data_7ZW8
# 
_entry.id   7ZW8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.385 
_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   7ZW8         pdb_00007zw8 10.2210/pdb7zw8/pdb 
WWPDB D_1292123060 ?            ?                   
# 
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 2023-02-22 
2 'Structure model' 1 1 2023-03-08 
3 'Structure model' 1 2 2024-02-07 
# 
_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' 'Refinement description' 
# 
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 2 'Structure model' citation                      
2 2 'Structure model' citation_author               
3 3 'Structure model' chem_comp_atom                
4 3 'Structure model' chem_comp_bond                
5 3 'Structure model' pdbx_initial_refinement_model 
# 
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 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7ZW8 
_pdbx_database_status.recvd_initial_deposition_date   2022-05-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ulrich.graedler@merckgroup.com 
_pdbx_contact_author.name_first         Ulrich 
_pdbx_contact_author.name_last          Graedler 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1869-6945 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Graedler, U.' 1 0000-0002-1869-6945 
'Lammens, A.'  2 0000-0002-4837-4277 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            66 
_citation.language                  ? 
_citation.page_first                2386 
_citation.page_last                 2395 
_citation.title                     
;Identification of M4205&#9472;A Highly Selective Inhibitor of KIT Mutations for Treatment of Unresectable Metastatic or Recurrent Gastrointestinal Stromal Tumors.
;
_citation.year                      2023 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.2c00851 
_citation.pdbx_database_id_PubMed   36728508 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Blum, A.'          1  ? 
primary 'Dorsch, D.'        2  ? 
primary 'Linde, N.'         3  ? 
primary 'Brandstetter, S.'  4  ? 
primary 'Buchstaller, H.P.' 5  ? 
primary 'Busch, M.'         6  ? 
primary 'Glaser, N.'        7  ? 
primary 'Gradler, U.'       8  ? 
primary 'Ruff, A.'          9  ? 
primary 'Petersson, C.'     10 ? 
primary 'Schieferstein, H.' 11 ? 
primary 'Sherbetjian, E.'   12 ? 
primary 'Esdar, C.'         13 ? 
# 
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 'Mast/stem cell growth factor receptor Kit' 37177.957 1  2.7.10.1 ? 'KINASE DOMAIN' ? 
2 non-polymer syn 
'~{N}-[[4-(1-methylpyrazol-4-yl)phenyl]methyl]-6-[7-(3-pyrrolidin-1-ylpropoxy)imidazo[1,2-a]pyridin-3-yl]pyrimidin-4-amine' 
508.617   1  ?        ? ?               ? 
3 water       nat water 18.015    40 ?        ? ?               ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;SCFR,Piebald trait protein,PBT,Proto-oncogene c-Kit,Tyrosine-protein kinase Kit,p145 c-kit,v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog
;
# 
_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       
;PMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAH
LTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKTEPAIMEDDELALDLED
LLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTF
ESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQI
SESTNHI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAH
LTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKTEPAIMEDDELALDLED
LLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTF
ESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQI
SESTNHI
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '~{N}-[[4-(1-methylpyrazol-4-yl)phenyl]methyl]-6-[7-(3-pyrrolidin-1-ylpropoxy)imidazo[1,2-a]pyridin-3-yl]pyrimidin-4-amine' K3R 
3 water                                                                                                                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   MET n 
1 3   TYR n 
1 4   GLU n 
1 5   VAL n 
1 6   GLN n 
1 7   TRP n 
1 8   LYS n 
1 9   VAL n 
1 10  VAL n 
1 11  GLU n 
1 12  GLU n 
1 13  ILE n 
1 14  ASN n 
1 15  GLY n 
1 16  ASN n 
1 17  ASN n 
1 18  TYR n 
1 19  VAL n 
1 20  TYR n 
1 21  ILE n 
1 22  ASP n 
1 23  PRO n 
1 24  THR n 
1 25  GLN n 
1 26  LEU n 
1 27  PRO n 
1 28  TYR n 
1 29  ASP n 
1 30  HIS n 
1 31  LYS n 
1 32  TRP n 
1 33  GLU n 
1 34  PHE n 
1 35  PRO n 
