data_4UA1
# 
_entry.id   4UA1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.387 
_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   4UA1         pdb_00004ua1 10.2210/pdb4ua1/pdb 
WWPDB D_1000203018 ?            ?                   
# 
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 2015-07-22 
2 'Structure model' 1 1 2015-09-16 
3 'Structure model' 1 2 2024-03-20 
# 
_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' 'Database references'  
2 3 'Structure model' 'Data collection'      
3 3 'Structure model' 'Database references'  
4 3 'Structure model' 'Derived calculations' 
# 
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 3 'Structure model' chem_comp_atom        
2 3 'Structure model' chem_comp_bond        
3 3 'Structure model' citation              
4 3 'Structure model' database_2            
5 3 'Structure model' pdbx_struct_oper_list 
6 3 'Structure model' struct_conn           
# 
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  3 'Structure model' '_citation.journal_id_CSD'                  
2  3 'Structure model' '_database_2.pdbx_DOI'                      
3  3 'Structure model' '_database_2.pdbx_database_accession'       
4  3 'Structure model' '_pdbx_struct_oper_list.symmetry_operation' 
5  3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'           
6  3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'           
7  3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'            
8  3 'Structure model' '_struct_conn.ptnr1_label_asym_id'          
9  3 'Structure model' '_struct_conn.ptnr1_label_atom_id'          
10 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'          
11 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'           
12 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'           
13 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'           
14 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'            
15 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'          
16 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'          
17 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'          
18 3 'Structure model' '_struct_conn.ptnr2_label_seq_id'           
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        4UA1 
_pdbx_database_status.recvd_initial_deposition_date   2014-08-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.db_id          4UA2 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Chang, C.C.' 1 
'Lin, L.Y.'   2 
'Zou, X.W.'   3 
'Huang, C.C.' 4 
'Chan, N.L.'  5 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nucleic Acids Res.' 
_citation.journal_id_ASTM           NARHAD 
_citation.journal_id_CSD            0389 
_citation.journal_id_ISSN           1362-4962 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            43 
_citation.language                  ? 
_citation.page_first                7612 
_citation.page_last                 7623 
_citation.title                     
'Structural basis of the mercury(II)-mediated conformational switching of the dual-function transcriptional regulator MerR' 
_citation.year                      2015 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1093/nar/gkv681 
_citation.pdbx_database_id_PubMed   26150423 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chang, C.C.' 1 ? 
primary 'Lin, L.Y.'   2 ? 
primary 'Zou, X.W.'   3 ? 
primary 'Huang, C.C.' 4 ? 
primary 'Chan, N.L.'  5 ? 
# 
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 'Regulatory protein' 15998.743 2  ? ? ? ? 
2 non-polymer syn 'MERCURY (II) ION'   200.590   2  ? ? ? ? 
3 water       nat water                18.015    38 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKFRIGELADKCGVNKETIRYYERLGLIPEPERTEKGYRMYSQQTVDRLHFIKRMQELGFTLNEIDKLLGVVDRDEAKCR
DMYDFTILKIEDIQRKIEDLKRIERMLMDLKERCPENKDIYECPIIETLMKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKFRIGELADKCGVNKETIRYYERLGLIPEPERTEKGYRMYSQQTVDRLHFIKRMQELGFTLNEIDKLLGVVDRDEAKCR
DMYDFTILKIEDIQRKIEDLKRIERMLMDLKERCPENKDIYECPIIETLMKK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MERCURY (II) ION' HG  
3 water              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   PHE n 
1 4   ARG n 
1 5   ILE n 
1 6   GLY n 
1 7   GLU n 
1 8   LEU n 
1 9   ALA n 
1 10  ASP n 
1 11  LYS n 
1 12  CYS n 
1 13  GLY n 
1 14  VAL n 
1 15  ASN n 
1 16  LYS n 
1 17  GLU n 
1 18  THR n 
1 19  ILE n 
1 20  ARG n 
1 21  TYR n 
1 22  TYR n 
1 23  GLU n 
1 24  ARG n 
1 25  LEU n 
1 26  GLY n 
1 27  LEU n 
1 28  ILE n 
1 29  PRO n 
1 30  GLU n 
1 31  PRO n 
1 32  GLU n 
1 33  ARG n 
1 34  THR n 
1 35  GLU n 
1 36  LYS n 
1 37  GLY n 
1 38  TYR n 
1 39  ARG n 
1 40  MET n 
1 41  TYR n 
1 42  SER n 
1 43  GLN n 
1 44  GLN n 
1 45  THR n 
1 46  VAL n 
1 47  ASP n 
1 48  ARG n 
1 49  LEU n 
1 50  HIS n 
1 51  PHE n 
1 52  ILE n 
1 53  LYS n 
1 54  ARG n 
1 55  MET n 
1 56  GLN n 
1 57  GLU n 
1 58  LEU n 
1 59  GLY n 
1 60  PHE n 
1 61  THR n 
1 62  LEU n 
1 63  ASN n 
1 64  GLU n 
1 65  ILE n 
1 66  ASP n 
1 67  LYS n 
1 68  LEU n 
1 69  LEU n 
1 70  GLY n 
1 71  VAL n 
1 72  VAL n 
1 73  ASP n 
1 74  ARG n 
1 75  ASP n 
1 76  GLU n 
1 77  ALA n 
1 78  LYS n 
1 79  CYS n 
1 80  ARG n 
1 81  ASP n 
1 82  MET n 
1 83  TYR n 
1 84  ASP n 
1 85  PHE n 
1 86  THR n 
1 87  ILE n 
1 88  LEU n 
1 89  LYS n 
1 90  ILE n 
1 91  GLU n 
1 92  ASP n 
1 93  ILE n 
1 94  GLN n 
1 95  ARG n 
1 96  LYS n 
1 97  ILE n 
1 98  GLU n 
1 99  ASP n 
1 100 LEU n 
1 101 LYS n 
1 102 ARG n 
1 103 ILE n 
1 104 GLU n 
1 105 ARG n 
1 106 MET n 
1 107 LEU n 
1 108 MET n 
1 109 ASP n 
1 110 LEU n 
1 111 LYS n 
1 112 GLU n 
1 113 ARG n 
1 114 CYS n 
1 115 PRO n 
1 116 GLU n 
1 117 ASN n 
1 118 LYS n 
1 119 ASP n 
1 120 ILE n 
1 121 TYR n 
1 122 GLU n 
1 123 CYS n 
1 124 PRO n 
1 125 ILE n 
1 126 ILE n 
1 127 GLU n 
1 128 THR n 
1 129 LEU n 
1 130 MET n 
1 131 LYS n 
1 132 LYS 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   132 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 merR 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    MB1 
_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      'Bacillus megaterium' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1404 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL-21(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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   21b-MerR 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET-21b 
_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 
GLN 'L-peptide linking' y GLUTAMINE          ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'    ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE            ? 'C2 H5 N O2'     75.067  
HG  non-polymer         . 'MERCURY (II) ION' ? 'Hg 2'           200.590 
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 
PHE 'L-peptide linking' y PHENYLALANINE      ? 'C9 H11 N O2'    165.189 
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 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   ?   ?   ?   A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  CYS 12  12  12  CYS CYS A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  GLU 32  32  ?   ?   ?   A . n 
A 1 33  ARG 33  33  ?   ?   ?   A . n 
A 1 34  THR 34  34  ?   ?   ?   A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  MET 40  40  40  MET MET A . n 
A 1 41  TYR 41  41  ?   ?   ?   A . n 
A 1 42  SER 42  42  ?   ?   ?   A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  GLN 44  44  44  GLN GLN A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  HIS 50  50  50  HIS HIS A . n 
A 1 51  PHE 51  51  51  PHE PHE A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  MET 55  55  55  MET MET A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ARG 74  74  74  ARG ARG A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  CYS 79  79  79  CYS CYS A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 MET 108 108 108 MET MET A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 CYS 114 114 114 CYS CYS A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 ASP 119 119 119 ASP ASP A . n 
A 1 120 ILE 120 120 120 ILE ILE A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 CYS 123 123 123 CYS CYS A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 LYS 131 131 131 LYS LYS A . n 
A 1 132 LYS 132 132 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LYS 2   2   ?   ?   ?   B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   ALA 9   9   9   ALA ALA B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  CYS 12  12  12  CYS CYS B . n 
B 1 13  GLY 13  13  13  GLY GLY B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  LYS 16  16  16  LYS LYS B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  THR 18  18  18  THR THR B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  TYR 22  22  22  TYR TYR B . n 
B 1 23  GLU 23  23  23  GLU GLU B . n 
B 1 24  ARG 24  24  24  ARG ARG B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ILE 28  28  28  ILE ILE B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  GLU 30  30  30  GLU GLU B . n 
B 1 31  PRO 31  31  31  PRO PRO B . n 
B 1 32  GLU 32  32  32  GLU GLU B . n 
B 1 33  ARG 33  33  ?   ?   ?   B . n 
B 1 34  THR 34  34  ?   ?   ?   B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  ARG 39  39  39  ARG ARG B . n 
B 1 40  MET 40  40  40  MET MET B . n 
B 1 41  TYR 41  41  ?   ?   ?   B . n 
B 1 42  SER 42  42  ?   ?   ?   B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  GLN 44  44  44  GLN GLN B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  ARG 48  48  48  ARG ARG B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  HIS 50  50  50  HIS HIS B . n 
B 1 51  PHE 51  51  51  PHE PHE B . n 
B 1 52  ILE 52  52  52  ILE ILE B . n 
B 1 53  LYS 53  53  53  LYS LYS B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  MET 55  55  55  MET MET B . n 
B 1 56  GLN 56  56  56  GLN GLN B . n 
B 1 57  GLU 57  57  57  GLU GLU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  PHE 60  60  60  PHE PHE B . n 
B 1 61  THR 61  61  61  THR THR B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  ILE 65  65  65  ILE ILE B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  LYS 67  67  67  LYS LYS B . n 
B 1 68  LEU 68  68  68  LEU LEU B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  ASP 73  73  73  ASP ASP B . n 
B 1 74  ARG 74  74  74  ARG ARG B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  GLU 76  76  76  GLU GLU B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  CYS 79  79  79  CYS CYS B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  TYR 83  83  83  TYR TYR B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  PHE 85  85  85  PHE PHE B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  ILE 87  87  87  ILE ILE B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  ILE 90  90  90  ILE ILE B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  ILE 93  93  93  ILE ILE B . n 
B 1 94  GLN 94  94  94  GLN GLN B . n 
B 1 95  ARG 95  95  95  ARG ARG B . n 
B 1 96  LYS 96  96  96  LYS LYS B . n 
B 1 97  ILE 97  97  97  ILE ILE B . n 
B 1 98  GLU 98  98  98  GLU GLU B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 LYS 101 101 101 LYS LYS B . n 
B 1 102 ARG 102 102 102 ARG ARG B . n 
B 1 103 ILE 103 103 103 ILE ILE B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 MET 106 106 106 MET MET B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 MET 108 108 108 MET MET B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 GLU 112 112 112 GLU GLU B . n 
B 1 113 ARG 113 113 113 ARG ARG B . n 
B 1 114 CYS 114 114 114 CYS CYS B . n 
B 1 115 PRO 115 115 115 PRO PRO B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 LYS 118 118 118 LYS LYS B . n 
B 1 119 ASP 119 119 119 ASP ASP B . n 
B 1 120 ILE 120 120 120 ILE ILE B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 GLU 122 122 122 GLU GLU B . n 
B 1 123 CYS 123 123 123 CYS CYS B . n 
B 1 124 PRO 124 124 124 PRO PRO B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 ILE 126 126 126 ILE ILE B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 THR 128 128 128 THR THR B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 LYS 131 131 131 LYS LYS B . n 
B 1 132 LYS 132 132 ?   ?   ?   B . 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 
C 2 HG  1  201 1  HG  HG  A . 
D 2 HG  1  202 2  HG  HG  A . 
E 3 HOH 1  301 11 HOH HOH A . 
E 3 HOH 2  302 21 HOH HOH A . 
E 3 HOH 3  303 14 HOH HOH A . 
E 3 HOH 4  304 18 HOH HOH A . 
E 3 HOH 5  305 24 HOH HOH A . 
E 3 HOH 6  306 19 HOH HOH A . 
E 3 HOH 7  307 49 HOH HOH A . 
E 3 HOH 8  308 10 HOH HOH A . 
E 3 HOH 9  309 2  HOH HOH A . 
E 3 HOH 10 310 5  HOH HOH A . 
E 3 HOH 11 311 36 HOH HOH A . 
E 3 HOH 12 312 16 HOH HOH A . 
E 3 HOH 13 313 68 HOH HOH A . 
E 3 HOH 14 314 30 HOH HOH A . 
E 3 HOH 15 315 43 HOH HOH A . 
E 3 HOH 16 316 3  HOH HOH A . 
E 3 HOH 17 317 26 HOH HOH A . 
E 3 HOH 18 318 37 HOH HOH A . 
E 3 HOH 19 319 38 HOH HOH A . 
E 3 HOH 20 320 44 HOH HOH A . 
E 3 HOH 21 321 45 HOH HOH A . 
E 3 HOH 22 322 70 HOH HOH A . 
E 3 HOH 23 323 71 HOH HOH A . 
F 3 HOH 1  201 69 HOH HOH B . 
F 3 HOH 2  202 20 HOH HOH B . 
F 3 HOH 3  203 4  HOH HOH B . 
F 3 HOH 4  204 6  HOH HOH B . 
F 3 HOH 5  205 32 HOH HOH B . 
F 3 HOH 6  206 17 HOH HOH B . 
F 3 HOH 7  207 78 HOH HOH B . 
F 3 HOH 8  208 55 HOH HOH B . 
F 3 HOH 9  209 28 HOH HOH B . 
F 3 HOH 10 210 7  HOH HOH B . 
F 3 HOH 11 211 9  HOH HOH B . 
F 3 HOH 12 212 22 HOH HOH B . 
F 3 HOH 13 213 35 HOH HOH B . 
F 3 HOH 14 214 50 HOH HOH B . 
F 3 HOH 15 215 67 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A PHE 3   ? CG  ? A PHE 3   CG  
2   1 Y 1 A PHE 3   ? CD1 ? A PHE 3   CD1 
3   1 Y 1 A PHE 3   ? CD2 ? A PHE 3   CD2 
4   1 Y 1 A PHE 3   ? CE1 ? A PHE 3   CE1 
5   1 Y 1 A PHE 3   ? CE2 ? A PHE 3   CE2 
6   1 Y 1 A PHE 3   ? CZ  ? A PHE 3   CZ  
7   1 Y 1 A ARG 4   ? CZ  ? A ARG 4   CZ  
8   1 Y 1 A ARG 4   ? NH1 ? A ARG 4   NH1 
9   1 Y 1 A ARG 4   ? NH2 ? A ARG 4   NH2 
10  1 Y 1 A ILE 5   ? CG1 ? A ILE 5   CG1 
11  1 Y 1 A ILE 5   ? CG2 ? A ILE 5   CG2 
12  1 Y 1 A ILE 5   ? CD1 ? A ILE 5   CD1 
13  1 Y 1 A GLU 7   ? CG  ? A GLU 7   CG  
14  1 Y 1 A GLU 7   ? CD  ? A GLU 7   CD  
15  1 Y 1 A GLU 7   ? OE1 ? A GLU 7   OE1 
16  1 Y 1 A GLU 7   ? OE2 ? A GLU 7   OE2 
17  1 Y 1 A LEU 8   ? CG  ? A LEU 8   CG  
18  1 Y 1 A LEU 8   ? CD1 ? A LEU 8   CD1 
19  1 Y 1 A LEU 8   ? CD2 ? A LEU 8   CD2 
20  1 Y 1 A ASP 10  ? CG  ? A ASP 10  CG  
21  1 Y 1 A ASP 10  ? OD1 ? A ASP 10  OD1 
22  1 Y 1 A ASP 10  ? OD2 ? A ASP 10  OD2 
23  1 Y 1 A LYS 11  ? CG  ? A LYS 11  CG  
24  1 Y 1 A LYS 11  ? CD  ? A LYS 11  CD  
25  1 Y 1 A LYS 11  ? CE  ? A LYS 11  CE  
26  1 Y 1 A LYS 11  ? NZ  ? A LYS 11  NZ  
27  1 Y 1 A LYS 16  ? CE  ? A LYS 16  CE  
28  1 Y 1 A LYS 16  ? NZ  ? A LYS 16  NZ  
29  1 Y 1 A THR 18  ? OG1 ? A THR 18  OG1 
30  1 Y 1 A THR 18  ? CG2 ? A THR 18  CG2 
31  1 Y 1 A TYR 21  ? CD1 ? A TYR 21  CD1 
32  1 Y 1 A TYR 21  ? CD2 ? A TYR 21  CD2 
33  1 Y 1 A TYR 21  ? CE1 ? A TYR 21  CE1 
34  1 Y 1 A TYR 21  ? CE2 ? A TYR 21  CE2 
35  1 Y 1 A TYR 21  ? CZ  ? A TYR 21  CZ  
36  1 Y 1 A TYR 21  ? OH  ? A TYR 21  OH  
37  1 Y 1 A TYR 22  ? CG  ? A TYR 22  CG  
38  1 Y 1 A TYR 22  ? CD1 ? A TYR 22  CD1 
39  1 Y 1 A TYR 22  ? CD2 ? A TYR 22  CD2 
40  1 Y 1 A TYR 22  ? CE1 ? A TYR 22  CE1 
41  1 Y 1 A TYR 22  ? CE2 ? A TYR 22  CE2 
42  1 Y 1 A TYR 22  ? CZ  ? A TYR 22  CZ  
43  1 Y 1 A TYR 22  ? OH  ? A TYR 22  OH  
44  1 Y 1 A ARG 24  ? CG  ? A ARG 24  CG  
45  1 Y 1 A ARG 24  ? CD  ? A ARG 24  CD  
46  1 Y 1 A ARG 24  ? NE  ? A ARG 24  NE  
47  1 Y 1 A ARG 24  ? CZ  ? A ARG 24  CZ  
48  1 Y 1 A ARG 24  ? NH1 ? A ARG 24  NH1 
49  1 Y 1 A ARG 24  ? NH2 ? A ARG 24  NH2 
50  1 Y 1 A LEU 27  ? CG  ? A LEU 27  CG  
51  1 Y 1 A LEU 27  ? CD1 ? A LEU 27  CD1 
52  1 Y 1 A LEU 27  ? CD2 ? A LEU 27  CD2 
53  1 Y 1 A GLU 30  ? CG  ? A GLU 30  CG  
54  1 Y 1 A GLU 30  ? CD  ? A GLU 30  CD  
55  1 Y 1 A GLU 30  ? OE1 ? A GLU 30  OE1 
56  1 Y 1 A GLU 30  ? OE2 ? A GLU 30  OE2 
57  1 Y 1 A PRO 31  ? CG  ? A PRO 31  CG  
58  1 Y 1 A PRO 31  ? CD  ? A PRO 31  CD  
59  1 Y 1 A GLU 35  ? CG  ? A GLU 35  CG  
60  1 Y 1 A GLU 35  ? CD  ? A GLU 35  CD  
61  1 Y 1 A GLU 35  ? OE1 ? A GLU 35  OE1 
62  1 Y 1 A GLU 35  ? OE2 ? A GLU 35  OE2 
63  1 Y 1 A LYS 36  ? CG  ? A LYS 36  CG  
64  1 Y 1 A LYS 36  ? CD  ? A LYS 36  CD  
65  1 Y 1 A LYS 36  ? CE  ? A LYS 36  CE  
66  1 Y 1 A LYS 36  ? NZ  ? A LYS 36  NZ  
67  1 Y 1 A TYR 38  ? CG  ? A TYR 38  CG  
68  1 Y 1 A TYR 38  ? CD1 ? A TYR 38  CD1 
69  1 Y 1 A TYR 38  ? CD2 ? A TYR 38  CD2 
70  1 Y 1 A TYR 38  ? CE1 ? A TYR 38  CE1 
71  1 Y 1 A TYR 38  ? CE2 ? A TYR 38  CE2 
72  1 Y 1 A TYR 38  ? CZ  ? A TYR 38  CZ  
73  1 Y 1 A TYR 38  ? OH  ? A TYR 38  OH  
74  1 Y 1 A ARG 39  ? CG  ? A ARG 39  CG  
75  1 Y 1 A ARG 39  ? CD  ? A ARG 39  CD  
76  1 Y 1 A ARG 39  ? NE  ? A ARG 39  NE  
77  1 Y 1 A ARG 39  ? CZ  ? A ARG 39  CZ  
78  1 Y 1 A ARG 39  ? NH1 ? A ARG 39  NH1 
79  1 Y 1 A ARG 39  ? NH2 ? A ARG 39  NH2 
80  1 Y 1 A GLN 44  ? CD  ? A GLN 44  CD  
81  1 Y 1 A GLN 44  ? OE1 ? A GLN 44  OE1 
82  1 Y 1 A GLN 44  ? NE2 ? A GLN 44  NE2 
83  1 Y 1 A LYS 131 ? CG  ? A LYS 131 CG  
84  1 Y 1 A LYS 131 ? CD  ? A LYS 131 CD  
85  1 Y 1 A LYS 131 ? CE  ? A LYS 131 CE  
86  1 Y 1 A LYS 131 ? NZ  ? A LYS 131 NZ  
87  1 Y 1 B ARG 4   ? CZ  ? B ARG 4   CZ  
88  1 Y 1 B ARG 4   ? NH1 ? B ARG 4   NH1 
89  1 Y 1 B ARG 4   ? NH2 ? B ARG 4   NH2 
90  1 Y 1 B ILE 5   ? CG1 ? B ILE 5   CG1 
91  1 Y 1 B ILE 5   ? CG2 ? B ILE 5   CG2 
92  1 Y 1 B ILE 5   ? CD1 ? B ILE 5   CD1 
93  1 Y 1 B GLU 7   ? CG  ? B GLU 7   CG  
94  1 Y 1 B GLU 7   ? CD  ? B GLU 7   CD  
95  1 Y 1 B GLU 7   ? OE1 ? B GLU 7   OE1 
96  1 Y 1 B GLU 7   ? OE2 ? B GLU 7   OE2 
97  1 Y 1 B ASP 10  ? CG  ? B ASP 10  CG  
98  1 Y 1 B ASP 10  ? OD1 ? B ASP 10  OD1 
99  1 Y 1 B ASP 10  ? OD2 ? B ASP 10  OD2 
100 1 Y 1 B LYS 11  ? CG  ? B LYS 11  CG  
101 1 Y 1 B LYS 11  ? CD  ? B LYS 11  CD  
102 1 Y 1 B LYS 11  ? CE  ? B LYS 11  CE  
103 1 Y 1 B LYS 11  ? NZ  ? B LYS 11  NZ  
104 1 Y 1 B LYS 16  ? CG  ? B LYS 16  CG  
105 1 Y 1 B LYS 16  ? CD  ? B LYS 16  CD  
106 1 Y 1 B LYS 16  ? CE  ? B LYS 16  CE  
107 1 Y 1 B LYS 16  ? NZ  ? B LYS 16  NZ  
108 1 Y 1 B THR 18  ? OG1 ? B THR 18  OG1 
109 1 Y 1 B THR 18  ? CG2 ? B THR 18  CG2 
110 1 Y 1 B TYR 22  ? CD1 ? B TYR 22  CD1 
111 1 Y 1 B TYR 22  ? CE1 ? B TYR 22  CE1 
112 1 Y 1 B TYR 22  ? CZ  ? B TYR 22  CZ  
113 1 Y 1 B TYR 22  ? OH  ? B TYR 22  OH  
114 1 Y 1 B GLU 30  ? CG  ? B GLU 30  CG  
115 1 Y 1 B GLU 30  ? CD  ? B GLU 30  CD  
116 1 Y 1 B GLU 30  ? OE1 ? B GLU 30  OE1 
117 1 Y 1 B GLU 30  ? OE2 ? B GLU 30  OE2 
118 1 Y 1 B PRO 31  ? CG  ? B PRO 31  CG  
119 1 Y 1 B PRO 31  ? CD  ? B PRO 31  CD  
120 1 Y 1 B GLU 32  ? CG  ? B GLU 32  CG  
121 1 Y 1 B GLU 32  ? CD  ? B GLU 32  CD  
122 1 Y 1 B GLU 32  ? OE1 ? B GLU 32  OE1 
123 1 Y 1 B GLU 32  ? OE2 ? B GLU 32  OE2 
124 1 Y 1 B GLU 35  ? CG  ? B GLU 35  CG  
125 1 Y 1 B GLU 35  ? CD  ? B GLU 35  CD  
126 1 Y 1 B GLU 35  ? OE1 ? B GLU 35  OE1 
127 1 Y 1 B GLU 35  ? OE2 ? B GLU 35  OE2 
128 1 Y 1 B LYS 36  ? CG  ? B LYS 36  CG  
129 1 Y 1 B LYS 36  ? CD  ? B LYS 36  CD  
130 1 Y 1 B LYS 36  ? CE  ? B LYS 36  CE  
131 1 Y 1 B LYS 36  ? NZ  ? B LYS 36  NZ  
132 1 Y 1 B TYR 38  ? CG  ? B TYR 38  CG  
133 1 Y 1 B TYR 38  ? CD1 ? B TYR 38  CD1 
134 1 Y 1 B TYR 38  ? CD2 ? B TYR 38  CD2 
135 1 Y 1 B TYR 38  ? CE1 ? B TYR 38  CE1 
136 1 Y 1 B TYR 38  ? CE2 ? B TYR 38  CE2 
137 1 Y 1 B TYR 38  ? CZ  ? B TYR 38  CZ  
138 1 Y 1 B TYR 38  ? OH  ? B TYR 38  OH  
139 1 Y 1 B ARG 39  ? NE  ? B ARG 39  NE  
140 1 Y 1 B ARG 39  ? CZ  ? B ARG 39  CZ  
141 1 Y 1 B ARG 39  ? NH1 ? B ARG 39  NH1 
142 1 Y 1 B ARG 39  ? NH2 ? B ARG 39  NH2 
143 1 Y 1 B LYS 67  ? CG  ? B LYS 67  CG  
144 1 Y 1 B LYS 67  ? CD  ? B LYS 67  CD  
145 1 Y 1 B LYS 67  ? CE  ? B LYS 67  CE  
146 1 Y 1 B LYS 67  ? NZ  ? B LYS 67  NZ  
147 1 Y 1 B LYS 131 ? CG  ? B LYS 131 CG  
148 1 Y 1 B LYS 131 ? CD  ? B LYS 131 CD  
149 1 Y 1 B LYS 131 ? CE  ? B LYS 131 CE  
150 1 Y 1 B LYS 131 ? NZ  ? B LYS 131 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(phenix.refine: 1.9_1692)' 1 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? Blu-Ice  ? ? ? .                           2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                           3 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                           4 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                           5 
# 
_cell.entry_id           4UA1 
_cell.length_a           70.005 
_cell.length_b           70.556 
_cell.length_c           71.614 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4UA1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                16 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   4UA1 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.76 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         55.49 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'di-Ammonium hydrogen citrate, PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-01-05 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'LN2-Cooled, Fixed-Exit Double Crystal Monochromator(crystal type Si(111))' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             MAD 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
loop_
_diffrn_radiation_wavelength.id 
_diffrn_radiation_wavelength.wavelength 
_diffrn_radiation_wavelength.wt 
1 0.9922 1.0 
2 0.9792 1.0 
3 0.9610 1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSRRC BEAMLINE BL13B1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        '0.9922, 0.9792, 0.9610' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL13B1 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         4UA1 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.56 
_reflns.d_resolution_low                 25.13 
_reflns.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.number_all                       ? 
_reflns.number_obs                       11808 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.9 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  11.7 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            19.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 4UA1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.56 
_refine.ls_d_res_low                             25.130 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     11681 
_refine.ls_number_reflns_R_free                  1166 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.69 
_refine.ls_percent_reflns_R_free                 9.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2316 
_refine.ls_R_factor_R_free                       0.2870 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2255 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       MLHL 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.21 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.32 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1943 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             38 
_refine_hist.number_atoms_total               1983 
_refine_hist.d_res_high                       2.56 
_refine_hist.d_res_low                        25.130 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  ? 1963 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.672  ? 2616 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.660 ? 763  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.064  ? 301  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 340  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
'X-RAY DIFFRACTION' 2.5672 2.6839  . . 134 1246 96.00  . . . 0.3497 . 0.2279 . . . . . . . . 
'X-RAY DIFFRACTION' 2.6839 2.8252  . . 157 1257 97.00  . . . 0.3117 . 0.2373 . . . . . . . . 
'X-RAY DIFFRACTION' 2.8252 3.0019  . . 136 1278 98.00  . . . 0.2808 . 0.2358 . . . . . . . . 
'X-RAY DIFFRACTION' 3.0019 3.2333  . . 152 1302 99.00  . . . 0.3024 . 0.2284 . . . . . . . . 
'X-RAY DIFFRACTION' 3.2333 3.5579  . . 144 1315 100.00 . . . 0.2511 . 0.2236 . . . . . . . . 
'X-RAY DIFFRACTION' 3.5579 4.0708  . . 146 1323 100.00 . . . 0.2519 . 0.2143 . . . . . . . . 
'X-RAY DIFFRACTION' 4.0708 5.1216  . . 151 1352 100.00 . . . 0.3158 . 0.2116 . . . . . . . . 
'X-RAY DIFFRACTION' 5.1216 25.1314 . . 146 1442 100.00 . . . 0.2812 . 0.2396 . . . . . . . . 
# 
_struct.entry_id                     4UA1 
_struct.title                        
'Crystal structure of dual function transcriptional regulator MerR form Bacillus megaterium MB1 in complex with mercury (II) ion' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        4UA1 
_struct_keywords.text            'Metalloregulatory protein, DNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'DNA BINDING PROTEIN' 
# 
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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q799U3_BACME 
_struct_ref.pdbx_db_accession          Q799U3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKFRIGELADKCGVNKETIRYYERLGLIPEPERTEKGYRMYSQQTVDRLHFIKRMQELGFTLNEIDKLLGVVDRDEAKCR
DMYDFTILKIEDIQRKIEDLKRIERMLMDLKERCPENKDIYECPIIETLMKK
;
_struct_ref.pdbx_align_begin           1 
# 
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 4UA1 A 1 ? 132 ? Q799U3 1 ? 132 ? 1 132 
2 1 4UA1 B 1 ? 132 ? Q799U3 1 ? 132 ? 1 132 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 4710  ? 
1 MORE         -108  ? 
1 'SSA (A^2)'  14540 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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  AA1 ILE A 5   ? GLY A 13  ? ILE A 5   GLY A 13  5 ? 9  
HELX_P HELX_P2  AA2 GLU A 17  ? GLU A 23  ? GLU A 17  GLU A 23  1 ? 7  
HELX_P HELX_P3  AA3 GLN A 44  ? LEU A 58  ? GLN A 44  LEU A 58  1 ? 15 
HELX_P HELX_P4  AA4 THR A 61  ? ASP A 75  ? THR A 61  ASP A 75  1 ? 15 
HELX_P HELX_P5  AA5 ALA A 77  ? ARG A 113 ? ALA A 77  ARG A 113 1 ? 37 
HELX_P HELX_P6  AA6 CYS A 123 ? LYS A 131 ? CYS A 123 LYS A 131 1 ? 9  
HELX_P HELX_P7  AA7 ALA B 9   ? GLY B 13  ? ALA B 9   GLY B 13  5 ? 5  
HELX_P HELX_P8  AA8 GLU B 17  ? GLU B 23  ? GLU B 17  GLU B 23  1 ? 7  
HELX_P HELX_P9  AA9 GLN B 44  ? LEU B 58  ? GLN B 44  LEU B 58  1 ? 15 
HELX_P HELX_P10 AB1 THR B 61  ? ASP B 75  ? THR B 61  ASP B 75  1 ? 15 
HELX_P HELX_P11 AB2 ALA B 77  ? ARG B 113 ? ALA B 77  ARG B 113 1 ? 37 
HELX_P HELX_P12 AB3 CYS B 123 ? LYS B 131 ? CYS B 123 LYS B 131 1 ? 9  
# 
_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 
metalc1 metalc ? ? A CYS 79  SG ? ? ? 1_555 D HG  .   HG ? ? A CYS 79  A HG  202 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc2 metalc ? ? A CYS 114 SG ? ? ? 1_555 C HG  .   HG ? ? A CYS 114 A HG  201 1_555 ? ? ? ? ? ? ? 2.440 ? ? 
metalc3 metalc ? ? A CYS 123 SG ? ? ? 1_555 C HG  .   HG ? ? A CYS 123 A HG  201 1_555 ? ? ? ? ? ? ? 2.463 ? ? 
metalc4 metalc ? ? C HG  .   HG ? ? ? 1_555 B CYS 79  O  ? ? A HG  201 B CYS 79  1_555 ? ? ? ? ? ? ? 3.174 ? ? 
metalc5 metalc ? ? C HG  .   HG ? ? ? 1_555 B CYS 79  SG ? ? A HG  201 B CYS 79  1_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc6 metalc ? ? D HG  .   HG ? ? ? 1_555 B CYS 114 SG ? ? A HG  202 B CYS 114 1_555 ? ? ? ? ? ? ? 2.460 ? ? 
metalc7 metalc ? ? D HG  .   HG ? ? ? 1_555 B CYS 123 SG ? ? A HG  202 B CYS 123 1_555 ? ? ? ? ? ? ? 2.469 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 79  ? A CYS 79  ? 1_555 HG ? D HG . ? A HG 202 ? 1_555 SG ? B CYS 114 ? B CYS 114 ? 1_555 110.3 ? 
2 SG ? A CYS 79  ? A CYS 79  ? 1_555 HG ? D HG . ? A HG 202 ? 1_555 SG ? B CYS 123 ? B CYS 123 ? 1_555 124.8 ? 
3 SG ? B CYS 114 ? B CYS 114 ? 1_555 HG ? D HG . ? A HG 202 ? 1_555 SG ? B CYS 123 ? B CYS 123 ? 1_555 124.8 ? 
4 SG ? A CYS 114 ? A CYS 114 ? 1_555 HG ? C HG . ? A HG 201 ? 1_555 SG ? A CYS 123 ? A CYS 123 ? 1_555 111.3 ? 
5 SG ? A CYS 114 ? A CYS 114 ? 1_555 HG ? C HG . ? A HG 201 ? 1_555 O  ? B CYS 79  ? B CYS 79  ? 1_555 115.0 ? 
6 SG ? A CYS 123 ? A CYS 123 ? 1_555 HG ? C HG . ? A HG 201 ? 1_555 O  ? B CYS 79  ? B CYS 79  ? 1_555 94.8  ? 
7 SG ? A CYS 114 ? A CYS 114 ? 1_555 HG ? C HG . ? A HG 201 ? 1_555 SG ? B CYS 79  ? B CYS 79  ? 1_555 116.9 ? 
8 SG ? A CYS 123 ? A CYS 123 ? 1_555 HG ? C HG . ? A HG 201 ? 1_555 SG ? B CYS 79  ? B CYS 79  ? 1_555 130.7 ? 
9 O  ? B CYS 79  ? B CYS 79  ? 1_555 HG ? C HG . ? A HG 201 ? 1_555 SG ? B CYS 79  ? B CYS 79  ? 1_555 74.4  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 37 A . ? GLY 37 A TYR 38 A ? TYR 38 A 1 1.89  
2 GLY 37 B . ? GLY 37 B TYR 38 B ? TYR 38 B 1 -9.28 
# 
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 HG 201 ? 4 'binding site for residue HG A 201' 
AC2 Software A HG 202 ? 4 'binding site for residue HG A 202' 
# 
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 4 CYS A 114 ? CYS A 114 . ? 1_555 ? 
2 AC1 4 CYS A 123 ? CYS A 123 . ? 1_555 ? 
3 AC1 4 PRO A 124 ? PRO A 124 . ? 1_555 ? 
4 AC1 4 CYS B 79  ? CYS B 79  . ? 1_555 ? 
5 AC2 4 CYS A 79  ? CYS A 79  . ? 1_555 ? 
6 AC2 4 CYS B 114 ? CYS B 114 . ? 1_555 ? 
7 AC2 4 CYS B 123 ? CYS B 123 . ? 1_555 ? 
8 AC2 4 PRO B 124 ? PRO B 124 . ? 1_555 ? 
# 
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 C  A ILE 28 ? ? N  A PRO 29 ? ? CA A PRO 29 ? ? 129.07 119.30 9.77  1.50 Y 
2 1 CA B LEU 8  ? ? CB B LEU 8  ? ? CG B LEU 8  ? ? 129.76 115.30 14.46 2.30 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 ARG A 24 ? ? 77.52   -0.18   
2 1 ILE A 28 ? ? 177.60  132.85  
3 1 TYR A 38 ? ? 66.43   75.25   
4 1 ARG A 39 ? ? -125.35 -73.88  
5 1 ALA B 9  ? ? 70.31   -13.09  
6 1 ARG B 24 ? ? 77.63   -3.90   
7 1 LYS B 36 ? ? 59.48   -142.39 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     304 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_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[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 56.1095 31.9169 -21.1715 0.4044 ? -0.0114 ? 0.1799  ? 0.3218 ? 0.1772 ? 0.9918 ? 1.9365 ? 1.1470  
? -0.0379 ? 0.8912 ? 0.7290  ? 2.6509 ? 0.4439  ? 0.0987  ? 0.0344  ? -0.0646 ? 0.0868  ? -0.6909 ? -0.6176 ? 0.1984  ? -0.1965 ? 
2 'X-RAY DIFFRACTION' ? refined 52.8887 17.5607 -19.3241 0.2640 ? -0.0048 ? -0.0737 ? 0.2737 ? 0.1388 ? 0.2585 ? 3.6606 ? 0.3913  
? -0.6628 ? 2.7981 ? 1.6839  ? 3.2597 ? 0.2756  ? 0.3176  ? 0.1920  ? -0.0901 ? -0.2905 ? -0.0471 ? 0.0789  ? 0.1182  ? 0.0073  ? 
3 'X-RAY DIFFRACTION' ? refined 46.5208 7.3170  7.2682   0.2055 ? -0.1208 ? -0.0651 ? 0.2747 ? 0.0954 ? 0.3063 ? 0.5159 ? -0.2810 
? -0.1366 ? 0.6733 ? 0.2348  ? 5.2151 ? -0.1606 ? -0.2329 ? -0.1942 ? 0.0213  ? -0.2852 ? 0.0356  ? 0.2487  ? 0.3521  ? 0.3027  ? 
4 'X-RAY DIFFRACTION' ? refined 65.7410 21.7785 20.1736  0.1691 ? -0.0610 ? 0.0044  ? 0.4329 ? 0.0512 ? 0.8773 ? 1.7882 ? -0.2983 
? 1.4141  ? 0.5209 ? -0.2381 ? 1.3235 ? -0.0768 ? 0.1033  ? 0.2063  ? -0.0525 ? 0.3127  ? 0.0376  ? -0.0664 ? -0.0730 ? -0.1055 ? 
5 'X-RAY DIFFRACTION' ? refined 55.2289 19.0148 21.2928  0.2765 ? -0.0740 ? -0.1324 ? 0.3030 ? 0.0133 ? 0.2853 ? 4.7455 ? 0.1751  
? -1.7732 ? 1.3006 ? -0.0032 ? 0.6640 ? -0.2018 ? -0.1462 ? -0.0941 ? 0.4235  ? 0.2542  ? -0.4069 ? 0.1615  ? 0.1689  ? -0.0522 ? 
6 'X-RAY DIFFRACTION' ? refined 41.3345 12.5553 -5.9225  0.2427 ? -0.0737 ? -0.0754 ? 0.2637 ? 0.0746 ? 0.2970 ? 0.8621 ? -0.2672 
? 1.3879  ? 0.3429 ? 0.6364  ? 6.4388 ? -0.0868 ? 0.0429  ? -0.0610 ? -0.0984 ? -0.3169 ? 0.0654  ? -0.1555 ? -0.5371 ? 0.2412  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 43 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 44 through 77 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 78 through 131 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 3 through 32 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 35 through 77 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 78 through 131 )
;
# 
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 MET 1   ? A MET 1   
2  1 Y 1 A LYS 2   ? A LYS 2   
3  1 Y 1 A GLU 32  ? A GLU 32  
4  1 Y 1 A ARG 33  ? A ARG 33  
5  1 Y 1 A THR 34  ? A THR 34  
6  1 Y 1 A TYR 41  ? A TYR 41  
7  1 Y 1 A SER 42  ? A SER 42  
8  1 Y 1 A LYS 132 ? A LYS 132 
9  1 Y 1 B MET 1   ? B MET 1   
10 1 Y 1 B LYS 2   ? B LYS 2   
11 1 Y 1 B ARG 33  ? B ARG 33  
12 1 Y 1 B THR 34  ? B THR 34  
13 1 Y 1 B TYR 41  ? B TYR 41  
14 1 Y 1 B SER 42  ? B SER 42  
15 1 Y 1 B LYS 132 ? B LYS 132 
# 
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  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HG  HG   HG N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TYR N    N  N N 322 
TYR CA   C  N S 323 
TYR C    C  N N 324 
TYR O    O  N N 325 
TYR CB   C  N N 326 
TYR CG   C  Y N 327 
TYR CD1  C  Y N 328 
TYR CD2  C  Y N 329 
TYR CE1  C  Y N 330 
TYR CE2  C  Y N 331 
TYR CZ   C  Y N 332 
TYR OH   O  N N 333 
TYR OXT  O  N N 334 
TYR H    H  N N 335 
TYR H2   H  N N 336 
TYR HA   H  N N 337 
TYR HB2  H  N N 338 
TYR HB3  H  N N 339 
TYR HD1  H  N N 340 
TYR HD2  H  N N 341 
TYR HE1  H  N N 342 
TYR HE2  H  N N 343 
TYR HH   H  N N 344 
TYR HXT  H  N N 345 
VAL N    N  N N 346 
VAL CA   C  N S 347 
VAL C    C  N N 348 
VAL O    O  N N 349 
VAL CB   C  N N 350 
VAL CG1  C  N N 351 
VAL CG2  C  N N 352 
VAL OXT  O  N N 353 
VAL H    H  N N 354 
VAL H2   H  N N 355 
VAL HA   H  N N 356 
VAL HB   H  N N 357 
VAL HG11 H  N N 358 
VAL HG12 H  N N 359 
VAL HG13 H  N N 360 
VAL HG21 H  N N 361 
VAL HG22 H  N N 362 
VAL HG23 H  N N 363 
VAL HXT  H  N N 364 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TYR N   CA   sing N N 306 
TYR N   H    sing N N 307 
TYR N   H2   sing N N 308 
TYR CA  C    sing N N 309 
TYR CA  CB   sing N N 310 
TYR CA  HA   sing N N 311 
TYR C   O    doub N N 312 
TYR C   OXT  sing N N 313 
TYR CB  CG   sing N N 314 
TYR CB  HB2  sing N N 315 
TYR CB  HB3  sing N N 316 
TYR CG  CD1  doub Y N 317 
TYR CG  CD2  sing Y N 318 
TYR CD1 CE1  sing Y N 319 
TYR CD1 HD1  sing N N 320 
TYR CD2 CE2  doub Y N 321 
TYR CD2 HD2  sing N N 322 
TYR CE1 CZ   doub Y N 323 
TYR CE1 HE1  sing N N 324 
TYR CE2 CZ   sing Y N 325 
TYR CE2 HE2  sing N N 326 
TYR CZ  OH   sing N N 327 
TYR OH  HH   sing N N 328 
TYR OXT HXT  sing N N 329 
VAL N   CA   sing N N 330 
VAL N   H    sing N N 331 
VAL N   H2   sing N N 332 
VAL CA  C    sing N N 333 
VAL CA  CB   sing N N 334 
VAL CA  HA   sing N N 335 
VAL C   O    doub N N 336 
VAL C   OXT  sing N N 337 
VAL CB  CG1  sing N N 338 
VAL CB  CG2  sing N N 339 
VAL CB  HB   sing N N 340 
VAL CG1 HG11 sing N N 341 
VAL CG1 HG12 sing N N 342 
VAL CG1 HG13 sing N N 343 
VAL CG2 HG21 sing N N 344 
VAL CG2 HG22 sing N N 345 
VAL CG2 HG23 sing N N 346 
VAL OXT HXT  sing N N 347 
# 
_atom_sites.entry_id                    4UA1 
_atom_sites.fract_transf_matrix[1][1]   0.014285 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.014173 
_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]   0.013964 
_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  
HG 
N  
O  
S  
# 
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   . PHE A 1 3   ? 49.090 35.102 -31.490 1.00 57.98 ? 3   PHE A N   1 
ATOM   2    C  CA  . PHE A 1 3   ? 50.217 35.099 -30.561 1.00 61.69 ? 3   PHE A CA  1 
ATOM   3    C  C   . PHE A 1 3   ? 49.878 35.836 -29.277 1.00 60.54 ? 3   PHE A C   1 
ATOM   4    O  O   . PHE A 1 3   ? 48.947 36.632 -29.230 1.00 67.02 ? 3   PHE A O   1 
ATOM   5    C  CB  . PHE A 1 3   ? 51.465 35.713 -31.195 1.00 56.81 ? 3   PHE A CB  1 
ATOM   6    N  N   . ARG A 1 4   ? 50.648 35.532 -28.239 1.00 66.98 ? 4   ARG A N   1 
ATOM   7    C  CA  . ARG A 1 4   ? 50.413 35.999 -26.873 1.00 62.40 ? 4   ARG A CA  1 
ATOM   8    C  C   . ARG A 1 4   ? 51.693 36.606 -26.353 1.00 60.00 ? 4   ARG A C   1 
ATOM   9    O  O   . ARG A 1 4   ? 52.664 36.658 -27.088 1.00 64.92 ? 4   ARG A O   1 
ATOM   10   C  CB  . ARG A 1 4   ? 49.961 34.850 -25.958 1.00 51.24 ? 4   ARG A CB  1 
ATOM   11   C  CG  . ARG A 1 4   ? 48.861 34.008 -26.546 1.00 48.87 ? 4   ARG A CG  1 
ATOM   12   C  CD  . ARG A 1 4   ? 47.542 34.762 -26.504 1.00 51.20 ? 4   ARG A CD  1 
ATOM   13   N  NE  . ARG A 1 4   ? 46.532 34.121 -27.335 1.00 56.95 ? 4   ARG A NE  1 
ATOM   14   N  N   . ILE A 1 5   ? 51.661 37.179 -25.153 1.00 63.66 ? 5   ILE A N   1 
ATOM   15   C  CA  . ILE A 1 5   ? 52.862 37.755 -24.547 1.00 60.79 ? 5   ILE A CA  1 
ATOM   16   C  C   . ILE A 1 5   ? 52.957 37.589 -23.025 1.00 65.92 ? 5   ILE A C   1 
ATOM   17   O  O   . ILE A 1 5   ? 51.978 37.802 -22.322 1.00 72.89 ? 5   ILE A O   1 
ATOM   18   C  CB  . ILE A 1 5   ? 52.966 39.256 -24.847 1.00 69.40 ? 5   ILE A CB  1 
ATOM   19   N  N   . GLY A 1 6   ? 54.095 37.146 -22.514 1.00 55.14 ? 6   GLY A N   1 
ATOM   20   C  CA  . GLY A 1 6   ? 54.420 37.424 -21.130 1.00 55.29 ? 6   GLY A CA  1 
ATOM   21   C  C   . GLY A 1 6   ? 53.458 37.056 -20.018 1.00 54.14 ? 6   GLY A C   1 
ATOM   22   O  O   . GLY A 1 6   ? 53.021 35.918 -19.831 1.00 60.88 ? 6   GLY A O   1 
ATOM   23   N  N   . GLU A 1 7   ? 53.090 38.100 -19.289 1.00 56.42 ? 7   GLU A N   1 
ATOM   24   C  CA  . GLU A 1 7   ? 52.156 38.025 -18.182 1.00 65.22 ? 7   GLU A CA  1 
ATOM   25   C  C   . GLU A 1 7   ? 50.732 37.861 -18.673 1.00 59.29 ? 7   GLU A C   1 
ATOM   26   O  O   . GLU A 1 7   ? 49.840 37.600 -17.877 1.00 54.28 ? 7   GLU A O   1 
ATOM   27   C  CB  . GLU A 1 7   ? 52.273 39.272 -17.298 1.00 69.64 ? 7   GLU A CB  1 
ATOM   28   N  N   . LEU A 1 8   ? 50.509 38.059 -19.970 1.00 53.83 ? 8   LEU A N   1 
ATOM   29   C  CA  . LEU A 1 8   ? 49.261 37.599 -20.554 1.00 52.97 ? 8   LEU A CA  1 
ATOM   30   C  C   . LEU A 1 8   ? 49.222 36.058 -20.533 1.00 64.04 ? 8   LEU A C   1 
ATOM   31   O  O   . LEU A 1 8   ? 48.175 35.470 -20.266 1.00 50.48 ? 8   LEU A O   1 
ATOM   32   C  CB  . LEU A 1 8   ? 49.084 38.134 -21.974 1.00 53.86 ? 8   LEU A CB  1 
ATOM   33   N  N   . ALA A 1 9   ? 50.360 35.400 -20.774 1.00 67.71 ? 9   ALA A N   1 
ATOM   34   C  CA  . ALA A 1 9   ? 50.408 33.935 -20.699 1.00 51.96 ? 9   ALA A CA  1 
ATOM   35   C  C   . ALA A 1 9   ? 50.218 33.475 -19.264 1.00 55.08 ? 9   ALA A C   1 
ATOM   36   O  O   . ALA A 1 9   ? 49.896 32.319 -19.011 1.00 57.36 ? 9   ALA A O   1 
ATOM   37   C  CB  . ALA A 1 9   ? 51.713 33.391 -21.251 1.00 51.59 ? 9   ALA A CB  1 
ATOM   38   N  N   . ASP A 1 10  ? 50.317 34.413 -18.333 1.00 54.39 ? 10  ASP A N   1 
ATOM   39   C  CA  . ASP A 1 10  ? 50.003 34.150 -16.939 1.00 51.23 ? 10  ASP A CA  1 
ATOM   40   C  C   . ASP A 1 10  ? 48.480 34.152 -16.720 1.00 65.28 ? 10  ASP A C   1 
ATOM   41   O  O   . ASP A 1 10  ? 48.010 34.113 -15.590 1.00 68.68 ? 10  ASP A O   1 
ATOM   42   C  CB  . ASP A 1 10  ? 50.703 35.169 -16.044 1.00 54.18 ? 10  ASP A CB  1 
ATOM   43   N  N   . LYS A 1 11  ? 47.736 34.221 -17.834 1.00 65.00 ? 11  LYS A N   1 
ATOM   44   C  CA  . LYS A 1 11  ? 46.295 33.901 -17.915 1.00 45.80 ? 11  LYS A CA  1 
ATOM   45   C  C   . LYS A 1 11  ? 46.043 32.395 -17.792 1.00 57.48 ? 11  LYS A C   1 
ATOM   46   O  O   . LYS A 1 11  ? 44.918 31.937 -17.918 1.00 68.63 ? 11  LYS A O   1 
ATOM   47   C  CB  . LYS A 1 11  ? 45.702 34.338 -19.237 1.00 47.10 ? 11  LYS A CB  1 
ATOM   48   N  N   . CYS A 1 12  ? 47.101 31.610 -17.626 1.00 48.71 ? 12  CYS A N   1 
ATOM   49   C  CA  . CYS A 1 12  ? 46.966 30.182 -17.370 1.00 44.52 ? 12  CYS A CA  1 
ATOM   50   C  C   . CYS A 1 12  ? 46.895 29.919 -15.876 1.00 48.62 ? 12  CYS A C   1 
ATOM   51   O  O   . CYS A 1 12  ? 46.856 28.772 -15.434 1.00 50.74 ? 12  CYS A O   1 
ATOM   52   C  CB  . CYS A 1 12  ? 48.150 29.421 -17.964 1.00 49.75 ? 12  CYS A CB  1 
ATOM   53   S  SG  . CYS A 1 12  ? 48.142 29.232 -19.739 1.00 53.06 ? 12  CYS A SG  1 
ATOM   54   N  N   . GLY A 1 13  ? 46.909 30.991 -15.094 1.00 46.07 ? 13  GLY A N   1 
ATOM   55   C  CA  . GLY A 1 13  ? 46.868 30.870 -13.652 1.00 46.21 ? 13  GLY A CA  1 
ATOM   56   C  C   . GLY A 1 13  ? 48.204 30.491 -13.067 1.00 46.60 ? 13  GLY A C   1 
ATOM   57   O  O   . GLY A 1 13  ? 48.265 29.871 -12.018 1.00 49.66 ? 13  GLY A O   1 
ATOM   58   N  N   . VAL A 1 14  ? 49.282 30.857 -13.746 1.00 48.42 ? 14  VAL A N   1 
ATOM   59   C  CA  . VAL A 1 14  ? 50.627 30.622 -13.222 1.00 57.00 ? 14  VAL A CA  1 
ATOM   60   C  C   . VAL A 1 14  ? 51.432 31.922 -13.224 1.00 58.04 ? 14  VAL A C   1 
ATOM   61   O  O   . VAL A 1 14  ? 51.478 32.621 -14.240 1.00 63.27 ? 14  VAL A O   1 
ATOM   62   C  CB  . VAL A 1 14  ? 51.387 29.541 -14.023 1.00 56.61 ? 14  VAL A CB  1 
ATOM   63   C  CG1 . VAL A 1 14  ? 52.699 29.208 -13.334 1.00 57.47 ? 14  VAL A CG1 1 
ATOM   64   C  CG2 . VAL A 1 14  ? 50.529 28.294 -14.183 1.00 48.41 ? 14  VAL A CG2 1 
ATOM   65   N  N   . ASN A 1 15  ? 52.069 32.244 -12.095 1.00 65.02 ? 15  ASN A N   1 
ATOM   66   C  CA  . ASN A 1 15  ? 52.877 33.469 -11.975 1.00 54.87 ? 15  ASN A CA  1 
ATOM   67   C  C   . ASN A 1 15  ? 54.133 33.366 -12.816 1.00 52.29 ? 15  ASN A C   1 
ATOM   68   O  O   . ASN A 1 15  ? 54.529 32.266 -13.197 1.00 61.22 ? 15  ASN A O   1 
ATOM   69   C  CB  . ASN A 1 15  ? 53.207 33.759 -10.509 1.00 58.89 ? 15  ASN A CB  1 
ATOM   70   C  CG  . ASN A 1 15  ? 53.948 32.624 -9.830  1.00 65.62 ? 15  ASN A CG  1 
ATOM   71   O  OD1 . ASN A 1 15  ? 54.958 32.133 -10.332 1.00 68.72 ? 15  ASN A OD1 1 
ATOM   72   N  ND2 . ASN A 1 15  ? 53.431 32.186 -8.682  1.00 60.40 ? 15  ASN A ND2 1 
ATOM   73   N  N   . LYS A 1 16  ? 54.766 34.496 -13.105 1.00 54.58 ? 16  LYS A N   1 
ATOM   74   C  CA  . LYS A 1 16  ? 55.650 34.561 -14.256 1.00 55.98 ? 16  LYS A CA  1 
ATOM   75   C  C   . LYS A 1 16  ? 56.833 33.622 -14.050 1.00 62.80 ? 16  LYS A C   1 
ATOM   76   O  O   . LYS A 1 16  ? 57.661 33.775 -13.147 1.00 56.37 ? 16  LYS A O   1 
ATOM   77   C  CB  . LYS A 1 16  ? 56.095 36.006 -14.476 1.00 56.50 ? 16  LYS A CB  1 
ATOM   78   C  CG  . LYS A 1 16  ? 54.914 36.950 -14.581 1.00 56.48 ? 16  LYS A CG  1 
ATOM   79   C  CD  . LYS A 1 16  ? 55.282 38.370 -14.229 1.00 58.12 ? 16  LYS A CD  1 
ATOM   80   N  N   . GLU A 1 17  ? 56.878 32.630 -14.934 1.00 85.49 ? 17  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 17  ? 57.602 31.406 -14.650 1.00 63.31 ? 17  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 17  ? 58.755 31.150 -15.585 1.00 73.51 ? 17  GLU A C   1 
ATOM   83   O  O   . GLU A 1 17  ? 58.575 30.622 -16.699 1.00 70.09 ? 17  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 17  ? 56.649 30.234 -14.747 1.00 51.78 ? 17  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 17  ? 57.051 29.040 -13.931 1.00 55.83 ? 17  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 17  ? 56.902 29.305 -12.431 1.00 67.39 ? 17  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 17  ? 56.979 30.477 -11.982 1.00 68.44 ? 17  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 17  ? 56.609 28.343 -11.703 1.00 70.23 ? 17  GLU A OE2 1 
ATOM   89   N  N   . THR A 1 18  ? 59.952 31.430 -15.103 1.00 60.42 ? 18  THR A N   1 
ATOM   90   C  CA  . THR A 1 18  ? 61.122 31.168 -15.899 1.00 57.93 ? 18  THR A CA  1 
ATOM   91   C  C   . THR A 1 18  ? 61.558 29.733 -15.715 1.00 57.97 ? 18  THR A C   1 
ATOM   92   O  O   . THR A 1 18  ? 62.229 29.190 -16.588 1.00 60.09 ? 18  THR A O   1 
ATOM   93   C  CB  . THR A 1 18  ? 62.275 32.131 -15.530 1.00 63.62 ? 18  THR A CB  1 
ATOM   94   N  N   . ILE A 1 19  ? 61.149 29.114 -14.602 1.00 54.24 ? 19  ILE A N   1 
ATOM   95   C  CA  . ILE A 1 19  ? 61.680 27.806 -14.234 1.00 54.72 ? 19  ILE A CA  1 
ATOM   96   C  C   . ILE A 1 19  ? 61.265 26.787 -15.293 1.00 57.50 ? 19  ILE A C   1 
ATOM   97   O  O   . ILE A 1 19  ? 62.015 25.858 -15.605 1.00 63.38 ? 19  ILE A O   1 
ATOM   98   C  CB  . ILE A 1 19  ? 61.222 27.348 -12.814 1.00 62.88 ? 19  ILE A CB  1 
ATOM   99   C  CG1 . ILE A 1 19  ? 61.818 25.977 -12.467 1.00 64.98 ? 19  ILE A CG1 1 
ATOM   100  C  CG2 . ILE A 1 19  ? 59.729 27.228 -12.725 1.00 67.84 ? 19  ILE A CG2 1 
ATOM   101  C  CD1 . ILE A 1 19  ? 61.358 25.406 -11.126 1.00 56.53 ? 19  ILE A CD1 1 
ATOM   102  N  N   . ARG A 1 20  ? 60.080 26.986 -15.859 1.00 52.38 ? 20  ARG A N   1 
ATOM   103  C  CA  . ARG A 1 20  ? 59.541 26.071 -16.851 1.00 51.57 ? 20  ARG A CA  1 
ATOM   104  C  C   . ARG A 1 20  ? 60.365 26.041 -18.111 1.00 54.92 ? 20  ARG A C   1 
ATOM   105  O  O   . ARG A 1 20  ? 60.631 24.966 -18.648 1.00 52.67 ? 20  ARG A O   1 
ATOM   106  C  CB  . ARG A 1 20  ? 58.114 26.434 -17.221 1.00 50.02 ? 20  ARG A CB  1 
ATOM   107  C  CG  . ARG A 1 20  ? 57.105 25.475 -16.693 1.00 48.98 ? 20  ARG A CG  1 
ATOM   108  C  CD  . ARG A 1 20  ? 57.203 25.374 -15.193 1.00 49.31 ? 20  ARG A CD  1 
ATOM   109  N  NE  . ARG A 1 20  ? 55.901 25.063 -14.602 1.00 48.81 ? 20  ARG A NE  1 
ATOM   110  C  CZ  . ARG A 1 20  ? 55.748 24.711 -13.333 1.00 48.35 ? 20  ARG A CZ  1 
ATOM   111  N  NH1 . ARG A 1 20  ? 56.811 24.649 -12.550 1.00 54.87 ? 20  ARG A NH1 1 
ATOM   112  N  NH2 . ARG A 1 20  ? 54.548 24.447 -12.843 1.00 47.42 ? 20  ARG A NH2 1 
ATOM   113  N  N   . TYR A 1 21  ? 60.727 27.224 -18.611 1.00 58.43 ? 21  TYR A N   1 
ATOM   114  C  CA  . TYR A 1 21  ? 61.506 27.306 -19.844 1.00 56.17 ? 21  TYR A CA  1 
ATOM   115  C  C   . TYR A 1 21  ? 62.963 26.963 -19.592 1.00 56.61 ? 21  TYR A C   1 
ATOM   116  O  O   . TYR A 1 21  ? 63.629 26.369 -20.446 1.00 57.47 ? 21  TYR A O   1 
ATOM   117  C  CB  . TYR A 1 21  ? 61.393 28.701 -20.464 1.00 53.29 ? 21  TYR A CB  1 
ATOM   118  C  CG  . TYR A 1 21  ? 61.246 29.814 -19.451 1.00 62.87 ? 21  TYR A CG  1 
ATOM   119  N  N   . TYR A 1 22  ? 63.433 27.284 -18.392 1.00 54.93 ? 22  TYR A N   1 
ATOM   120  C  CA  . TYR A 1 22  ? 64.774 26.914 -17.972 1.00 56.75 ? 22  TYR A CA  1 
ATOM   121  C  C   . TYR A 1 22  ? 64.891 25.396 -17.896 1.00 68.12 ? 22  TYR A C   1 
ATOM   122  O  O   . TYR A 1 22  ? 65.917 24.816 -18.264 1.00 69.44 ? 22  TYR A O   1 
ATOM   123  C  CB  . TYR A 1 22  ? 65.118 27.554 -16.625 1.00 57.38 ? 22  TYR A CB  1 
ATOM   124  N  N   . GLU A 1 23  ? 63.820 24.760 -17.430 1.00 55.89 ? 23  GLU A N   1 
ATOM   125  C  CA  . GLU A 1 23  ? 63.775 23.310 -17.289 1.00 56.08 ? 23  GLU A CA  1 
ATOM   126  C  C   . GLU A 1 23  ? 63.355 22.605 -18.567 1.00 55.52 ? 23  GLU A C   1 
ATOM   127  O  O   . GLU A 1 23  ? 63.199 21.383 -18.561 1.00 56.83 ? 23  GLU A O   1 
ATOM   128  C  CB  . GLU A 1 23  ? 62.840 22.915 -16.153 1.00 55.05 ? 23  GLU A CB  1 
ATOM   129  C  CG  . GLU A 1 23  ? 63.490 22.899 -14.789 1.00 58.13 ? 23  GLU A CG  1 
ATOM   130  C  CD  . GLU A 1 23  ? 62.476 22.956 -13.663 1.00 63.67 ? 23  GLU A CD  1 
ATOM   131  O  OE1 . GLU A 1 23  ? 61.264 23.038 -13.974 1.00 54.08 ? 23  GLU A OE1 1 
ATOM   132  O  OE2 . GLU A 1 23  ? 62.888 22.875 -12.476 1.00 60.31 ? 23  GLU A OE2 1 
ATOM   133  N  N   . ARG A 1 24  ? 63.164 23.383 -19.637 1.00 56.96 ? 24  ARG A N   1 
ATOM   134  C  CA  . ARG A 1 24  ? 62.850 22.881 -20.987 1.00 54.99 ? 24  ARG A CA  1 
ATOM   135  C  C   . ARG A 1 24  ? 61.406 22.446 -21.195 1.00 52.18 ? 24  ARG A C   1 
