   . HOH X 4 .   ? 60.295  68.331  70.909  1.00 31.21 ? 544 HOH F O   1 
HETATM 9074 O  O   . HOH X 4 .   ? 64.514  92.790  58.805  1.00 35.53 ? 545 HOH F O   1 
HETATM 9075 O  O   . HOH X 4 .   ? 64.939  81.374  82.310  1.00 35.99 ? 546 HOH F O   1 
HETATM 9076 O  O   . HOH X 4 .   ? 56.536  97.113  56.798  1.00 44.78 ? 547 HOH F O   1 
HETATM 9077 O  O   . HOH X 4 .   ? 48.884  74.935  51.874  1.00 33.97 ? 548 HOH F O   1 
HETATM 9078 O  O   . HOH X 4 .   ? 45.951  67.734  67.021  1.00 34.40 ? 549 HOH F O   1 
HETATM 9079 O  O   . HOH X 4 .   ? 42.767  97.452  53.127  1.00 35.44 ? 550 HOH F O   1 
HETATM 9080 O  O   . HOH X 4 .   ? 48.210  72.584  84.457  1.00 26.54 ? 551 HOH F O   1 
HETATM 9081 O  O   . HOH X 4 .   ? 41.970  76.818  69.029  1.00 31.14 ? 552 HOH F O   1 
HETATM 9082 O  O   . HOH X 4 .   ? 65.695  84.816  50.896  1.00 35.50 ? 553 HOH F O   1 
HETATM 9083 O  O   . HOH X 4 .   ? 65.821  94.885  61.537  1.00 37.17 ? 554 HOH F O   1 
HETATM 9084 O  O   . HOH X 4 .   ? 44.451  72.234  54.434  1.00 38.07 ? 555 HOH F O   1 
HETATM 9085 O  O   . HOH X 4 .   ? 67.705  71.143  70.286  1.00 49.69 ? 556 HOH F O   1 
HETATM 9086 O  O   . HOH X 4 .   ? 44.233  61.014  73.089  1.00 35.74 ? 557 HOH F O   1 
HETATM 9087 O  O   . HOH X 4 .   ? 73.738  78.677  72.424  1.00 29.52 ? 558 HOH F O   1 
HETATM 9088 O  O   . HOH X 4 .   ? 52.260  86.371  47.844  1.00 36.74 ? 559 HOH F O   1 
HETATM 9089 O  O   . HOH X 4 .   ? 71.777  73.477  69.529  1.00 30.33 ? 560 HOH F O   1 
HETATM 9090 O  O   . HOH X 4 .   ? 61.848  79.456  49.976  1.00 54.62 ? 561 HOH F O   1 
HETATM 9091 O  O   . HOH X 4 .   ? 68.692  72.091  63.427  1.00 42.72 ? 562 HOH F O   1 
HETATM 9092 O  O   . HOH X 4 .   ? 73.161  80.361  66.630  1.00 36.54 ? 563 HOH F O   1 
HETATM 9093 O  O   . HOH X 4 .   ? 31.701  88.445  59.643  1.00 48.07 ? 564 HOH F O   1 
HETATM 9094 O  O   . HOH X 4 .   ? 53.788  61.613  63.721  1.00 43.37 ? 565 HOH F O   1 
HETATM 9095 O  O   . HOH X 4 .   ? 56.431  62.899  67.322  1.00 43.73 ? 566 HOH F O   1 
HETATM 9096 O  O   . HOH X 4 .   ? 63.426  97.804  59.265  1.00 34.75 ? 567 HOH F O   1 
HETATM 9097 O  O   . HOH X 4 .   ? 64.111  97.374  64.221  1.00 33.91 ? 568 HOH F O   1 
HETATM 9098 O  O   . HOH X 4 .   ? 44.854  88.757  46.949  1.00 52.27 ? 569 HOH F O   1 
HETATM 9099 O  O   . HOH X 4 .   ? 57.534  68.970  56.464  1.00 33.87 ? 570 HOH F O   1 
HETATM 9100 O  O   . HOH X 4 .   ? 46.710  65.711  57.296  1.00 48.59 ? 571 HOH F O   1 
HETATM 9101 O  O   . HOH X 4 .   ? 38.540  75.381  63.061  1.00 29.82 ? 572 HOH F O   1 
HETATM 9102 O  O   . HOH X 4 .   ? 41.063  63.355  71.023  1.00 47.04 ? 573 HOH F O   1 
HETATM 9103 O  O   . HOH X 4 .   ? 55.781  73.689  52.974  1.00 32.90 ? 574 HOH F O   1 
HETATM 9104 O  O   . HOH X 4 .   ? 56.953  62.228  64.123  1.00 50.01 ? 575 HOH F O   1 
HETATM 9105 O  O   . HOH X 4 .   ? 64.131  68.210  56.935  1.00 44.34 ? 576 HOH F O   1 
HETATM 9106 O  O   . HOH X 4 .   ? 58.997  94.540  54.631  1.00 29.39 ? 577 HOH F O   1 
HETATM 9107 O  O   . HOH X 4 .   ? 58.364  67.552  74.443  1.00 30.55 ? 578 HOH F O   1 
HETATM 9108 O  O   . HOH X 4 .   ? 70.664  87.464  55.886  1.00 38.15 ? 579 HOH F O   1 
HETATM 9109 O  O   . HOH X 4 .   ? 60.168  70.853  55.004  1.00 42.11 ? 580 HOH F O   1 
HETATM 9110 O  O   . HOH X 4 .   ? 63.258  77.328  55.182  1.00 31.57 ? 581 HOH F O   1 
HETATM 9111 O  O   . HOH X 4 .   ? 49.257  95.722  47.866  1.00 54.41 ? 582 HOH F O   1 
HETATM 9112 O  O   . HOH X 4 .   ? 41.656  59.844  65.073  1.00 42.23 ? 583 HOH F O   1 
HETATM 9113 O  O   . HOH X 4 .   ? 41.129  69.993  65.710  1.00 44.40 ? 584 HOH F O   1 
HETATM 9114 O  O   . HOH X 4 .   ? 63.660  96.084  57.573  1.00 33.29 ? 585 HOH F O   1 
HETATM 9115 O  O   . HOH X 4 .   ? 45.882  88.999  51.468  1.00 35.87 ? 586 HOH F O   1 
HETATM 9116 O  O   . HOH X 4 .   ? 44.542  98.477  50.668  1.00 38.08 ? 587 HOH F O   1 
HETATM 9117 O  O   . HOH X 4 .   ? 39.700  76.168  67.263  1.00 31.10 ? 588 HOH F O   1 
HETATM 9118 O  O   . HOH X 4 .   ? 70.315  74.267  77.355  1.00 47.53 ? 589 HOH F O   1 
HETATM 9119 O  O   . HOH X 4 .   ? 38.042  85.850  51.619  1.00 40.20 ? 590 HOH F O   1 
# 