1 36  ARG n 
1 37  ASN n 
1 38  ARG n 
1 39  LEU n 
1 40  SER n 
1 41  PHE n 
1 42  GLY n 
1 43  LYS n 
1 44  THR n 
1 45  LEU n 
1 46  GLY n 
1 47  ALA n 
1 48  GLY n 
1 49  ALA n 
1 50  PHE n 
1 51  GLY n 
1 52  LYS n 
1 53  VAL n 
1 54  VAL n 
1 55  GLU n 
1 56  ALA n 
1 57  THR n 
1 58  ALA n 
1 59  TYR n 
1 60  GLY n 
1 61  LEU n 
1 62  ILE n 
1 63  LYS n 
1 64  SER n 
1 65  ASP n 
1 66  ALA n 
1 67  ALA n 
1 68  MET n 
1 69  THR n 
1 70  VAL n 
1 71  ALA n 
1 72  VAL n 
1 73  LYS n 
1 74  MET n 
1 75  LEU n 
1 76  LYS n 
1 77  PRO n 
1 78  SER n 
1 79  ALA n 
1 80  HIS n 
1 81  LEU n 
1 82  THR n 
1 83  GLU n 
1 84  ARG n 
1 85  GLU n 
1 86  ALA n 
1 87  LEU n 
1 88  MET n 
1 89  SER n 
1 90  GLU n 
1 91  LEU n 
1 92  LYS n 
1 93  VAL n 
1 94  LEU n 
1 95  SER n 
1 96  TYR n 
1 97  LEU n 
1 98  GLY n 
1 99  ASN n 
1 100 HIS n 
1 101 MET n 
1 102 ASN n 
1 103 ILE n 
1 104 VAL n 
1 105 ASN n 
1 106 LEU n 
1 107 LEU n 
1 108 GLY n 
1 109 ALA n 
1 110 CYS n 
1 111 THR n 
1 112 ILE n 
1 113 GLY n 
1 114 GLY n 
1 115 PRO n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 ILE n 
1 120 THR n 
1 121 GLU n 
1 122 TYR n 
1 123 CYS n 
1 124 CYS n 
1 125 TYR n 
1 126 GLY n 
1 127 ASP n 
1 128 LEU n 
1 129 LEU n 
1 130 ASN n 
1 131 PHE n 
1 132 LEU n 
1 133 ARG n 
1 134 ARG n 
1 135 LYS n 
1 136 ARG n 
1 137 ASP n 
1 138 SER n 
1 139 PHE n 
1 140 ILE n 
1 141 CYS n 
1 142 SER n 
1 143 LYS n 
1 144 THR n 
1 145 GLU n 
1 146 PRO n 
1 147 ALA n 
1 148 ILE n 
1 149 MET n 
1 150 GLU n 
1 151 ASP n 
1 152 ASP n 
1 153 GLU n 
1 154 LEU n 
1 155 ALA n 
1 156 LEU n 
1 157 ASP n 
1 158 LEU n 
1 159 GLU n 
1 160 ASP n 
1 161 LEU n 
1 162 LEU n 
1 163 SER n 
1 164 PHE n 
1 165 SER n 
1 166 TYR n 
1 167 GLN n 
1 168 VAL n 
1 169 ALA n 
1 170 LYS n 
1 171 GLY n 
1 172 MET n 
1 173 ALA n 
1 174 PHE n 
1 175 LEU n 
1 176 ALA n 
1 177 SER n 
1 178 LYS n 
1 179 ASN n 
1 180 CYS n 
1 181 ILE n 
1 182 HIS n 
1 183 ARG n 
1 184 ASP n 
1 185 LEU n 
1 186 ALA n 
1 187 ALA n 
1 188 ARG n 
1 189 ASN n 
1 190 ILE n 
1 191 LEU n 
1 192 LEU n 
1 193 THR n 
1 194 HIS n 
1 195 GLY n 
1 196 ARG n 
1 197 ILE n 
1 198 THR n 
1 199 LYS n 
1 200 ILE n 
1 201 CYS n 
1 202 ASP n 
1 203 PHE n 
1 204 GLY n 
1 205 LEU n 
1 206 ALA n 
1 207 ARG n 
1 208 ASP n 
1 209 ILE n 
1 210 LYS n 
1 211 ASN n 
1 212 ASP n 
1 213 SER n 
1 214 ASN n 
1 215 TYR n 
1 216 VAL n 
1 217 VAL n 
1 218 LYS n 
1 219 GLY n 
1 220 ASN n 
1 221 ALA n 
1 222 ARG n 
1 223 LEU n 
1 224 PRO n 
1 225 VAL n 
1 226 LYS n 
1 227 TRP n 
1 228 MET n 
1 229 ALA n 
1 230 PRO n 
1 231 GLU n 
1 232 SER n 
1 233 ILE n 
1 234 PHE n 
1 235 ASN n 
1 236 CYS n 
1 237 VAL n 
1 238 TYR n 
1 239 THR n 
1 240 PHE n 
1 241 GLU n 
1 242 SER n 
1 243 ASP n 
1 244 VAL n 
1 245 TRP n 
1 246 SER n 
1 247 TYR n 
1 248 GLY n 
1 249 ILE n 
1 250 PHE n 
1 251 LEU n 
1 252 TRP n 
1 253 GLU n 
1 254 LEU n 
1 255 PHE n 
1 256 SER n 
1 257 LEU n 
1 258 GLY n 
1 259 SER n 
1 260 SER n 
1 261 PRO n 
1 262 TYR n 
1 263 PRO n 
1 264 GLY n 
1 265 MET n 
1 266 PRO n 
1 267 VAL n 
1 268 ASP n 
1 269 SER n 
1 270 LYS n 
1 271 PHE n 
1 272 TYR n 
1 273 LYS n 
1 274 MET n 
1 275 ILE n 
1 276 LYS n 
1 277 GLU n 
1 278 GLY n 
1 279 PHE n 
1 280 ARG n 
1 281 MET n 
1 282 LEU n 
1 283 SER n 
1 284 PRO n 
1 285 GLU n 
1 286 HIS n 
1 287 ALA n 
1 288 PRO n 
1 289 ALA n 
1 290 GLU n 
1 291 MET n 
1 292 TYR n 
1 293 ASP n 
1 294 ILE n 
1 295 MET n 
1 296 LYS n 
1 297 THR n 
1 298 CYS n 
1 299 TRP n 
1 300 ASP n 
1 301 ALA n 
1 302 ASP n 
1 303 PRO n 
1 304 LEU n 
1 305 LYS n 
1 306 ARG n 
1 307 PRO n 
1 308 THR n 
1 309 PHE n 
1 310 LYS n 
1 311 GLN n 
1 312 ILE n 
1 313 VAL n 
1 314 GLN n 
1 315 LEU n 
1 316 ILE n 
1 317 GLU n 
1 318 LYS n 
1 319 GLN n 
1 320 ILE n 
1 321 SER n 
1 322 GLU n 
1 323 SER n 
1 324 THR n 
1 325 ASN n 
1 326 HIS n 
1 327 ILE 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                   327 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'KIT, SCFR' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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               ? 
_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                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_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  
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 
K3R non-polymer         . 