ATOM   136  O  O   . ARG A 1 24  ? 61.060 21.977 -22.283 1.00 57.88 ? 24  ARG A O   1 
ATOM   137  C  CB  . ARG A 1 24  ? 63.776 21.719 -21.380 1.00 72.61 ? 24  ARG A CB  1 
ATOM   138  N  N   . LEU A 1 25  ? 60.570 22.549 -20.166 1.00 48.30 ? 25  LEU A N   1 
ATOM   139  C  CA  . LEU A 1 25  ? 59.159 22.190 -20.330 1.00 46.66 ? 25  LEU A CA  1 
ATOM   140  C  C   . LEU A 1 25  ? 58.477 23.065 -21.376 1.00 45.79 ? 25  LEU A C   1 
ATOM   141  O  O   . LEU A 1 25  ? 57.785 22.567 -22.264 1.00 45.14 ? 25  LEU A O   1 
ATOM   142  C  CB  . LEU A 1 25  ? 58.400 22.303 -19.005 1.00 45.81 ? 25  LEU A CB  1 
ATOM   143  C  CG  . LEU A 1 25  ? 58.644 21.394 -17.782 1.00 46.40 ? 25  LEU A CG  1 
ATOM   144  C  CD1 . LEU A 1 25  ? 60.082 21.223 -17.410 1.00 48.23 ? 25  LEU A CD1 1 
ATOM   145  C  CD2 . LEU A 1 25  ? 57.844 21.920 -16.561 1.00 45.56 ? 25  LEU A CD2 1 
ATOM   146  N  N   . GLY A 1 26  ? 58.654 24.378 -21.255 1.00 60.84 ? 26  GLY A N   1 
ATOM   147  C  CA  . GLY A 1 26  ? 58.105 25.308 -22.226 1.00 49.27 ? 26  GLY A CA  1 
ATOM   148  C  C   . GLY A 1 26  ? 59.106 25.802 -23.260 1.00 48.51 ? 26  GLY A C   1 
ATOM   149  O  O   . GLY A 1 26  ? 60.317 25.840 -23.045 1.00 49.85 ? 26  GLY A O   1 
ATOM   150  N  N   . LEU A 1 27  ? 58.557 26.236 -24.380 1.00 52.53 ? 27  LEU A N   1 
ATOM   151  C  CA  . LEU A 1 27  ? 59.296 26.796 -25.502 1.00 59.96 ? 27  LEU A CA  1 
ATOM   152  C  C   . LEU A 1 27  ? 59.637 28.280 -25.200 1.00 66.95 ? 27  LEU A C   1 
ATOM   153  O  O   . LEU A 1 27  ? 59.557 28.651 -24.026 1.00 65.20 ? 27  LEU A O   1 
ATOM   154  C  CB  . LEU A 1 27  ? 58.440 26.643 -26.753 1.00 61.46 ? 27  LEU A CB  1 
ATOM   155  N  N   . ILE A 1 28  ? 60.169 29.045 -26.181 1.00 72.76 ? 28  ILE A N   1 
ATOM   156  C  CA  . ILE A 1 28  ? 60.137 30.545 -26.190 1.00 59.92 ? 28  ILE A CA  1 
ATOM   157  C  C   . ILE A 1 28  ? 60.848 31.272 -27.370 1.00 83.72 ? 28  ILE A C   1 
ATOM   158  O  O   . ILE A 1 28  ? 61.968 30.906 -27.737 1.00 85.51 ? 28  ILE A O   1 
ATOM   159  C  CB  . ILE A 1 28  ? 60.715 31.119 -24.866 1.00 61.51 ? 28  ILE A CB  1 
ATOM   160  C  CG1 . ILE A 1 28  ? 60.503 32.641 -24.811 1.00 67.02 ? 28  ILE A CG1 1 
ATOM   161  C  CG2 . ILE A 1 28  ? 62.186 30.766 -24.735 1.00 66.96 ? 28  ILE A CG2 1 
ATOM   162  C  CD1 . ILE A 1 28  ? 60.839 33.275 -23.477 1.00 63.50 ? 28  ILE A CD1 1 
ATOM   163  N  N   . PRO A 1 29  ? 60.159 32.279 -27.995 1.00 73.51 ? 29  PRO A N   1 
ATOM   164  C  CA  . PRO A 1 29  ? 60.591 33.154 -29.117 1.00 57.95 ? 29  PRO A CA  1 
ATOM   165  C  C   . PRO A 1 29  ? 61.101 34.610 -28.894 1.00 80.49 ? 29  PRO A C   1 
ATOM   166  O  O   . PRO A 1 29  ? 60.887 35.208 -27.842 1.00 84.80 ? 29  PRO A O   1 
ATOM   167  C  CB  . PRO A 1 29  ? 59.319 33.247 -29.962 1.00 59.39 ? 29  PRO A CB  1 
ATOM   168  C  CG  . PRO A 1 29  ? 58.200 33.107 -28.972 1.00 68.39 ? 29  PRO A CG  1 
ATOM   169  C  CD  . PRO A 1 29  ? 58.711 32.394 -27.749 1.00 73.54 ? 29  PRO A CD  1 
ATOM   170  N  N   . GLU A 1 30  ? 61.721 35.171 -29.943 1.00 72.19 ? 30  GLU A N   1 
ATOM   171  C  CA  . GLU A 1 30  ? 62.086 36.597 -30.089 1.00 76.71 ? 30  GLU A CA  1 
ATOM   172  C  C   . GLU A 1 30  ? 61.308 37.332 -31.210 1.00 71.63 ? 30  GLU A C   1 
ATOM   173  O  O   . GLU A 1 30  ? 61.278 36.849 -32.339 1.00 77.21 ? 30  GLU A O   1 
ATOM   174  C  CB  . GLU A 1 30  ? 63.589 36.737 -30.342 1.00 76.07 ? 30  GLU A CB  1 
ATOM   175  N  N   . PRO A 1 31  ? 60.740 38.521 -30.941 1.00 65.36 ? 31  PRO A N   1 
ATOM   176  C  CA  . PRO A 1 31  ? 59.984 39.080 -32.081 1.00 68.63 ? 31  PRO A CA  1 
ATOM   177  C  C   . PRO A 1 31  ? 60.854 39.799 -33.098 1.00 71.62 ? 31  PRO A C   1 
ATOM   178  O  O   . PRO A 1 31  ? 61.424 40.840 -32.775 1.00 70.83 ? 31  PRO A O   1 
ATOM   179  C  CB  . PRO A 1 31  ? 59.018 40.074 -31.427 1.00 71.79 ? 31  PRO A CB  1 
ATOM   180  N  N   . GLU A 1 35  ? 60.315 43.290 -33.770 1.00 67.89 ? 35  GLU A N   1 
ATOM   181  C  CA  . GLU A 1 35  ? 60.023 44.382 -32.843 1.00 68.56 ? 35  GLU A CA  1 
ATOM   182  C  C   . GLU A 1 35  ? 60.676 44.159 -31.484 1.00 70.72 ? 35  GLU A C   1 
ATOM   183  O  O   . GLU A 1 35  ? 60.906 45.120 -30.756 1.00 73.38 ? 35  GLU A O   1 
ATOM   184  C  CB  . GLU A 1 35  ? 58.513 44.558 -32.655 1.00 67.54 ? 35  GLU A CB  1 
ATOM   185  N  N   . LYS A 1 36  ? 61.111 42.916 -31.254 1.00 70.21 ? 36  LYS A N   1 
ATOM   186  C  CA  . LYS A 1 36  ? 61.702 42.365 -30.003 1.00 65.62 ? 36  LYS A CA  1 
ATOM   187  C  C   . LYS A 1 36  ? 60.909 42.145 -28.678 1.00 63.75 ? 36  LYS A C   1 
ATOM   188  O  O   . LYS A 1 36  ? 61.402 42.501 -27.601 1.00 64.05 ? 36  LYS A O   1 
ATOM   189  C  CB  . LYS A 1 36  ? 62.915 43.229 -29.620 1.00 67.74 ? 36  LYS A CB  1 
ATOM   190  N  N   . GLY A 1 37  ? 59.749 41.474 -28.752 1.00 67.92 ? 37  GLY A N   1 
ATOM   191  C  CA  . GLY A 1 37  ? 59.169 40.801 -27.581 1.00 68.99 ? 37  GLY A CA  1 
ATOM   192  C  C   . GLY A 1 37  ? 60.028 39.524 -27.509 1.00 67.33 ? 37  GLY A C   1 
ATOM   193  O  O   . GLY A 1 37  ? 60.911 39.426 -28.361 1.00 64.24 ? 37  GLY A O   1 
ATOM   194  N  N   . TYR A 1 38  ? 59.847 38.513 -26.637 1.00 73.69 ? 38  TYR A N   1 
ATOM   195  C  CA  . TYR A 1 38  ? 58.844 38.292 -25.590 1.00 69.60 ? 38  TYR A CA  1 
ATOM   196  C  C   . TYR A 1 38  ? 57.409 38.087 -26.116 1.00 69.40 ? 38  TYR A C   1 
ATOM   197  O  O   . TYR A 1 38  ? 56.533 38.951 -26.010 1.00 72.32 ? 38  TYR A O   1 
ATOM   198  C  CB  . TYR A 1 38  ? 58.885 39.434 -24.562 1.00 72.56 ? 38  TYR A CB  1 
ATOM   199  N  N   . ARG A 1 39  ? 57.180 36.896 -26.657 1.00 59.08 ? 39  ARG A N   1 
ATOM   200  C  CA  . ARG A 1 39  ? 55.900 36.560 -27.265 1.00 60.01 ? 39  ARG A CA  1 
ATOM   201  C  C   . ARG A 1 39  ? 55.298 35.269 -26.648 1.00 76.80 ? 39  ARG A C   1 
ATOM   202  O  O   . ARG A 1 39  ? 54.362 35.361 -25.847 1.00 76.81 ? 39  ARG A O   1 
ATOM   203  C  CB  . ARG A 1 39  ? 56.053 36.419 -28.782 1.00 55.60 ? 39  ARG A CB  1 
ATOM   204  N  N   . MET A 1 40  ? 55.854 34.098 -26.986 1.00 62.05 ? 40  MET A N   1 
ATOM   205  C  CA  . MET A 1 40  ? 55.392 32.761 -26.518 1.00 63.67 ? 40  MET A CA  1 
ATOM   206  C  C   . MET A 1 40  ? 54.261 32.174 -27.376 1.00 56.77 ? 40  MET A C   1 
ATOM   207  O  O   . MET A 1 40  ? 53.150 32.690 -27.399 1.00 58.46 ? 40  MET A O   1 
ATOM   208  C  CB  . MET A 1 40  ? 54.942 32.775 -25.046 1.00 56.44 ? 40  MET A CB  1 
ATOM   209  C  CG  . MET A 1 40  ? 55.874 33.502 -24.057 1.00 55.87 ? 40  MET A CG  1 
ATOM   210  S  SD  . MET A 1 40  ? 57.123 32.456 -23.287 1.00 74.13 ? 40  MET A SD  1 
ATOM   211  C  CE  . MET A 1 40  ? 57.748 33.649 -22.100 1.00 53.68 ? 40  MET A CE  1 
ATOM   212  N  N   . GLN A 1 43  ? 51.251 30.307 -28.719 1.00 43.80 ? 43  GLN A N   1 
ATOM   213  C  CA  . GLN A 1 43  ? 49.902 29.793 -28.524 1.00 42.83 ? 43  GLN A CA  1 
ATOM   214  C  C   . GLN A 1 43  ? 49.871 28.319 -28.194 1.00 51.83 ? 43  GLN A C   1 
ATOM   215  O  O   . GLN A 1 43  ? 49.027 27.862 -27.416 1.00 55.65 ? 43  GLN A O   1 
ATOM   216  C  CB  . GLN A 1 43  ? 49.068 30.026 -29.776 1.00 43.99 ? 43  GLN A CB  1 
ATOM   217  C  CG  . GLN A 1 43  ? 47.641 29.475 -29.731 1.00 42.56 ? 43  GLN A CG  1 
ATOM   218  C  CD  . GLN A 1 43  ? 46.772 30.135 -28.698 1.00 56.71 ? 43  GLN A CD  1 
ATOM   219  O  OE1 . GLN A 1 43  ? 46.708 31.352 -28.645 1.00 58.48 ? 43  GLN A OE1 1 
ATOM   220  N  NE2 . GLN A 1 43  ? 46.028 29.349 -27.937 1.00 56.91 ? 43  GLN A NE2 1 
ATOM   221  N  N   . GLN A 1 44  ? 50.784 27.569 -28.789 1.00 60.57 ? 44  GLN A N   1 
ATOM   222  C  CA  . GLN A 1 44  ? 50.832 26.146 -28.544 1.00 40.02 ? 44  GLN A CA  1 
ATOM   223  C  C   . GLN A 1 44  ? 51.465 26.013 -27.174 1.00 43.10 ? 44  GLN A C   1 
ATOM   224  O  O   . GLN A 1 44  ? 51.349 24.976 -26.482 1.00 48.80 ? 44  GLN A O   1 
ATOM   225  C  CB  . GLN A 1 44  ? 51.640 25.423 -29.624 1.00 40.71 ? 44  GLN A CB  1 
ATOM   226  C  CG  . GLN A 1 44  ? 51.389 25.932 -31.045 1.00 58.99 ? 44  GLN A CG  1 
ATOM   227  N  N   . THR A 1 45  ? 52.110 27.102 -26.772 1.00 39.80 ? 45  THR A N   1 
ATOM   228  C  CA  . THR A 1 45  ? 52.699 27.187 -25.447 1.00 43.90 ? 45  THR A CA  1 
ATOM   229  C  C   . THR A 1 45  ? 51.581 27.388 -24.439 1.00 41.34 ? 45  THR A C   1 
ATOM   230  O  O   . THR A 1 45  ? 51.651 26.881 -23.313 1.00 35.28 ? 45  THR A O   1 
ATOM   231  C  CB  . THR A 1 45  ? 53.753 28.335 -25.354 1.00 40.30 ? 45  THR A CB  1 
ATOM   232  O  OG1 . THR A 1 45  ? 54.827 28.072 -26.261 1.00 42.01 ? 45  THR A OG1 1 
ATOM   233  C  CG2 . THR A 1 45  ? 54.346 28.430 -23.973 1.00 38.22 ? 45  THR A CG2 1 
ATOM   234  N  N   . VAL A 1 46  ? 50.534 28.098 -24.853 1.00 37.64 ? 46  VAL A N   1 
ATOM   235  C  CA  . VAL A 1 46  ? 49.381 28.312 -23.990 1.00 37.19 ? 46  VAL A CA  1 
ATOM   236  C  C   . VAL A 1 46  ? 48.745 26.973 -23.654 1.00 42.42 ? 46  VAL A C   1 
ATOM   237  O  O   . VAL A 1 46  ? 48.523 26.642 -22.464 1.00 36.08 ? 46  VAL A O   1 
ATOM   238  C  CB  . VAL A 1 46  ? 48.345 29.241 -24.645 1.00 40.79 ? 46  VAL A CB  1 
ATOM   239  C  CG1 . VAL A 1 46  ? 47.059 29.307 -23.814 1.00 39.45 ? 46  VAL A CG1 1 
ATOM   240  C  CG2 . VAL A 1 46  ? 48.936 30.618 -24.821 1.00 42.04 ? 46  VAL A CG2 1 
ATOM   241  N  N   . ASP A 1 47  ? 48.510 26.181 -24.702 1.00 37.24 ? 47  ASP A N   1 
ATOM   242  C  CA  . ASP A 1 47  ? 47.978 24.837 -24.537 1.00 38.54 ? 47  ASP A CA  1 
ATOM   243  C  C   . ASP A 1 47  ? 48.906 24.008 -23.627 1.00 42.34 ? 47  ASP A C   1 
ATOM   244  O  O   . ASP A 1 47  ? 48.450 23.404 -22.663 1.00 32.17 ? 47  ASP A O   1 
ATOM   245  C  CB  . ASP A 1 47  ? 47.819 24.125 -25.889 1.00 38.53 ? 47  ASP A CB  1 
ATOM   246  C  CG  . ASP A 1 47  ? 46.792 24.787 -26.816 1.00 45.15 ? 47  ASP A CG  1 
ATOM   247  O  OD1 . ASP A 1 47  ? 46.849 24.498 -28.021 1.00 57.88 ? 47  ASP A OD1 1 
ATOM   248  O  OD2 . ASP A 1 47  ? 45.923 25.564 -26.372 1.00 47.81 ? 47  ASP A OD2 1 
ATOM   249  N  N   . ARG A 1 48  ? 50.208 24.019 -23.897 1.00 34.39 ? 48  ARG A N   1 
ATOM   250  C  CA  . ARG A 1 48  ? 51.088 23.163 -23.133 1.00 32.73 ? 48  ARG A CA  1 
ATOM   251  C  C   . ARG A 1 48  ? 51.126 23.529 -21.652 1.00 33.41 ? 48  ARG A C   1 
ATOM   252  O  O   . ARG A 1 48  ? 51.106 22.655 -20.779 1.00 30.42 ? 48  ARG A O   1 
ATOM   253  C  CB  . ARG A 1 48  ? 52.485 23.207 -23.730 1.00 39.39 ? 48  ARG A CB  1 
ATOM   254  C  CG  . ARG A 1 48  ? 53.472 22.224 -23.124 1.00 41.32 ? 48  ARG A CG  1 
ATOM   255  C  CD  . ARG A 1 48  ? 54.680 22.188 -24.021 1.00 44.08 ? 48  ARG A CD  1 
ATOM   256  N  NE  . ARG A 1 48  ? 55.735 21.301 -23.550 1.00 52.66 ? 48  ARG A NE  1 
ATOM   257  C  CZ  . ARG A 1 48  ? 55.970 20.087 -24.039 1.00 45.50 ? 48  ARG A CZ  1 
ATOM   258  N  NH1 . ARG A 1 48  ? 55.209 19.580 -25.002 1.00 39.96 ? 48  ARG A NH1 1 
ATOM   259  N  NH2 . ARG A 1 48  ? 56.970 19.376 -23.550 1.00 46.39 ? 48  ARG A NH2 1 
ATOM   260  N  N   . LEU A 1 49  ? 51.130 24.825 -21.367 1.00 45.71 ? 49  LEU A N   1 
ATOM   261  C  CA  . LEU A 1 49  ? 51.149 25.292 -19.987 1.00 34.99 ? 49  LEU A CA  1 
ATOM   262  C  C   . LEU A 1 49  ? 49.831 24.978 -19.259 1.00 31.49 ? 49  LEU A C   1 
ATOM   263  O  O   . LEU A 1 49  ? 49.858 24.624 -18.073 1.00 38.04 ? 49  LEU A O   1 
ATOM   264  C  CB  . LEU A 1 49  ? 51.460 26.786 -19.955 1.00 41.30 ? 49  LEU A CB  1 
ATOM   265  C  CG  . LEU A 1 49  ? 51.732 27.389 -18.581 1.00 37.50 ? 49  LEU A CG  1 
ATOM   266  C  CD1 . LEU A 1 49  ? 52.777 26.596 -17.858 1.00 29.04 ? 49  LEU A CD1 1 
ATOM   267  C  CD2 . LEU A 1 49  ? 52.203 28.811 -18.767 1.00 39.29 ? 49  LEU A CD2 1 
ATOM   268  N  N   . HIS A 1 50  ? 48.699 25.060 -19.965 1.00 33.37 ? 50  HIS A N   1 
ATOM   269  C  CA  . HIS A 1 50  ? 47.437 24.571 -19.398 1.00 32.40 ? 50  HIS A CA  1 
ATOM   270  C  C   . HIS A 1 50  ? 47.608 23.120 -19.003 1.00 33.50 ? 50  HIS A C   1 
ATOM   271  O  O   . HIS A 1 50  ? 47.249 22.704 -17.900 1.00 31.58 ? 50  HIS A O   1 
ATOM   272  C  CB  . HIS A 1 50  ? 46.267 24.638 -20.392 1.00 35.31 ? 50  HIS A CB  1 
ATOM   273  C  CG  . HIS A 1 50  ? 45.599 25.969 -20.477 1.00 45.29 ? 50  HIS A CG  1 
ATOM   274  N  ND1 . HIS A 1 50  ? 45.063 26.609 -19.381 1.00 47.70 ? 50  HIS A ND1 1 
ATOM   275  C  CD2 . HIS A 1 50  ? 45.345 26.764 -21.543 1.00 44.07 ? 50  HIS A CD2 1 
ATOM   276  C  CE1 . HIS A 1 50  ? 44.543 27.762 -19.763 1.00 50.00 ? 50  HIS A CE1 1 
ATOM   277  N  NE2 . HIS A 1 50  ? 44.693 27.874 -21.071 1.00 44.83 ? 50  HIS A NE2 1 
ATOM   278  N  N   . PHE A 1 51  ? 48.135 22.353 -19.945 1.00 28.77 ? 51  PHE A N   1 
ATOM   279  C  CA  . PHE A 1 51  ? 48.310 20.924 -19.778 1.00 27.62 ? 51  PHE A CA  1 
ATOM   280  C  C   . PHE A 1 51  ? 49.122 20.660 -18.514 1.00 28.64 ? 51  PHE A C   1 
ATOM   281  O  O   . PHE A 1 51  ? 48.750 19.809 -17.694 1.00 26.99 ? 51  PHE A O   1 
ATOM   282  C  CB  . PHE A 1 51  ? 48.964 20.330 -21.041 1.00 27.33 ? 51  PHE A CB  1 
ATOM   283  C  CG  . PHE A 1 51  ? 49.159 18.833 -21.007 1.00 31.25 ? 51  PHE A CG  1 
ATOM   284  C  CD1 . PHE A 1 51  ? 48.246 18.002 -20.377 1.00 31.26 ? 51  PHE A CD1 1 
ATOM   285  C  CD2 . PHE A 1 51  ? 50.260 18.257 -21.635 1.00 28.50 ? 51  PHE A CD2 1 
ATOM   286  C  CE1 . PHE A 1 51  ? 48.440 16.625 -20.351 1.00 27.68 ? 51  PHE A CE1 1 
ATOM   287  C  CE2 . PHE A 1 51  ? 50.453 16.879 -21.622 1.00 31.80 ? 51  PHE A CE2 1 
ATOM   288  C  CZ  . PHE A 1 51  ? 49.549 16.068 -20.976 1.00 29.40 ? 51  PHE A CZ  1 
ATOM   289  N  N   . ILE A 1 52  ? 50.203 21.421 -18.343 1.00 26.21 ? 52  ILE A N   1 
ATOM   290  C  CA  . ILE A 1 52  ? 51.134 21.174 -17.241 1.00 40.63 ? 52  ILE A CA  1 
ATOM   291  C  C   . ILE A 1 52  ? 50.432 21.498 -15.920 1.00 30.70 ? 52  ILE A C   1 
ATOM   292  O  O   . ILE A 1 52  ? 50.435 20.698 -14.976 1.00 31.40 ? 52  ILE A O   1 
ATOM   293  C  CB  . ILE A 1 52  ? 52.464 21.998 -17.408 1.00 26.72 ? 52  ILE A CB  1 
ATOM   294  C  CG1 . ILE A 1 52  ? 53.271 21.473 -18.595 1.00 27.11 ? 52  ILE A CG1 1 
ATOM   295  C  CG2 . ILE A 1 52  ? 53.313 21.955 -16.135 1.00 25.56 ? 52  ILE A CG2 1 
ATOM   296  C  CD1 . ILE A 1 52  ? 54.377 22.403 -19.051 1.00 32.82 ? 52  ILE A CD1 1 
ATOM   297  N  N   . LYS A 1 53  ? 49.796 22.665 -15.888 1.00 27.34 ? 53  LYS A N   1 
ATOM   298  C  CA  . LYS A 1 53  ? 49.046 23.119 -14.733 1.00 28.10 ? 53  LYS A CA  1 
ATOM   299  C  C   . LYS A 1 53  ? 48.009 22.100 -14.280 1.00 36.51 ? 53  LYS A C   1 
ATOM   300  O  O   . LYS A 1 53  ? 47.936 21.754 -13.092 1.00 32.67 ? 53  LYS A O   1 
ATOM   301  C  CB  . LYS A 1 53  ? 48.351 24.438 -15.070 1.00 34.48 ? 53  LYS A CB  1 
ATOM   302  C  CG  . LYS A 1 53  ? 47.473 25.037 -13.974 1.00 29.15 ? 53  LYS A CG  1 
ATOM   303  C  CD  . LYS A 1 53  ? 48.292 25.482 -12.769 1.00 45.35 ? 53  LYS A CD  1 
ATOM   304  C  CE  . LYS A 1 53  ? 47.375 26.129 -11.757 1.00 54.47 ? 53  LYS A CE  1 
ATOM   305  N  NZ  . LYS A 1 53  ? 46.326 26.911 -12.483 1.00 58.08 ? 53  LYS A NZ  1 
ATOM   306  N  N   . ARG A 1 54  ? 47.200 21.612 -15.215 1.00 36.36 ? 54  ARG A N   1 
ATOM   307  C  CA  . ARG A 1 54  ? 46.128 20.724 -14.806 1.00 29.25 ? 54  ARG A CA  1 
ATOM   308  C  C   . ARG A 1 54  ? 46.693 19.390 -14.401 1.00 29.67 ? 54  ARG A C   1 
ATOM   309  O  O   . ARG A 1 54  ? 46.193 18.775 -13.453 1.00 33.80 ? 54  ARG A O   1 
ATOM   310  C  CB  . ARG A 1 54  ? 45.049 20.608 -15.879 1.00 31.63 ? 54  ARG A CB  1 
ATOM   311  C  CG  . ARG A 1 54  ? 44.215 21.870 -15.914 1.00 39.66 ? 54  ARG A CG  1 
ATOM   312  C  CD  . ARG A 1 54  ? 43.519 22.084 -17.220 1.00 47.27 ? 54  ARG A CD  1 
ATOM   313  N  NE  . ARG A 1 54  ? 43.103 23.480 -17.422 1.00 54.31 ? 54  ARG A NE  1 
ATOM   314  C  CZ  . ARG A 1 54  ? 42.813 23.981 -18.614 1.00 51.88 ? 54  ARG A CZ  1 
ATOM   315  N  NH1 . ARG A 1 54  ? 42.898 23.192 -19.663 1.00 47.37 ? 54  ARG A NH1 1 
ATOM   316  N  NH2 . ARG A 1 54  ? 42.424 25.241 -18.756 1.00 58.07 ? 54  ARG A NH2 1 
ATOM   317  N  N   . MET A 1 55  ? 47.784 18.965 -15.027 1.00 23.91 ? 55  MET A N   1 
ATOM   318  C  CA  . MET A 1 55  ? 48.407 17.720 -14.564 1.00 28.91 ? 55  MET A CA  1 
ATOM   319  C  C   . MET A 1 55  ? 48.849 17.870 -13.099 1.00 34.94 ? 55  MET A C   1 
ATOM   320  O  O   . MET A 1 55  ? 48.693 16.962 -12.283 1.00 32.17 ? 55  MET A O   1 
ATOM   321  C  CB  . MET A 1 55  ? 49.578 17.323 -15.470 1.00 23.31 ? 55  MET A CB  1 
ATOM   322  C  CG  . MET A 1 55  ? 49.119 16.625 -16.768 1.00 24.93 ? 55  MET A CG  1 
ATOM   323  S  SD  . MET A 1 55  ? 50.435 15.656 -17.523 1.00 54.84 ? 55  MET A SD  1 
ATOM   324  C  CE  . MET A 1 55  ? 51.603 16.960 -17.943 1.00 25.36 ? 55  MET A CE  1 
ATOM   325  N  N   . GLN A 1 56  ? 49.378 19.035 -12.754 1.00 26.96 ? 56  GLN A N   1 
ATOM   326  C  CA  . GLN A 1 56  ? 49.760 19.259 -11.371 1.00 34.19 ? 56  GLN A CA  1 
ATOM   327  C  C   . GLN A 1 56  ? 48.548 19.330 -10.442 1.00 43.11 ? 56  GLN A C   1 
ATOM   328  O  O   . GLN A 1 56  ? 48.621 18.922 -9.275  1.00 32.82 ? 56  GLN A O   1 
ATOM   329  C  CB  . GLN A 1 56  ? 50.598 20.516 -11.252 1.00 24.98 ? 56  GLN A CB  1 
ATOM   330  C  CG  . GLN A 1 56  ? 52.052 20.231 -11.455 1.00 28.28 ? 56  GLN A CG  1 
ATOM   331  C  CD  . GLN A 1 56  ? 52.875 21.478 -11.501 1.00 38.37 ? 56  GLN A CD  1 
ATOM   332  O  OE1 . GLN A 1 56  ? 52.808 22.245 -12.459 1.00 42.54 ? 56  GLN A OE1 1 
ATOM   333  N  NE2 . GLN A 1 56  ? 53.632 21.718 -10.442 1.00 41.40 ? 56  GLN A NE2 1 
ATOM   334  N  N   . GLU A 1 57  ? 47.423 19.822 -10.955 1.00 37.10 ? 57  GLU A N   1 
ATOM   335  C  CA  . GLU A 1 57  ? 46.217 19.845 -10.142 1.00 31.02 ? 57  GLU A CA  1 
ATOM   336  C  C   . GLU A 1 57  ? 45.687 18.422 -9.971  1.00 31.09 ? 57  GLU A C   1 
ATOM   337  O  O   . GLU A 1 57  ? 44.916 18.146 -9.061  1.00 32.56 ? 57  GLU A O   1 
ATOM   338  C  CB  . GLU A 1 57  ? 45.170 20.759 -10.769 1.00 33.64 ? 57  GLU A CB  1 
ATOM   339  C  CG  . GLU A 1 57  ? 45.642 22.200 -10.871 1.00 37.29 ? 57  GLU A CG  1 
ATOM   340  C  CD  . GLU A 1 57  ? 44.684 23.090 -11.638 1.00 40.30 ? 57  GLU A CD  1 
ATOM   341  O  OE1 . GLU A 1 57  ? 43.919 22.564 -12.480 1.00 34.98 ? 57  GLU A OE1 1 
ATOM   342  O  OE2 . GLU A 1 57  ? 44.709 24.319 -11.399 1.00 50.44 ? 57  GLU A OE2 1 
ATOM   343  N  N   . LEU A 1 58  ? 46.129 17.518 -10.841 1.00 25.20 ? 58  LEU A N   1 
ATOM   344  C  CA  . LEU A 1 58  ? 45.750 16.119 -10.761 1.00 24.86 ? 58  LEU A CA  1 
ATOM   345  C  C   . LEU A 1 58  ? 46.767 15.228 -10.033 1.00 31.97 ? 58  LEU A C   1 
ATOM   346  O  O   . LEU A 1 58  ? 46.629 14.006 -10.013 1.00 25.80 ? 58  LEU A O   1 
ATOM   347  C  CB  . LEU A 1 58  ? 45.497 15.591 -12.164 1.00 30.05 ? 58  LEU A CB  1 
ATOM   348  C  CG  . LEU A 1 58  ? 44.225 16.245 -12.701 1.00 34.01 ? 58  LEU A CG  1 
ATOM   349  C  CD1 . LEU A 1 58  ? 43.990 15.884 -14.163 1.00 33.79 ? 58  LEU A CD1 1 
ATOM   350  C  CD2 . LEU A 1 58  ? 43.042 15.876 -11.828 1.00 28.92 ? 58  LEU A CD2 1 
ATOM   351  N  N   . GLY A 1 59  ? 47.809 15.822 -9.471  1.00 28.89 ? 59  GLY A N   1 
ATOM   352  C  CA  . GLY A 1 59  ? 48.748 15.055 -8.680  1.00 24.02 ? 59  GLY A CA  1 
ATOM   353  C  C   . GLY A 1 59  ? 50.004 14.579 -9.394  1.00 23.64 ? 59  GLY A C   1 
ATOM   354  O  O   . GLY A 1 59  ? 50.776 13.804 -8.827  1.00 32.60 ? 59  GLY A O   1 
ATOM   355  N  N   . PHE A 1 60  ? 50.236 15.003 -10.628 1.00 24.12 ? 60  PHE A N   1 
ATOM   356  C  CA  . PHE A 1 60  ? 51.547 14.729 -11.216 1.00 23.99 ? 60  PHE A CA  1 
ATOM   357  C  C   . PHE A 1 60  ? 52.576 15.697 -10.676 1.00 24.10 ? 60  PHE A C   1 
ATOM   358  O  O   . PHE A 1 60  ? 52.327 16.893 -10.642 1.00 23.75 ? 60  PHE A O   1 
ATOM   359  C  CB  . PHE A 1 60  ? 51.559 14.873 -12.727 1.00 23.26 ? 60  PHE A CB  1 
ATOM   360  C  CG  . PHE A 1 60  ? 50.692 13.912 -13.465 1.00 23.35 ? 60  PHE A CG  1 
ATOM   361  C  CD1 . PHE A 1 60  ? 51.249 12.829 -14.128 1.00 33.61 ? 60  PHE A CD1 1 
ATOM   362  C  CD2 . PHE A 1 60  ? 49.332 14.133 -13.577 1.00 23.28 ? 60  PHE A CD2 1 
ATOM   363  C  CE1 . PHE A 1 60  ? 50.459 11.976 -14.866 1.00 24.01 ? 60  PHE A CE1 1 
ATOM   364  C  CE2 . PHE A 1 60  ? 48.543 13.276 -14.291 1.00 23.60 ? 60  PHE A CE2 1 
ATOM   365  C  CZ  . PHE A 1 60  ? 49.108 12.203 -14.943 1.00 23.95 ? 60  PHE A CZ  1 
ATOM   366  N  N   . THR A 1 61  ? 53.731 15.196 -10.270 1.00 24.20 ? 61  THR A N   1 
ATOM   367  C  CA  . THR A 1 61  ? 54.859 16.071 -9.917  1.00 27.50 ? 61  THR A CA  1 
ATOM   368  C  C   . THR A 1 61  ? 55.560 16.600 -11.158 1.00 31.35 ? 61  THR A C   1 
ATOM   369  O  O   . THR A 1 61  ? 55.437 16.032 -12.257 1.00 28.42 ? 61  THR A O   1 
ATOM   370  C  CB  . THR A 1 61  ? 55.934 15.384 -9.059  1.00 25.99 ? 61  THR A CB  1 
ATOM   371  O  OG1 . THR A 1 61  ? 56.668 14.482 -9.887  1.00 26.24 ? 61  THR A OG1 1 
ATOM   372  C  CG2 . THR A 1 61  ? 55.356 14.666 -7.862  1.00 27.03 ? 61  THR A CG2 1 
ATOM   373  N  N   . LEU A 1 62  ? 56.309 17.681 -10.957 1.00 36.42 ? 62  LEU A N   1 
ATOM   374  C  CA  . LEU A 1 62  ? 57.100 18.310 -12.000 1.00 37.45 ? 62  LEU A CA  1 
ATOM   375  C  C   . LEU A 1 62  ? 58.068 17.334 -12.652 1.00 29.65 ? 62  LEU A C   1 
ATOM   376  O  O   . LEU A 1 62  ? 58.250 17.343 -13.861 1.00 27.17 ? 62  LEU A O   1 
ATOM   377  C  CB  . LEU A 1 62  ? 57.891 19.471 -11.411 1.00 27.73 ? 62  LEU A CB  1 
ATOM   378  C  CG  . LEU A 1 62  ? 57.198 20.813 -11.612 1.00 38.13 ? 62  LEU A CG  1 
ATOM   379  C  CD1 . LEU A 1 62  ? 57.958 21.900 -10.875 1.00 46.32 ? 62  LEU A CD1 1 
ATOM   380  C  CD2 . LEU A 1 62  ? 57.039 21.136 -13.089 1.00 36.31 ? 62  LEU A CD2 1 
ATOM   381  N  N   . ASN A 1 63  ? 58.699 16.505 -11.836 1.00 28.70 ? 63  ASN A N   1 
ATOM   382  C  CA  . ASN A 1 63  ? 59.594 15.495 -12.352 1.00 29.42 ? 63  ASN A CA  1 
ATOM   383  C  C   . ASN A 1 63  ? 58.848 14.481 -13.251 1.00 33.78 ? 63  ASN A C   1 
ATOM   384  O  O   . ASN A 1 63  ? 59.281 14.145 -14.377 1.00 36.24 ? 63  ASN A O   1 
ATOM   385  C  CB  . ASN A 1 63  ? 60.282 14.811 -11.199 1.00 35.05 ? 63  ASN A CB  1 
ATOM   386  C  CG  . ASN A 1 63  ? 61.546 14.127 -11.621 1.00 50.99 ? 63  ASN A CG  1 
ATOM   387  O  OD1 . ASN A 1 63  ? 61.651 12.903 -11.571 1.00 61.68 ? 63  ASN A OD1 1 
ATOM   388  N  ND2 . ASN A 1 63  ? 62.520 14.919 -12.072 1.00 38.84 ? 63  ASN A ND2 1 
ATOM   389  N  N   . GLU A 1 64  ? 57.714 14.008 -12.748 1.00 28.16 ? 64  GLU A N   1 
ATOM   390  C  CA  . GLU A 1 64  ? 56.848 13.156 -13.529 1.00 27.70 ? 64  GLU A CA  1 
ATOM   391  C  C   . GLU A 1 64  ? 56.461 13.799 -14.841 1.00 27.94 ? 64  GLU A C   1 
ATOM   392  O  O   . GLU A 1 64  ? 56.562 13.172 -15.891 1.00 33.97 ? 64  GLU A O   1 
ATOM   393  C  CB  . GLU A 1 64  ? 55.606 12.807 -12.722 1.00 27.54 ? 64  GLU A CB  1 
ATOM   394  C  CG  . GLU A 1 64  ? 55.954 11.979 -11.522 1.00 28.95 ? 64  GLU A CG  1 
ATOM   395  C  CD  . GLU A 1 64  ? 54.760 11.529 -10.699 1.00 38.66 ? 64  GLU A CD  1 
ATOM   396  O  OE1 . GLU A 1 64  ? 53.765 12.271 -10.601 1.00 29.75 ? 64  GLU A OE1 1 
ATOM   397  O  OE2 . GLU A 1 64  ? 54.824 10.410 -10.150 1.00 50.04 ? 64  GLU A OE2 1 
ATOM   398  N  N   . ILE A 1 65  ? 56.068 15.067 -14.791 1.00 29.60 ? 65  ILE A N   1 
ATOM   399  C  CA  . ILE A 1 65  ? 55.648 15.783 -15.991 1.00 27.53 ? 65  ILE A CA  1 
ATOM   400  C  C   . ILE A 1 65  ? 56.817 15.960 -16.964 1.00 32.41 ? 65  ILE A C   1 
ATOM   401  O  O   . ILE A 1 65  ? 56.651 15.943 -18.191 1.00 28.30 ? 65  ILE A O   1 
ATOM   402  C  CB  . ILE A 1 65  ? 55.035 17.140 -15.608 1.00 27.11 ? 65  ILE A CB  1 
ATOM   403  C  CG1 . ILE A 1 65  ? 53.654 16.931 -14.986 1.00 32.07 ? 65  ILE A CG1 1 
ATOM   404  C  CG2 . ILE A 1 65  ? 54.935 18.092 -16.801 1.00 27.12 ? 65  ILE A CG2 1 
ATOM   405  C  CD1 . ILE A 1 65  ? 53.018 18.200 -14.448 1.00 29.21 ? 65  ILE A CD1 1 
ATOM   406  N  N   . ASP A 1 66  ? 58.005 16.122 -16.404 1.00 31.15 ? 66  ASP A N   1 
ATOM   407  C  CA  . ASP A 1 66  ? 59.233 16.266 -17.171 1.00 35.03 ? 66  ASP A CA  1 
ATOM   408  C  C   . ASP A 1 66  ? 59.432 15.020 -18.024 1.00 32.33 ? 66  ASP A C   1 
ATOM   409  O  O   . ASP A 1 66  ? 59.499 15.083 -19.276 1.00 31.76 ? 66  ASP A O   1 
ATOM   410  C  CB  . ASP A 1 66  ? 60.391 16.498 -16.190 1.00 42.09 ? 66  ASP A CB  1 
ATOM   411  C  CG  . ASP A 1 66  ? 61.642 17.061 -16.838 1.00 42.41 ? 66  ASP A CG  1 
ATOM   412  O  OD1 . ASP A 1 66  ? 62.336 17.822 -16.134 1.00 51.47 ? 66  ASP A OD1 1 
ATOM   413  O  OD2 . ASP A 1 66  ? 61.939 16.767 -18.016 1.00 43.16 ? 66  ASP A OD2 1 
ATOM   414  N  N   . LYS A 1 67  ? 59.435 13.877 -17.345 1.00 33.26 ? 67  LYS A N   1 
ATOM   415  C  CA  . LYS A 1 67  ? 59.612 12.607 -18.041 1.00 36.54 ? 67  LYS A CA  1 
ATOM   416  C  C   . LYS A 1 67  ? 58.529 12.393 -19.090 1.00 31.63 ? 67  LYS A C   1 
ATOM   417  O  O   . LYS A 1 67  ? 58.810 12.163 -20.281 1.00 32.10 ? 67  LYS A O   1 
ATOM   418  C  CB  . LYS A 1 67  ? 59.605 11.456 -17.049 1.00 35.54 ? 67  LYS A CB  1 
ATOM   419  C  CG  . LYS A 1 67  ? 60.664 11.574 -15.966 1.00 46.83 ? 67  LYS A CG  1 
ATOM   420  C  CD  . LYS A 1 67  ? 60.374 10.627 -14.817 1.00 45.21 ? 67  LYS A CD  1 
ATOM   421  C  CE  . LYS A 1 67  ? 61.619 9.876  -14.393 1.00 53.76 ? 67  LYS A CE  1 
ATOM   422  N  NZ  . LYS A 1 67  ? 62.656 10.775 -13.834 1.00 56.04 ? 67  LYS A NZ  1 
ATOM   423  N  N   . LEU A 1 68  ? 57.290 12.490 -18.623 1.00 29.13 ? 68  LEU A N   1 
ATOM   424  C  CA  . LEU A 1 68  ? 56.108 12.242 -19.427 1.00 28.41 ? 68  LEU A CA  1 
ATOM   425  C  C   . LEU A 1 68  ? 56.155 13.039 -20.717 1.00 33.70 ? 68  LEU A C   1 
ATOM   426  O  O   . LEU A 1 68  ? 55.957 12.486 -21.792 1.00 30.31 ? 68  LEU A O   1 
ATOM   427  C  CB  . LEU A 1 68  ? 54.861 12.576 -18.605 1.00 30.74 ? 68  LEU A CB  1 
ATOM   428  C  CG  . LEU A 1 68  ? 53.419 12.559 -19.127 1.00 38.91 ? 68  LEU A CG  1 
ATOM   429  C  CD1 . LEU A 1 68  ? 52.553 12.439 -17.913 1.00 49.75 ? 68  LEU A CD1 1 
ATOM   430  C  CD2 . LEU A 1 68  ? 53.022 13.808 -19.901 1.00 31.07 ? 68  LEU A CD2 1 
ATOM   431  N  N   . LEU A 1 69  ? 56.435 14.337 -20.601 1.00 34.36 ? 69  LEU A N   1 
ATOM   432  C  CA  . LEU A 1 69  ? 56.498 15.205 -21.767 1.00 37.28 ? 69  LEU A CA  1 
ATOM   433  C  C   . LEU A 1 69  ? 57.596 14.731 -22.693 1.00 41.01 ? 69  LEU A C   1 
ATOM   434  O  O   . LEU A 1 69  ? 57.461 14.847 -23.906 1.00 33.12 ? 69  LEU A O   1 
ATOM   435  C  CB  . LEU A 1 69  ? 56.754 16.664 -21.385 1.00 37.10 ? 69  LEU A CB  1 
ATOM   436  C  CG  . LEU A 1 69  ? 55.612 17.539 -20.859 1.00 42.24 ? 69  LEU A CG  1 
ATOM   437  C  CD1 . LEU A 1 69  ? 56.132 18.932 -20.510 1.00 32.01 ? 69  LEU A CD1 1 
ATOM   438  C  CD2 . LEU A 1 69  ? 54.441 17.613 -21.836 1.00 35.37 ? 69  LEU A CD2 1 
ATOM   439  N  N   . GLY A 1 70  ? 58.692 14.223 -22.139 1.00 34.20 ? 70  GLY A N   1 
ATOM   440  C  CA  . GLY A 1 70  ? 59.727 13.695 -23.023 1.00 36.83 ? 70  GLY A CA  1 
ATOM   441  C  C   . GLY A 1 70  ? 59.215 12.545 -23.880 1.00 38.23 ? 70  GLY A C   1 
ATOM   442  O  O   . GLY A 1 70  ? 59.320 12.544 -25.131 1.00 39.14 ? 70  GLY A O   1 
ATOM   443  N  N   . VAL A 1 71  ? 58.590 11.584 -23.206 1.00 34.04 ? 71  VAL A N   1 
ATOM   444  C  CA  . VAL A 1 71  ? 58.060 10.419 -23.897 1.00 36.40 ? 71  VAL A CA  1 
ATOM   445  C  C   . VAL A 1 71  ? 56.991 10.810 -24.917 1.00 36.30 ? 71  VAL A C   1 
ATOM   446  O  O   . VAL A 1 71  ? 57.125 10.509 -26.108 1.00 37.88 ? 71  VAL A O   1 
ATOM   447  C  CB  . VAL A 1 71  ? 57.485 9.399  -22.903 1.00 35.06 ? 71  VAL A CB  1 
ATOM   448  C  CG1 . VAL A 1 71  ? 56.876 8.248  -23.628 1.00 34.81 ? 71  VAL A CG1 1 
ATOM   449  C  CG2 . VAL A 1 71  ? 58.570 8.907  -21.990 1.00 33.06 ? 71  VAL A CG2 1 
ATOM   450  N  N   . VAL A 1 72  ? 55.957 11.514 -24.462 1.00 34.54 ? 72  VAL A N   1 
ATOM   451  C  CA  . VAL A 1 72  ? 54.831 11.872 -25.325 1.00 41.66 ? 72  VAL A CA  1 
ATOM   452  C  C   . VAL A 1 72  ? 55.269 12.762 -26.477 1.00 34.18 ? 72  VAL A C   1 
ATOM   453  O  O   . VAL A 1 72  ? 54.805 12.596 -27.595 1.00 35.08 ? 72  VAL A O   1 
ATOM   454  C  CB  . VAL A 1 72  ? 53.678 12.557 -24.540 1.00 33.53 ? 72  VAL A CB  1 
ATOM   455  C  CG1 . VAL A 1 72  ? 52.516 12.891 -25.469 1.00 35.28 ? 72  VAL A CG1 1 
ATOM   456  C  CG2 . VAL A 1 72  ? 53.177 11.660 -23.449 1.00 28.17 ? 72  VAL A CG2 1 
ATOM   457  N  N   . ASP A 1 73  ? 56.149 13.721 -26.217 1.00 35.08 ? 73  ASP A N   1 
ATOM   458  C  CA  . ASP A 1 73  ? 56.658 14.534 -27.318 1.00 40.92 ? 73  ASP A CA  1 
ATOM   459  C  C   . ASP A 1 73  ? 57.383 13.711 -28.353 1.00 40.82 ? 73  ASP A C   1 
ATOM   460  O  O   . ASP A 1 73  ? 57.265 14.021 -29.518 1.00 39.73 ? 73  ASP A O   1 
ATOM   461  C  CB  . ASP A 1 73  ? 57.587 15.643 -26.836 1.00 35.93 ? 73  ASP A CB  1 
ATOM   462  C  CG  . ASP A 1 73  ? 56.838 16.788 -26.200 1.00 42.61 ? 73  ASP A CG  1 
ATOM   463  O  OD1 . ASP A 1 73  ? 55.598 16.919 -26.416 1.00 39.69 ? 73  ASP A OD1 1 
ATOM   464  O  OD2 . ASP A 1 73  ? 57.498 17.556 -25.477 1.00 49.77 ? 73  ASP A OD2 1 
ATOM   465  N  N   . ARG A 1 74  ? 58.101 12.656 -27.959 1.00 41.31 ? 74  ARG A N   1 
ATOM   466  C  CA  . ARG A 1 74  ? 58.875 11.929 -28.972 1.00 44.49 ? 74  ARG A CA  1 
ATOM   467  C  C   . ARG A 1 74  ? 58.199 10.709 -29.628 1.00 46.50 ? 74  ARG A C   1 
ATOM   468  O  O   . ARG A 1 74  ? 58.784 10.084 -30.506 1.00 43.45 ? 74  ARG A O   1 
ATOM   469  C  CB  . ARG A 1 74  ? 60.207 11.477 -28.362 1.00 47.92 ? 74  ARG A CB  1 
ATOM   470  C  CG  . ARG A 1 74  ? 61.134 12.645 -28.017 1.00 51.41 ? 74  ARG A CG  1 
ATOM   471  C  CD  . ARG A 1 74  ? 62.500 12.175 -27.607 1.00 51.91 ? 74  ARG A CD  1 
ATOM   472  N  NE  . ARG A 1 74  ? 62.427 11.367 -26.397 1.00 56.26 ? 74  ARG A NE  1 
ATOM   473  C  CZ  . ARG A 1 74  ? 62.464 11.858 -25.156 1.00 61.85 ? 74  ARG A CZ  1 
ATOM   474  N  NH1 . ARG A 1 74  ? 62.581 13.170 -24.962 1.00 64.63 ? 74  ARG A NH1 1 
ATOM   475  N  NH2 . ARG A 1 74  ? 62.395 11.032 -24.109 1.00 64.28 ? 74  ARG A NH2 1 
ATOM   476  N  N   . ASP A 1 75  ? 56.955 10.411 -29.274 1.00 40.67 ? 75  ASP A N   1 
ATOM   477  C  CA  . ASP A 1 75  ? 56.342 9.153  -29.700 1.00 41.88 ? 75  ASP A CA  1 
ATOM   478  C  C   . ASP A 1 75  ? 55.209 9.322  -30.718 1.00 46.22 ? 75  ASP A C   1 
ATOM   479  O  O   . ASP A 1 75  ? 54.529 10.357 -30.775 1.00 36.77 ? 75  ASP A O   1 
ATOM   480  C  CB  . ASP A 1 75  ? 55.805 8.390  -28.480 1.00 47.71 ? 75  ASP A CB  1 
ATOM   481  C  CG  . ASP A 1 75  ? 56.877 7.554  -27.765 1.00 46.22 ? 75  ASP A CG  1 
ATOM   482  O  OD1 . ASP A 1 75  ? 58.009 7.446  -28.274 1.00 48.08 ? 75  ASP A OD1 1 
ATOM   483  O  OD2 . ASP A 1 75  ? 56.582 6.989  -26.686 1.00 43.61 ? 75  ASP A OD2 1 
ATOM   484  N  N   . GLU A 1 76  ? 55.013 8.279  -31.521 1.00 42.97 ? 76  GLU A N   1 
ATOM   485  C  CA  . GLU A 1 76  ? 53.919 8.247  -32.467 1.00 40.18 ? 76  GLU A CA  1 
ATOM   486  C  C   . GLU A 1 76  ? 52.606 8.031  -31.751 1.00 39.26 ? 76  GLU A C   1 
ATOM   487  O  O   . GLU A 1 76  ? 51.640 8.762  -31.979 1.00 36.58 ? 76  GLU A O   1 
ATOM   488  C  CB  . GLU A 1 76  ? 54.138 7.163  -33.509 1.00 44.77 ? 76  GLU A CB  1 
ATOM   489  C  CG  . GLU A 1 76  ? 55.232 7.491  -34.516 1.00 58.28 ? 76  GLU A CG  1 
ATOM   490  C  CD  . GLU A 1 76  ? 54.981 8.789  -35.271 1.00 66.19 ? 76  GLU A CD  1 
ATOM   491  O  OE1 . GLU A 1 76  ? 54.609 8.722  -36.463 1.00 70.46 ? 76  GLU A OE1 1 
ATOM   492  O  OE2 . GLU A 1 76  ? 55.163 9.880  -34.680 1.00 68.51 ? 76  GLU A OE2 1 
ATOM   493  N  N   . ALA A 1 77  ? 52.557 7.064  -30.847 1.00 45.28 ? 77  ALA A N   1 
ATOM   494  C  CA  . ALA A 1 77  ? 51.280 6.837  -30.212 1.00 41.52 ? 77  ALA A CA  1 
ATOM   495  C  C   . ALA A 1 77  ? 51.272 7.601  -28.894 1.00 36.37 ? 77  ALA A C   1 
ATOM   496  O  O   . ALA A 1 77  ? 51.561 7.065  -27.825 1.00 32.07 ? 77  ALA A O   1 
ATOM   497  C  CB  . ALA A 1 77  ? 51.063 5.344  -29.989 1.00 35.95 ? 77  ALA A CB  1 
ATOM   498  N  N   . LYS A 1 78  ? 50.752 8.819  -28.976 1.00 30.45 ? 78  LYS A N   1 
ATOM   499  C  CA  . LYS A 1 78  ? 50.799 9.721  -27.859 1.00 42.66 ? 78  LYS A CA  1 
ATOM   500  C  C   . LYS A 1 78  ? 49.669 9.367  -26.906 1.00 46.66 ? 78  LYS A C   1 
ATOM   501  O  O   . LYS A 1 78  ? 49.852 9.345  -25.699 1.00 39.29 ? 78  LYS A O   1 
ATOM   502  C  CB  . LYS A 1 78  ? 50.698 11.164 -28.345 1.00 44.92 ? 78  LYS A CB  1 
ATOM   503  C  CG  . LYS A 1 78  ? 51.778 11.542 -29.340 1.00 32.33 ? 78  LYS A CG  1 
ATOM   504  C  CD  . LYS A 1 78  ? 51.776 13.031 -29.602 1.00 38.25 ? 78  LYS A CD  1 
ATOM   505  C  CE  . LYS A 1 78  ? 52.806 13.410 -30.649 1.00 37.17 ? 78  LYS A CE  1 
ATOM   506  N  NZ  . LYS A 1 78  ? 54.144 12.879 -30.275 1.00 50.08 ? 78  LYS A NZ  1 
ATOM   507  N  N   . CYS A 1 79  ? 48.512 9.064  -27.481 1.00 43.17 ? 79  CYS A N   1 
ATOM   508  C  CA  . CYS A 1 79  ? 47.337 8.667  -26.736 1.00 27.26 ? 79  CYS A CA  1 
ATOM   509  C  C   . CYS A 1 79  ? 47.614 7.461  -25.861 1.00 30.69 ? 79  CYS A C   1 
ATOM   510  O  O   . CYS A 1 79  ? 47.220 7.426  -24.707 1.00 28.23 ? 79  CYS A O   1 
ATOM   511  C  CB  . CYS A 1 79  ? 46.214 8.380  -27.704 1.00 27.75 ? 79  CYS A CB  1 
ATOM   512  S  SG  . CYS A 1 79  ? 44.758 7.707  -26.974 1.00 27.11 ? 79  CYS A SG  1 
ATOM   513  N  N   . ARG A 1 80  ? 48.302 6.470  -26.420 1.00 42.31 ? 80  ARG A N   1 
ATOM   514  C  CA  . ARG A 1 80  ? 48.661 5.257  -25.685 1.00 28.75 ? 80  ARG A CA  1 
ATOM   515  C  C   . ARG A 1 80  ? 49.551 5.613  -24.497 1.00 28.44 ? 80  ARG A C   1 
ATOM   516  O  O   . ARG A 1 80  ? 49.340 5.133  -23.373 1.00 33.30 ? 80  ARG A O   1 
ATOM   517  C  CB  . ARG A 1 80  ? 49.355 4.262  -26.627 1.00 31.00 ? 80  ARG A CB  1 
ATOM   518  C  CG  . ARG A 1 80  ? 49.944 2.993  -25.975 1.00 35.96 ? 80  ARG A CG  1 
ATOM   519  C  CD  . ARG A 1 80  ? 48.978 1.839  -25.936 1.00 34.08 ? 80  ARG A CD  1 
ATOM   520  N  NE  . ARG A 1 80  ? 48.212 1.834  -24.697 1.00 30.98 ? 80  ARG A NE  1 
ATOM   521  C  CZ  . ARG A 1 80  ? 47.291 0.929  -24.368 1.00 32.98 ? 80  ARG A CZ  1 
ATOM   522  N  NH1 . ARG A 1 80  ? 47.000 -0.081 -25.185 1.00 31.93 ? 80  ARG A NH1 1 
ATOM   523  N  NH2 . ARG A 1 80  ? 46.663 1.034  -23.201 1.00 35.29 ? 80  ARG A NH2 1 
ATOM   524  N  N   . ASP A 1 81  ? 50.534 6.469  -24.749 1.00 33.10 ? 81  ASP A N   1 
ATOM   525  C  CA  . ASP A 1 81  ? 51.453 6.924  -23.718 1.00 32.97 ? 81  ASP A CA  1 
ATOM   526  C  C   . ASP A 1 81  ? 50.710 7.639  -22.596 1.00 28.06 ? 81  ASP A C   1 
ATOM   527  O  O   . ASP A 1 81  ? 50.863 7.322  -21.423 1.00 28.42 ? 81  ASP A O   1 
ATOM   528  C  CB  . ASP A 1 81  ? 52.507 7.855  -24.309 1.00 41.20 ? 81  ASP A CB  1 
ATOM   529  C  CG  . ASP A 1 81  ? 53.507 7.130  -25.200 1.00 36.78 ? 81  ASP A CG  1 
ATOM   530  O  OD1 . ASP A 1 81  ? 53.624 5.890  -25.129 1.00 31.68 ? 81  ASP A OD1 1 
ATOM   531  O  OD2 . ASP A 1 81  ? 54.186 7.818  -25.980 1.00 34.41 ? 81  ASP A OD2 1 
ATOM   532  N  N   . MET A 1 82  ? 49.915 8.622  -22.967 1.00 27.75 ? 82  MET A N   1 
ATOM   533  C  CA  . MET A 1 82  ? 49.189 9.423  -22.002 1.00 40.81 ? 82  MET A CA  1 
ATOM   534  C  C   . MET A 1 82  ? 48.215 8.568  -21.193 1.00 29.96 ? 82  MET A C   1 
ATOM   535  O  O   . MET A 1 82  ? 48.028 8.778  -19.992 1.00 25.91 ? 82  MET A O   1 
ATOM   536  C  CB  . MET A 1 82  ? 48.453 10.552 -22.723 1.00 26.82 ? 82  MET A CB  1 
ATOM   537  C  CG  . MET A 1 82  ? 47.865 11.597 -21.802 1.00 26.33 ? 82  MET A CG  1 
ATOM   538  S  SD  . MET A 1 82  ? 49.114 12.295 -20.721 1.00 27.78 ? 82  MET A SD  1 
ATOM   539  C  CE  . MET A 1 82  ? 50.270 12.862 -21.963 1.00 52.61 ? 82  MET A CE  1 
ATOM   540  N  N   . TYR A 1 83  ? 47.600 7.607  -21.873 1.00 25.92 ? 83  TYR A N   1 
ATOM   541  C  CA  . TYR A 1 83  ? 46.697 6.667  -21.233 1.00 32.62 ? 83  TYR A CA  1 
ATOM   542  C  C   . TYR A 1 83  ? 47.448 5.880  -20.146 1.00 27.78 ? 83  TYR A C   1 
ATOM   543  O  O   . TYR A 1 83  ? 47.041 5.884  -18.973 1.00 28.40 ? 83  TYR A O   1 
ATOM   544  C  CB  . TYR A 1 83  ? 46.068 5.720  -22.275 1.00 28.14 ? 83  TYR A CB  1 
ATOM   545  C  CG  . TYR A 1 83  ? 45.089 4.724  -21.693 1.00 30.29 ? 83  TYR A CG  1 
ATOM   546  C  CD1 . TYR A 1 83  ? 43.760 5.069  -21.430 1.00 29.67 ? 83  TYR A CD1 1 
ATOM   547  C  CD2 . TYR A 1 83  ? 45.516 3.455  -21.336 1.00 28.83 ? 83  TYR A CD2 1 
ATOM   548  C  CE1 . TYR A 1 83  ? 42.879 4.134  -20.866 1.00 25.83 ? 83  TYR A CE1 1 
ATOM   549  C  CE2 . TYR A 1 83  ? 44.667 2.543  -20.779 1.00 28.38 ? 83  TYR A CE2 1 
ATOM   550  C  CZ  . TYR A 1 83  ? 43.353 2.863  -20.547 1.00 30.00 ? 83  TYR A CZ  1 
ATOM   551  O  OH  . TYR A 1 83  ? 42.540 1.883  -19.997 1.00 27.24 ? 83  TYR A OH  1 
ATOM   552  N  N   . ASP A 1 84  ? 48.561 5.255  -20.540 1.00 25.61 ? 84  ASP A N   1 
ATOM   553  C  CA  . ASP A 1 84  ? 49.414 4.510  -19.619 1.00 25.27 ? 84  ASP A CA  1 
ATOM   554  C  C   . ASP A 1 84  ? 49.841 5.331  -18.398 1.00 32.48 ? 84  ASP A C   1 
ATOM   555  O  O   . ASP A 1 84  ? 49.686 4.897  -17.233 1.00 25.82 ? 84  ASP A O   1 
ATOM   556  C  CB  . ASP A 1 84  ? 50.672 4.028  -20.341 1.00 26.43 ? 84  ASP A CB  1 
ATOM   557  C  CG  . ASP A 1 84  ? 50.401 2.886  -21.307 1.00 31.63 ? 84  ASP A CG  1 
ATOM   558  O  OD1 . ASP A 1 84  ? 49.357 2.198  -21.183 1.00 30.07 ? 84  ASP A OD1 1 
ATOM   559  O  OD2 . ASP A 1 84  ? 51.255 2.660  -22.193 1.00 39.09 ? 84  ASP A OD2 1 
ATOM   560  N  N   . PHE A 1 85  ? 50.360 6.524  -18.664 1.00 25.38 ? 85  PHE A N   1 
ATOM   561  C  CA  . PHE A 1 85  ? 50.827 7.377  -17.599 1.00 25.14 ? 85  PHE A CA  1 
ATOM   562  C  C   . PHE A 1 85  ? 49.696 7.718  -16.647 1.00 25.54 ? 85  PHE A C   1 
ATOM   563  O  O   . PHE A 1 85  ? 49.907 7.825  -15.436 1.00 24.00 ? 85  PHE A O   1 
ATOM   564  C  CB  . PHE A 1 85  ? 51.420 8.659  -18.152 1.00 25.38 ? 85  PHE A CB  1 
ATOM   565  C  CG  . PHE A 1 85  ? 52.746 8.484  -18.805 1.00 30.87 ? 85  PHE A CG  1 
ATOM   566  C  CD1 . PHE A 1 85  ? 53.799 7.913  -18.113 1.00 33.27 ? 85  PHE A CD1 1 
ATOM   567  C  CD2 . PHE A 1 85  ? 52.966 8.959  -20.097 1.00 27.04 ? 85  PHE A CD2 1 
ATOM   568  C  CE1 . PHE A 1 85  ? 55.050 7.782  -18.702 1.00 35.01 ? 85  PHE A CE1 1 
ATOM   569  C  CE2 . PHE A 1 85  ? 54.208 8.840  -20.686 1.00 30.84 ? 85  PHE A CE2 1 
ATOM   570  C  CZ  . PHE A 1 85  ? 55.259 8.247  -19.983 1.00 34.75 ? 85  PHE A CZ  1 
ATOM   571  N  N   . THR A 1 86  ? 48.504 7.904  -17.207 1.00 23.92 ? 86  THR A N   1 
ATOM   572  C  CA  . THR A 1 86  ? 47.326 8.245  -16.414 1.00 23.22 ? 86  THR A CA  1 
ATOM   573  C  C   . THR A 1 86  ? 46.933 7.101  -15.474 1.00 26.47 ? 86  THR A C   1 
ATOM   574  O  O   . THR A 1 86  ? 46.560 7.341  -14.308 1.00 22.83 ? 86  THR A O   1 
ATOM   575  C  CB  . THR A 1 86  ? 46.143 8.644  -17.319 1.00 27.00 ? 86  THR A CB  1 
ATOM   576  O  OG1 . THR A 1 86  ? 46.539 9.772  -18.102 1.00 30.92 ? 86  THR A OG1 1 
ATOM   577  C  CG2 . THR A 1 86  ? 44.909 9.029  -16.493 1.00 23.53 ? 86  THR A CG2 1 
ATOM   578  N  N   . ILE A 1 87  ? 47.016 5.867  -15.980 1.00 24.78 ? 87  ILE A N   1 
ATOM   579  C  CA  . ILE A 1 87  ? 46.790 4.677  -15.147 1.00 29.53 ? 87  ILE A CA  1 
ATOM   580  C  C   . ILE A 1 87  ? 47.797 4.646  -13.995 1.00 24.95 ? 87  ILE A C   1 
ATOM   581  O  O   . ILE A 1 87  ? 47.442 4.353  -12.830 1.00 24.85 ? 87  ILE A O   1 
ATOM   582  C  CB  . ILE A 1 87  ? 46.929 3.353  -15.956 1.00 33.96 ? 87  ILE A CB  1 
ATOM   583  C  CG1 . ILE A 1 87  ? 45.798 3.183  -16.954 1.00 26.73 ? 87  ILE A CG1 1 
ATOM   584  C  CG2 . ILE A 1 87  ? 46.963 2.137  -15.020 1.00 26.22 ? 87  ILE A CG2 1 
ATOM   585  C  CD1 . ILE A 1 87  ? 44.475 2.888  -16.324 1.00 28.59 ? 87  ILE A CD1 1 
ATOM   586  N  N   . LEU A 1 88  ? 49.058 4.950  -14.325 1.00 24.70 ? 88  LEU A N   1 
ATOM   587  C  CA  . LEU A 1 88  ? 50.102 4.970  -13.303 1.00 34.69 ? 88  LEU A CA  1 
ATOM   588  C  C   . LEU A 1 88  ? 49.789 6.024  -12.244 1.00 22.60 ? 88  LEU A C   1 
ATOM   589  O  O   . LEU A 1 88  ? 49.969 5.798  -11.051 1.00 22.67 ? 88  LEU A O   1 
ATOM   590  C  CB  . LEU A 1 88  ? 51.481 5.259  -13.908 1.00 24.25 ? 88  LEU A CB  1 
ATOM   591  C  CG  . LEU A 1 88  ? 52.172 4.213  -14.788 1.00 34.15 ? 88  LEU A CG  1 
ATOM   592  C  CD1 . LEU A 1 88  ? 53.514 4.759  -15.299 1.00 33.97 ? 88  LEU A CD1 1 
ATOM   593  C  CD2 . LEU A 1 88  ? 52.365 2.880  -14.073 1.00 28.88 ? 88  LEU A CD2 1 
ATOM   594  N  N   . LYS A 1 89  ? 49.259 7.152  -12.678 1.00 23.24 ? 89  LYS A N   1 
ATOM   595  C  CA  . LYS A 1 89  ? 48.982 8.205  -11.736 1.00 27.93 ? 89  LYS A CA  1 
ATOM   596  C  C   . LYS A 1 89  ? 47.844 7.779  -10.821 1.00 33.90 ? 89  LYS A C   1 
ATOM   597  O  O   . LYS A 1 89  ? 47.974 7.868  -9.608  1.00 22.09 ? 89  LYS A O   1 
ATOM   598  C  CB  . LYS A 1 89  ? 48.650 9.514  -12.459 1.00 22.37 ? 89  LYS A CB  1 
ATOM   599  C  CG  . LYS A 1 89  ? 48.401 10.713 -11.534 1.00 27.51 ? 89  LYS A CG  1 
ATOM   600  C  CD  . LYS A 1 89  ? 49.343 10.830 -10.323 1.00 22.36 ? 89  LYS A CD  1 
ATOM   601  C  CE  . LYS A 1 89  ? 50.761 11.078 -10.727 1.00 28.57 ? 89  LYS A CE  1 
ATOM   602  N  NZ  . LYS A 1 89  ? 51.631 11.282 -9.535  1.00 24.92 ? 89  LYS A NZ  1 
ATOM   603  N  N   . ILE A 1 90  ? 46.770 7.247  -11.398 1.00 24.83 ? 90  ILE A N   1 
ATOM   604  C  CA  . ILE A 1 90  ? 45.657 6.737  -10.613 1.00 23.60 ? 90  ILE A CA  1 
ATOM   605  C  C   . ILE A 1 90  ? 46.146 5.763  -9.540  1.00 26.42 ? 90  ILE A C   1 
ATOM   606  O  O   . ILE A 1 90  ? 45.748 5.844  -8.373  1.00 23.83 ? 90  ILE A O   1 
ATOM   607  C  CB  . ILE A 1 90  ? 44.639 6.022  -11.502 1.00 31.05 ? 90  ILE A CB  1 
ATOM   608  C  CG1 . ILE A 1 90  ? 44.012 6.997  -12.510 1.00 31.07 ? 90  ILE A CG1 1 
ATOM   609  C  CG2 . ILE A 1 90  ? 43.581 5.297  -10.643 1.00 24.14 ? 90  ILE A CG2 1 
ATOM   610  C  CD1 . ILE A 1 90  ? 43.218 6.297  -13.643 1.00 24.09 ? 90  ILE A CD1 1 
ATOM   611  N  N   . GLU A 1 91  ? 47.017 4.838  -9.932  1.00 24.57 ? 91  GLU A N   1 
ATOM   612  C  CA  . GLU A 1 91  ? 47.522 3.889  -8.967  1.00 23.19 ? 91  GLU A CA  1 
ATOM   613  C  C   . GLU A 1 91  ? 48.367 4.574  -7.875  1.00 23.03 ? 91  GLU A C   1 
ATOM   614  O  O   . GLU A 1 91  ? 48.353 4.154  -6.696  1.00 23.25 ? 91  GLU A O   1 
ATOM   615  C  CB  . GLU A 1 91  ? 48.322 2.804  -9.681  1.00 24.30 ? 91  GLU A CB  1 
ATOM   616  C  CG  . GLU A 1 91  ? 47.453 1.828  -10.496 1.00 29.89 ? 91  GLU A CG  1 
ATOM   617  C  CD  . GLU A 1 91  ? 46.511 0.941  -9.650  1.00 33.49 ? 91  GLU A CD  1 
ATOM   618  O  OE1 . GLU A 1 91  ? 46.682 0.876  -8.409  1.00 40.43 ? 91  GLU A OE1 1 
ATOM   619  O  OE2 . GLU A 1 91  ? 45.597 0.297  -10.234 1.00 25.79 ? 91  GLU A OE2 1 
ATOM   620  N  N   . ASP A 1 92  ? 49.082 5.636  -8.250  1.00 24.60 ? 92  ASP A N   1 
ATOM   621  C  CA  . ASP A 1 92  ? 49.895 6.378  -7.291  1.00 24.65 ? 92  ASP A CA  1 
ATOM   622  C  C   . ASP A 1 92  ? 49.003 7.074  -6.247  1.00 23.87 ? 92  ASP A C   1 
ATOM   623  O  O   . ASP A 1 92  ? 49.264 7.030  -5.024  1.00 24.01 ? 92  ASP A O   1 
ATOM   624  C  CB  . ASP A 1 92  ? 50.783 7.353  -8.035  1.00 24.86 ? 92  ASP A CB  1 
ATOM   625  C  CG  . ASP A 1 92  ? 51.808 8.010  -7.143  1.00 49.22 ? 92  ASP A CG  1 
ATOM   626  O  OD1 . ASP A 1 92  ? 52.526 7.282  -6.420  1.00 51.22 ? 92  ASP A OD1 1 
ATOM   627  O  OD2 . ASP A 1 92  ? 51.924 9.256  -7.192  1.00 45.31 ? 92  ASP A OD2 1 
ATOM   628  N  N   . ILE A 1 93  ? 47.932 7.686  -6.743  1.00 24.65 ? 93  ILE A N   1 
ATOM   629  C  CA  . ILE A 1 93  ? 46.906 8.290  -5.912  1.00 24.10 ? 93  ILE A CA  1 
ATOM   630  C  C   . ILE A 1 93  ? 46.302 7.256  -4.957  1.00 24.25 ? 93  ILE A C   1 
ATOM   631  O  O   . ILE A 1 93  ? 46.052 7.552  -3.777  1.00 24.10 ? 93  ILE A O   1 
ATOM   632  C  CB  . ILE A 1 93  ? 45.794 8.909  -6.773  1.00 23.70 ? 93  ILE A CB  1 
ATOM   633  C  CG1 . ILE A 1 93  ? 46.384 9.992  -7.670  1.00 32.74 ? 93  ILE A CG1 1 
ATOM   634  C  CG2 . ILE A 1 93  ? 44.710 9.527  -5.897  1.00 23.39 ? 93  ILE A CG2 1 
ATOM   635  C  CD1 . ILE A 1 93  ? 47.040 11.095 -6.895  1.00 23.79 ? 93  ILE A CD1 1 
ATOM   636  N  N   . GLN A 1 94  ? 46.103 6.038  -5.462  1.00 32.73 ? 94  GLN A N   1 
ATOM   637  C  CA  . GLN A 1 94  ? 45.544 4.949  -4.657  1.00 31.81 ? 94  GLN A CA  1 
ATOM   638  C  C   . GLN A 1 94  ? 46.474 4.578  -3.494  1.00 29.09 ? 94  GLN A C   1 
ATOM   639  O  O   . GLN A 1 94  ? 45.998 4.448  -2.346  1.00 28.45 ? 94  GLN A O   1 
ATOM   640  C  CB  . GLN A 1 94  ? 45.275 3.734  -5.536  1.00 26.89 ? 94  GLN A CB  1 
ATOM   641  C  CG  . GLN A 1 94  ? 44.569 2.532  -4.888  1.00 27.74 ? 94  GLN A CG  1 
ATOM   642  C  CD  . GLN A 1 94  ? 43.315 2.852  -4.055  1.00 39.62 ? 94  GLN A CD  1 
ATOM   643  O  OE1 . GLN A 1 94  ? 43.053 2.176  -3.051  1.00 49.60 ? 94  GLN A OE1 1 
ATOM   644  N  NE2 . GLN A 1 94  ? 42.534 3.857  -4.473  1.00 27.80 ? 94  GLN A NE2 1 
ATOM   645  N  N   . ARG A 1 95  ? 47.782 4.459  -3.772  1.00 24.76 ? 95  ARG A N   1 
ATOM   646  C  CA  . ARG A 1 95  ? 48.755 4.253  -2.692  1.00 31.38 ? 95  ARG A CA  1 
ATOM   647  C  C   . ARG A 1 95  ? 48.647 5.336  -1.624  1.00 35.37 ? 95  ARG A C   1 
ATOM   648  O  O   . ARG A 1 95  ? 48.561 5.030  -0.420  1.00 29.71 ? 95  ARG A O   1 
ATOM   649  C  CB  . ARG A 1 95  ? 50.198 4.237  -3.209  1.00 26.10 ? 95  ARG A CB  1 
ATOM   650  C  CG  . ARG A 1 95  ? 50.515 3.046  -4.049  1.00 36.65 ? 95  ARG A CG  1 
ATOM   651  C  CD  . ARG A 1 95  ? 51.988 2.961  -4.355  1.00 36.62 ? 95  ARG A CD  1 
ATOM   652  N  NE  . ARG A 1 95  ? 52.288 1.794  -5.181  1.00 39.13 ? 95  ARG A NE  1 
ATOM   653  C  CZ  . ARG A 1 95  ? 52.473 0.561  -4.712  1.00 33.90 ? 95  ARG A CZ  1 
ATOM   654  N  NH1 . ARG A 1 95  ? 52.373 0.300  -3.409  1.00 37.16 ? 95  ARG A NH1 1 
ATOM   655  N  NH2 . ARG A 1 95  ? 52.753 -0.418 -5.557  1.00 32.48 ? 95  ARG A NH2 1 
ATOM   656  N  N   . LYS A 1 96  ? 48.611 6.594  -2.061  1.00 25.34 ? 96  LYS A N   1 
ATOM   657  C  CA  . LYS A 1 96  ? 48.557 7.685  -1.092  1.00 27.73 ? 96  LYS A CA  1 
ATOM   658  C  C   . LYS A 1 96  ? 47.310 7.557  -0.202  1.00 33.07 ? 96  LYS A C   1 
ATOM   659  O  O   . LYS A 1 96  ? 47.397 7.652  1.041   1.00 33.20 ? 96  LYS A O   1 
ATOM   660  C  CB  . LYS A 1 96  ? 48.590 9.043  -1.803  1.00 32.34 ? 96  LYS A CB  1 
ATOM   661  C  CG  . LYS A 1 96  ? 49.894 9.331  -2.541  1.00 25.17 ? 96  LYS A CG  1 
ATOM   662  C  CD  . LYS A 1 96  ? 49.902 10.760 -3.117  1.00 44.87 ? 96  LYS A CD  1 
ATOM   663  C  CE  . LYS A 1 96  ? 51.036 10.994 -4.131  1.00 34.11 ? 96  LYS A CE  1 
ATOM   664  N  NZ  . LYS A 1 96  ? 52.365 10.490 -3.676  1.00 39.48 ? 96  LYS A NZ  1 
ATOM   665  N  N   . ILE A 1 97  ? 46.168 7.292  -0.835  1.00 28.54 ? 97  ILE A N   1 
ATOM   666  C  CA  . ILE A 1 97  ? 44.919 7.082  -0.107  1.00 31.63 ? 97  ILE A CA  1 
ATOM   667  C  C   . ILE A 1 97  ? 45.059 5.987  0.944   1.00 33.70 ? 97  ILE A C   1 
ATOM   668  O  O   . ILE A 1 97  ? 44.574 6.135  2.074   1.00 25.50 ? 97  ILE A O   1 
ATOM   669  C  CB  . ILE A 1 97  ? 43.771 6.753  -1.070  1.00 26.80 ? 97  ILE A CB  1 
ATOM   670  C  CG1 . ILE A 1 97  ? 43.318 8.045  -1.745  1.00 24.32 ? 97  ILE A CG1 1 
ATOM   671  C  CG2 . ILE A 1 97  ? 42.570 6.132  -0.348  1.00 25.26 ? 97  ILE A CG2 1 
ATOM   672  C  CD1 . ILE A 1 97  ? 42.214 7.876  -2.757  1.00 24.42 ? 97  ILE A CD1 1 
ATOM   673  N  N   . GLU A 1 98  ? 45.723 4.894  0.580   1.00 29.19 ? 98  GLU A N   1 
ATOM   674  C  CA  . GLU A 1 98  ? 45.890 3.805  1.528   1.00 28.50 ? 98  GLU A CA  1 
ATOM   675  C  C   . GLU A 1 98  ? 46.802 4.212  2.706   1.00 27.80 ? 98  GLU A C   1 
ATOM   676  O  O   . GLU A 1 98  ? 46.550 3.829  3.860   1.00 27.05 ? 98  GLU A O   1 
ATOM   677  C  CB  . GLU A 1 98  ? 46.405 2.564  0.794   1.00 30.81 ? 98  GLU A CB  1 
ATOM   678  C  CG  . GLU A 1 98  ? 45.421 2.090  -0.298  1.00 30.98 ? 98  GLU A CG  1 
ATOM   679  C  CD  . GLU A 1 98  ? 45.997 1.063  -1.274  1.00 40.54 ? 98  GLU A CD  1 
ATOM   680  O  OE1 . GLU A 1 98  ? 47.244 0.909  -1.351  1.00 37.85 ? 98  GLU A OE1 1 
ATOM   681  O  OE2 . GLU A 1 98  ? 45.186 0.412  -1.977  1.00 33.20 ? 98  GLU A OE2 1 
ATOM   682  N  N   . ASP A 1 99  ? 47.841 5.001  2.416   1.00 25.11 ? 99  ASP A N   1 
ATOM   683  C  CA  . ASP A 1 99  ? 48.734 5.505  3.456   1.00 25.38 ? 99  ASP A CA  1 
ATOM   684  C  C   . ASP A 1 99  ? 47.963 6.374  4.464   1.00 25.52 ? 99  ASP A C   1 
ATOM   685  O  O   . ASP A 1 99  ? 48.084 6.240  5.707   1.00 25.13 ? 99  ASP A O   1 
ATOM   686  C  CB  . ASP A 1 99  ? 49.885 6.291  2.826   1.00 25.49 ? 99  ASP A CB  1 
ATOM   687  C  CG  . ASP A 1 99  ? 50.860 5.387  2.057   1.00 37.18 ? 99  ASP A CG  1 
ATOM   688  O  OD1 . ASP A 1 99  ? 50.780 4.143  2.212   1.00 44.27 ? 99  ASP A OD1 1 
ATOM   689  O  OD2 . ASP A 1 99  ? 51.718 5.912  1.301   1.00 27.41 ? 99  ASP A OD2 1 
ATOM   690  N  N   . LEU A 1 100 ? 47.104 7.217  3.909   1.00 22.86 ? 100 LEU A N   1 
ATOM   691  C  CA  . LEU A 1 100 ? 46.219 8.037  4.710   1.00 22.43 ? 100 LEU A CA  1 
ATOM   692  C  C   . LEU A 1 100 ? 45.238 7.197  5.569   1.00 26.29 ? 100 LEU A C   1 
ATOM   693  O  O   . LEU A 1 100 ? 44.971 7.524  6.732   1.00 43.18 ? 100 LEU A O   1 
ATOM   694  C  CB  . LEU A 1 100 ? 45.485 9.004  3.778   1.00 21.83 ? 100 LEU A CB  1 
ATOM   695  C  CG  . LEU A 1 100 ? 46.449 10.099 3.299   1.00 24.48 ? 100 LEU A CG  1 
ATOM   696  C  CD1 . LEU A 1 100 ? 45.779 11.029 2.333   1.00 34.44 ? 100 LEU A CD1 1 
ATOM   697  C  CD2 . LEU A 1 100 ? 46.945 10.884 4.500   1.00 22.05 ? 100 LEU A CD2 1 
ATOM   698  N  N   . LYS A 1 101 ? 44.733 6.104  5.026   1.00 24.16 ? 101 LYS A N   1 
ATOM   699  C  CA  . LYS A 1 101 ? 43.871 5.228  5.813   1.00 24.75 ? 101 LYS A CA  1 
ATOM   700  C  C   . LYS A 1 101 ? 44.654 4.557  6.945   1.00 26.10 ? 101 LYS A C   1 
ATOM   701  O  O   . LYS A 1 101 ? 44.112 4.352  8.053   1.00 25.84 ? 101 LYS A O   1 
ATOM   702  C  CB  . LYS A 1 101 ? 43.191 4.195  4.924   1.00 25.25 ? 101 LYS A CB  1 
ATOM   703  C  CG  . LYS A 1 101 ? 41.960 4.749  4.228   1.00 30.56 ? 101 LYS A CG  1 
ATOM   704  C  CD  . LYS A 1 101 ? 41.356 3.740  3.291   1.00 39.52 ? 101 LYS A CD  1 
ATOM   705  C  CE  . LYS A 1 101 ? 39.951 4.133  2.947   1.00 42.89 ? 101 LYS A CE  1 
ATOM   706  N  NZ  . LYS A 1 101 ? 39.115 3.995  4.177   1.00 58.07 ? 101 LYS A NZ  1 
ATOM   707  N  N   . ARG A 1 102 ? 45.921 4.218  6.688   1.00 23.61 ? 102 ARG A N   1 
ATOM   708  C  CA  . ARG A 1 102 ? 46.713 3.669  7.789   1.00 30.59 ? 102 ARG A CA  1 
ATOM   709  C  C   . ARG A 1 102 ? 46.860 4.684  8.912   1.00 24.11 ? 102 ARG A C   1 
ATOM   710  O  O   . ARG A 1 102 ? 46.662 4.345  10.085  1.00 24.61 ? 102 ARG A O   1 
ATOM   711  C  CB  . ARG A 1 102 ? 48.091 3.184  7.335   1.00 25.22 ? 102 ARG A CB  1 
ATOM   712  C  CG  . ARG A 1 102 ? 48.035 1.786  6.738   1.00 26.22 ? 102 ARG A CG  1 
ATOM   713  C  CD  . ARG A 1 102 ? 49.392 1.317  6.222   1.00 27.17 ? 102 ARG A CD  1 
ATOM   714  N  NE  . ARG A 1 102 ? 49.691 1.884  4.920   1.00 26.52 ? 102 ARG A NE  1 
ATOM   715  C  CZ  . ARG A 1 102 ? 49.226 1.411  3.773   1.00 26.46 ? 102 ARG A CZ  1 
ATOM   716  N  NH1 . ARG A 1 102 ? 48.449 0.342  3.752   1.00 27.13 ? 102 ARG A NH1 1 
ATOM   717  N  NH2 . ARG A 1 102 ? 49.551 2.012  2.639   1.00 27.97 ? 102 ARG A NH2 1 
ATOM   718  N  N   . ILE A 1 103 ? 47.117 5.938  8.552   1.00 29.10 ? 103 ILE A N   1 
ATOM   719  C  CA  . ILE A 1 103 ? 47.280 6.972  9.579   1.00 37.88 ? 103 ILE A CA  1 
ATOM   720  C  C   . ILE A 1 103 ? 45.974 7.193  10.368  1.00 37.83 ? 103 ILE A C   1 
ATOM   721  O  O   . ILE A 1 103 ? 45.955 7.233  11.619  1.00 24.04 ? 103 ILE A O   1 
ATOM   722  C  CB  . ILE A 1 103 ? 47.743 8.288  8.959   1.00 23.45 ? 103 ILE A CB  1 
ATOM   723  C  CG1 . ILE A 1 103 ? 49.181 8.163  8.447   1.00 24.04 ? 103 ILE A CG1 1 
ATOM   724  C  CG2 . ILE A 1 103 ? 47.597 9.420  9.947   1.00 23.35 ? 103 ILE A CG2 1 
ATOM   725  C  CD1 . ILE A 1 103 ? 49.574 9.288  7.521   1.00 29.26 ? 103 ILE A CD1 1 
ATOM   726  N  N   . GLU A 1 104 ? 44.877 7.267  9.631   1.00 28.70 ? 104 GLU A N   1 
ATOM   727  C  CA  . GLU A 1 104 ? 43.569 7.401  10.248  1.00 28.88 ? 104 GLU A CA  1 
ATOM   728  C  C   . GLU A 1 104 ? 43.284 6.314  11.273  1.00 25.04 ? 104 GLU A C   1 
ATOM   729  O  O   . GLU A 1 104 ? 42.822 6.601  12.387  1.00 26.63 ? 104 GLU A O   1 
ATOM   730  C  CB  . GLU A 1 104 ? 42.489 7.373  9.186   1.00 23.98 ? 104 GLU A CB  1 
ATOM   731  C  CG  . GLU A 1 104 ? 41.288 8.170  9.566   1.00 25.86 ? 104 GLU A CG  1 
ATOM   732  C  CD  . GLU A 1 104 ? 40.200 8.071  8.532   1.00 42.05 ? 104 GLU A CD  1 
ATOM   733  O  OE1 . GLU A 1 104 ? 40.436 7.448  7.473   1.00 53.24 ? 104 GLU A OE1 1 
ATOM   734  O  OE2 . GLU A 1 104 ? 39.110 8.620  8.779   1.00 39.78 ? 104 GLU A OE2 1 
ATOM   735  N  N   . ARG A 1 105 ? 43.528 5.064  10.900  1.00 23.40 ? 105 ARG A N   1 
ATOM   736  C  CA  . ARG A 1 105 ? 43.282 3.962  11.835  1.00 25.74 ? 105 ARG A CA  1 
ATOM   737  C  C   . ARG A 1 105 ? 44.219 4.048  13.070  1.00 24.84 ? 105 ARG A C   1 
ATOM   738  O  O   . ARG A 1 105 ? 43.802 3.803  14.193  1.00 25.41 ? 105 ARG A O   1 
ATOM   739  C  CB  . ARG A 1 105 ? 43.411 2.617  11.109  1.00 27.66 ? 105 ARG A CB  1 
ATOM   740  C  CG  . ARG A 1 105 ? 42.245 2.329  10.136  1.00 25.35 ? 105 ARG A CG  1 
ATOM   741  C  CD  . ARG A 1 105 ? 42.273 0.896  9.603   1.00 26.57 ? 105 ARG A CD  1 
ATOM   742  N  NE  . ARG A 1 105 ? 43.503 0.654  8.860   1.00 32.11 ? 105 ARG A NE  1 
ATOM   743  C  CZ  . ARG A 1 105 ? 43.634 0.770  7.539   1.00 26.03 ? 105 ARG A CZ  1 
ATOM   744  N  NH1 . ARG A 1 105 ? 42.600 1.099  6.775   1.00 25.57 ? 105 ARG A NH1 1 
ATOM   745  N  NH2 . ARG A 1 105 ? 44.810 0.520  6.976   1.00 26.19 ? 105 ARG A NH2 1 
ATOM   746  N  N   . MET A 1 106 ? 45.469 4.444  12.839  1.00 25.88 ? 106 MET A N   1 
ATOM   747  C  CA  . MET A 1 106 ? 46.405 4.701  13.914  1.00 26.31 ? 106 MET A CA  1 
ATOM   748  C  C   . MET A 1 106 ? 45.801 5.696  14.939  1.00 35.70 ? 106 MET A C   1 
ATOM   749  O  O   . MET A 1 106 ? 45.833 5.467  16.163  1.00 26.55 ? 106 MET A O   1 
ATOM   750  C  CB  . MET A 1 106 ? 47.701 5.249  13.319  1.00 26.19 ? 106 MET A CB  1 
ATOM   751  C  CG  . MET A 1 106 ? 48.966 4.800  14.025  1.00 40.97 ? 106 MET A CG  1 
ATOM   752  S  SD  . MET A 1 106 ? 50.519 5.173  13.143  1.00 71.33 ? 106 MET A SD  1 
ATOM   753  C  CE  . MET A 1 106 ? 50.233 4.472  11.520  1.00 34.77 ? 106 MET A CE  1 
ATOM   754  N  N   . LEU A 1 107 ? 45.218 6.776  14.428  1.00 24.72 ? 107 LEU A N   1 
ATOM   755  C  CA  . LEU A 1 107 ? 44.574 7.778  15.258  1.00 24.49 ? 107 LEU A CA  1 
ATOM   756  C  C   . LEU A 1 107 ? 43.335 7.212  15.978  1.00 24.93 ? 107 LEU A C   1 
ATOM   757  O  O   . LEU A 1 107 ? 43.101 7.500  17.161  1.00 25.27 ? 107 LEU A O   1 
ATOM   758  C  CB  . LEU A 1 107 ? 44.179 8.973  14.396  1.00 30.57 ? 107 LEU A CB  1 
ATOM   759  C  CG  . LEU A 1 107 ? 45.297 9.787  13.741  1.00 23.44 ? 107 LEU A CG  1 
ATOM   760  C  CD1 . LEU A 1 107 ? 44.679 10.661 12.661  1.00 22.83 ? 107 LEU A CD1 1 
ATOM   761  C  CD2 . LEU A 1 107 ? 45.995 10.634 14.777  1.00 23.83 ? 107 LEU A CD2 1 
ATOM   762  N  N   . MET A 1 108 ? 42.539 6.407  15.275  1.00 24.06 ? 108 MET A N   1 
ATOM   763  C  CA  . MET A 1 108 ? 41.399 5.772  15.927  1.00 26.56 ? 108 MET A CA  1 
ATOM   764  C  C   . MET A 1 108 ? 41.856 4.957  17.147  1.00 33.72 ? 108 MET A C   1 
ATOM   765  O  O   . MET A 1 108 ? 41.266 5.091  18.243  1.00 27.26 ? 108 MET A O   1 
ATOM   766  C  CB  . MET A 1 108 ? 40.603 4.904  14.934  1.00 25.18 ? 108 MET A CB  1 
ATOM   767  C  CG  . MET A 1 108 ? 39.857 5.728  13.866  1.00 28.95 ? 108 MET A CG  1 
ATOM   768  S  SD  . MET A 1 108 ? 39.222 4.844  12.408  1.00 37.39 ? 108 MET A SD  1 
ATOM   769  C  CE  . MET A 1 108 ? 38.356 3.513  13.185  1.00 26.43 ? 108 MET A CE  1 
ATOM   770  N  N   . ASP A 1 109 ? 42.914 4.152  16.981  1.00 28.60 ? 109 ASP A N   1 
ATOM   771  C  CA  . ASP A 1 109 ? 43.419 3.327  18.087  1.00 37.55 ? 109 ASP A CA  1 
ATOM   772  C  C   . ASP A 1 109 ? 43.941 4.163  19.280  1.00 38.85 ? 109 ASP A C   1 
ATOM   773  O  O   . ASP A 1 109 ? 43.643 3.889  20.490  1.00 30.31 ? 109 ASP A O   1 
ATOM   774  C  CB  . ASP A 1 109 ? 44.535 2.407  17.579  1.00 29.63 ? 109 ASP A CB  1 
ATOM   775  C  CG  . ASP A 1 109 ? 44.941 1.378  18.612  1.00 31.13 ? 109 ASP A CG  1 
ATOM   776  O  OD1 . ASP A 1 109 ? 44.236 0.354  18.729  1.00 32.19 ? 109 ASP A OD1 1 
ATOM   777  O  OD2 . ASP A 1 109 ? 45.947 1.600  19.317  1.00 43.12 ? 109 ASP A OD2 1 
ATOM   778  N  N   . LEU A 1 110 ? 44.706 5.192  18.928  1.00 27.96 ? 110 LEU A N   1 
ATOM   779  C  CA  . LEU A 1 110 ? 45.206 6.116  19.922  1.00 27.94 ? 110 LEU A CA  1 
ATOM   780  C  C   . LEU A 1 110 ? 44.061 6.661  20.785  1.00 27.90 ? 110 LEU A C   1 
ATOM   781  O  O   . LEU A 1 110 ? 44.153 6.635  22.016  1.00 28.53 ? 110 LEU A O   1 
ATOM   782  C  CB  . LEU A 1 110 ? 45.975 7.271  19.262  1.00 27.21 ? 110 LEU A CB  1 
ATOM   783  C  CG  . LEU A 1 110 ? 47.404 7.005  18.797  1.00 36.14 ? 110 LEU A CG  1 
ATOM   784  C  CD1 . LEU A 1 110 ? 47.946 8.166  17.932  1.00 26.95 ? 110 LEU A CD1 1 
ATOM   785  C  CD2 . LEU A 1 110 ? 48.321 6.717  19.990  1.00 33.90 ? 110 LEU A CD2 1 
ATOM   786  N  N   . LYS A 1 111 ? 43.003 7.156  20.136  1.00 26.22 ? 111 LYS A N   1 
ATOM   787  C  CA  . LYS A 1 111 ? 41.866 7.750  20.848  1.00 26.36 ? 111 LYS A CA  1 
ATOM   788  C  C   . LYS A 1 111 ? 41.109 6.675  21.654  1.00 33.69 ? 111 LYS A C   1 
ATOM   789  O  O   . LYS A 1 111 ? 40.490 6.986  22.673  1.00 27.88 ? 111 LYS A O   1 
ATOM   790  C  CB  . LYS A 1 111 ? 40.937 8.493  19.873  1.00 27.92 ? 111 LYS A CB  1 
ATOM   791  C  CG  . LYS A 1 111 ? 39.694 7.742  19.407  1.00 26.17 ? 111 LYS A CG  1 
ATOM   792  C  CD  . LYS A 1 111 ? 38.841 8.618  18.531  1.00 25.74 ? 111 LYS A CD  1 
ATOM   793  C  CE  . LYS A 1 111 ? 37.358 8.221  18.526  1.00 32.40 ? 111 LYS A CE  1 
ATOM   794  N  NZ  . LYS A 1 111 ? 37.135 6.889  17.979  1.00 40.08 ? 111 LYS A NZ  1 
ATOM   795  N  N   . GLU A 1 112 ? 41.171 5.414  21.215  1.00 27.96 ? 112 GLU A N   1 
ATOM   796  C  CA  . GLU A 1 112 ? 40.572 4.342  22.017  1.00 30.59 ? 112 GLU A CA  1 
ATOM   797  C  C   . GLU A 1 112 ? 41.318 4.122  23.351  1.00 35.01 ? 112 GLU A C   1 
ATOM   798  O  O   . GLU A 1 112 ? 40.743 3.621  24.328  1.00 31.03 ? 112 GLU A O   1 
ATOM   799  C  CB  . GLU A 1 112 ? 40.583 3.012  21.236  1.00 40.68 ? 112 GLU A CB  1 
ATOM   800  C  CG  . GLU A 1 112 ? 39.707 2.942  19.970  1.00 52.87 ? 112 GLU A CG  1 
ATOM   801  C  CD  . GLU A 1 112 ? 40.096 1.767  19.037  1.00 59.94 ? 112 GLU A CD  1 
ATOM   802  O  OE1 . GLU A 1 112 ? 40.961 0.945  19.429  1.00 67.88 ? 112 GLU A OE1 1 
ATOM   803  O  OE2 . GLU A 1 112 ? 39.567 1.685  17.898  1.00 54.98 ? 112 GLU A OE2 1 
ATOM   804  N  N   . ARG A 1 113 ? 42.585 4.517  23.420  1.00 30.33 ? 113 ARG A N   1 
ATOM   805  C  CA  . ARG A 1 113 ? 43.285 4.363  24.709  1.00 31.15 ? 113 ARG A CA  1 
ATOM   806  C  C   . ARG A 1 113 ? 42.781 5.259  25.883  1.00 31.23 ? 113 ARG A C   1 
ATOM   807  O  O   . ARG A 1 113 ? 43.090 4.993  27.048  1.00 32.06 ? 113 ARG A O   1 
ATOM   808  C  CB  . ARG A 1 113 ? 44.789 4.631  24.522  1.00 36.59 ? 113 ARG A CB  1 
ATOM   809  C  CG  . ARG A 1 113 ? 45.510 3.682  23.578  1.00 32.56 ? 113 ARG A CG  1 
ATOM   810  C  CD  . ARG A 1 113 ? 46.903 4.234  23.245  1.00 33.34 ? 113 ARG A CD  1 
ATOM   811  N  NE  . ARG A 1 113 ? 47.630 3.363  22.330  1.00 46.04 ? 113 ARG A NE  1 
ATOM   812  C  CZ  . ARG A 1 113 ? 48.491 2.426  22.715  1.00 35.53 ? 113 ARG A CZ  1 
ATOM   813  N  NH1 . ARG A 1 113 ? 48.743 2.241  24.010  1.00 33.96 ? 113 ARG A NH1 1 
ATOM   814  N  NH2 . ARG A 1 113 ? 49.104 1.682  21.803  1.00 33.45 ? 113 ARG A NH2 1 
ATOM   815  N  N   . CYS A 1 114 ? 42.064 6.337  25.590  1.00 28.17 ? 114 CYS A N   1 
ATOM   816  C  CA  . CYS A 1 114 ? 41.781 7.324  26.633  1.00 28.28 ? 114 CYS A CA  1 
ATOM   817  C  C   . CYS A 1 114 ? 40.651 6.802  27.588  1.00 29.32 ? 114 CYS A C   1 
ATOM   818  O  O   . CYS A 1 114 ? 39.706 6.128  27.154  1.00 29.70 ? 114 CYS A O   1 
ATOM   819  C  CB  . CYS A 1 114 ? 41.472 8.688  25.964  1.00 27.33 ? 114 CYS A CB  1 
ATOM   820  S  SG  . CYS A 1 114 ? 42.910 9.393  25.001  1.00 26.45 ? 114 CYS A SG  1 
ATOM   821  N  N   . PRO A 1 115 ? 40.765 7.080  28.907  1.00 31.72 ? 115 PRO A N   1 
ATOM   822  C  CA  . PRO A 1 115 ? 39.749 6.614  29.871  1.00 31.10 ? 115 PRO A CA  1 
ATOM   823  C  C   . PRO A 1 115 ? 38.411 7.361  29.726  1.00 31.08 ? 115 PRO A C   1 
ATOM   824  O  O   . PRO A 1 115 ? 38.348 8.385  29.024  1.00 30.17 ? 115 PRO A O   1 
ATOM   825  C  CB  . PRO A 1 115 ? 40.384 6.913  31.235  1.00 31.67 ? 115 PRO A CB  1 
ATOM   826  C  CG  . PRO A 1 115 ? 41.327 8.028  30.985  1.00 30.75 ? 115 PRO A CG  1 
ATOM   827  C  CD  . PRO A 1 115 ? 41.866 7.808  29.572  1.00 29.85 ? 115 PRO A CD  1 
ATOM   828  N  N   . GLU A 1 116 ? 37.362 6.852  30.372  1.00 32.28 ? 116 GLU A N   1 
ATOM   829  C  CA  . GLU A 1 116 ? 36.047 7.485  30.326  1.00 32.67 ? 116 GLU A CA  1 
ATOM   830  C  C   . GLU A 1 116 ? 36.093 8.888  30.911  1.00 32.37 ? 116 GLU A C   1 
ATOM   831  O  O   . GLU A 1 116 ? 35.603 9.830  30.280  1.00 31.95 ? 116 GLU A O   1 
ATOM   832  C  CB  . GLU A 1 116 ? 35.004 6.647  31.064  1.00 34.36 ? 116 GLU A CB  1 
ATOM   833  C  CG  . GLU A 1 116 ? 34.783 5.298  30.411  1.00 35.00 ? 116 GLU A CG  1 
ATOM   834  C  CD  . GLU A 1 116 ? 33.457 4.672  30.768  1.00 36.83 ? 116 GLU A CD  1 
ATOM   835  O  OE1 . GLU A 1 116 ? 32.917 5.015  31.853  1.00 37.79 ? 116 GLU A OE1 1 
ATOM   836  O  OE2 . GLU A 1 116 ? 32.960 3.843  29.958  1.00 37.45 ? 116 GLU A OE2 1 
ATOM   837  N  N   . ASN A 1 117 ? 36.698 9.038  32.095  1.00 32.74 ? 117 ASN A N   1 
ATOM   838  C  CA  . ASN A 1 117 ? 36.867 10.375 32.644  1.00 32.58 ? 117 ASN A CA  1 
ATOM   839  C  C   . ASN A 1 117 ? 38.207 10.997 32.222  1.00 31.50 ? 117 ASN A C   1 
ATOM   840  O  O   . ASN A 1 117 ? 39.286 10.657 32.699  1.00 31.50 ? 117 ASN A O   1 
ATOM   841  C  CB  . ASN A 1 117 ? 36.749 10.349 34.161  1.00 33.72 ? 117 ASN A CB  1 
ATOM   842  C  CG  . ASN A 1 117 ? 37.089 11.688 34.793  1.00 34.34 ? 117 ASN A CG  1 
ATOM   843  O  OD1 . ASN A 1 117 ? 36.869 12.755 34.201  1.00 33.29 ? 117 ASN A OD1 1 
ATOM   844  N  ND2 . ASN A 1 117 ? 37.640 11.640 35.992  1.00 34.32 ? 117 ASN A ND2 1 
ATOM   845  N  N   . LYS A 1 118 ? 38.091 11.963 31.334  1.00 33.69 ? 118 LYS A N   1 
ATOM   846  C  CA  . LYS A 1 118 ? 39.216 12.568 30.664  1.00 30.55 ? 118 LYS A CA  1 
ATOM   847  C  C   . LYS A 1 118 ? 39.617 13.865 31.329  1.00 30.88 ? 118 LYS A C   1 
ATOM   848  O  O   . LYS A 1 118 ? 40.428 14.609 30.782  1.00 32.61 ? 118 LYS A O   1 
ATOM   849  C  CB  . LYS A 1 118 ? 38.891 12.766 29.190  1.00 29.73 ? 118 LYS A CB  1 
ATOM   850  C  CG  . LYS A 1 118 ? 38.485 11.454 28.520  1.00 29.58 ? 118 LYS A CG  1 
ATOM   851  C  CD  . LYS A 1 118 ? 38.338 11.582 27.004  1.00 28.73 ? 118 LYS A CD  1 
ATOM   852  C  CE  . LYS A 1 118 ? 37.941 10.263 26.383  1.00 28.79 ? 118 LYS A CE  1 
ATOM   853  N  NZ  . LYS A 1 118 ? 36.832 9.659  27.157  1.00 30.00 ? 118 LYS A NZ  1 
ATOM   854  N  N   . ASP A 1 119 ? 39.036 14.177 32.485  1.00 33.23 ? 119 ASP A N   1 
ATOM   855  C  CA  . ASP A 1 119 ? 39.494 15.395 33.109  1.00 33.70 ? 119 ASP A CA  1 
ATOM   856  C  C   . ASP A 1 119 ? 40.663 15.029 34.005  1.00 33.99 ? 119 ASP A C   1 
ATOM   857  O  O   . ASP A 1 119 ? 40.523 14.903 35.206  1.00 46.90 ? 119 ASP A O   1 
ATOM   858  C  CB  . ASP A 1 119 ? 38.357 16.003 33.930  1.00 34.78 ? 119 ASP A CB  1 
ATOM   859  C  CG  . ASP A 1 119 ? 38.794 17.204 34.746  1.00 57.54 ? 119 ASP A CG  1 
ATOM   860  O  OD1 . ASP A 1 119 ? 39.791 17.875 34.382  1.00 51.85 ? 119 ASP A OD1 1 
ATOM   861  O  OD2 . ASP A 1 119 ? 38.141 17.461 35.778  1.00 66.26 ? 119 ASP A OD2 1 
ATOM   862  N  N   . ILE A 1 120 ? 41.850 15.044 33.412  1.00 34.67 ? 120 ILE A N   1 
ATOM   863  C  CA  . ILE A 1 120 ? 43.083 14.572 34.055  1.00 33.34 ? 120 ILE A CA  1 
ATOM   864  C  C   . ILE A 1 120 ? 44.292 15.096 33.297  1.00 34.64 ? 120 ILE A C   1 
ATOM   865  O  O   . ILE A 1 120 ? 44.195 15.539 32.127  1.00 33.65 ? 120 ILE A O   1 
ATOM   866  C  CB  . ILE A 1 120 ? 43.191 13.027 34.128  1.00 36.65 ? 120 ILE A CB  1 
ATOM   867  C  CG1 . ILE A 1 120 ? 42.925 12.401 32.753  1.00 35.23 ? 120 ILE A CG1 1 
ATOM   868  C  CG2 . ILE A 1 120 ? 42.260 12.449 35.199  1.00 34.07 ? 120 ILE A CG2 1 
ATOM   869  C  CD1 . ILE A 1 120 ? 43.003 10.912 32.759  1.00 32.51 ? 120 ILE A CD1 1 
ATOM   870  N  N   . TYR A 1 121 ? 45.424 15.027 33.984  1.00 33.13 ? 121 TYR A N   1 
ATOM   871  C  CA  . TYR A 1 121 ? 46.730 15.428 33.497  1.00 33.32 ? 121 TYR A CA  1 
ATOM   872  C  C   . TYR A 1 121 ? 47.356 14.424 32.537  1.00 32.72 ? 121 TYR A C   1 
ATOM   873  O  O   . TYR A 1 121 ? 47.961 14.802 31.535  1.00 32.40 ? 121 TYR A O   1 
ATOM   874  C  CB  . TYR A 1 121 ? 47.636 15.623 34.706  1.00 34.64 ? 121 TYR A CB  1 
ATOM   875  C  CG  . TYR A 1 121 ? 48.960 16.275 34.414  1.00 35.36 ? 121 TYR A CG  1 
ATOM   876  C  CD1 . TYR A 1 121 ? 49.153 17.633 34.656  1.00 36.18 ? 121 TYR A CD1 1 
ATOM   877  C  CD2 . TYR A 1 121 ? 50.032 15.530 33.925  1.00 35.50 ? 121 TYR A CD2 1 
ATOM   878  C  CE1 . TYR A 1 121 ? 50.384 18.237 34.398  1.00 40.47 ? 121 TYR A CE1 1 
ATOM   879  C  CE2 . TYR A 1 121 ? 51.261 16.119 33.674  1.00 40.16 ? 121 TYR A CE2 1 
ATOM   880  C  CZ  . TYR A 1 121 ? 51.431 17.469 33.909  1.00 42.02 ? 121 TYR A CZ  1 
ATOM   881  O  OH  . TYR A 1 121 ? 52.655 18.043 33.644  1.00 45.18 ? 121 TYR A OH  1 
ATOM   882  N  N   . GLU A 1 122 ? 47.158 13.147 32.839  1.00 35.18 ? 122 GLU A N   1 
ATOM   883  C  CA  . GLU A 1 122 ? 47.756 12.034 32.106  1.00 35.28 ? 122 GLU A CA  1 
ATOM   884  C  C   . GLU A 1 122 ? 46.947 11.743 30.857  1.00 33.77 ? 122 GLU A C   1 
ATOM   885  O  O   . GLU A 1 122 ? 45.769 11.406 30.965  1.00 57.56 ? 122 GLU A O   1 
ATOM   886  C  CB  . GLU A 1 122 ? 47.747 10.733 32.926  1.00 41.91 ? 122 GLU A CB  1 
ATOM   887  C  CG  . GLU A 1 122 ? 48.315 10.718 34.335  1.00 43.10 ? 122 GLU A CG  1 
ATOM   888  C  CD  . GLU A 1 122 ? 47.221 10.930 35.395  1.00 41.00 ? 122 GLU A CD  1 
ATOM   889  O  OE1 . GLU A 1 122 ? 47.355 10.408 36.525  1.00 40.40 ? 122 GLU A OE1 1 
ATOM   890  O  OE2 . GLU A 1 122 ? 46.175 11.526 35.072  1.00 37.23 ? 122 GLU A OE2 1 
ATOM   891  N  N   . CYS A 1 123 ? 47.528 11.876 29.674  1.00 31.26 ? 123 CYS A N   1 
ATOM   892  C  CA  . CYS A 1 123 ? 46.810 11.420 28.476  1.00 30.23 ? 123 CYS A CA  1 
ATOM   893  C  C   . CYS A 1 123 ? 47.565 10.262 27.816  1.00 30.32 ? 123 CYS A C   1 
ATOM   894  O  O   . CYS A 1 123 ? 48.709 10.419 27.367  1.00 35.00 ? 123 CYS A O   1 
ATOM   895  C  CB  . CYS A 1 123 ? 46.601 12.550 27.473  1.00 29.48 ? 123 CYS A CB  1 
ATOM   896  S  SG  . CYS A 1 123 ? 45.882 11.995 25.882  1.00 28.33 ? 123 CYS A SG  1 
ATOM   897  N  N   . PRO A 1 124 ? 46.934 9.096  27.755  1.00 29.03 ? 124 PRO A N   1 
ATOM   898  C  CA  . PRO A 1 124 ? 47.533 7.929  27.094  1.00 29.30 ? 124 PRO A CA  1 
ATOM   899  C  C   . PRO A 1 124 ? 47.986 8.199  25.657  1.00 28.53 ? 124 PRO A C   1 
ATOM   900  O  O   . PRO A 1 124 ? 48.944 7.587  25.200  1.00 29.02 ? 124 PRO A O   1 
ATOM   901  C  CB  . PRO A 1 124 ? 46.397 6.903  27.100  1.00 29.36 ? 124 PRO A CB  1 
ATOM   902  C  CG  . PRO A 1 124 ? 45.512 7.330  28.240  1.00 29.60 ? 124 PRO A CG  1 
ATOM   903  C  CD  . PRO A 1 124 ? 45.607 8.818  28.319  1.00 29.05 ? 124 PRO A CD  1 
ATOM   904  N  N   . ILE A 1 125 ? 47.315 9.097  24.952  1.00 27.62 ? 125 ILE A N   1 
ATOM   905  C  CA  . ILE A 1 125 ? 47.722 9.412  23.595  1.00 26.95 ? 125 ILE A CA  1 
ATOM   906  C  C   . ILE A 1 125 ? 49.120 10.039 23.611  1.00 27.53 ? 125 ILE A C   1 
ATOM   907  O  O   . ILE A 1 125 ? 50.051 9.554  22.951  1.00 27.87 ? 125 ILE A O   1 
ATOM   908  C  CB  . ILE A 1 125 ? 46.714 10.341 22.915  1.00 25.97 ? 125 ILE A CB  1 
ATOM   909  C  CG1 . ILE A 1 125 ? 45.359 9.632  22.789  1.00 25.67 ? 125 ILE A CG1 1 
ATOM   910  C  CG2 . ILE A 1 125 ? 47.200 10.733 21.536  1.00 25.39 ? 125 ILE A CG2 1 
ATOM   911  C  CD1 . ILE A 1 125 ? 44.268 10.439 22.055  1.00 24.92 ? 125 ILE A CD1 1 
ATOM   912  N  N   . ILE A 1 126 ? 49.262 11.102 24.398  1.00 29.46 ? 126 ILE A N   1 
ATOM   913  C  CA  . ILE A 1 126 ? 50.498 11.826 24.508  1.00 30.84 ? 126 ILE A CA  1 
ATOM   914  C  C   . ILE A 1 126 ? 51.612 10.901 25.003  1.00 31.51 ? 126 ILE A C   1 
ATOM   915  O  O   . ILE A 1 126 ? 52.719 10.895 24.454  1.00 32.17 ? 126 ILE A O   1 
ATOM   916  C  CB  . ILE A 1 126 ? 50.323 13.033 25.444  1.00 36.29 ? 126 ILE A CB  1 
ATOM   917  C  CG1 . ILE A 1 126 ? 49.276 13.979 24.842  1.00 31.66 ? 126 ILE A CG1 1 
ATOM   918  C  CG2 . ILE A 1 126 ? 51.658 13.773 25.648  1.00 31.94 ? 126 ILE A CG2 1 
ATOM   919  C  CD1 . ILE A 1 126 ? 48.849 15.128 25.765  1.00 30.26 ? 126 ILE A CD1 1 
ATOM   920  N  N   . GLU A 1 127 ? 51.313 10.100 26.014  1.00 33.67 ? 127 GLU A N   1 
ATOM   921  C  CA  . GLU A 1 127 ? 52.278 9.131  26.519  1.00 35.02 ? 127 GLU A CA  1 
ATOM   922  C  C   . GLU A 1 127 ? 52.731 8.141  25.445  1.00 37.19 ? 127 GLU A C   1 
ATOM   923  O  O   . GLU A 1 127 ? 53.912 7.830  25.343  1.00 36.64 ? 127 GLU A O   1 
ATOM   924  C  CB  . GLU A 1 127 ? 51.685 8.381  27.695  1.00 39.52 ? 127 GLU A CB  1 
ATOM   925  C  CG  . GLU A 1 127 ? 51.463 9.257  28.911  1.00 44.93 ? 127 GLU A CG  1 
ATOM   926  C  CD  . GLU A 1 127 ? 50.655 8.564  29.991  1.00 50.22 ? 127 GLU A CD  1 
ATOM   927  O  OE1 . GLU A 1 127 ? 49.876 7.623  29.669  1.00 39.19 ? 127 GLU A OE1 1 
ATOM   928  O  OE2 . GLU A 1 127 ? 50.823 8.954  31.169  1.00 53.62 ? 127 GLU A OE2 1 
ATOM   929  N  N   . THR A 1 128 ? 51.801 7.664  24.628  1.00 33.13 ? 128 THR A N   1 
ATOM   930  C  CA  . THR A 1 128 ? 52.143 6.691  23.603  1.00 32.78 ? 128 THR A CA  1 
ATOM   931  C  C   . THR A 1 128 ? 53.034 7.342  22.559  1.00 32.70 ? 128 THR A C   1 
ATOM   932  O  O   . THR A 1 128 ? 54.023 6.758  22.127  1.00 45.11 ? 128 THR A O   1 
ATOM   933  C  CB  . THR A 1 128 ? 50.895 6.104  22.902  1.00 31.71 ? 128 THR A CB  1 
ATOM   934  O  OG1 . THR A 1 128 ? 50.015 5.498  23.856  1.00 31.99 ? 128 THR A OG1 1 
ATOM   935  C  CG2 . THR A 1 128 ? 51.304 5.089  21.844  1.00 32.06 ? 128 THR A CG2 1 
ATOM   936  N  N   . LEU A 1 129 ? 52.673 8.540  22.118  1.00 33.46 ? 129 LEU A N   1 
ATOM   937  C  CA  . LEU A 1 129 ? 53.474 9.214  21.100  1.00 35.42 ? 129 LEU A CA  1 
ATOM   938  C  C   . LEU A 1 129 ? 54.836 9.687  21.623  1.00 42.16 ? 129 LEU A C   1 
ATOM   939  O  O   . LEU A 1 129 ? 55.747 9.963  20.850  1.00 35.70 ? 129 LEU A O   1 
ATOM   940  C  CB  . LEU A 1 129 ? 52.708 10.398 20.517  1.00 32.24 ? 129 LEU A CB  1 
ATOM   941  C  CG  . LEU A 1 129 ? 51.492 9.991  19.690  1.00 33.40 ? 129 LEU A CG  1 
ATOM   942  C  CD1 . LEU A 1 129 ? 50.882 11.188 18.944  1.00 29.90 ? 129 LEU A CD1 1 
ATOM   943  C  CD2 . LEU A 1 129 ? 51.882 8.883  18.721  1.00 41.42 ? 129 LEU A CD2 1 
ATOM   944  N  N   . MET A 1 130 ? 54.970 9.761  22.941  1.00 49.95 ? 130 MET A N   1 
ATOM   945  C  CA  . MET A 1 130 ? 56.212 10.190 23.550  1.00 38.78 ? 130 MET A CA  1 
ATOM   946  C  C   . MET A 1 130 ? 57.258 9.086  23.575  1.00 43.45 ? 130 MET A C   1 
ATOM   947  O  O   . MET A 1 130 ? 58.447 9.362  23.441  1.00 48.71 ? 130 MET A O   1 
ATOM   948  C  CB  . MET A 1 130 ? 55.943 10.681 24.968  1.00 43.19 ? 130 MET A CB  1 
ATOM   949  C  CG  . MET A 1 130 ? 55.559 12.136 25.038  1.00 42.10 ? 130 MET A CG  1 
ATOM   950  S  SD  . MET A 1 130 ? 55.358 12.795 26.713  1.00 42.46 ? 130 MET A SD  1 
ATOM   951  C  CE  . MET A 1 130 ? 55.601 14.534 26.320  1.00 49.88 ? 130 MET A CE  1 
ATOM   952  N  N   . LYS A 1 131 ? 56.832 7.840  23.765  1.00 42.91 ? 131 LYS A N   1 
ATOM   953  C  CA  . LYS A 1 131 ? 57.794 6.738  23.841  1.00 53.73 ? 131 LYS A CA  1 
ATOM   954  C  C   . LYS A 1 131 ? 58.271 6.321  22.455  1.00 58.09 ? 131 LYS A C   1 
ATOM   955  O  O   . LYS A 1 131 ? 57.923 5.237  21.981  1.00 59.86 ? 131 LYS A O   1 
ATOM   956  C  CB  . LYS A 1 131 ? 57.202 5.538  24.567  1.00 42.17 ? 131 LYS A CB  1 
ATOM   957  N  N   . PHE B 1 3   ? 70.353 17.220 29.740  1.00 49.13 ? 3   PHE B N   1 
ATOM   958  C  CA  . PHE B 1 3   ? 71.084 15.982 29.485  1.00 50.90 ? 3   PHE B CA  1 
ATOM   959  C  C   . PHE B 1 3   ? 71.719 15.951 28.084  1.00 52.96 ? 3   PHE B C   1 
ATOM   960  O  O   . PHE B 1 3   ? 72.792 15.384 27.931  1.00 59.14 ? 3   PHE B O   1 
ATOM   961  C  CB  . PHE B 1 3   ? 70.159 14.765 29.674  1.00 62.12 ? 3   PHE B CB  1 
ATOM   962  C  CG  . PHE B 1 3   ? 70.873 13.503 30.085  1.00 57.03 ? 3   PHE B CG  1 
ATOM   963  C  CD1 . PHE B 1 3   ? 70.514 12.848 31.252  1.00 56.44 ? 3   PHE B CD1 1 
ATOM   964  C  CD2 . PHE B 1 3   ? 71.889 12.958 29.303  1.00 63.94 ? 3   PHE B CD2 1 
ATOM   965  C  CE1 . PHE B 1 3   ? 71.163 11.673 31.623  1.00 64.01 ? 3   PHE B CE1 1 
ATOM   966  C  CE2 . PHE B 1 3   ? 72.536 11.793 29.668  1.00 59.36 ? 3   PHE B CE2 1 
ATOM   967  C  CZ  . PHE B 1 3   ? 72.170 11.151 30.836  1.00 60.91 ? 3   PHE B CZ  1 
ATOM   968  N  N   . ARG B 1 4   ? 71.113 16.585 27.074  1.00 50.75 ? 4   ARG B N   1 
ATOM   969  C  CA  . ARG B 1 4   ? 71.623 16.394 25.710  1.00 50.75 ? 4   ARG B CA  1 
ATOM   970  C  C   . ARG B 1 4   ? 71.985 17.717 25.014  1.00 50.09 ? 4   ARG B C   1 
ATOM   971  O  O   . ARG B 1 4   ? 71.479 18.774 25.386  1.00 53.35 ? 4   ARG B O   1 
ATOM   972  C  CB  . ARG B 1 4   ? 70.577 15.632 24.875  1.00 52.02 ? 4   ARG B CB  1 
ATOM   973  C  CG  . ARG B 1 4   ? 69.569 14.796 25.674  1.00 43.85 ? 4   ARG B CG  1 
ATOM   974  C  CD  . ARG B 1 4   ? 70.194 13.526 26.213  1.00 47.40 ? 4   ARG B CD  1 
ATOM   975  N  NE  . ARG B 1 4   ? 69.247 12.739 27.000  1.00 51.35 ? 4   ARG B NE  1 
ATOM   976  N  N   . ILE B 1 5   ? 72.780 17.640 23.945  1.00 48.35 ? 5   ILE B N   1 
ATOM   977  C  CA  . ILE B 1 5   ? 73.350 18.843 23.313  1.00 52.26 ? 5   ILE B CA  1 
ATOM   978  C  C   . ILE B 1 5   ? 72.852 19.316 21.945  1.00 57.61 ? 5   ILE B C   1 
ATOM   979  O  O   . ILE B 1 5   ? 73.396 20.276 21.396  1.00 77.11 ? 5   ILE B O   1 
ATOM   980  C  CB  . ILE B 1 5   ? 74.897 18.711 23.164  1.00 54.27 ? 5   ILE B CB  1 
ATOM   981  N  N   . GLY B 1 6   ? 71.875 18.655 21.359  1.00 51.56 ? 6   GLY B N   1 
ATOM   982  C  CA  . GLY B 1 6   ? 71.185 19.258 20.228  1.00 57.03 ? 6   GLY B CA  1 
ATOM   983  C  C   . GLY B 1 6   ? 71.724 18.710 18.926  1.00 61.15 ? 6   GLY B C   1 
ATOM   984  O  O   . GLY B 1 6   ? 71.002 18.646 17.933  1.00 65.18 ? 6   GLY B O   1 
ATOM   985  N  N   . GLU B 1 7   ? 72.987 18.292 18.937  1.00 52.94 ? 7   GLU B N   1 
ATOM   986  C  CA  . GLU B 1 7   ? 73.520 17.463 17.864  1.00 53.06 ? 7   GLU B CA  1 
ATOM   987  C  C   . GLU B 1 7   ? 73.095 16.036 18.249  1.00 56.46 ? 7   GLU B C   1 
ATOM   988  O  O   . GLU B 1 7   ? 72.589 15.244 17.446  1.00 56.34 ? 7   GLU B O   1 
ATOM   989  C  CB  . GLU B 1 7   ? 75.036 17.621 17.760  1.00 67.81 ? 7   GLU B CB  1 
ATOM   990  N  N   . LEU B 1 8   ? 73.271 15.781 19.547  1.00 52.84 ? 8   LEU B N   1 
ATOM   991  C  CA  . LEU B 1 8   ? 72.601 14.737 20.306  1.00 55.22 ? 8   LEU B CA  1 
ATOM   992  C  C   . LEU B 1 8   ? 71.149 15.238 20.350  1.00 64.01 ? 8   LEU B C   1 
ATOM   993  O  O   . LEU B 1 8   ? 70.916 16.371 19.970  1.00 63.02 ? 8   LEU B O   1 
ATOM   994  C  CB  . LEU B 1 8   ? 73.208 14.577 21.715  1.00 60.12 ? 8   LEU B CB  1 
ATOM   995  C  CG  . LEU B 1 8   ? 74.699 14.497 22.153  1.00 57.49 ? 8   LEU B CG  1 
ATOM   996  C  CD1 . LEU B 1 8   ? 75.782 15.107 21.232  1.00 59.99 ? 8   LEU B CD1 1 
ATOM   997  C  CD2 . LEU B 1 8   ? 74.880 14.987 23.615  1.00 47.18 ? 8   LEU B CD2 1 
ATOM   998  N  N   . ALA B 1 9   ? 70.156 14.430 20.709  1.00 52.93 ? 9   ALA B N   1 
ATOM   999  C  CA  . ALA B 1 9   ? 68.772 14.959 20.796  1.00 58.76 ? 9   ALA B CA  1 
ATOM   1000 C  C   . ALA B 1 9   ? 68.203 15.271 19.412  1.00 51.78 ? 9   ALA B C   1 
ATOM   1001 O  O   . ALA B 1 9   ? 67.010 15.456 19.249  1.00 67.36 ? 9   ALA B O   1 
ATOM   1002 C  CB  . ALA B 1 9   ? 68.690 16.210 21.699  1.00 50.80 ? 9   ALA B CB  1 
ATOM   1003 N  N   . ASP B 1 10  ? 69.076 15.290 18.414  1.00 56.07 ? 10  ASP B N   1 
ATOM   1004 C  CA  . ASP B 1 10  ? 68.677 15.203 17.023  1.00 58.70 ? 10  ASP B CA  1 
ATOM   1005 C  C   . ASP B 1 10  ? 68.476 13.699 16.790  1.00 64.00 ? 10  ASP B C   1 
ATOM   1006 O  O   . ASP B 1 10  ? 68.263 13.252 15.665  1.00 70.63 ? 10  ASP B O   1 
ATOM   1007 C  CB  . ASP B 1 10  ? 69.719 15.804 16.083  1.00 58.30 ? 10  ASP B CB  1 
ATOM   1008 N  N   . LYS B 1 11  ? 68.572 12.954 17.905  1.00 70.48 ? 11  LYS B N   1 
ATOM   1009 C  CA  . LYS B 1 11  ? 68.185 11.542 18.080  1.00 52.12 ? 11  LYS B CA  1 
ATOM   1010 C  C   . LYS B 1 11  ? 66.674 11.333 18.051  1.00 53.56 ? 11  LYS B C   1 
ATOM   1011 O  O   . LYS B 1 11  ? 66.176 10.221 18.205  1.00 65.60 ? 11  LYS B O   1 
ATOM   1012 C  CB  . LYS B 1 11  ? 68.697 11.026 19.420  1.00 44.38 ? 11  LYS B CB  1 
ATOM   1013 N  N   . CYS B 1 12  ? 65.937 12.418 17.899  1.00 60.44 ? 12  CYS B N   1 
ATOM   1014 C  CA  . CYS B 1 12  ? 64.504 12.319 17.708  1.00 54.43 ? 12  CYS B CA  1 
ATOM   1015 C  C   . CYS B 1 12  ? 64.216 12.273 16.214  1.00 52.20 ? 12  CYS B C   1 
ATOM   1016 O  O   . CYS B 1 12  ? 63.061 12.285 15.807  1.00 49.12 ? 12  CYS B O   1 
ATOM   1017 C  CB  . CYS B 1 12  ? 63.787 13.507 18.341  1.00 53.57 ? 12  CYS B CB  1 
ATOM   1018 S  SG  . CYS B 1 12  ? 63.759 13.496 20.131  1.00 51.57 ? 12  CYS B SG  1 
ATOM   1019 N  N   . GLY B 1 13  ? 65.272 12.259 15.400  1.00 58.25 ? 13  GLY B N   1 
ATOM   1020 C  CA  . GLY B 1 13  ? 65.122 12.261 13.956  1.00 45.35 ? 13  GLY B CA  1 
ATOM   1021 C  C   . GLY B 1 13  ? 64.807 13.627 13.370  1.00 45.29 ? 13  GLY B C   1 
ATOM   1022 O  O   . GLY B 1 13  ? 64.120 13.728 12.365  1.00 45.70 ? 13  GLY B O   1 
ATOM   1023 N  N   . VAL B 1 14  ? 65.288 14.682 14.010  1.00 44.80 ? 14  VAL B N   1 
ATOM   1024 C  CA  . VAL B 1 14  ? 65.077 16.045 13.535  1.00 44.86 ? 14  VAL B CA  1 
ATOM   1025 C  C   . VAL B 1 14  ? 66.430 16.757 13.383  1.00 44.92 ? 14  VAL B C   1 
ATOM   1026 O  O   . VAL B 1 14  ? 67.259 16.714 14.299  1.00 44.58 ? 14  VAL B O   1 
ATOM   1027 C  CB  . VAL B 1 14  ? 64.155 16.830 14.520  1.00 48.69 ? 14  VAL B CB  1 
ATOM   1028 C  CG1 . VAL B 1 14  ? 63.730 18.191 13.954  1.00 44.70 ? 14  VAL B CG1 1 
ATOM   1029 C  CG2 . VAL B 1 14  ? 62.931 16.006 14.861  1.00 44.50 ? 14  VAL B CG2 1 
ATOM   1030 N  N   . ASN B 1 15  ? 66.687 17.372 12.225  1.00 46.55 ? 15  ASN B N   1 
ATOM   1031 C  CA  . ASN B 1 15  ? 67.970 18.073 12.040  1.00 46.80 ? 15  ASN B CA  1 
ATOM   1032 C  C   . ASN B 1 15  ? 67.997 19.364 12.857  1.00 46.50 ? 15  ASN B C   1 
ATOM   1033 O  O   . ASN B 1 15  ? 66.937 19.910 13.182  1.00 46.31 ? 15  ASN B O   1 
ATOM   1034 C  CB  . ASN B 1 15  ? 68.278 18.353 10.558  1.00 47.66 ? 15  ASN B CB  1 
ATOM   1035 C  CG  . ASN B 1 15  ? 67.212 19.174 9.873   1.00 52.07 ? 15  ASN B CG  1 
ATOM   1036 O  OD1 . ASN B 1 15  ? 66.752 20.188 10.401  1.00 60.47 ? 15  ASN B OD1 1 
ATOM   1037 N  ND2 . ASN B 1 15  ? 66.848 18.772 8.658   1.00 52.23 ? 15  ASN B ND2 1 
ATOM   1038 N  N   . LYS B 1 16  ? 69.202 19.873 13.124  1.00 53.18 ? 16  LYS B N   1 
ATOM   1039 C  CA  . LYS B 1 16  ? 69.398 20.724 14.281  1.00 52.78 ? 16  LYS B CA  1 
ATOM   1040 C  C   . LYS B 1 16  ? 68.497 21.937 14.121  1.00 61.41 ? 16  LYS B C   1 
ATOM   1041 O  O   . LYS B 1 16  ? 68.675 22.774 13.227  1.00 47.43 ? 16  LYS B O   1 
ATOM   1042 C  CB  . LYS B 1 16  ? 70.873 21.114 14.415  1.00 50.61 ? 16  LYS B CB  1 
ATOM   1043 N  N   . GLU B 1 17  ? 67.541 22.007 15.051  1.00 76.03 ? 17  GLU B N   1 
ATOM   1044 C  CA  . GLU B 1 17  ? 66.313 22.745 14.813  1.00 64.39 ? 17  GLU B CA  1 
ATOM   1045 C  C   . GLU B 1 17  ? 66.085 23.916 15.731  1.00 64.01 ? 17  GLU B C   1 
ATOM   1046 O  O   . GLU B 1 17  ? 65.475 23.779 16.802  1.00 55.77 ? 17  GLU B O   1 
ATOM   1047 C  CB  . GLU B 1 17  ? 65.142 21.800 14.991  1.00 45.13 ? 17  GLU B CB  1 
ATOM   1048 C  CG  . GLU B 1 17  ? 63.916 22.218 14.258  1.00 45.48 ? 17  GLU B CG  1 
ATOM   1049 C  CD  . GLU B 1 17  ? 64.056 22.012 12.745  1.00 56.45 ? 17  GLU B CD  1 
ATOM   1050 O  OE1 . GLU B 1 17  ? 65.179 22.086 12.194  1.00 59.37 ? 17  GLU B OE1 1 
ATOM   1051 O  OE2 . GLU B 1 17  ? 63.029 21.706 12.107  1.00 51.28 1 17  GLU B OE2 1 
ATOM   1052 N  N   . THR B 1 18  ? 66.431 25.086 15.227  1.00 58.57 ? 18  THR B N   1 
ATOM   1053 C  CA  . THR B 1 18  ? 66.224 26.294 15.969  1.00 59.45 ? 18  THR B CA  1 
ATOM   1054 C  C   . THR B 1 18  ? 64.817 26.787 15.732  1.00 55.24 ? 18  THR B C   1 
ATOM   1055 O  O   . THR B 1 18  ? 64.301 27.519 16.543  1.00 55.95 ? 18  THR B O   1 
ATOM   1056 C  CB  . THR B 1 18  ? 67.235 27.381 15.577  1.00 65.40 ? 18  THR B CB  1 
ATOM   1057 N  N   . ILE B 1 19  ? 64.189 26.383 14.630  1.00 46.71 ? 19  ILE B N   1 
ATOM   1058 C  CA  . ILE B 1 19  ? 62.901 26.963 14.284  1.00 47.09 ? 19  ILE B CA  1 
ATOM   1059 C  C   . ILE B 1 19  ? 61.897 26.548 15.333  1.00 46.70 ? 19  ILE B C   1 
ATOM   1060 O  O   . ILE B 1 19  ? 61.033 27.324 15.709  1.00 57.17 ? 19  ILE B O   1 
ATOM   1061 C  CB  . ILE B 1 19  ? 62.415 26.568 12.856  1.00 53.29 ? 19  ILE B CB  1 
ATOM   1062 C  CG1 . ILE B 1 19  ? 61.101 27.295 12.520  1.00 55.58 ? 19  ILE B CG1 1 
ATOM   1063 C  CG2 . ILE B 1 19  ? 62.243 25.073 12.719  1.00 54.09 ? 19  ILE B CG2 1 
ATOM   1064 C  CD1 . ILE B 1 19  ? 60.510 26.949 11.174  1.00 53.40 ? 19  ILE B CD1 1 
ATOM   1065 N  N   . ARG B 1 20  ? 62.054 25.346 15.862  1.00 48.95 ? 20  ARG B N   1 
ATOM   1066 C  CA  . ARG B 1 20  ? 61.100 24.831 16.827  1.00 44.51 ? 20  ARG B CA  1 
ATOM   1067 C  C   . ARG B 1 20  ? 61.051 25.683 18.077  1.00 44.70 ? 20  ARG B C   1 
ATOM   1068 O  O   . ARG B 1 20  ? 59.967 26.063 18.502  1.00 45.03 ? 20  ARG B O   1 
ATOM   1069 C  CB  . ARG B 1 20  ? 61.447 23.397 17.202  1.00 43.92 ? 20  ARG B CB  1 
ATOM   1070 C  CG  . ARG B 1 20  ? 60.485 22.369 16.713  1.00 43.88 ? 20  ARG B CG  1 
ATOM   1071 C  CD  . ARG B 1 20  ? 60.312 22.443 15.242  1.00 44.18 ? 20  ARG B CD  1 
ATOM   1072 N  NE  . ARG B 1 20  ? 59.961 21.129 14.727  1.00 44.07 ? 20  ARG B NE  1 
ATOM   1073 C  CZ  . ARG B 1 20  ? 59.499 20.940 13.498  1.00 45.00 ? 20  ARG B CZ  1 
ATOM   1074 N  NH1 . ARG B 1 20  ? 59.336 21.975 12.690  1.00 54.23 ? 20  ARG B NH1 1 
ATOM   1075 N  NH2 . ARG B 1 20  ? 59.196 19.731 13.071  1.00 44.40 ? 20  ARG B NH2 1 
ATOM   1076 N  N   . TYR B 1 21  ? 62.195 25.993 18.683  1.00 51.11 ? 21  TYR B N   1 
ATOM   1077 C  CA  . TYR B 1 21  ? 62.117 26.849 19.868  1.00 60.18 ? 21  TYR B CA  1 
ATOM   1078 C  C   . TYR B 1 21  ? 61.955 28.318 19.458  1.00 59.39 ? 21  TYR B C   1 
ATOM   1079 O  O   . TYR B 1 21  ? 61.422 29.122 20.223  1.00 61.34 ? 21  TYR B O   1 
ATOM   1080 C  CB  . TYR B 1 21  ? 63.266 26.623 20.882  1.00 54.54 ? 21  TYR B CB  1 
ATOM   1081 C  CG  . TYR B 1 21  ? 64.730 26.810 20.549  1.00 63.43 ? 21  TYR B CG  1 
ATOM   1082 C  CD1 . TYR B 1 21  ? 65.344 28.056 20.674  1.00 69.64 ? 21  TYR B CD1 1 
ATOM   1083 C  CD2 . TYR B 1 21  ? 65.541 25.707 20.280  1.00 58.52 ? 21  TYR B CD2 1 
ATOM   1084 C  CE1 . TYR B 1 21  ? 66.710 28.216 20.435  1.00 61.51 ? 21  TYR B CE1 1 
ATOM   1085 C  CE2 . TYR B 1 21  ? 66.901 25.851 20.044  1.00 57.03 ? 21  TYR B CE2 1 
ATOM   1086 C  CZ  . TYR B 1 21  ? 67.484 27.103 20.119  1.00 64.19 ? 21  TYR B CZ  1 
ATOM   1087 O  OH  . TYR B 1 21  ? 68.844 27.230 19.874  1.00 68.04 ? 21  TYR B OH  1 
ATOM   1088 N  N   . TYR B 1 22  ? 62.378 28.647 18.246  1.00 51.17 ? 22  TYR B N   1 
ATOM   1089 C  CA  . TYR B 1 22  ? 62.139 29.963 17.677  1.00 49.41 ? 22  TYR B CA  1 
ATOM   1090 C  C   . TYR B 1 22  ? 60.623 30.140 17.618  1.00 52.94 ? 22  TYR B C   1 
ATOM   1091 O  O   . TYR B 1 22  ? 60.104 31.238 17.849  1.00 51.79 ? 22  TYR B O   1 
ATOM   1092 C  CB  . TYR B 1 22  ? 62.776 30.102 16.278  1.00 51.79 ? 22  TYR B CB  1 
ATOM   1093 C  CG  . TYR B 1 22  ? 63.762 31.244 16.135  1.00 50.38 ? 22  TYR B CG  1 
ATOM   1094 C  CD2 . TYR B 1 22  ? 64.639 31.333 15.050  1.00 51.01 ? 22  TYR B CD2 1 
ATOM   1095 C  CE2 . TYR B 1 22  ? 64.660 30.382 14.048  1.00 49.88 ? 22  TYR B CE2 1 
ATOM   1096 N  N   . GLU B 1 23  ? 59.915 29.054 17.311  1.00 46.88 ? 23  GLU B N   1 
ATOM   1097 C  CA  . GLU B 1 23  ? 58.449 29.080 17.261  1.00 47.19 ? 23  GLU B CA  1 
ATOM   1098 C  C   . GLU B 1 23  ? 57.760 28.769 18.569  1.00 47.14 ? 23  GLU B C   1 
ATOM   1099 O  O   . GLU B 1 23  ? 56.547 28.639 18.570  1.00 60.31 ? 23  GLU B O   1 
ATOM   1100 C  CB  . GLU B 1 23  ? 57.925 28.108 16.217  1.00 48.97 ? 23  GLU B CB  1 
ATOM   1101 C  CG  . GLU B 1 23  ? 57.967 28.673 14.829  1.00 58.26 ? 23  GLU B CG  1 
ATOM   1102 C  CD  . GLU B 1 23  ? 57.829 27.605 13.785  1.00 67.87 ? 23  GLU B CD  1 
ATOM   1103 O  OE1 . GLU B 1 23  ? 57.623 26.430 14.176  1.00 51.01 ? 23  GLU B OE1 1 
ATOM   1104 O  OE2 . GLU B 1 23  ? 57.960 27.934 12.584  1.00 75.42 ? 23  GLU B OE2 1 
ATOM   1105 N  N   . ARG B 1 24  ? 58.524 28.592 19.647  1.00 48.90 ? 24  ARG B N   1 
ATOM   1106 C  CA  . ARG B 1 24  ? 57.997 28.304 21.002  1.00 52.09 ? 24  ARG B CA  1 
ATOM   1107 C  C   . ARG B 1 24  ? 57.554 26.836 21.193  1.00 48.40 ? 24  ARG B C   1 
ATOM   1108 O  O   . ARG B 1 24  ? 57.240 26.413 22.304  1.00 52.26 ? 24  ARG B O   1 
ATOM   1109 C  CB  . ARG B 1 24  ? 56.845 29.273 21.338  1.00 63.16 ? 24  ARG B CB  1 
ATOM   1110 C  CG  . ARG B 1 24  ? 55.843 28.848 22.408  1.00 59.86 ? 24  ARG B CG  1 
ATOM   1111 C  CD  . ARG B 1 24  ? 54.435 29.299 22.033  1.00 59.80 ? 24  ARG B CD  1 
ATOM   1112 N  NE  . ARG B 1 24  ? 53.438 28.753 22.945  1.00 66.95 ? 24  ARG B NE  1 
ATOM   1113 C  CZ  . ARG B 1 24  ? 52.727 27.650 22.727  1.00 62.15 ? 24  ARG B CZ  1 
ATOM   1114 N  NH1 . ARG B 1 24  ? 52.882 26.945 21.613  1.00 50.46 ? 24  ARG B NH1 1 
ATOM   1115 N  NH2 . ARG B 1 24  ? 51.850 27.256 23.636  1.00 62.06 ? 24  ARG B NH2 1 
ATOM   1116 N  N   . LEU B 1 25  ? 57.613 26.033 20.135  1.00 45.52 ? 25  LEU B N   1 
ATOM   1117 C  CA  . LEU B 1 25  ? 57.236 24.623 20.250  1.00 49.18 ? 25  LEU B CA  1 
ATOM   1118 C  C   . LEU B 1 25  ? 58.165 23.854 21.184  1.00 48.08 ? 25  LEU B C   1 
ATOM   1119 O  O   . LEU B 1 25  ? 57.723 23.102 22.060  1.00 49.98 ? 25  LEU B O   1 
ATOM   1120 C  CB  . LEU B 1 25  ? 57.220 23.946 18.880  1.00 46.67 ? 25  LEU B CB  1 
ATOM   1121 C  CG  . LEU B 1 25  ? 56.223 24.484 17.856  1.00 45.32 ? 25  LEU B CG  1 
ATOM   1122 C  CD1 . LEU B 1 25  ? 56.459 23.755 16.563  1.00 45.06 ? 25  LEU B CD1 1 
ATOM   1123 C  CD2 . LEU B 1 25  ? 54.785 24.348 18.322  1.00 45.78 ? 25  LEU B CD2 1 
ATOM   1124 N  N   . GLY B 1 26  ? 59.458 24.033 20.974  1.00 57.33 ? 26  GLY B N   1 
ATOM   1125 C  CA  . GLY B 1 26  ? 60.451 23.405 21.817  1.00 60.45 ? 26  GLY B CA  1 
ATOM   1126 C  C   . GLY B 1 26  ? 60.904 24.402 22.850  1.00 48.93 ? 26  GLY B C   1 
ATOM   1127 O  O   . GLY B 1 26  ? 60.836 25.596 22.641  1.00 46.86 ? 26  GLY B O   1 
ATOM   1128 N  N   . LEU B 1 27  ? 61.439 23.909 23.943  1.00 52.83 ? 27  LEU B N   1 
ATOM   1129 C  CA  . LEU B 1 27  ? 61.845 24.779 25.009  1.00 52.91 ? 27  LEU B CA  1 
ATOM   1130 C  C   . LEU B 1 27  ? 63.174 25.445 24.654  1.00 59.10 ? 27  LEU B C   1 
ATOM   1131 O  O   . LEU B 1 27  ? 63.788 25.101 23.634  1.00 55.03 ? 27  LEU B O   1 
ATOM   1132 C  CB  . LEU B 1 27  ? 61.969 23.932 26.245  1.00 53.65 ? 27  LEU B CB  1 
ATOM   1133 C  CG  . LEU B 1 27  ? 61.778 24.616 27.555  1.00 60.29 ? 27  LEU B CG  1 
ATOM   1134 C  CD1 . LEU B 1 27  ? 60.365 25.125 27.490  1.00 67.01 ? 27  LEU B CD1 1 
ATOM   1135 C  CD2 . LEU B 1 27  ? 61.892 23.561 28.604  1.00 67.39 ? 27  LEU B CD2 1 
ATOM   1136 N  N   . ILE B 1 28  ? 63.685 26.340 25.495  1.00 55.91 ? 28  ILE B N   1 
ATOM   1137 C  CA  . ILE B 1 28  ? 65.035 26.857 25.228  1.00 56.63 ? 28  ILE B CA  1 
ATOM   1138 C  C   . ILE B 1 28  ? 66.055 26.056 26.023  1.00 47.63 ? 28  ILE B C   1 
ATOM   1139 O  O   . ILE B 1 28  ? 65.807 25.684 27.170  1.00 54.96 ? 28  ILE B O   1 
ATOM   1140 C  CB  . ILE B 1 28  ? 65.147 28.376 25.518  1.00 60.18 ? 28  ILE B CB  1 
ATOM   1141 C  CG1 . ILE B 1 28  ? 66.062 29.075 24.506  1.00 58.71 ? 28  ILE B CG1 1 
ATOM   1142 C  CG2 . ILE B 1 28  ? 65.405 28.679 26.986  1.00 65.22 ? 28  ILE B CG2 1 
ATOM   1143 C  CD1 . ILE B 1 28  ? 66.091 30.615 24.615  1.00 55.78 ? 28  ILE B CD1 1 
ATOM   1144 N  N   . PRO B 1 29  ? 67.205 25.755 25.426  1.00 46.93 ? 29  PRO B N   1 
ATOM   1145 C  CA  . PRO B 1 29  ? 68.059 24.959 26.309  1.00 48.28 ? 29  PRO B CA  1 
ATOM   1146 C  C   . PRO B 1 29  ? 68.668 25.742 27.475  1.00 59.06 ? 29  PRO B C   1 
ATOM   1147 O  O   . PRO B 1 29  ? 68.749 26.977 27.491  1.00 63.14 ? 29  PRO B O   1 
ATOM   1148 C  CB  . PRO B 1 29  ? 69.166 24.472 25.376  1.00 51.67 ? 29  PRO B CB  1 
ATOM   1149 C  CG  . PRO B 1 29  ? 69.201 25.481 24.252  1.00 52.56 ? 29  PRO B CG  1 
ATOM   1150 C  CD  . PRO B 1 29  ? 67.875 26.166 24.183  1.00 53.89 ? 29  PRO B CD  1 
ATOM   1151 N  N   . GLU B 1 30  ? 69.101 24.968 28.459  1.00 59.66 ? 30  GLU B N   1 
ATOM   1152 C  CA  . GLU B 1 30  ? 69.758 25.462 29.659  1.00 59.60 ? 30  GLU B CA  1 
ATOM   1153 C  C   . GLU B 1 30  ? 71.281 25.357 29.563  1.00 50.24 ? 30  GLU B C   1 
ATOM   1154 O  O   . GLU B 1 30  ? 71.800 24.416 28.970  1.00 55.15 ? 30  GLU B O   1 
ATOM   1155 C  CB  . GLU B 1 30  ? 69.237 24.694 30.876  1.00 63.28 ? 30  GLU B CB  1 
ATOM   1156 N  N   . PRO B 1 31  ? 71.999 26.365 30.082  1.00 51.96 ? 31  PRO B N   1 
ATOM   1157 C  CA  . PRO B 1 31  ? 73.462 26.520 30.092  1.00 62.94 ? 31  PRO B CA  1 
ATOM   1158 C  C   . PRO B 1 31  ? 74.177 25.736 31.216  1.00 64.24 ? 31  PRO B C   1 
ATOM   1159 O  O   . PRO B 1 31  ? 74.414 26.307 32.275  1.00 67.94 ? 31  PRO B O   1 
ATOM   1160 C  CB  . PRO B 1 31  ? 73.648 28.029 30.277  1.00 52.51 ? 31  PRO B CB  1 
ATOM   1161 N  N   . GLU B 1 32  ? 74.485 24.459 30.968  1.00 63.91 ? 32  GLU B N   1 
ATOM   1162 C  CA  . GLU B 1 32  ? 75.194 23.542 31.885  1.00 66.48 ? 32  GLU B CA  1 
ATOM   1163 C  C   . GLU B 1 32  ? 75.863 24.175 33.107  1.00 61.86 ? 32  GLU B C   1 
ATOM   1164 O  O   . GLU B 1 32  ? 76.935 24.773 33.012  1.00 63.42 ? 32  GLU B O   1 
ATOM   1165 C  CB  . GLU B 1 32  ? 76.253 22.756 31.102  1.00 64.55 ? 32  GLU B CB  1 
ATOM   1166 N  N   . GLU B 1 35  ? 79.641 24.119 33.368  1.00 74.35 ? 35  GLU B N   1 
ATOM   1167 C  CA  . GLU B 1 35  ? 80.660 24.242 32.326  1.00 73.58 ? 35  GLU B CA  1 
ATOM   1168 C  C   . GLU B 1 35  ? 80.094 24.998 31.141  1.00 70.14 ? 35  GLU B C   1 
ATOM   1169 O  O   . GLU B 1 35  ? 80.103 24.505 30.019  1.00 77.12 ? 35  GLU B O   1 
ATOM   1170 C  CB  . GLU B 1 35  ? 81.162 22.865 31.887  1.00 73.27 ? 35  GLU B CB  1 
ATOM   1171 N  N   . LYS B 1 36  ? 79.600 26.199 31.419  1.00 79.64 ? 36  LYS B N   1 
ATOM   1172 C  CA  . LYS B 1 36  ? 78.949 27.086 30.451  1.00 74.48 ? 36  LYS B CA  1 
ATOM   1173 C  C   . LYS B 1 36  ? 77.728 26.420 29.836  1.00 66.72 ? 36  LYS B C   1 
ATOM   1174 O  O   . LYS B 1 36  ? 77.039 25.701 30.543  1.00 74.97 ? 36  LYS B O   1 
ATOM   1175 C  CB  . LYS B 1 36  ? 79.922 27.537 29.376  1.00 76.74 ? 36  LYS B CB  1 
ATOM   1176 N  N   . GLY B 1 37  ? 77.462 26.625 28.543  1.00 64.09 ? 37  GLY B N   1 
ATOM   1177 C  CA  . GLY B 1 37  ? 76.398 25.888 27.846  1.00 64.91 ? 37  GLY B CA  1 
ATOM   1178 C  C   . GLY B 1 37  ? 76.703 24.500 27.308  1.00 64.86 ? 37  GLY B C   1 
ATOM   1179 O  O   . GLY B 1 37  ? 77.785 23.952 27.584  1.00 63.80 ? 37  GLY B O   1 
ATOM   1180 N  N   . TYR B 1 38  ? 75.779 23.900 26.549  1.00 57.09 ? 38  TYR B N   1 
ATOM   1181 C  CA  . TYR B 1 38  ? 74.390 24.329 26.299  1.00 60.41 ? 38  TYR B CA  1 
ATOM   1182 C  C   . TYR B 1 38  ? 73.501 23.061 26.090  1.00 59.71 ? 38  TYR B C   1 
ATOM   1183 O  O   . TYR B 1 38  ? 73.632 22.396 25.062  1.00 52.03 ? 38  TYR B O   1 
ATOM   1184 C  CB  . TYR B 1 38  ? 74.319 25.250 25.082  1.00 63.29 ? 38  TYR B CB  1 
ATOM   1185 N  N   . ARG B 1 39  ? 72.600 22.712 27.008  1.00 48.77 ? 39  ARG B N   1 
ATOM   1186 C  CA  . ARG B 1 39  ? 71.931 21.407 26.884  1.00 47.79 ? 39  ARG B CA  1 
ATOM   1187 C  C   . ARG B 1 39  ? 70.376 21.364 27.003  1.00 55.95 ? 39  ARG B C   1 
ATOM   1188 O  O   . ARG B 1 39  ? 69.768 22.176 27.712  1.00 52.67 ? 39  ARG B O   1 
ATOM   1189 C  CB  . ARG B 1 39  ? 72.550 20.452 27.914  1.00 50.31 ? 39  ARG B CB  1 
ATOM   1190 C  CG  . ARG B 1 39  ? 74.098 20.403 27.868  1.00 53.38 ? 39  ARG B CG  1 
ATOM   1191 C  CD  . ARG B 1 39  ? 74.660 18.998 27.706  1.00 53.01 ? 39  ARG B CD  1 
ATOM   1192 N  N   . MET B 1 40  ? 69.749 20.385 26.339  1.00 49.33 ? 40  MET B N   1 
ATOM   1193 C  CA  . MET B 1 40  ? 68.281 20.241 26.336  1.00 44.46 ? 40  MET B CA  1 
ATOM   1194 C  C   . MET B 1 40  ? 67.719 19.180 27.316  1.00 42.49 ? 40  MET B C   1 
ATOM   1195 O  O   . MET B 1 40  ? 68.406 18.222 27.697  1.00 44.11 ? 40  MET B O   1 
ATOM   1196 C  CB  . MET B 1 40  ? 67.801 19.920 24.920  1.00 39.19 ? 40  MET B CB  1 
ATOM   1197 C  CG  . MET B 1 40  ? 68.425 20.787 23.847  1.00 38.41 ? 40  MET B CG  1 
ATOM   1198 S  SD  . MET B 1 40  ? 67.450 22.270 23.551  1.00 75.13 ? 40  MET B SD  1 
ATOM   1199 C  CE  . MET B 1 40  ? 68.276 22.945 22.109  1.00 36.37 ? 40  MET B CE  1 
ATOM   1200 N  N   . GLN B 1 43  ? 65.350 16.426 28.940  1.00 47.83 ? 43  GLN B N   1 
ATOM   1201 C  CA  . GLN B 1 43  ? 64.748 15.118 28.649  1.00 54.95 ? 43  GLN B CA  1 
ATOM   1202 C  C   . GLN B 1 43  ? 63.276 15.222 28.308  1.00 48.71 ? 43  GLN B C   1 
ATOM   1203 O  O   . GLN B 1 43  ? 62.751 14.459 27.496  1.00 43.46 ? 43  GLN B O   1 
ATOM   1204 C  CB  . GLN B 1 43  ? 64.885 14.172 29.835  1.00 45.98 ? 43  GLN B CB  1 
ATOM   1205 C  CG  . GLN B 1 43  ? 65.672 12.891 29.586  1.00 47.39 ? 43  GLN B CG  1 