'~{N}-[[4-(1-methylpyrazol-4-yl)phenyl]methyl]-6-[7-(3-pyrrolidin-1-ylpropoxy)imidazo[1,2-a]pyridin-3-yl]pyrimidin-4-amine' 
'[4-(1-Methyl-1H-pyrazol-4-yl)-benzyl]-{6-[7-(3-pyrrolidin-1-yl-propoxy)-imidazo[1,2-a]pyridin-3-yl]-pyrimidin-4-yl}-amine' 
'C29 H32 N8 O'   508.617 
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 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   PRO 1   551 ?   ?   ?   A . n 
A 1 2   MET 2   552 ?   ?   ?   A . n 
A 1 3   TYR 3   553 ?   ?   ?   A . n 
A 1 4   GLU 4   554 554 GLU GLU A . n 
A 1 5   VAL 5   555 555 VAL VAL A . n 
A 1 6   GLN 6   556 556 GLN GLN A . n 
A 1 7   TRP 7   557 557 TRP TRP A . n 
A 1 8   LYS 8   558 558 LYS LYS A . n 
A 1 9   VAL 9   559 559 VAL VAL A . n 
A 1 10  VAL 10  560 560 VAL VAL A . n 
A 1 11  GLU 11  561 561 GLU GLU A . n 
A 1 12  GLU 12  562 562 GLU GLU A . n 
A 1 13  ILE 13  563 ?   ?   ?   A . n 
A 1 14  ASN 14  564 ?   ?   ?   A . n 
A 1 15  GLY 15  565 ?   ?   ?   A . n 
A 1 16  ASN 16  566 ?   ?   ?   A . n 
A 1 17  ASN 17  567 ?   ?   ?   A . n 
A 1 18  TYR 18  568 ?   ?   ?   A . n 
A 1 19  VAL 19  569 569 VAL VAL A . n 
A 1 20  TYR 20  570 570 TYR TYR A . n 
A 1 21  ILE 21  571 571 ILE ILE A . n 
A 1 22  ASP 22  572 572 ASP ASP A . n 
A 1 23  PRO 23  573 573 PRO PRO A . n 
A 1 24  THR 24  574 574 THR THR A . n 
A 1 25  GLN 25  575 575 GLN GLN A . n 
A 1 26  LEU 26  576 576 LEU LEU A . n 
A 1 27  PRO 27  577 577 PRO PRO A . n 
A 1 28  TYR 28  578 578 TYR TYR A . n 
A 1 29  ASP 29  579 579 ASP ASP A . n 
A 1 30  HIS 30  580 580 HIS HIS A . n 
A 1 31  LYS 31  581 581 LYS LYS A . n 
A 1 32  TRP 32  582 582 TRP TRP A . n 
A 1 33  GLU 33  583 583 GLU GLU A . n 
A 1 34  PHE 34  584 584 PHE PHE A . n 
A 1 35  PRO 35  585 585 PRO PRO A . n 
A 1 36  ARG 36  586 586 ARG ARG A . n 
A 1 37  ASN 37  587 587 ASN ASN A . n 
A 1 38  ARG 38  588 588 ARG ARG A . n 
A 1 39  LEU 39  589 589 LEU LEU A . n 
A 1 40  SER 40  590 590 SER SER A . n 
A 1 41  PHE 41  591 591 PHE PHE A . n 
A 1 42  GLY 42  592 592 GLY GLY A . n 
A 1 43  LYS 43  593 593 LYS LYS A . n 
A 1 44  THR 44  594 594 THR THR A . n 
A 1 45  LEU 45  595 595 LEU LEU A . n 
A 1 46  GLY 46  596 596 GLY GLY A . n 
A 1 47  ALA 47  597 597 ALA ALA A . n 
A 1 48  GLY 48  598 598 GLY GLY A . n 
A 1 49  ALA 49  599 599 ALA ALA A . n 
A 1 50  PHE 50  600 600 PHE PHE A . n 
A 1 51  GLY 51  601 601 GLY GLY A . n 
A 1 52  LYS 52  602 602 LYS LYS A . n 
A 1 53  VAL 53  603 603 VAL VAL A . n 
A 1 54  VAL 54  604 604 VAL VAL A . n 
A 1 55  GLU 55  605 605 GLU GLU A . n 
A 1 56  ALA 56  606 606 ALA ALA A . n 
A 1 57  THR 57  607 607 THR THR A . n 
A 1 58  ALA 58  608 608 ALA ALA A . n 
A 1 59  TYR 59  609 609 TYR TYR A . n 
A 1 60  GLY 60  610 610 GLY GLY A . n 
A 1 61  LEU 61  611 611 LEU LEU A . n 
A 1 62  ILE 62  612 612 ILE ILE A . n 
A 1 63  LYS 63  613 613 LYS LYS A . n 
A 1 64  SER 64  614 614 SER SER A . n 
A 1 65  ASP 65  615 615 ASP ASP A . n 
A 1 66  ALA 66  616 616 ALA ALA A . n 
A 1 67  ALA 67  617 617 ALA ALA A . n 
A 1 68  MET 68  618 618 MET MET A . n 
A 1 69  THR 69  619 619 THR THR A . n 
A 1 70  VAL 70  620 620 VAL VAL A . n 
A 1 71  ALA 71  621 621 ALA ALA A . n 
A 1 72  VAL 72  622 622 VAL VAL A . n 
A 1 73  LYS 73  623 623 LYS LYS A . n 
A 1 74  MET 74  624 624 MET MET A . n 
A 1 75  LEU 75  625 625 LEU LEU A . n 
A 1 76  LYS 76  626 626 LYS LYS A . n 
A 1 77  PRO 77  627 627 PRO PRO A . n 
A 1 78  SER 78  628 628 SER SER A . n 
A 1 79  ALA 79  629 629 ALA ALA A . n 
A 1 80  HIS 80  630 630 HIS HIS A . n 
A 1 81  LEU 81  631 631 LEU LEU A . n 
A 1 82  THR 82  632 632 THR THR A . n 
A 1 83  GLU 83  633 633 GLU GLU A . n 
A 1 84  ARG 84  634 634 ARG ARG A . n 
A 1 85  GLU 85  635 635 GLU GLU A . n 
A 1 86  ALA 86  636 636 ALA ALA A . n 
A 1 87  LEU 87  637 637 LEU LEU A . n 
A 1 88  MET 88  638 638 MET MET A . n 
A 1 89  SER 89  639 639 SER SER A . n 
A 1 90  GLU 90  640 640 GLU GLU A . n 
A 1 91  LEU 91  641 641 LEU LEU A . n 
A 1 92  LYS 92  642 642 LYS LYS A . n 
A 1 93  VAL 93  643 643 VAL VAL A . n 
A 1 94  LEU 94  644 644 LEU LEU A . n 
A 1 95  SER 95  645 645 SER SER A . n 
A 1 96  TYR 96  646 646 TYR TYR A . n 
A 1 97  LEU 97  647 647 LEU LEU A . n 
A 1 98  GLY 98  648 648 GLY GLY A . n 
A 1 99  ASN 99  649 649 ASN ASN A . n 
A 1 100 HIS 100 650 650 HIS HIS A . n 
A 1 101 MET 101 651 651 MET MET A . n 
A 1 102 ASN 102 652 652 ASN ASN A . n 
A 1 103 ILE 103 653 653 ILE ILE A . n 