ATOM   1206 C  CD  . GLN B 1 43  ? 65.028 11.938 28.600  1.00 50.80 ? 43  GLN B CD  1 
ATOM   1207 O  OE1 . GLN B 1 43  ? 63.814 11.749 28.599  1.00 48.01 ? 43  GLN B OE1 1 
ATOM   1208 N  NE2 . GLN B 1 43  ? 65.856 11.266 27.808  1.00 53.12 ? 43  GLN B NE2 1 
ATOM   1209 N  N   . GLN B 1 44  ? 62.608 16.174 28.935  1.00 43.10 ? 44  GLN B N   1 
ATOM   1210 C  CA  . GLN B 1 44  ? 61.196 16.352 28.709  1.00 43.33 ? 44  GLN B CA  1 
ATOM   1211 C  C   . GLN B 1 44  ? 61.038 17.043 27.372  1.00 40.83 ? 44  GLN B C   1 
ATOM   1212 O  O   . GLN B 1 44  ? 59.967 17.046 26.781  1.00 37.42 ? 44  GLN B O   1 
ATOM   1213 C  CB  . GLN B 1 44  ? 60.574 17.166 29.835  1.00 45.56 ? 44  GLN B CB  1 
ATOM   1214 C  CG  . GLN B 1 44  ? 61.058 16.741 31.181  1.00 59.28 ? 44  GLN B CG  1 
ATOM   1215 C  CD  . GLN B 1 44  ? 60.605 17.670 32.273  1.00 56.50 ? 44  GLN B CD  1 
ATOM   1216 O  OE1 . GLN B 1 44  ? 59.709 18.498 32.073  1.00 56.83 ? 44  GLN B OE1 1 
ATOM   1217 N  NE2 . GLN B 1 44  ? 61.224 17.544 33.444  1.00 54.28 ? 44  GLN B NE2 1 
ATOM   1218 N  N   . THR B 1 45  ? 62.131 17.652 26.935  1.00 37.80 ? 45  THR B N   1 
ATOM   1219 C  CA  . THR B 1 45  ? 62.235 18.252 25.621  1.00 37.44 ? 45  THR B CA  1 
ATOM   1220 C  C   . THR B 1 45  ? 62.442 17.149 24.596  1.00 39.72 ? 45  THR B C   1 
ATOM   1221 O  O   . THR B 1 45  ? 61.982 17.244 23.462  1.00 34.36 ? 45  THR B O   1 
ATOM   1222 C  CB  . THR B 1 45  ? 63.408 19.238 25.553  1.00 36.80 ? 45  THR B CB  1 
ATOM   1223 O  OG1 . THR B 1 45  ? 63.224 20.252 26.541  1.00 38.42 ? 45  THR B OG1 1 
ATOM   1224 C  CG2 . THR B 1 45  ? 63.520 19.864 24.167  1.00 35.23 ? 45  THR B CG2 1 
ATOM   1225 N  N   . VAL B 1 46  ? 63.157 16.103 25.003  1.00 39.11 ? 46  VAL B N   1 
ATOM   1226 C  CA  . VAL B 1 46  ? 63.344 14.947 24.148  1.00 45.31 ? 46  VAL B CA  1 
ATOM   1227 C  C   . VAL B 1 46  ? 61.976 14.366 23.864  1.00 39.34 ? 46  VAL B C   1 
ATOM   1228 O  O   . VAL B 1 46  ? 61.631 14.090 22.715  1.00 37.92 ? 46  VAL B O   1 
ATOM   1229 C  CB  . VAL B 1 46  ? 64.251 13.897 24.798  1.00 46.93 ? 46  VAL B CB  1 
ATOM   1230 C  CG1 . VAL B 1 46  ? 64.241 12.594 23.992  1.00 45.89 ? 46  VAL B CG1 1 
ATOM   1231 C  CG2 . VAL B 1 46  ? 65.650 14.452 24.942  1.00 39.14 ? 46  VAL B CG2 1 
ATOM   1232 N  N   . ASP B 1 47  ? 61.207 14.204 24.937  1.00 37.90 ? 47  ASP B N   1 
ATOM   1233 C  CA  . ASP B 1 47  ? 59.818 13.751 24.876  1.00 45.17 ? 47  ASP B CA  1 
ATOM   1234 C  C   . ASP B 1 47  ? 58.911 14.685 24.054  1.00 37.17 ? 47  ASP B C   1 
ATOM   1235 O  O   . ASP B 1 47  ? 58.140 14.211 23.207  1.00 35.97 ? 47  ASP B O   1 
ATOM   1236 C  CB  . ASP B 1 47  ? 59.290 13.548 26.307  1.00 44.63 ? 47  ASP B CB  1 
ATOM   1237 C  CG  . ASP B 1 47  ? 59.998 12.376 27.026  1.00 52.63 ? 47  ASP B CG  1 
ATOM   1238 O  OD1 . ASP B 1 47  ? 60.557 11.494 26.326  1.00 48.82 ? 47  ASP B OD1 1 
ATOM   1239 O  OD2 . ASP B 1 47  ? 60.014 12.336 28.276  1.00 46.23 ? 47  ASP B OD2 1 
ATOM   1240 N  N   . ARG B 1 48  ? 58.999 15.997 24.288  1.00 32.99 ? 48  ARG B N   1 
ATOM   1241 C  CA  . ARG B 1 48  ? 58.154 16.937 23.565  1.00 31.47 ? 48  ARG B CA  1 
ATOM   1242 C  C   . ARG B 1 48  ? 58.473 16.894 22.079  1.00 34.06 ? 48  ARG B C   1 
ATOM   1243 O  O   . ARG B 1 48  ? 57.591 16.998 21.230  1.00 37.54 ? 48  ARG B O   1 
ATOM   1244 C  CB  . ARG B 1 48  ? 58.300 18.356 24.095  1.00 40.76 ? 48  ARG B CB  1 
ATOM   1245 C  CG  . ARG B 1 48  ? 57.361 19.312 23.381  1.00 34.59 ? 48  ARG B CG  1 
ATOM   1246 C  CD  . ARG B 1 48  ? 57.240 20.644 24.072  1.00 38.06 ? 48  ARG B CD  1 
ATOM   1247 N  NE  . ARG B 1 48  ? 56.152 20.599 25.044  1.00 50.56 ? 48  ARG B NE  1 
ATOM   1248 C  CZ  . ARG B 1 48  ? 55.161 21.479 25.122  1.00 39.95 ? 48  ARG B CZ  1 
ATOM   1249 N  NH1 . ARG B 1 48  ? 55.112 22.523 24.306  1.00 37.62 ? 48  ARG B NH1 1 
ATOM   1250 N  NH2 . ARG B 1 48  ? 54.233 21.326 26.049  1.00 49.04 ? 48  ARG B NH2 1 
ATOM   1251 N  N   . LEU B 1 49  ? 59.745 16.737 21.772  1.00 30.33 ? 49  LEU B N   1 
ATOM   1252 C  CA  . LEU B 1 49  ? 60.181 16.633 20.403  1.00 30.73 ? 49  LEU B CA  1 
ATOM   1253 C  C   . LEU B 1 49  ? 59.760 15.305 19.753  1.00 34.63 ? 49  LEU B C   1 
ATOM   1254 O  O   . LEU B 1 49  ? 59.449 15.289 18.556  1.00 40.03 ? 49  LEU B O   1 
ATOM   1255 C  CB  . LEU B 1 49  ? 61.693 16.818 20.343  1.00 34.49 ? 49  LEU B CB  1 
ATOM   1256 C  CG  . LEU B 1 49  ? 62.358 17.014 18.984  1.00 30.34 ? 49  LEU B CG  1 
ATOM   1257 C  CD1 . LEU B 1 49  ? 61.696 18.148 18.285  1.00 29.15 ? 49  LEU B CD1 1 
ATOM   1258 C  CD2 . LEU B 1 49  ? 63.865 17.272 19.145  1.00 31.40 ? 49  LEU B CD2 1 
ATOM   1259 N  N   . HIS B 1 50  ? 59.757 14.199 20.507  1.00 30.04 ? 50  HIS B N   1 
ATOM   1260 C  CA  . HIS B 1 50  ? 59.188 12.937 19.984  1.00 37.61 ? 50  HIS B CA  1 
ATOM   1261 C  C   . HIS B 1 50  ? 57.735 13.144 19.625  1.00 33.45 ? 50  HIS B C   1 
ATOM   1262 O  O   . HIS B 1 50  ? 57.296 12.817 18.517  1.00 28.69 ? 50  HIS B O   1 
ATOM   1263 C  CB  . HIS B 1 50  ? 59.286 11.776 20.987  1.00 33.22 ? 50  HIS B CB  1 
ATOM   1264 C  CG  . HIS B 1 50  ? 60.589 11.051 20.945  1.00 44.33 ? 50  HIS B CG  1 
ATOM   1265 N  ND1 . HIS B 1 50  ? 61.062 10.442 19.805  1.00 54.77 ? 50  HIS B ND1 1 
ATOM   1266 C  CD2 . HIS B 1 50  ? 61.541 10.868 21.893  1.00 47.52 ? 50  HIS B CD2 1 
ATOM   1267 C  CE1 . HIS B 1 50  ? 62.242 9.901  20.056  1.00 52.22 ? 50  HIS B CE1 1 
ATOM   1268 N  NE2 . HIS B 1 50  ? 62.557 10.148 21.314  1.00 47.40 ? 50  HIS B NE2 1 
ATOM   1269 N  N   . PHE B 1 51  ? 57.010 13.703 20.594  1.00 29.96 ? 51  PHE B N   1 
ATOM   1270 C  CA  . PHE B 1 51  ? 55.594 13.972 20.475  1.00 30.27 ? 51  PHE B CA  1 
ATOM   1271 C  C   . PHE B 1 51  ? 55.322 14.791 19.191  1.00 38.26 ? 51  PHE B C   1 
ATOM   1272 O  O   . PHE B 1 51  ? 54.444 14.454 18.375  1.00 26.12 ? 51  PHE B O   1 
ATOM   1273 C  CB  . PHE B 1 51  ? 55.126 14.730 21.722  1.00 30.63 ? 51  PHE B CB  1 
ATOM   1274 C  CG  . PHE B 1 51  ? 53.651 15.030 21.745  1.00 32.28 ? 51  PHE B CG  1 
ATOM   1275 C  CD1 . PHE B 1 51  ? 52.728 14.115 21.253  1.00 34.97 ? 51  PHE B CD1 1 
ATOM   1276 C  CD2 . PHE B 1 51  ? 53.187 16.230 22.254  1.00 30.40 ? 51  PHE B CD2 1 
ATOM   1277 C  CE1 . PHE B 1 51  ? 51.372 14.390 21.269  1.00 30.32 ? 51  PHE B CE1 1 
ATOM   1278 C  CE2 . PHE B 1 51  ? 51.835 16.515 22.280  1.00 33.28 ? 51  PHE B CE2 1 
ATOM   1279 C  CZ  . PHE B 1 51  ? 50.927 15.598 21.780  1.00 41.26 ? 51  PHE B CZ  1 
ATOM   1280 N  N   . ILE B 1 52  ? 56.112 15.843 18.996  1.00 27.03 ? 52  ILE B N   1 
ATOM   1281 C  CA  . ILE B 1 52  ? 55.906 16.728 17.868  1.00 32.66 ? 52  ILE B CA  1 
ATOM   1282 C  C   . ILE B 1 52  ? 56.202 16.010 16.553  1.00 28.45 ? 52  ILE B C   1 
ATOM   1283 O  O   . ILE B 1 52  ? 55.413 16.066 15.596  1.00 26.10 ? 52  ILE B O   1 
ATOM   1284 C  CB  . ILE B 1 52  ? 56.777 17.981 18.008  1.00 26.84 ? 52  ILE B CB  1 
ATOM   1285 C  CG1 . ILE B 1 52  ? 56.220 18.873 19.117  1.00 27.86 ? 52  ILE B CG1 1 
ATOM   1286 C  CG2 . ILE B 1 52  ? 56.822 18.743 16.711  1.00 25.73 ? 52  ILE B CG2 1 
ATOM   1287 C  CD1 . ILE B 1 52  ? 57.193 19.896 19.592  1.00 40.32 ? 52  ILE B CD1 1 
ATOM   1288 N  N   . LYS B 1 53  ? 57.339 15.326 16.516  1.00 36.37 ? 53  LYS B N   1 
ATOM   1289 C  CA  . LYS B 1 53  ? 57.710 14.569 15.337  1.00 40.64 ? 53  LYS B CA  1 
ATOM   1290 C  C   . LYS B 1 53  ? 56.570 13.605 14.949  1.00 29.07 ? 53  LYS B C   1 
ATOM   1291 O  O   . LYS B 1 53  ? 56.142 13.552 13.785  1.00 29.94 ? 53  LYS B O   1 
ATOM   1292 C  CB  . LYS B 1 53  ? 59.037 13.824 15.584  1.00 36.07 ? 53  LYS B CB  1 
ATOM   1293 C  CG  . LYS B 1 53  ? 59.513 12.936 14.434  1.00 34.47 ? 53  LYS B CG  1 
ATOM   1294 C  CD  . LYS B 1 53  ? 59.817 13.769 13.211  1.00 52.34 ? 53  LYS B CD  1 
ATOM   1295 C  CE  . LYS B 1 53  ? 60.290 12.933 12.041  1.00 50.23 ? 53  LYS B CE  1 
ATOM   1296 N  NZ  . LYS B 1 53  ? 59.938 13.623 10.762  1.00 47.97 ? 53  LYS B NZ  1 
ATOM   1297 N  N   . ARG B 1 54  ? 56.042 12.870 15.921  1.00 28.31 ? 54  ARG B N   1 
ATOM   1298 C  CA  . ARG B 1 54  ? 55.074 11.843 15.570  1.00 34.57 ? 54  ARG B CA  1 
ATOM   1299 C  C   . ARG B 1 54  ? 53.745 12.443 15.183  1.00 27.82 ? 54  ARG B C   1 
ATOM   1300 O  O   . ARG B 1 54  ? 53.069 11.909 14.309  1.00 43.28 ? 54  ARG B O   1 
ATOM   1301 C  CB  . ARG B 1 54  ? 54.895 10.823 16.695  1.00 29.62 ? 54  ARG B CB  1 
ATOM   1302 C  CG  . ARG B 1 54  ? 56.165 10.038 16.849  1.00 35.13 ? 54  ARG B CG  1 
ATOM   1303 C  CD  . ARG B 1 54  ? 56.152 9.070  17.982  1.00 48.51 ? 54  ARG B CD  1 
ATOM   1304 N  NE  . ARG B 1 54  ? 57.527 8.807  18.385  1.00 60.24 ? 54  ARG B NE  1 
ATOM   1305 C  CZ  . ARG B 1 54  ? 57.928 7.766  19.107  1.00 57.24 ? 54  ARG B CZ  1 
ATOM   1306 N  NH1 . ARG B 1 54  ? 57.074 6.803  19.461  1.00 50.16 ? 54  ARG B NH1 1 
ATOM   1307 N  NH2 . ARG B 1 54  ? 59.207 7.662  19.420  1.00 50.33 ? 54  ARG B NH2 1 
ATOM   1308 N  N   . MET B 1 55  ? 53.371 13.551 15.814  1.00 24.76 ? 55  MET B N   1 
ATOM   1309 C  CA  . MET B 1 55  ? 52.150 14.234 15.422  1.00 23.97 ? 55  MET B CA  1 
ATOM   1310 C  C   . MET B 1 55  ? 52.276 14.641 13.975  1.00 24.04 ? 55  MET B C   1 
ATOM   1311 O  O   . MET B 1 55  ? 51.317 14.512 13.209  1.00 24.16 ? 55  MET B O   1 
ATOM   1312 C  CB  . MET B 1 55  ? 51.856 15.448 16.314  1.00 23.09 ? 55  MET B CB  1 
ATOM   1313 C  CG  . MET B 1 55  ? 51.145 15.099 17.625  1.00 23.06 ? 55  MET B CG  1 
ATOM   1314 S  SD  . MET B 1 55  ? 50.325 16.502 18.418  1.00 46.49 ? 55  MET B SD  1 
ATOM   1315 C  CE  . MET B 1 55  ? 51.713 17.537 18.867  1.00 22.28 ? 55  MET B CE  1 
ATOM   1316 N  N   . GLN B 1 56  ? 53.467 15.099 13.578  1.00 26.72 ? 56  GLN B N   1 
ATOM   1317 C  CA  . GLN B 1 56  ? 53.641 15.438 12.170  1.00 32.76 ? 56  GLN B CA  1 
ATOM   1318 C  C   . GLN B 1 56  ? 53.575 14.224 11.277  1.00 28.16 ? 56  GLN B C   1 
ATOM   1319 O  O   . GLN B 1 56  ? 53.087 14.317 10.164  1.00 36.83 ? 56  GLN B O   1 
ATOM   1320 C  CB  . GLN B 1 56  ? 54.947 16.140 11.942  1.00 27.11 ? 56  GLN B CB  1 
ATOM   1321 C  CG  . GLN B 1 56  ? 54.863 17.613 12.141  1.00 30.27 ? 56  GLN B CG  1 
ATOM   1322 C  CD  . GLN B 1 56  ? 56.241 18.221 12.147  1.00 35.81 ? 56  GLN B CD  1 
ATOM   1323 O  OE1 . GLN B 1 56  ? 57.020 17.993 13.088  1.00 26.64 ? 56  GLN B OE1 1 
ATOM   1324 N  NE2 . GLN B 1 56  ? 56.572 18.972 11.098  1.00 36.40 ? 56  GLN B NE2 1 
ATOM   1325 N  N   . GLU B 1 57  ? 54.033 13.078 11.751  1.00 28.84 ? 57  GLU B N   1 
ATOM   1326 C  CA  . GLU B 1 57  ? 53.913 11.871 10.929  1.00 30.17 ? 57  GLU B CA  1 
ATOM   1327 C  C   . GLU B 1 57  ? 52.453 11.438 10.887  1.00 30.29 ? 57  GLU B C   1 
ATOM   1328 O  O   . GLU B 1 57  ? 52.043 10.659 10.041  1.00 32.49 ? 57  GLU B O   1 
ATOM   1329 C  CB  . GLU B 1 57  ? 54.829 10.767 11.460  1.00 32.07 ? 57  GLU B CB  1 
ATOM   1330 C  CG  . GLU B 1 57  ? 56.315 11.180 11.387  1.00 39.51 ? 57  GLU B CG  1 
ATOM   1331 C  CD  . GLU B 1 57  ? 57.269 10.243 12.118  1.00 41.57 ? 57  GLU B CD  1 
ATOM   1332 O  OE1 . GLU B 1 57  ? 56.831 9.567  13.067  1.00 42.91 ? 57  GLU B OE1 1 
ATOM   1333 O  OE2 . GLU B 1 57  ? 58.471 10.205 11.764  1.00 44.12 ? 57  GLU B OE2 1 
ATOM   1334 N  N   . LEU B 1 58  ? 51.654 11.974 11.799  1.00 27.46 ? 58  LEU B N   1 
ATOM   1335 C  CA  . LEU B 1 58  ? 50.233 11.652 11.830  1.00 27.51 ? 58  LEU B CA  1 
ATOM   1336 C  C   . LEU B 1 58  ? 49.406 12.680 11.074  1.00 35.11 ? 58  LEU B C   1 
ATOM   1337 O  O   . LEU B 1 58  ? 48.177 12.610 11.091  1.00 27.01 ? 58  LEU B O   1 
ATOM   1338 C  CB  . LEU B 1 58  ? 49.733 11.559 13.271  1.00 26.84 ? 58  LEU B CB  1 
ATOM   1339 C  CG  . LEU B 1 58  ? 50.279 10.370 14.062  1.00 29.31 ? 58  LEU B CG  1 
ATOM   1340 C  CD1 . LEU B 1 58  ? 49.842 10.432 15.502  1.00 27.22 ? 58  LEU B CD1 1 
ATOM   1341 C  CD2 . LEU B 1 58  ? 49.865 9.065  13.436  1.00 29.22 ? 58  LEU B CD2 1 
ATOM   1342 N  N   . GLY B 1 59  ? 50.065 13.653 10.449  1.00 26.30 ? 59  GLY B N   1 
ATOM   1343 C  CA  . GLY B 1 59  ? 49.362 14.589 9.601   1.00 26.28 ? 59  GLY B CA  1 
ATOM   1344 C  C   . GLY B 1 59  ? 48.918 15.885 10.233  1.00 25.09 ? 59  GLY B C   1 
ATOM   1345 O  O   . GLY B 1 59  ? 48.166 16.635 9.614   1.00 25.41 ? 59  GLY B O   1 
ATOM   1346 N  N   . PHE B 1 60  ? 49.329 16.152 11.471  1.00 27.66 ? 60  PHE B N   1 
ATOM   1347 C  CA  . PHE B 1 60  ? 49.129 17.489 12.043  1.00 25.79 ? 60  PHE B CA  1 
ATOM   1348 C  C   . PHE B 1 60  ? 50.160 18.444 11.438  1.00 23.98 ? 60  PHE B C   1 
ATOM   1349 O  O   . PHE B 1 60  ? 51.349 18.122 11.409  1.00 24.22 ? 60  PHE B O   1 
ATOM   1350 C  CB  . PHE B 1 60  ? 49.311 17.511 13.558  1.00 23.15 ? 60  PHE B CB  1 
ATOM   1351 C  CG  . PHE B 1 60  ? 48.309 16.737 14.345  1.00 23.03 ? 60  PHE B CG  1 
ATOM   1352 C  CD1 . PHE B 1 60  ? 47.343 17.394 15.081  1.00 33.29 ? 60  PHE B CD1 1 
ATOM   1353 C  CD2 . PHE B 1 60  ? 48.404 15.364 14.456  1.00 23.65 ? 60  PHE B CD2 1 
ATOM   1354 C  CE1 . PHE B 1 60  ? 46.451 16.679 15.878  1.00 22.39 ? 60  PHE B CE1 1 
ATOM   1355 C  CE2 . PHE B 1 60  ? 47.518 14.653 15.227  1.00 23.70 ? 60  PHE B CE2 1 
ATOM   1356 C  CZ  . PHE B 1 60  ? 46.549 15.314 15.951  1.00 23.02 ? 60  PHE B CZ  1 
ATOM   1357 N  N   . THR B 1 61  ? 49.724 19.623 11.004  1.00 25.08 ? 61  THR B N   1 
ATOM   1358 C  CA  . THR B 1 61  ? 50.646 20.666 10.529  1.00 25.99 ? 61  THR B CA  1 
ATOM   1359 C  C   . THR B 1 61  ? 51.317 21.293 11.713  1.00 34.86 ? 61  THR B C   1 
ATOM   1360 O  O   . THR B 1 61  ? 50.825 21.145 12.836  1.00 26.15 ? 61  THR B O   1 
ATOM   1361 C  CB  . THR B 1 61  ? 49.951 21.790 9.793   1.00 25.78 ? 61  THR B CB  1 
ATOM   1362 O  OG1 . THR B 1 61  ? 49.238 22.569 10.767  1.00 25.80 ? 61  THR B OG1 1 
ATOM   1363 C  CG2 . THR B 1 61  ? 49.001 21.258 8.728   1.00 26.62 ? 61  THR B CG2 1 
ATOM   1364 N  N   . LEU B 1 62  ? 52.432 21.985 11.478  1.00 26.51 ? 62  LEU B N   1 
ATOM   1365 C  CA  . LEU B 1 62  ? 53.131 22.676 12.556  1.00 25.14 ? 62  LEU B CA  1 
ATOM   1366 C  C   . LEU B 1 62  ? 52.203 23.668 13.273  1.00 30.34 ? 62  LEU B C   1 
ATOM   1367 O  O   . LEU B 1 62  ? 52.211 23.795 14.491  1.00 30.31 ? 62  LEU B O   1 
ATOM   1368 C  CB  . LEU B 1 62  ? 54.349 23.426 12.027  1.00 25.70 ? 62  LEU B CB  1 
ATOM   1369 C  CG  . LEU B 1 62  ? 55.701 22.719 12.098  1.00 37.68 ? 62  LEU B CG  1 
ATOM   1370 C  CD1 . LEU B 1 62  ? 56.781 23.659 11.569  1.00 38.41 ? 62  LEU B CD1 1 
ATOM   1371 C  CD2 . LEU B 1 62  ? 56.058 22.181 13.505  1.00 29.70 ? 62  LEU B CD2 1 
ATOM   1372 N  N   . ASN B 1 63  ? 51.378 24.347 12.495  1.00 27.47 ? 63  ASN B N   1 
ATOM   1373 C  CA  . ASN B 1 63  ? 50.436 25.300 13.031  1.00 27.36 ? 63  ASN B CA  1 
ATOM   1374 C  C   . ASN B 1 63  ? 49.437 24.680 13.983  1.00 28.33 ? 63  ASN B C   1 
ATOM   1375 O  O   . ASN B 1 63  ? 49.244 25.169 15.102  1.00 35.14 ? 63  ASN B O   1 
ATOM   1376 C  CB  . ASN B 1 63  ? 49.704 25.971 11.884  1.00 39.91 ? 63  ASN B CB  1 
ATOM   1377 C  CG  . ASN B 1 63  ? 49.015 27.216 12.310  1.00 41.90 ? 63  ASN B CG  1 
ATOM   1378 O  OD1 . ASN B 1 63  ? 47.786 27.278 12.318  1.00 37.77 ? 63  ASN B OD1 1 
ATOM   1379 N  ND2 . ASN B 1 63  ? 49.794 28.221 12.695  1.00 41.41 ? 63  ASN B ND2 1 
ATOM   1380 N  N   . GLU B 1 64  ? 48.819 23.589 13.539  1.00 25.64 ? 64  GLU B N   1 
ATOM   1381 C  CA  . GLU B 1 64  ? 47.928 22.804 14.383  1.00 24.69 ? 64  GLU B CA  1 
ATOM   1382 C  C   . GLU B 1 64  ? 48.625 22.353 15.661  1.00 24.37 ? 64  GLU B C   1 
ATOM   1383 O  O   . GLU B 1 64  ? 48.057 22.390 16.757  1.00 24.11 ? 64  GLU B O   1 
ATOM   1384 C  CB  . GLU B 1 64  ? 47.405 21.600 13.616  1.00 26.59 ? 64  GLU B CB  1 
ATOM   1385 C  CG  . GLU B 1 64  ? 46.605 22.024 12.419  1.00 41.23 ? 64  GLU B CG  1 
ATOM   1386 C  CD  . GLU B 1 64  ? 45.991 20.882 11.634  1.00 35.27 ? 64  GLU B CD  1 
ATOM   1387 O  OE1 . GLU B 1 64  ? 46.584 19.776 11.575  1.00 28.49 ? 64  GLU B OE1 1 
ATOM   1388 O  OE2 . GLU B 1 64  ? 44.918 21.138 11.045  1.00 33.23 ? 64  GLU B OE2 1 
ATOM   1389 N  N   . ILE B 1 65  ? 49.866 21.921 15.517  1.00 23.17 ? 65  ILE B N   1 
ATOM   1390 C  CA  . ILE B 1 65  ? 50.625 21.446 16.657  1.00 23.19 ? 65  ILE B CA  1 
ATOM   1391 C  C   . ILE B 1 65  ? 50.871 22.578 17.648  1.00 26.73 ? 65  ILE B C   1 
ATOM   1392 O  O   . ILE B 1 65  ? 50.817 22.376 18.863  1.00 34.81 ? 65  ILE B O   1 
ATOM   1393 C  CB  . ILE B 1 65  ? 51.935 20.817 16.177  1.00 28.92 ? 65  ILE B CB  1 
ATOM   1394 C  CG1 . ILE B 1 65  ? 51.625 19.473 15.478  1.00 27.60 ? 65  ILE B CG1 1 
ATOM   1395 C  CG2 . ILE B 1 65  ? 52.906 20.651 17.320  1.00 23.90 ? 65  ILE B CG2 1 
ATOM   1396 C  CD1 . ILE B 1 65  ? 52.809 18.811 14.847  1.00 24.30 ? 65  ILE B CD1 1 
ATOM   1397 N  N   . ASP B 1 66  ? 51.085 23.776 17.116  1.00 31.89 ? 66  ASP B N   1 
ATOM   1398 C  CA  . ASP B 1 66  ? 51.251 25.002 17.899  1.00 36.84 ? 66  ASP B CA  1 
ATOM   1399 C  C   . ASP B 1 66  ? 50.018 25.276 18.770  1.00 33.61 ? 66  ASP B C   1 
ATOM   1400 O  O   . ASP B 1 66  ? 50.118 25.519 20.000  1.00 28.26 ? 66  ASP B O   1 
ATOM   1401 C  CB  . ASP B 1 66  ? 51.486 26.177 16.950  1.00 27.50 ? 66  ASP B CB  1 
ATOM   1402 C  CG  . ASP B 1 66  ? 52.034 27.403 17.640  1.00 37.97 ? 66  ASP B CG  1 
ATOM   1403 O  OD1 . ASP B 1 66  ? 51.756 27.612 18.834  1.00 52.41 ? 66  ASP B OD1 1 
ATOM   1404 O  OD2 . ASP B 1 66  ? 52.721 28.188 16.959  1.00 56.24 ? 66  ASP B OD2 1 
ATOM   1405 N  N   . LYS B 1 67  ? 48.858 25.277 18.111  1.00 29.50 ? 67  LYS B N   1 
ATOM   1406 C  CA  . LYS B 1 67  ? 47.607 25.512 18.813  1.00 30.84 ? 67  LYS B CA  1 
ATOM   1407 C  C   . LYS B 1 67  ? 47.400 24.452 19.895  1.00 28.64 ? 67  LYS B C   1 
ATOM   1408 O  O   . LYS B 1 67  ? 47.284 24.774 21.092  1.00 30.07 ? 67  LYS B O   1 
ATOM   1409 C  CB  . LYS B 1 67  ? 46.441 25.523 17.821  1.00 35.53 ? 67  LYS B CB  1 
ATOM   1410 N  N   . LEU B 1 68  ? 47.424 23.194 19.463  1.00 23.77 ? 68  LEU B N   1 
ATOM   1411 C  CA  . LEU B 1 68  ? 47.197 22.045 20.324  1.00 27.78 ? 68  LEU B CA  1 
ATOM   1412 C  C   . LEU B 1 68  ? 48.055 22.137 21.566  1.00 40.59 ? 68  LEU B C   1 
ATOM   1413 O  O   . LEU B 1 68  ? 47.557 21.983 22.676  1.00 29.04 ? 68  LEU B O   1 
ATOM   1414 C  CB  . LEU B 1 68  ? 47.491 20.747 19.558  1.00 23.74 ? 68  LEU B CB  1 
ATOM   1415 C  CG  . LEU B 1 68  ? 47.492 19.365 20.230  1.00 29.50 ? 68  LEU B CG  1 
ATOM   1416 C  CD1 . LEU B 1 68  ? 47.314 18.241 19.200  1.00 24.04 ? 68  LEU B CD1 1 
ATOM   1417 C  CD2 . LEU B 1 68  ? 48.784 19.107 21.010  1.00 24.60 ? 68  LEU B CD2 1 
ATOM   1418 N  N   . LEU B 1 69  ? 49.343 22.394 21.375  1.00 24.74 ? 69  LEU B N   1 
ATOM   1419 C  CA  . LEU B 1 69  ? 50.249 22.473 22.497  1.00 26.66 ? 69  LEU B CA  1 
ATOM   1420 C  C   . LEU B 1 69  ? 49.888 23.620 23.442  1.00 38.69 ? 69  LEU B C   1 
ATOM   1421 O  O   . LEU B 1 69  ? 49.997 23.472 24.658  1.00 39.29 ? 69  LEU B O   1 
ATOM   1422 C  CB  . LEU B 1 69  ? 51.693 22.611 22.014  1.00 33.81 ? 69  LEU B CB  1 
ATOM   1423 C  CG  . LEU B 1 69  ? 52.414 21.330 21.585  1.00 33.05 ? 69  LEU B CG  1 
ATOM   1424 C  CD1 . LEU B 1 69  ? 53.831 21.655 21.118  1.00 26.42 ? 69  LEU B CD1 1 
ATOM   1425 C  CD2 . LEU B 1 69  ? 52.436 20.330 22.743  1.00 26.68 ? 69  LEU B CD2 1 
ATOM   1426 N  N   . GLY B 1 70  ? 49.431 24.746 22.895  1.00 34.22 ? 70  GLY B N   1 
ATOM   1427 C  CA  . GLY B 1 70  ? 48.991 25.835 23.753  1.00 28.52 ? 70  GLY B CA  1 
ATOM   1428 C  C   . GLY B 1 70  ? 47.848 25.433 24.663  1.00 33.54 ? 70  GLY B C   1 
ATOM   1429 O  O   . GLY B 1 70  ? 47.862 25.678 25.889  1.00 45.64 ? 70  GLY B O   1 
ATOM   1430 N  N   . VAL B 1 71  ? 46.849 24.807 24.050  1.00 28.76 ? 71  VAL B N   1 
ATOM   1431 C  CA  . VAL B 1 71  ? 45.667 24.336 24.762  1.00 33.80 ? 71  VAL B CA  1 
ATOM   1432 C  C   . VAL B 1 71  ? 46.006 23.276 25.817  1.00 37.75 ? 71  VAL B C   1 
ATOM   1433 O  O   . VAL B 1 71  ? 45.683 23.439 26.999  1.00 37.23 ? 71  VAL B O   1 
ATOM   1434 C  CB  . VAL B 1 71  ? 44.616 23.793 23.765  1.00 40.84 ? 71  VAL B CB  1 
ATOM   1435 C  CG1 . VAL B 1 71  ? 43.421 23.225 24.482  1.00 24.82 ? 71  VAL B CG1 1 
ATOM   1436 C  CG2 . VAL B 1 71  ? 44.173 24.913 22.841  1.00 28.55 ? 71  VAL B CG2 1 
ATOM   1437 N  N   . VAL B 1 72  ? 46.675 22.201 25.415  1.00 42.11 ? 72  VAL B N   1 
ATOM   1438 C  CA  . VAL B 1 72  ? 46.968 21.142 26.372  1.00 37.75 ? 72  VAL B CA  1 
ATOM   1439 C  C   . VAL B 1 72  ? 47.822 21.689 27.511  1.00 39.27 ? 72  VAL B C   1 
ATOM   1440 O  O   . VAL B 1 72  ? 47.542 21.433 28.680  1.00 43.49 ? 72  VAL B O   1 
ATOM   1441 C  CB  . VAL B 1 72  ? 47.708 19.937 25.733  1.00 23.89 ? 72  VAL B CB  1 
ATOM   1442 C  CG1 . VAL B 1 72  ? 47.987 18.873 26.790  1.00 25.11 ? 72  VAL B CG1 1 
ATOM   1443 C  CG2 . VAL B 1 72  ? 46.904 19.349 24.577  1.00 27.14 ? 72  VAL B CG2 1 
ATOM   1444 N  N   . ASP B 1 73  ? 48.830 22.489 27.183  1.00 31.97 ? 73  ASP B N   1 
ATOM   1445 C  CA  . ASP B 1 73  ? 49.676 23.067 28.229  1.00 37.28 ? 73  ASP B CA  1 
ATOM   1446 C  C   . ASP B 1 73  ? 48.890 23.942 29.201  1.00 41.72 ? 73  ASP B C   1 
ATOM   1447 O  O   . ASP B 1 73  ? 49.202 23.976 30.386  1.00 44.07 ? 73  ASP B O   1 
ATOM   1448 C  CB  . ASP B 1 73  ? 50.816 23.889 27.623  1.00 41.28 ? 73  ASP B CB  1 
ATOM   1449 C  CG  . ASP B 1 73  ? 51.874 23.017 26.937  1.00 56.52 ? 73  ASP B CG  1 
ATOM   1450 O  OD1 . ASP B 1 73  ? 51.894 21.786 27.191  1.00 56.36 ? 73  ASP B OD1 1 
ATOM   1451 O  OD2 . ASP B 1 73  ? 52.673 23.562 26.124  1.00 48.25 ? 73  ASP B OD2 1 
ATOM   1452 N  N   . ARG B 1 74  ? 47.868 24.655 28.738  1.00 45.19 ? 74  ARG B N   1 
ATOM   1453 C  CA  . ARG B 1 74  ? 47.206 25.528 29.704  1.00 41.39 ? 74  ARG B CA  1 
ATOM   1454 C  C   . ARG B 1 74  ? 45.953 24.970 30.408  1.00 41.08 ? 74  ARG B C   1 
ATOM   1455 O  O   . ARG B 1 74  ? 45.409 25.630 31.281  1.00 42.46 ? 74  ARG B O   1 
ATOM   1456 C  CB  . ARG B 1 74  ? 46.878 26.847 29.011  1.00 44.35 ? 74  ARG B CB  1 
ATOM   1457 C  CG  . ARG B 1 74  ? 48.161 27.561 28.596  1.00 54.23 ? 74  ARG B CG  1 
ATOM   1458 C  CD  . ARG B 1 74  ? 47.956 28.929 27.983  1.00 49.90 ? 74  ARG B CD  1 
ATOM   1459 N  NE  . ARG B 1 74  ? 49.021 29.178 27.012  1.00 56.99 ? 74  ARG B NE  1 
ATOM   1460 C  CZ  . ARG B 1 74  ? 48.995 30.136 26.086  1.00 59.89 ? 74  ARG B CZ  1 
ATOM   1461 N  NH1 . ARG B 1 74  ? 47.961 30.966 26.000  1.00 65.69 ? 74  ARG B NH1 1 
ATOM   1462 N  NH2 . ARG B 1 74  ? 50.015 30.273 25.245  1.00 67.43 ? 74  ARG B NH2 1 
ATOM   1463 N  N   . ASP B 1 75  ? 45.563 23.727 30.143  1.00 34.70 ? 75  ASP B N   1 
ATOM   1464 C  CA  . ASP B 1 75  ? 44.263 23.247 30.612  1.00 39.77 ? 75  ASP B CA  1 
ATOM   1465 C  C   . ASP B 1 75  ? 44.333 22.194 31.700  1.00 35.52 ? 75  ASP B C   1 
ATOM   1466 O  O   . ASP B 1 75  ? 45.335 21.499 31.846  1.00 33.96 ? 75  ASP B O   1 
ATOM   1467 C  CB  . ASP B 1 75  ? 43.430 22.667 29.455  1.00 48.87 ? 75  ASP B CB  1 
ATOM   1468 C  CG  . ASP B 1 75  ? 42.638 23.736 28.676  1.00 42.03 ? 75  ASP B CG  1 
ATOM   1469 O  OD1 . ASP B 1 75  ? 42.629 24.916 29.095  1.00 49.88 ? 75  ASP B OD1 1 
ATOM   1470 O  OD2 . ASP B 1 75  ? 42.007 23.389 27.653  1.00 35.36 ? 75  ASP B OD2 1 
ATOM   1471 N  N   . GLU B 1 76  ? 43.256 22.097 32.474  1.00 33.91 ? 76  GLU B N   1 
ATOM   1472 C  CA  . GLU B 1 76  ? 43.157 21.051 33.469  1.00 45.69 ? 76  GLU B CA  1 
ATOM   1473 C  C   . GLU B 1 76  ? 42.900 19.693 32.812  1.00 35.76 ? 76  GLU B C   1 
ATOM   1474 O  O   . GLU B 1 76  ? 43.571 18.712 33.122  1.00 33.33 ? 76  GLU B O   1 
ATOM   1475 C  CB  . GLU B 1 76  ? 42.063 21.382 34.497  1.00 45.00 ? 76  GLU B CB  1 
ATOM   1476 C  CG  . GLU B 1 76  ? 41.779 20.277 35.517  1.00 45.32 ? 76  GLU B CG  1 
ATOM   1477 C  CD  . GLU B 1 76  ? 40.818 20.724 36.614  1.00 62.06 ? 76  GLU B CD  1 
ATOM   1478 O  OE1 . GLU B 1 76  ? 39.779 20.053 36.812  1.00 60.41 ? 76  GLU B OE1 1 
ATOM   1479 O  OE2 . GLU B 1 76  ? 41.111 21.740 37.291  1.00 60.45 ? 76  GLU B OE2 1 
ATOM   1480 N  N   . ALA B 1 77  ? 41.953 19.608 31.892  1.00 41.21 ? 77  ALA B N   1 
ATOM   1481 C  CA  . ALA B 1 77  ? 41.721 18.285 31.348  1.00 39.61 ? 77  ALA B CA  1 
ATOM   1482 C  C   . ALA B 1 77  ? 42.547 18.129 30.091  1.00 36.12 ? 77  ALA B C   1 
ATOM   1483 O  O   . ALA B 1 77  ? 42.093 18.426 28.987  1.00 29.48 ? 77  ALA B O   1 
ATOM   1484 C  CB  . ALA B 1 77  ? 40.249 18.089 31.052  1.00 31.31 ? 77  ALA B CB  1 
ATOM   1485 N  N   . LYS B 1 78  ? 43.725 17.541 30.254  1.00 43.38 ? 78  LYS B N   1 
ATOM   1486 C  CA  . LYS B 1 78  ? 44.653 17.456 29.138  1.00 42.06 ? 78  LYS B CA  1 
ATOM   1487 C  C   . LYS B 1 78  ? 44.265 16.264 28.282  1.00 36.82 ? 78  LYS B C   1 
ATOM   1488 O  O   . LYS B 1 78  ? 44.278 16.326 27.062  1.00 27.32 ? 78  LYS B O   1 
ATOM   1489 C  CB  . LYS B 1 78  ? 46.095 17.361 29.625  1.00 29.15 ? 78  LYS B CB  1 
ATOM   1490 C  CG  . LYS B 1 78  ? 46.502 18.503 30.500  1.00 27.47 ? 78  LYS B CG  1 
ATOM   1491 C  CD  . LYS B 1 78  ? 48.003 18.469 30.760  1.00 28.71 ? 78  LYS B CD  1 
ATOM   1492 C  CE  . LYS B 1 78  ? 48.420 19.569 31.747  1.00 40.46 ? 78  LYS B CE  1 
ATOM   1493 N  NZ  . LYS B 1 78  ? 47.930 20.915 31.321  1.00 28.16 ? 78  LYS B NZ  1 
ATOM   1494 N  N   . CYS B 1 79  ? 43.906 15.175 28.944  1.00 31.85 ? 79  CYS B N   1 
ATOM   1495 C  CA  . CYS B 1 79  ? 43.446 14.001 28.251  1.00 30.38 ? 79  CYS B CA  1 
ATOM   1496 C  C   . CYS B 1 79  ? 42.235 14.328 27.354  1.00 31.27 ? 79  CYS B C   1 
ATOM   1497 O  O   . CYS B 1 79  ? 42.198 13.940 26.184  1.00 30.86 ? 79  CYS B O   1 
ATOM   1498 C  CB  . CYS B 1 79  ? 43.114 12.918 29.269  1.00 30.29 ? 79  CYS B CB  1 
ATOM   1499 S  SG  . CYS B 1 79  ? 42.369 11.459 28.567  1.00 31.25 ? 79  CYS B SG  1 
ATOM   1500 N  N   . ARG B 1 80  ? 41.271 15.079 27.880  1.00 28.60 ? 80  ARG B N   1 
ATOM   1501 C  CA  . ARG B 1 80  ? 40.098 15.435 27.085  1.00 35.43 ? 80  ARG B CA  1 
ATOM   1502 C  C   . ARG B 1 80  ? 40.488 16.274 25.849  1.00 28.79 ? 80  ARG B C   1 
ATOM   1503 O  O   . ARG B 1 80  ? 39.984 16.038 24.736  1.00 28.91 ? 80  ARG B O   1 
ATOM   1504 C  CB  . ARG B 1 80  ? 39.075 16.197 27.947  1.00 34.46 ? 80  ARG B CB  1 
ATOM   1505 C  CG  . ARG B 1 80  ? 37.825 16.637 27.198  1.00 33.53 ? 80  ARG B CG  1 
ATOM   1506 C  CD  . ARG B 1 80  ? 37.089 17.719 27.969  1.00 35.50 ? 80  ARG B CD  1 
ATOM   1507 N  NE  . ARG B 1 80  ? 37.900 18.934 27.989  1.00 56.32 ? 80  ARG B NE  1 
ATOM   1508 C  CZ  . ARG B 1 80  ? 37.691 19.974 28.794  1.00 49.30 ? 80  ARG B CZ  1 
ATOM   1509 N  NH1 . ARG B 1 80  ? 36.683 19.946 29.662  1.00 38.20 ? 80  ARG B NH1 1 
ATOM   1510 N  NH2 . ARG B 1 80  ? 38.502 21.038 28.734  1.00 38.60 ? 80  ARG B NH2 1 
ATOM   1511 N  N   . ASP B 1 81  ? 41.375 17.251 26.061  1.00 27.64 ? 81  ASP B N   1 
ATOM   1512 C  CA  . ASP B 1 81  ? 41.824 18.127 24.992  1.00 26.98 ? 81  ASP B CA  1 
ATOM   1513 C  C   . ASP B 1 81  ? 42.420 17.311 23.883  1.00 25.56 ? 81  ASP B C   1 
ATOM   1514 O  O   . ASP B 1 81  ? 42.047 17.421 22.715  1.00 25.58 ? 81  ASP B O   1 
ATOM   1515 C  CB  . ASP B 1 81  ? 42.875 19.125 25.488  1.00 28.20 ? 81  ASP B CB  1 
ATOM   1516 C  CG  . ASP B 1 81  ? 42.288 20.246 26.332  1.00 35.67 ? 81  ASP B CG  1 
ATOM   1517 O  OD1 . ASP B 1 81  ? 41.064 20.500 26.282  1.00 29.75 ? 81  ASP B OD1 1 
ATOM   1518 O  OD2 . ASP B 1 81  ? 43.075 20.886 27.059  1.00 37.85 ? 81  ASP B OD2 1 
ATOM   1519 N  N   . MET B 1 82  ? 43.358 16.474 24.268  1.00 24.19 ? 82  MET B N   1 
ATOM   1520 C  CA  . MET B 1 82  ? 44.092 15.702 23.303  1.00 23.00 ? 82  MET B CA  1 
ATOM   1521 C  C   . MET B 1 82  ? 43.171 14.740 22.541  1.00 26.47 ? 82  MET B C   1 
ATOM   1522 O  O   . MET B 1 82  ? 43.309 14.557 21.328  1.00 22.92 ? 82  MET B O   1 
ATOM   1523 C  CB  . MET B 1 82  ? 45.218 14.956 23.999  1.00 22.20 ? 82  MET B CB  1 
ATOM   1524 C  CG  . MET B 1 82  ? 46.227 14.463 23.010  1.00 24.04 ? 82  MET B CG  1 
ATOM   1525 S  SD  . MET B 1 82  ? 46.877 15.799 22.017  1.00 50.42 ? 82  MET B SD  1 
ATOM   1526 C  CE  . MET B 1 82  ? 47.501 14.842 20.644  1.00 24.40 ? 82  MET B CE  1 
ATOM   1527 N  N   . TYR B 1 83  ? 42.208 14.172 23.261  1.00 24.39 ? 83  TYR B N   1 
ATOM   1528 C  CA  . TYR B 1 83  ? 41.193 13.306 22.681  1.00 25.38 ? 83  TYR B CA  1 
ATOM   1529 C  C   . TYR B 1 83  ? 40.417 14.008 21.574  1.00 25.83 ? 83  TYR B C   1 
ATOM   1530 O  O   . TYR B 1 83  ? 40.251 13.477 20.446  1.00 25.62 ? 83  TYR B O   1 
ATOM   1531 C  CB  . TYR B 1 83  ? 40.271 12.828 23.803  1.00 27.12 ? 83  TYR B CB  1 
ATOM   1532 C  CG  . TYR B 1 83  ? 39.126 11.920 23.410  1.00 28.74 ? 83  TYR B CG  1 
ATOM   1533 C  CD1 . TYR B 1 83  ? 39.340 10.577 23.118  1.00 28.79 ? 83  TYR B CD1 1 
ATOM   1534 C  CD2 . TYR B 1 83  ? 37.808 12.387 23.431  1.00 30.63 ? 83  TYR B CD2 1 
ATOM   1535 C  CE1 . TYR B 1 83  ? 38.280 9.746  22.795  1.00 30.61 ? 83  TYR B CE1 1 
ATOM   1536 C  CE2 . TYR B 1 83  ? 36.745 11.561 23.118  1.00 32.46 ? 83  TYR B CE2 1 
ATOM   1537 C  CZ  . TYR B 1 83  ? 36.980 10.238 22.809  1.00 32.45 ? 83  TYR B CZ  1 
ATOM   1538 O  OH  . TYR B 1 83  ? 35.915 9.405  22.509  1.00 34.58 ? 83  TYR B OH  1 
ATOM   1539 N  N   . ASP B 1 84  ? 39.925 15.195 21.921  1.00 26.65 ? 84  ASP B N   1 
ATOM   1540 C  CA  . ASP B 1 84  ? 39.221 16.071 20.977  1.00 27.35 ? 84  ASP B CA  1 
ATOM   1541 C  C   . ASP B 1 84  ? 40.025 16.418 19.728  1.00 25.91 ? 84  ASP B C   1 
ATOM   1542 O  O   . ASP B 1 84  ? 39.512 16.315 18.613  1.00 26.14 ? 84  ASP B O   1 
ATOM   1543 C  CB  . ASP B 1 84  ? 38.808 17.355 21.673  1.00 28.58 ? 84  ASP B CB  1 
ATOM   1544 C  CG  . ASP B 1 84  ? 37.691 17.129 22.617  1.00 30.58 ? 84  ASP B CG  1 
ATOM   1545 O  OD1 . ASP B 1 84  ? 37.022 16.093 22.454  1.00 31.31 ? 84  ASP B OD1 1 
ATOM   1546 O  OD2 . ASP B 1 84  ? 37.455 17.976 23.493  1.00 32.98 ? 84  ASP B OD2 1 
ATOM   1547 N  N   . PHE B 1 85  ? 41.268 16.861 19.924  1.00 25.37 ? 85  PHE B N   1 
ATOM   1548 C  CA  . PHE B 1 85  ? 42.120 17.206 18.795  1.00 25.81 ? 85  PHE B CA  1 
ATOM   1549 C  C   . PHE B 1 85  ? 42.378 15.982 17.913  1.00 23.37 ? 85  PHE B C   1 
ATOM   1550 O  O   . PHE B 1 85  ? 42.414 16.106 16.698  1.00 23.05 ? 85  PHE B O   1 
ATOM   1551 C  CB  . PHE B 1 85  ? 43.446 17.809 19.255  1.00 23.39 ? 85  PHE B CB  1 
ATOM   1552 C  CG  . PHE B 1 85  ? 43.341 19.236 19.755  1.00 24.58 ? 85  PHE B CG  1 
ATOM   1553 C  CD1 . PHE B 1 85  ? 42.847 20.240 18.932  1.00 31.54 ? 85  PHE B CD1 1 
ATOM   1554 C  CD2 . PHE B 1 85  ? 43.756 19.569 21.048  1.00 24.56 ? 85  PHE B CD2 1 
ATOM   1555 C  CE1 . PHE B 1 85  ? 42.753 21.554 19.379  1.00 29.07 ? 85  PHE B CE1 1 
ATOM   1556 C  CE2 . PHE B 1 85  ? 43.671 20.873 21.509  1.00 32.51 ? 85  PHE B CE2 1 
ATOM   1557 C  CZ  . PHE B 1 85  ? 43.171 21.873 20.675  1.00 34.65 ? 85  PHE B CZ  1 
ATOM   1558 N  N   . THR B 1 86  ? 42.538 14.812 18.520  1.00 22.44 ? 86  THR B N   1 
ATOM   1559 C  CA  . THR B 1 86  ? 42.755 13.585 17.768  1.00 21.97 ? 86  THR B CA  1 
ATOM   1560 C  C   . THR B 1 86  ? 41.539 13.277 16.882  1.00 27.06 ? 86  THR B C   1 
ATOM   1561 O  O   . THR B 1 86  ? 41.705 12.912 15.713  1.00 22.44 ? 86  THR B O   1 
ATOM   1562 C  CB  . THR B 1 86  ? 43.003 12.374 18.713  1.00 30.93 ? 86  THR B CB  1 
ATOM   1563 O  OG1 . THR B 1 86  ? 44.136 12.635 19.543  1.00 21.38 ? 86  THR B OG1 1 
ATOM   1564 C  CG2 . THR B 1 86  ? 43.215 11.082 17.935  1.00 22.04 ? 86  THR B CG2 1 
ATOM   1565 N  N   . ILE B 1 87  ? 40.326 13.431 17.432  1.00 27.47 ? 87  ILE B N   1 
ATOM   1566 C  CA  . ILE B 1 87  ? 39.097 13.291 16.619  1.00 28.13 ? 87  ILE B CA  1 
ATOM   1567 C  C   . ILE B 1 87  ? 39.038 14.308 15.464  1.00 25.37 ? 87  ILE B C   1 
ATOM   1568 O  O   . ILE B 1 87  ? 38.689 13.968 14.300  1.00 25.44 ? 87  ILE B O   1 
ATOM   1569 C  CB  . ILE B 1 87  ? 37.839 13.443 17.484  1.00 27.72 ? 87  ILE B CB  1 
ATOM   1570 C  CG1 . ILE B 1 87  ? 37.604 12.174 18.317  1.00 28.58 ? 87  ILE B CG1 1 
ATOM   1571 C  CG2 . ILE B 1 87  ? 36.618 13.687 16.624  1.00 29.21 ? 87  ILE B CG2 1 
ATOM   1572 C  CD1 . ILE B 1 87  ? 36.612 12.384 19.454  1.00 30.60 ? 87  ILE B CD1 1 
ATOM   1573 N  N   . LEU B 1 88  ? 39.380 15.558 15.763  1.00 25.20 ? 88  LEU B N   1 
ATOM   1574 C  CA  . LEU B 1 88  ? 39.382 16.550 14.703  1.00 25.17 ? 88  LEU B CA  1 
ATOM   1575 C  C   . LEU B 1 88  ? 40.390 16.131 13.641  1.00 23.62 ? 88  LEU B C   1 
ATOM   1576 O  O   . LEU B 1 88  ? 40.208 16.419 12.465  1.00 23.64 ? 88  LEU B O   1 
ATOM   1577 C  CB  . LEU B 1 88  ? 39.674 17.954 15.232  1.00 25.54 ? 88  LEU B CB  1 
ATOM   1578 C  CG  . LEU B 1 88  ? 38.532 18.597 16.018  1.00 27.53 ? 88  LEU B CG  1 
ATOM   1579 C  CD1 . LEU B 1 88  ? 38.995 19.936 16.594  1.00 27.94 ? 88  LEU B CD1 1 
ATOM   1580 C  CD2 . LEU B 1 88  ? 37.312 18.764 15.150  1.00 29.04 ? 88  LEU B CD2 1 
ATOM   1581 N  N   . LYS B 1 89  ? 41.461 15.471 14.061  1.00 23.01 ? 89  LYS B N   1 
ATOM   1582 C  CA  . LYS B 1 89  ? 42.460 15.022 13.115  1.00 26.84 ? 89  LYS B CA  1 
ATOM   1583 C  C   . LYS B 1 89  ? 41.917 13.878 12.249  1.00 21.98 ? 89  LYS B C   1 
ATOM   1584 O  O   . LYS B 1 89  ? 42.123 13.879 11.031  1.00 21.58 ? 89  LYS B O   1 
ATOM   1585 C  CB  . LYS B 1 89  ? 43.747 14.606 13.821  1.00 20.87 ? 89  LYS B CB  1 
ATOM   1586 C  CG  . LYS B 1 89  ? 44.890 14.234 12.852  1.00 19.93 ? 89  LYS B CG  1 
ATOM   1587 C  CD  . LYS B 1 89  ? 44.997 15.158 11.610  1.00 19.88 ? 89  LYS B CD  1 
ATOM   1588 C  CE  . LYS B 1 89  ? 45.340 16.592 11.980  1.00 35.85 ? 89  LYS B CE  1 
ATOM   1589 N  NZ  . LYS B 1 89  ? 45.535 17.518 10.801  1.00 24.75 ? 89  LYS B NZ  1 
ATOM   1590 N  N   . ILE B 1 90  ? 41.230 12.920 12.871  1.00 22.19 ? 90  ILE B N   1 
ATOM   1591 C  CA  . ILE B 1 90  ? 40.613 11.843 12.117  1.00 22.76 ? 90  ILE B CA  1 
ATOM   1592 C  C   . ILE B 1 90  ? 39.744 12.433 11.004  1.00 23.34 ? 90  ILE B C   1 
ATOM   1593 O  O   . ILE B 1 90  ? 39.832 12.019 9.843   1.00 23.04 ? 90  ILE B O   1 
ATOM   1594 C  CB  . ILE B 1 90  ? 39.787 10.900 13.033  1.00 24.14 ? 90  ILE B CB  1 
ATOM   1595 C  CG1 . ILE B 1 90  ? 40.721 10.158 14.012  1.00 23.65 ? 90  ILE B CG1 1 
ATOM   1596 C  CG2 . ILE B 1 90  ? 38.920 9.910  12.214  1.00 25.29 ? 90  ILE B CG2 1 
ATOM   1597 C  CD1 . ILE B 1 90  ? 39.985 9.407  15.154  1.00 25.18 ? 90  ILE B CD1 1 
ATOM   1598 N  N   . GLU B 1 91  ? 38.946 13.436 11.369  1.00 24.30 ? 91  GLU B N   1 
ATOM   1599 C  CA  . GLU B 1 91  ? 38.034 14.079 10.429  1.00 25.22 ? 91  GLU B CA  1 
ATOM   1600 C  C   . GLU B 1 91  ? 38.788 14.853 9.332   1.00 24.16 ? 91  GLU B C   1 
ATOM   1601 O  O   . GLU B 1 91  ? 38.383 14.859 8.149   1.00 24.41 ? 91  GLU B O   1 
ATOM   1602 C  CB  . GLU B 1 91  ? 37.064 14.963 11.211  1.00 26.82 ? 91  GLU B CB  1 
ATOM   1603 C  CG  . GLU B 1 91  ? 36.066 14.105 12.016  1.00 34.55 ? 91  GLU B CG  1 
ATOM   1604 C  CD  . GLU B 1 91  ? 35.215 14.874 13.042  1.00 38.88 ? 91  GLU B CD  1 
ATOM   1605 O  OE1 . GLU B 1 91  ? 35.259 16.127 13.059  1.00 41.50 ? 91  GLU B OE1 1 
ATOM   1606 O  OE2 . GLU B 1 91  ? 34.495 14.206 13.834  1.00 31.61 ? 91  GLU B OE2 1 
ATOM   1607 N  N   . ASP B 1 92  ? 39.926 15.442 9.699   1.00 32.75 ? 92  ASP B N   1 
ATOM   1608 C  CA  . ASP B 1 92  ? 40.761 16.133 8.711   1.00 27.17 ? 92  ASP B CA  1 
ATOM   1609 C  C   . ASP B 1 92  ? 41.342 15.144 7.680   1.00 23.84 ? 92  ASP B C   1 
ATOM   1610 O  O   . ASP B 1 92  ? 41.282 15.364 6.463   1.00 23.83 ? 92  ASP B O   1 
ATOM   1611 C  CB  . ASP B 1 92  ? 41.895 16.898 9.411   1.00 29.04 ? 92  ASP B CB  1 
ATOM   1612 C  CG  . ASP B 1 92  ? 42.667 17.805 8.461   1.00 42.85 ? 92  ASP B CG  1 
ATOM   1613 O  OD1 . ASP B 1 92  ? 42.019 18.619 7.771   1.00 41.98 ? 92  ASP B OD1 1 
ATOM   1614 O  OD2 . ASP B 1 92  ? 43.914 17.709 8.397   1.00 46.04 ? 92  ASP B OD2 1 
ATOM   1615 N  N   . ILE B 1 93  ? 41.888 14.044 8.176   1.00 24.30 ? 93  ILE B N   1 
ATOM   1616 C  CA  . ILE B 1 93  ? 42.429 13.014 7.311   1.00 23.73 ? 93  ILE B CA  1 
ATOM   1617 C  C   . ILE B 1 93  ? 41.340 12.497 6.391   1.00 24.49 ? 93  ILE B C   1 
ATOM   1618 O  O   . ILE B 1 93  ? 41.601 12.191 5.222   1.00 24.19 ? 93  ILE B O   1 
ATOM   1619 C  CB  . ILE B 1 93  ? 43.029 11.835 8.107   1.00 42.15 ? 93  ILE B CB  1 
ATOM   1620 C  CG1 . ILE B 1 93  ? 44.105 12.322 9.088   1.00 30.35 ? 93  ILE B CG1 1 
ATOM   1621 C  CG2 . ILE B 1 93  ? 43.596 10.789 7.150   1.00 23.20 ? 93  ILE B CG2 1 
ATOM   1622 C  CD1 . ILE B 1 93  ? 45.248 13.007 8.436   1.00 30.60 ? 93  ILE B CD1 1 
ATOM   1623 N  N   . GLN B 1 94  ? 40.116 12.388 6.908   1.00 24.80 ? 94  GLN B N   1 
ATOM   1624 C  CA  . GLN B 1 94  ? 39.066 11.842 6.058   1.00 28.85 ? 94  GLN B CA  1 
ATOM   1625 C  C   . GLN B 1 94  ? 38.792 12.812 4.905   1.00 27.78 ? 94  GLN B C   1 
ATOM   1626 O  O   . GLN B 1 94  ? 38.671 12.393 3.755   1.00 25.85 ? 94  GLN B O   1 
ATOM   1627 C  CB  . GLN B 1 94  ? 37.797 11.538 6.843   1.00 27.86 ? 94  GLN B CB  1 
ATOM   1628 C  CG  . GLN B 1 94  ? 36.799 10.715 6.045   1.00 28.73 ? 94  GLN B CG  1 
ATOM   1629 C  CD  . GLN B 1 94  ? 35.386 11.108 6.354   1.00 39.72 ? 94  GLN B CD  1 
ATOM   1630 O  OE1 . GLN B 1 94  ? 35.157 12.116 7.020   1.00 40.47 ? 94  GLN B OE1 1 
ATOM   1631 N  NE2 . GLN B 1 94  ? 34.419 10.315 5.885   1.00 47.52 ? 94  GLN B NE2 1 
ATOM   1632 N  N   . ARG B 1 95  ? 38.740 14.107 5.213   1.00 37.85 ? 95  ARG B N   1 
ATOM   1633 C  CA  . ARG B 1 95  ? 38.618 15.112 4.161   1.00 26.38 ? 95  ARG B CA  1 
ATOM   1634 C  C   . ARG B 1 95  ? 39.728 15.008 3.085   1.00 25.17 ? 95  ARG B C   1 
ATOM   1635 O  O   . ARG B 1 95  ? 39.434 15.111 1.885   1.00 25.55 ? 95  ARG B O   1 
ATOM   1636 C  CB  . ARG B 1 95  ? 38.596 16.516 4.758   1.00 26.96 ? 95  ARG B CB  1 
ATOM   1637 C  CG  . ARG B 1 95  ? 38.592 17.574 3.677   1.00 43.01 ? 95  ARG B CG  1 
ATOM   1638 C  CD  . ARG B 1 95  ? 39.216 18.866 4.141   1.00 48.28 ? 95  ARG B CD  1 
ATOM   1639 N  NE  . ARG B 1 95  ? 40.603 18.712 4.577   1.00 57.64 ? 95  ARG B NE  1 
ATOM   1640 C  CZ  . ARG B 1 95  ? 41.663 18.889 3.792   1.00 59.52 ? 95  ARG B CZ  1 
ATOM   1641 N  NH1 . ARG B 1 95  ? 41.502 19.211 2.513   1.00 51.02 ? 95  ARG B NH1 1 
ATOM   1642 N  NH2 . ARG B 1 95  ? 42.887 18.744 4.286   1.00 58.82 ? 95  ARG B NH2 1 
ATOM   1643 N  N   . LYS B 1 96  ? 40.989 14.846 3.501   1.00 29.96 ? 96  LYS B N   1 
ATOM   1644 C  CA  . LYS B 1 96  ? 42.103 14.703 2.539   1.00 33.65 ? 96  LYS B CA  1 
ATOM   1645 C  C   . LYS B 1 96  ? 41.898 13.497 1.639   1.00 27.82 ? 96  LYS B C   1 
ATOM   1646 O  O   . LYS B 1 96  ? 42.123 13.534 0.412   1.00 23.89 ? 96  LYS B O   1 
ATOM   1647 C  CB  . LYS B 1 96  ? 43.449 14.538 3.236   1.00 31.88 ? 96  LYS B CB  1 
ATOM   1648 C  CG  . LYS B 1 96  ? 43.949 15.740 4.017   1.00 40.42 ? 96  LYS B CG  1 
ATOM   1649 C  CD  . LYS B 1 96  ? 45.366 15.475 4.550   1.00 40.95 ? 96  LYS B CD  1 
ATOM   1650 C  CE  . LYS B 1 96  ? 45.788 16.497 5.588   1.00 42.26 ? 96  LYS B CE  1 
ATOM   1651 N  NZ  . LYS B 1 96  ? 45.480 17.900 5.154   1.00 47.71 ? 96  LYS B NZ  1 
ATOM   1652 N  N   . ILE B 1 97  ? 41.497 12.409 2.279   1.00 24.49 ? 97  ILE B N   1 
ATOM   1653 C  CA  . ILE B 1 97  ? 41.201 11.184 1.564   1.00 30.17 ? 97  ILE B CA  1 
ATOM   1654 C  C   . ILE B 1 97  ? 40.146 11.415 0.481   1.00 40.90 ? 97  ILE B C   1 
ATOM   1655 O  O   . ILE B 1 97  ? 40.297 10.962 -0.670  1.00 28.63 ? 97  ILE B O   1 
ATOM   1656 C  CB  . ILE B 1 97  ? 40.717 10.088 2.529   1.00 25.45 ? 97  ILE B CB  1 
ATOM   1657 C  CG1 . ILE B 1 97  ? 41.870 9.629  3.430   1.00 29.19 ? 97  ILE B CG1 1 
ATOM   1658 C  CG2 . ILE B 1 97  ? 40.128 8.930  1.750   1.00 26.30 ? 97  ILE B CG2 1 
ATOM   1659 C  CD1 . ILE B 1 97  ? 41.478 8.592  4.476   1.00 25.59 ? 97  ILE B CD1 1 
ATOM   1660 N  N   . GLU B 1 98  ? 39.095 12.153 0.841   1.00 39.31 ? 98  GLU B N   1 
ATOM   1661 C  CA  . GLU B 1 98  ? 37.989 12.348 -0.082  1.00 28.75 ? 98  GLU B CA  1 
ATOM   1662 C  C   . GLU B 1 98  ? 38.471 13.175 -1.261  1.00 39.45 ? 98  GLU B C   1 
ATOM   1663 O  O   . GLU B 1 98  ? 38.127 12.901 -2.414  1.00 39.72 ? 98  GLU B O   1 
ATOM   1664 C  CB  . GLU B 1 98  ? 36.802 13.028 0.608   1.00 35.57 ? 98  GLU B CB  1 
ATOM   1665 C  CG  . GLU B 1 98  ? 36.223 12.296 1.853   1.00 35.46 ? 98  GLU B CG  1 
ATOM   1666 C  CD  . GLU B 1 98  ? 35.589 10.936 1.581   1.00 47.44 ? 98  GLU B CD  1 
ATOM   1667 O  OE1 . GLU B 1 98  ? 36.181 10.080 0.881   1.00 45.45 ? 98  GLU B OE1 1 
ATOM   1668 O  OE2 . GLU B 1 98  ? 34.476 10.715 2.102   1.00 63.37 ? 98  GLU B OE2 1 
ATOM   1669 N  N   . ASP B 1 99  ? 39.314 14.162 -0.975  1.00 40.43 ? 99  ASP B N   1 
ATOM   1670 C  CA  . ASP B 1 99  ? 39.864 14.998 -2.040  1.00 30.43 ? 99  ASP B CA  1 
ATOM   1671 C  C   . ASP B 1 99  ? 40.675 14.188 -3.071  1.00 41.34 ? 99  ASP B C   1 
ATOM   1672 O  O   . ASP B 1 99  ? 40.549 14.395 -4.303  1.00 28.85 ? 99  ASP B O   1 
ATOM   1673 C  CB  . ASP B 1 99  ? 40.718 16.081 -1.426  1.00 25.86 ? 99  ASP B CB  1 
ATOM   1674 C  CG  . ASP B 1 99  ? 39.895 17.112 -0.680  1.00 38.67 ? 99  ASP B CG  1 
ATOM   1675 O  OD1 . ASP B 1 99  ? 38.650 17.134 -0.841  1.00 53.03 ? 99  ASP B OD1 1 
ATOM   1676 O  OD2 . ASP B 1 99  ? 40.500 17.918 0.061   1.00 34.88 ? 99  ASP B OD2 1 
ATOM   1677 N  N   . LEU B 1 100 ? 41.490 13.264 -2.556  1.00 38.05 ? 100 LEU B N   1 
ATOM   1678 C  CA  . LEU B 1 100 ? 42.238 12.329 -3.400  1.00 25.38 ? 100 LEU B CA  1 
ATOM   1679 C  C   . LEU B 1 100 ? 41.337 11.402 -4.210  1.00 31.40 ? 100 LEU B C   1 
ATOM   1680 O  O   . LEU B 1 100 ? 41.636 11.058 -5.359  1.00 27.44 ? 100 LEU B O   1 
ATOM   1681 C  CB  . LEU B 1 100 ? 43.184 11.477 -2.556  1.00 24.40 ? 100 LEU B CB  1 
ATOM   1682 C  CG  . LEU B 1 100 ? 44.390 12.248 -2.050  1.00 22.96 ? 100 LEU B CG  1 
ATOM   1683 C  CD1 . LEU B 1 100 ? 45.295 11.342 -1.214  1.00 27.69 ? 100 LEU B CD1 1 
ATOM   1684 C  CD2 . LEU B 1 100 ? 45.127 12.868 -3.220  1.00 22.99 ? 100 LEU B CD2 1 
ATOM   1685 N  N   . LYS B 1 101 ? 40.241 10.980 -3.599  1.00 33.22 ? 101 LYS B N   1 
ATOM   1686 C  CA  . LYS B 1 101 ? 39.269 10.178 -4.316  1.00 31.63 ? 101 LYS B CA  1 
ATOM   1687 C  C   . LYS B 1 101 ? 38.623 10.968 -5.460  1.00 38.53 ? 101 LYS B C   1 
ATOM   1688 O  O   . LYS B 1 101 ? 38.356 10.444 -6.541  1.00 28.53 ? 101 LYS B O   1 
ATOM   1689 C  CB  . LYS B 1 101 ? 38.195 9.692  -3.356  1.00 40.00 ? 101 LYS B CB  1 
ATOM   1690 C  CG  . LYS B 1 101 ? 38.592 8.474  -2.542  1.00 48.75 ? 101 LYS B CG  1 
ATOM   1691 C  CD  . LYS B 1 101 ? 37.489 8.108  -1.574  1.00 41.65 ? 101 LYS B CD  1 
ATOM   1692 C  CE  . LYS B 1 101 ? 37.663 6.710  -1.040  1.00 44.04 ? 101 LYS B CE  1 
ATOM   1693 N  NZ  . LYS B 1 101 ? 39.059 6.479  -0.593  1.00 54.30 ? 101 LYS B NZ  1 
ATOM   1694 N  N   . ARG B 1 102 ? 38.369 12.242 -5.218  1.00 31.45 ? 102 ARG B N   1 
ATOM   1695 C  CA  . ARG B 1 102 ? 37.784 13.080 -6.243  1.00 28.01 ? 102 ARG B CA  1 
ATOM   1696 C  C   . ARG B 1 102 ? 38.756 13.198 -7.426  1.00 30.53 ? 102 ARG B C   1 
ATOM   1697 O  O   . ARG B 1 102 ? 38.350 13.149 -8.593  1.00 29.14 ? 102 ARG B O   1 
ATOM   1698 C  CB  . ARG B 1 102 ? 37.412 14.414 -5.628  1.00 28.61 ? 102 ARG B CB  1 
ATOM   1699 C  CG  . ARG B 1 102 ? 36.126 14.276 -4.812  1.00 29.91 ? 102 ARG B CG  1 
ATOM   1700 C  CD  . ARG B 1 102 ? 35.780 15.536 -4.068  1.00 30.71 ? 102 ARG B CD  1 
ATOM   1701 N  NE  . ARG B 1 102 ? 35.457 16.620 -4.978  1.00 42.18 ? 102 ARG B NE  1 
ATOM   1702 C  CZ  . ARG B 1 102 ? 35.607 17.899 -4.677  1.00 40.26 ? 102 ARG B CZ  1 
ATOM   1703 N  NH1 . ARG B 1 102 ? 36.080 18.239 -3.487  1.00 45.56 ? 102 ARG B NH1 1 
ATOM   1704 N  NH2 . ARG B 1 102 ? 35.290 18.827 -5.563  1.00 40.72 ? 102 ARG B NH2 1 
ATOM   1705 N  N   . ILE B 1 103 ? 40.044 13.338 -7.118  1.00 36.74 ? 103 ILE B N   1 
ATOM   1706 C  CA  . ILE B 1 103 ? 41.052 13.371 -8.173  1.00 34.92 ? 103 ILE B CA  1 
ATOM   1707 C  C   . ILE B 1 103 ? 41.144 12.044 -8.934  1.00 25.54 ? 103 ILE B C   1 
ATOM   1708 O  O   . ILE B 1 103 ? 41.224 12.005 -10.157 1.00 26.61 ? 103 ILE B O   1 
ATOM   1709 C  CB  . ILE B 1 103 ? 42.411 13.723 -7.597  1.00 23.32 ? 103 ILE B CB  1 
ATOM   1710 C  CG1 . ILE B 1 103 ? 42.439 15.212 -7.310  1.00 21.84 ? 103 ILE B CG1 1 
ATOM   1711 C  CG2 . ILE B 1 103 ? 43.536 13.350 -8.559  1.00 21.18 ? 103 ILE B CG2 1 
ATOM   1712 C  CD1 . ILE B 1 103 ? 43.555 15.615 -6.368  1.00 30.94 ? 103 ILE B CD1 1 
ATOM   1713 N  N   . GLU B 1 104 ? 41.130 10.956 -8.195  1.00 24.71 ? 104 GLU B N   1 
ATOM   1714 C  CA  . GLU B 1 104 ? 41.146 9.651  -8.797  1.00 33.86 ? 104 GLU B CA  1 
ATOM   1715 C  C   . GLU B 1 104 ? 39.990 9.512  -9.792  1.00 28.85 ? 104 GLU B C   1 
ATOM   1716 O  O   . GLU B 1 104 ? 40.184 9.096  -10.928 1.00 24.83 ? 104 GLU B O   1 
ATOM   1717 C  CB  . GLU B 1 104 ? 41.065 8.613  -7.704  1.00 25.14 ? 104 GLU B CB  1 
ATOM   1718 C  CG  . GLU B 1 104 ? 41.775 7.314  -7.983  1.00 33.86 ? 104 GLU B CG  1 
ATOM   1719 C  CD  . GLU B 1 104 ? 41.580 6.366  -6.811  1.00 49.28 ? 104 GLU B CD  1 
ATOM   1720 O  OE1 . GLU B 1 104 ? 41.947 5.171  -6.891  1.00 40.08 ? 104 GLU B OE1 1 
ATOM   1721 O  OE2 . GLU B 1 104 ? 41.012 6.841  -5.806  1.00 54.10 ? 104 GLU B OE2 1 
ATOM   1722 N  N   . ARG B 1 105 ? 38.798 9.915  -9.373  1.00 25.20 ? 105 ARG B N   1 
ATOM   1723 C  CA  . ARG B 1 105 ? 37.613 9.796  -10.207 1.00 27.00 ? 105 ARG B CA  1 
ATOM   1724 C  C   . ARG B 1 105 ? 37.763 10.642 -11.466 1.00 30.53 ? 105 ARG B C   1 
ATOM   1725 O  O   . ARG B 1 105 ? 37.350 10.214 -12.564 1.00 28.23 ? 105 ARG B O   1 
ATOM   1726 C  CB  . ARG B 1 105 ? 36.357 10.194 -9.397  1.00 26.90 ? 105 ARG B CB  1 
ATOM   1727 C  CG  . ARG B 1 105 ? 35.044 10.480 -10.190 1.00 28.33 ? 105 ARG B CG  1 
ATOM   1728 C  CD  . ARG B 1 105 ? 34.659 9.353  -11.136 1.00 29.06 ? 105 ARG B CD  1 
ATOM   1729 N  NE  . ARG B 1 105 ? 34.791 8.064  -10.475 1.00 39.98 ? 105 ARG B NE  1 
ATOM   1730 C  CZ  . ARG B 1 105 ? 35.092 6.927  -11.089 1.00 43.38 ? 105 ARG B CZ  1 
ATOM   1731 N  NH1 . ARG B 1 105 ? 35.292 6.899  -12.405 1.00 54.60 ? 105 ARG B NH1 1 
ATOM   1732 N  NH2 . ARG B 1 105 ? 35.194 5.818  -10.377 1.00 33.67 ? 105 ARG B NH2 1 
ATOM   1733 N  N   . MET B 1 106 ? 38.329 11.838 -11.309 1.00 23.86 ? 106 MET B N   1 
ATOM   1734 C  CA  . MET B 1 106 ? 38.638 12.683 -12.475 1.00 23.92 ? 106 MET B CA  1 
ATOM   1735 C  C   . MET B 1 106 ? 39.570 12.021 -13.475 1.00 23.46 ? 106 MET B C   1 
ATOM   1736 O  O   . MET B 1 106 ? 39.385 12.127 -14.675 1.00 23.87 ? 106 MET B O   1 
ATOM   1737 C  CB  . MET B 1 106 ? 39.246 14.010 -12.035 1.00 28.01 ? 106 MET B CB  1 
ATOM   1738 C  CG  . MET B 1 106 ? 38.201 15.035 -11.621 1.00 24.75 ? 106 MET B CG  1 
ATOM   1739 S  SD  . MET B 1 106 ? 38.933 16.345 -10.621 1.00 51.46 ? 106 MET B SD  1 
ATOM   1740 C  CE  . MET B 1 106 ? 37.822 17.668 -11.070 1.00 26.45 ? 106 MET B CE  1 
ATOM   1741 N  N   . LEU B 1 107 ? 40.603 11.382 -12.955 1.00 22.75 ? 107 LEU B N   1 
ATOM   1742 C  CA  . LEU B 1 107 ? 41.581 10.728 -13.777 1.00 22.56 ? 107 LEU B CA  1 
ATOM   1743 C  C   . LEU B 1 107 ? 40.944 9.577  -14.507 1.00 23.12 ? 107 LEU B C   1 
ATOM   1744 O  O   . LEU B 1 107 ? 41.198 9.372  -15.693 1.00 23.38 ? 107 LEU B O   1 
ATOM   1745 C  CB  . LEU B 1 107 ? 42.756 10.265 -12.928 1.00 24.29 ? 107 LEU B CB  1 
ATOM   1746 C  CG  . LEU B 1 107 ? 43.607 11.360 -12.260 1.00 21.59 ? 107 LEU B CG  1 
ATOM   1747 C  CD1 . LEU B 1 107 ? 44.526 10.745 -11.197 1.00 21.17 ? 107 LEU B CD1 1 
ATOM   1748 C  CD2 . LEU B 1 107 ? 44.405 12.176 -13.261 1.00 21.87 ? 107 LEU B CD2 1 
ATOM   1749 N  N   . MET B 1 108 ? 40.092 8.849  -13.789 1.00 23.99 ? 108 MET B N   1 
ATOM   1750 C  CA  . MET B 1 108 ? 39.335 7.748  -14.357 1.00 24.44 ? 108 MET B CA  1 
ATOM   1751 C  C   . MET B 1 108 ? 38.469 8.211  -15.557 1.00 31.03 ? 108 MET B C   1 
ATOM   1752 O  O   . MET B 1 108 ? 38.496 7.617  -16.646 1.00 25.50 ? 108 MET B O   1 
ATOM   1753 C  CB  . MET B 1 108 ? 38.453 7.124  -13.278 1.00 34.50 ? 108 MET B CB  1 
ATOM   1754 C  CG  . MET B 1 108 ? 39.207 6.429  -12.124 1.00 32.50 ? 108 MET B CG  1 
ATOM   1755 S  SD  . MET B 1 108 ? 39.934 4.821  -12.534 1.00 66.18 ? 108 MET B SD  1 
ATOM   1756 C  CE  . MET B 1 108 ? 38.501 3.912  -13.126 1.00 34.20 ? 108 MET B CE  1 
ATOM   1757 N  N   . ASP B 1 109 ? 37.719 9.292  -15.367 1.00 25.26 ? 109 ASP B N   1 
ATOM   1758 C  CA  . ASP B 1 109 ? 36.866 9.785  -16.430 1.00 26.05 ? 109 ASP B CA  1 
ATOM   1759 C  C   . ASP B 1 109 ? 37.678 10.253 -17.644 1.00 29.30 ? 109 ASP B C   1 
ATOM   1760 O  O   . ASP B 1 109 ? 37.302 9.993  -18.819 1.00 26.25 ? 109 ASP B O   1 
ATOM   1761 C  CB  . ASP B 1 109 ? 35.984 10.895 -15.895 1.00 28.19 ? 109 ASP B CB  1 
ATOM   1762 C  CG  . ASP B 1 109 ? 35.033 10.401 -14.817 1.00 37.78 ? 109 ASP B CG  1 
ATOM   1763 O  OD1 . ASP B 1 109 ? 34.582 9.220  -14.934 1.00 32.24 ? 109 ASP B OD1 1 
ATOM   1764 O  OD2 . ASP B 1 109 ? 34.757 11.187 -13.870 1.00 27.53 ? 109 ASP B OD2 1 
ATOM   1765 N  N   . LEU B 1 110 ? 38.783 10.946 -17.357 1.00 24.85 ? 110 LEU B N   1 
ATOM   1766 C  CA  . LEU B 1 110 ? 39.738 11.307 -18.389 1.00 24.68 ? 110 LEU B CA  1 
ATOM   1767 C  C   . LEU B 1 110 ? 40.217 10.105 -19.228 1.00 29.92 ? 110 LEU B C   1 
ATOM   1768 O  O   . LEU B 1 110 ? 40.110 10.113 -20.456 1.00 25.22 ? 110 LEU B O   1 
ATOM   1769 C  CB  . LEU B 1 110 ? 40.926 11.980 -17.740 1.00 25.58 ? 110 LEU B CB  1 
ATOM   1770 C  CG  . LEU B 1 110 ? 40.626 13.424 -17.413 1.00 25.02 ? 110 LEU B CG  1 
ATOM   1771 C  CD1 . LEU B 1 110 ? 41.694 14.009 -16.470 1.00 23.89 ? 110 LEU B CD1 1 
ATOM   1772 C  CD2 . LEU B 1 110 ? 40.554 14.162 -18.743 1.00 25.56 ? 110 LEU B CD2 1 
ATOM   1773 N  N   . LYS B 1 111 ? 40.704 9.068  -18.548 1.00 24.49 ? 111 LYS B N   1 
ATOM   1774 C  CA  . LYS B 1 111 ? 41.244 7.867  -19.189 1.00 31.38 ? 111 LYS B CA  1 
ATOM   1775 C  C   . LYS B 1 111 ? 40.151 7.057  -19.966 1.00 25.77 ? 111 LYS B C   1 
ATOM   1776 O  O   . LYS B 1 111 ? 40.426 6.421  -20.987 1.00 26.29 ? 111 LYS B O   1 
ATOM   1777 C  CB  . LYS B 1 111 ? 41.888 6.956  -18.118 1.00 31.63 ? 111 LYS B CB  1 
ATOM   1778 C  CG  . LYS B 1 111 ? 40.954 5.778  -17.709 1.00 25.43 ? 111 LYS B CG  1 
ATOM   1779 C  CD  . LYS B 1 111 ? 41.588 4.764  -16.795 1.00 34.59 ? 111 LYS B CD  1 
ATOM   1780 C  CE  . LYS B 1 111 ? 40.980 3.361  -17.007 1.00 37.22 ? 111 LYS B CE  1 
ATOM   1781 N  NZ  . LYS B 1 111 ? 39.521 3.264  -16.711 1.00 44.67 ? 111 LYS B NZ  1 
ATOM   1782 N  N   . GLU B 1 112 ? 38.917 7.093  -19.465 1.00 27.46 ? 112 GLU B N   1 
ATOM   1783 C  CA  . GLU B 1 112 ? 37.796 6.442  -20.116 1.00 27.32 ? 112 GLU B CA  1 
ATOM   1784 C  C   . GLU B 1 112 ? 37.411 7.206  -21.355 1.00 27.57 ? 112 GLU B C   1 
ATOM   1785 O  O   . GLU B 1 112 ? 36.631 6.719  -22.174 1.00 28.55 ? 112 GLU B O   1 
ATOM   1786 C  CB  . GLU B 1 112 ? 36.628 6.268  -19.161 1.00 28.02 ? 112 GLU B CB  1 
ATOM   1787 C  CG  . GLU B 1 112 ? 36.996 5.296  -18.068 1.00 35.06 ? 112 GLU B CG  1 
ATOM   1788 C  CD  . GLU B 1 112 ? 36.026 5.270  -16.901 1.00 32.95 ? 112 GLU B CD  1 
ATOM   1789 O  OE1 . GLU B 1 112 ? 34.968 5.930  -16.991 1.00 31.56 ? 112 GLU B OE1 1 
ATOM   1790 O  OE2 . GLU B 1 112 ? 36.324 4.569  -15.896 1.00 32.97 ? 112 GLU B OE2 1 
ATOM   1791 N  N   . ARG B 1 113 ? 37.910 8.435  -21.475 1.00 26.89 ? 113 ARG B N   1 
ATOM   1792 C  CA  . ARG B 1 113 ? 37.668 9.142  -22.738 1.00 27.57 ? 113 ARG B CA  1 
ATOM   1793 C  C   . ARG B 1 113 ? 38.418 8.519  -23.932 1.00 27.43 ? 113 ARG B C   1 
ATOM   1794 O  O   . ARG B 1 113 ? 38.051 8.793  -25.070 1.00 28.00 ? 113 ARG B O   1 
ATOM   1795 C  CB  . ARG B 1 113 ? 38.024 10.637 -22.641 1.00 26.96 ? 113 ARG B CB  1 
ATOM   1796 C  CG  . ARG B 1 113 ? 37.208 11.395 -21.611 1.00 27.14 ? 113 ARG B CG  1 
ATOM   1797 C  CD  . ARG B 1 113 ? 37.695 12.826 -21.404 1.00 27.02 ? 113 ARG B CD  1 
ATOM   1798 N  NE  . ARG B 1 113 ? 36.899 13.636 -22.299 1.00 38.14 ? 113 ARG B NE  1 
ATOM   1799 C  CZ  . ARG B 1 113 ? 35.950 14.480 -21.913 1.00 30.61 ? 113 ARG B CZ  1 
ATOM   1800 N  NH1 . ARG B 1 113 ? 35.728 14.711 -20.622 1.00 28.99 ? 113 ARG B NH1 1 
ATOM   1801 N  NH2 . ARG B 1 113 ? 35.253 15.128 -22.834 1.00 30.18 ? 113 ARG B NH2 1 
ATOM   1802 N  N   . CYS B 1 114 ? 39.446 7.695  -23.696 1.00 27.11 ? 114 CYS B N   1 
ATOM   1803 C  CA  . CYS B 1 114 ? 40.325 7.259  -24.798 1.00 27.41 ? 114 CYS B CA  1 
ATOM   1804 C  C   . CYS B 1 114 ? 39.671 6.241  -25.690 1.00 28.38 ? 114 CYS B C   1 
ATOM   1805 O  O   . CYS B 1 114 ? 38.887 5.444  -25.228 1.00 29.00 ? 114 CYS B O   1 
ATOM   1806 C  CB  . CYS B 1 114 ? 41.647 6.684  -24.287 1.00 28.01 ? 114 CYS B CB  1 
ATOM   1807 S  SG  . CYS B 1 114 ? 42.707 7.892  -23.534 1.00 34.79 ? 114 CYS B SG  1 
ATOM   1808 N  N   . PRO B 1 115 ? 39.962 6.303  -26.992 1.00 28.82 ? 115 PRO B N   1 
ATOM   1809 C  CA  . PRO B 1 115 ? 39.394 5.340  -27.948 1.00 29.88 ? 115 PRO B CA  1 
ATOM   1810 C  C   . PRO B 1 115 ? 40.015 3.938  -27.850 1.00 30.53 ? 115 PRO B C   1 
ATOM   1811 O  O   . PRO B 1 115 ? 40.972 3.723  -27.109 1.00 30.17 ? 115 PRO B O   1 
ATOM   1812 C  CB  . PRO B 1 115 ? 39.691 5.984  -29.309 1.00 30.10 ? 115 PRO B CB  1 
ATOM   1813 C  CG  . PRO B 1 115 ? 40.876 6.866  -29.063 1.00 29.42 ? 115 PRO B CG  1 
ATOM   1814 C  CD  . PRO B 1 115 ? 40.725 7.378  -27.656 1.00 28.58 ? 115 PRO B CD  1 
ATOM   1815 N  N   . GLU B 1 116 ? 39.454 2.999  -28.606 1.00 32.90 ? 116 GLU B N   1 
ATOM   1816 C  CA  . GLU B 1 116 ? 39.963 1.635  -28.657 1.00 34.72 ? 116 GLU B CA  1 
ATOM   1817 C  C   . GLU B 1 116 ? 41.381 1.584  -29.229 1.00 35.98 ? 116 GLU B C   1 
ATOM   1818 O  O   . GLU B 1 116 ? 42.288 1.008  -28.624 1.00 39.46 ? 116 GLU B O   1 
ATOM   1819 C  CB  . GLU B 1 116 ? 39.030 0.755  -29.484 1.00 38.49 ? 116 GLU B CB  1 
ATOM   1820 C  CG  . GLU B 1 116 ? 39.624 -0.596 -29.866 1.00 42.90 ? 116 GLU B CG  1 
ATOM   1821 C  CD  . GLU B 1 116 ? 38.684 -1.433 -30.721 1.00 59.74 ? 116 GLU B CD  1 
ATOM   1822 O  OE1 . GLU B 1 116 ? 37.535 -0.990 -30.950 1.00 57.07 ? 116 GLU B OE1 1 
ATOM   1823 O  OE2 . GLU B 1 116 ? 39.096 -2.526 -31.176 1.00 65.06 ? 116 GLU B OE2 1 
ATOM   1824 N  N   . ASN B 1 117 ? 41.581 2.235  -30.367 1.00 34.82 ? 117 ASN B N   1 
ATOM   1825 C  CA  . ASN B 1 117 ? 42.909 2.331  -30.943 1.00 35.36 ? 117 ASN B CA  1 
ATOM   1826 C  C   . ASN B 1 117 ? 43.610 3.573  -30.422 1.00 31.99 ? 117 ASN B C   1 
ATOM   1827 O  O   . ASN B 1 117 ? 43.266 4.703  -30.776 1.00 31.41 ? 117 ASN B O   1 
ATOM   1828 C  CB  . ASN B 1 117 ? 42.839 2.370  -32.478 1.00 33.95 ? 117 ASN B CB  1 
ATOM   1829 C  CG  . ASN B 1 117 ? 44.177 2.722  -33.115 1.00 35.36 ? 117 ASN B CG  1 
ATOM   1830 O  OD1 . ASN B 1 117 ? 45.255 2.407  -32.578 1.00 34.67 ? 117 ASN B OD1 1 
ATOM   1831 N  ND2 . ASN B 1 117 ? 44.116 3.422  -34.247 1.00 39.43 ? 117 ASN B ND2 1 
ATOM   1832 N  N   . LYS B 1 118 ? 44.606 3.350  -29.585 1.00 31.93 ? 118 LYS B N   1 
ATOM   1833 C  CA  . LYS B 1 118 ? 45.284 4.436  -28.915 1.00 31.03 ? 118 LYS B CA  1 
ATOM   1834 C  C   . LYS B 1 118 ? 46.580 4.818  -29.632 1.00 34.45 ? 118 LYS B C   1 
ATOM   1835 O  O   . LYS B 1 118 ? 47.331 5.663  -29.146 1.00 35.32 ? 118 LYS B O   1 
ATOM   1836 C  CB  . LYS B 1 118 ? 45.545 4.070  -27.465 1.00 30.53 ? 118 LYS B CB  1 
ATOM   1837 C  CG  . LYS B 1 118 ? 44.272 3.743  -26.703 1.00 30.02 ? 118 LYS B CG  1 
ATOM   1838 C  CD  . LYS B 1 118 ? 44.549 3.509  -25.236 1.00 29.52 ? 118 LYS B CD  1 
ATOM   1839 C  CE  . LYS B 1 118 ? 43.279 3.295  -24.452 1.00 29.18 ? 118 LYS B CE  1 
ATOM   1840 N  NZ  . LYS B 1 118 ? 42.305 2.390  -25.103 1.00 30.25 ? 118 LYS B NZ  1 
ATOM   1841 N  N   . ASP B 1 119 ? 46.852 4.216  -30.789 1.00 37.26 ? 119 ASP B N   1 
ATOM   1842 C  CA  . ASP B 1 119 ? 48.016 4.670  -31.515 1.00 39.69 ? 119 ASP B CA  1 
ATOM   1843 C  C   . ASP B 1 119 ? 47.582 5.762  -32.479 1.00 38.81 ? 119 ASP B C   1 
ATOM   1844 O  O   . ASP B 1 119 ? 47.332 5.520  -33.647 1.00 47.70 ? 119 ASP B O   1 
ATOM   1845 C  CB  . ASP B 1 119 ? 48.663 3.496  -32.257 1.00 48.04 ? 119 ASP B CB  1 
ATOM   1846 C  CG  . ASP B 1 119 ? 49.743 3.930  -33.225 1.00 55.96 ? 119 ASP B CG  1 
ATOM   1847 O  OD1 . ASP B 1 119 ? 50.281 5.044  -33.078 1.00 66.43 ? 119 ASP B OD1 1 
ATOM   1848 O  OD2 . ASP B 1 119 ? 50.069 3.142  -34.137 1.00 61.76 ? 119 ASP B OD2 1 
ATOM   1849 N  N   . ILE B 1 120 ? 47.654 6.991  -31.981 1.00 37.54 ? 120 ILE B N   1 
ATOM   1850 C  CA  . ILE B 1 120 ? 47.190 8.188  -32.669 1.00 33.14 ? 120 ILE B CA  1 
ATOM   1851 C  C   . ILE B 1 120 ? 47.855 9.370  -31.970 1.00 35.99 ? 120 ILE B C   1 
ATOM   1852 O  O   . ILE B 1 120 ? 48.238 9.256  -30.791 1.00 34.56 ? 120 ILE B O   1 
ATOM   1853 C  CB  . ILE B 1 120 ? 45.640 8.372  -32.622 1.00 32.20 ? 120 ILE B CB  1 
ATOM   1854 C  CG1 . ILE B 1 120 ? 45.110 8.219  -31.192 1.00 37.17 ? 120 ILE B CG1 1 
ATOM   1855 C  CG2 . ILE B 1 120 ? 44.913 7.402  -33.555 1.00 33.35 ? 120 ILE B CG2 1 
ATOM   1856 C  CD1 . ILE B 1 120 ? 43.609 8.381  -31.083 1.00 30.44 ? 120 ILE B CD1 1 
ATOM   1857 N  N   . TYR B 1 121 ? 47.931 10.511 -32.662 1.00 34.55 ? 121 TYR B N   1 
ATOM   1858 C  CA  . TYR B 1 121 ? 48.467 11.747 -32.075 1.00 39.02 ? 121 TYR B CA  1 
ATOM   1859 C  C   . TYR B 1 121 ? 47.445 12.396 -31.137 1.00 34.44 ? 121 TYR B C   1 
ATOM   1860 O  O   . TYR B 1 121 ? 47.811 13.026 -30.141 1.00 32.54 ? 121 TYR B O   1 
ATOM   1861 C  CB  . TYR B 1 121 ? 48.866 12.751 -33.146 1.00 36.82 ? 121 TYR B CB  1 
ATOM   1862 C  CG  . TYR B 1 121 ? 50.129 12.411 -33.867 1.00 43.63 ? 121 TYR B CG  1 
ATOM   1863 C  CD1 . TYR B 1 121 ? 50.552 13.172 -34.957 1.00 49.02 ? 121 TYR B CD1 1 
ATOM   1864 C  CD2 . TYR B 1 121 ? 50.913 11.335 -33.466 1.00 43.03 ? 121 TYR B CD2 1 
ATOM   1865 C  CE1 . TYR B 1 121 ? 51.720 12.873 -35.625 1.00 51.28 ? 121 TYR B CE1 1 
ATOM   1866 C  CE2 . TYR B 1 121 ? 52.084 11.021 -34.134 1.00 42.80 ? 121 TYR B CE2 1 
ATOM   1867 C  CZ  . TYR B 1 121 ? 52.483 11.797 -35.211 1.00 55.31 ? 121 TYR B CZ  1 
ATOM   1868 O  OH  . TYR B 1 121 ? 53.647 11.496 -35.880 1.00 68.86 ? 121 TYR B OH  1 
ATOM   1869 N  N   . GLU B 1 122 ? 46.167 12.281 -31.485 1.00 32.02 ? 122 GLU B N   1 
ATOM   1870 C  CA  . GLU B 1 122 ? 45.141 12.927 -30.690 1.00 32.30 ? 122 GLU B CA  1 
ATOM   1871 C  C   . GLU B 1 122 ? 44.709 12.093 -29.483 1.00 33.49 ? 122 GLU B C   1 
ATOM   1872 O  O   . GLU B 1 122 ? 44.065 11.063 -29.593 1.00 44.69 ? 122 GLU B O   1 
ATOM   1873 C  CB  . GLU B 1 122 ? 43.960 13.282 -31.592 1.00 31.56 ? 122 GLU B CB  1 
ATOM   1874 C  CG  . GLU B 1 122 ? 44.406 14.248 -32.661 1.00 33.16 ? 122 GLU B CG  1 
ATOM   1875 C  CD  . GLU B 1 122 ? 44.817 13.626 -34.000 1.00 33.80 ? 122 GLU B CD  1 
ATOM   1876 O  OE1 . GLU B 1 122 ? 45.032 12.395 -34.110 1.00 33.43 ? 122 GLU B OE1 1 
ATOM   1877 O  OE2 . GLU B 1 122 ? 45.008 14.422 -34.938 1.00 44.01 ? 122 GLU B OE2 1 
ATOM   1878 N  N   . CYS B 1 123 ? 45.013 12.612 -28.311 1.00 30.29 ? 123 CYS B N   1 
ATOM   1879 C  CA  . CYS B 1 123 ? 44.595 11.985 -27.081 1.00 38.37 ? 123 CYS B CA  1 
ATOM   1880 C  C   . CYS B 1 123 ? 43.558 12.857 -26.393 1.00 29.46 ? 123 CYS B C   1 
ATOM   1881 O  O   . CYS B 1 123 ? 43.835 14.014 -26.077 1.00 29.01 ? 123 CYS B O   1 
ATOM   1882 C  CB  . CYS B 1 123 ? 45.791 11.754 -26.170 1.00 28.82 ? 123 CYS B CB  1 
ATOM   1883 S  SG  . CYS B 1 123 ? 45.274 11.274 -24.562 1.00 27.62 ? 123 CYS B SG  1 
ATOM   1884 N  N   . PRO B 1 124 ? 42.343 12.318 -26.203 1.00 27.66 ? 124 PRO B N   1 
ATOM   1885 C  CA  . PRO B 1 124 ? 41.255 13.056 -25.528 1.00 33.99 ? 124 PRO B CA  1 
ATOM   1886 C  C   . PRO B 1 124 ? 41.666 13.555 -24.134 1.00 27.00 ? 124 PRO B C   1 
ATOM   1887 O  O   . PRO B 1 124 ? 41.144 14.567 -23.668 1.00 27.30 ? 124 PRO B O   1 
ATOM   1888 C  CB  . PRO B 1 124 ? 40.115 12.028 -25.442 1.00 27.45 ? 124 PRO B CB  1 
ATOM   1889 C  CG  . PRO B 1 124 ? 40.410 11.033 -26.536 1.00 27.75 ? 124 PRO B CG  1 
ATOM   1890 C  CD  . PRO B 1 124 ? 41.930 10.970 -26.631 1.00 27.61 ? 124 PRO B CD  1 
ATOM   1891 N  N   . ILE B 1 125 ? 42.590 12.843 -23.485 1.00 28.43 ? 125 ILE B N   1 
ATOM   1892 C  CA  . ILE B 1 125 ? 43.079 13.274 -22.197 1.00 27.93 ? 125 ILE B CA  1 
ATOM   1893 C  C   . ILE B 1 125 ? 43.772 14.617 -22.392 1.00 31.58 ? 125 ILE B C   1 
ATOM   1894 O  O   . ILE B 1 125 ? 43.436 15.611 -21.743 1.00 31.45 ? 125 ILE B O   1 
ATOM   1895 C  CB  . ILE B 1 125 ? 44.068 12.274 -21.568 1.00 27.38 ? 125 ILE B CB  1 
ATOM   1896 C  CG1 . ILE B 1 125 ? 43.431 10.891 -21.362 1.00 32.11 ? 125 ILE B CG1 1 
ATOM   1897 C  CG2 . ILE B 1 125 ? 44.589 12.806 -20.222 1.00 26.91 ? 125 ILE B CG2 1 
ATOM   1898 C  CD1 . ILE B 1 125 ? 44.368 9.872  -20.650 1.00 26.78 ? 125 ILE B CD1 1 
ATOM   1899 N  N   . ILE B 1 126 ? 44.741 14.641 -23.303 1.00 29.98 ? 126 ILE B N   1 
ATOM   1900 C  CA  . ILE B 1 126 ? 45.526 15.840 -23.540 1.00 35.43 ? 126 ILE B CA  1 
ATOM   1901 C  C   . ILE B 1 126 ? 44.649 16.968 -24.057 1.00 31.18 ? 126 ILE B C   1 
ATOM   1902 O  O   . ILE B 1 126 ? 44.741 18.110 -23.605 1.00 29.92 ? 126 ILE B O   1 
ATOM   1903 C  CB  . ILE B 1 126 ? 46.672 15.574 -24.528 1.00 33.84 ? 126 ILE B CB  1 
ATOM   1904 C  CG1 . ILE B 1 126 ? 47.635 14.533 -23.944 1.00 30.61 ? 126 ILE B CG1 1 
ATOM   1905 C  CG2 . ILE B 1 126 ? 47.418 16.873 -24.833 1.00 30.67 ? 126 ILE B CG2 1 
ATOM   1906 C  CD1 . ILE B 1 126 ? 48.698 14.055 -24.919 1.00 29.68 ? 126 ILE B CD1 1 
ATOM   1907 N  N   . GLU B 1 127 ? 43.788 16.635 -25.003 1.00 29.31 ? 127 GLU B N   1 
ATOM   1908 C  CA  . GLU B 1 127 ? 42.891 17.624 -25.540 1.00 30.35 ? 127 GLU B CA  1 
ATOM   1909 C  C   . GLU B 1 127 ? 42.033 18.211 -24.440 1.00 34.41 ? 127 GLU B C   1 
ATOM   1910 O  O   . GLU B 1 127 ? 41.901 19.435 -24.367 1.00 31.44 ? 127 GLU B O   1 
ATOM   1911 C  CB  . GLU B 1 127 ? 42.025 17.018 -26.629 1.00 38.81 ? 127 GLU B CB  1 
ATOM   1912 C  CG  . GLU B 1 127 ? 42.830 16.582 -27.837 1.00 41.51 ? 127 GLU B CG  1 
ATOM   1913 C  CD  . GLU B 1 127 ? 42.007 15.795 -28.827 1.00 42.85 ? 127 GLU B CD  1 
ATOM   1914 O  OE1 . GLU B 1 127 ? 42.437 15.702 -29.992 1.00 53.50 ? 127 GLU B OE1 1 
ATOM   1915 O  OE2 . GLU B 1 127 ? 40.950 15.243 -28.437 1.00 34.52 ? 127 GLU B OE2 1 
ATOM   1916 N  N   . THR B 1 128 ? 41.524 17.361 -23.543 1.00 29.04 ? 128 THR B N   1 
ATOM   1917 C  CA  . THR B 1 128 ? 40.636 17.844 -22.488 1.00 31.18 ? 128 THR B CA  1 
ATOM   1918 C  C   . THR B 1 128 ? 41.357 18.765 -21.537 1.00 29.31 ? 128 THR B C   1 
ATOM   1919 O  O   . THR B 1 128 ? 40.889 19.878 -21.268 1.00 30.80 ? 128 THR B O   1 
ATOM   1920 C  CB  . THR B 1 128 ? 40.006 16.700 -21.651 1.00 33.39 ? 128 THR B CB  1 
ATOM   1921 O  OG1 . THR B 1 128 ? 39.123 15.937 -22.483 1.00 28.12 ? 128 THR B OG1 1 
ATOM   1922 C  CG2 . THR B 1 128 ? 39.197 17.276 -20.509 1.00 28.20 ? 128 THR B CG2 1 
ATOM   1923 N  N   . LEU B 1 129 ? 42.519 18.323 -21.073 1.00 28.56 ? 129 LEU B N   1 
ATOM   1924 C  CA  . LEU B 1 129 ? 43.320 19.112 -20.142 1.00 34.67 ? 129 LEU B CA  1 
ATOM   1925 C  C   . LEU B 1 129 ? 43.921 20.378 -20.783 1.00 32.81 ? 129 LEU B C   1 
ATOM   1926 O  O   . LEU B 1 129 ? 44.391 21.265 -20.084 1.00 31.31 ? 129 LEU B O   1 
ATOM   1927 C  CB  . LEU B 1 129 ? 44.425 18.243 -19.581 1.00 27.76 ? 129 LEU B CB  1 
ATOM   1928 C  CG  . LEU B 1 129 ? 43.870 17.124 -18.709 1.00 26.35 ? 129 LEU B CG  1 
ATOM   1929 C  CD1 . LEU B 1 129 ? 45.030 16.364 -18.075 1.00 25.60 ? 129 LEU B CD1 1 
ATOM   1930 C  CD2 . LEU B 1 129 ? 42.907 17.674 -17.659 1.00 26.34 ? 129 LEU B CD2 1 
ATOM   1931 N  N   . MET B 1 130 ? 43.928 20.430 -22.114 1.00 31.35 ? 130 MET B N   1 
ATOM   1932 C  CA  . MET B 1 130 ? 44.457 21.572 -22.838 1.00 42.73 ? 130 MET B CA  1 
ATOM   1933 C  C   . MET B 1 130 ? 43.459 22.714 -22.880 1.00 48.25 ? 130 MET B C   1 
ATOM   1934 O  O   . MET B 1 130 ? 43.853 23.877 -22.878 1.00 51.47 ? 130 MET B O   1 
ATOM   1935 C  CB  . MET B 1 130 ? 44.856 21.188 -24.271 1.00 36.40 ? 130 MET B CB  1 
ATOM   1936 C  CG  . MET B 1 130 ? 46.261 20.663 -24.347 1.00 35.63 ? 130 MET B CG  1 
ATOM   1937 S  SD  . MET B 1 130 ? 46.891 20.400 -25.993 1.00 50.41 ? 130 MET B SD  1 
ATOM   1938 C  CE  . MET B 1 130 ? 48.651 20.466 -25.608 1.00 35.70 ? 130 MET B CE  1 
ATOM   1939 N  N   . LYS B 1 131 ? 42.172 22.365 -22.935 1.00 47.67 ? 131 LYS B N   1 
ATOM   1940 C  CA  . LYS B 1 131 ? 41.091 23.344 -23.037 1.00 52.00 ? 131 LYS B CA  1 
ATOM   1941 C  C   . LYS B 1 131 ? 40.852 24.015 -21.682 1.00 54.55 ? 131 LYS B C   1 
ATOM   1942 O  O   . LYS B 1 131 ? 39.829 24.662 -21.456 1.00 60.57 ? 131 LYS B O   1 
ATOM   1943 C  CB  . LYS B 1 131 ? 39.804 22.677 -23.548 1.00 38.71 ? 131 LYS B CB  1 
HETATM 1944 HG HG  . HG  C 2 .   ? 43.662 11.144 26.525  1.00 38.35 ? 201 HG  A HG  1 
HETATM 1945 HG HG  . HG  D 2 .   ? 44.330 9.033  -24.989 1.00 37.04 ? 202 HG  A HG  1 
HETATM 1946 O  O   . HOH E 3 .   ? 51.202 0.514  22.593  1.00 34.35 ? 301 HOH A O   1 
HETATM 1947 O  O   . HOH E 3 .   ? 53.230 -2.026 -2.560  1.00 42.30 ? 302 HOH A O   1 
HETATM 1948 O  O   . HOH E 3 .   ? 47.532 1.557  -5.992  1.00 26.99 ? 303 HOH A O   1 
HETATM 1949 O  O   . HOH E 3 .   ? 49.388 0.000  0.000   0.50 38.30 ? 304 HOH A O   1 
HETATM 1950 O  O   . HOH E 3 .   ? 63.173 25.496 -22.986 1.00 51.91 ? 305 HOH A O   1 
HETATM 1951 O  O   . HOH E 3 .   ? 30.434 3.880  32.143  1.00 30.94 ? 306 HOH A O   1 
HETATM 1952 O  O   . HOH E 3 .   ? 54.578 39.326 -27.914 1.00 54.79 ? 307 HOH A O   1 
HETATM 1953 O  O   . HOH E 3 .   ? 41.790 -0.166 -3.791  1.00 38.46 ? 308 HOH A O   1 
HETATM 1954 O  O   . HOH E 3 .   ? 45.220 1.414  4.341   1.00 28.23 ? 309 HOH A O   1 
HETATM 1955 O  O   . HOH E 3 .   ? 38.016 7.229  33.792  1.00 25.59 ? 310 HOH A O   1 
HETATM 1956 O  O   . HOH E 3 .   ? 33.796 2.900  27.431  1.00 40.71 ? 311 HOH A O   1 
HETATM 1957 O  O   . HOH E 3 .   ? 38.401 6.142  24.570  1.00 23.38 ? 312 HOH A O   1 
HETATM 1958 O  O   . HOH E 3 .   ? 36.105 7.423  25.221  1.00 34.36 ? 313 HOH A O   1 
HETATM 1959 O  O   . HOH E 3 .   ? 43.948 1.378  -12.558 1.00 35.94 ? 314 HOH A O   1 
HETATM 1960 O  O   . HOH E 3 .   ? 37.126 3.287  24.957  1.00 34.29 ? 315 HOH A O   1 
HETATM 1961 O  O   . HOH E 3 .   ? 40.295 9.019  34.542  1.00 29.30 ? 316 HOH A O   1 
HETATM 1962 O  O   . HOH E 3 .   ? 53.804 16.162 -28.443 1.00 38.96 ? 317 HOH A O   1 
HETATM 1963 O  O   . HOH E 3 .   ? 61.969 18.878 -13.614 1.00 40.68 ? 318 HOH A O   1 
HETATM 1964 O  O   . HOH E 3 .   ? 51.082 2.789  18.279  1.00 48.89 ? 319 HOH A O   1 
HETATM 1965 O  O   . HOH E 3 .   ? 56.601 5.641  -31.569 1.00 43.15 ? 320 HOH A O   1 
HETATM 1966 O  O   . HOH E 3 .   ? 57.548 4.798  -25.478 1.00 51.03 ? 321 HOH A O   1 
HETATM 1967 O  O   . HOH E 3 .   ? 61.692 11.138 -21.348 1.00 46.73 ? 322 HOH A O   1 
HETATM 1968 O  O   . HOH E 3 .   ? 47.912 3.541  18.351  1.00 33.90 ? 323 HOH A O   1 
HETATM 1969 O  O   . HOH F 3 .   ? 41.490 2.990  -7.713  1.00 34.44 ? 201 HOH B O   1 
HETATM 1970 O  O   . HOH F 3 .   ? 41.456 5.684  -32.398 1.00 32.89 ? 202 HOH B O   1 
HETATM 1971 O  O   . HOH F 3 .   ? 36.975 14.607 -18.317 1.00 32.11 ? 203 HOH B O   1 
HETATM 1972 O  O   . HOH F 3 .   ? 32.481 14.001 15.536  1.00 30.16 ? 204 HOH B O   1 
HETATM 1973 O  O   . HOH F 3 .   ? 36.525 13.287 -25.034 1.00 34.36 ? 205 HOH B O   1 
HETATM 1974 O  O   . HOH F 3 .   ? 36.771 17.249 -24.556 1.00 39.48 ? 206 HOH B O   1 
HETATM 1975 O  O   . HOH F 3 .   ? 40.193 1.838  -22.758 1.00 38.49 ? 207 HOH B O   1 
HETATM 1976 O  O   . HOH F 3 .   ? 33.814 16.514 -18.723 1.00 36.97 ? 208 HOH B O   1 
HETATM 1977 O  O   . HOH F 3 .   ? 38.978 2.631  -19.881 1.00 38.09 ? 209 HOH B O   1 
HETATM 1978 O  O   . HOH F 3 .   ? 38.523 16.435 -26.634 1.00 33.65 ? 210 HOH B O   1 
HETATM 1979 O  O   . HOH F 3 .   ? 40.198 21.845 31.260  1.00 48.39 ? 211 HOH B O   1 
HETATM 1980 O  O   . HOH F 3 .   ? 57.443 16.871 27.472  1.00 38.42 ? 212 HOH B O   1 
HETATM 1981 O  O   . HOH F 3 .   ? 45.845 0.610  -28.892 1.00 32.51 ? 213 HOH B O   1 
HETATM 1982 O  O   . HOH F 3 .   ? 53.485 21.696 8.591   1.00 30.84 ? 214 HOH B O   1 
HETATM 1983 O  O   . HOH F 3 .   ? 39.313 4.577  -22.598 1.00 27.30 ? 215 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . PHE A 3   ? 0.6698 0.5574 0.9760 0.1157  0.2977  0.2739  3   PHE A N   
2    C CA  . PHE A 3   ? 0.7113 0.5879 1.0448 0.0985  0.2952  0.2593  3   PHE A CA  
3    C C   . PHE A 3   ? 0.7072 0.5654 1.0277 0.1012  0.2885  0.2561  3   PHE A C   
4    O O   . PHE A 3   ? 0.8042 0.6500 1.0923 0.1148  0.2909  0.2639  3   PHE A O   
5    C CB  . PHE A 3   ? 0.6552 0.5128 0.9906 0.0820  0.3117  0.2516  3   PHE A CB  
6    N N   . ARG A 4   ? 0.7795 0.6380 1.1273 0.0875  0.2799  0.2441  4   ARG A N   
7    C CA  . ARG A 4   ? 0.7275 0.5742 1.0691 0.0861  0.2712  0.2393  4   ARG A CA  
8    C C   . ARG A 4   ? 0.7003 0.5260 1.0534 0.0675  0.2775  0.2266  4   ARG A C   
9    O O   . ARG A 4   ? 0.7599 0.5823 1.1243 0.0568  0.2883  0.2216  4   ARG A O   
10   C CB  . ARG A 4   ? 0.5699 0.4439 0.9330 0.0864  0.2494  0.2378  4   ARG A CB  
11   C CG  . ARG A 4   ? 0.5330 0.4339 0.8901 0.1005  0.2423  0.2482  4   ARG A CG  
12   C CD  . ARG A 4   ? 0.5770 0.4725 0.8958 0.1170  0.2452  0.2570  4   ARG A CD  
13   N NE  . ARG A 4   ? 0.6445 0.5663 0.9532 0.1303  0.2425  0.2671  4   ARG A NE  
14   N N   . ILE A 5   ? 0.7538 0.5647 1.1002 0.0630  0.2730  0.2212  5   ILE A N   
15   C CA  . ILE A 5   ? 0.7199 0.5132 1.0764 0.0437  0.2780  0.2083  5   ILE A CA  
16   C C   . ILE A 5   ? 0.7793 0.5762 1.1491 0.0347  0.2633  0.2007  5   ILE A C   
17   O O   . ILE A 5   ? 0.8748 0.6676 1.2271 0.0438  0.2575  0.2056  5   ILE A O   
18   C CB  . ILE A 5   ? 0.8539 0.6084 1.1748 0.0430  0.2972  0.2088  5   ILE A CB  
19   N N   . GLY A 6   ? 0.6285 0.4362 1.0305 0.0168  0.2563  0.1891  6   GLY A N   
20   C CA  . GLY A 6   ? 0.6307 0.4328 1.0374 0.0039  0.2479  0.1807  6   GLY A CA  
21   C C   . GLY A 6   ? 0.6148 0.4248 1.0174 0.0091  0.2314  0.1853  6   GLY A C   
22   O O   . GLY A 6   ? 0.6858 0.5216 1.1060 0.0137  0.2134  0.1900  6   GLY A O   
23   N N   . GLU A 7   ? 0.6609 0.4456 1.0373 0.0077  0.2391  0.1839  7   GLU A N   
24   C CA  . GLU A 7   ? 0.7746 0.5610 1.1422 0.0108  0.2285  0.1872  7   GLU A CA  
25   C C   . GLU A 7   ? 0.7045 0.4960 1.0522 0.0335  0.2286  0.2001  7   GLU A C   
26   O O   . GLU A 7   ? 0.6403 0.4392 0.9829 0.0377  0.2189  0.2042  7   GLU A O   
27   C CB  . GLU A 7   ? 0.8476 0.6034 1.1951 0.0013  0.2401  0.1799  7   GLU A CB  
28   N N   . LEU A 8   ? 0.6407 0.4289 0.9758 0.0472  0.2402  0.2065  8   LEU A N   
29   C CA  . LEU A 8   ? 0.6285 0.4331 0.9511 0.0673  0.2365  0.2183  8   LEU A CA  
30   C C   . LEU A 8   ? 0.7473 0.5883 1.0975 0.0647  0.2161  0.2203  8   LEU A C   
31   O O   . LEU A 8   ? 0.5714 0.4304 0.9160 0.0738  0.2050  0.2271  8   LEU A O   
32   C CB  . LEU A 8   ? 0.6496 0.4444 0.9526 0.0803  0.2525  0.2250  8   LEU A CB  
33   N N   . ALA A 9   ? 0.7801 0.6318 1.1608 0.0520  0.2109  0.2140  9   ALA A N   
34   C CA  . ALA A 9   ? 0.5607 0.4432 0.9702 0.0491  0.1905  0.2150  9   ALA A CA  
35   C C   . ALA A 9   ? 0.5949 0.4851 1.0129 0.0393  0.1706  0.2132  9   ALA A C   
36   O O   . ALA A 9   ? 0.6114 0.5242 1.0437 0.0385  0.1511  0.2166  9   ALA A O   
37   C CB  . ALA A 9   ? 0.5417 0.4324 0.9859 0.0386  0.1903  0.2076  9   ALA A CB  
38   N N   . ASP A 10  ? 0.5971 0.4670 1.0026 0.0315  0.1761  0.2087  10  ASP A N   
39   C CA  . ASP A 10  ? 0.5547 0.4294 0.9624 0.0211  0.1601  0.2083  10  ASP A CA  
40   C C   . ASP A 10  ? 0.7396 0.6183 1.1224 0.0350  0.1588  0.2186  10  ASP A C   
41   O O   . ASP A 10  ? 0.7835 0.6635 1.1624 0.0274  0.1498  0.2199  10  ASP A O   
42   C CB  . ASP A 10  ? 0.6006 0.4531 1.0048 0.0056  0.1683  0.1985  10  ASP A CB  
43   N N   . LYS A 11  ? 0.7403 0.6228 1.1067 0.0545  0.1687  0.2256  11  LYS A N   
44   C CA  . LYS A 11  ? 0.4982 0.3962 0.8458 0.0699  0.1647  0.2357  11  LYS A CA  
45   C C   . LYS A 11  ? 0.6303 0.5593 0.9942 0.0650  0.1414  0.2396  11  LYS A C   
46   O O   . LYS A 11  ? 0.7700 0.7172 1.1203 0.0753  0.1359  0.2474  11  LYS A O   
47   C CB  . LYS A 11  ? 0.5216 0.4193 0.8486 0.0899  0.1802  0.2411  11  LYS A CB  
48   N N   . CYS A 12  ? 0.5073 0.4430 0.9003 0.0501  0.1276  0.2340  12  CYS A N   
49   C CA  . CYS A 12  ? 0.4408 0.4007 0.8500 0.0433  0.1032  0.2368  12  CYS A CA  
50   C C   . CYS A 12  ? 0.4912 0.4525 0.9037 0.0265  0.0848  0.2375  12  CYS A C   
51   O O   . CYS A 12  ? 0.5087 0.4864 0.9329 0.0169  0.0613  0.2398  12  CYS A O   
52   C CB  . CYS A 12  ? 0.4942 0.4603 0.9358 0.0372  0.0964  0.2304  12  CYS A CB  
53   S SG  . CYS A 12  ? 0.5334 0.5070 0.9758 0.0524  0.1121  0.2317  12  CYS A SG  
54   N N   . GLY A 13  ? 0.4686 0.4115 0.8702 0.0210  0.0954  0.2351  13  GLY A N   
55   C CA  . GLY A 13  ? 0.4693 0.4173 0.8694 0.0021  0.0793  0.2318  13  GLY A CA  
56   C C   . GLY A 13  ? 0.4646 0.4116 0.8943 -0.0179 0.0649  0.2255  13  GLY A C   
57   O O   . GLY A 13  ? 0.4978 0.4572 0.9318 -0.0348 0.0425  0.2248  13  GLY A O   
58   N N   . VAL A 14  ? 0.4856 0.4227 0.9314 -0.0157 0.0762  0.2177  14  VAL A N   
59   C CA  . VAL A 14  ? 0.5841 0.5245 1.0570 -0.0324 0.0640  0.2082  14  VAL A CA  
60   C C   . VAL A 14  ? 0.6053 0.5248 1.0751 -0.0374 0.0860  0.1980  14  VAL A C   
61   O O   . VAL A 14  ? 0.6792 0.5844 1.1404 -0.0248 0.1086  0.1968  14  VAL A O   
62   C CB  . VAL A 14  ? 0.5639 0.5189 1.0681 -0.0283 0.0520  0.2068  14  VAL A CB  
63   C CG1 . VAL A 14  ? 0.5623 0.5248 1.0965 -0.0444 0.0356  0.1982  14  VAL A CG1 
64   C CG2 . VAL A 14  ? 0.4550 0.4265 0.9577 -0.0222 0.0331  0.2163  14  VAL A CG2 
65   N N   . ASN A 15  ? 0.6926 0.6110 1.1670 -0.0569 0.0790  0.1903  15  ASN A N   
66   C CA  . ASN A 15  ? 0.5721 0.4710 1.0416 -0.0654 0.0988  0.1790  15  ASN A CA  
67   C C   . ASN A 15  ? 0.5299 0.4323 1.0246 -0.0652 0.1035  0.1715  15  ASN A C   
68   O O   . ASN A 15  ? 0.6270 0.5496 1.1495 -0.0621 0.0870  0.1734  15  ASN A O   
69   C CB  . ASN A 15  ? 0.6232 0.5245 1.0899 -0.0884 0.0888  0.1720  15  ASN A CB  
70   C CG  . ASN A 15  ? 0.6907 0.6190 1.1835 -0.1016 0.0579  0.1708  15  ASN A CG  
71   O OD1 . ASN A 15  ? 0.7172 0.6561 1.2378 -0.1005 0.0516  0.1667  15  ASN A OD1 
72   N ND2 . ASN A 15  ? 0.6237 0.5638 1.1075 -0.1140 0.0382  0.1744  15  ASN A ND2 
73   N N   . LYS A 16  ? 0.5684 0.4510 1.0544 -0.0693 0.1260  0.1627  16  LYS A N   
74   C CA  . LYS A 16  ? 0.5808 0.4631 1.0830 -0.0650 0.1381  0.1577  16  LYS A CA  
75   C C   . LYS A 16  ? 0.6443 0.5537 1.1881 -0.0758 0.1184  0.1507  16  LYS A C   
76   O O   . LYS A 16  ? 0.5570 0.4736 1.1112 -0.0934 0.1101  0.1418  16  LYS A O   
77   C CB  . LYS A 16  ? 0.6042 0.4583 1.0844 -0.0707 0.1648  0.1493  16  LYS A CB  
78   C CG  . LYS A 16  ? 0.6266 0.4523 1.0672 -0.0583 0.1822  0.1561  16  LYS A CG  
79   C CD  . LYS A 16  ? 0.6653 0.4607 1.0824 -0.0691 0.2022  0.1469  16  LYS A CD  
80   N N   . GLU A 17  ? 0.9183 0.8435 1.4863 -0.0641 0.1110  0.1548  17  GLU A N   
81   C CA  . GLU A 17  ? 0.6148 0.5674 1.2234 -0.0685 0.0850  0.1522  17  GLU A CA  
82   C C   . GLU A 17  ? 0.7280 0.6929 1.3722 -0.0681 0.0912  0.1423  17  GLU A C   
83   O O   . GLU A 17  ? 0.6791 0.6486 1.3356 -0.0554 0.0966  0.1452  17  GLU A O   
84   C CB  . GLU A 17  ? 0.4643 0.4273 1.0758 -0.0565 0.0658  0.1644  17  GLU A CB  
85   C CG  . GLU A 17  ? 0.4993 0.4834 1.1386 -0.0629 0.0325  0.1651  17  GLU A CG  
86   C CD  . GLU A 17  ? 0.6520 0.6356 1.2728 -0.0783 0.0183  0.1660  17  GLU A CD  
87   O OE1 . GLU A 17  ? 0.6772 0.6472 1.2758 -0.0881 0.0351  0.1604  17  GLU A OE1 
88   O OE2 . GLU A 17  ? 0.6830 0.6780 1.3074 -0.0811 -0.0093 0.1728  17  GLU A OE2 
89   N N   . THR A 18  ? 0.5528 0.5272 1.2158 -0.0830 0.0890  0.1297  18  THR A N   
90   C CA  . THR A 18  ? 0.5034 0.4947 1.2029 -0.0843 0.0939  0.1176  18  THR A CA  
91   C C   . THR A 18  ? 0.4800 0.4993 1.2231 -0.0794 0.0642  0.1165  18  THR A C   
92   O O   . THR A 18  ? 0.4904 0.5259 1.2669 -0.0736 0.0658  0.1080  18  THR A O   
93   C CB  . THR A 18  ? 0.5750 0.5671 1.2750 -0.1028 0.1057  0.1027  18  THR A CB  
94   N N   . ILE A 19  ? 0.4322 0.4561 1.1725 -0.0813 0.0371  0.1248  19  ILE A N   
95   C CA  . ILE A 19  ? 0.4183 0.4647 1.1962 -0.0778 0.0056  0.1240  19  ILE A CA  
96   C C   . ILE A 19  ? 0.4458 0.4960 1.2430 -0.0605 0.0020  0.1279  19  ILE A C   
97   O O   . ILE A 19  ? 0.5019 0.5693 1.3370 -0.0540 -0.0124 0.1201  19  ILE A O   
98   C CB  . ILE A 19  ? 0.5265 0.5733 1.2894 -0.0845 -0.0232 0.1346  19  ILE A CB  
99   C CG1 . ILE A 19  ? 0.5355 0.5999 1.3335 -0.0792 -0.0567 0.1351  19  ILE A CG1 
100  C CG2 . ILE A 19  ? 0.6063 0.6370 1.3342 -0.0786 -0.0239 0.1497  19  ILE A CG2 
101  C CD1 . ILE A 19  ? 0.4351 0.4980 1.2150 -0.0859 -0.0867 0.1474  19  ILE A CD1 
102  N N   . ARG A 20  ? 0.3957 0.4299 1.1646 -0.0528 0.0162  0.1388  20  ARG A N   
103  C CA  . ARG A 20  ? 0.3799 0.4177 1.1616 -0.0384 0.0146  0.1434  20  ARG A CA  
104  C C   . ARG A 20  ? 0.4088 0.4584 1.2194 -0.0331 0.0321  0.1293  20  ARG A C   
105  O O   . ARG A 20  ? 0.3663 0.4294 1.2054 -0.0234 0.0201  0.1239  20  ARG A O   
106  C CB  . ARG A 20  ? 0.3803 0.4000 1.1203 -0.0316 0.0290  0.1574  20  ARG A CB  
107  C CG  . ARG A 20  ? 0.3713 0.3906 1.0990 -0.0274 0.0050  0.1704  20  ARG A CG  
108  C CD  . ARG A 20  ? 0.3776 0.3985 1.0976 -0.0391 -0.0192 0.1732  20  ARG A CD  
109  N NE  . ARG A 20  ? 0.3851 0.4000 1.0695 -0.0388 -0.0310 0.1864  20  ARG A NE  
110  C CZ  . ARG A 20  ? 0.3820 0.3994 1.0558 -0.0492 -0.0555 0.1914  20  ARG A CZ  
111  N NH1 . ARG A 20  ? 0.4552 0.4796 1.1498 -0.0589 -0.0705 0.1854  20  ARG A NH1 
112  N NH2 . ARG A 20  ? 0.3824 0.3967 1.0228 -0.0507 -0.0643 0.2019  20  ARG A NH2 
113  N N   . TYR A 21  ? 0.4606 0.5023 1.2572 -0.0393 0.0610  0.1226  21  TYR A N   
114  C CA  . TYR A 21  ? 0.4214 0.4744 1.2385 -0.0369 0.0803  0.1084  21  TYR A CA  
115  C C   . TYR A 21  ? 0.4065 0.4824 1.2620 -0.0425 0.0686  0.0896  21  TYR A C   
116  O O   . TYR A 21  ? 0.4030 0.4957 1.2850 -0.0363 0.0701  0.0758  21  TYR A O   
117  C CB  . TYR A 21  ? 0.4028 0.4361 1.1858 -0.0429 0.1145  0.1086  21  TYR A CB  
118  C CG  . TYR A 21  ? 0.5425 0.5548 1.2917 -0.0541 0.1193  0.1130  21  TYR A CG  
119  N N   . TYR A 22  ? 0.3848 0.4622 1.2402 -0.0538 0.0556  0.0886  22  TYR A N   
120  C CA  . TYR A 22  ? 0.3883 0.4895 1.2786 -0.0587 0.0406  0.0728  22  TYR A CA  
121  C C   . TYR A 22  ? 0.5186 0.6317 1.4381 -0.0446 0.0106  0.0723  22  TYR A C   
122  O O   . TYR A 22  ? 0.5185 0.6507 1.4693 -0.0402 0.0044  0.0561  22  TYR A O   
123  C CB  . TYR A 22  ? 0.4004 0.5007 1.2792 -0.0745 0.0317  0.0743  22  TYR A CB  
124  N N   . GLU A 23  ? 0.3732 0.4725 1.2777 -0.0380 -0.0074 0.0896  23  GLU A N   
125  C CA  . GLU A 23  ? 0.3701 0.4703 1.2905 -0.0262 -0.0364 0.0918  23  GLU A CA  
126  C C   . GLU A 23  ? 0.3638 0.4604 1.2854 -0.0130 -0.0277 0.0881  23  GLU A C   
127  O O   . GLU A 23  ? 0.3811 0.4718 1.3064 -0.0049 -0.0485 0.0892  23  GLU A O   
128  C CB  . GLU A 23  ? 0.3691 0.4551 1.2676 -0.0286 -0.0606 0.1115  23  GLU A CB  
129  C CG  . GLU A 23  ? 0.4046 0.4966 1.3076 -0.0385 -0.0837 0.1130  23  GLU A CG  
130  C CD  . GLU A 23  ? 0.4904 0.5688 1.3599 -0.0465 -0.0989 0.1320  23  GLU A CD  
131  O OE1 . GLU A 23  ? 0.3815 0.4473 1.2259 -0.0436 -0.0905 0.1433  23  GLU A OE1 
132  O OE2 . GLU A 23  ? 0.4476 0.5298 1.3143 -0.0558 -0.1195 0.1353  23  GLU A OE2 
133  N N   . ARG A 24  ? 0.3846 0.4824 1.2972 -0.0131 0.0036  0.0838  24  ARG A N   
134  C CA  . ARG A 24  ? 0.3606 0.4586 1.2702 -0.0030 0.0168  0.0779  24  ARG A CA  
135  C C   . ARG A 24  ? 0.3396 0.4226 1.2205 0.0040  0.0143  0.0950  24  ARG A C   
136  O O   . ARG A 24  ? 0.4142 0.4978 1.2870 0.0111  0.0241  0.0908  24  ARG A O   
137  C CB  . ARG A 24  ? 0.5710 0.6800 1.5078 0.0037  0.0025  0.0598  24  ARG A CB  
138  N N   . LEU A 25  ? 0.2996 0.3720 1.1634 0.0009  0.0007  0.1131  25  LEU A N   
139  C CA  . LEU A 25  ? 0.2925 0.3544 1.1259 0.0065  -0.0010 0.1289  25  LEU A CA  
140  C C   . LEU A 25  ? 0.2882 0.3498 1.1016 0.0110  0.0312  0.1334  25  LEU A C   
141  O O   . LEU A 25  ? 0.2869 0.3469 1.0812 0.0187  0.0371  0.1349  25  LEU A O   
142  C CB  . LEU A 25  ? 0.2895 0.3436 1.1075 0.0004  -0.0192 0.1466  25  LEU A CB  
143  C CG  . LEU A 25  ? 0.2970 0.3461 1.1200 -0.0055 -0.0545 0.1501  25  LEU A CG  
144  C CD1 . LEU A 25  ? 0.3072 0.3636 1.1616 -0.0083 -0.0657 0.1360  25  LEU A CD1 
145  C CD2 . LEU A 25  ? 0.2945 0.3394 1.0972 -0.0150 -0.0644 0.1675  25  LEU A CD2 
146  N N   . GLY A 26  ? 0.4830 0.5404 1.2881 0.0032  0.0522  0.1352  26  GLY A N   
147  C CA  . GLY A 26  ? 0.3515 0.3978 1.1228 0.0063  0.0830  0.1393  26  GLY A CA  
148  C C   . GLY A 26  ? 0.3319 0.3884 1.1229 0.0022  0.1070  0.1241  26  GLY A C   
149  O O   . GLY A 26  ? 0.3355 0.4027 1.1558 -0.0057 0.1038  0.1087  26  GLY A O   
150  N N   . LEU A 27  ? 0.3936 0.4443 1.1581 0.0076  0.1305  0.1283  27  LEU A N   
151  C CA  . LEU A 27  ? 0.4833 0.5405 1.2543 0.0024  0.1566  0.1165  27  LEU A CA  
152  C C   . LEU A 27  ? 0.5865 0.6222 1.3351 -0.0103 0.1768  0.1190  27  LEU A C   
153  O O   . LEU A 27  ? 0.5712 0.5938 1.3125 -0.0155 0.1662  0.1247  27  LEU A O   
154  C CB  . LEU A 27  ? 0.5102 0.5685 1.2566 0.0124  0.1714  0.1233  27  LEU A CB  
155  N N   . ILE A 28  ? 0.6657 0.6973 1.4016 -0.0165 0.2020  0.1112  28  ILE A N   
156  C CA  . ILE A 28  ? 0.5268 0.5278 1.2222 -0.0249 0.2248  0.1177  28  ILE A CA  
157  C C   . ILE A 28  ? 0.8332 0.8320 1.5159 -0.0343 0.2507  0.1076  28  ILE A C   
158  O O   . ILE A 28  ? 0.8374 0.8604 1.5511 -0.0428 0.2506  0.0874  28  ILE A O   
159  C CB  . ILE A 28  ? 0.5494 0.5404 1.2472 -0.0365 0.2159  0.1129  28  ILE A CB  
160  C CG1 . ILE A 28  ? 0.6477 0.6026 1.2964 -0.0424 0.2370  0.1195  28  ILE A CG1 
161  C CG2 . ILE A 28  ? 0.5954 0.6133 1.3356 -0.0482 0.2092  0.0902  28  ILE A CG2 
162  C CD1 . ILE A 28  ? 0.6095 0.5522 1.2511 -0.0530 0.2293  0.1161  28  ILE A CD1 
163  N N   . PRO A 29  ? 0.7298 0.6994 1.3640 -0.0318 0.2715  0.1217  29  PRO A N   
164  C CA  . PRO A 29  ? 0.5451 0.5034 1.1532 -0.0410 0.2965  0.1180  29  PRO A CA  
165  C C   . PRO A 29  ? 0.8523 0.7785 1.4275 -0.0552 0.3127  0.1164  29  PRO A C   
166  O O   . PRO A 29  ? 0.9192 0.8236 1.4795 -0.0556 0.3076  0.1213  29  PRO A O   
167  C CB  . PRO A 29  ? 0.5799 0.5253 1.1512 -0.0258 0.3048  0.1381  29  PRO A CB  
168  C CG  . PRO A 29  ? 0.7017 0.6348 1.2620 -0.0112 0.2898  0.1544  29  PRO A CG  
169  C CD  . PRO A 29  ? 0.7475 0.6976 1.3490 -0.0159 0.2679  0.1441  29  PRO A CD  
170  N N   . GLU A 30  ? 0.7529 0.6765 1.3135 -0.0673 0.3322  0.1093  30  GLU A N   
171  C CA  . GLU A 30  ? 0.8351 0.7244 1.3551 -0.0810 0.3508  0.1102  30  GLU A CA  
172  C C   . GLU A 30  ? 0.7968 0.6582 1.2667 -0.0747 0.3674  0.1273  30  GLU A C   
173  O O   . GLU A 30  ? 0.8602 0.7405 1.3330 -0.0740 0.3735  0.1269  30  GLU A O   
174  C CB  . GLU A 30  ? 0.8130 0.7223 1.3549 -0.1045 0.3588  0.0867  30  GLU A CB  
175  N N   . PRO A 31  ? 0.7473 0.5653 1.1709 -0.0708 0.3744  0.1408  31  PRO A N   
176  C CA  . PRO A 31  ? 0.8104 0.6066 1.1904 -0.0625 0.3868  0.1577  31  PRO A CA  
177  C C   . PRO A 31  ? 0.8579 0.6452 1.2181 -0.0835 0.4055  0.1510  31  PRO A C   
178  O O   . PRO A 31  ? 0.8640 0.6236 1.2037 -0.0978 0.4140  0.1465  31  PRO A O   
179  C CB  . PRO A 31  ? 0.8778 0.6324 1.2174 -0.0482 0.3853  0.1734  31  PRO A CB  
180  N N   . GLU A 35  ? 0.8932 0.5618 1.1246 -0.0908 0.4349  0.1792  35  GLU A N   
181  C CA  . GLU A 35  ? 0.9245 0.5511 1.1294 -0.0867 0.4347  0.1833  35  GLU A CA  
182  C C   . GLU A 35  ? 0.9370 0.5759 1.1740 -0.0958 0.4269  0.1659  35  GLU A C   
183  O O   . GLU A 35  ? 0.9869 0.5955 1.2056 -0.1035 0.4305  0.1622  35  GLU A O   
184  C CB  . GLU A 35  ? 0.9253 0.5337 1.1073 -0.0562 0.4263  0.2031  35  GLU A CB  
185  N N   . LYS A 36  ? 0.8993 0.5840 1.1844 -0.0983 0.4173  0.1540  36  LYS A N   
186  C CA  . LYS A 36  ? 0.8199 0.5283 1.1452 -0.1050 0.4051  0.1381  36  LYS A CA  
187  C C   . LYS A 36  ? 0.7945 0.5002 1.1276 -0.0886 0.3886  0.1428  36  LYS A C   
188  O O   . LYS A 36  ? 0.7978 0.4984 1.1374 -0.0995 0.3848  0.1325  36  LYS A O   
189  C CB  . LYS A 36  ? 0.8524 0.5486 1.1726 -0.1319 0.4148  0.1222  36  LYS A CB  
190  N N   . GLY A 37  ? 0.8436 0.5585 1.1787 -0.0648 0.3782  0.1567  37  GLY A N   
191  C CA  . GLY A 37  ? 0.8448 0.5749 1.2015 -0.0528 0.3593  0.1576  37  GLY A CA  
192  C C   . GLY A 37  ? 0.7908 0.5659 1.2014 -0.0623 0.3491  0.1438  37  GLY A C   
193  O O   . GLY A 37  ? 0.7436 0.5317 1.1656 -0.0761 0.3593  0.1343  37  GLY A O   
194  N N   . TYR A 38  ? 0.8510 0.6526 1.2962 -0.0562 0.3292  0.1415  38  TYR A N   
195  C CA  . TYR A 38  ? 0.8018 0.6003 1.2424 -0.0418 0.3131  0.1506  38  TYR A CA  
196  C C   . TYR A 38  ? 0.8086 0.6025 1.2259 -0.0179 0.3114  0.1692  38  TYR A C   
197  O O   . TYR A 38  ? 0.8675 0.6341 1.2460 -0.0068 0.3165  0.1794  38  TYR A O   
198  C CB  . TYR A 38  ? 0.8580 0.6267 1.2723 -0.0494 0.3161  0.1475  38  TYR A CB  
199  N N   . ARG A 39  ? 0.6591 0.4830 1.1028 -0.0101 0.3032  0.1725  39  ARG A N   
200  C CA  . ARG A 39  ? 0.6761 0.5030 1.1010 0.0107  0.3013  0.1890  39  ARG A CA  
201  C C   . ARG A 39  ? 0.8699 0.7257 1.3224 0.0198  0.2792  0.1923  39  ARG A C   
202  O O   . ARG A 39  ? 0.8773 0.7282 1.3131 0.0301  0.2687  0.1994  39  ARG A O   
203  C CB  . ARG A 39  ? 0.6194 0.4530 1.0402 0.0109  0.3156  0.1923  39  ARG A CB  
204  N N   . MET A 40  ? 0.6592 0.5449 1.1535 0.0147  0.2719  0.1855  40  MET A N   
205  C CA  . MET A 40  ? 0.6611 0.5734 1.1846 0.0211  0.2501  0.1882  40  MET A CA  
206  C C   . MET A 40  ? 0.5746 0.4981 1.0843 0.0373  0.2505  0.2024  40  MET A C   
207  O O   . MET A 40  ? 0.6130 0.5243 1.0840 0.0511  0.2526  0.2152  40  MET A O   
208  C CB  . MET A 40  ? 0.5730 0.4802 1.0915 0.0223  0.2314  0.1898  40  MET A CB  
209  C CG  . MET A 40  ? 0.5684 0.4628 1.0918 0.0066  0.2311  0.1778  40  MET A CG  
210  S SD  . MET A 40  ? 0.7708 0.6933 1.3525 -0.0089 0.2103  0.1623  40  MET A SD  
211  C CE  . MET A 40  ? 0.5241 0.4260 1.0897 -0.0244 0.2133  0.1535  40  MET A CE  
212  N N   . GLN A 43  ? 0.4063 0.3752 0.8826 0.0754  0.2341  0.2316  43  GLN A N   
213  C CA  . GLN A 43  ? 0.3963 0.3780 0.8532 0.0891  0.2215  0.2429  43  GLN A CA  
214  C C   . GLN A 43  ? 0.4920 0.5010 0.9762 0.0862  0.1984  0.2339  43  GLN A C   
215  O O   . GLN A 43  ? 0.5412 0.5564 1.0169 0.0906  0.1817  0.2393  43  GLN A O   
216  C CB  . GLN A 43  ? 0.4183 0.4074 0.8455 0.1013  0.2358  0.2554  43  GLN A CB  
217  C CG  . GLN A 43  ? 0.4004 0.4094 0.8071 0.1153  0.2243  0.2662  43  GLN A CG  
218  C CD  . GLN A 43  ? 0.5915 0.5922 0.9710 0.1216  0.2169  0.2695  43  GLN A CD  
219  O OE1 . GLN A 43  ? 0.6287 0.6084 0.9850 0.1257  0.2283  0.2711  43  GLN A OE1 
220  N NE2 . GLN A 43  ? 0.5882 0.6074 0.9666 0.1213  0.1976  0.2679  43  GLN A NE2 
221  N N   . GLN A 44  ? 0.8196 0.7558 0.7260 0.0838  -0.0397 0.2586  44  GLN A N   
222  C CA  . GLN A 44  ? 0.5478 0.5146 0.4584 0.0806  -0.0454 0.2408  44  GLN A CA  
223  C C   . GLN A 44  ? 0.5767 0.5438 0.5171 0.0648  -0.0362 0.2331  44  GLN A C   
224  O O   . GLN A 44  ? 0.6389 0.6239 0.5913 0.0603  -0.0419 0.2177  44  GLN A O   
225  C CB  . GLN A 44  ? 0.5600 0.5434 0.4436 0.0796  -0.0408 0.2439  44  GLN A CB  
226  C CG  . GLN A 44  ? 0.8052 0.7815 0.6545 0.0906  -0.0441 0.2591  44  GLN A CG  
227  N N   . THR A 45  ? 0.5385 0.4837 0.4901 0.0554  -0.0223 0.2440  45  THR A N   
228  C CA  . THR A 45  ? 0.5808 0.5251 0.5623 0.0391  -0.0141 0.2376  45  THR A CA  
229  C C   . THR A 45  ? 0.5420 0.4812 0.5474 0.0414  -0.0231 0.2287  45  THR A C   
230  O O   . THR A 45  ? 0.4554 0.4039 0.4813 0.0303  -0.0246 0.2175  45  THR A O   
231  C CB  . THR A 45  ? 0.5398 0.4629 0.5284 0.0260  0.0049  0.2498  45  THR A CB  
232  O OG1 . THR A 45  ? 0.5650 0.4974 0.5340 0.0221  0.0150  0.2581  45  THR A OG1 
233  C CG2 . THR A 45  ? 0.5021 0.4273 0.5230 0.0079  0.0119  0.2406  45  THR A CG2 
234  N N   . VAL A 46  ? 0.5007 0.4261 0.5035 0.0563  -0.0301 0.2343  46  VAL A N   
235  C CA  . VAL A 46  ? 0.4864 0.4103 0.5163 0.0612  -0.0387 0.2263  46  VAL A CA  
236  C C   . VAL A 46  ? 0.5419 0.4949 0.5752 0.0621  -0.0521 0.2106  46  VAL A C   
237  O O   . VAL A 46  ? 0.4514 0.4096 0.5099 0.0509  -0.0537 0.2010  46  VAL A O   
238  C CB  . VAL A 46  ? 0.5385 0.4463 0.5652 0.0818  -0.0466 0.2348  46  VAL A CB  
239  C CG1 . VAL A 46  ? 0.5077 0.4226 0.5687 0.0899  -0.0574 0.2237  46  VAL A CG1 
240  C CG2 . VAL A 46  ? 0.5668 0.4387 0.5920 0.0787  -0.0325 0.2505  46  VAL A CG2 
241  N N   . ASP A 47  ? 0.4794 0.4495 0.4862 0.0729  -0.0613 0.2078  47  ASP A N   
242  C CA  . ASP A 47  ? 0.4870 0.4834 0.4939 0.0728  -0.0727 0.1919  47  ASP A CA  
243  C C   . ASP A 47  ? 0.5318 0.5326 0.5445 0.0538  -0.0659 0.1851  47  ASP A C   
244  O O   . ASP A 47  ? 0.3950 0.4032 0.4239 0.0456  -0.0719 0.1752  47  ASP A O   
245  C CB  . ASP A 47  ? 0.4918 0.5037 0.4686 0.0845  -0.0811 0.1893  47  ASP A CB  
246  C CG  . ASP A 47  ? 0.5786 0.5901 0.5470 0.1041  -0.0933 0.1943  47  ASP A CG  
247  O OD1 . ASP A 47  ? 0.7464 0.7651 0.6877 0.1114  -0.0986 0.1972  47  ASP A OD1 
248  O OD2 . ASP A 47  ? 0.6070 0.6127 0.5969 0.1126  -0.0988 0.1952  47  ASP A OD2 
249  N N   . ARG A 48  ? 0.4366 0.4326 0.4375 0.0467  -0.0546 0.1913  48  ARG A N   
250  C CA  . ARG A 48  ? 0.4117 0.4148 0.4171 0.0329  -0.0515 0.1842  48  ARG A CA  
251  C C   . ARG A 48  ? 0.4149 0.4090 0.4455 0.0177  -0.0494 0.1820  48  ARG A C   
252  O O   . ARG A 48  ? 0.3743 0.3736 0.4081 0.0082  -0.0546 0.1711  48  ARG A O   
253  C CB  . ARG A 48  ? 0.4988 0.5042 0.4936 0.0299  -0.0405 0.1924  48  ARG A CB  
254  C CG  . ARG A 48  ? 0.5180 0.5350 0.5171 0.0206  -0.0400 0.1860  48  ARG A CG  
255  C CD  . ARG A 48  ? 0.5528 0.5798 0.5421 0.0222  -0.0306 0.1955  48  ARG A CD  
256  N NE  . ARG A 48  ? 0.6542 0.6962 0.6505 0.0169  -0.0310 0.1924  48  ARG A NE  
257  C CZ  . ARG A 48  ? 0.5625 0.6191 0.5473 0.0249  -0.0364 0.1862  48  ARG A CZ  
258  N NH1 . ARG A 48  ? 0.4978 0.5574 0.4631 0.0359  -0.0414 0.1810  48  ARG A NH1 
259  N NH2 . ARG A 48  ? 0.5666 0.6348 0.5614 0.0221  -0.0373 0.1812  48  ARG A NH2 
260  N N   . LEU A 49  ? 0.5710 0.5483 0.6173 0.0147  -0.0415 0.1904  49  LEU A N   
261  C CA  . LEU A 49  ? 0.4305 0.3986 0.5006 -0.0017 -0.0371 0.1816  49  LEU A CA  
262  C C   . LEU A 49  ? 0.3813 0.3534 0.4617 -0.0026 -0.0451 0.1626  49  LEU A C   
263  O O   . LEU A 49  ? 0.4614 0.4357 0.5484 -0.0186 -0.0439 0.1469  49  LEU A O   
264  C CB  . LEU A 49  ? 0.5121 0.4584 0.5985 -0.0049 -0.0244 0.1926  49  LEU A CB  
265  C CG  . LEU A 49  ? 0.4585 0.3973 0.5690 -0.0247 -0.0161 0.1779  49  LEU A CG  
266  C CD1 . LEU A 49  ? 0.3472 0.3027 0.4535 -0.0401 -0.0162 0.1687  49  LEU A CD1 
267  C CD2 . LEU A 49  ? 0.4843 0.3989 0.6097 -0.0283 -0.0013 0.1899  49  LEU A CD2 
268  N N   . HIS A 50  ? 0.4038 0.3798 0.4844 0.0138  -0.0532 0.1632  50  HIS A N   
269  C CA  . HIS A 50  ? 0.3841 0.3716 0.4756 0.0122  -0.0604 0.1419  50  HIS A CA  
270  C C   . HIS A 50  ? 0.3995 0.3983 0.4752 0.0012  -0.0641 0.1298  50  HIS A C   
271  O O   . HIS A 50  ? 0.3731 0.3725 0.4544 -0.0143 -0.0621 0.1129  50  HIS A O   
272  C CB  . HIS A 50  ? 0.4163 0.4159 0.5094 0.0336  -0.0718 0.1425  50  HIS A CB  
273  C CG  . HIS A 50  ? 0.5389 0.5272 0.6548 0.0462  -0.0714 0.1473  50  HIS A CG  
274  N ND1 . HIS A 50  ? 0.5616 0.5436 0.7072 0.0370  -0.0650 0.1309  50  HIS A ND1 
275  C CD2 . HIS A 50  ? 0.5270 0.5081 0.6394 0.0688  -0.0770 0.1666  50  HIS A CD2 
276  C CE1 . HIS A 50  ? 0.5889 0.5585 0.7524 0.0543  -0.0663 0.1392  50  HIS A CE1 
277  N NE2 . HIS A 50  ? 0.5312 0.4986 0.6736 0.0744  -0.0744 0.1625  50  HIS A NE2 
278  N N   . PHE A 51  ? 0.3443 0.3504 0.3984 0.0096  -0.0687 0.1387  51  PHE A N   
279  C CA  . PHE A 51  ? 0.3327 0.3453 0.3713 0.0031  -0.0728 0.1288  51  PHE A CA  
280  C C   . PHE A 51  ? 0.3492 0.3516 0.3875 -0.0149 -0.0673 0.1251  51  PHE A C   
281  O O   . PHE A 51  ? 0.3309 0.3306 0.3640 -0.0265 -0.0689 0.1119  51  PHE A O   
282  C CB  . PHE A 51  ? 0.3331 0.3542 0.3512 0.0159  -0.0762 0.1393  51  PHE A CB  
283  C CG  . PHE A 51  ? 0.3864 0.4109 0.3901 0.0121  -0.0801 0.1285  51  PHE A CG  
284  C CD1 . PHE A 51  ? 0.3865 0.4096 0.3917 0.0028  -0.0833 0.1104  51  PHE A CD1 
285  C CD2 . PHE A 51  ? 0.3551 0.3828 0.3448 0.0176  -0.0789 0.1357  51  PHE A CD2 
286  C CE1 . PHE A 51  ? 0.3473 0.3661 0.3384 -0.0010 -0.0855 0.1018  51  PHE A CE1 
287  C CE2 . PHE A 51  ? 0.4009 0.4276 0.3796 0.0162  -0.0824 0.1252  51  PHE A CE2 
288  C CZ  . PHE A 51  ? 0.3731 0.3924 0.3516 0.0071  -0.0858 0.1094  51  PHE A CZ  
289  N N   . ILE A 52  ? 0.3186 0.3155 0.3618 -0.0181 -0.0607 0.1364  52  ILE A N   
290  C CA  . ILE A 52  ? 0.5028 0.4962 0.5449 -0.0329 -0.0583 0.1333  52  ILE A CA  
291  C C   . ILE A 52  ? 0.3758 0.3633 0.4275 -0.0487 -0.0555 0.1190  52  ILE A C   
292  O O   . ILE A 52  ? 0.3895 0.3741 0.4294 -0.0604 -0.0581 0.1105  52  ILE A O   
293  C CB  . ILE A 52  ? 0.3233 0.3183 0.3737 -0.0342 -0.0510 0.1454  52  ILE A CB  
294  C CG1 . ILE A 52  ? 0.3291 0.3335 0.3676 -0.0215 -0.0519 0.1565  52  ILE A CG1 
295  C CG2 . ILE A 52  ? 0.3066 0.3035 0.3612 -0.0500 -0.0502 0.1388  52  ILE A CG2 
296  C CD1 . ILE A 52  ? 0.3972 0.4047 0.4451 -0.0227 -0.0413 0.1686  52  ILE A CD1 
297  N N   . LYS A 53  ? 0.3278 0.3119 0.3993 -0.0483 -0.0498 0.1165  53  LYS A N   
298  C CA  . LYS A 53  ? 0.3339 0.3152 0.4187 -0.0624 -0.0448 0.0999  53  LYS A CA  
299  C C   . LYS A 53  ? 0.4423 0.4277 0.5174 -0.0690 -0.0483 0.0848  53  LYS A C   
300  O O   . LYS A 53  ? 0.3971 0.3799 0.4644 -0.0870 -0.0452 0.0735  53  LYS A O   