A 1 104 VAL 104 654 654 VAL VAL A . n 
A 1 105 ASN 105 655 655 ASN ASN A . n 
A 1 106 LEU 106 656 656 LEU LEU A . n 
A 1 107 LEU 107 657 657 LEU LEU A . n 
A 1 108 GLY 108 658 658 GLY GLY A . n 
A 1 109 ALA 109 659 659 ALA ALA A . n 
A 1 110 CYS 110 660 660 CYS CYS A . n 
A 1 111 THR 111 661 661 THR THR A . n 
A 1 112 ILE 112 662 662 ILE ILE A . n 
A 1 113 GLY 113 663 663 GLY GLY A . n 
A 1 114 GLY 114 664 664 GLY GLY A . n 
A 1 115 PRO 115 665 665 PRO PRO A . n 
A 1 116 THR 116 666 666 THR THR A . n 
A 1 117 LEU 117 667 667 LEU LEU A . n 
A 1 118 VAL 118 668 668 VAL VAL A . n 
A 1 119 ILE 119 669 669 ILE ILE A . n 
A 1 120 THR 120 670 670 THR THR A . n 
A 1 121 GLU 121 671 671 GLU GLU A . n 
A 1 122 TYR 122 672 672 TYR TYR A . n 
A 1 123 CYS 123 673 673 CYS CYS A . n 
A 1 124 CYS 124 674 674 CYS CYS A . n 
A 1 125 TYR 125 675 675 TYR TYR A . n 
A 1 126 GLY 126 676 676 GLY GLY A . n 
A 1 127 ASP 127 677 677 ASP ASP A . n 
A 1 128 LEU 128 678 678 LEU LEU A . n 
A 1 129 LEU 129 679 679 LEU LEU A . n 
A 1 130 ASN 130 680 680 ASN ASN A . n 
A 1 131 PHE 131 681 681 PHE PHE A . n 
A 1 132 LEU 132 682 682 LEU LEU A . n 
A 1 133 ARG 133 683 683 ARG ARG A . n 
A 1 134 ARG 134 684 684 ARG ARG A . n 
A 1 135 LYS 135 685 685 LYS LYS A . n 
A 1 136 ARG 136 686 686 ARG ARG A . n 
A 1 137 ASP 137 687 687 ASP ASP A . n 
A 1 138 SER 138 746 ?   ?   ?   A . n 
A 1 139 PHE 139 747 ?   ?   ?   A . n 
A 1 140 ILE 140 748 ?   ?   ?   A . n 
A 1 141 CYS 141 749 ?   ?   ?   A . n 
A 1 142 SER 142 750 ?   ?   ?   A . n 
A 1 143 LYS 143 751 ?   ?   ?   A . n 
A 1 144 THR 144 752 ?   ?   ?   A . n 
A 1 145 GLU 145 753 ?   ?   ?   A . n 
A 1 146 PRO 146 754 ?   ?   ?   A . n 
A 1 147 ALA 147 755 ?   ?   ?   A . n 
A 1 148 ILE 148 756 ?   ?   ?   A . n 
A 1 149 MET 149 757 ?   ?   ?   A . n 
A 1 150 GLU 150 758 ?   ?   ?   A . n 
A 1 151 ASP 151 759 ?   ?   ?   A . n 
A 1 152 ASP 152 760 760 ASP ASP A . n 
A 1 153 GLU 153 761 761 GLU GLU A . n 
A 1 154 LEU 154 762 762 LEU LEU A . n 
A 1 155 ALA 155 763 763 ALA ALA A . n 
A 1 156 LEU 156 764 764 LEU LEU A . n 
A 1 157 ASP 157 765 765 ASP ASP A . n 
A 1 158 LEU 158 766 766 LEU LEU A . n 
A 1 159 GLU 159 767 767 GLU GLU A . n 
A 1 160 ASP 160 768 768 ASP ASP A . n 
A 1 161 LEU 161 769 769 LEU LEU A . n 
A 1 162 LEU 162 770 770 LEU LEU A . n 
A 1 163 SER 163 771 771 SER SER A . n 
A 1 164 PHE 164 772 772 PHE PHE A . n 
A 1 165 SER 165 773 773 SER SER A . n 
A 1 166 TYR 166 774 774 TYR TYR A . n 
A 1 167 GLN 167 775 775 GLN GLN A . n 
A 1 168 VAL 168 776 776 VAL VAL A . n 
A 1 169 ALA 169 777 777 ALA ALA A . n 
A 1 170 LYS 170 778 778 LYS LYS A . n 
A 1 171 GLY 171 779 779 GLY GLY A . n 
A 1 172 MET 172 780 780 MET MET A . n 
A 1 173 ALA 173 781 781 ALA ALA A . n 
A 1 174 PHE 174 782 782 PHE PHE A . n 
A 1 175 LEU 175 783 783 LEU LEU A . n 
A 1 176 ALA 176 784 784 ALA ALA A . n 
A 1 177 SER 177 785 785 SER SER A . n 
A 1 178 LYS 178 786 786 LYS LYS A . n 
A 1 179 ASN 179 787 787 ASN ASN A . n 
A 1 180 CYS 180 788 788 CYS CYS A . n 
A 1 181 ILE 181 789 789 ILE ILE A . n 
A 1 182 HIS 182 790 790 HIS HIS A . n 
A 1 183 ARG 183 791 791 ARG ARG A . n 
A 1 184 ASP 184 792 792 ASP ASP A . n 
A 1 185 LEU 185 793 793 LEU LEU A . n 
A 1 186 ALA 186 794 794 ALA ALA A . n 
A 1 187 ALA 187 795 795 ALA ALA A . n 
A 1 188 ARG 188 796 796 ARG ARG A . n 
A 1 189 ASN 189 797 797 ASN ASN A . n 
A 1 190 ILE 190 798 798 ILE ILE A . n 
A 1 191 LEU 191 799 799 LEU LEU A . n 
A 1 192 LEU 192 800 800 LEU LEU A . n 
A 1 193 THR 193 801 801 THR THR A . n 
A 1 194 HIS 194 802 802 HIS HIS A . n 
A 1 195 GLY 195 803 803 GLY GLY A . n 
A 1 196 ARG 196 804 804 ARG ARG A . n 
A 1 197 ILE 197 805 805 ILE ILE A . n 
A 1 198 THR 198 806 806 THR THR A . n 
A 1 199 LYS 199 807 807 LYS LYS A . n 
A 1 200 ILE 200 808 808 ILE ILE A . n 
A 1 201 CYS 201 809 809 CYS CYS A . n 
A 1 202 ASP 202 810 810 ASP ASP A . n 
A 1 203 PHE 203 811 811 PHE PHE A . n 
A 1 204 GLY 204 812 812 GLY GLY A . n 
A 1 205 LEU 205 813 813 LEU LEU A . n 
A 1 206 ALA 206 814 814 ALA ALA A . n 
A 1 207 ARG 207 815 815 ARG ARG A . n 
A 1 208 ASP 208 816 816 ASP ASP A . n 
A 1 209 ILE 209 817 817 ILE ILE A . n 
A 1 210 LYS 210 818 818 LYS LYS A . n 
A 1 211 ASN 211 819 819 ASN ASN A . n 
A 1 212 ASP 212 820 820 ASP ASP A . n 
A 1 213 SER 213 821 821 SER SER A . n 
A 1 214 ASN 214 822 822 ASN ASN A . n 
A 1 215 TYR 215 823 823 TYR TYR A . n 
A 1 216 VAL 216 824 824 VAL VAL A . n 