301  C CB  . LYS A 53  ? 0.4076 0.3842 0.5184 -0.0543 -0.0395 0.0992  53  LYS A CB  
302  C CG  . LYS A 53  ? 0.3335 0.3095 0.4647 -0.0667 -0.0326 0.0785  53  LYS A CG  
303  C CD  . LYS A 53  ? 0.5394 0.5110 0.6729 -0.0872 -0.0244 0.0712  53  LYS A CD  
304  C CE  . LYS A 53  ? 0.6477 0.6202 0.8018 -0.0993 -0.0157 0.0482  53  LYS A CE  
305  N NZ  . LYS A 53  ? 0.6851 0.6549 0.8665 -0.0813 -0.0150 0.0463  53  LYS A NZ  
306  N N   . ARG A 54  ? 0.4383 0.4310 0.5124 -0.0561 -0.0541 0.0838  54  ARG A N   
307  C CA  . ARG A 54  ? 0.3479 0.3457 0.4179 -0.0650 -0.0548 0.0664  54  ARG A CA  
308  C C   . ARG A 54  ? 0.3659 0.3540 0.4074 -0.0748 -0.0572 0.0683  54  ARG A C   
309  O O   . ARG A 54  ? 0.4234 0.4058 0.4551 -0.0922 -0.0530 0.0561  54  ARG A O   
310  C CB  . ARG A 54  ? 0.3691 0.3823 0.4502 -0.0496 -0.0611 0.0607  54  ARG A CB  
311  C CG  . ARG A 54  ? 0.4578 0.4790 0.5700 -0.0417 -0.0590 0.0540  54  ARG A CG  
312  C CD  . ARG A 54  ? 0.5458 0.5824 0.6677 -0.0183 -0.0692 0.0574  54  ARG A CD  
313  N NE  . ARG A 54  ? 0.6264 0.6623 0.7750 -0.0040 -0.0691 0.0608  54  ARG A NE  
314  C CZ  . ARG A 54  ? 0.5924 0.6343 0.7445 0.0206  -0.0791 0.0733  54  ARG A CZ  
315  N NH1 . ARG A 54  ? 0.5385 0.5922 0.6690 0.0311  -0.0890 0.0805  54  ARG A NH1 
316  N NH2 . ARG A 54  ? 0.6651 0.7006 0.8407 0.0352  -0.0794 0.0781  54  ARG A NH2 
317  N N   . MET A 55  ? 0.2988 0.2833 0.3263 -0.0647 -0.0627 0.0837  55  MET A N   
318  C CA  . MET A 55  ? 0.3747 0.3467 0.3771 -0.0714 -0.0660 0.0862  55  MET A CA  
319  C C   . MET A 55  ? 0.4572 0.4197 0.4507 -0.0892 -0.0627 0.0848  55  MET A C   
320  O O   . MET A 55  ? 0.4339 0.3827 0.4059 -0.1016 -0.0627 0.0811  55  MET A O   
321  C CB  . MET A 55  ? 0.3059 0.2793 0.3004 -0.0559 -0.0719 0.1006  55  MET A CB  
322  C CG  . MET A 55  ? 0.3254 0.3053 0.3163 -0.0420 -0.0760 0.0984  55  MET A CG  
323  S SD  . MET A 55  ? 0.7098 0.6878 0.6861 -0.0286 -0.0812 0.1083  55  MET A SD  
324  C CE  . MET A 55  ? 0.3272 0.3192 0.3170 -0.0207 -0.0777 0.1236  55  MET A CE  
325  N N   . GLN A 56  ? 0.3490 0.3181 0.3574 -0.0914 -0.0593 0.0874  56  GLN A N   
326  C CA  . GLN A 56  ? 0.4443 0.4099 0.4447 -0.1089 -0.0567 0.0829  56  GLN A CA  
327  C C   . GLN A 56  ? 0.5586 0.5216 0.5578 -0.1269 -0.0483 0.0654  56  GLN A C   
328  O O   . GLN A 56  ? 0.4381 0.3937 0.4152 -0.1438 -0.0469 0.0613  56  GLN A O   
329  C CB  . GLN A 56  ? 0.3179 0.2929 0.3381 -0.1092 -0.0536 0.0857  56  GLN A CB  
330  C CG  . GLN A 56  ? 0.3603 0.3402 0.3742 -0.1020 -0.0609 0.0986  56  GLN A CG  
331  C CD  . GLN A 56  ? 0.4767 0.4673 0.5140 -0.1037 -0.0555 0.1000  56  GLN A CD  
332  O OE1 . GLN A 56  ? 0.5231 0.5142 0.5789 -0.0944 -0.0496 0.1054  56  GLN A OE1 
333  N NE2 . GLN A 56  ? 0.5130 0.5114 0.5485 -0.1167 -0.0570 0.0947  56  GLN A NE2 
334  N N   . GLU A 57  ? 0.4722 0.4431 0.4942 -0.1231 -0.0429 0.0547  57  GLU A N   
335  C CA  . GLU A 57  ? 0.3930 0.3665 0.4189 -0.1400 -0.0334 0.0346  57  GLU A CA  
336  C C   . GLU A 57  ? 0.4062 0.3691 0.4059 -0.1493 -0.0334 0.0314  57  GLU A C   
337  O O   . GLU A 57  ? 0.4285 0.3890 0.4194 -0.1695 -0.0238 0.0170  57  GLU A O   
338  C CB  . GLU A 57  ? 0.4091 0.3975 0.4717 -0.1302 -0.0293 0.0227  57  GLU A CB  
339  C CG  . GLU A 57  ? 0.4462 0.4367 0.5340 -0.1223 -0.0269 0.0263  57  GLU A CG  
340  C CD  . GLU A 57  ? 0.4695 0.4697 0.5921 -0.1064 -0.0260 0.0196  57  GLU A CD  
341  O OE1 . GLU A 57  ? 0.3978 0.4076 0.5239 -0.0945 -0.0322 0.0180  57  GLU A OE1 
342  O OE2 . GLU A 57  ? 0.5905 0.5885 0.7376 -0.1050 -0.0198 0.0154  57  GLU A OE2 
343  N N   . LEU A 58  ? 0.3385 0.2936 0.3254 -0.1360 -0.0425 0.0441  58  LEU A N   
344  C CA  . LEU A 58  ? 0.3479 0.2866 0.3100 -0.1441 -0.0422 0.0423  58  LEU A CA  
345  C C   . LEU A 58  ? 0.4588 0.3723 0.3838 -0.1495 -0.0472 0.0573  58  LEU A C   
346  O O   . LEU A 58  ? 0.3956 0.2875 0.2973 -0.1537 -0.0476 0.0598  58  LEU A O   
347  C CB  . LEU A 58  ? 0.4084 0.3534 0.3801 -0.1265 -0.0485 0.0429  58  LEU A CB  
348  C CG  . LEU A 58  ? 0.4395 0.4094 0.4432 -0.1237 -0.0447 0.0252  58  LEU A CG  
349  C CD1 . LEU A 58  ? 0.4294 0.4122 0.4424 -0.1044 -0.0532 0.0253  58  LEU A CD1 
350  C CD2 . LEU A 58  ? 0.3747 0.3451 0.3789 -0.1474 -0.0325 0.0040  58  LEU A CD2 
351  N N   . GLY A 59  ? 0.4203 0.3364 0.3409 -0.1481 -0.0519 0.0671  59  GLY A N   
352  C CA  . GLY A 59  ? 0.3766 0.2732 0.2630 -0.1515 -0.0594 0.0807  59  GLY A CA  
353  C C   . GLY A 59  ? 0.3732 0.2674 0.2577 -0.1298 -0.0728 0.0972  59  GLY A C   
354  O O   . GLY A 59  ? 0.5011 0.3784 0.3589 -0.1281 -0.0816 0.1089  59  GLY A O   
355  N N   . PHE A 60  ? 0.3648 0.2757 0.2760 -0.1122 -0.0748 0.0984  60  PHE A N   
356  C CA  . PHE A 60  ? 0.3612 0.2763 0.2742 -0.0935 -0.0852 0.1113  60  PHE A CA  
357  C C   . PHE A 60  ? 0.3530 0.2863 0.2766 -0.0945 -0.0884 0.1153  60  PHE A C   
358  O O   . PHE A 60  ? 0.3365 0.2849 0.2811 -0.1007 -0.0810 0.1086  60  PHE A O   
359  C CB  . PHE A 60  ? 0.3404 0.2692 0.2743 -0.0759 -0.0848 0.1118  60  PHE A CB  
360  C CG  . PHE A 60  ? 0.3473 0.2649 0.2748 -0.0725 -0.0833 0.1054  60  PHE A CG  
361  C CD1 . PHE A 60  ? 0.4837 0.3913 0.4021 -0.0590 -0.0892 0.1098  60  PHE A CD1 
362  C CD2 . PHE A 60  ? 0.3427 0.2638 0.2780 -0.0820 -0.0759 0.0921  60  PHE A CD2 
363  C CE1 . PHE A 60  ? 0.3661 0.2652 0.2810 -0.0570 -0.0870 0.1006  60  PHE A CE1 
364  C CE2 . PHE A 60  ? 0.3492 0.2655 0.2821 -0.0800 -0.0748 0.0830  60  PHE A CE2 
365  C CZ  . PHE A 60  ? 0.3612 0.2658 0.2830 -0.0684 -0.0801 0.0870  60  PHE A CZ  
366  N N   . THR A 61  ? 0.3583 0.2909 0.2703 -0.0878 -0.0995 0.1246  61  THR A N   
367  C CA  . THR A 61  ? 0.3867 0.3437 0.3144 -0.0873 -0.1036 0.1259  61  THR A CA  
368  C C   . THR A 61  ? 0.4186 0.3963 0.3760 -0.0725 -0.1012 0.1285  61  THR A C   
369  O O   . THR A 61  ? 0.3823 0.3557 0.3419 -0.0586 -0.1006 0.1318  61  THR A O   
370  C CB  . THR A 61  ? 0.3741 0.3307 0.2826 -0.0830 -0.1190 0.1337  61  THR A CB  
371  O OG1 . THR A 61  ? 0.3759 0.3314 0.2896 -0.0608 -0.1253 0.1393  61  THR A OG1 
372  C CG2 . THR A 61  ? 0.4092 0.3397 0.2783 -0.0960 -0.1224 0.1361  61  THR A CG2 
373  N N   . LEU A 62  ? 0.4682 0.4685 0.4470 -0.0773 -0.0987 0.1258  62  LEU A N   
374  C CA  . LEU A 62  ? 0.4656 0.4859 0.4715 -0.0677 -0.0935 0.1286  62  LEU A CA  
375  C C   . LEU A 62  ? 0.3643 0.3925 0.3699 -0.0492 -0.1023 0.1350  62  LEU A C   
376  O O   . LEU A 62  ? 0.3270 0.3618 0.3435 -0.0381 -0.0964 0.1381  62  LEU A O   
377  C CB  . LEU A 62  ? 0.3282 0.3701 0.3555 -0.0797 -0.0899 0.1226  62  LEU A CB  
378  C CG  . LEU A 62  ? 0.4551 0.4931 0.5005 -0.0908 -0.0744 0.1175  62  LEU A CG  
379  C CD1 . LEU A 62  ? 0.5459 0.6019 0.6121 -0.1060 -0.0699 0.1081  62  LEU A CD1 
380  C CD2 . LEU A 62  ? 0.4291 0.4642 0.4862 -0.0787 -0.0652 0.1262  62  LEU A CD2 
381  N N   . ASN A 63  ? 0.3569 0.3848 0.3490 -0.0453 -0.1164 0.1367  63  ASN A N   
382  C CA  . ASN A 63  ? 0.3634 0.3970 0.3572 -0.0253 -0.1261 0.1410  63  ASN A CA  
383  C C   . ASN A 63  ? 0.4317 0.4402 0.4116 -0.0139 -0.1218 0.1413  63  ASN A C   
384  O O   . ASN A 63  ? 0.4558 0.4738 0.4474 0.0006  -0.1191 0.1411  63  ASN A O   
385  C CB  . ASN A 63  ? 0.4395 0.4729 0.4191 -0.0215 -0.1430 0.1429  63  ASN A CB  
386  C CG  . ASN A 63  ? 0.6302 0.6818 0.6253 0.0003  -0.1512 0.1416  63  ASN A CG  
387  O OD1 . ASN A 63  ? 0.7781 0.8086 0.7569 0.0162  -0.1557 0.1410  63  ASN A OD1 
388  N ND2 . ASN A 63  ? 0.4513 0.5435 0.4810 0.0009  -0.1500 0.1384  63  ASN A ND2 
389  N N   . GLU A 64  ? 0.3781 0.3574 0.3343 -0.0223 -0.1191 0.1386  64  GLU A N   
390  C CA  . GLU A 64  ? 0.3828 0.3413 0.3286 -0.0164 -0.1135 0.1351  64  GLU A CA  
391  C C   . GLU A 64  ? 0.3759 0.3484 0.3375 -0.0134 -0.1050 0.1343  64  GLU A C   
392  O O   . GLU A 64  ? 0.4515 0.4248 0.4144 -0.0002 -0.1042 0.1328  64  GLU A O   
393  C CB  . GLU A 64  ? 0.3978 0.3286 0.3202 -0.0320 -0.1115 0.1331  64  GLU A CB  
394  C CG  . GLU A 64  ? 0.4293 0.3414 0.3292 -0.0331 -0.1187 0.1361  64  GLU A CG  
395  C CD  . GLU A 64  ? 0.5714 0.4536 0.4438 -0.0509 -0.1148 0.1351  64  GLU A CD  
396  O OE1 . GLU A 64  ? 0.4578 0.3416 0.3308 -0.0680 -0.1080 0.1313  64  GLU A OE1 
397  O OE2 . GLU A 64  ? 0.7317 0.5879 0.5818 -0.0478 -0.1180 0.1387  64  GLU A OE2 
398  N N   . ILE A 65  ? 0.3894 0.3731 0.3623 -0.0249 -0.0995 0.1365  65  ILE A N   
399  C CA  . ILE A 65  ? 0.3554 0.3501 0.3406 -0.0208 -0.0906 0.1372  65  ILE A CA  
400  C C   . ILE A 65  ? 0.4050 0.4219 0.4046 -0.0083 -0.0878 0.1416  65  ILE A C   
401  O O   . ILE A 65  ? 0.3507 0.3742 0.3505 0.0010  -0.0825 0.1426  65  ILE A O   
402  C CB  . ILE A 65  ? 0.3453 0.3429 0.3418 -0.0340 -0.0827 0.1359  65  ILE A CB  
403  C CG1 . ILE A 65  ? 0.4176 0.3980 0.4028 -0.0448 -0.0822 0.1280  65  ILE A CG1 
404  C CG2 . ILE A 65  ? 0.3372 0.3458 0.3473 -0.0275 -0.0737 0.1409  65  ILE A CG2 
405  C CD1 . ILE A 65  ? 0.3760 0.3586 0.3751 -0.0573 -0.0746 0.1232  65  ILE A CD1 
406  N N   . ASP A 66  ? 0.3803 0.4119 0.3915 -0.0088 -0.0912 0.1428  66  ASP A N   
407  C CA  . ASP A 66  ? 0.4148 0.4722 0.4439 0.0005  -0.0872 0.1439  66  ASP A CA  
408  C C   . ASP A 66  ? 0.3835 0.4396 0.4053 0.0179  -0.0909 0.1413  66  ASP A C   
409  O O   . ASP A 66  ? 0.3719 0.4390 0.3957 0.0254  -0.0820 0.1412  66  ASP A O   
410  C CB  . ASP A 66  ? 0.4927 0.5690 0.5376 -0.0038 -0.0936 0.1416  66  ASP A CB  
411  C CG  . ASP A 66  ? 0.4766 0.5863 0.5484 -0.0013 -0.0851 0.1399  66  ASP A CG  
412  O OD1 . ASP A 66  ? 0.5790 0.7073 0.6692 -0.0122 -0.0845 0.1362  66  ASP A OD1 
413  O OD2 . ASP A 66  ? 0.4818 0.6012 0.5569 0.0096  -0.0779 0.1402  66  ASP A OD2 
414  N N   . LYS A 67  ? 0.4051 0.4438 0.4148 0.0239  -0.1033 0.1392  67  LYS A N   
415  C CA  . LYS A 67  ? 0.4508 0.4824 0.4551 0.0406  -0.1069 0.1345  67  LYS A CA  
416  C C   . LYS A 67  ? 0.3962 0.4175 0.3879 0.0412  -0.0993 0.1305  67  LYS A C   
417  O O   . LYS A 67  ? 0.3959 0.4320 0.3917 0.0516  -0.0932 0.1256  67  LYS A O   
418  C CB  . LYS A 67  ? 0.4526 0.4562 0.4415 0.0452  -0.1202 0.1347  67  LYS A CB  
419  C CG  . LYS A 67  ? 0.5890 0.6044 0.5860 0.0472  -0.1296 0.1362  67  LYS A CG  
420  C CD  . LYS A 67  ? 0.5881 0.5701 0.5594 0.0475  -0.1368 0.1364  67  LYS A CD  
421  C CE  . LYS A 67  ? 0.6916 0.6811 0.6699 0.0666  -0.1498 0.1371  67  LYS A CE  
422  N NZ  . LYS A 67  ? 0.7010 0.7281 0.7001 0.0648  -0.1570 0.1368  67  LYS A NZ  
423  N N   . LEU A 68  ? 0.3767 0.3765 0.3536 0.0292  -0.0997 0.1307  68  LEU A N   
424  C CA  . LEU A 68  ? 0.3738 0.3656 0.3399 0.0284  -0.0954 0.1243  68  LEU A CA  
425  C C   . LEU A 68  ? 0.4302 0.4475 0.4029 0.0336  -0.0868 0.1257  68  LEU A C   
426  O O   . LEU A 68  ? 0.3873 0.4105 0.3537 0.0426  -0.0847 0.1187  68  LEU A O   
427  C CB  . LEU A 68  ? 0.4120 0.3867 0.3695 0.0123  -0.0955 0.1234  68  LEU A CB  
428  C CG  . LEU A 68  ? 0.5185 0.4896 0.4701 0.0072  -0.0923 0.1147  68  LEU A CG  
429  C CD1 . LEU A 68  ? 0.6655 0.6155 0.6092 -0.0094 -0.0929 0.1114  68  LEU A CD1 
430  C CD2 . LEU A 68  ? 0.4089 0.4017 0.3701 0.0088  -0.0872 0.1183  68  LEU A CD2 
431  N N   . LEU A 69  ? 0.4306 0.4612 0.4139 0.0274  -0.0811 0.1348  69  LEU A N   
432  C CA  . LEU A 69  ? 0.4609 0.5097 0.4460 0.0312  -0.0717 0.1407  69  LEU A CA  
433  C C   . LEU A 69  ? 0.5006 0.5691 0.4886 0.0426  -0.0669 0.1383  69  LEU A C   
434  O O   . LEU A 69  ? 0.3997 0.4805 0.3782 0.0489  -0.0606 0.1389  69  LEU A O   
435  C CB  . LEU A 69  ? 0.4528 0.5062 0.4506 0.0212  -0.0646 0.1513  69  LEU A CB  
436  C CG  . LEU A 69  ? 0.5224 0.5619 0.5207 0.0118  -0.0647 0.1540  69  LEU A CG  
437  C CD1 . LEU A 69  ? 0.3866 0.4286 0.4009 0.0023  -0.0556 0.1627  69  LEU A CD1 
438  C CD2 . LEU A 69  ? 0.4399 0.4778 0.4261 0.0190  -0.0647 0.1519  69  LEU A CD2 
439  N N   . GLY A 70  ? 0.4080 0.4824 0.4092 0.0459  -0.0701 0.1348  70  GLY A N   
440  C CA  . GLY A 70  ? 0.4315 0.5278 0.4400 0.0579  -0.0647 0.1286  70  GLY A CA  
441  C C   . GLY A 70  ? 0.4562 0.5464 0.4498 0.0689  -0.0667 0.1169  70  GLY A C   
442  O O   . GLY A 70  ? 0.4640 0.5724 0.4506 0.0748  -0.0578 0.1130  70  GLY A O   
443  N N   . VAL A 71  ? 0.4146 0.4779 0.4009 0.0697  -0.0773 0.1107  71  VAL A N   
444  C CA  . VAL A 71  ? 0.4518 0.5049 0.4264 0.0777  -0.0789 0.0966  71  VAL A CA  
445  C C   . VAL A 71  ? 0.4530 0.5147 0.4114 0.0744  -0.0743 0.0941  71  VAL A C   
446  O O   . VAL A 71  ? 0.4693 0.5490 0.4211 0.0824  -0.0686 0.0850  71  VAL A O   
447  C CB  . VAL A 71  ? 0.4494 0.4656 0.4172 0.0751  -0.0889 0.0922  71  VAL A CB  
448  C CG1 . VAL A 71  ? 0.4539 0.4573 0.4116 0.0802  -0.0884 0.0754  71  VAL A CG1 
449  C CG2 . VAL A 71  ? 0.4230 0.4306 0.4026 0.0828  -0.0964 0.0958  71  VAL A CG2 
450  N N   . VAL A 72  ? 0.4360 0.4880 0.3885 0.0636  -0.0771 0.1012  72  VAL A N   
451  C CA  . VAL A 72  ? 0.5276 0.5887 0.4667 0.0627  -0.0767 0.0985  72  VAL A CA  
452  C C   . VAL A 72  ? 0.4262 0.5139 0.3587 0.0686  -0.0685 0.1079  72  VAL A C   
453  O O   . VAL A 72  ? 0.4378 0.5404 0.3547 0.0747  -0.0679 0.1015  72  VAL A O   
454  C CB  . VAL A 72  ? 0.4284 0.4770 0.3686 0.0515  -0.0813 0.1036  72  VAL A CB  
455  C CG1 . VAL A 72  ? 0.4492 0.5121 0.3792 0.0542  -0.0837 0.0993  72  VAL A CG1 
456  C CG2 . VAL A 72  ? 0.3690 0.3909 0.3104 0.0427  -0.0866 0.0944  72  VAL A CG2 
457  N N   . ASP A 73  ? 0.4322 0.5261 0.3746 0.0656  -0.0615 0.1228  73  ASP A N   
458  C CA  . ASP A 73  ? 0.5022 0.6171 0.4354 0.0690  -0.0504 0.1333  73  ASP A CA  
459  C C   . ASP A 73  ? 0.4964 0.6318 0.4228 0.0782  -0.0439 0.1212  73  ASP A C   
460  O O   . ASP A 73  ? 0.4839 0.6358 0.3900 0.0821  -0.0376 0.1244  73  ASP A O   
461  C CB  . ASP A 73  ? 0.4331 0.5503 0.3817 0.0611  -0.0409 0.1486  73  ASP A CB  
462  C CG  . ASP A 73  ? 0.5224 0.6227 0.4737 0.0526  -0.0430 0.1620  73  ASP A CG  
463  O OD1 . ASP A 73  ? 0.4921 0.5846 0.4312 0.0553  -0.0504 0.1626  73  ASP A OD1 
464  O OD2 . ASP A 73  ? 0.6085 0.7057 0.5770 0.0433  -0.0372 0.1696  73  ASP A OD2 
465  N N   . ARG A 74  ? 0.4980 0.6322 0.4396 0.0827  -0.0455 0.1069  74  ARG A N   
466  C CA  . ARG A 74  ? 0.5314 0.6879 0.4710 0.0922  -0.0371 0.0927  74  ARG A CA  
467  C C   . ARG A 74  ? 0.5621 0.7163 0.4884 0.0996  -0.0422 0.0712  74  ARG A C   
468  O O   . ARG A 74  ? 0.5178 0.6911 0.4422 0.1074  -0.0344 0.0562  74  ARG A O   
469  C CB  . ARG A 74  ? 0.5634 0.7259 0.5315 0.0966  -0.0348 0.0866  74  ARG A CB  
470  C CG  . ARG A 74  ? 0.5972 0.7747 0.5814 0.0884  -0.0257 0.1017  74  ARG A CG  
471  C CD  . ARG A 74  ? 0.5874 0.7824 0.6026 0.0948  -0.0238 0.0917  74  ARG A CD  
472  N NE  . ARG A 74  ? 0.6461 0.8174 0.6740 0.1003  -0.0409 0.0873  74  ARG A NE  
473  C CZ  . ARG A 74  ? 0.7176 0.8767 0.7558 0.0926  -0.0496 0.0980  74  ARG A CZ  
474  N NH1 . ARG A 74  ? 0.7484 0.9167 0.7905 0.0788  -0.0422 0.1113  74  ARG A NH1 
475  N NH2 . ARG A 74  ? 0.7544 0.8906 0.7973 0.0983  -0.0652 0.0952  74  ARG A NH2 
476  N N   . ASP A 75  ? 0.4977 0.6319 0.4159 0.0958  -0.0533 0.0674  75  ASP A N   
477  C CA  . ASP A 75  ? 0.5172 0.6454 0.4287 0.0998  -0.0577 0.0435  75  ASP A CA  
478  C C   . ASP A 75  ? 0.5746 0.7194 0.4622 0.0990  -0.0605 0.0369  75  ASP A C   
479  O O   . ASP A 75  ? 0.4565 0.6068 0.3339 0.0953  -0.0642 0.0527  75  ASP A O   
480  C CB  . ASP A 75  ? 0.5996 0.6911 0.5219 0.0945  -0.0673 0.0384  75  ASP A CB  
481  C CG  . ASP A 75  ? 0.5805 0.6543 0.5215 0.1016  -0.0675 0.0345  75  ASP A CG  
482  O OD1 . ASP A 75  ? 0.5940 0.6879 0.5449 0.1117  -0.0604 0.0306  75  ASP A OD1 
483  O OD2 . ASP A 75  ? 0.5571 0.5971 0.5028 0.0975  -0.0749 0.0354  75  ASP A OD2 
484  N N   . GLU A 76  ? 0.5330 0.6865 0.4132 0.1035  -0.0597 0.0118  76  GLU A N   
485  C CA  . GLU A 76  ? 0.4982 0.6713 0.3571 0.1030  -0.0649 -0.0001 76  GLU A CA  
486  C C   . GLU A 76  ? 0.4907 0.6451 0.3559 0.0941  -0.0764 -0.0062 76  GLU A C   
487  O O   . GLU A 76  ? 0.4554 0.6236 0.3108 0.0923  -0.0842 0.0004  76  GLU A O   
488  C CB  . GLU A 76  ? 0.5533 0.7434 0.4043 0.1086  -0.0595 -0.0295 76  GLU A CB  
489  C CG  . GLU A 76  ? 0.7186 0.9389 0.5568 0.1161  -0.0464 -0.0266 76  GLU A CG  
490  C CD  . GLU A 76  ? 0.8201 1.0657 0.6292 0.1163  -0.0460 -0.0038 76  GLU A CD  
491  O OE1 . GLU A 76  ? 0.8740 1.1486 0.6545 0.1195  -0.0459 -0.0145 76  GLU A OE1 
492  O OE2 . GLU A 76  ? 0.8516 1.0869 0.6646 0.1134  -0.0457 0.0249  76  GLU A OE2 
493  N N   . ALA A 77  ? 0.5720 0.6942 0.4541 0.0885  -0.0773 -0.0178 77  ALA A N   
494  C CA  . ALA A 77  ? 0.5280 0.6345 0.4151 0.0769  -0.0850 -0.0257 77  ALA A CA  
495  C C   . ALA A 77  ? 0.4667 0.5506 0.3645 0.0699  -0.0872 -0.0020 77  ALA A C   
496  O O   . ALA A 77  ? 0.4201 0.4704 0.3280 0.0644  -0.0861 0.0001  77  ALA A O   
497  C CB  . ALA A 77  ? 0.4637 0.5435 0.3586 0.0713  -0.0829 -0.0521 77  ALA A CB  
498  N N   . LYS A 78  ? 0.4998 0.3076 0.3495 0.0608  -0.0684 0.0406  78  LYS A N   
499  C CA  . LYS A 78  ? 0.6477 0.4670 0.5060 0.0414  -0.0749 0.0455  78  LYS A CA  
500  C C   . LYS A 78  ? 0.6972 0.5045 0.5710 0.0395  -0.0805 0.0306  78  LYS A C   
501  O O   . LYS A 78  ? 0.5927 0.4172 0.4829 0.0301  -0.0794 0.0367  78  LYS A O   
502  C CB  . LYS A 78  ? 0.6898 0.4921 0.5247 0.0292  -0.0855 0.0447  78  LYS A CB  
503  C CG  . LYS A 78  ? 0.5329 0.3461 0.3494 0.0277  -0.0795 0.0591  78  LYS A CG  
504  C CD  . LYS A 78  ? 0.6247 0.4163 0.4124 0.0106  -0.0891 0.0607  78  LYS A CD  
505  C CE  . LYS A 78  ? 0.6149 0.4161 0.3813 0.0063  -0.0825 0.0746  78  LYS A CE  
506  N NZ  . LYS A 78  ? 0.7538 0.6095 0.5396 0.0012  -0.0692 0.0942  78  LYS A NZ  
507  N N   . CYS A 79  ? 0.6636 0.4449 0.5319 0.0481  -0.0861 0.0109  79  CYS A N   
508  C CA  . CYS A 79  ? 0.4602 0.2338 0.3419 0.0455  -0.0910 -0.0054 79  CYS A CA  
509  C C   . CYS A 79  ? 0.4942 0.2789 0.3931 0.0464  -0.0797 0.0002  79  CYS A C   
510  O O   . CYS A 79  ? 0.4556 0.2476 0.3695 0.0370  -0.0815 -0.0021 79  CYS A O   
511  C CB  . CYS A 79  ? 0.4771 0.2287 0.3485 0.0549  -0.0969 -0.0265 79  CYS A CB  
512  S SG  . CYS A 79  ? 0.4645 0.2140 0.3516 0.0499  -0.1011 -0.0480 79  CYS A SG  
513  N N   . ARG A 80  ? 0.6437 0.4272 0.5365 0.0594  -0.0679 0.0079  80  ARG A N   
514  C CA  . ARG A 80  ? 0.4687 0.2552 0.3686 0.0649  -0.0560 0.0146  80  ARG A CA  
515  C C   . ARG A 80  ? 0.4490 0.2674 0.3641 0.0573  -0.0530 0.0326  80  ARG A C   
516  O O   . ARG A 80  ? 0.5059 0.3268 0.4326 0.0527  -0.0503 0.0329  80  ARG A O   
517  C CB  . ARG A 80  ? 0.5061 0.2829 0.3888 0.0849  -0.0442 0.0208  80  ARG A CB  
518  C CG  . ARG A 80  ? 0.5704 0.3455 0.4504 0.0969  -0.0305 0.0309  80  ARG A CG  
519  C CD  . ARG A 80  ? 0.5640 0.2989 0.4319 0.0981  -0.0272 0.0150  80  ARG A CD  
520  N NE  . ARG A 80  ? 0.5197 0.2543 0.4032 0.0808  -0.0308 0.0082  80  ARG A NE  
521  C CZ  . ARG A 80  ? 0.5576 0.2621 0.4334 0.0739  -0.0283 -0.0056 80  ARG A CZ  
522  N NH1 . ARG A 80  ? 0.5655 0.2326 0.4152 0.0820  -0.0224 -0.0147 80  ARG A NH1 
523  N NH2 . ARG A 80  ? 0.5794 0.2905 0.4710 0.0573  -0.0315 -0.0102 80  ARG A NH2 
524  N N   . ASP A 81  ? 0.5004 0.3435 0.4137 0.0543  -0.0537 0.0472  81  ASP A N   
525  C CA  . ASP A 81  ? 0.4826 0.3615 0.4088 0.0442  -0.0518 0.0644  81  ASP A CA  
526  C C   . ASP A 81  ? 0.4174 0.2935 0.3553 0.0260  -0.0620 0.0572  81  ASP A C   
527  O O   . ASP A 81  ? 0.4124 0.3032 0.3642 0.0219  -0.0590 0.0629  81  ASP A O   
528  C CB  . ASP A 81  ? 0.5808 0.4855 0.4993 0.0379  -0.0521 0.0787  81  ASP A CB  
529  C CG  . ASP A 81  ? 0.5215 0.4441 0.4319 0.0571  -0.0400 0.0903  81  ASP A CG  
530  O OD1 . ASP A 81  ? 0.4582 0.3770 0.3686 0.0768  -0.0301 0.0913  81  ASP A OD1 
531  O OD2 . ASP A 81  ? 0.4896 0.4281 0.3898 0.0526  -0.0399 0.0985  81  ASP A OD2 
532  N N   . MET A 82  ? 0.4229 0.2794 0.3521 0.0172  -0.0741 0.0449  82  MET A N   
533  C CA  . MET A 82  ? 0.5879 0.4399 0.5228 0.0029  -0.0847 0.0373  82  MET A CA  
534  C C   . MET A 82  ? 0.4479 0.2926 0.3976 0.0047  -0.0835 0.0249  82  MET A C   
535  O O   . MET A 82  ? 0.3895 0.2440 0.3512 -0.0052 -0.0859 0.0258  82  MET A O   
536  C CB  . MET A 82  ? 0.4255 0.2525 0.3409 -0.0001 -0.0976 0.0249  82  MET A CB  
537  C CG  . MET A 82  ? 0.4224 0.2427 0.3353 -0.0125 -0.1091 0.0191  82  MET A CG  
538  S SD  . MET A 82  ? 0.4315 0.2769 0.3469 -0.0321 -0.1073 0.0405  82  MET A SD  
539  C CE  . MET A 82  ? 0.7529 0.6006 0.6454 -0.0360 -0.1042 0.0546  82  MET A CE  
540  N N   . TYR A 83  ? 0.4039 0.2308 0.3504 0.0157  -0.0794 0.0131  83  TYR A N   
541  C CA  . TYR A 83  ? 0.4886 0.3064 0.4446 0.0145  -0.0765 0.0012  83  TYR A CA  
542  C C   . TYR A 83  ? 0.4195 0.2506 0.3853 0.0146  -0.0654 0.0161  83  TYR A C   
543  O O   . TYR A 83  ? 0.4211 0.2588 0.3992 0.0049  -0.0668 0.0142  83  TYR A O   
544  C CB  . TYR A 83  ? 0.4436 0.2374 0.3882 0.0238  -0.0730 -0.0126 83  TYR A CB  
545  C CG  . TYR A 83  ? 0.4732 0.2550 0.4226 0.0176  -0.0695 -0.0261 83  TYR A CG  
546  C CD1 . TYR A 83  ? 0.4620 0.2462 0.4190 0.0070  -0.0792 -0.0457 83  TYR A CD1 
547  C CD2 . TYR A 83  ? 0.4610 0.2299 0.4045 0.0221  -0.0560 -0.0187 83  TYR A CD2 
548  C CE1 . TYR A 83  ? 0.4144 0.1917 0.3753 -0.0030 -0.0749 -0.0578 83  TYR A CE1 
549  C CE2 . TYR A 83  ? 0.4611 0.2139 0.4034 0.0129  -0.0518 -0.0300 83  TYR A CE2 
550  C CZ  . TYR A 83  ? 0.4764 0.2350 0.4285 -0.0018 -0.0609 -0.0495 83  TYR A CZ  
551  O OH  . TYR A 83  ? 0.4471 0.1917 0.3962 -0.0146 -0.0552 -0.0603 83  TYR A OH  
552  N N   . ASP A 84  ? 0.3924 0.2296 0.3511 0.0276  -0.0547 0.0313  84  ASP A N   
553  C CA  . ASP A 84  ? 0.3815 0.2338 0.3450 0.0335  -0.0439 0.0471  84  ASP A CA  
554  C C   . ASP A 84  ? 0.4571 0.3402 0.4368 0.0203  -0.0484 0.0576  84  ASP A C   
555  O O   . ASP A 84  ? 0.3690 0.2549 0.3572 0.0166  -0.0453 0.0595  84  ASP A O   
556  C CB  . ASP A 84  ? 0.3957 0.2605 0.3480 0.0524  -0.0337 0.0630  84  ASP A CB  
557  C CG  . ASP A 84  ? 0.4801 0.3099 0.4117 0.0694  -0.0259 0.0553  84  ASP A CG  
558  O OD1 . ASP A 84  ? 0.4738 0.2697 0.3990 0.0653  -0.0255 0.0400  84  ASP A OD1 
559  O OD2 . ASP A 84  ? 0.5763 0.4132 0.4957 0.0860  -0.0197 0.0646  84  ASP A OD2 
560  N N   . PHE A 85  ? 0.3604 0.2632 0.3409 0.0115  -0.0557 0.0641  85  PHE A N   
561  C CA  . PHE A 85  ? 0.3448 0.2745 0.3357 -0.0035 -0.0606 0.0739  85  PHE A CA  
562  C C   . PHE A 85  ? 0.3520 0.2677 0.3508 -0.0156 -0.0689 0.0604  85  PHE A C   
563  O O   . PHE A 85  ? 0.3233 0.2559 0.3327 -0.0235 -0.0689 0.0671  85  PHE A O   
564  C CB  . PHE A 85  ? 0.3465 0.2889 0.3288 -0.0152 -0.0679 0.0803  85  PHE A CB  
565  C CG  . PHE A 85  ? 0.4076 0.3798 0.3857 -0.0080 -0.0595 0.0973  85  PHE A CG  
566  C CD1 . PHE A 85  ? 0.4213 0.4328 0.4099 -0.0020 -0.0503 0.1140  85  PHE A CD1 
567  C CD2 . PHE A 85  ? 0.3665 0.3317 0.3293 -0.0069 -0.0610 0.0969  85  PHE A CD2 
568  C CE1 . PHE A 85  ? 0.4319 0.4809 0.4176 0.0059  -0.0425 0.1298  85  PHE A CE1 
569  C CE2 . PHE A 85  ? 0.4044 0.4036 0.3638 -0.0013 -0.0528 0.1129  85  PHE A CE2 
570  C CZ  . PHE A 85  ? 0.4347 0.4789 0.4066 0.0053  -0.0435 0.1293  85  PHE A CZ  
571  N N   . THR A 86  ? 0.3422 0.2310 0.3355 -0.0160 -0.0759 0.0414  86  THR A N   
572  C CA  . THR A 86  ? 0.3340 0.2142 0.3340 -0.0252 -0.0840 0.0266  86  THR A CA  
573  C C   . THR A 86  ? 0.3715 0.2512 0.3829 -0.0247 -0.0756 0.0245  86  THR A C   
574  O O   . THR A 86  ? 0.3194 0.2074 0.3407 -0.0341 -0.0785 0.0228  86  THR A O   
575  C CB  . THR A 86  ? 0.3920 0.2510 0.3829 -0.0226 -0.0933 0.0062  86  THR A CB  
576  O OG1 . THR A 86  ? 0.4487 0.3027 0.4235 -0.0231 -0.1011 0.0095  86  THR A OG1 
577  C CG2 . THR A 86  ? 0.3458 0.2043 0.3438 -0.0295 -0.1018 -0.0096 86  THR A CG2 
578  N N   . ILE A 87  ? 0.3566 0.2226 0.3623 -0.0140 -0.0648 0.0245  87  ILE A N   
579  C CA  . ILE A 87  ? 0.4192 0.2761 0.4266 -0.0134 -0.0547 0.0248  87  ILE A CA  
580  C C   . ILE A 87  ? 0.3510 0.2311 0.3659 -0.0128 -0.0497 0.0439  87  ILE A C   
581  O O   . ILE A 87  ? 0.3470 0.2283 0.3688 -0.0198 -0.0476 0.0433  87  ILE A O   
582  C CB  . ILE A 87  ? 0.4902 0.3202 0.4800 0.0000  -0.0431 0.0244  87  ILE A CB  
583  C CG1 . ILE A 87  ? 0.4089 0.2158 0.3909 -0.0033 -0.0473 0.0035  87  ILE A CG1 
584  C CG2 . ILE A 87  ? 0.3996 0.2142 0.3825 0.0021  -0.0312 0.0293  87  ILE A CG2 
585  C CD1 . ILE A 87  ? 0.4332 0.2323 0.4208 -0.0188 -0.0495 -0.0139 87  ILE A CD1 
586  N N   . LEU A 88  ? 0.3411 0.2431 0.3543 -0.0049 -0.0477 0.0606  88  LEU A N   
587  C CA  . LEU A 88  ? 0.4548 0.3878 0.4754 -0.0038 -0.0437 0.0790  88  LEU A CA  
588  C C   . LEU A 88  ? 0.2923 0.2407 0.3257 -0.0226 -0.0540 0.0771  88  LEU A C   
589  O O   . LEU A 88  ? 0.2865 0.2475 0.3272 -0.0253 -0.0514 0.0839  88  LEU A O   
590  C CB  . LEU A 88  ? 0.3130 0.2773 0.3310 0.0047  -0.0410 0.0961  88  LEU A CB  
591  C CG  . LEU A 88  ? 0.4443 0.4046 0.4484 0.0285  -0.0292 0.1037  88  LEU A CG  
592  C CD1 . LEU A 88  ? 0.4270 0.4312 0.4325 0.0327  -0.0282 0.1202  88  LEU A CD1 
593  C CD2 . LEU A 88  ? 0.3842 0.3333 0.3797 0.0455  -0.0171 0.1101  88  LEU A CD2 
594  N N   . LYS A 89  ? 0.3026 0.2454 0.3349 -0.0338 -0.0658 0.0670  89  LYS A N   
595  C CA  . LYS A 89  ? 0.3574 0.3089 0.3950 -0.0495 -0.0760 0.0649  89  LYS A CA  
596  C C   . LYS A 89  ? 0.4345 0.3739 0.4798 -0.0529 -0.0760 0.0523  89  LYS A C   
597  O O   . LYS A 89  ? 0.2778 0.2308 0.3308 -0.0595 -0.0760 0.0579  89  LYS A O   
598  C CB  . LYS A 89  ? 0.2948 0.2347 0.3206 -0.0575 -0.0885 0.0566  89  LYS A CB  
599  C CG  . LYS A 89  ? 0.3605 0.3017 0.3831 -0.0724 -0.0997 0.0544  89  LYS A CG  
600  C CD  . LYS A 89  ? 0.2832 0.2529 0.3136 -0.0821 -0.0975 0.0705  89  LYS A CD  
601  C CE  . LYS A 89  ? 0.3547 0.3502 0.3808 -0.0866 -0.0945 0.0884  89  LYS A CE  
602  N NZ  . LYS A 89  ? 0.2949 0.3235 0.3283 -0.0978 -0.0940 0.1026  89  LYS A NZ  
603  N N   . ILE A 90  ? 0.3279 0.2448 0.3709 -0.0492 -0.0752 0.0358  90  ILE A N   
604  C CA  . ILE A 90  ? 0.3125 0.2221 0.3623 -0.0549 -0.0737 0.0231  90  ILE A CA  
605  C C   . ILE A 90  ? 0.3456 0.2596 0.3989 -0.0537 -0.0623 0.0353  90  ILE A C   
606  O O   . ILE A 90  ? 0.3076 0.2291 0.3686 -0.0621 -0.0632 0.0337  90  ILE A O   
607  C CB  . ILE A 90  ? 0.4154 0.3041 0.4601 -0.0524 -0.0714 0.0058  90  ILE A CB  
608  C CG1 . ILE A 90  ? 0.4184 0.3040 0.4584 -0.0512 -0.0837 -0.0081 90  ILE A CG1 
609  C CG2 . ILE A 90  ? 0.3275 0.2121 0.3777 -0.0619 -0.0670 -0.0057 90  ILE A CG2 
610  C CD1 . ILE A 90  ? 0.3377 0.2065 0.3710 -0.0473 -0.0817 -0.0237 90  ILE A CD1 
611  N N   . GLU A 91  ? 0.3267 0.2353 0.3715 -0.0411 -0.0514 0.0476  91  GLU A N   
612  C CA  . GLU A 91  ? 0.3102 0.2189 0.3521 -0.0356 -0.0404 0.0598  91  GLU A CA  
613  C C   . GLU A 91  ? 0.2934 0.2357 0.3459 -0.0391 -0.0440 0.0746  91  GLU A C   
614  O O   . GLU A 91  ? 0.2944 0.2398 0.3491 -0.0408 -0.0395 0.0795  91  GLU A O   
615  C CB  . GLU A 91  ? 0.3347 0.2291 0.3594 -0.0163 -0.0285 0.0700  91  GLU A CB  
616  C CG  . GLU A 91  ? 0.4250 0.2778 0.4329 -0.0145 -0.0224 0.0556  91  GLU A CG  
617  C CD  . GLU A 91  ? 0.4823 0.3081 0.4821 -0.0250 -0.0156 0.0469  91  GLU A CD  
618  O OE1 . GLU A 91  ? 0.5652 0.4013 0.5698 -0.0281 -0.0132 0.0549  91  GLU A OE1 
619  O OE2 . GLU A 91  ? 0.3993 0.1942 0.3864 -0.0317 -0.0126 0.0318  91  GLU A OE2 
620  N N   . ASP A 92  ? 0.3038 0.2701 0.3607 -0.0421 -0.0521 0.0813  92  ASP A N   
621  C CA  . ASP A 92  ? 0.2909 0.2902 0.3555 -0.0496 -0.0567 0.0943  92  ASP A CA  
622  C C   . ASP A 92  ? 0.2798 0.2761 0.3512 -0.0651 -0.0652 0.0842  92  ASP A C   
623  O O   . ASP A 92  ? 0.2746 0.2865 0.3514 -0.0688 -0.0641 0.0917  92  ASP A O   
624  C CB  . ASP A 92  ? 0.2870 0.3080 0.3497 -0.0541 -0.0631 0.1021  92  ASP A CB  
625  C CG  . ASP A 92  ? 0.5809 0.6406 0.6488 -0.0639 -0.0666 0.1171  92  ASP A CG  
626  O OD1 . ASP A 92  ? 0.5969 0.6800 0.6694 -0.0543 -0.0586 0.1301  92  ASP A OD1 
627  O OD2 . ASP A 92  ? 0.5307 0.5962 0.5948 -0.0810 -0.0772 0.1160  92  ASP A OD2 
628  N N   . ILE A 93  ? 0.2966 0.2740 0.3661 -0.0717 -0.0737 0.0667  93  ILE A N   
629  C CA  . ILE A 93  ? 0.2897 0.2629 0.3630 -0.0820 -0.0815 0.0541  93  ILE A CA  
630  C C   . ILE A 93  ? 0.2910 0.2599 0.3705 -0.0819 -0.0725 0.0510  93  ILE A C   
631  O O   . ILE A 93  ? 0.2842 0.2626 0.3688 -0.0892 -0.0751 0.0510  93  ILE A O   
632  C CB  . ILE A 93  ? 0.2924 0.2478 0.3602 -0.0828 -0.0905 0.0347  93  ILE A CB  
633  C CG1 . ILE A 93  ? 0.4119 0.3647 0.4673 -0.0839 -0.0993 0.0383  93  ILE A CG1 
634  C CG2 . ILE A 93  ? 0.2875 0.2433 0.3578 -0.0895 -0.0984 0.0211  93  ILE A CG2 
635  C CD1 . ILE A 93  ? 0.2971 0.2607 0.3462 -0.0952 -0.1072 0.0476  93  ILE A CD1 
636  N N   . GLN A 94  ? 0.4056 0.3572 0.4809 -0.0744 -0.0616 0.0491  94  GLN A N   
637  C CA  . GLN A 94  ? 0.3985 0.3379 0.4724 -0.0764 -0.0514 0.0465  94  GLN A CA  
638  C C   . GLN A 94  ? 0.3599 0.3120 0.4333 -0.0723 -0.0450 0.0648  94  GLN A C   
639  O O   . GLN A 94  ? 0.3500 0.3042 0.4267 -0.0798 -0.0434 0.0629  94  GLN A O   
640  C CB  . GLN A 94  ? 0.3503 0.2606 0.4110 -0.0702 -0.0410 0.0418  94  GLN A CB  
641  C CG  . GLN A 94  ? 0.3721 0.2588 0.4229 -0.0764 -0.0295 0.0369  94  GLN A CG  
642  C CD  . GLN A 94  ? 0.5158 0.4120 0.5775 -0.0939 -0.0336 0.0219  94  GLN A CD  
643  O OE1 . GLN A 94  ? 0.6466 0.5348 0.7030 -0.1007 -0.0253 0.0241  94  GLN A OE1 
644  N NE2 . GLN A 94  ? 0.3565 0.2693 0.4305 -0.0998 -0.0458 0.0067  94  GLN A NE2 
645  N N   . ARG A 95  ? 0.3019 0.2673 0.3715 -0.0599 -0.0419 0.0819  95  ARG A N   
646  C CA  . ARG A 95  ? 0.3783 0.3655 0.4483 -0.0541 -0.0378 0.0996  95  ARG A CA  
647  C C   . ARG A 95  ? 0.4172 0.4277 0.4991 -0.0687 -0.0482 0.0991  95  ARG A C   
648  O O   . ARG A 95  ? 0.3440 0.3583 0.4266 -0.0706 -0.0448 0.1031  95  ARG A O   
649  C CB  . ARG A 95  ? 0.3038 0.3166 0.3713 -0.0398 -0.0356 0.1170  95  ARG A CB  
650  C CG  . ARG A 95  ? 0.4501 0.4411 0.5011 -0.0198 -0.0237 0.1212  95  ARG A CG  
651  C CD  . ARG A 95  ? 0.4390 0.4645 0.4878 -0.0023 -0.0204 0.1398  95  ARG A CD  
652  N NE  . ARG A 95  ? 0.4859 0.4868 0.5140 0.0211  -0.0087 0.1435  95  ARG A NE  
653  C CZ  . ARG A 95  ? 0.4345 0.4122 0.4412 0.0403  0.0035  0.1507  95  ARG A CZ  
654  N NH1 . ARG A 95  ? 0.4765 0.4541 0.4815 0.0384  0.0059  0.1552  95  ARG A NH1 
655  N NH2 . ARG A 95  ? 0.4339 0.3841 0.4163 0.0625  0.0135  0.1534  95  ARG A NH2 
656  N N   . LYS A 96  ? 0.2850 0.3060 0.3718 -0.0788 -0.0606 0.0937  96  LYS A N   
657  C CA  . LYS A 96  ? 0.3085 0.3453 0.3997 -0.0923 -0.0711 0.0931  96  LYS A CA  
658  C C   . LYS A 96  ? 0.3797 0.4030 0.4739 -0.0985 -0.0712 0.0799  96  LYS A C   
659  O O   . LYS A 96  ? 0.3765 0.4118 0.4732 -0.1030 -0.0715 0.0848  96  LYS A O   
660  C CB  . LYS A 96  ? 0.3685 0.4054 0.4549 -0.1020 -0.0842 0.0876  96  LYS A CB  
661  C CG  . LYS A 96  ? 0.2722 0.3293 0.3550 -0.1013 -0.0846 0.1018  96  LYS A CG  
662  C CD  . LYS A 96  ? 0.5279 0.5780 0.5989 -0.1150 -0.0976 0.0966  96  LYS A CD  
663  C CE  . LYS A 96  ? 0.3878 0.4546 0.4535 -0.1162 -0.0969 0.1082  96  LYS A CE  
664  N NZ  . LYS A 96  ? 0.4387 0.5486 0.5127 -0.1135 -0.0898 0.1277  96  LYS A NZ  
665  N N   . ILE A 97  ? 0.3295 0.3316 0.4233 -0.0988 -0.0703 0.0632  97  ILE A N   
666  C CA  . ILE A 97  ? 0.3695 0.3651 0.4670 -0.1054 -0.0691 0.0494  97  ILE A CA  
667  C C   . ILE A 97  ? 0.3969 0.3905 0.4929 -0.1046 -0.0568 0.0584  97  ILE A C   
668  O O   . ILE A 97  ? 0.2896 0.2905 0.3890 -0.1116 -0.0574 0.0555  97  ILE A O   
669  C CB  . ILE A 97  ? 0.3138 0.2935 0.4109 -0.1062 -0.0682 0.0310  97  ILE A CB  
670  C CG1 . ILE A 97  ? 0.2831 0.2667 0.3743 -0.1009 -0.0782 0.0178  97  ILE A CG1 
671  C CG2 . ILE A 97  ? 0.2942 0.2724 0.3930 -0.1127 -0.0609 0.0181  97  ILE A CG2 
672  C CD1 . ILE A 97  ? 0.2873 0.2637 0.3770 -0.0983 -0.0776 -0.0006 97  ILE A CD1 
673  N N   . GLU A 98  ? 0.3468 0.3281 0.4342 -0.0944 -0.0454 0.0693  98  GLU A N   
674  C CA  . GLU A 98  ? 0.3445 0.3157 0.4226 -0.0908 -0.0330 0.0786  98  GLU A CA  
675  C C   . GLU A 98  ? 0.3256 0.3233 0.4074 -0.0881 -0.0357 0.0940  98  GLU A C   
676  O O   . GLU A 98  ? 0.3178 0.3137 0.3964 -0.0912 -0.0308 0.0965  98  GLU A O   
677  C CB  . GLU A 98  ? 0.3884 0.3336 0.4487 -0.0765 -0.0205 0.0864  98  GLU A CB  
678  C CG  . GLU A 98  ? 0.4023 0.3188 0.4561 -0.0823 -0.0176 0.0697  98  GLU A CG  
679  C CD  . GLU A 98  ? 0.5396 0.4278 0.5729 -0.0669 -0.0076 0.0762  98  GLU A CD  
680  O OE1 . GLU A 98  ? 0.5043 0.4024 0.5316 -0.0486 -0.0049 0.0935  98  GLU A OE1 
681  O OE2 . GLU A 98  ? 0.4607 0.3184 0.4822 -0.0732 -0.0026 0.0635  98  GLU A OE2 
682  N N   . ASP A 99  ? 0.2810 0.3047 0.3683 -0.0843 -0.0437 0.1040  99  ASP A N   
683  C CA  . ASP A 99  ? 0.2729 0.3275 0.3639 -0.0850 -0.0481 0.1175  99  ASP A CA  
684  C C   . ASP A 99  ? 0.2711 0.3306 0.3681 -0.1002 -0.0568 0.1079  99  ASP A C   
685  O O   . ASP A 99  ? 0.2631 0.3325 0.3593 -0.1014 -0.0549 0.1143  99  ASP A O   
686  C CB  . ASP A 99  ? 0.2634 0.3470 0.3582 -0.0843 -0.0557 0.1273  99  ASP A CB  
687  C CG  . ASP A 99  ? 0.4115 0.5011 0.5001 -0.0652 -0.0461 0.1403  99  ASP A CG  
688  O OD1 . ASP A 99  ? 0.5120 0.5807 0.5893 -0.0504 -0.0337 0.1441  99  ASP A OD1 
689  O OD2 . ASP A 99  ? 0.2788 0.3923 0.3703 -0.0646 -0.0506 0.1469  99  ASP A OD2 
690  N N   . LEU A 100 ? 0.2393 0.2898 0.3394 -0.1094 -0.0659 0.0919  100 LEU A N   
691  C CA  . LEU A 100 ? 0.2349 0.2846 0.3329 -0.1158 -0.0723 0.0783  100 LEU A CA  
692  C C   . LEU A 100 ? 0.2855 0.3271 0.3863 -0.1192 -0.0638 0.0722  100 LEU A C   
693  O O   . LEU A 100 ? 0.4977 0.5469 0.5961 -0.1211 -0.0646 0.0701  100 LEU A O   
694  C CB  . LEU A 100 ? 0.2343 0.2711 0.3241 -0.1123 -0.0783 0.0601  100 LEU A CB  
695  C CG  . LEU A 100 ? 0.2700 0.3111 0.3491 -0.1120 -0.0861 0.0664  100 LEU A CG  
696  C CD1 . LEU A 100 ? 0.4054 0.4295 0.4737 -0.1083 -0.0911 0.0515  100 LEU A CD1 
697  C CD2 . LEU A 100 ? 0.2391 0.2899 0.3087 -0.1154 -0.0896 0.0719  100 LEU A CD2 
698  N N   . LYS A 101 ? 0.2646 0.2880 0.3653 -0.1191 -0.0538 0.0688  101 LYS A N   
699  C CA  . LYS A 101 ? 0.2768 0.2894 0.3741 -0.1248 -0.0433 0.0636  101 LYS A CA  
700  C C   . LYS A 101 ? 0.2964 0.3099 0.3853 -0.1194 -0.0349 0.0810  101 LYS A C   
701  O O   . LYS A 101 ? 0.2935 0.3079 0.3805 -0.1261 -0.0308 0.0792  101 LYS A O   
702  C CB  . LYS A 101 ? 0.2937 0.2811 0.3845 -0.1268 -0.0333 0.0546  101 LYS A CB  
703  C CG  . LYS A 101 ? 0.3567 0.3496 0.4549 -0.1327 -0.0393 0.0319  101 LYS A CG  
704  C CD  . LYS A 101 ? 0.4797 0.4504 0.5717 -0.1384 -0.0308 0.0234  101 LYS A CD  
705  C CE  . LYS A 101 ? 0.5146 0.5009 0.6141 -0.1406 -0.0325 -0.0010 101 LYS A CE  
706  N NZ  . LYS A 101 ? 0.7011 0.7008 0.8045 -0.1473 -0.0278 -0.0068 101 LYS A NZ  
707  N N   . ARG A 102 ? 0.2659 0.2821 0.3488 -0.1061 -0.0321 0.0979  102 ARG A N   
708  C CA  . ARG A 102 ? 0.3554 0.3777 0.4291 -0.0975 -0.0255 0.1148  102 ARG A CA  
709  C C   . ARG A 102 ? 0.2607 0.3118 0.3436 -0.1048 -0.0358 0.1166  102 ARG A C   
710  O O   . ARG A 102 ? 0.2691 0.3195 0.3465 -0.1063 -0.0309 0.1201  102 ARG A O   
711  C CB  . ARG A 102 ? 0.2875 0.3173 0.3533 -0.0784 -0.0216 0.1326  102 ARG A CB  
712  C CG  . ARG A 102 ? 0.3202 0.3115 0.3646 -0.0659 -0.0068 0.1352  102 ARG A CG  
713  C CD  . ARG A 102 ? 0.3322 0.3334 0.3667 -0.0422 -0.0029 0.1523  102 ARG A CD  
714  N NE  . ARG A 102 ? 0.3160 0.3297 0.3618 -0.0418 -0.0098 0.1486  102 ARG A NE  
715  C CZ  . ARG A 102 ? 0.3280 0.3112 0.3661 -0.0403 -0.0052 0.1398  102 ARG A CZ  
716  N NH1 . ARG A 102 ? 0.3586 0.2960 0.3762 -0.0410 0.0062  0.1334  102 ARG A NH1 
717  N NH2 . ARG A 102 ? 0.3390 0.3363 0.3873 -0.0396 -0.0121 0.1373  102 ARG A NH2 
718  N N   . ILE A 103 ? 0.3137 0.3850 0.4068 -0.1110 -0.0499 0.1132  103 ILE A N   
719  C CA  . ILE A 103 ? 0.4167 0.5098 0.5128 -0.1194 -0.0606 0.1142  103 ILE A CA  
720  C C   . ILE A 103 ? 0.4190 0.5028 0.5156 -0.1281 -0.0611 0.0994  103 ILE A C   
721  O O   . ILE A 103 ? 0.2421 0.3351 0.3364 -0.1308 -0.0607 0.1035  103 ILE A O   
722  C CB  . ILE A 103 ? 0.2310 0.3342 0.3257 -0.1231 -0.0739 0.1103  103 ILE A CB  
723  C CG1 . ILE A 103 ? 0.2288 0.3571 0.3277 -0.1203 -0.0748 0.1288  103 ILE A CG1 
724  C CG2 . ILE A 103 ? 0.2336 0.3381 0.3156 -0.1255 -0.0811 0.1030  103 ILE A CG2 
725  C CD1 . ILE A 103 ? 0.2992 0.4248 0.3878 -0.1220 -0.0831 0.1223  103 ILE A CD1 
726  N N   . GLU A 104 ? 0.3090 0.3763 0.4053 -0.1281 -0.0601 0.0806  104 GLU A N   
727  C CA  . GLU A 104 ? 0.3127 0.3767 0.4079 -0.1313 -0.0578 0.0640  104 GLU A CA  
728  C C   . GLU A 104 ? 0.2651 0.3264 0.3598 -0.1384 -0.0464 0.0709  104 GLU A C   
729  O O   . GLU A 104 ? 0.2829 0.3531 0.3760 -0.1415 -0.0470 0.0673  104 GLU A O   
730  C CB  . GLU A 104 ? 0.2529 0.3071 0.3509 -0.1304 -0.0560 0.0453  104 GLU A CB  
731  C CG  . GLU A 104 ? 0.2739 0.3364 0.3724 -0.1293 -0.0598 0.0268  104 GLU A CG  
732  C CD  . GLU A 104 ? 0.4774 0.5386 0.5816 -0.1282 -0.0581 0.0090  104 GLU A CD  
733  O OE1 . GLU A 104 ? 0.6226 0.6724 0.7278 -0.1288 -0.0544 0.0106  104 GLU A OE1 
734  O OE2 . GLU A 104 ? 0.4434 0.5169 0.5511 -0.1264 -0.0613 -0.0064 104 GLU A OE2 
735  N N   . ARG A 105 ? 0.2522 0.2953 0.3416 -0.1379 -0.0342 0.0800  105 ARG A N   
736  C CA  . ARG A 105 ? 0.2910 0.3194 0.3675 -0.1401 -0.0199 0.0857  105 ARG A CA  
737  C C   . ARG A 105 ? 0.2773 0.3187 0.3479 -0.1326 -0.0206 0.1024  105 ARG A C   
738  O O   . ARG A 105 ? 0.2866 0.3278 0.3511 -0.1375 -0.0154 0.1030  105 ARG A O   
739  C CB  . ARG A 105 ? 0.3321 0.3266 0.3922 -0.1358 -0.0058 0.0904  105 ARG A CB  
740  C CG  . ARG A 105 ? 0.3067 0.2873 0.3692 -0.1484 -0.0026 0.0719  105 ARG A CG  
741  C CD  . ARG A 105 ? 0.3443 0.2827 0.3825 -0.1478 0.0129  0.0760  105 ARG A CD  
742  N NE  . ARG A 105 ? 0.4206 0.3485 0.4510 -0.1280 0.0128  0.0900  105 ARG A NE  
743  C CZ  . ARG A 105 ? 0.3434 0.2671 0.3785 -0.1237 0.0089  0.0851  105 ARG A CZ  
744  N NH1 . ARG A 105 ? 0.3326 0.2596 0.3792 -0.1372 0.0046  0.0662  105 ARG A NH1 
745  N NH2 . ARG A 105 ? 0.3499 0.2685 0.3769 -0.1043 0.0098  0.0992  105 ARG A NH2 
746  N N   . MET A 106 ? 0.2846 0.3415 0.3574 -0.1217 -0.0277 0.1153  106 MET A N   
747  C CA  . MET A 106 ? 0.2838 0.3625 0.3536 -0.1157 -0.0312 0.1298  106 MET A CA  
748  C C   . MET A 106 ? 0.3954 0.4899 0.4710 -0.1273 -0.0405 0.1211  106 MET A C   
749  O O   . MET A 106 ? 0.2805 0.3795 0.3488 -0.1268 -0.0368 0.1273  106 MET A O   
750  C CB  . MET A 106 ? 0.2723 0.3752 0.3477 -0.1081 -0.0402 0.1407  106 MET A CB  
751  C CG  . MET A 106 ? 0.4553 0.5788 0.5226 -0.0938 -0.0372 0.1608  106 MET A CG  
752  S SD  . MET A 106 ? 0.8255 0.9852 0.8993 -0.0843 -0.0444 0.1742  106 MET A SD  
753  C CE  . MET A 106 ? 0.3734 0.5027 0.4450 -0.0765 -0.0363 0.1687  106 MET A CE  
754  N N   . LEU A 107 ? 0.2515 0.3513 0.3365 -0.1359 -0.0521 0.1065  107 LEU A N   
755  C CA  . LEU A 107 ? 0.2459 0.3545 0.3301 -0.1418 -0.0609 0.0953  107 LEU A CA  
756  C C   . LEU A 107 ? 0.2534 0.3564 0.3373 -0.1481 -0.0514 0.0861  107 LEU A C   
757  O O   . LEU A 107 ? 0.2556 0.3687 0.3361 -0.1514 -0.0528 0.0863  107 LEU A O   
758  C CB  . LEU A 107 ? 0.3266 0.4280 0.4070 -0.1372 -0.0706 0.0783  107 LEU A CB  
759  C CG  . LEU A 107 ? 0.2380 0.3410 0.3116 -0.1335 -0.0793 0.0845  107 LEU A CG  
760  C CD1 . LEU A 107 ? 0.2373 0.3242 0.3057 -0.1292 -0.0836 0.0681  107 LEU A CD1 
761  C CD2 . LEU A 107 ? 0.2433 0.3565 0.3055 -0.1361 -0.0866 0.0912  107 LEU A CD2 
762  N N   . MET A 108 ? 0.2468 0.3348 0.3327 -0.1511 -0.0413 0.0776  108 MET A N   
763  C CA  . MET A 108 ? 0.2805 0.3653 0.3636 -0.1599 -0.0303 0.0689  108 MET A CA  
764  C C   . MET A 108 ? 0.3777 0.4559 0.4475 -0.1595 -0.0197 0.0845  108 MET A C   
765  O O   . MET A 108 ? 0.2934 0.3817 0.3607 -0.1652 -0.0177 0.0809  108 MET A O   
766  C CB  . MET A 108 ? 0.2687 0.3364 0.3515 -0.1648 -0.0198 0.0580  108 MET A CB  
767  C CG  . MET A 108 ? 0.3099 0.3866 0.4035 -0.1599 -0.0287 0.0381  108 MET A CG  
768  S SD  . MET A 108 ? 0.4219 0.4817 0.5171 -0.1636 -0.0202 0.0273  108 MET A SD  
769  C CE  . MET A 108 ? 0.2902 0.3393 0.3746 -0.1788 -0.0024 0.0257  108 MET A CE  
770  N N   . ASP A 109 ? 0.3220 0.3840 0.3806 -0.1494 -0.0131 0.1016  109 ASP A N   
771  C CA  . ASP A 109 ? 0.4449 0.4967 0.4851 -0.1435 -0.0028 0.1171  109 ASP A CA  
772  C C   . ASP A 109 ? 0.4516 0.5303 0.4942 -0.1399 -0.0126 0.1238  109 ASP A C   
773  O O   . ASP A 109 ? 0.3470 0.4252 0.3793 -0.1425 -0.0066 0.1268  109 ASP A O   
774  C CB  . ASP A 109 ? 0.3561 0.3883 0.3813 -0.1274 0.0043  0.1340  109 ASP A CB  
775  C CG  . ASP A 109 ? 0.3905 0.4031 0.3891 -0.1182 0.0170  0.1494  109 ASP A CG  
776  O OD1 . ASP A 109 ? 0.4228 0.3995 0.4007 -0.1254 0.0320  0.1471  109 ASP A OD1 
777  O OD2 . ASP A 109 ? 0.5365 0.5692 0.5324 -0.1048 0.0121  0.1634  109 ASP A OD2 
778  N N   . LEU A 110 ? 0.3026 0.4033 0.3563 -0.1359 -0.0277 0.1257  110 LEU A N   
779  C CA  . LEU A 110 ? 0.2940 0.4193 0.3483 -0.1360 -0.0391 0.1300  110 LEU A CA  
780  C C   . LEU A 110 ? 0.2920 0.4212 0.3467 -0.1458 -0.0411 0.1162  110 LEU A C   
781  O O   . LEU A 110 ? 0.3005 0.4370 0.3467 -0.1450 -0.0396 0.1220  110 LEU A O   
782  C CB  . LEU A 110 ? 0.2757 0.4194 0.3387 -0.1371 -0.0555 0.1299  110 LEU A CB  
783  C CG  . LEU A 110 ? 0.3843 0.5418 0.4470 -0.1274 -0.0567 0.1466  110 LEU A CG  
784  C CD1 . LEU A 110 ? 0.2606 0.4326 0.3308 -0.1345 -0.0717 0.1433  110 LEU A CD1 
785  C CD2 . LEU A 110 ? 0.3522 0.5299 0.4059 -0.1194 -0.0556 0.1630  110 LEU A CD2 
786  N N   . LYS A 111 ? 0.2684 0.3957 0.3321 -0.1529 -0.0445 0.0981  111 LYS A N   
787  C CA  . LYS A 111 ? 0.2668 0.4037 0.3309 -0.1590 -0.0471 0.0833  111 LYS A CA  
788  C C   . LYS A 111 ? 0.3636 0.4951 0.4214 -0.1646 -0.0303 0.0836  111 LYS A C   
789  O O   . LYS A 111 ? 0.2871 0.4308 0.3415 -0.1677 -0.0301 0.0781  111 LYS A O   
790  C CB  . LYS A 111 ? 0.2825 0.4224 0.3559 -0.1613 -0.0548 0.0638  111 LYS A CB  
791  C CG  . LYS A 111 ? 0.2586 0.3972 0.3386 -0.1676 -0.0429 0.0506  111 LYS A CG  
792  C CD  . LYS A 111 ? 0.2497 0.3935 0.3349 -0.1608 -0.0513 0.0305  111 LYS A CD  
793  C CE  . LYS A 111 ? 0.3268 0.4857 0.4184 -0.1665 -0.0425 0.0138  111 LYS A CE  
794  N NZ  . LYS A 111 ? 0.4281 0.5737 0.5213 -0.1752 -0.0274 0.0154  111 LYS A NZ  
795  N N   . GLU A 112 ? 0.2999 0.4103 0.3521 -0.1664 -0.0158 0.0902  112 GLU A N   
796  C CA  . GLU A 112 ? 0.3422 0.4395 0.3804 -0.1743 0.0012  0.0927  112 GLU A CA  
797  C C   . GLU A 112 ? 0.4037 0.5001 0.4263 -0.1668 0.0039  0.1091  112 GLU A C   
798  O O   . GLU A 112 ? 0.3588 0.4510 0.3693 -0.1737 0.0145  0.1096  112 GLU A O   
799  C CB  . GLU A 112 ? 0.4853 0.5490 0.5113 -0.1778 0.0162  0.0974  112 GLU A CB  
800  C CG  . GLU A 112 ? 0.6365 0.6982 0.6741 -0.1885 0.0171  0.0809  112 GLU A CG  
801  C CD  . GLU A 112 ? 0.7440 0.7673 0.7662 -0.1876 0.0283  0.0882  112 GLU A CD  
802  O OE1 . GLU A 112 ? 0.8612 0.8573 0.8606 -0.1774 0.0367  0.1058  112 GLU A OE1 
803  O OE2 . GLU A 112 ? 0.6798 0.6992 0.7101 -0.1928 0.0280  0.0755  112 GLU A OE2 
804  N N   . ARG A 113 ? 0.3422 0.4459 0.3644 -0.1536 -0.0059 0.1223  113 ARG A N   
805  C CA  . ARG A 113 ? 0.3556 0.4644 0.3634 -0.1456 -0.0047 0.1370  113 ARG A CA  
806  C C   . ARG A 113 ? 0.3490 0.4795 0.3583 -0.1508 -0.0120 0.1298  113 ARG A C   
807  O O   . ARG A 113 ? 0.3637 0.4958 0.3588 -0.1465 -0.0082 0.1400  113 ARG A O   
808  C CB  . ARG A 113 ? 0.4199 0.5419 0.4283 -0.1314 -0.0145 0.1521  113 ARG A CB  
809  C CG  . ARG A 113 ? 0.3771 0.4808 0.3790 -0.1201 -0.0068 0.1630  113 ARG A CG  
810  C CD  . ARG A 113 ? 0.3753 0.5068 0.3847 -0.1087 -0.0194 0.1742  113 ARG A CD  
811  N NE  . ARG A 113 ? 0.5426 0.6614 0.5453 -0.0944 -0.0122 0.1847  113 ARG A NE  
812  C CZ  . ARG A 113 ? 0.4180 0.5315 0.4007 -0.0747 -0.0039 0.2022  113 ARG A CZ  
813  N NH1 . ARG A 113 ? 0.4005 0.5210 0.3690 -0.0682 -0.0018 0.2114  113 ARG A NH1 
814  N NH2 . ARG A 113 ? 0.3986 0.4994 0.3730 -0.0593 0.0023  0.2103  113 ARG A NH2 
815  N N   . CYS A 114 ? 0.3006 0.4464 0.3234 -0.1572 -0.0230 0.1128  114 CYS A N   
816  C CA  . CYS A 114 ? 0.2967 0.4609 0.3167 -0.1579 -0.0325 0.1067  114 CYS A CA  
817  C C   . CYS A 114 ? 0.3117 0.4775 0.3247 -0.1648 -0.0192 0.1007  114 CYS A C   
818  O O   . CYS A 114 ? 0.3174 0.4773 0.3340 -0.1740 -0.0071 0.0923  114 CYS A O   
819  C CB  . CYS A 114 ? 0.2785 0.4522 0.3076 -0.1587 -0.0493 0.0913  114 CYS A CB  
820  S SG  . CYS A 114 ? 0.2667 0.4393 0.2988 -0.1551 -0.0650 0.1000  114 CYS A SG  
821  N N   . PRO A 115 ? 0.3428 0.5180 0.3444 -0.1621 -0.0209 0.1053  115 PRO A N   
822  C CA  . PRO A 115 ? 0.3363 0.5156 0.3298 -0.1691 -0.0079 0.1006  115 PRO A CA  
823  C C   . PRO A 115 ? 0.3251 0.5262 0.3295 -0.1744 -0.0113 0.0786  115 PRO A C   
824  O O   . PRO A 115 ? 0.3080 0.5168 0.3216 -0.1694 -0.0259 0.0676  115 PRO A O   
825  C CB  . PRO A 115 ? 0.3463 0.5320 0.3248 -0.1619 -0.0124 0.1113  115 PRO A CB  
826  C CG  . PRO A 115 ? 0.3307 0.5247 0.3129 -0.1548 -0.0323 0.1127  115 PRO A CG  
827  C CD  . PRO A 115 ? 0.3187 0.5028 0.3128 -0.1542 -0.0344 0.1153  115 PRO A CD  
828  N N   . GLU A 116 ? 0.3381 0.5495 0.3388 -0.1837 0.0023  0.0723  116 GLU A N   
829  C CA  . GLU A 116 ? 0.3297 0.5712 0.3404 -0.1865 0.0005  0.0515  116 GLU A CA  
830  C C   . GLU A 116 ? 0.3227 0.5788 0.3285 -0.1724 -0.0168 0.0443  116 GLU A C   
831  O O   . GLU A 116 ? 0.3112 0.5793 0.3236 -0.1651 -0.0284 0.0289  116 GLU A O   
832  C CB  . GLU A 116 ? 0.3482 0.6035 0.3537 -0.2011 0.0193  0.0480  116 GLU A CB  
833  C CG  . GLU A 116 ? 0.3633 0.5990 0.3675 -0.2189 0.0366  0.0520  116 GLU A CG  
834  C CD  . GLU A 116 ? 0.3792 0.6376 0.3825 -0.2393 0.0535  0.0415  116 GLU A CD  
835  O OE1 . GLU A 116 ? 0.3843 0.6685 0.3830 -0.2387 0.0556  0.0375  116 GLU A OE1 
836  O OE2 . GLU A 116 ? 0.3887 0.6397 0.3944 -0.2568 0.0645  0.0369  116 GLU A OE2 
837  N N   . ASN A 117 ? 0.3340 0.5857 0.3242 -0.1676 -0.0189 0.0552  117 ASN A N   
838  C CA  . ASN A 117 ? 0.3337 0.5912 0.3131 -0.1554 -0.0362 0.0491  117 ASN A CA  
839  C C   . ASN A 117 ? 0.3282 0.5658 0.3027 -0.1505 -0.0523 0.0586  117 ASN A C   
840  O O   . ASN A 117 ? 0.3337 0.5620 0.3010 -0.1510 -0.0527 0.0753  117 ASN A O   
841  C CB  . ASN A 117 ? 0.3505 0.6167 0.3138 -0.1535 -0.0316 0.0536  117 ASN A CB  
842  C CG  . ASN A 117 ? 0.3646 0.6294 0.3106 -0.1417 -0.0499 0.0492  117 ASN A CG  
843  O OD1 . ASN A 117 ? 0.3531 0.6154 0.2962 -0.1339 -0.0640 0.0362  117 ASN A OD1 
844  N ND2 . ASN A 117 ? 0.3705 0.6328 0.3006 -0.1402 -0.0499 0.0601  117 ASN A ND2 
845  N N   . LYS A 118 ? 0.3567 0.5903 0.3330 -0.1456 -0.0660 0.0468  118 LYS A N   
846  C CA  . LYS A 118 ? 0.3241 0.5399 0.2967 -0.1452 -0.0804 0.0532  118 LYS A CA  
847  C C   . LYS A 118 ? 0.3391 0.5466 0.2875 -0.1404 -0.0977 0.0502  118 LYS A C   