A 1 217 VAL 217 825 825 VAL VAL A . n 
A 1 218 LYS 218 826 826 LYS LYS A . n 
A 1 219 GLY 219 827 827 GLY GLY A . n 
A 1 220 ASN 220 828 828 ASN ASN A . n 
A 1 221 ALA 221 829 829 ALA ALA A . n 
A 1 222 ARG 222 830 830 ARG ARG A . n 
A 1 223 LEU 223 831 831 LEU LEU A . n 
A 1 224 PRO 224 832 832 PRO PRO A . n 
A 1 225 VAL 225 833 833 VAL VAL A . n 
A 1 226 LYS 226 834 834 LYS LYS A . n 
A 1 227 TRP 227 835 835 TRP TRP A . n 
A 1 228 MET 228 836 836 MET MET A . n 
A 1 229 ALA 229 837 837 ALA ALA A . n 
A 1 230 PRO 230 838 838 PRO PRO A . n 
A 1 231 GLU 231 839 839 GLU GLU A . n 
A 1 232 SER 232 840 840 SER SER A . n 
A 1 233 ILE 233 841 841 ILE ILE A . n 
A 1 234 PHE 234 842 842 PHE PHE A . n 
A 1 235 ASN 235 843 843 ASN ASN A . n 
A 1 236 CYS 236 844 844 CYS CYS A . n 
A 1 237 VAL 237 845 845 VAL VAL A . n 
A 1 238 TYR 238 846 846 TYR TYR A . n 
A 1 239 THR 239 847 847 THR THR A . n 
A 1 240 PHE 240 848 848 PHE PHE A . n 
A 1 241 GLU 241 849 849 GLU GLU A . n 
A 1 242 SER 242 850 850 SER SER A . n 
A 1 243 ASP 243 851 851 ASP ASP A . n 
A 1 244 VAL 244 852 852 VAL VAL A . n 
A 1 245 TRP 245 853 853 TRP TRP A . n 
A 1 246 SER 246 854 854 SER SER A . n 
A 1 247 TYR 247 855 855 TYR TYR A . n 
A 1 248 GLY 248 856 856 GLY GLY A . n 
A 1 249 ILE 249 857 857 ILE ILE A . n 
A 1 250 PHE 250 858 858 PHE PHE A . n 
A 1 251 LEU 251 859 859 LEU LEU A . n 
A 1 252 TRP 252 860 860 TRP TRP A . n 
A 1 253 GLU 253 861 861 GLU GLU A . n 
A 1 254 LEU 254 862 862 LEU LEU A . n 
A 1 255 PHE 255 863 863 PHE PHE A . n 
A 1 256 SER 256 864 864 SER SER A . n 
A 1 257 LEU 257 865 865 LEU LEU A . n 
A 1 258 GLY 258 866 866 GLY GLY A . n 
A 1 259 SER 259 867 867 SER SER A . n 
A 1 260 SER 260 868 868 SER SER A . n 
A 1 261 PRO 261 869 869 PRO PRO A . n 
A 1 262 TYR 262 870 870 TYR TYR A . n 
A 1 263 PRO 263 871 871 PRO PRO A . n 
A 1 264 GLY 264 872 872 GLY GLY A . n 
A 1 265 MET 265 873 873 MET MET A . n 
A 1 266 PRO 266 874 874 PRO PRO A . n 
A 1 267 VAL 267 875 875 VAL VAL A . n 
A 1 268 ASP 268 876 876 ASP ASP A . n 
A 1 269 SER 269 877 877 SER SER A . n 
A 1 270 LYS 270 878 878 LYS LYS A . n 
A 1 271 PHE 271 879 879 PHE PHE A . n 
A 1 272 TYR 272 880 880 TYR TYR A . n 
A 1 273 LYS 273 881 881 LYS LYS A . n 
A 1 274 MET 274 882 882 MET MET A . n 
A 1 275 ILE 275 883 883 ILE ILE A . n 
A 1 276 LYS 276 884 884 LYS LYS A . n 
A 1 277 GLU 277 885 885 GLU GLU A . n 
A 1 278 GLY 278 886 886 GLY GLY A . n 
A 1 279 PHE 279 887 887 PHE PHE A . n 
A 1 280 ARG 280 888 888 ARG ARG A . n 
A 1 281 MET 281 889 889 MET MET A . n 
A 1 282 LEU 282 890 890 LEU LEU A . n 
A 1 283 SER 283 891 891 SER SER A . n 
A 1 284 PRO 284 892 892 PRO PRO A . n 
A 1 285 GLU 285 893 893 GLU GLU A . n 
A 1 286 HIS 286 894 894 HIS HIS A . n 
A 1 287 ALA 287 895 895 ALA ALA A . n 
A 1 288 PRO 288 896 896 PRO PRO A . n 
A 1 289 ALA 289 897 897 ALA ALA A . n 
A 1 290 GLU 290 898 898 GLU GLU A . n 
A 1 291 MET 291 899 899 MET MET A . n 
A 1 292 TYR 292 900 900 TYR TYR A . n 
A 1 293 ASP 293 901 901 ASP ASP A . n 
A 1 294 ILE 294 902 902 ILE ILE A . n 
A 1 295 MET 295 903 903 MET MET A . n 
A 1 296 LYS 296 904 904 LYS LYS A . n 
A 1 297 THR 297 905 905 THR THR A . n 
A 1 298 CYS 298 906 906 CYS CYS A . n 
A 1 299 TRP 299 907 907 TRP TRP A . n 
A 1 300 ASP 300 908 908 ASP ASP A . n 
A 1 301 ALA 301 909 909 ALA ALA A . n 
A 1 302 ASP 302 910 910 ASP ASP A . n 
A 1 303 PRO 303 911 911 PRO PRO A . n 
A 1 304 LEU 304 912 912 LEU LEU A . n 
A 1 305 LYS 305 913 913 LYS LYS A . n 
A 1 306 ARG 306 914 914 ARG ARG A . n 
A 1 307 PRO 307 915 915 PRO PRO A . n 
A 1 308 THR 308 916 916 THR THR A . n 
A 1 309 PHE 309 917 917 PHE PHE A . n 
A 1 310 LYS 310 918 918 LYS LYS A . n 
A 1 311 GLN 311 919 919 GLN GLN A . n 
A 1 312 ILE 312 920 920 ILE ILE A . n 
A 1 313 VAL 313 921 921 VAL VAL A . n 
A 1 314 GLN 314 922 922 GLN GLN A . n 
A 1 315 LEU 315 923 923 LEU LEU A . n 
A 1 316 ILE 316 924 924 ILE ILE A . n 
A 1 317 GLU 317 925 925 GLU GLU A . n 
A 1 318 LYS 318 926 926 LYS LYS A . n 
A 1 319 GLN 319 927 927 GLN GLN A . n 
A 1 320 ILE 320 928 928 ILE ILE A . n 
A 1 321 SER 321 929 929 SER SER A . n 
A 1 322 GLU 322 930 930 GLU GLU A . n 
A 1 323 SER 323 931 931 SER SER A . n 
A 1 324 THR 324 932 932 THR THR A . n 
A 1 325 ASN 325 933 ?   ?   ?   A . n 
A 1 326 HIS 326 934 ?   ?   ?   A . n 
A 1 327 ILE 327 935 ?   ?   ?   A . 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 
B 2 K3R 1  1001 1  K3R INX A . 