848  O O   . LYS A 118 ? 0.3692 0.5611 0.3089 -0.1426 -0.1116 0.0522  118 LYS A O   
849  C CB  . LYS A 118 ? 0.3114 0.5215 0.2966 -0.1448 -0.0839 0.0433  118 LYS A CB  
850  C CG  . LYS A 118 ? 0.3009 0.5163 0.3067 -0.1517 -0.0668 0.0456  118 LYS A CG  
851  C CD  . LYS A 118 ? 0.2881 0.4970 0.3064 -0.1517 -0.0707 0.0378  118 LYS A CD  
852  C CE  . LYS A 118 ? 0.2831 0.4936 0.3174 -0.1603 -0.0538 0.0397  118 LYS A CE  
853  N NZ  . LYS A 118 ? 0.2916 0.5211 0.3272 -0.1663 -0.0397 0.0330  118 LYS A NZ  
854  N N   . ASP A 119 ? 0.3709 0.5867 0.3050 -0.1350 -0.0970 0.0446  119 ASP A N   
855  C CA  . ASP A 119 ? 0.3912 0.5925 0.2967 -0.1315 -0.1138 0.0420  119 ASP A CA  
856  C C   . ASP A 119 ? 0.3958 0.5997 0.2957 -0.1386 -0.1142 0.0603  119 ASP A C   
857  O O   . ASP A 119 ? 0.5600 0.7724 0.4494 -0.1359 -0.1104 0.0631  119 ASP A O   
858  C CB  . ASP A 119 ? 0.4082 0.6164 0.2967 -0.1193 -0.1145 0.0267  119 ASP A CB  
859  C CG  . ASP A 119 ? 0.7155 0.9031 0.5675 -0.1153 -0.1309 0.0241  119 ASP A CG  
860  O OD1 . ASP A 119 ? 0.6565 0.8203 0.4933 -0.1230 -0.1450 0.0288  119 ASP A OD1 
861  O OD2 . ASP A 119 ? 0.8285 1.0240 0.6651 -0.1060 -0.1291 0.0174  119 ASP A OD2 
862  N N   . ILE A 120 ? 0.4054 0.6031 0.3088 -0.1467 -0.1212 0.0716  120 ILE A N   
863  C CA  . ILE A 120 ? 0.3853 0.5939 0.2876 -0.1522 -0.1213 0.0903  120 ILE A CA  
864  C C   . ILE A 120 ? 0.4042 0.6046 0.3073 -0.1592 -0.1306 0.0957  120 ILE A C   
865  O O   . ILE A 120 ? 0.3954 0.5788 0.3041 -0.1596 -0.1326 0.0876  120 ILE A O   
866  C CB  . ILE A 120 ? 0.4161 0.6381 0.3382 -0.1495 -0.1023 0.1043  120 ILE A CB  
867  C CG1 . ILE A 120 ? 0.3927 0.6093 0.3365 -0.1504 -0.0942 0.1025  120 ILE A CG1 
868  C CG2 . ILE A 120 ? 0.3829 0.6108 0.3007 -0.1445 -0.0888 0.1021  120 ILE A CG2 
869  C CD1 . ILE A 120 ? 0.3538 0.5728 0.3085 -0.1481 -0.0758 0.1152  120 ILE A CD1 
870  N N   . TYR A 121 ? 0.3828 0.5930 0.2830 -0.1617 -0.1308 0.1075  121 TYR A N   
871  C CA  . TYR A 121 ? 0.3843 0.5930 0.2888 -0.1675 -0.1330 0.1127  121 TYR A CA  
872  C C   . TYR A 121 ? 0.3632 0.5900 0.2901 -0.1675 -0.1267 0.1257  121 TYR A C   
873  O O   . TYR A 121 ? 0.3595 0.5793 0.2922 -0.1719 -0.1276 0.1247  121 TYR A O   
874  C CB  . TYR A 121 ? 0.3998 0.6217 0.2947 -0.1697 -0.1350 0.1194  121 TYR A CB  
875  C CG  . TYR A 121 ? 0.4081 0.6325 0.3028 -0.1793 -0.1383 0.1221  121 TYR A CG  
876  C CD1 . TYR A 121 ? 0.4339 0.6338 0.3069 -0.1879 -0.1464 0.1118  121 TYR A CD1 
877  C CD2 . TYR A 121 ? 0.3941 0.6471 0.3077 -0.1800 -0.1333 0.1357  121 TYR A CD2 
878  C CE1 . TYR A 121 ? 0.4873 0.6924 0.3579 -0.2010 -0.1490 0.1155  121 TYR A CE1 
879  C CE2 . TYR A 121 ? 0.4500 0.7127 0.3631 -0.1906 -0.1356 0.1385  121 TYR A CE2 
880  C CZ  . TYR A 121 ? 0.4884 0.7278 0.3803 -0.2029 -0.1433 0.1288  121 TYR A CZ  
881  O OH  . TYR A 121 ? 0.5251 0.7766 0.4147 -0.2171 -0.1451 0.1329  121 TYR A OH  
882  N N   . GLU A 122 ? 0.3847 0.6321 0.3197 -0.1614 -0.1199 0.1384  122 GLU A N   
883  C CA  . GLU A 122 ? 0.3754 0.6390 0.3259 -0.1568 -0.1134 0.1537  122 GLU A CA  
884  C C   . GLU A 122 ? 0.3578 0.6031 0.3220 -0.1564 -0.1074 0.1454  122 GLU A C   
885  O O   . GLU A 122 ? 0.6635 0.8937 0.6297 -0.1531 -0.0975 0.1359  122 GLU A O   
886  C CB  . GLU A 122 ? 0.4577 0.7286 0.4062 -0.1439 -0.0989 0.1673  122 GLU A CB  
887  C CG  . GLU A 122 ? 0.4717 0.7612 0.4046 -0.1401 -0.1018 0.1771  122 GLU A CG  
888  C CD  . GLU A 122 ? 0.4543 0.7295 0.3742 -0.1402 -0.0981 0.1672  122 GLU A CD  
889  O OE1 . GLU A 122 ? 0.4483 0.7305 0.3564 -0.1326 -0.0921 0.1762  122 GLU A OE1 
890  O OE2 . GLU A 122 ? 0.4119 0.6696 0.3330 -0.1457 -0.0996 0.1506  122 GLU A OE2 
891  N N   . CYS A 123 ? 0.3218 0.5695 0.2962 -0.1601 -0.1119 0.1474  123 CYS A N   
892  C CA  . CYS A 123 ? 0.3101 0.5399 0.2988 -0.1574 -0.1033 0.1400  123 CYS A CA  
893  C C   . CYS A 123 ? 0.3048 0.5423 0.3050 -0.1488 -0.0928 0.1548  123 CYS A C   
894  O O   . CYS A 123 ? 0.3565 0.6135 0.3599 -0.1497 -0.0997 0.1646  123 CYS A O   
895  C CB  . CYS A 123 ? 0.3065 0.5197 0.2939 -0.1646 -0.1135 0.1259  123 CYS A CB  
896  S SG  . CYS A 123 ? 0.2900 0.4901 0.2962 -0.1628 -0.1071 0.1187  123 CYS A SG  
897  N N   . PRO A 124 ? 0.2926 0.5146 0.2957 -0.1406 -0.0760 0.1564  124 PRO A N   
898  C CA  . PRO A 124 ? 0.2958 0.5148 0.3026 -0.1297 -0.0647 0.1693  124 PRO A CA  
899  C C   . PRO A 124 ? 0.2812 0.5024 0.3006 -0.1317 -0.0703 0.1678  124 PRO A C   
900  O O   . PRO A 124 ? 0.2832 0.5151 0.3041 -0.1215 -0.0669 0.1811  124 PRO A O   
901  C CB  . PRO A 124 ? 0.3073 0.4974 0.3106 -0.1282 -0.0471 0.1642  124 PRO A CB  
902  C CG  . PRO A 124 ? 0.3125 0.5031 0.3090 -0.1347 -0.0475 0.1552  124 PRO A CG  
903  C CD  . PRO A 124 ? 0.2994 0.5053 0.2989 -0.1423 -0.0663 0.1456  124 PRO A CD  
904  N N   . ILE A 125 ? 0.2705 0.4821 0.2967 -0.1425 -0.0785 0.1520  125 ILE A N   
905  C CA  . ILE A 125 ? 0.2588 0.4706 0.2946 -0.1451 -0.0841 0.1503  125 ILE A CA  
906  C C   . ILE A 125 ? 0.2568 0.4983 0.2910 -0.1490 -0.0964 0.1615  125 ILE A C   
907  O O   . ILE A 125 ? 0.2537 0.5112 0.2940 -0.1423 -0.0939 0.1730  125 ILE A O   
908  C CB  . ILE A 125 ? 0.2514 0.4456 0.2897 -0.1543 -0.0917 0.1309  125 ILE A CB  
909  C CG1 . ILE A 125 ? 0.2523 0.4277 0.2953 -0.1517 -0.0788 0.1197  125 ILE A CG1 
910  C CG2 . ILE A 125 ? 0.2452 0.4329 0.2866 -0.1543 -0.0958 0.1287  125 ILE A CG2 
911  C CD1 . ILE A 125 ? 0.2457 0.4095 0.2919 -0.1563 -0.0853 0.0996  125 ILE A CD1 
912  N N   . ILE A 126 ? 0.2857 0.5271 0.3067 -0.1566 -0.1040 0.1555  126 ILE A N   
913  C CA  . ILE A 126 ? 0.3019 0.5546 0.3153 -0.1602 -0.1054 0.1588  126 ILE A CA  
914  C C   . ILE A 126 ? 0.2944 0.5867 0.3161 -0.1512 -0.1009 0.1767  126 ILE A C   
915  O O   . ILE A 126 ? 0.2941 0.6070 0.3212 -0.1498 -0.0984 0.1828  126 ILE A O   
916  C CB  . ILE A 126 ? 0.3819 0.6199 0.3772 -0.1688 -0.1110 0.1483  126 ILE A CB  
917  C CG1 . ILE A 126 ? 0.3397 0.5388 0.3245 -0.1714 -0.1150 0.1304  126 ILE A CG1 
918  C CG2 . ILE A 126 ? 0.3242 0.5775 0.3120 -0.1772 -0.1127 0.1525  126 ILE A CG2 
919  C CD1 . ILE A 126 ? 0.3350 0.5151 0.2997 -0.1763 -0.1214 0.1192  126 ILE A CD1 
920  N N   . GLU A 127 ? 0.3194 0.6211 0.3390 -0.1422 -0.0986 0.1849  127 GLU A N   
921  C CA  . GLU A 127 ? 0.3265 0.6565 0.3476 -0.1252 -0.0914 0.2004  127 GLU A CA  
922  C C   . GLU A 127 ? 0.3500 0.6846 0.3784 -0.1096 -0.0834 0.2104  127 GLU A C   
923  O O   . GLU A 127 ? 0.3314 0.6956 0.3654 -0.0984 -0.0797 0.2174  127 GLU A O   
924  C CB  . GLU A 127 ? 0.3912 0.7120 0.3984 -0.1148 -0.0856 0.2071  127 GLU A CB  
925  C CG  . GLU A 127 ? 0.4615 0.7849 0.4607 -0.1258 -0.0929 0.1990  127 GLU A CG  
926  C CD  . GLU A 127 ? 0.5387 0.8476 0.5217 -0.1180 -0.0860 0.2045  127 GLU A CD  
927  O OE1 . GLU A 127 ? 0.4096 0.6890 0.3905 -0.1104 -0.0715 0.2045  127 GLU A OE1 
928  O OE2 . GLU A 127 ? 0.5809 0.9001 0.5565 -0.1193 -0.0894 0.2026  127 GLU A OE2 
929  N N   . THR A 128 ? 0.3095 0.6130 0.3364 -0.1086 -0.0791 0.2093  128 THR A N   
930  C CA  . THR A 128 ? 0.3064 0.6029 0.3360 -0.0926 -0.0686 0.2166  128 THR A CA  
931  C C   . THR A 128 ? 0.2914 0.6152 0.3357 -0.0987 -0.0766 0.2151  128 THR A C   
932  O O   . THR A 128 ? 0.4403 0.7851 0.4886 -0.0827 -0.0703 0.2231  128 THR A O   
933  C CB  . THR A 128 ? 0.3094 0.5566 0.3388 -0.0933 -0.0569 0.2051  128 THR A CB  
934  O OG1 . THR A 128 ? 0.3262 0.5465 0.3427 -0.0915 -0.0464 0.2028  128 THR A OG1 
935  C CG2 . THR A 128 ? 0.3183 0.5540 0.3456 -0.0766 -0.0463 0.2128  128 THR A CG2 
936  N N   . LEU A 129 ? 0.3016 0.6180 0.3516 -0.1204 -0.0867 0.2015  129 LEU A N   
937  C CA  . LEU A 129 ? 0.3213 0.6474 0.3769 -0.1279 -0.0876 0.1975  129 LEU A CA  
938  C C   . LEU A 129 ? 0.3955 0.7571 0.4492 -0.1308 -0.0864 0.2016  129 LEU A C   
939  O O   . LEU A 129 ? 0.3070 0.6865 0.3629 -0.1335 -0.0846 0.2037  129 LEU A O   
940  C CB  . LEU A 129 ? 0.2968 0.5851 0.3432 -0.1444 -0.0936 0.1805  129 LEU A CB  
941  C CG  . LEU A 129 ? 0.3190 0.5781 0.3718 -0.1422 -0.0938 0.1730  129 LEU A CG  
942  C CD1 . LEU A 129 ? 0.2915 0.5127 0.3318 -0.1501 -0.0976 0.1540  129 LEU A CD1 
943  C CD2 . LEU A 129 ? 0.4103 0.6856 0.4779 -0.1302 -0.0894 0.1854  129 LEU A CD2 
944  N N   . MET A 130 ? 0.4919 0.8657 0.5404 -0.1307 -0.0874 0.2032  130 MET A N   
945  C CA  . MET A 130 ? 0.3389 0.7491 0.3854 -0.1347 -0.0870 0.2071  130 MET A CA  
946  C C   . MET A 130 ? 0.3804 0.8337 0.4367 -0.1115 -0.0792 0.2202  130 MET A C   
947  O O   . MET A 130 ? 0.4337 0.9247 0.4924 -0.1142 -0.0774 0.2240  130 MET A O   
948  C CB  . MET A 130 ? 0.3994 0.8056 0.4358 -0.1420 -0.0914 0.2032  130 MET A CB  
949  C CG  . MET A 130 ? 0.4013 0.7765 0.4218 -0.1647 -0.0987 0.1905  130 MET A CG  
950  S SD  . MET A 130 ? 0.4115 0.7834 0.4183 -0.1728 -0.1042 0.1857  130 MET A SD  
951  C CE  . MET A 130 ? 0.5214 0.8668 0.5072 -0.1974 -0.1110 0.1751  130 MET A CE  
952  N N   . LYS A 131 ? 0.3767 0.8210 0.4326 -0.0872 -0.0737 0.2272  131 LYS A N   
953  C CA  . LYS A 131 ? 0.5039 0.9779 0.5598 -0.0583 -0.0648 0.2388  131 LYS A CA  
954  C C   . LYS A 131 ? 0.5541 1.0360 0.6169 -0.0480 -0.0597 0.2421  131 LYS A C   
955  O O   . LYS A 131 ? 0.5875 1.0440 0.6427 -0.0252 -0.0522 0.2473  131 LYS A O   
956  C CB  . LYS A 131 ? 0.3724 0.8179 0.4121 -0.0335 -0.0576 0.2455  131 LYS A CB  
957  N N   . PHE B 3   ? 0.3530 0.5580 0.9557 -0.0101 -0.0071 -0.0210 3   PHE B N   
958  C CA  . PHE B 3   ? 0.3785 0.5778 0.9775 -0.0145 -0.0138 -0.0273 3   PHE B CA  
959  C C   . PHE B 3   ? 0.4073 0.6011 1.0038 -0.0203 -0.0142 -0.0328 3   PHE B C   
960  O O   . PHE B 3   ? 0.4880 0.6767 1.0825 -0.0210 -0.0174 -0.0445 3   PHE B O   
961  C CB  . PHE B 3   ? 0.5187 0.7241 1.1173 -0.0177 -0.0212 -0.0156 3   PHE B CB  
962  C CG  . PHE B 3   ? 0.4564 0.6562 1.0542 -0.0190 -0.0301 -0.0224 3   PHE B CG  
963  C CD1 . PHE B 3   ? 0.4462 0.6521 1.0461 -0.0173 -0.0347 -0.0163 3   PHE B CD1 
964  C CD2 . PHE B 3   ? 0.5478 0.7382 1.1433 -0.0217 -0.0346 -0.0345 3   PHE B CD2 
965  C CE1 . PHE B 3   ? 0.5442 0.7435 1.1443 -0.0189 -0.0446 -0.0219 3   PHE B CE1 
966  C CE2 . PHE B 3   ? 0.4919 0.6762 1.0874 -0.0219 -0.0443 -0.0417 3   PHE B CE2 
967  C CZ  . PHE B 3   ? 0.5097 0.6968 1.1076 -0.0208 -0.0498 -0.0352 3   PHE B CZ  
968  N N   . ARG B 4   ? 0.3782 0.5750 0.9749 -0.0239 -0.0109 -0.0252 4   ARG B N   
969  C CA  . ARG B 4   ? 0.3794 0.5756 0.9732 -0.0297 -0.0121 -0.0290 4   ARG B CA  
970  C C   . ARG B 4   ? 0.3702 0.5671 0.9660 -0.0313 -0.0052 -0.0297 4   ARG B C   
971  O O   . ARG B 4   ? 0.4101 0.6066 1.0104 -0.0286 -0.0009 -0.0242 4   ARG B O   
972  C CB  . ARG B 4   ? 0.3948 0.5950 0.9868 -0.0348 -0.0174 -0.0182 4   ARG B CB  
973  C CG  . ARG B 4   ? 0.2904 0.4924 0.8834 -0.0341 -0.0231 -0.0082 4   ARG B CG  
974  C CD  . ARG B 4   ? 0.3370 0.5343 0.9296 -0.0336 -0.0320 -0.0157 4   ARG B CD  
975  N NE  . ARG B 4   ? 0.3854 0.5858 0.9798 -0.0343 -0.0384 -0.0039 4   ARG B NE  
976  N N   . ILE B 5   ? 0.3479 0.5477 0.9414 -0.0359 -0.0051 -0.0355 5   ILE B N   
977  C CA  . ILE B 5   ? 0.3958 0.5980 0.9918 -0.0388 0.0004  -0.0361 5   ILE B CA  
978  C C   . ILE B 5   ? 0.4612 0.6711 1.0567 -0.0455 0.0021  -0.0267 5   ILE B C   
979  O O   . ILE B 5   ? 0.7062 0.9193 1.3043 -0.0491 0.0058  -0.0261 5   ILE B O   
980  C CB  . ILE B 5   ? 0.4208 0.6252 1.0159 -0.0394 0.0009  -0.0497 5   ILE B CB  
981  N N   . GLY B 6   ? 0.3845 0.5977 0.9771 -0.0479 -0.0012 -0.0190 6   GLY B N   
982  C CA  . GLY B 6   ? 0.4517 0.6707 1.0443 -0.0535 0.0006  -0.0082 6   GLY B CA  
983  C C   . GLY B 6   ? 0.5011 0.7319 1.0905 -0.0592 -0.0011 -0.0121 6   GLY B C   
984  O O   . GLY B 6   ? 0.5504 0.7874 1.1387 -0.0638 -0.0023 -0.0040 6   GLY B O   
985  N N   . GLU B 7   ? 0.3956 0.6312 0.9847 -0.0585 -0.0015 -0.0250 7   GLU B N   
986  C CA  . GLU B 7   ? 0.3928 0.6426 0.9808 -0.0614 -0.0048 -0.0321 7   GLU B CA  
987  C C   . GLU B 7   ? 0.4381 0.6815 1.0255 -0.0575 -0.0139 -0.0369 7   GLU B C   
988  O O   . GLU B 7   ? 0.4346 0.6835 1.0226 -0.0595 -0.0203 -0.0359 7   GLU B O   
989  C CB  . GLU B 7   ? 0.5759 0.8356 1.1650 -0.0614 -0.0018 -0.0442 7   GLU B CB  
990  N N   . LEU B 8   ? 0.3964 0.6274 0.9837 -0.0521 -0.0151 -0.0411 8   LEU B N   
991  C CA  . LEU B 8   ? 0.4299 0.6512 1.0172 -0.0491 -0.0232 -0.0397 8   LEU B CA  
992  C C   . LEU B 8   ? 0.5422 0.7606 1.1294 -0.0512 -0.0213 -0.0226 8   LEU B C   
993  O O   . LEU B 8   ? 0.5286 0.7501 1.1159 -0.0533 -0.0142 -0.0158 8   LEU B O   
994  C CB  . LEU B 8   ? 0.4950 0.7067 1.0826 -0.0434 -0.0233 -0.0472 8   LEU B CB  
995  C CG  . LEU B 8   ? 0.4618 0.6729 1.0494 -0.0397 -0.0222 -0.0633 8   LEU B CG  
996  C CD1 . LEU B 8   ? 0.4895 0.7128 1.0772 -0.0421 -0.0167 -0.0708 8   LEU B CD1 
997  C CD2 . LEU B 8   ? 0.3344 0.5356 0.9228 -0.0349 -0.0187 -0.0640 8   LEU B CD2 
998  N N   . ALA B 9   ? 0.4032 0.6171 0.9906 -0.0511 -0.0283 -0.0149 9   ALA B N   
999  C CA  . ALA B 9   ? 0.4771 0.6908 1.0647 -0.0524 -0.0259 0.0015  9   ALA B CA  
1000 C C   . ALA B 9   ? 0.3870 0.6070 0.9736 -0.0579 -0.0254 0.0087  9   ALA B C   
1001 O O   . ALA B 9   ? 0.5842 0.8045 1.1707 -0.0596 -0.0257 0.0218  9   ALA B O   
1002 C CB  . ALA B 9   ? 0.3763 0.5882 0.9656 -0.0483 -0.0168 0.0047  9   ALA B CB  
1003 N N   . ASP B 10  ? 0.4389 0.6662 1.0252 -0.0605 -0.0248 -0.0002 10  ASP B N   
1004 C CA  . ASP B 10  ? 0.4693 0.7054 1.0556 -0.0659 -0.0272 0.0040  10  ASP B CA  
1005 C C   . ASP B 10  ? 0.5364 0.7708 1.1243 -0.0660 -0.0403 -0.0002 10  ASP B C   
1006 O O   . ASP B 10  ? 0.6176 0.8592 1.2070 -0.0693 -0.0463 -0.0006 10  ASP B O   
1007 C CB  . ASP B 10  ? 0.4599 0.7089 1.0465 -0.0686 -0.0217 -0.0034 10  ASP B CB  
1008 N N   . LYS B 11  ? 0.6217 0.8462 1.2100 -0.0622 -0.0458 -0.0036 11  LYS B N   
1009 C CA  . LYS B 11  ? 0.3910 0.6083 0.9809 -0.0622 -0.0605 -0.0040 11  LYS B CA  
1010 C C   . LYS B 11  ? 0.4108 0.6242 1.0001 -0.0659 -0.0652 0.0139  11  LYS B C   
1011 O O   . LYS B 11  ? 0.5653 0.7716 1.1556 -0.0672 -0.0783 0.0175  11  LYS B O   
1012 C CB  . LYS B 11  ? 0.2959 0.5042 0.8860 -0.0578 -0.0634 -0.0097 11  LYS B CB  
1013 N N   . CYS B 12  ? 0.4971 0.7147 1.0848 -0.0674 -0.0551 0.0256  12  CYS B N   
1014 C CA  . CYS B 12  ? 0.4214 0.6380 1.0086 -0.0707 -0.0586 0.0423  12  CYS B CA  
1015 C C   . CYS B 12  ? 0.3914 0.6131 0.9787 -0.0753 -0.0624 0.0436  12  CYS B C   
1016 O O   . CYS B 12  ? 0.3527 0.5742 0.9393 -0.0785 -0.0650 0.0570  12  CYS B O   
1017 C CB  . CYS B 12  ? 0.4101 0.6289 0.9963 -0.0686 -0.0472 0.0535  12  CYS B CB  
1018 S SG  . CYS B 12  ? 0.3850 0.6018 0.9726 -0.0631 -0.0444 0.0554  12  CYS B SG  
1019 N N   . GLY B 13  ? 0.4652 0.6939 1.0539 -0.0754 -0.0623 0.0298  13  GLY B N   
1020 C CA  . GLY B 13  ? 0.2984 0.5365 0.8884 -0.0794 -0.0655 0.0297  13  GLY B CA  
1021 C C   . GLY B 13  ? 0.2958 0.5416 0.8836 -0.0822 -0.0530 0.0386  13  GLY B C   
1022 O O   . GLY B 13  ? 0.2993 0.5500 0.8872 -0.0863 -0.0554 0.0462  13  GLY B O   
1023 N N   . VAL B 14  ? 0.2904 0.5357 0.8762 -0.0800 -0.0411 0.0379  14  VAL B N   
1024 C CA  . VAL B 14  ? 0.2901 0.5401 0.8742 -0.0825 -0.0310 0.0459  14  VAL B CA  
1025 C C   . VAL B 14  ? 0.2881 0.5463 0.8726 -0.0827 -0.0233 0.0358  14  VAL B C   
1026 O O   . VAL B 14  ? 0.2850 0.5391 0.8698 -0.0785 -0.0211 0.0267  14  VAL B O   
1027 C CB  . VAL B 14  ? 0.3422 0.5824 0.9252 -0.0793 -0.0259 0.0574  14  VAL B CB  
1028 C CG1 . VAL B 14  ? 0.2911 0.5335 0.8738 -0.0816 -0.0188 0.0668  14  VAL B CG1 
1029 C CG2 . VAL B 14  ? 0.2910 0.5258 0.8740 -0.0789 -0.0335 0.0672  14  VAL B CG2 
1030 N N   . ASN B 15  ? 0.3043 0.5753 0.8890 -0.0879 -0.0197 0.0378  15  ASN B N   
1031 C CA  . ASN B 15  ? 0.3037 0.5853 0.8891 -0.0895 -0.0127 0.0304  15  ASN B CA  
1032 C C   . ASN B 15  ? 0.3038 0.5745 0.8884 -0.0882 -0.0053 0.0361  15  ASN B C   
1033 O O   . ASN B 15  ? 0.3051 0.5651 0.8894 -0.0870 -0.0047 0.0471  15  ASN B O   
1034 C CB  . ASN B 15  ? 0.3071 0.6098 0.8939 -0.0964 -0.0112 0.0322  15  ASN B CB  
1035 C CG  . ASN B 15  ? 0.3644 0.6651 0.9490 -0.1014 -0.0095 0.0482  15  ASN B CG  
1036 O OD1 . ASN B 15  ? 0.4755 0.7634 1.0586 -0.1009 -0.0053 0.0570  15  ASN B OD1 
1037 N ND2 . ASN B 15  ? 0.3613 0.6760 0.9472 -0.1058 -0.0135 0.0513  15  ASN B ND2 
1038 N N   . LYS B 16  ? 0.3867 0.6616 0.9725 -0.0882 -0.0006 0.0285  16  LYS B N   
1039 C CA  . LYS B 16  ? 0.3855 0.6469 0.9732 -0.0841 0.0031  0.0287  16  LYS B CA  
1040 C C   . LYS B 16  ? 0.4963 0.7509 1.0862 -0.0862 0.0052  0.0426  16  LYS B C   
1041 O O   . LYS B 16  ? 0.3165 0.5785 0.9073 -0.0928 0.0073  0.0490  16  LYS B O   
1042 C CB  . LYS B 16  ? 0.3551 0.6234 0.9445 -0.0853 0.0068  0.0194  16  LYS B CB  
1043 N N   . GLU B 17  ? 0.6850 0.9267 1.2770 -0.0801 0.0040  0.0471  17  GLU B N   
1044 C CA  . GLU B 17  ? 0.5382 0.7753 1.1330 -0.0805 0.0037  0.0605  17  GLU B CA  
1045 C C   . GLU B 17  ? 0.5336 0.7607 1.1378 -0.0754 0.0054  0.0637  17  GLU B C   
1046 O O   . GLU B 17  ? 0.4298 0.6512 1.0379 -0.0680 0.0049  0.0637  17  GLU B O   
1047 C CB  . GLU B 17  ? 0.2959 0.5310 0.8878 -0.0776 -0.0003 0.0652  17  GLU B CB  
1048 C CG  . GLU B 17  ? 0.3000 0.5354 0.8924 -0.0802 -0.0017 0.0788  17  GLU B CG  
1049 C CD  . GLU B 17  ? 0.4372 0.6827 1.0248 -0.0886 -0.0030 0.0814  17  GLU B CD  
1050 O OE1 . GLU B 17  ? 0.4717 0.7261 1.0581 -0.0930 -0.0010 0.0746  17  GLU B OE1 
1051 O OE2 . GLU B 17  ? 0.3720 0.6188 0.9577 -0.0906 -0.0065 0.0901  17  GLU B OE2 
1052 N N   . THR B 18  ? 0.4630 0.6898 1.0726 -0.0799 0.0065  0.0683  18  THR B N   
1053 C CA  . THR B 18  ? 0.4729 0.6900 1.0958 -0.0755 0.0061  0.0714  18  THR B CA  
1054 C C   . THR B 18  ? 0.4186 0.6332 1.0471 -0.0739 0.0040  0.0839  18  THR B C   
1055 O O   . THR B 18  ? 0.4253 0.6338 1.0669 -0.0672 0.0028  0.0859  18  THR B O   
1056 C CB  . THR B 18  ? 0.5465 0.7629 1.1756 -0.0817 0.0060  0.0719  18  THR B CB  
1057 N N   . ILE B 19  ? 0.3114 0.5319 0.9313 -0.0796 0.0031  0.0917  19  ILE B N   
1058 C CA  . ILE B 19  ? 0.3150 0.5334 0.9408 -0.0789 0.0007  0.1044  19  ILE B CA  
1059 C C   . ILE B 19  ? 0.3091 0.5262 0.9389 -0.0695 0.0004  0.1049  19  ILE B C   
1060 O O   . ILE B 19  ? 0.4384 0.6534 1.0805 -0.0644 -0.0009 0.1116  19  ILE B O   
1061 C CB  . ILE B 19  ? 0.3946 0.6200 1.0100 -0.0869 -0.0007 0.1126  19  ILE B CB  
1062 C CG1 . ILE B 19  ? 0.4223 0.6446 1.0450 -0.0860 -0.0036 0.1262  19  ILE B CG1 
1063 C CG2 . ILE B 19  ? 0.4066 0.6380 1.0106 -0.0869 -0.0012 0.1081  19  ILE B CG2 
1064 C CD1 . ILE B 19  ? 0.3958 0.6241 1.0092 -0.0931 -0.0055 0.1349  19  ILE B CD1 
1065 N N   . ARG B 20  ? 0.3396 0.5596 0.9608 -0.0670 0.0013  0.0978  20  ARG B N   
1066 C CA  . ARG B 20  ? 0.2820 0.5041 0.9051 -0.0594 0.0008  0.1000  20  ARG B CA  
1067 C C   . ARG B 20  ? 0.2803 0.5005 0.9174 -0.0501 0.0024  0.0969  20  ARG B C   
1068 O O   . ARG B 20  ? 0.2805 0.5049 0.9257 -0.0441 0.0019  0.1039  20  ARG B O   
1069 C CB  . ARG B 20  ? 0.2773 0.5018 0.8898 -0.0595 0.0000  0.0930  20  ARG B CB  
1070 C CG  . ARG B 20  ? 0.2778 0.5063 0.8830 -0.0624 -0.0039 0.1007  20  ARG B CG  
1071 C CD  . ARG B 20  ? 0.2827 0.5125 0.8835 -0.0702 -0.0059 0.1063  20  ARG B CD  
1072 N NE  . ARG B 20  ? 0.2829 0.5155 0.8760 -0.0741 -0.0111 0.1078  20  ARG B NE  
1073 C CZ  . ARG B 20  ? 0.2950 0.5303 0.8845 -0.0801 -0.0144 0.1142  20  ARG B CZ  
1074 N NH1 . ARG B 20  ? 0.4111 0.6470 1.0025 -0.0831 -0.0123 0.1202  20  ARG B NH1 
1075 N NH2 . ARG B 20  ? 0.2882 0.5255 0.8734 -0.0832 -0.0208 0.1149  20  ARG B NH2 
1076 N N   . TYR B 21  ? 0.3617 0.5774 1.0027 -0.0481 0.0038  0.0861  21  TYR B N   
1077 C CA  . TYR B 21  ? 0.4718 0.6863 1.1283 -0.0381 0.0042  0.0822  21  TYR B CA  
1078 C C   . TYR B 21  ? 0.4579 0.6673 1.1315 -0.0383 0.0014  0.0875  21  TYR B C   
1079 O O   . TYR B 21  ? 0.4767 0.6874 1.1665 -0.0287 -0.0003 0.0873  21  TYR B O   
1080 C CB  . TYR B 21  ? 0.4016 0.6129 1.0578 -0.0339 0.0057  0.0683  21  TYR B CB  
1081 C CG  . TYR B 21  ? 0.5170 0.7214 1.1717 -0.0399 0.0059  0.0598  21  TYR B CG  
1082 C CD1 . TYR B 21  ? 0.5930 0.7903 1.2629 -0.0394 0.0040  0.0571  21  TYR B CD1 
1083 C CD2 . TYR B 21  ? 0.4593 0.6651 1.0990 -0.0450 0.0072  0.0534  21  TYR B CD2 
1084 C CE1 . TYR B 21  ? 0.4919 0.6848 1.1603 -0.0453 0.0040  0.0501  21  TYR B CE1 
1085 C CE2 . TYR B 21  ? 0.4420 0.6449 1.0801 -0.0495 0.0078  0.0452  21  TYR B CE2 
1086 C CZ  . TYR B 21  ? 0.5302 0.7272 1.1817 -0.0501 0.0067  0.0442  21  TYR B CZ  
1087 O OH  . TYR B 21  ? 0.5800 0.7761 1.2294 -0.0555 0.0072  0.0373  21  TYR B OH  
1088 N N   . TYR B 22  ? 0.3561 0.5615 1.0265 -0.0487 0.0000  0.0923  22  TYR B N   
1089 C CA  . TYR B 22  ? 0.3304 0.5306 1.0162 -0.0513 -0.0044 0.1005  22  TYR B CA  
1090 C C   . TYR B 22  ? 0.3712 0.5766 1.0635 -0.0462 -0.0060 0.1108  22  TYR B C   
1091 O O   . TYR B 22  ? 0.3507 0.5539 1.0633 -0.0408 -0.0105 0.1146  22  TYR B O   
1092 C CB  . TYR B 22  ? 0.3645 0.5631 1.0401 -0.0645 -0.0051 0.1060  22  TYR B CB  
1093 C CG  . TYR B 22  ? 0.3453 0.5362 1.0327 -0.0694 -0.0089 0.1055  22  TYR B CG  
1094 C CD2 . TYR B 22  ? 0.3561 0.5493 1.0326 -0.0813 -0.0086 0.1086  22  TYR B CD2 
1095 C CE2 . TYR B 22  ? 0.3451 0.5487 1.0014 -0.0880 -0.0048 0.1105  22  TYR B CE2 
1096 N N   . GLU B 23  ? 0.2973 0.5100 0.9738 -0.0477 -0.0035 0.1151  23  GLU B N   
1097 C CA  . GLU B 23  ? 0.2976 0.5172 0.9781 -0.0434 -0.0048 0.1254  23  GLU B CA  
1098 C C   . GLU B 23  ? 0.2925 0.5218 0.9768 -0.0312 -0.0028 0.1223  23  GLU B C   
1099 O O   . GLU B 23  ? 0.4561 0.6942 1.1410 -0.0276 -0.0032 0.1309  23  GLU B O   
1100 C CB  . GLU B 23  ? 0.3250 0.5479 0.9878 -0.0515 -0.0047 0.1331  23  GLU B CB  
1101 C CG  . GLU B 23  ? 0.4445 0.6630 1.1059 -0.0610 -0.0075 0.1412  23  GLU B CG  
1102 C CD  . GLU B 23  ? 0.5714 0.7934 1.2139 -0.0690 -0.0075 0.1444  23  GLU B CD  
1103 O OE1 . GLU B 23  ? 0.3597 0.5860 0.9926 -0.0671 -0.0066 0.1410  23  GLU B OE1 
1104 O OE2 . GLU B 23  ? 0.6688 0.8898 1.3069 -0.0772 -0.0093 0.1501  23  GLU B OE2 
1105 N N   . ARG B 24  ? 0.3147 0.5439 0.9994 -0.0251 -0.0006 0.1105  24  ARG B N   
1106 C CA  . ARG B 24  ? 0.3511 0.5916 1.0364 -0.0127 0.0015  0.1064  24  ARG B CA  
1107 C C   . ARG B 24  ? 0.3073 0.5568 0.9749 -0.0155 0.0038  0.1099  24  ARG B C   
1108 O O   . ARG B 24  ? 0.3534 0.6139 1.0184 -0.0074 0.0056  0.1074  24  ARG B O   
1109 C CB  . ARG B 24  ? 0.4835 0.7327 1.1836 -0.0015 -0.0006 0.1114  24  ARG B CB  
1110 C CG  . ARG B 24  ? 0.4372 0.7051 1.1322 0.0103  0.0020  0.1124  24  ARG B CG  
1111 C CD  . ARG B 24  ? 0.4309 0.7091 1.1319 0.0144  0.0002  0.1237  24  ARG B CD  
1112 N NE  . ARG B 24  ? 0.5170 0.8167 1.2103 0.0235  0.0032  0.1266  24  ARG B NE  
1113 C CZ  . ARG B 24  ? 0.4569 0.7663 1.1383 0.0164  0.0047  0.1370  24  ARG B CZ  
1114 N NH1 . ARG B 24  ? 0.3151 0.6132 0.9890 0.0016  0.0031  0.1441  24  ARG B NH1 
1115 N NH2 . ARG B 24  ? 0.4501 0.7814 1.1266 0.0247  0.0070  0.1402  24  ARG B NH2 
1116 N N   . LEU B 25  ? 0.2764 0.5213 0.9319 -0.0269 0.0026  0.1151  25  LEU B N   
1117 C CA  . LEU B 25  ? 0.3253 0.5762 0.9669 -0.0302 0.0020  0.1185  25  LEU B CA  
1118 C C   . LEU B 25  ? 0.3136 0.5640 0.9492 -0.0284 0.0032  0.1078  25  LEU B C   
1119 O O   . LEU B 25  ? 0.3357 0.5959 0.9676 -0.0247 0.0032  0.1097  25  LEU B O   
1120 C CB  . LEU B 25  ? 0.2992 0.5440 0.9301 -0.0415 -0.0011 0.1237  25  LEU B CB  
1121 C CG  . LEU B 25  ? 0.2807 0.5264 0.9149 -0.0446 -0.0032 0.1357  25  LEU B CG  
1122 C CD1 . LEU B 25  ? 0.2832 0.5236 0.9055 -0.0549 -0.0064 0.1375  25  LEU B CD1 
1123 C CD2 . LEU B 25  ? 0.2814 0.5393 0.9189 -0.0395 -0.0038 0.1464  25  LEU B CD2 
1124 N N   . GLY B 26  ? 0.4346 0.6744 1.0694 -0.0314 0.0038  0.0973  26  GLY B N   
1125 C CA  . GLY B 26  ? 0.4762 0.7142 1.1065 -0.0296 0.0047  0.0862  26  GLY B CA  
1126 C C   . GLY B 26  ? 0.3266 0.5643 0.9681 -0.0200 0.0072  0.0777  26  GLY B C   
1127 O O   . GLY B 26  ? 0.2976 0.5320 0.9508 -0.0172 0.0072  0.0782  26  GLY B O   
1128 N N   . LEU B 27  ? 0.3762 0.6162 1.0148 -0.0150 0.0081  0.0695  27  LEU B N   
1129 C CA  . LEU B 27  ? 0.3740 0.6144 1.0221 -0.0044 0.0097  0.0603  27  LEU B CA  
1130 C C   . LEU B 27  ? 0.4553 0.6812 1.1089 -0.0079 0.0092  0.0502  27  LEU B C   
1131 O O   . LEU B 27  ? 0.4082 0.6271 1.0557 -0.0182 0.0086  0.0504  27  LEU B O   
1132 C CB  . LEU B 27  ? 0.3829 0.6316 1.0241 0.0012  0.0105  0.0558  27  LEU B CB  
1133 C CG  . LEU B 27  ? 0.4620 0.7199 1.1089 0.0155  0.0121  0.0500  27  LEU B CG  
1134 C CD1 . LEU B 27  ? 0.5411 0.8125 1.1923 0.0214  0.0126  0.0604  27  LEU B CD1 
1135 C CD2 . LEU B 27  ? 0.5516 0.8194 1.1894 0.0181  0.0126  0.0482  27  LEU B CD2 
1136 N N   . ILE B 28  ? 0.4126 0.6350 1.0767 0.0009  0.0090  0.0407  28  ILE B N   
1137 C CA  . ILE B 28  ? 0.4243 0.6336 1.0940 -0.0036 0.0078  0.0314  28  ILE B CA  
1138 C C   . ILE B 28  ? 0.3138 0.5210 0.9748 -0.0025 0.0089  0.0200  28  ILE B C   
1139 O O   . ILE B 28  ? 0.4057 0.6197 1.0630 0.0065  0.0097  0.0163  28  ILE B O   
1140 C CB  . ILE B 28  ? 0.4646 0.6677 1.1541 0.0036  0.0042  0.0273  28  ILE B CB  
1141 C CG1 . ILE B 28  ? 0.4468 0.6386 1.1454 -0.0073 0.0015  0.0279  28  ILE B CG1 
1142 C CG2 . ILE B 28  ? 0.5273 0.7309 1.2199 0.0177  0.0033  0.0151  28  ILE B CG2 
1143 C CD1 . ILE B 28  ? 0.4043 0.5884 1.1269 -0.0023 -0.0052 0.0266  28  ILE B CD1 
1144 N N   . PRO B 29  ? 0.3091 0.5087 0.9654 -0.0112 0.0089  0.0148  29  PRO B N   
1145 C CA  . PRO B 29  ? 0.3290 0.5274 0.9779 -0.0084 0.0094  0.0039  29  PRO B CA  
1146 C C   . PRO B 29  ? 0.4641 0.6576 1.1225 0.0012  0.0084  -0.0075 29  PRO B C   
1147 O O   . PRO B 29  ? 0.5126 0.7007 1.1857 0.0045  0.0061  -0.0093 29  PRO B O   
1148 C CB  . PRO B 29  ? 0.3761 0.5696 1.0175 -0.0187 0.0093  0.0001  29  PRO B CB  
1149 C CG  . PRO B 29  ? 0.3857 0.5765 1.0347 -0.0254 0.0090  0.0063  29  PRO B CG  
1150 C CD  . PRO B 29  ? 0.3987 0.5925 1.0563 -0.0217 0.0082  0.0168  29  PRO B CD  
1151 N N   . GLU B 30  ? 0.4738 0.6689 1.1243 0.0057  0.0088  -0.0153 30  GLU B N   
1152 C CA  . GLU B 30  ? 0.4730 0.6637 1.1279 0.0152  0.0075  -0.0276 30  GLU B CA  
1153 C C   . GLU B 30  ? 0.3579 0.5381 1.0130 0.0097  0.0065  -0.0385 30  GLU B C   
1154 O O   . GLU B 30  ? 0.4232 0.6033 1.0689 0.0015  0.0074  -0.0385 30  GLU B O   
1155 C CB  . GLU B 30  ? 0.5194 0.7207 1.1642 0.0240  0.0085  -0.0282 30  GLU B CB  
1156 N N   . PRO B 31  ? 0.3788 0.5504 1.0452 0.0145  0.0038  -0.0481 31  PRO B N   
1157 C CA  . PRO B 31  ? 0.5196 0.6819 1.1898 0.0102  0.0021  -0.0586 31  PRO B CA  
1158 C C   . PRO B 31  ? 0.5400 0.7008 1.2002 0.0155  0.0020  -0.0700 31  PRO B C   
1159 O O   . PRO B 31  ? 0.5871 0.7433 1.2511 0.0249  -0.0008 -0.0790 31  PRO B O   
1160 C CB  . PRO B 31  ? 0.3838 0.5378 1.0737 0.0146  -0.0031 -0.0622 31  PRO B CB  
1161 N N   . GLU B 32  ? 0.5390 0.7032 1.1862 0.0099  0.0039  -0.0698 32  GLU B N   
1162 C CA  . GLU B 32  ? 0.5750 0.7378 1.2130 0.0130  0.0030  -0.0794 32  GLU B CA  
1163 C C   . GLU B 32  ? 0.5175 0.6734 1.1596 0.0216  0.0004  -0.0916 32  GLU B C   
1164 O O   . GLU B 32  ? 0.5374 0.6847 1.1876 0.0192  -0.0016 -0.0998 32  GLU B O   
1165 C CB  . GLU B 32  ? 0.5533 0.7137 1.1857 0.0041  0.0030  -0.0836 32  GLU B CB  
1166 N N   . GLU B 35  ? 0.6850 1.1808 0.9592 -0.0164 -0.3773 -0.1544 35  GLU B N   
1167 C CA  . GLU B 35  ? 0.6642 1.1512 0.9803 -0.0168 -0.3693 -0.1612 35  GLU B CA  
1168 C C   . GLU B 35  ? 0.6324 1.0730 0.9596 -0.0241 -0.3449 -0.1756 35  GLU B C   
1169 O O   . GLU B 35  ? 0.7245 1.1387 1.0672 -0.0202 -0.3333 -0.1647 35  GLU B O   
1170 C CB  . GLU B 35  ? 0.6531 1.1469 0.9838 -0.0034 -0.3743 -0.1314 35  GLU B CB  
1171 N N   . LYS B 36  ? 0.7575 1.1901 1.0785 -0.0342 -0.3372 -0.1998 36  LYS B N   
1172 C CA  . LYS B 36  ? 0.7016 1.0947 1.0337 -0.0412 -0.3143 -0.2121 36  LYS B CA  
1173 C C   . LYS B 36  ? 0.6212 0.9833 0.9306 -0.0379 -0.3044 -0.1908 36  LYS B C   
1174 O O   . LYS B 36  ? 0.7334 1.1047 1.0104 -0.0334 -0.3139 -0.1757 36  LYS B O   
1175 C CB  . LYS B 36  ? 0.7205 1.1001 1.0951 -0.0425 -0.3030 -0.2216 36  LYS B CB  
1176 N N   . GLY B 37  ? 0.5937 0.9215 0.9200 -0.0397 -0.2857 -0.1885 37  GLY B N   
1177 C CA  . GLY B 37  ? 0.6190 0.9198 0.9273 -0.0365 -0.2767 -0.1683 37  GLY B CA  
1178 C C   . GLY B 37  ? 0.6180 0.9163 0.9299 -0.0268 -0.2805 -0.1467 37  GLY B C   
1179 O O   . GLY B 37  ? 0.5918 0.9131 0.9193 -0.0207 -0.2927 -0.1434 37  GLY B O   
1180 N N   . TYR B 38  ? 0.5319 0.8043 0.8330 -0.0250 -0.2703 -0.1324 38  TYR B N   
1181 C CA  . TYR B 38  ? 0.5888 0.8382 0.8685 -0.0308 -0.2581 -0.1314 38  TYR B CA  
1182 C C   . TYR B 38  ? 0.5905 0.8280 0.8501 -0.0238 -0.2585 -0.1104 38  TYR B C   
1183 O O   . TYR B 38  ? 0.4933 0.7152 0.7684 -0.0217 -0.2510 -0.1018 38  TYR B O   
1184 C CB  . TYR B 38  ? 0.6259 0.8514 0.9275 -0.0387 -0.2386 -0.1390 38  TYR B CB  
1185 N N   . ARG B 39  ? 0.4607 0.7045 0.6880 -0.0204 -0.2660 -0.1028 39  ARG B N   
1186 C CA  . ARG B 39  ? 0.4558 0.6904 0.6696 -0.0111 -0.2679 -0.0824 39  ARG B CA  
1187 C C   . ARG B 39  ? 0.5758 0.7923 0.7578 -0.0130 -0.2616 -0.0759 39  ARG B C   
1188 O O   . ARG B 39  ? 0.5399 0.7604 0.7008 -0.0185 -0.2617 -0.0845 39  ARG B O   
1189 C CB  . ARG B 39  ? 0.4792 0.7437 0.6887 0.0022  -0.2863 -0.0689 39  ARG B CB  
1190 C CG  . ARG B 39  ? 0.5000 0.7861 0.7421 0.0050  -0.2941 -0.0732 39  ARG B CG  
1191 C CD  . ARG B 39  ? 0.4867 0.7791 0.7484 0.0194  -0.3008 -0.0530 39  ARG B CD  
1192 N N   . MET B 40  ? 0.4989 0.6957 0.6798 -0.0087 -0.2567 -0.0615 40  MET B N   
1193 C CA  . MET B 40  ? 0.4527 0.6304 0.6060 -0.0104 -0.2505 -0.0543 40  MET B CA  
1194 C C   . MET B 40  ? 0.4349 0.6178 0.5619 0.0029  -0.2617 -0.0357 40  MET B C   
1195 O O   . MET B 40  ? 0.4475 0.6443 0.5841 0.0154  -0.2723 -0.0222 40  MET B O   
1196 C CB  . MET B 40  ? 0.3896 0.5419 0.5575 -0.0168 -0.2362 -0.0505 40  MET B CB  
1197 C CG  . MET B 40  ? 0.3720 0.5212 0.5663 -0.0269 -0.2235 -0.0627 40  MET B CG  
1198 S SD  . MET B 40  ? 0.8439 0.9835 1.0272 -0.0392 -0.2089 -0.0717 40  MET B SD  
1199 C CE  . MET B 40  ? 0.3425 0.4792 0.5602 -0.0470 -0.1937 -0.0774 40  MET B CE  
1200 N N   . GLN B 43  ? 0.5324 0.6932 0.5917 0.0346  -0.2706 0.0248  43  GLN B N   
1201 C CA  . GLN B 43  ? 0.6291 0.7663 0.6925 0.0429  -0.2659 0.0497  43  GLN B CA  
1202 C C   . GLN B 43  ? 0.5685 0.6761 0.6063 0.0336  -0.2478 0.0495  43  GLN B C   
1203 O O   . GLN B 43  ? 0.5061 0.5893 0.5559 0.0301  -0.2290 0.0568  43  GLN B O   
1204 C CB  . GLN B 43  ? 0.5145 0.6678 0.5649 0.0632  -0.2735 0.0775  43  GLN B CB  
1205 C CG  . GLN B 43  ? 0.5192 0.6728 0.6087 0.0761  -0.2692 0.0994  43  GLN B CG  
1206 C CD  . GLN B 43  ? 0.5680 0.6845 0.6779 0.0717  -0.2423 0.1071  43  GLN B CD  
1207 O OE1 . GLN B 43  ? 0.5481 0.6417 0.6342 0.0681  -0.2279 0.1118  43  GLN B OE1 
1208 N NE2 . GLN B 43  ? 0.5830 0.6956 0.7396 0.0722  -0.2346 0.1082  43  GLN B NE2 
1209 N N   . GLN B 44  ? 0.5071 0.6188 0.5118 0.0288  -0.2530 0.0394  44  GLN B N   
1210 C CA  . GLN B 44  ? 0.5265 0.6128 0.5070 0.0206  -0.2370 0.0399  44  GLN B CA  
1211 C C   . GLN B 44  ? 0.4920 0.5658 0.4936 0.0033  -0.2259 0.0227  44  GLN B C   
1212 O O   . GLN B 44  ? 0.4583 0.5120 0.4514 -0.0051 -0.2101 0.0241  44  GLN B O   
1213 C CB  . GLN B 44  ? 0.5642 0.6604 0.5064 0.0210  -0.2431 0.0339  44  GLN B CB  
1214 C CG  . GLN B 44  ? 0.7343 0.8589 0.6594 0.0368  -0.2526 0.0459  44  GLN B CG  
1215 C CD  . GLN B 44  ? 0.7030 0.8469 0.5967 0.0333  -0.2531 0.0339  44  GLN B CD  
1216 O OE1 . GLN B 44  ? 0.7165 0.8442 0.5984 0.0216  -0.2446 0.0201  44  GLN B OE1 
1217 N NE2 . GLN B 44  ? 0.6664 0.8472 0.5487 0.0408  -0.2635 0.0408  44  GLN B NE2 
1218 N N   . THR B 45  ? 0.4389 0.5286 0.4687 -0.0013 -0.2348 0.0074  45  THR B N   
1219 C CA  . THR B 45  ? 0.4276 0.5115 0.4835 -0.0157 -0.2248 -0.0058 45  THR B CA  
1220 C C   . THR B 45  ? 0.4519 0.5255 0.5320 -0.0164 -0.2122 0.0024  45  THR B C   
1221 O O   . THR B 45  ? 0.3837 0.4484 0.4735 -0.0283 -0.1974 -0.0019 45  THR B O   
1222 C CB  . THR B 45  ? 0.4057 0.5089 0.4834 -0.0190 -0.2260 -0.0234 45  THR B CB  
1223 O OG1 . THR B 45  ? 0.4291 0.5435 0.4870 -0.0198 -0.2284 -0.0337 45  THR B OG1 
1224 C CG2 . THR B 45  ? 0.3793 0.4769 0.4825 -0.0319 -0.2112 -0.0326 45  THR B CG2 
1225 N N   . VAL B 46  ? 0.4386 0.5167 0.5307 -0.0038 -0.2174 0.0141  46  VAL B N   
1226 C CA  . VAL B 46  ? 0.5116 0.5790 0.6308 -0.0039 -0.2029 0.0209  46  VAL B CA  
1227 C C   . VAL B 46  ? 0.4492 0.4949 0.5505 -0.0084 -0.1843 0.0285  46  VAL B C   
1228 O O   . VAL B 46  ? 0.4289 0.4670 0.5450 -0.0201 -0.1679 0.0216  46  VAL B O   
1229 C CB  . VAL B 46  ? 0.5233 0.5985 0.6613 0.0127  -0.2100 0.0365  46  VAL B CB  
1230 C CG1 . VAL B 46  ? 0.5052 0.5646 0.6737 0.0125  -0.1897 0.0436  46  VAL B CG1 
1231 C CG2 . VAL B 46  ? 0.4089 0.5087 0.5697 0.0157  -0.2281 0.0271  46  VAL B CG2 
1232 N N   . ASP B 47  ? 0.4438 0.4833 0.5131 0.0006  -0.1870 0.0417  47  ASP B N   
1233 C CA  . ASP B 47  ? 0.5494 0.5685 0.5983 -0.0027 -0.1706 0.0493  47  ASP B CA  
1234 C C   . ASP B 47  ? 0.4533 0.4683 0.4907 -0.0196 -0.1625 0.0356  47  ASP B C   
1235 O O   . ASP B 47  ? 0.4397 0.4447 0.4823 -0.0288 -0.1452 0.0343  47  ASP B O   
1236 C CB  . ASP B 47  ? 0.5544 0.5713 0.5700 0.0114  -0.1772 0.0665  47  ASP B CB  
1237 C CG  . ASP B 47  ? 0.6492 0.6707 0.6796 0.0298  -0.1801 0.0878  47  ASP B CG  
1238 O OD1 . ASP B 47  ? 0.5900 0.6068 0.6583 0.0304  -0.1700 0.0901  47  ASP B OD1 
1239 O OD2 . ASP B 47  ? 0.5725 0.6049 0.5790 0.0438  -0.1916 0.1027  47  ASP B OD2 
1240 N N   . ARG B 48  ? 0.4009 0.4263 0.4265 -0.0240 -0.1737 0.0256  48  ARG B N   
1241 C CA  . ARG B 48  ? 0.3843 0.4078 0.4035 -0.0381 -0.1653 0.0172  48  ARG B CA  
1242 C C   . ARG B 48  ? 0.4050 0.4357 0.4534 -0.0501 -0.1551 0.0089  48  ARG B C   
1243 O O   . ARG B 48  ? 0.4501 0.4799 0.4963 -0.0610 -0.1419 0.0081  48  ARG B O   
1244 C CB  . ARG B 48  ? 0.5015 0.5347 0.5123 -0.0401 -0.1766 0.0074  48  ARG B CB  
1245 C CG  . ARG B 48  ? 0.4247 0.4556 0.4338 -0.0530 -0.1655 0.0036  48  ARG B CG  
1246 C CD  . ARG B 48  ? 0.4699 0.5050 0.4714 -0.0546 -0.1718 -0.0051 48  ARG B CD  
1247 N NE  . ARG B 48  ? 0.6435 0.6663 0.6114 -0.0505 -0.1697 0.0013  48  ARG B NE  
1248 C CZ  . ARG B 48  ? 0.5141 0.5309 0.4728 -0.0568 -0.1617 0.0001  48  ARG B CZ  
1249 N NH1 . ARG B 48  ? 0.4745 0.4976 0.4571 -0.0668 -0.1548 -0.0052 48  ARG B NH1 
1250 N NH2 . ARG B 48  ? 0.6432 0.6486 0.5713 -0.0525 -0.1595 0.0056  48  ARG B NH2 
1251 N N   . LEU B 49  ? 0.3450 0.3863 0.4210 -0.0481 -0.1614 0.0030  49  LEU B N   
1252 C CA  . LEU B 49  ? 0.3375 0.3883 0.4419 -0.0589 -0.1516 -0.0055 49  LEU B CA  
1253 C C   . LEU B 49  ? 0.3863 0.4298 0.4995 -0.0624 -0.1348 -0.0035 49  LEU B C   
1254 O O   . LEU B 49  ? 0.4482 0.5012 0.5716 -0.0756 -0.1218 -0.0111 49  LEU B O   
1255 C CB  . LEU B 49  ? 0.3714 0.4346 0.5045 -0.0552 -0.1626 -0.0129 49  LEU B CB  
1256 C CG  . LEU B 49  ? 0.3040 0.3809 0.4679 -0.0663 -0.1546 -0.0233 49  LEU B CG  
1257 C CD1 . LEU B 49  ? 0.2887 0.3739 0.4448 -0.0773 -0.1469 -0.0256 49  LEU B CD1 
1258 C CD2 . LEU B 49  ? 0.3044 0.3921 0.4966 -0.0608 -0.1673 -0.0302 49  LEU B CD2 
1259 N N   . HIS B 50  ? 0.3331 0.3630 0.4455 -0.0510 -0.1336 0.0062  50  HIS B N   
1260 C CA  . HIS B 50  ? 0.4282 0.4484 0.5523 -0.0549 -0.1141 0.0067  50  HIS B CA  
1261 C C   . HIS B 50  ? 0.3843 0.4013 0.4853 -0.0654 -0.1030 0.0057  50  HIS B C   
1262 O O   . HIS B 50  ? 0.3174 0.3429 0.4297 -0.0791 -0.0879 -0.0047 50  HIS B O   
1263 C CB  . HIS B 50  ? 0.3765 0.3806 0.5051 -0.0389 -0.1124 0.0222  50  HIS B CB  
1264 C CG  . HIS B 50  ? 0.5035 0.5112 0.6695 -0.0310 -0.1136 0.0234  50  HIS B CG  
1265 N ND1 . HIS B 50  ? 0.6221 0.6340 0.8248 -0.0410 -0.0988 0.0097  50  HIS B ND1 
1266 C CD2 . HIS B 50  ? 0.5401 0.5512 0.7141 -0.0144 -0.1280 0.0364  50  HIS B CD2 
1267 C CE1 . HIS B 50  ? 0.5787 0.5925 0.8128 -0.0304 -0.1028 0.0148  50  HIS B CE1 
1268 N NE2 . HIS B 50  ? 0.5229 0.5376 0.7405 -0.0138 -0.1212 0.0322  50  HIS B NE2 
1269 N N   . PHE B 51  ? 0.3538 0.3617 0.4228 -0.0590 -0.1108 0.0159  51  PHE B N   
1270 C CA  . PHE B 51  ? 0.3669 0.3704 0.4127 -0.0665 -0.1021 0.0179  51  PHE B CA  
1271 C C   . PHE B 51  ? 0.4593 0.4837 0.5109 -0.0830 -0.0970 0.0075  51  PHE B C   
1272 O O   . PHE B 51  ? 0.3028 0.3345 0.3551 -0.0944 -0.0830 0.0033  51  PHE B O   
1273 C CB  . PHE B 51  ? 0.3854 0.3794 0.3990 -0.0574 -0.1137 0.0279  51  PHE B CB  
1274 C CG  . PHE B 51  ? 0.4164 0.4035 0.4067 -0.0634 -0.1048 0.0318  51  PHE B CG  
1275 C CD1 . PHE B 51  ? 0.4514 0.4325 0.4447 -0.0695 -0.0880 0.0322  51  PHE B CD1 
1276 C CD2 . PHE B 51  ? 0.3994 0.3870 0.3687 -0.0637 -0.1121 0.0336  51  PHE B CD2 
1277 C CE1 . PHE B 51  ? 0.4005 0.3772 0.3745 -0.0751 -0.0802 0.0359  51  PHE B CE1 
1278 C CE2 . PHE B 51  ? 0.4440 0.4253 0.3951 -0.0688 -0.1033 0.0383  51  PHE B CE2 
1279 C CZ  . PHE B 51  ? 0.5462 0.5227 0.4988 -0.0743 -0.0882 0.0402  51  PHE B CZ  
1280 N N   . ILE B 52  ? 0.3103 0.3478 0.3691 -0.0841 -0.1077 0.0038  52  ILE B N   
1281 C CA  . ILE B 52  ? 0.3718 0.4314 0.4376 -0.0972 -0.1030 -0.0007 52  ILE B CA  
1282 C C   . ILE B 52  ? 0.3047 0.3829 0.3933 -0.1084 -0.0907 -0.0113 52  ILE B C   
1283 O O   . ILE B 52  ? 0.2693 0.3665 0.3559 -0.1208 -0.0796 -0.0136 52  ILE B O   
1284 C CB  . ILE B 52  ? 0.2924 0.3601 0.3675 -0.0948 -0.1151 -0.0020 52  ILE B CB  
1285 C CG1 . ILE B 52  ? 0.3166 0.3721 0.3699 -0.0885 -0.1231 0.0043  52  ILE B CG1 
1286 C CG2 . ILE B 52  ? 0.2645 0.3576 0.3556 -0.1065 -0.1076 -0.0041 52  ILE B CG2 
1287 C CD1 . ILE B 52  ? 0.4691 0.5287 0.5342 -0.0843 -0.1355 -0.0012 52  ILE B CD1 
1288 N N   . LYS B 53  ? 0.3984 0.4740 0.5095 -0.1043 -0.0922 -0.0182 53  LYS B N   
1289 C CA  . LYS B 53  ? 0.4388 0.5310 0.5744 -0.1152 -0.0789 -0.0315 53  LYS B CA  
1290 C C   . LYS B 53  ? 0.2937 0.3865 0.4245 -0.1240 -0.0622 -0.0366 53  LYS B C   
1291 O O   . LYS B 53  ? 0.2943 0.4138 0.4297 -0.1392 -0.0506 -0.0469 53  LYS B O   
1292 C CB  . LYS B 53  ? 0.3746 0.4577 0.5380 -0.1071 -0.0817 -0.0365 53  LYS B CB  
1293 C CG  . LYS B 53  ? 0.3394 0.4371 0.5334 -0.1183 -0.0657 -0.0531 53  LYS B CG  
1294 C CD  . LYS B 53  ? 0.5540 0.6823 0.7525 -0.1307 -0.0632 -0.0605 53  LYS B CD  
1295 C CE  . LYS B 53  ? 0.5194 0.6570 0.7320 -0.1360 -0.0461 -0.0719 53  LYS B CE  
1296 N NZ  . LYS B 53  ? 0.4893 0.6483 0.6852 -0.1395 -0.0395 -0.0694 53  LYS B NZ  
1297 N N   . ARG B 54  ? 0.2958 0.3624 0.4173 -0.1147 -0.0604 -0.0294 54  ARG B N   
1298 C CA  . ARG B 54  ? 0.3743 0.4397 0.4993 -0.1230 -0.0423 -0.0368 54  ARG B CA  
1299 C C   . ARG B 54  ? 0.2918 0.3722 0.3929 -0.1331 -0.0391 -0.0348 54  ARG B C   
1300 O O   . ARG B 54  ? 0.4790 0.5784 0.5872 -0.1473 -0.0244 -0.0477 54  ARG B O   
1301 C CB  . ARG B 54  ? 0.3217 0.3547 0.4491 -0.1094 -0.0383 -0.0274 54  ARG B CB  
1302 C CG  . ARG B 54  ? 0.3833 0.4078 0.5435 -0.1012 -0.0371 -0.0294 54  ARG B CG  
1303 C CD  . ARG B 54  ? 0.5599 0.5562 0.7272 -0.0849 -0.0334 -0.0145 54  ARG B CD  
1304 N NE  . ARG B 54  ? 0.7018 0.6940 0.8929 -0.0723 -0.0416 -0.0083 54  ARG B NE  
1305 C CZ  . ARG B 54  ? 0.6619 0.6366 0.8764 -0.0580 -0.0355 0.0045  54  ARG B CZ  
1306 N NH1 . ARG B 54  ? 0.5760 0.5326 0.7971 -0.0551 -0.0181 0.0113  54  ARG B NH1 
1307 N NH2 . ARG B 54  ? 0.5664 0.5432 0.8025 -0.0468 -0.0452 0.0112  54  ARG B NH2 
1308 N N   . MET B 55  ? 0.2633 0.3382 0.3393 -0.1266 -0.0519 -0.0200 55  MET B N   
1309 C CA  . MET B 55  ? 0.2540 0.3452 0.3115 -0.1353 -0.0489 -0.0152 55  MET B CA  
1310 C C   . MET B 55  ? 0.2388 0.3678 0.3068 -0.1463 -0.0427 -0.0233 55  MET B C   
1311 O O   . MET B 55  ? 0.2373 0.3828 0.2978 -0.1500 -0.0314 -0.0258 55  MET B O   
1312 C CB  . MET B 55  ? 0.2545 0.3330 0.2897 -0.1260 -0.0617 0.0010  55  MET B CB  
1313 C CG  . MET B 55  ? 0.2718 0.3183 0.2862 -0.1149 -0.0629 0.0105  55  MET B CG  
1314 S SD  . MET B 55  ? 0.5797 0.6185 0.5682 -0.1101 -0.0710 0.0249  55  MET B SD  
1315 C CE  . MET B 55  ? 0.2708 0.3092 0.2667 -0.1022 -0.0874 0.0244  55  MET B CE  
1316 N N   . GLN B 56  ? 0.2660 0.4016 0.3477 -0.1417 -0.0477 -0.0255 56  GLN B N   
1317 C CA  . GLN B 56  ? 0.3323 0.4939 0.4184 -0.1422 -0.0387 -0.0294 56  GLN B CA  
1318 C C   . GLN B 56  ? 0.2672 0.4400 0.3629 -0.1490 -0.0245 -0.0460 56  GLN B C   
1319 O O   . GLN B 56  ? 0.3720 0.5690 0.4585 -0.1527 -0.0155 -0.0489 56  GLN B O   
1320 C CB  . GLN B 56  ? 0.2550 0.4192 0.3558 -0.1369 -0.0455 -0.0284 56  GLN B CB  
1321 C CG  . GLN B 56  ? 0.2970 0.4633 0.3899 -0.1313 -0.0523 -0.0135 56  GLN B CG  
1322 C CD  . GLN B 56  ? 0.3612 0.5256 0.4737 -0.1261 -0.0593 -0.0153 56  GLN B CD  
1323 O OE1 . GLN B 56  ? 0.2479 0.3951 0.3694 -0.1221 -0.0702 -0.0197 56  GLN B OE1 
1324 N NE2 . GLN B 56  ? 0.3599 0.5438 0.4792 -0.1264 -0.0535 -0.0114 56  GLN B NE2 
1325 N N   . GLU B 57  ? 0.2750 0.4317 0.3892 -0.1515 -0.0214 -0.0573 57  GLU B N   
1326 C CA  . GLU B 57  ? 0.2850 0.4504 0.4111 -0.1579 -0.0046 -0.0752 57  GLU B CA  
1327 C C   . GLU B 57  ? 0.2899 0.4593 0.4018 -0.1628 0.0047  -0.0781 57  GLU B C   
1328 O O   . GLU B 57  ? 0.3121 0.4958 0.4266 -0.1685 0.0188  -0.0937 57  GLU B O   
1329 C CB  . GLU B 57  ? 0.3057 0.4506 0.4621 -0.1581 -0.0003 -0.0857 57  GLU B CB  
1330 C CG  . GLU B 57  ? 0.3949 0.5395 0.5669 -0.1534 -0.0094 -0.0841 57  GLU B CG  
1331 C CD  . GLU B 57  ? 0.4168 0.5398 0.6228 -0.1509 -0.0072 -0.0907 57  GLU B CD  
1332 O OE1 . GLU B 57  ? 0.4371 0.5385 0.6546 -0.1496 -0.0036 -0.0895 57  GLU B OE1 
1333 O OE2 . GLU B 57  ? 0.4420 0.5678 0.6665 -0.1481 -0.0081 -0.0951 57  GLU B OE2 
1334 N N   . LEU B 58  ? 0.2631 0.4209 0.3592 -0.1610 -0.0031 -0.0640 58  LEU B N   
1335 C CA  . LEU B 58  ? 0.2671 0.4279 0.3501 -0.1653 0.0050  -0.0648 58  LEU B CA  
1336 C C   . LEU B 58  ? 0.3627 0.5500 0.4215 -0.1648 0.0029  -0.0552 58  LEU B C   
1337 O O   . LEU B 58  ? 0.2624 0.4553 0.3085 -0.1678 0.0073  -0.0535 58  LEU B O   
1338 C CB  . LEU B 58  ? 0.2700 0.4015 0.3481 -0.1653 0.0002  -0.0543 58  LEU B CB  
1339 C CG  . LEU B 58  ? 0.3032 0.4050 0.4054 -0.1652 0.0075  -0.0616 58  LEU B CG  
1340 C CD1 . LEU B 58  ? 0.2965 0.3587 0.3789 -0.1480 0.0009  -0.0406 58  LEU B CD1 
1341 C CD2 . LEU B 58  ? 0.2933 0.3994 0.4176 -0.1713 0.0285  -0.0814 58  LEU B CD2 
1342 N N   . GLY B 59  ? 0.2473 0.4504 0.3018 -0.1612 -0.0032 -0.0477 59  GLY B N   
1343 C CA  . GLY B 59  ? 0.2441 0.4751 0.2794 -0.1617 -0.0028 -0.0375 59  GLY B CA  
1344 C C   . GLY B 59  ? 0.2349 0.4602 0.2581 -0.1560 -0.0124 -0.0147 59  GLY B C   
1345 O O   . GLY B 59  ? 0.2361 0.4839 0.2453 -0.1565 -0.0114 -0.0035 59  GLY B O   
1346 N N   . PHE B 60  ? 0.2754 0.4722 0.3035 -0.1512 -0.0217 -0.0075 60  PHE B N   
1347 C CA  . PHE B 60  ? 0.2562 0.4472 0.2767 -0.1458 -0.0302 0.0124  60  PHE B CA  
1348 C C   . PHE B 60  ? 0.2261 0.4285 0.2568 -0.1415 -0.0332 0.0177  60  PHE B C   
1349 O O   . PHE B 60  ? 0.2264 0.4223 0.2717 -0.1399 -0.0358 0.0078  60  PHE B O   
1350 C CB  . PHE B 60  ? 0.2340 0.3923 0.2533 -0.1429 -0.0406 0.0167  60  PHE B CB  
1351 C CG  . PHE B 60  ? 0.2414 0.3838 0.2498 -0.1475 -0.0386 0.0159  60  PHE B CG  
1352 C CD1 . PHE B 60  ? 0.3792 0.5121 0.3735 -0.1472 -0.0420 0.0304  60  PHE B CD1 
1353 C CD2 . PHE B 60  ? 0.2497 0.3831 0.2659 -0.1528 -0.0326 0.0011  60  PHE B CD2 
1354 C CE1 . PHE B 60  ? 0.2526 0.3632 0.2348 -0.1475 -0.0382 0.0306  60  PHE B CE1 
1355 C CE2 . PHE B 60  ? 0.2602 0.3726 0.2678 -0.1543 -0.0279 0.0019  60  PHE B CE2 
1356 C CZ  . PHE B 60  ? 0.2628 0.3614 0.2506 -0.1488 -0.0306 0.0170  60  PHE B CZ  
1357 N N   . THR B 61  ? 0.2361 0.4544 0.2624 -0.1394 -0.0328 0.0344  61  THR B N   
1358 C CA  . THR B 61  ? 0.2401 0.4675 0.2798 -0.1354 -0.0348 0.0423  61  THR B CA  
1359 C C   . THR B 61  ? 0.3571 0.5582 0.4091 -0.1301 -0.0440 0.0453  61  THR B C   
1360 O O   . THR B 61  ? 0.2565 0.4364 0.3008 -0.1297 -0.0493 0.0463  61  THR B O   
1361 C CB  . THR B 61  ? 0.2308 0.4820 0.2666 -0.1338 -0.0320 0.0619  61  THR B CB  
1362 O OG1 . THR B 61  ? 0.2363 0.4715 0.2725 -0.1299 -0.0358 0.0756  61  THR B OG1 
1363 C CG2 . THR B 61  ? 0.2378 0.5183 0.2554 -0.1390 -0.0263 0.0606  61  THR B CG2 
1364 N N   . LEU B 62  ? 0.2446 0.4477 0.3150 -0.1267 -0.0461 0.0457  62  LEU B N   
1365 C CA  . LEU B 62  ? 0.2299 0.4114 0.3140 -0.1221 -0.0553 0.0458  62  LEU B CA  
1366 C C   . LEU B 62  ? 0.2988 0.4730 0.3809 -0.1210 -0.0562 0.0607  62  LEU B C   
1367 O O   . LEU B 62  ? 0.3063 0.4583 0.3869 -0.1197 -0.0648 0.0577  62  LEU B O   
1368 C CB  . LEU B 62  ? 0.2262 0.4158 0.3345 -0.1193 -0.0547 0.0448  62  LEU B CB  
1369 C CG  . LEU B 62  ? 0.3766 0.5584 0.4969 -0.1177 -0.0601 0.0272  62  LEU B CG  
1370 C CD1 . LEU B 62  ? 0.3740 0.5653 0.5203 -0.1155 -0.0581 0.0283  62  LEU B CD1 
1371 C CD2 . LEU B 62  ? 0.2858 0.4408 0.4020 -0.1142 -0.0730 0.0168  62  LEU B CD2 
1372 N N   . ASN B 63  ? 0.2560 0.4499 0.3377 -0.1210 -0.0477 0.0766  63  ASN B N   
1373 C CA  . ASN B 63  ? 0.2554 0.4440 0.3403 -0.1187 -0.0459 0.0917  63  ASN B CA  
1374 C C   . ASN B 63  ? 0.2797 0.4521 0.3445 -0.1218 -0.0494 0.0900  63  ASN B C   
1375 O O   . ASN B 63  ? 0.3715 0.5237 0.4401 -0.1217 -0.0534 0.0916  63  ASN B O   
1376 C CB  . ASN B 63  ? 0.4052 0.6195 0.4917 -0.1152 -0.0376 0.1090  63  ASN B CB  
1377 C CG  . ASN B 63  ? 0.4275 0.6351 0.5295 -0.1090 -0.0336 0.1241  63  ASN B CG  
1378 O OD1 . ASN B 63  ? 0.3771 0.5885 0.4695 -0.1066 -0.0320 0.1326  63  ASN B OD1 
1379 N ND2 . ASN B 63  ? 0.4157 0.6124 0.5454 -0.1059 -0.0312 0.1251  63  ASN B ND2 
1380 N N   . GLU B 64  ? 0.2495 0.4306 0.2940 -0.1255 -0.0470 0.0852  64  GLU B N   
1381 C CA  . GLU B 64  ? 0.2489 0.4141 0.2751 -0.1292 -0.0490 0.0819  64  GLU B CA  
1382 C C   . GLU B 64  ? 0.2557 0.3913 0.2791 -0.1297 -0.0600 0.0708  64  GLU B C   
1383 O O   . GLU B 64  ? 0.2643 0.3764 0.2752 -0.1282 -0.0635 0.0726  64  GLU B O   
1384 C CB  . GLU B 64  ? 0.2729 0.4528 0.2846 -0.1336 -0.0432 0.0732  64  GLU B CB  
1385 C CG  . GLU B 64  ? 0.4491 0.6598 0.4578 -0.1325 -0.0373 0.0830  64  GLU B CG  
1386 C CD  . GLU B 64  ? 0.3723 0.6009 0.3670 -0.1384 -0.0318 0.0715  64  GLU B CD  
1387 O OE1 . GLU B 64  ? 0.2881 0.5114 0.2831 -0.1428 -0.0291 0.0537  64  GLU B OE1 
1388 O OE2 . GLU B 64  ? 0.3418 0.5912 0.3294 -0.1379 -0.0310 0.0795  64  GLU B OE2 
1389 N N   . ILE B 65  ? 0.2389 0.3718 0.2699 -0.1274 -0.0648 0.0582  65  ILE B N   
1390 C CA  . ILE B 65  ? 0.2495 0.3562 0.2756 -0.1239 -0.0777 0.0476  65  ILE B CA  
1391 C C   . ILE B 65  ? 0.2993 0.3879 0.3282 -0.1164 -0.0837 0.0496  65  ILE B C   
1392 O O   . ILE B 65  ? 0.4164 0.4789 0.4274 -0.1086 -0.0899 0.0447  65  ILE B O   
1393 C CB  . ILE B 65  ? 0.3163 0.4272 0.3552 -0.1214 -0.0797 0.0348  65  ILE B CB  
1394 C CG1 . ILE B 65  ? 0.2981 0.4180 0.3326 -0.1269 -0.0710 0.0272  65  ILE B CG1 
1395 C CG2 . ILE B 65  ? 0.2609 0.3485 0.2989 -0.1136 -0.0939 0.0270  65  ILE B CG2 
1396 C CD1 . ILE B 65  ? 0.2483 0.3752 0.2998 -0.1264 -0.0698 0.0141  65  ILE B CD1 
1397 N N   . ASP B 66  ? 0.3511 0.4564 0.4042 -0.1192 -0.0802 0.0568  66  ASP B N   
1398 C CA  . ASP B 66  ? 0.4141 0.5064 0.4795 -0.1147 -0.0816 0.0567  66  ASP B CA  
1399 C C   . ASP B 66  ? 0.3852 0.4592 0.4325 -0.1125 -0.0772 0.0622  66  ASP B C   
1400 O O   . ASP B 66  ? 0.3287 0.3799 0.3652 -0.1067 -0.0826 0.0524  66  ASP B O   
1401 C CB  . ASP B 66  ? 0.2756 0.3923 0.3770 -0.1190 -0.0730 0.0682  66  ASP B CB  
1402 C CG  . ASP B 66  ? 0.4038 0.5087 0.5301 -0.1156 -0.0730 0.0624  66  ASP B CG  
1403 O OD1 . ASP B 66  ? 0.5989 0.6803 0.7124 -0.1116 -0.0763 0.0531  66  ASP B OD1 
1404 O OD2 . ASP B 66  ? 0.6197 0.7390 0.7782 -0.1157 -0.0670 0.0658  66  ASP B OD2 
1405 N N   . LYS B 67  ? 0.3292 0.4171 0.3744 -0.1175 -0.0670 0.0777  67  LYS B N   
1406 C CA  . LYS B 67  ? 0.3562 0.4285 0.3871 -0.1160 -0.0609 0.0845  67  LYS B CA  
1407 C C   . LYS B 67  ? 0.3491 0.3940 0.3450 -0.1106 -0.0675 0.0736  67  LYS B C   
1408 O O   . LYS B 67  ? 0.3790 0.4009 0.3626 -0.1051 -0.0700 0.0673  67  LYS B O   
1409 C CB  . LYS B 67  ? 0.4057 0.5034 0.4409 -0.1225 -0.0502 0.1033  67  LYS B CB  
1410 N N   . LEU B 68  ? 0.2903 0.3398 0.2732 -0.1124 -0.0692 0.0709  68  LEU B N   
1411 C CA  . LEU B 68  ? 0.3580 0.3842 0.3134 -0.1068 -0.0723 0.0648  68  LEU B CA  
1412 C C   . LEU B 68  ? 0.5305 0.5361 0.4756 -0.0972 -0.0834 0.0550  68  LEU B C   
1413 O O   . LEU B 68  ? 0.3986 0.3839 0.3209 -0.0911 -0.0841 0.0549  68  LEU B O   
1414 C CB  . LEU B 68  ? 0.3031 0.3397 0.2594 -0.1106 -0.0713 0.0598  68  LEU B CB  
1415 C CG  . LEU B 68  ? 0.3888 0.4041 0.3279 -0.1046 -0.0718 0.0546  68  LEU B CG  
1416 C CD1 . LEU B 68  ? 0.3114 0.3422 0.2600 -0.1131 -0.0632 0.0495  68  LEU B CD1 
1417 C CD2 . LEU B 68  ? 0.3314 0.3337 0.2696 -0.0946 -0.0837 0.0476  68  LEU B CD2 
1418 N N   . LEU B 69  ? 0.3212 0.3355 0.2832 -0.0960 -0.0919 0.0467  69  LEU B N   
1419 C CA  . LEU B 69  ? 0.3520 0.3546 0.3063 -0.0875 -0.1041 0.0361  69  LEU B CA  
1420 C C   . LEU B 69  ? 0.5085 0.5026 0.4589 -0.0861 -0.1037 0.0320  69  LEU B C   
1421 O O   . LEU B 69  ? 0.5272 0.5098 0.4559 -0.0791 -0.1108 0.0254  69  LEU B O   
1422 C CB  . LEU B 69  ? 0.4298 0.4465 0.4084 -0.0877 -0.1127 0.0272  69  LEU B CB  
1423 C CG  . LEU B 69  ? 0.4185 0.4383 0.3988 -0.0855 -0.1165 0.0254  69  LEU B CG  
1424 C CD1 . LEU B 69  ? 0.3207 0.3548 0.3282 -0.0861 -0.1241 0.0164  69  LEU B CD1 
1425 C CD2 . LEU B 69  ? 0.3519 0.3544 0.3075 -0.0746 -0.1229 0.0263  69  LEU B CD2 
1426 N N   . GLY B 70  ? 0.4418 0.4438 0.4147 -0.0929 -0.0940 0.0365  70  GLY B N   
1427 C CA  . GLY B 70  ? 0.3720 0.3646 0.3472 -0.0929 -0.0894 0.0313  70  GLY B CA  
1428 C C   . GLY B 70  ? 0.4525 0.4268 0.3951 -0.0896 -0.0852 0.0350  70  GLY B C   
1429 O O   . GLY B 70  ? 0.6150 0.5787 0.5404 -0.0856 -0.0889 0.0238  70  GLY B O   
1430 N N   . VAL B 71  ? 0.3950 0.3685 0.3293 -0.0920 -0.0770 0.0499  71  VAL B N   
1431 C CA  . VAL B 71  ? 0.4740 0.4300 0.3802 -0.0893 -0.0708 0.0557  71  VAL B CA  
1432 C C   . VAL B 71  ? 0.5396 0.4818 0.4128 -0.0801 -0.0801 0.0504  71  VAL B C   
1433 O O   . VAL B 71  ? 0.5445 0.4742 0.3958 -0.0753 -0.0804 0.0460  71  VAL B O   
1434 C CB  . VAL B 71  ? 0.5600 0.5232 0.4687 -0.0948 -0.0606 0.0710  71  VAL B CB  
1435 C CG1 . VAL B 71  ? 0.3722 0.3165 0.2545 -0.0920 -0.0535 0.0765  71  VAL B CG1 
1436 C CG2 . VAL B 71  ? 0.3877 0.3690 0.3281 -0.1021 -0.0510 0.0812  71  VAL B CG2 
1437 N N   . VAL B 72  ? 0.5939 0.5406 0.4656 -0.0772 -0.0866 0.0516  72  VAL B N   
1438 C CA  . VAL B 72  ? 0.5511 0.4863 0.3967 -0.0668 -0.0933 0.0521  72  VAL B CA  
1439 C C   . VAL B 72  ? 0.5729 0.5111 0.4082 -0.0603 -0.1058 0.0406  72  VAL B C   
1440 O O   . VAL B 72  ? 0.6384 0.5684 0.4455 -0.0528 -0.1078 0.0416  72  VAL B O   
1441 C CB  . VAL B 72  ? 0.3708 0.3111 0.2257 -0.0644 -0.0969 0.0546  72  VAL B CB  
1442 C CG1 . VAL B 72  ? 0.3973 0.3264 0.2303 -0.0516 -0.1018 0.0599  72  VAL B CG1 
1443 C CG2 . VAL B 72  ? 0.4072 0.3505 0.2736 -0.0729 -0.0841 0.0609  72  VAL B CG2 
1444 N N   . ASP B 73  ? 0.4676 0.4205 0.3264 -0.0638 -0.1135 0.0288  73  ASP B N   
1445 C CA  . ASP B 73  ? 0.5342 0.4954 0.3870 -0.0596 -0.1256 0.0136  73  ASP B CA  
1446 C C   . ASP B 73  ? 0.5974 0.5524 0.4354 -0.0615 -0.1195 0.0055  73  ASP B C   
1447 O O   . ASP B 73  ? 0.6327 0.5935 0.4485 -0.0559 -0.1280 -0.0041 73  ASP B O   
1448 C CB  . ASP B 73  ? 0.5678 0.5454 0.4554 -0.0649 -0.1319 0.0004  73  ASP B CB  
1449 C CG  . ASP B 73  ? 0.7536 0.7402 0.6538 -0.0615 -0.1408 0.0039  73  ASP B CG  
1450 O OD1 . ASP B 73  ? 0.7595 0.7408 0.6413 -0.0534 -0.1441 0.0141  73  ASP B OD1 
1451 O OD2 . ASP B 73  ? 0.6342 0.6328 0.5663 -0.0669 -0.1425 -0.0028 73  ASP B OD2 
1452 N N   . ARG B 74  ? 0.6399 0.5862 0.4908 -0.0693 -0.1044 0.0094  74  ARG B N   
1453 C CA  . ARG B 74  ? 0.5970 0.5372 0.4385 -0.0716 -0.0972 -0.0011 74  ARG B CA  
1454 C C   . ARG B 74  ? 0.6101 0.5333 0.4175 -0.0677 -0.0885 0.0096  74  ARG B C   
1455 O O   . ARG B 74  ? 0.6325 0.5510 0.4296 -0.0695 -0.0820 -0.0002 74  ARG B O   
1456 C CB  . ARG B 74  ? 0.6208 0.5620 0.5025 -0.0818 -0.0840 -0.0048 74  ARG B CB  
1457 C CG  . ARG B 74  ? 0.7288 0.6865 0.6451 -0.0853 -0.0911 -0.0190 74  ARG B CG  
1458 C CD  . ARG B 74  ? 0.6577 0.6175 0.6206 -0.0941 -0.0761 -0.0216 74  ARG B CD  
1459 N NE  . ARG B 74  ? 0.7311 0.7057 0.7284 -0.0963 -0.0807 -0.0218 74  ARG B NE  
1460 C CZ  . ARG B 74  ? 0.7507 0.7313 0.7936 -0.1022 -0.0678 -0.0150 74  ARG B CZ  
1461 N NH1 . ARG B 74  ? 0.8198 0.7933 0.8828 -0.1062 -0.0495 -0.0068 74  ARG B NH1 
1462 N NH2 . ARG B 74  ? 0.8320 0.8269 0.9032 -0.1034 -0.0723 -0.0147 74  ARG B NH2 
1463 N N   . ASP B 75  ? 0.5379 0.4525 0.3281 -0.0621 -0.0880 0.0274  75  ASP B N   
1464 C CA  . ASP B 75  ? 0.6162 0.5131 0.3818 -0.0597 -0.0763 0.0392  75  ASP B CA  
1465 C C   . ASP B 75  ? 0.5764 0.4689 0.3044 -0.0478 -0.0819 0.0455  75  ASP B C   
1466 O O   . ASP B 75  ? 0.5549 0.4575 0.2779 -0.0403 -0.0946 0.0471  75  ASP B O   
1467 C CB  . ASP B 75  ? 0.7293 0.6191 0.5083 -0.0639 -0.0657 0.0557  75  ASP B CB  
1468 C CG  . ASP B 75  ? 0.6326 0.5244 0.4398 -0.0743 -0.0533 0.0577  75  ASP B CG  
1469 O OD1 . ASP B 75  ? 0.7280 0.6207 0.5464 -0.0778 -0.0498 0.0470  75  ASP B OD1 
1470 O OD2 . ASP B 75  ? 0.5428 0.4375 0.3632 -0.0790 -0.0461 0.0700  75  ASP B OD2 
1471 N N   . GLU B 76  ? 0.5687 0.4474 0.2723 -0.0456 -0.0713 0.0510  76  GLU B N   
1472 C CA  . GLU B 76  ? 0.7309 0.6052 0.3997 -0.0333 -0.0732 0.0624  76  GLU B CA  
1473 C C   . GLU B 76  ? 0.6073 0.4700 0.2814 -0.0286 -0.0679 0.0822  76  GLU B C   
1474 O O   . GLU B 76  ? 0.5740 0.4450 0.2473 -0.0171 -0.0732 0.0902  76  GLU B O   
1475 C CB  . GLU B 76  ? 0.7347 0.5982 0.3767 -0.0327 -0.0615 0.0619  76  GLU B CB  
1476 C CG  . GLU B 76  ? 0.7475 0.6112 0.3631 -0.0184 -0.0581 0.0770  76  GLU B CG  
1477 C CD  . GLU B 76  ? 0.9699 0.8285 0.5596 -0.0182 -0.0471 0.0733  76  GLU B CD  
1478 O OE1 . GLU B 76  ? 0.9504 0.7998 0.5451 -0.0132 -0.0321 0.0869  76  GLU B OE1 
1479 O OE2 . GLU B 76  ? 0.9536 0.8207 0.5226 -0.0237 -0.0529 0.0540  76  GLU B OE2 
1480 N N   . ALA B 77  ? 0.6733 0.5252 0.3674 -0.0361 -0.0544 0.0874  77  ALA B N   
1481 C CA  . ALA B 77  ? 0.6477 0.4975 0.3597 -0.0312 -0.0460 0.0982  77  ALA B CA  
1482 C C   . ALA B 77  ? 0.5944 0.4510 0.3269 -0.0386 -0.0540 0.0962  77  ALA B C   
1483 O O   . ALA B 77  ? 0.5024 0.3623 0.2555 -0.0499 -0.0482 0.0943  77  ALA B O   
1484 C CB  . ALA B 77  ? 0.5403 0.3829 0.2664 -0.0344 -0.0275 0.1019  77  ALA B CB  
1485 N N   . LYS B 78  ? 0.4779 0.6634 0.5069 -0.0026 -0.1046 0.0964  78  LYS B N   
1486 C CA  . LYS B 78  ? 0.4765 0.6138 0.5078 -0.0143 -0.1048 0.1075  78  LYS B CA  
1487 C C   . LYS B 78  ? 0.4014 0.5529 0.4447 -0.0373 -0.0876 0.1121  78  LYS B C   
1488 O O   . LYS B 78  ? 0.2853 0.4218 0.3308 -0.0406 -0.0891 0.1120  78  LYS B O   
1489 C CB  . LYS B 78  ? 0.3269 0.4236 0.3572 -0.0214 -0.1047 0.1226  78  LYS B CB  
1490 C CG  . LYS B 78  ? 0.3159 0.3960 0.3317 -0.0025 -0.1222 0.1184  78  LYS B CG  
1491 C CD  . LYS B 78  ? 0.3442 0.3871 0.3596 -0.0124 -0.1210 0.1309  78  LYS B CD  
1492 C CE  . LYS B 78  ? 0.5049 0.5294 0.5030 0.0032  -0.1312 0.1203  78  LYS B CE  
1493 N NZ  . LYS B 78  ? 0.3628 0.3686 0.3385 0.0212  -0.1460 0.1046  78  LYS B NZ  
1494 N N   . CYS B 79  ? 0.3286 0.5061 0.3755 -0.0545 -0.0720 0.1163  79  CYS B N   
1495 C CA  . CYS B 79  ? 0.3055 0.4927 0.3559 -0.0792 -0.0570 0.1202  79  CYS B CA  
1496 C C   . CYS B 79  ? 0.3019 0.5290 0.3573 -0.0755 -0.0600 0.1053  79  CYS B C   
1497 O O   . CYS B 79  ? 0.2999 0.5139 0.3586 -0.0863 -0.0563 0.1071  79  CYS B O   
1498 C CB  . CYS B 79  ? 0.2996 0.5073 0.3438 -0.0994 -0.0428 0.1259  79  CYS B CB  
1499 S SG  . CYS B 79  ? 0.3107 0.5282 0.3484 -0.1354 -0.0263 0.1299  79  CYS B SG  
1500 N N   . ARG B 80  ? 0.2517 0.5288 0.3060 -0.0567 -0.0680 0.0894  80  ARG B N   
1501 C CA  . ARG B 80  ? 0.3220 0.6449 0.3792 -0.0480 -0.0722 0.0729  80  ARG B CA  
1502 C C   . ARG B 80  ? 0.2531 0.5339 0.3068 -0.0311 -0.0857 0.0703  80  ARG B C   
1503 O O   . ARG B 80  ? 0.2495 0.5412 0.3079 -0.0377 -0.0830 0.0659  80  ARG B O   
1504 C CB  . ARG B 80  ? 0.2897 0.6769 0.3426 -0.0227 -0.0811 0.0543  80  ARG B CB  
1505 C CG  . ARG B 80  ? 0.2586 0.7031 0.3123 -0.0069 -0.0873 0.0343  80  ARG B CG  
1506 C CD  . ARG B 80  ? 0.2789 0.7514 0.3186 0.0313  -0.0969 0.0135  80  ARG B CD  
1507 N NE  . ARG B 80  ? 0.5729 0.9729 0.5941 0.0610  -0.1162 0.0125  80  ARG B NE  
1508 C CZ  . ARG B 80  ? 0.4946 0.8814 0.4972 0.0913  -0.1254 -0.0005 80  ARG B CZ  
1509 N NH1 . ARG B 80  ? 0.3331 0.7823 0.3360 0.1008  -0.1163 -0.0144 80  ARG B NH1 
1510 N NH2 . ARG B 80  ? 0.3910 0.7028 0.3728 0.1086  -0.1426 0.0015  80  ARG B NH2 
1511 N N   . ASP B 81  ? 0.2585 0.4909 0.3010 -0.0116 -0.1007 0.0732  81  ASP B N   
1512 C CA  . ASP B 81  ? 0.2689 0.4551 0.3009 0.0012  -0.1152 0.0725  81  ASP B CA  
1513 C C   . ASP B 81  ? 0.2566 0.4152 0.2995 -0.0234 -0.1037 0.0857  81  ASP B C   
1514 O O   . ASP B 81  ? 0.2571 0.4148 0.3001 -0.0223 -0.1060 0.0808  81  ASP B O   
1515 C CB  . ASP B 81  ? 0.3082 0.4407 0.3227 0.0146  -0.1313 0.0780  81  ASP B CB  
1516 C CG  . ASP B 81  ? 0.4059 0.5503 0.3990 0.0474  -0.1498 0.0620  81  ASP B CG  
1517 O OD1 . ASP B 81  ? 0.3164 0.5087 0.3052 0.0673  -0.1542 0.0440  81  ASP B OD1 
1518 O OD2 . ASP B 81  ? 0.4510 0.5579 0.4293 0.0546  -0.1610 0.0666  81  ASP B OD2 
1519 N N   . MET B 82  ? 0.2442 0.3808 0.2942 -0.0432 -0.0920 0.1017  82  MET B N   
1520 C CA  . MET B 82  ? 0.2368 0.3438 0.2933 -0.0621 -0.0827 0.1143  82  MET B CA  
1521 C C   . MET B 82  ? 0.2689 0.4041 0.3326 -0.0780 -0.0702 0.1101  82  MET B C   
1522 O O   . MET B 82  ? 0.2287 0.3475 0.2948 -0.0836 -0.0691 0.1122  82  MET B O   
1523 C CB  . MET B 82  ? 0.2344 0.3170 0.2921 -0.0745 -0.0738 0.1298  82  MET B CB  
1524 C CG  . MET B 82  ? 0.2682 0.3171 0.3281 -0.0847 -0.0693 0.1417  82  MET B CG  
1525 S SD  . MET B 82  ? 0.6133 0.6343 0.6683 -0.0740 -0.0863 0.1417  82  MET B SD  
1526 C CE  . MET B 82  ? 0.2849 0.2962 0.3460 -0.0823 -0.0733 0.1396  82  MET B CE  
1527 N N   . TYR B 83  ? 0.2270 0.4073 0.2925 -0.0867 -0.0618 0.1039  83  TYR B N   
1528 C CA  . TYR B 83  ? 0.2268 0.4419 0.2958 -0.1061 -0.0510 0.0985  83  TYR B CA  
1529 C C   . TYR B 83  ? 0.2238 0.4613 0.2964 -0.0919 -0.0598 0.0843  83  TYR B C   
1530 O O   . TYR B 83  ? 0.2220 0.4536 0.2977 -0.1047 -0.0546 0.0850  83  TYR B O   
1531 C CB  . TYR B 83  ? 0.2314 0.5001 0.2989 -0.1179 -0.0431 0.0932  83  TYR B CB  
1532 C CG  . TYR B 83  ? 0.2364 0.5515 0.3042 -0.1446 -0.0319 0.0874  83  TYR B CG  
1533 C CD1 . TYR B 83  ? 0.2516 0.5346 0.3077 -0.1763 -0.0191 0.0989  83  TYR B CD1 
1534 C CD2 . TYR B 83  ? 0.2329 0.6241 0.3068 -0.1368 -0.0352 0.0689  83  TYR B CD2 
1535 C CE1 . TYR B 83  ? 0.2727 0.5761 0.3143 -0.1932 -0.0116 0.0891  83  TYR B CE1 
1536 C CE2 . TYR B 83  ? 0.2409 0.6797 0.3127 -0.1640 -0.0247 0.0630  83  TYR B CE2 
1537 C CZ  . TYR B 83  ? 0.2665 0.6498 0.3167 -0.1913 -0.0131 0.0732  83  TYR B CZ  
1538 O OH  . TYR B 83  ? 0.2919 0.6973 0.3248 -0.2109 -0.0064 0.0649  83  TYR B OH  
1539 N N   . ASP B 84  ? 0.2275 0.4891 0.2960 -0.0631 -0.0742 0.0704  84  ASP B N   
1540 C CA  . ASP B 84  ? 0.2325 0.5099 0.2968 -0.0406 -0.0869 0.0551  84  ASP B CA  
1541 C C   . ASP B 84  ? 0.2351 0.4544 0.2950 -0.0381 -0.0933 0.0626  84  ASP B C   
1542 O O   . ASP B 84  ? 0.2337 0.4636 0.2961 -0.0393 -0.0929 0.0565  84  ASP B O   
1543 C CB  . ASP B 84  ? 0.2473 0.5412 0.2973 -0.0045 -0.1049 0.0403  84  ASP B CB  
1544 C CG  . ASP B 84  ? 0.2450 0.6171 0.2997 -0.0016 -0.1001 0.0272  84  ASP B CG  
1545 O OD1 . ASP B 84  ? 0.2342 0.6535 0.3020 -0.0286 -0.0844 0.0268  84  ASP B OD1 
1546 O OD2 . ASP B 84  ? 0.2739 0.6623 0.3168 0.0264  -0.1125 0.0168  84  ASP B OD2 
1547 N N   . PHE B 85  ? 0.2495 0.4124 0.3021 -0.0353 -0.0997 0.0753  85  PHE B N   
1548 C CA  . PHE B 85  ? 0.2738 0.3863 0.3207 -0.0366 -0.1055 0.0839  85  PHE B CA  
1549 C C   . PHE B 85  ? 0.2394 0.3480 0.3004 -0.0616 -0.0893 0.0935  85  PHE B C   
1550 O O   . PHE B 85  ? 0.2406 0.3349 0.3003 -0.0614 -0.0918 0.0932  85  PHE B O   
1551 C CB  . PHE B 85  ? 0.2631 0.3259 0.2998 -0.0353 -0.1139 0.0967  85  PHE B CB  
1552 C CG  . PHE B 85  ? 0.2925 0.3370 0.3044 -0.0098 -0.1355 0.0878  85  PHE B CG  
1553 C CD1 . PHE B 85  ? 0.3937 0.4214 0.3832 0.0099  -0.1524 0.0771  85  PHE B CD1 
1554 C CD2 . PHE B 85  ? 0.2965 0.3345 0.3021 -0.0043 -0.1403 0.0901  85  PHE B CD2 
1555 C CE1 . PHE B 85  ? 0.3824 0.3825 0.3396 0.0349  -0.1704 0.0668  85  PHE B CE1 
1556 C CE2 . PHE B 85  ? 0.4151 0.4287 0.3916 0.0197  -0.1612 0.0811  85  PHE B CE2 
1557 C CZ  . PHE B 85  ? 0.4573 0.4506 0.4087 0.0388  -0.1708 0.0674  85  PHE B CZ  
1558 N N   . THR B 86  ? 0.2220 0.3394 0.2914 -0.0817 -0.0740 0.1014  86  THR B N   
1559 C CA  . THR B 86  ? 0.2182 0.3245 0.2923 -0.1034 -0.0604 0.1096  86  THR B CA  
1560 C C   . THR B 86  ? 0.2697 0.4109 0.3476 -0.1092 -0.0572 0.0974  86  THR B C   
1561 O O   . THR B 86  ? 0.2165 0.3408 0.2954 -0.1156 -0.0546 0.0999  86  THR B O   
1562 C CB  . THR B 86  ? 0.3334 0.4368 0.4050 -0.1228 -0.0469 0.1189  86  THR B CB  
1563 O OG1 . THR B 86  ? 0.2226 0.2984 0.2913 -0.1158 -0.0498 0.1293  86  THR B OG1 
1564 C CG2 . THR B 86  ? 0.2337 0.3102 0.2937 -0.1318 -0.0352 0.1178  86  THR B CG2 
1565 N N   . ILE B 87  ? 0.2562 0.4513 0.3361 -0.1063 -0.0577 0.0834  87  ILE B N   
1566 C CA  . ILE B 87  ? 0.2480 0.4889 0.3320 -0.1094 -0.0565 0.0691  87  ILE B CA  
1567 C C   . ILE B 87  ? 0.2180 0.4467 0.2992 -0.0855 -0.0700 0.0612  87  ILE B C   
1568 O O   . ILE B 87  ? 0.2164 0.4494 0.3007 -0.0922 -0.0673 0.0578  87  ILE B O   
1569 C CB  . ILE B 87  ? 0.2178 0.5312 0.3040 -0.1063 -0.0564 0.0538  87  ILE B CB  
1570 C CG1 . ILE B 87  ? 0.2226 0.5554 0.3080 -0.1409 -0.0405 0.0609  87  ILE B CG1 
1571 C CG2 . ILE B 87  ? 0.2171 0.5854 0.3071 -0.0988 -0.0600 0.0355  87  ILE B CG2 
1572 C CD1 . ILE B 87  ? 0.2236 0.6284 0.3106 -0.1386 -0.0401 0.0490  87  ILE B CD1 
1573 N N   . LEU B 88  ? 0.2261 0.4347 0.2969 -0.0582 -0.0856 0.0585  88  LEU B N   
1574 C CA  . LEU B 88  ? 0.2373 0.4227 0.2963 -0.0368 -0.1002 0.0526  88  LEU B CA  
1575 C C   . LEU B 88  ? 0.2328 0.3700 0.2944 -0.0524 -0.0952 0.0678  88  LEU B C   
1576 O O   . LEU B 88  ? 0.2375 0.3661 0.2947 -0.0462 -0.1002 0.0639  88  LEU B O   
1577 C CB  . LEU B 88  ? 0.2590 0.4158 0.2958 -0.0081 -0.1200 0.0488  88  LEU B CB  
1578 C CG  . LEU B 88  ? 0.2706 0.4772 0.2982 0.0189  -0.1300 0.0288  88  LEU B CG  
1579 C CD1 . LEU B 88  ? 0.3008 0.4623 0.2987 0.0466  -0.1513 0.0270  88  LEU B CD1 
1580 C CD2 . LEU B 88  ? 0.2753 0.5276 0.3007 0.0348  -0.1344 0.0100  88  LEU B CD2 
1581 N N   . LYS B 89  ? 0.2329 0.3414 0.3000 -0.0701 -0.0859 0.0843  89  LYS B N   
1582 C CA  . LYS B 89  ? 0.2931 0.3645 0.3622 -0.0820 -0.0810 0.0977  89  LYS B CA  
1583 C C   . LYS B 89  ? 0.2233 0.3112 0.3007 -0.0983 -0.0687 0.0954  89  LYS B C   
1584 O O   . LYS B 89  ? 0.2236 0.2962 0.3003 -0.0981 -0.0698 0.0969  89  LYS B O   
1585 C CB  . LYS B 89  ? 0.2265 0.2697 0.2968 -0.0920 -0.0754 0.1140  89  LYS B CB  
1586 C CG  . LYS B 89  ? 0.2247 0.2378 0.2948 -0.0982 -0.0715 0.1253  89  LYS B CG  
1587 C CD  . LYS B 89  ? 0.2315 0.2288 0.2950 -0.0916 -0.0829 0.1255  89  LYS B CD  
1588 C CE  . LYS B 89  ? 0.4462 0.4225 0.4935 -0.0798 -0.0998 0.1260  89  LYS B CE  
1589 N NZ  . LYS B 89  ? 0.3190 0.2711 0.3503 -0.0749 -0.1115 0.1256  89  LYS B NZ  
1590 N N   . ILE B 90  ? 0.2146 0.3320 0.2965 -0.1141 -0.0577 0.0919  90  ILE B N   
1591 C CA  . ILE B 90  ? 0.2168 0.3477 0.3004 -0.1333 -0.0477 0.0888  90  ILE B CA  
1592 C C   . ILE B 90  ? 0.2146 0.3712 0.3012 -0.1217 -0.0548 0.0749  90  ILE B C   
1593 O O   . ILE B 90  ? 0.2154 0.3580 0.3020 -0.1275 -0.0522 0.0761  90  ILE B O   
1594 C CB  . ILE B 90  ? 0.2243 0.3877 0.3052 -0.1548 -0.0372 0.0849  90  ILE B CB  
1595 C CG1 . ILE B 90  ? 0.2383 0.3572 0.3030 -0.1545 -0.0293 0.0936  90  ILE B CG1 
1596 C CG2 . ILE B 90  ? 0.2391 0.4116 0.3103 -0.1678 -0.0284 0.0750  90  ILE B CG2 
1597 C CD1 . ILE B 90  ? 0.2540 0.3945 0.3082 -0.1688 -0.0214 0.0891  90  ILE B CD1 
1598 N N   . GLU B 91  ? 0.2149 0.4072 0.3010 -0.1015 -0.0650 0.0610  91  GLU B N   
1599 C CA  . GLU B 91  ? 0.2176 0.4383 0.3022 -0.0844 -0.0738 0.0453  91  GLU B CA  
1600 C C   . GLU B 91  ? 0.2238 0.3953 0.2990 -0.0688 -0.0842 0.0508  91  GLU B C   
1601 O O   . GLU B 91  ? 0.2254 0.4022 0.3000 -0.0655 -0.0860 0.0445  91  GLU B O   
1602 C CB  . GLU B 91  ? 0.2229 0.4929 0.3034 -0.0610 -0.0840 0.0282  91  GLU B CB  
1603 C CG  . GLU B 91  ? 0.2948 0.6322 0.3857 -0.0813 -0.0723 0.0202  91  GLU B CG  
1604 C CD  . GLU B 91  ? 0.3316 0.7264 0.4194 -0.0583 -0.0806 0.0042  91  GLU B CD  
1605 O OE1 . GLU B 91  ? 0.3742 0.7547 0.4479 -0.0218 -0.0978 -0.0037 91  GLU B OE1 
1606 O OE2 . GLU B 91  ? 0.2178 0.6702 0.3130 -0.0773 -0.0704 -0.0005 91  GLU B OE2 
1607 N N   . ASP B 92  ? 0.3512 0.4754 0.4179 -0.0629 -0.0904 0.0635  92  ASP B N   
1608 C CA  . ASP B 92  ? 0.3000 0.3776 0.3547 -0.0554 -0.0995 0.0717  92  ASP B CA  
1609 C C   . ASP B 92  ? 0.2595 0.3223 0.3238 -0.0742 -0.0878 0.0819  92  ASP B C   
1610 O O   . ASP B 92  ? 0.2640 0.3176 0.3238 -0.0696 -0.0916 0.0801  92  ASP B O   
1611 C CB  . ASP B 92  ? 0.3417 0.3777 0.3842 -0.0519 -0.1080 0.0840  92  ASP B CB  
1612 C CG  . ASP B 92  ? 0.5381 0.5287 0.5612 -0.0471 -0.1201 0.0918  92  ASP B CG  
1613 O OD1 . ASP B 92  ? 0.5352 0.5198 0.5400 -0.0297 -0.1330 0.0814  92  ASP B OD1 
1614 O OD2 . ASP B 92  ? 0.5874 0.5507 0.6110 -0.0609 -0.1173 0.1081  92  ASP B OD2 
1615 N N   . ILE B 93  ? 0.2634 0.3226 0.3374 -0.0929 -0.0744 0.0918  93  ILE B N   
1616 C CA  . ILE B 93  ? 0.2602 0.3036 0.3379 -0.1069 -0.0644 0.1000  93  ILE B CA  
1617 C C   . ILE B 93  ? 0.2603 0.3291 0.3412 -0.1117 -0.0608 0.0879  93  ILE B C   
1618 O O   . ILE B 93  ? 0.2613 0.3164 0.3413 -0.1134 -0.0592 0.0903  93  ILE B O   
1619 C CB  . ILE B 93  ? 0.4987 0.5300 0.5727 -0.1157 -0.0512 0.1050  93  ILE B CB  
1620 C CG1 . ILE B 93  ? 0.3564 0.3712 0.4258 -0.1054 -0.0536 0.1108  93  ILE B CG1 
1621 C CG2 . ILE B 93  ? 0.2687 0.2799 0.3328 -0.1125 -0.0416 0.1019  93  ILE B CG2 
1622 C CD1 . ILE B 93  ? 0.3668 0.3641 0.4317 -0.0941 -0.0589 0.1139  93  ILE B CD1 
1623 N N   . GLN B 94  ? 0.2490 0.3599 0.3335 -0.1144 -0.0596 0.0745  94  GLN B N   
1624 C CA  . GLN B 94  ? 0.2887 0.4309 0.3764 -0.1227 -0.0559 0.0625  94  GLN B CA  
1625 C C   . GLN B 94  ? 0.2757 0.4195 0.3604 -0.1012 -0.0671 0.0543  94  GLN B C   
1626 O O   . GLN B 94  ? 0.2522 0.3927 0.3374 -0.1057 -0.0647 0.0526  94  GLN B O   
1627 C CB  . GLN B 94  ? 0.2558 0.4548 0.3478 -0.1329 -0.0522 0.0491  94  GLN B CB  
1628 C CG  . GLN B 94  ? 0.2549 0.4879 0.3489 -0.1512 -0.0462 0.0387  94  GLN B CG  
1629 C CD  . GLN B 94  ? 0.3671 0.6753 0.4670 -0.1467 -0.0494 0.0192  94  GLN B CD  
1630 O OE1 . GLN B 94  ? 0.3688 0.6995 0.4694 -0.1226 -0.0582 0.0121  94  GLN B OE1 
1631 N NE2 . GLN B 94  ? 0.4581 0.7942 0.5531 -0.1625 -0.0409 0.0094  94  GLN B NE2 
1632 N N   . ARG B 95  ? 0.4065 0.5486 0.4830 -0.0771 -0.0806 0.0498  95  ARG B N   
1633 C CA  . ARG B 95  ? 0.2701 0.3986 0.3338 -0.0554 -0.0938 0.0442  95  ARG B CA  
1634 C C   . ARG B 95  ? 0.2715 0.3537 0.3313 -0.0617 -0.0925 0.0591  95  ARG B C   
1635 O O   . ARG B 95  ? 0.2775 0.3597 0.3336 -0.0559 -0.0954 0.0542  95  ARG B O   
1636 C CB  . ARG B 95  ? 0.2885 0.4032 0.3326 -0.0293 -0.1110 0.0398  95  ARG B CB  
1637 C CG  . ARG B 95  ? 0.5096 0.5943 0.5301 -0.0080 -0.1266 0.0363  95  ARG B CG  
1638 C CD  . ARG B 95  ? 0.6027 0.6381 0.5934 0.0080  -0.1440 0.0420  95  ARG B CD  
1639 N NE  . ARG B 95  ? 0.7328 0.7302 0.7268 -0.0125 -0.1388 0.0628  95  ARG B NE  
1640 C CZ  . ARG B 95  ? 0.7730 0.7300 0.7583 -0.0240 -0.1399 0.0783  95  ARG B CZ  
1641 N NH1 . ARG B 95  ? 0.6746 0.6177 0.6464 -0.0180 -0.1457 0.0763  95  ARG B NH1 
1642 N NH2 . ARG B 95  ? 0.7701 0.7054 0.7595 -0.0415 -0.1352 0.0954  95  ARG B NH2 
1643 N N   . LYS B 96  ? 0.3432 0.3917 0.4035 -0.0719 -0.0887 0.0763  96  LYS B N   
1644 C CA  . LYS B 96  ? 0.4016 0.4179 0.4590 -0.0781 -0.0866 0.0902  96  LYS B CA  
1645 C C   . LYS B 96  ? 0.3208 0.3479 0.3881 -0.0893 -0.0752 0.0884  96  LYS B C   
1646 O O   . LYS B 96  ? 0.2756 0.2928 0.3393 -0.0868 -0.0765 0.0902  96  LYS B O   
1647 C CB  . LYS B 96  ? 0.3864 0.3798 0.4451 -0.0876 -0.0827 0.1070  96  LYS B CB  
1648 C CG  . LYS B 96  ? 0.5057 0.4791 0.5509 -0.0807 -0.0948 0.1122  96  LYS B CG  
1649 C CD  . LYS B 96  ? 0.5142 0.4800 0.5619 -0.0867 -0.0872 0.1205  96  LYS B CD  
1650 C CE  . LYS B 96  ? 0.5384 0.4918 0.5753 -0.0832 -0.0962 0.1210  96  LYS B CE  
1651 N NZ  . LYS B 96  ? 0.6248 0.5510 0.6371 -0.0760 -0.1139 0.1199  96  LYS B NZ  
1652 N N   . ILE B 97  ? 0.2703 0.3141 0.3460 -0.1032 -0.0646 0.0855  97  ILE B N   
1653 C CA  . ILE B 97  ? 0.3404 0.3879 0.4181 -0.1166 -0.0552 0.0827  97  ILE B CA  
1654 C C   . ILE B 97  ? 0.4677 0.5400 0.5464 -0.1108 -0.0593 0.0685  97  ILE B C   
1655 O O   . ILE B 97  ? 0.3163 0.3785 0.3931 -0.1125 -0.0571 0.0691  97  ILE B O   
1656 C CB  . ILE B 97  ? 0.2768 0.3356 0.3546 -0.1361 -0.0458 0.0805  97  ILE B CB  
1657 C CG1 . ILE B 97  ? 0.3386 0.3648 0.4054 -0.1303 -0.0390 0.0889  97  ILE B CG1 
1658 C CG2 . ILE B 97  ? 0.2894 0.3498 0.3601 -0.1495 -0.0386 0.0732  97  ILE B CG2 
1659 C CD1 . ILE B 97  ? 0.2966 0.3226 0.3533 -0.1406 -0.0298 0.0839  97  ILE B CD1 
1660 N N   . GLU B 98  ? 0.4355 0.5424 0.5158 -0.1007 -0.0662 0.0547  98  GLU B N   
1661 C CA  . GLU B 98  ? 0.2907 0.4303 0.3715 -0.0929 -0.0705 0.0386  98  GLU B CA  
1662 C C   . GLU B 98  ? 0.4388 0.5504 0.5098 -0.0750 -0.0797 0.0420  98  GLU B C   
1663 O O   . GLU B 98  ? 0.4401 0.5581 0.5110 -0.0743 -0.0791 0.0364  98  GLU B O   
1664 C CB  . GLU B 98  ? 0.3603 0.5492 0.4419 -0.0799 -0.0775 0.0216  98  GLU B CB  
1665 C CG  . GLU B 98  ? 0.3433 0.5701 0.4337 -0.0997 -0.0686 0.0177  98  GLU B CG  
1666 C CD  . GLU B 98  ? 0.4849 0.7372 0.5802 -0.1306 -0.0567 0.0134  98  GLU B CD  
1667 O OE1 . GLU B 98  ? 0.4736 0.6884 0.5649 -0.1454 -0.0504 0.0227  98  GLU B OE1 
1668 O OE2 . GLU B 98  ? 0.6653 0.9771 0.7655 -0.1410 -0.0543 0.0001  98  GLU B OE2 
1669 N N   . ASP B 99  ? 0.4660 0.5442 0.5259 -0.0632 -0.0883 0.0522  99  ASP B N   
1670 C CA  . ASP B 99  ? 0.3552 0.4015 0.3994 -0.0512 -0.0978 0.0581  99  ASP B CA  
1671 C C   . ASP B 99  ? 0.4969 0.5273 0.5465 -0.0637 -0.0888 0.0690  99  ASP B C   
1672 O O   . ASP B 99  ? 0.3424 0.3686 0.3852 -0.0568 -0.0925 0.0664  99  ASP B O   
1673 C CB  . ASP B 99  ? 0.3151 0.3253 0.3422 -0.0450 -0.1082 0.0694  99  ASP B CB  
1674 C CG  . ASP B 99  ? 0.4803 0.4971 0.4917 -0.0244 -0.1221 0.0567  99  ASP B CG  
1675 O OD1 . ASP B 99  ? 0.6493 0.7034 0.6621 -0.0105 -0.1252 0.0381  99  ASP B OD1 
1676 O OD2 . ASP B 99  ? 0.4478 0.4343 0.4432 -0.0209 -0.1311 0.0645  99  ASP B OD2 
1677 N N   . LEU B 100 ? 0.4549 0.4770 0.5139 -0.0792 -0.0778 0.0801  100 LEU B N   
1678 C CA  . LEU B 100 ? 0.2973 0.3080 0.3591 -0.0873 -0.0693 0.0882  100 LEU B CA  
1679 C C   . LEU B 100 ? 0.3666 0.3943 0.4322 -0.0920 -0.0640 0.0761  100 LEU B C   
1680 O O   . LEU B 100 ? 0.3199 0.3399 0.3826 -0.0902 -0.0624 0.0779  100 LEU B O   
1681 C CB  . LEU B 100 ? 0.2878 0.2861 0.3531 -0.0978 -0.0604 0.0996  100 LEU B CB  
1682 C CG  . LEU B 100 ? 0.2760 0.2590 0.3376 -0.0956 -0.0645 0.1141  100 LEU B CG  
1683 C CD1 . LEU B 100 ? 0.3371 0.3182 0.3969 -0.0929 -0.0537 0.1132  100 LEU B CD1 
1684 C CD2 . LEU B 100 ? 0.2817 0.2566 0.3351 -0.0906 -0.0693 0.1212  100 LEU B CD2 
1685 N N   . LYS B 101 ? 0.3792 0.4329 0.4501 -0.0998 -0.0613 0.0638  101 LYS B N   
1686 C CA  . LYS B 101 ? 0.3515 0.4264 0.4240 -0.1085 -0.0576 0.0511  101 LYS B CA  
1687 C C   . LYS B 101 ? 0.4338 0.5255 0.5048 -0.0920 -0.0660 0.0405  101 LYS B C   
1688 O O   . LYS B 101 ? 0.3064 0.4013 0.3763 -0.0943 -0.0641 0.0354  101 LYS B O   
1689 C CB  . LYS B 101 ? 0.4447 0.5534 0.5216 -0.1241 -0.0537 0.0402  101 LYS B CB  
1690 C CG  . LYS B 101 ? 0.5647 0.6522 0.6355 -0.1467 -0.0441 0.0483  101 LYS B CG  
1691 C CD  . LYS B 101 ? 0.4613 0.5869 0.5343 -0.1658 -0.0407 0.0384  101 LYS B CD  
1692 C CE  . LYS B 101 ? 0.5082 0.6026 0.5623 -0.1858 -0.0310 0.0429  101 LYS B CE  
1693 N NZ  . LYS B 101 ? 0.6580 0.7021 0.7029 -0.1751 -0.0285 0.0577  101 LYS B NZ  
1694 N N   . ARG B 102 ? 0.3433 0.4418 0.4099 -0.0737 -0.0767 0.0368  102 ARG B N   
1695 C CA  . ARG B 102 ? 0.2997 0.4070 0.3575 -0.0540 -0.0870 0.0267  102 ARG B CA  
1696 C C   . ARG B 102 ? 0.3463 0.4183 0.3956 -0.0509 -0.0879 0.0390  102 ARG B C   
1697 O O   . ARG B 102 ? 0.3273 0.4065 0.3735 -0.0444 -0.0899 0.0320  102 ARG B O   
1698 C CB  . ARG B 102 ? 0.3108 0.4205 0.3558 -0.0325 -0.1005 0.0209  102 ARG B CB  
1699 C CG  . ARG B 102 ? 0.3058 0.4706 0.3598 -0.0305 -0.1004 0.0025  102 ARG B CG  
1700 C CD  . ARG B 102 ? 0.3206 0.4877 0.3587 -0.0050 -0.1147 -0.0046 102 ARG B CD  
1701 N NE  . ARG B 102 ? 0.4788 0.6315 0.4921 0.0241  -0.1306 -0.0126 102 ARG B NE  
1702 C CZ  . ARG B 102 ? 0.4757 0.5947 0.4593 0.0485  -0.1474 -0.0126 102 ARG B CZ  
1703 N NH1 . ARG B 102 ? 0.5500 0.6514 0.5297 0.0465  -0.1496 -0.0052 102 ARG B NH1 
1704 N NH2 . ARG B 102 ? 0.4984 0.5967 0.4520 0.0750  -0.1630 -0.0198 102 ARG B NH2 
1705 N N   . ILE B 103 ? 0.4369 0.4763 0.4826 -0.0560 -0.0863 0.0571  103 ILE B N   
1706 C CA  . ILE B 103 ? 0.4240 0.4400 0.4627 -0.0560 -0.0857 0.0696  103 ILE B CA  
1707 C C   . ILE B 103 ? 0.3000 0.3227 0.3475 -0.0646 -0.0751 0.0682  103 ILE B C   
1708 O O   . ILE B 103 ? 0.3158 0.3366 0.3586 -0.0591 -0.0761 0.0677  103 ILE B O   
1709 C CB  . ILE B 103 ? 0.2865 0.2787 0.3208 -0.0624 -0.0855 0.0882  103 ILE B CB  
1710 C CG1 . ILE B 103 ? 0.2813 0.2533 0.2953 -0.0537 -0.0998 0.0911  103 ILE B CG1 
1711 C CG2 . ILE B 103 ? 0.2628 0.2467 0.2952 -0.0665 -0.0806 0.1009  103 ILE B CG2 
1712 C CD1 . ILE B 103 ? 0.4041 0.3577 0.4139 -0.0633 -0.1008 0.1067  103 ILE B CD1 
1713 N N   . GLU B 104 ? 0.2856 0.3117 0.3413 -0.0776 -0.0661 0.0676  104 GLU B N   
1714 C CA  . GLU B 104 ? 0.4031 0.4255 0.4581 -0.0856 -0.0584 0.0650  104 GLU B CA  
1715 C C   . GLU B 104 ? 0.3326 0.3759 0.3878 -0.0838 -0.0607 0.0492  104 GLU B C   
1716 O O   . GLU B 104 ? 0.2854 0.3221 0.3359 -0.0802 -0.0598 0.0486  104 GLU B O   
1717 C CB  . GLU B 104 ? 0.2946 0.3112 0.3494 -0.1015 -0.0512 0.0649  104 GLU B CB  
1718 C CG  . GLU B 104 ? 0.4181 0.4076 0.4607 -0.1065 -0.0450 0.0703  104 GLU B CG  
1719 C CD  . GLU B 104 ? 0.6208 0.5966 0.6551 -0.1235 -0.0400 0.0700  104 GLU B CD  
1720 O OE1 . GLU B 104 ? 0.5210 0.4660 0.5358 -0.1288 -0.0367 0.0719  104 GLU B OE1 
1721 O OE2 . GLU B 104 ? 0.6726 0.6669 0.7158 -0.1307 -0.0403 0.0673  104 GLU B OE2 
1722 N N   . ARG B 105 ? 0.2746 0.3479 0.3351 -0.0843 -0.0644 0.0355  105 ARG B N   
1723 C CA  . ARG B 105 ? 0.2868 0.3906 0.3486 -0.0828 -0.0670 0.0185  105 ARG B CA  
1724 C C   . ARG B 105 ? 0.3358 0.4336 0.3908 -0.0622 -0.0747 0.0184  105 ARG B C   
1725 O O   . ARG B 105 ? 0.3041 0.4108 0.3577 -0.0611 -0.0744 0.0103  105 ARG B O   
1726 C CB  . ARG B 105 ? 0.2684 0.4170 0.3369 -0.0836 -0.0703 0.0032  105 ARG B CB  
1727 C CG  . ARG B 105 ? 0.2705 0.4653 0.3407 -0.0741 -0.0762 -0.0172 105 ARG B CG  
1728 C CD  . ARG B 105 ? 0.2772 0.4794 0.3474 -0.0906 -0.0706 -0.0241 105 ARG B CD  
1729 N NE  . ARG B 105 ? 0.4203 0.6101 0.4886 -0.1213 -0.0610 -0.0196 105 ARG B NE  
1730 C CZ  . ARG B 105 ? 0.4765 0.6377 0.5343 -0.1369 -0.0562 -0.0166 105 ARG B CZ  
1731 N NH1 . ARG B 105 ? 0.6240 0.7731 0.6774 -0.1248 -0.0588 -0.0180 105 ARG B NH1 
1732 N NH2 . ARG B 105 ? 0.3639 0.5046 0.4110 -0.1638 -0.0499 -0.0123 105 ARG B NH2 
1733 N N   . MET B 106 ? 0.2598 0.3398 0.3068 -0.0477 -0.0824 0.0274  106 MET B N   
1734 C CA  . MET B 106 ? 0.2707 0.3347 0.3036 -0.0316 -0.0905 0.0311  106 MET B CA  
1735 C C   . MET B 106 ? 0.2706 0.3180 0.3027 -0.0365 -0.0842 0.0416  106 MET B C   
1736 O O   . MET B 106 ? 0.2773 0.3266 0.3029 -0.0278 -0.0871 0.0377  106 MET B O   
1737 C CB  . MET B 106 ? 0.3372 0.3738 0.3533 -0.0221 -0.1005 0.0421  106 MET B CB  
1738 C CG  . MET B 106 ? 0.2966 0.3437 0.3002 -0.0037 -0.1134 0.0281  106 MET B CG  
1739 S SD  . MET B 106 ? 0.6560 0.6627 0.6366 0.0015  -0.1249 0.0410  106 MET B SD  
1740 C CE  . MET B 106 ? 0.3523 0.3532 0.2994 0.0342  -0.1454 0.0243  106 MET B CE  
1741 N N   . LEU B 107 ? 0.2651 0.2977 0.3017 -0.0476 -0.0763 0.0547  107 LEU B N   
1742 C CA  . LEU B 107 ? 0.2671 0.2888 0.3011 -0.0483 -0.0708 0.0642  107 LEU B CA  
1743 C C   . LEU B 107 ? 0.2711 0.3007 0.3067 -0.0509 -0.0664 0.0518  107 LEU B C   
1744 O O   . LEU B 107 ? 0.2767 0.3049 0.3068 -0.0436 -0.0664 0.0520  107 LEU B O   
1745 C CB  . LEU B 107 ? 0.2924 0.3018 0.3286 -0.0556 -0.0645 0.0782  107 LEU B CB  
1746 C CG  . LEU B 107 ? 0.2620 0.2635 0.2948 -0.0566 -0.0688 0.0926  107 LEU B CG  
1747 C CD1 . LEU B 107 ? 0.2566 0.2533 0.2945 -0.0638 -0.0620 0.1022  107 LEU B CD1 
1748 C CD2 . LEU B 107 ? 0.2706 0.2689 0.2916 -0.0526 -0.0735 0.1039  107 LEU B CD2 
1749 N N   . MET B 108 ? 0.2775 0.3157 0.3181 -0.0632 -0.0631 0.0410  108 MET B N   
1750 C CA  . MET B 108 ? 0.2826 0.3261 0.3198 -0.0721 -0.0603 0.0282  108 MET B CA  
1751 C C   . MET B 108 ? 0.3582 0.4246 0.3962 -0.0617 -0.0660 0.0155  108 MET B C   
1752 O O   . MET B 108 ? 0.2920 0.3533 0.3235 -0.0590 -0.0654 0.0118  108 MET B O   
1753 C CB  . MET B 108 ? 0.4054 0.4603 0.4452 -0.0925 -0.0572 0.0193  108 MET B CB  
1754 C CG  . MET B 108 ? 0.3913 0.4185 0.4250 -0.1042 -0.0515 0.0303  108 MET B CG  
1755 S SD  . MET B 108 ? 0.8412 0.8232 0.8501 -0.1101 -0.0475 0.0342  108 MET B SD  
1756 C CE  . MET B 108 ? 0.4367 0.4282 0.4347 -0.1316 -0.0486 0.0156  108 MET B CE  
1757 N N   . ASP B 109 ? 0.2756 0.3659 0.3183 -0.0528 -0.0728 0.0082  109 ASP B N   
1758 C CA  . ASP B 109 ? 0.2790 0.3917 0.3192 -0.0392 -0.0795 -0.0049 109 ASP B CA  
1759 C C   . ASP B 109 ? 0.3308 0.4220 0.3605 -0.0239 -0.0827 0.0048  109 ASP B C   
1760 O O   . ASP B 109 ? 0.2905 0.3903 0.3167 -0.0176 -0.0840 -0.0034 109 ASP B O   
1761 C CB  . ASP B 109 ? 0.2972 0.4361 0.3379 -0.0267 -0.0882 -0.0150 109 ASP B CB  
1762 C CG  . ASP B 109 ? 0.4027 0.5778 0.4548 -0.0423 -0.0847 -0.0273 109 ASP B CG  
1763 O OD1 . ASP B 109 ? 0.3265 0.5155 0.3832 -0.0635 -0.0779 -0.0346 109 ASP B OD1 
1764 O OD2 . ASP B 109 ? 0.2686 0.4562 0.3214 -0.0345 -0.0895 -0.0293 109 ASP B OD2 
1765 N N   . LEU B 110 ? 0.2848 0.3512 0.3083 -0.0199 -0.0839 0.0224  110 LEU B N   
1766 C CA  . LEU B 110 ? 0.2919 0.3413 0.3043 -0.0118 -0.0853 0.0350  110 LEU B CA  
1767 C C   . LEU B 110 ? 0.3581 0.4065 0.3724 -0.0145 -0.0778 0.0357  110 LEU B C   
1768 O O   . LEU B 110 ? 0.2993 0.3518 0.3072 -0.0051 -0.0799 0.0321  110 LEU B O   
1769 C CB  . LEU B 110 ? 0.3120 0.3413 0.3186 -0.0158 -0.0859 0.0544  110 LEU B CB  
1770 C CG  . LEU B 110 ? 0.3143 0.3313 0.3052 -0.0082 -0.0977 0.0557  110 LEU B CG  
1771 C CD1 . LEU B 110 ? 0.3085 0.3055 0.2937 -0.0179 -0.0985 0.0736  110 LEU B CD1 
1772 C CD2 . LEU B 110 ? 0.3310 0.3389 0.3012 0.0041  -0.1059 0.0563  110 LEU B CD2 
1773 N N   . LYS B 111 ? 0.2905 0.3304 0.3094 -0.0251 -0.0702 0.0393  111 LYS B N   
1774 C CA  . LYS B 111 ? 0.3830 0.4135 0.3959 -0.0241 -0.0650 0.0396  111 LYS B CA  
1775 C C   . LYS B 111 ? 0.3110 0.3475 0.3205 -0.0265 -0.0660 0.0215  111 LYS B C   
1776 O O   . LYS B 111 ? 0.3227 0.3530 0.3230 -0.0190 -0.0655 0.0194  111 LYS B O   
1777 C CB  . LYS B 111 ? 0.3929 0.4052 0.4036 -0.0330 -0.0592 0.0457  111 LYS B CB  
1778 C CG  . LYS B 111 ? 0.3199 0.3215 0.3248 -0.0479 -0.0574 0.0319  111 LYS B CG  
1779 C CD  . LYS B 111 ? 0.4498 0.4224 0.4422 -0.0550 -0.0534 0.0375  111 LYS B CD  
1780 C CE  . LYS B 111 ? 0.4993 0.4455 0.4694 -0.0669 -0.0538 0.0258  111 LYS B CE  
1781 N NZ  . LYS B 111 ? 0.5867 0.5492 0.5614 -0.0899 -0.0548 0.0119  111 LYS B NZ  
1782 N N   . GLU B 112 ? 0.3248 0.3776 0.3410 -0.0373 -0.0678 0.0081  112 GLU B N   
1783 C CA  . GLU B 112 ? 0.3189 0.3863 0.3327 -0.0440 -0.0693 -0.0097 112 GLU B CA  
1784 C C   . GLU B 112 ? 0.3156 0.4020 0.3299 -0.0263 -0.0751 -0.0159 112 GLU B C   
1785 O O   . GLU B 112 ? 0.3244 0.4244 0.3359 -0.0278 -0.0769 -0.0300 112 GLU B O   
1786 C CB  . GLU B 112 ? 0.3175 0.4086 0.3386 -0.0632 -0.0691 -0.0221 112 GLU B CB  
1787 C CG  . GLU B 112 ? 0.4179 0.4828 0.4316 -0.0835 -0.0635 -0.0161 112 GLU B CG  
1788 C CD  . GLU B 112 ? 0.3800 0.4709 0.4013 -0.1044 -0.0623 -0.0241 112 GLU B CD  
1789 O OE1 . GLU B 112 ? 0.3431 0.4797 0.3762 -0.1022 -0.0660 -0.0372 112 GLU B OE1 
1790 O OE2 . GLU B 112 ? 0.3907 0.4583 0.4039 -0.1219 -0.0580 -0.0179 112 GLU B OE2 
1791 N N   . ARG B 113 ? 0.3074 0.3927 0.3215 -0.0111 -0.0790 -0.0056 113 ARG B N   
1792 C CA  . ARG B 113 ? 0.3154 0.4096 0.3225 0.0065  -0.0853 -0.0093 113 ARG B CA  
1793 C C   . ARG B 113 ? 0.3202 0.4029 0.3193 0.0130  -0.0825 -0.0043 113 ARG B C   
1794 O O   . ARG B 113 ? 0.3261 0.4183 0.3193 0.0251  -0.0867 -0.0108 113 ARG B O   
1795 C CB  . ARG B 113 ? 0.3136 0.3990 0.3118 0.0191  -0.0925 0.0014  113 ARG B CB  
1796 C CG  . ARG B 113 ? 0.3115 0.4079 0.3118 0.0205  -0.0984 -0.0062 113 ARG B CG  
1797 C CD  . ARG B 113 ? 0.3241 0.3965 0.3060 0.0315  -0.1074 0.0061  113 ARG B CD  
1798 N NE  . ARG B 113 ? 0.4692 0.5463 0.4337 0.0521  -0.1186 -0.0049 113 ARG B NE  
1799 C CZ  . ARG B 113 ? 0.3745 0.4604 0.3281 0.0680  -0.1295 -0.0176 113 ARG B CZ  
1800 N NH1 . ARG B 113 ? 0.3506 0.4414 0.3095 0.0647  -0.1306 -0.0195 113 ARG B NH1 
1801 N NH2 . ARG B 113 ? 0.3744 0.4638 0.3084 0.0904  -0.1402 -0.0287 113 ARG B NH2 
1802 N N   . CYS B 114 ? 0.3231 0.3874 0.3197 0.0080  -0.0761 0.0061  114 CYS B N   
1803 C CA  . CYS B 114 ? 0.3322 0.3904 0.3189 0.0197  -0.0743 0.0121  114 CYS B CA  
1804 C C   . CYS B 114 ? 0.3469 0.4048 0.3267 0.0214  -0.0752 -0.0036 114 CYS B C   
1805 O O   . CYS B 114 ? 0.3566 0.4096 0.3358 0.0072  -0.0749 -0.0157 114 CYS B O   
1806 C CB  . CYS B 114 ? 0.3459 0.3900 0.3285 0.0197  -0.0687 0.0260  114 CYS B CB  
1807 S SG  . CYS B 114 ? 0.4284 0.4774 0.4161 0.0174  -0.0679 0.0470  114 CYS B SG  
1808 N N   . PRO B 115 ? 0.3530 0.4169 0.3253 0.0367  -0.0769 -0.0034 115 PRO B N   
1809 C CA  . PRO B 115 ? 0.3703 0.4318 0.3331 0.0399  -0.0788 -0.0187 115 PRO B CA  
1810 C C   . PRO B 115 ? 0.3937 0.4266 0.3399 0.0395  -0.0766 -0.0193 115 PRO B C   
1811 O O   . PRO B 115 ? 0.3948 0.4139 0.3376 0.0405  -0.0730 -0.0075 115 PRO B O   
1812 C CB  . PRO B 115 ? 0.3695 0.4460 0.3281 0.0589  -0.0814 -0.0153 115 PRO B CB  
1813 C CG  . PRO B 115 ? 0.3596 0.4391 0.3191 0.0634  -0.0789 0.0056  115 PRO B CG  
1814 C CD  . PRO B 115 ? 0.3474 0.4213 0.3170 0.0491  -0.0782 0.0106  115 PRO B CD  
1815 N N   . GLU B 116 ? 0.4324 0.4539 0.3638 0.0395  -0.0800 -0.0338 116 GLU B N   
1816 C CA  . GLU B 116 ? 0.4771 0.4607 0.3814 0.0427  -0.0812 -0.0368 116 GLU B CA  
1817 C C   . GLU B 116 ? 0.4959 0.4804 0.3908 0.0701  -0.0797 -0.0251 116 GLU B C   
1818 O O   . GLU B 116 ? 0.5515 0.5152 0.4326 0.0768  -0.0784 -0.0181 116 GLU B O   
1819 C CB  . GLU B 116 ? 0.5355 0.5053 0.4216 0.0365  -0.0872 -0.0552 116 GLU B CB  
1820 C CG  . GLU B 116 ? 0.6197 0.5426 0.4675 0.0475  -0.0918 -0.0593 116 GLU B CG  
1821 C CD  . GLU B 116 ? 0.8464 0.7514 0.6720 0.0387  -0.0992 -0.0777 116 GLU B CD  
1822 O OE1 . GLU B 116 ? 0.7963 0.7323 0.6399 0.0220  -0.0997 -0.0877 116 GLU B OE1 
1823 O OE2 . GLU B 116 ? 0.9413 0.8019 0.7287 0.0501  -0.1055 -0.0830 116 GLU B OE2 
1824 N N   . ASN B 117 ? 0.4691 0.4829 0.3710 0.0862  -0.0800 -0.0229 117 ASN B N   
1825 C CA  . ASN B 117 ? 0.4725 0.5025 0.3684 0.1097  -0.0778 -0.0111 117 ASN B CA  
1826 C C   . ASN B 117 ? 0.4136 0.4727 0.3293 0.1055  -0.0728 0.0075  117 ASN B C   
1827 O O   . ASN B 117 ? 0.3951 0.4749 0.3234 0.1005  -0.0732 0.0121  117 ASN B O   
1828 C CB  . ASN B 117 ? 0.4508 0.4988 0.3402 0.1275  -0.0807 -0.0170 117 ASN B CB  
1829 C CG  . ASN B 117 ? 0.4585 0.5393 0.3458 0.1487  -0.0774 -0.0032 117 ASN B CG  
1830 O OD1 . ASN B 117 ? 0.4504 0.5353 0.3318 0.1576  -0.0746 0.0056  117 ASN B OD1 
1831 N ND2 . ASN B 117 ? 0.4993 0.6084 0.3905 0.1561  -0.0778 -0.0011 117 ASN B ND2 
1832 N N   . LYS B 118 ? 0.4141 0.4714 0.3276 0.1079  -0.0693 0.0180  118 LYS B N   
1833 C CA  . LYS B 118 ? 0.3896 0.4704 0.3190 0.0991  -0.0652 0.0355  118 LYS B CA  
1834 C C   . LYS B 118 ? 0.4206 0.5413 0.3470 0.1136  -0.0624 0.0490  118 LYS B C   
1835 O O   . LYS B 118 ? 0.4210 0.5647 0.3561 0.1043  -0.0592 0.0650  118 LYS B O   
1836 C CB  . LYS B 118 ? 0.3894 0.4504 0.3204 0.0894  -0.0629 0.0391  118 LYS B CB  
1837 C CG  . LYS B 118 ? 0.3926 0.4218 0.3261 0.0707  -0.0651 0.0271  118 LYS B CG  
1838 C CD  . LYS B 118 ? 0.3916 0.4032 0.3267 0.0596  -0.0625 0.0326  118 LYS B CD  
1839 C CE  . LYS B 118 ? 0.3935 0.3831 0.3322 0.0375  -0.0639 0.0220  118 LYS B CE  
1840 N NZ  . LYS B 118 ? 0.4188 0.3885 0.3420 0.0336  -0.0682 0.0048  118 LYS B NZ  
1841 N N   . ASP B 119 ? 0.4568 0.5892 0.3696 0.1347  -0.0638 0.0427  119 ASP B N   
1842 C CA  . ASP B 119 ? 0.4720 0.6531 0.3831 0.1459  -0.0608 0.0555  119 ASP B CA  
1843 C C   . ASP B 119 ? 0.4541 0.6514 0.3694 0.1371  -0.0620 0.0605  119 ASP B C   
1844 O O   . ASP B 119 ? 0.5671 0.7716 0.4738 0.1510  -0.0642 0.0528  119 ASP B O   
1845 C CB  . ASP B 119 ? 0.5809 0.7726 0.4720 0.1774  -0.0622 0.0466  119 ASP B CB  
1846 C CG  . ASP B 119 ? 0.6612 0.9148 0.5504 0.1903  -0.0590 0.0573  119 ASP B CG  
1847 O OD1 . ASP B 119 ? 0.7780 1.0671 0.6791 0.1716  -0.0549 0.0749  119 ASP B OD1 
1848 O OD2 . ASP B 119 ? 0.7357 1.0027 0.6083 0.2183  -0.0614 0.0482  119 ASP B OD2 
1849 N N   . ILE B 120 ? 0.4333 0.6362 0.3569 0.1153  -0.0612 0.0749  120 ILE B N   
1850 C CA  . ILE B 120 ? 0.3785 0.5825 0.2982 0.1043  -0.0647 0.0812  120 ILE B CA  
1851 C C   . ILE B 120 ? 0.4119 0.6243 0.3312 0.0815  -0.0640 0.1015  120 ILE B C   
1852 O O   . ILE B 120 ? 0.3922 0.6007 0.3204 0.0729  -0.0615 0.1061  120 ILE B O   
1853 C CB  . ILE B 120 ? 0.3780 0.5447 0.3006 0.1009  -0.0707 0.0660  120 ILE B CB  
1854 C CG1 . ILE B 120 ? 0.4459 0.5861 0.3803 0.0888  -0.0708 0.0613  120 ILE B CG1 
1855 C CG2 . ILE B 120 ? 0.3957 0.5568 0.3146 0.1186  -0.0728 0.0467  120 ILE B CG2 
1856 C CD1 . ILE B 120 ? 0.3668 0.4845 0.3051 0.0855  -0.0763 0.0454  120 ILE B CD1 
1857 N N   . TYR B 121 ? 0.3968 0.6142 0.3015 0.0702  -0.0676 0.1135  121 TYR B N   
1858 C CA  . TYR B 121 ? 0.4581 0.6719 0.3525 0.0442  -0.0698 0.1332  121 TYR B CA  
1859 C C   . TYR B 121 ? 0.4168 0.5810 0.3106 0.0350  -0.0768 0.1284  121 TYR B C   
1860 O O   . TYR B 121 ? 0.3972 0.5503 0.2888 0.0170  -0.0782 0.1396  121 TYR B O   
1861 C CB  . TYR B 121 ? 0.4347 0.6606 0.3036 0.0325  -0.0731 0.1482  121 TYR B CB  
1862 C CG  . TYR B 121 ? 0.5010 0.7885 0.3683 0.0334  -0.0659 0.1588  121 TYR B CG  
1863 C CD1 . TYR B 121 ? 0.5707 0.8780 0.4137 0.0217  -0.0677 0.1726  121 TYR B CD1 
1864 C CD2 . TYR B 121 ? 0.4737 0.8017 0.3597 0.0472  -0.0581 0.1548  121 TYR B CD2 
1865 C CE1 . TYR B 121 ? 0.5775 0.9469 0.4240 0.0214  -0.0591 0.1784  121 TYR B CE1 
1866 C CE2 . TYR B 121 ? 0.4494 0.8439 0.3330 0.0527  -0.0521 0.1626  121 TYR B CE2 
1867 C CZ  . TYR B 121 ? 0.6057 1.0219 0.4740 0.0382  -0.0511 0.1727  121 TYR B CZ  
1868 O OH  . TYR B 121 ? 0.7531 1.2352 0.6282 0.0415  -0.0422 0.1747  121 TYR B OH  
1869 N N   . GLU B 122 ? 0.3946 0.5333 0.2888 0.0481  -0.0819 0.1111  122 GLU B N   
1870 C CA  . GLU B 122 ? 0.4115 0.5126 0.3032 0.0439  -0.0896 0.1043  122 GLU B CA  
1871 C C   . GLU B 122 ? 0.4201 0.5160 0.3362 0.0449  -0.0856 0.0924  122 GLU B C   
1872 O O   . GLU B 122 ? 0.5563 0.6558 0.4859 0.0560  -0.0829 0.0755  122 GLU B O   
1873 C CB  . GLU B 122 ? 0.4118 0.4966 0.2906 0.0580  -0.0978 0.0907  122 GLU B CB  
1874 C CG  . GLU B 122 ? 0.4440 0.5245 0.2915 0.0542  -0.1031 0.1050  122 GLU B CG  
1875 C CD  . GLU B 122 ? 0.4411 0.5540 0.2889 0.0648  -0.0978 0.1044  122 GLU B CD  
1876 O OE1 . GLU B 122 ? 0.4198 0.5603 0.2902 0.0755  -0.0895 0.0954  122 GLU B OE1 
1877 O OE2 . GLU B 122 ? 0.5815 0.6894 0.4014 0.0619  -0.1029 0.1145  122 GLU B OE2 
1878 N N   . CYS B 123 ? 0.3834 0.4668 0.3006 0.0307  -0.0864 0.1016  123 CYS B N   
1879 C CA  . CYS B 123 ? 0.4816 0.5578 0.4184 0.0289  -0.0834 0.0923  123 CYS B CA  
1880 C C   . CYS B 123 ? 0.3794 0.4294 0.3104 0.0267  -0.0922 0.0857  123 CYS B C   
1881 O O   . CYS B 123 ? 0.3864 0.4173 0.2986 0.0179  -0.0992 0.0979  123 CYS B O   
1882 C CB  . CYS B 123 ? 0.3543 0.4421 0.2988 0.0178  -0.0769 0.1063  123 CYS B CB  
1883 S SG  . CYS B 123 ? 0.3386 0.4102 0.3006 0.0125  -0.0749 0.0979  123 CYS B SG  
1884 N N   . PRO B 124 ? 0.3526 0.4029 0.2956 0.0348  -0.0932 0.0657  124 PRO B N   
1885 C CA  . PRO B 124 ? 0.4384 0.4755 0.3774 0.0375  -0.1017 0.0556  124 PRO B CA  
1886 C C   . PRO B 124 ? 0.3543 0.3772 0.2944 0.0254  -0.1025 0.0656  124 PRO B C   
1887 O O   . PRO B 124 ? 0.3692 0.3738 0.2941 0.0289  -0.1125 0.0638  124 PRO B O   
1888 C CB  . PRO B 124 ? 0.3432 0.3987 0.3012 0.0418  -0.0986 0.0335  124 PRO B CB  
1889 C CG  . PRO B 124 ? 0.3419 0.4091 0.3033 0.0461  -0.0928 0.0306  124 PRO B CG  
1890 C CD  . PRO B 124 ? 0.3421 0.4074 0.2995 0.0413  -0.0871 0.0508  124 PRO B CD  
1891 N N   . ILE B 125 ? 0.3650 0.3954 0.3199 0.0141  -0.0931 0.0749  125 ILE B N   
1892 C CA  . ILE B 125 ? 0.3618 0.3811 0.3182 0.0023  -0.0932 0.0851  125 ILE B CA  
1893 C C   . ILE B 125 ? 0.4237 0.4231 0.3531 -0.0048 -0.1016 0.1025  125 ILE B C   
1894 O O   . ILE B 125 ? 0.4361 0.4099 0.3489 -0.0063 -0.1114 0.1038  125 ILE B O   
1895 C CB  . ILE B 125 ? 0.3450 0.3772 0.3181 -0.0059 -0.0823 0.0927  125 ILE B CB  
1896 C CG1 . ILE B 125 ? 0.3972 0.4364 0.3865 -0.0021 -0.0758 0.0769  125 ILE B CG1 
1897 C CG2 . ILE B 125 ? 0.3421 0.3641 0.3164 -0.0182 -0.0830 0.1036  125 ILE B CG2 
1898 C CD1 . ILE B 125 ? 0.3262 0.3679 0.3234 -0.0063 -0.0672 0.0831  125 ILE B CD1 
1899 N N   . ILE B 126 ? 0.4028 0.4131 0.3233 -0.0097 -0.0986 0.1156  126 ILE B N   
1900 C CA  . ILE B 126 ? 0.4876 0.4806 0.3779 -0.0240 -0.1060 0.1347  126 ILE B CA  
1901 C C   . ILE B 126 ? 0.4578 0.4129 0.3140 -0.0159 -0.1208 0.1303  126 ILE B C   
1902 O O   . ILE B 126 ? 0.4648 0.3822 0.2898 -0.0247 -0.1324 0.1393  126 ILE B O   
1903 C CB  . ILE B 126 ? 0.4581 0.4818 0.3458 -0.0316 -0.0992 0.1483  126 ILE B CB  
1904 C CG1 . ILE B 126 ? 0.3957 0.4568 0.3106 -0.0350 -0.0866 0.1524  126 ILE B CG1 
1905 C CG2 . ILE B 126 ? 0.4366 0.4418 0.2869 -0.0530 -0.1077 0.1690  126 ILE B CG2 
1906 C CD1 . ILE B 126 ? 0.3692 0.4736 0.2850 -0.0348 -0.0792 0.1612  126 ILE B CD1 
1907 N N   . GLU B 127 ? 0.4312 0.3933 0.2893 0.0025  -0.1218 0.1156  127 GLU B N   
1908 C CA  . GLU B 127 ? 0.4667 0.3956 0.2909 0.0163  -0.1366 0.1086  127 GLU B CA  
1909 C C   . GLU B 127 ? 0.5290 0.4332 0.3453 0.0252  -0.1467 0.0981  127 GLU B C   
1910 O O   . GLU B 127 ? 0.5209 0.3796 0.2941 0.0277  -0.1623 0.1030  127 GLU B O   
1911 C CB  . GLU B 127 ? 0.5636 0.5133 0.3976 0.0364  -0.1349 0.0913  127 GLU B CB  
1912 C CG  . GLU B 127 ? 0.5906 0.5614 0.4251 0.0316  -0.1275 0.1011  127 GLU B CG  
1913 C CD  . GLU B 127 ? 0.5951 0.5892 0.4438 0.0509  -0.1245 0.0827  127 GLU B CD  
1914 O OE1 . GLU B 127 ? 0.7296 0.7341 0.5690 0.0527  -0.1225 0.0885  127 GLU B OE1 
1915 O OE2 . GLU B 127 ? 0.4791 0.4848 0.3479 0.0624  -0.1240 0.0626  127 GLU B OE2 
1916 N N   . THR B 128 ? 0.4398 0.3710 0.2925 0.0287  -0.1387 0.0847  128 THR B N   
1917 C CA  . THR B 128 ? 0.4724 0.3915 0.3207 0.0391  -0.1475 0.0726  128 THR B CA  
1918 C C   . THR B 128 ? 0.4687 0.3511 0.2939 0.0257  -0.1547 0.0885  128 THR B C   
1919 O O   . THR B 128 ? 0.5132 0.3563 0.3008 0.0372  -0.1713 0.0857  128 THR B O   
1920 C CB  . THR B 128 ? 0.4728 0.4318 0.3638 0.0394  -0.1364 0.0570  128 THR B CB  
1921 O OG1 . THR B 128 ? 0.3907 0.3807 0.2971 0.0509  -0.1326 0.0393  128 THR B OG1 
1922 C CG2 . THR B 128 ? 0.4110 0.3641 0.2965 0.0490  -0.1452 0.0462  128 THR B CG2 
1923 N N   . LEU B 129 ? 0.4496 0.3429 0.2925 0.0029  -0.1438 0.1047  129 LEU B N   
1924 C CA  . LEU B 129 ? 0.5432 0.4071 0.3669 -0.0145 -0.1495 0.1209  129 LEU B CA  
1925 C C   . LEU B 129 ? 0.5457 0.3723 0.3285 -0.0248 -0.1547 0.1305  129 LEU B C   
1926 O O   . LEU B 129 ? 0.5406 0.3411 0.3079 -0.0370 -0.1562 0.1339  129 LEU B O   
1927 C CB  . LEU B 129 ? 0.4340 0.3302 0.2907 -0.0342 -0.1340 0.1326  129 LEU B CB  
1928 C CG  . LEU B 129 ? 0.3925 0.3188 0.2900 -0.0268 -0.1232 0.1180  129 LEU B CG  
1929 C CD1 . LEU B 129 ? 0.3674 0.3167 0.2884 -0.0431 -0.1105 0.1301  129 LEU B CD1 
1930 C CD2 . LEU B 129 ? 0.4003 0.3090 0.2914 -0.0164 -0.1327 0.1060  129 LEU B CD2 
1931 N N   . MET B 130 ? 0.5317 0.3591 0.3002 -0.0214 -0.1554 0.1325  130 MET B N   
1932 C CA  . MET B 130 ? 0.6985 0.4942 0.4308 -0.0329 -0.1585 0.1396  130 MET B CA  
1933 C C   . MET B 130 ? 0.7971 0.5442 0.4921 -0.0139 -0.1728 0.1260  130 MET B C   
1934 O O   . MET B 130 ? 0.8630 0.5687 0.5240 -0.0260 -0.1790 0.1299  130 MET B O   
1935 C CB  . MET B 130 ? 0.6119 0.4291 0.3420 -0.0363 -0.1536 0.1474  130 MET B CB  
1936 C CG  . MET B 130 ? 0.5824 0.4385 0.3327 -0.0619 -0.1404 0.1637  130 MET B CG  
1937 S SD  . MET B 130 ? 0.7624 0.6471 0.5057 -0.0680 -0.1347 0.1735  130 MET B SD  
1938 C CE  . MET B 130 ? 0.5599 0.4802 0.3162 -0.1029 -0.1232 0.1896  130 MET B CE  
1939 N N   . LYS B 131 ? 0.7852 0.5401 0.4860 0.0159  -0.1789 0.1083  131 LYS B N   
1940 C CA  . LYS B 131 ? 0.8630 0.5817 0.5309 0.0408  -0.1919 0.0912  131 LYS B CA  
1941 C C   . LYS B 131 ? 0.9068 0.6004 0.5655 0.0442  -0.1979 0.0842  131 LYS B C   
1942 O O   . LYS B 131 ? 0.9971 0.6698 0.6346 0.0699  -0.2082 0.0663  131 LYS B O   
1943 C CB  . LYS B 131 ? 0.6790 0.4297 0.3621 0.0720  -0.1946 0.0712  131 LYS B CB  
# 