C 3 HOH 1  1101 6  HOH HOH A . 
C 3 HOH 2  1102 3  HOH HOH A . 
C 3 HOH 3  1103 16 HOH HOH A . 
C 3 HOH 4  1104 39 HOH HOH A . 
C 3 HOH 5  1105 43 HOH HOH A . 
C 3 HOH 6  1106 35 HOH HOH A . 
C 3 HOH 7  1107 41 HOH HOH A . 
C 3 HOH 8  1108 40 HOH HOH A . 
C 3 HOH 9  1109 53 HOH HOH A . 
C 3 HOH 10 1110 11 HOH HOH A . 
C 3 HOH 11 1111 7  HOH HOH A . 
C 3 HOH 12 1112 51 HOH HOH A . 
C 3 HOH 13 1113 5  HOH HOH A . 
C 3 HOH 14 1114 29 HOH HOH A . 
C 3 HOH 15 1115 8  HOH HOH A . 
C 3 HOH 16 1116 10 HOH HOH A . 
C 3 HOH 17 1117 20 HOH HOH A . 
C 3 HOH 18 1118 52 HOH HOH A . 
C 3 HOH 19 1119 17 HOH HOH A . 
C 3 HOH 20 1120 49 HOH HOH A . 
C 3 HOH 21 1121 27 HOH HOH A . 
C 3 HOH 22 1122 45 HOH HOH A . 
C 3 HOH 23 1123 46 HOH HOH A . 
C 3 HOH 24 1124 60 HOH HOH A . 
C 3 HOH 25 1125 62 HOH HOH A . 
C 3 HOH 26 1126 54 HOH HOH A . 
C 3 HOH 27 1127 42 HOH HOH A . 
C 3 HOH 28 1128 36 HOH HOH A . 
C 3 HOH 29 1129 23 HOH HOH A . 
C 3 HOH 30 1130 28 HOH HOH A . 
C 3 HOH 31 1131 15 HOH HOH A . 
C 3 HOH 32 1132 48 HOH HOH A . 
C 3 HOH 33 1133 65 HOH HOH A . 
C 3 HOH 34 1134 32 HOH HOH A . 
C 3 HOH 35 1135 61 HOH HOH A . 
C 3 HOH 36 1136 24 HOH HOH A . 
C 3 HOH 37 1137 50 HOH HOH A . 
C 3 HOH 38 1138 63 HOH HOH A . 
C 3 HOH 39 1139 4  HOH HOH A . 
C 3 HOH 40 1140 37 HOH HOH A . 
# 
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        ? ? ? ? ? ? ? ? ? ? ? BUSTER      ? ? ? '2.11.8 (3-FEB-2022)'  1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? 'VERSION Jan 31, 2020' 2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? STARANISO   ? ? ? .                      3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .                      4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27                   5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7ZW8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.056 
_cell.length_a_esd                 ? 
_cell.length_b                     81.307 
_cell.length_b_esd                 ? 
_cell.length_c                     96.049 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         7ZW8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   7ZW8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.480 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.480 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.25 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '9% (w/v) PEG 8K,  0.1 M HEPES' 
_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.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-09-03 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_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             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000067 
_diffrn_radiation_wavelength.wt           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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000067 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          66.280 
_reflns.entry_id                                       7ZW8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.119 
_reflns.d_resolution_low                               48.025 
_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                                     13325 
_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                           92.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.700 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.046 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.3 
_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                                0.049 
_reflns.pdbx_Rpim_I_all                                0.018 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
_reflns.pdbx_CC_split_method                           ? 
# 
_reflns_shell.d_res_high                                    2.119 
_reflns_shell.d_res_low                                     2.41 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             666 
_reflns_shell.percent_possible_all                          62.5 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.400 
_reflns_shell.pdbx_Rsym_value                               0.879 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.996 
_reflns_shell.pdbx_Rpim_I_all                               0.458 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.804 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.5252 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            -1.8052 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            2.3304 
_refine.B_iso_max                                140.220 
_refine.B_iso_mean                               76.5600 
_refine.B_iso_min                                44.210 
_refine.correlation_coeff_Fo_to_Fc               0.9460 
_refine.correlation_coeff_Fo_to_Fc_free          0.9350 
_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                                 7ZW8 
_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                            2.1190 
_refine.ls_d_res_low                             48.0200 
_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                     13325 
_refine.ls_number_reflns_R_free                  988 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    62.9000 
_refine.ls_percent_reflns_R_free                 7.4100 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2118 
_refine.ls_R_factor_R_free                       0.2498 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2087 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_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                          0.000 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      3g0e 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.2660 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2640 
_refine.pdbx_overall_SU_R_Blow_DPI               0.4490 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.4400 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        7ZW8 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.320 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.1190 
_refine_hist.d_res_low                        48.0200 
_refine_hist.number_atoms_solvent             40 
_refine_hist.number_atoms_total               2477 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       301 
_refine_hist.pdbx_B_iso_mean_ligand           56.95 
_refine_hist.pdbx_B_iso_mean_solvent          65.22 
_refine_hist.pdbx_number_atoms_protein        2399 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? ?      ? 870  ? t_dihedral_angle_d        2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_trig_c_planes           ?      ?            
'X-RAY DIFFRACTION' ? ?      ? 410  ? t_gen_planes              5.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?      ? 2505 ? t_it                      10.000 HARMONIC     
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_nbd                     ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_improper_torsion        ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_pseud_angle             ?      ?            
'X-RAY DIFFRACTION' ? ?      ? 315  ? t_chiral_improper_torsion 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_sum_occupancies         ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_utility_distance        ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_utility_angle           ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_utility_torsion         ?      ?            
'X-RAY DIFFRACTION' ? ?      ? 1911 ? t_ideal_dist_contact      4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 0.009  ? 2505 ? t_bond_d                  2.000  HARMONIC     
'X-RAY DIFFRACTION' ? 0.950  ? 3389 ? t_angle_deg               2.000  HARMONIC     
'X-RAY DIFFRACTION' ? 3.080  ? ?    ? t_omega_torsion           ?      ?            
'X-RAY DIFFRACTION' ? 17.430 ? ?    ? t_other_torsion           ?      ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.1200 
_refine_ls_shell.d_res_low                        2.3000 
_refine_ls_shell.number_reflns_all                272 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             16 
_refine_ls_shell.number_reflns_R_work             256 
_refine_ls_shell.percent_reflns_obs               5.8600 
_refine_ls_shell.percent_reflns_R_free            5.8800 
_refine_ls_shell.R_factor_all                     0.3425 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.4351 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.3373 
_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_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   50 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     7ZW8 
_struct.title                        
'Identification of M4205 a highly selective inhibitor of cKIT mutations for unresectable metastatic or recurrent GIST' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        7ZW8 
_struct_keywords.text            'TYROSINE-PROTEIN KINASE, cKIT, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    KIT_HUMAN 
_struct_ref.pdbx_db_accession          P10721 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAH
LTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSK
ESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIH
RDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPY
PGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHI
;
_struct_ref.pdbx_align_begin           551 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7ZW8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 327 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P10721 
_struct_ref_seq.db_align_beg                  551 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  935 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       551 
_struct_ref_seq.pdbx_auth_seq_align_end       935 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7ZW8 THR A 144 ? UNP P10721 GLN 694 conflict 752 1  
1 7ZW8 ?   A ?   ? UNP P10721 ASP 696 deletion ?   2  
1 7ZW8 ?   A ?   ? UNP P10721 HIS 697 deletion ?   3  
1 7ZW8 ?   A ?   ? UNP P10721 ALA 698 deletion ?   4  
1 7ZW8 ?   A ?   ? UNP P10721 GLU 699 deletion ?   5  
1 7ZW8 ?   A ?   ? UNP P10721 ALA 700 deletion ?   6  
1 7ZW8 ?   A ?   ? UNP P10721 ALA 701 deletion ?   7  
1 7ZW8 ?   A ?   ? UNP P10721 LEU 702 deletion ?   8  
1 7ZW8 ?   A ?   ? UNP P10721 TYR 703 deletion ?   9  
1 7ZW8 ?   A ?   ? UNP P10721 LYS 704 deletion ?   10 
1 7ZW8 ?   A ?   ? UNP P10721 ASN 705 deletion ?   11 
1 7ZW8 ?   A ?   ? UNP P10721 LEU 706 deletion ?   12 
1 7ZW8 ?   A ?   ? UNP P10721 LEU 707 deletion ?   13 
1 7ZW8 ?   A ?   ? UNP P10721 HIS 708 deletion ?   14 
1 7ZW8 ?   A ?   ? UNP P10721 SER 709 deletion ?   15 
1 7ZW8 ?   A ?   ? UNP P10721 LYS 710 deletion ?   16 
1 7ZW8 ?   A ?   ? UNP P10721 GLU 711 deletion ?   17 
1 7ZW8 ?   A ?   ? UNP P10721 SER 712 deletion ?   18 
1 7ZW8 ?   A ?   ? UNP P10721 SER 713 deletion ?   19 
1 7ZW8 ?   A ?   ? UNP P10721 CYS 714 deletion ?   20 
1 7ZW8 ?   A ?   ? UNP P10721 SER 715 deletion ?   21 
1 7ZW8 ?   A ?   ? UNP P10721 ASP 716 deletion ?   22 
1 7ZW8 ?   A ?   ? UNP P10721 SER 717 deletion ?   23 
1 7ZW8 ?   A ?   ? UNP P10721 THR 718 deletion ?   24 
1 7ZW8 ?   A ?   ? UNP P10721 ASN 719 deletion ?   25 
1 7ZW8 ?   A ?   ? UNP P10721 GLU 720 deletion ?   26 
1 7ZW8 ?   A ?   ? UNP P10721 TYR 721 deletion ?   27 
1 7ZW8 ?   A ?   ? UNP P10721 MET 722 deletion ?   28 
1 7ZW8 ?   A ?   ? UNP P10721 ASP 723 deletion ?   29 
1 7ZW8 ?   A ?   ? UNP P10721 MET 724 deletion ?   30 
1 7ZW8 ?   A ?   ? UNP P10721 LYS 725 deletion ?   31 
1 7ZW8 ?   A ?   ? UNP P10721 PRO 726 deletion ?   32 
1 7ZW8 ?   A ?   ? UNP P10721 GLY 727 deletion ?   33 
1 7ZW8 ?   A ?   ? UNP P10721 VAL 728 deletion ?   34 
1 7ZW8 ?   A ?   ? UNP P10721 SER 729 deletion ?   35 
1 7ZW8 ?   A ?   ? UNP P10721 TYR 730 deletion ?   36 
1 7ZW8 ?   A ?   ? UNP P10721 VAL 731 deletion ?   37 
1 7ZW8 ?   A ?   ? UNP P10721 VAL 732 deletion ?   38 
1 7ZW8 ?   A ?   ? UNP P10721 PRO 733 deletion ?   39 
1 7ZW8 ?   A ?   ? UNP P10721 THR 734 deletion ?   40 
1 7ZW8 ?   A ?   ? UNP P10721 LYS 735 deletion ?   41 
1 7ZW8 ?   A ?   ? UNP P10721 ALA 736 deletion ?   42 
1 7ZW8 ?   A ?   ? UNP P10721 ASP 737 deletion ?   43 
1 7ZW8 ?   A ?   ? UNP P10721 LYS 738 deletion ?   44 
1 7ZW8 ?   A ?   ? UNP P10721 ARG 739 deletion ?   45 
1 7ZW8 ?   A ?   ? UNP P10721 ARG 740 deletion ?   46 
1 7ZW8 ?   A ?   ? UNP P10721 SER 741 deletion ?   47 
1 7ZW8 ?   A ?   ? UNP P10721 VAL 742 deletion ?   48 
1 7ZW8 ?   A ?   ? UNP P10721 ARG 743 deletion ?   49 
1 7ZW8 ?   A ?   ? UNP P10721 ILE 744 deletion ?   50 
1 7ZW8 ?   A ?   ? UNP P10721 GLY 745 deletion ?   51 
1 7ZW8 ?   A ?   ? UNP P10721 SER 746 deletion ?   52 
1 7ZW8 ?   A ?   ? UNP P10721 TYR 747 deletion ?   53 
1 7ZW8 ?   A ?   ? UNP P10721 ILE 748 deletion ?   54 
1 7ZW8 ?   A ?   ? UNP P10721 GLU 749 deletion ?   55 
1 7ZW8 ?   A ?   ? UNP P10721 ARG 750 deletion ?   56 
1 7ZW8 ?   A ?   ? UNP P10721 ASP 751 deletion ?   57 
1 7ZW8 ?   A ?   ? UNP P10721 VAL 752 deletion ?   58 
1 7ZW8 ?   A ?   ? UNP P10721 THR 753 deletion ?   59 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  14900 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 ASP A 22  ? LEU A 26  ? ASP A 572 LEU A 576 5 ? 5  
HELX_P HELX_P2  AA2 ASP A 29  ? GLU A 33  ? ASP A 579 GLU A 583 5 ? 5  
HELX_P HELX_P3  AA3 PRO A 35  ? ASN A 37  ? PRO A 585 ASN A 587 5 ? 3  
HELX_P HELX_P4  AA4 HIS A 80  ? GLY A 98  ? HIS A 630 GLY A 648 1 ? 19 
HELX_P HELX_P5  AA5 LEU A 128 ? LYS A 135 ? LEU A 678 LYS A 685 1 ? 8  
HELX_P HELX_P6  AA6 ASP A 157 ? LYS A 178 ? ASP A 765 LYS A 786 1 ? 22 
HELX_P HELX_P7  AA7 ALA A 186 ? ARG A 188 ? ALA A 794 ARG A 796 5 ? 3  
HELX_P HELX_P8  AA8 PHE A 203 ? ARG A 207 ? PHE A 811 ARG A 815 5 ? 5  
HELX_P HELX_P9  AA9 ASP A 208 ? ASP A 212 ? ASP A 816 ASP A 820 5 ? 5  
HELX_P HELX_P10 AB1 PRO A 224 ? MET A 228 ? PRO A 832 MET A 836 5 ? 5  
HELX_P HELX_P11 AB2 ALA A 229 ? CYS A 236 ? ALA A 837 CYS A 844 1 ? 8  
HELX_P HELX_P12 AB3 THR A 239 ? SER A 256 ? THR A 847 SER A 864 1 ? 18 
HELX_P HELX_P13 AB4 ASP A 268 ? GLY A 278 ? ASP A 876 GLY A 886 1 ? 11 
HELX_P HELX_P14 AB5 PRO A 288 ? TRP A 299 ? PRO A 896 TRP A 907 1 ? 12 
HELX_P HELX_P15 AB6 ASP A 302 ? ARG A 306 ? ASP A 910 ARG A 914 5 ? 5  
HELX_P HELX_P16 AB7 THR A 308 ? THR A 324 ? THR A 916 THR A 932 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 8   ? VAL A 9   ? LYS A 558 VAL A 559 
AA1 2 CYS A 180 ? ILE A 181 ? CYS A 788 ILE A 789 
AA2 1 LEU A 39  ? ALA A 47  ? LEU A 589 ALA A 597 
AA2 2 GLY A 51  ? TYR A 59  ? GLY A 601 TYR A 609 
AA2 3 ALA A 67  ? LEU A 75  ? ALA A 617 LEU A 625 
AA2 4 LEU A 117 ? GLU A 121 ? LEU A 667 GLU A 671 
AA2 5 LEU A 106 ? CYS A 110 ? LEU A 656 CYS A 660 
AA3 1 GLY A 126 ? ASP A 127 ? GLY A 676 ASP A 677 
AA3 2 ILE A 190 ? THR A 193 ? ILE A 798 THR A 801 
AA3 3 ILE A 197 ? ILE A 200 ? ILE A 805 ILE A 808 
AA4 1 VAL A 216 ? VAL A 217 ? VAL A 824 VAL A 825 
AA4 2 ARG A 222 ? LEU A 223 ? ARG A 830 LEU A 831 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 8   ? N LYS A 558 O ILE A 181 ? O ILE A 789 
AA2 1 2 N LYS A 43  ? N LYS A 593 O GLU A 55  ? O GLU A 605 
AA2 2 3 N VAL A 54  ? N VAL A 604 O VAL A 72  ? O VAL A 622 
AA2 3 4 N LYS A 73  ? N LYS A 623 O VAL A 118 ? O VAL A 668 
AA2 4 5 O ILE A 119 ? O ILE A 669 N LEU A 107 ? N LEU A 657 
AA3 1 2 N GLY A 126 ? N GLY A 676 O LEU A 192 ? O LEU A 800 
AA3 2 3 N LEU A 191 ? N LEU A 799 O LYS A 199 ? O LYS A 807 
AA4 1 2 N VAL A 216 ? N VAL A 824 O LEU A 223 ? O LEU A 831 
# 
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 791 ? ? 83.28   -7.92   
2 1 ASP A 792 ? ? -146.21 51.14   
3 1 CYS A 809 ? B -145.19 -158.94 
4 1 ASP A 810 ? ? -163.81 110.19  
# 
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 11.6880 14.6891 -9.9217  -0.0229 ? -0.0145 ? -0.0085 ? -0.0743 ? -0.0422 ? -0.0913 ? 4.7081 ? 
0.1672  ? -1.7221 ? 4.7431 ? 0.4479 ? 3.3166 ? 0.2005 ? -0.4327 ? 0.2117  ? 0.3058  ? -0.2074 ? 0.1330  ? -0.1220 ? -0.0828 ? 
0.0069  ? 
2 'X-RAY DIFFRACTION' ? refined 19.0315 2.6151  -29.6598 -0.0794 ? -0.0006 ? -0.0215 ? -0.0828 ? -0.0771 ? 0.0173  ? 3.2496 ? 
-1.2328 ? -1.1671 ? 5.0930 ? 2.2326 ? 3.1812 ? 0.2366 ? 0.2925  ? -0.4942 ? -0.4362 ? -0.1755 ? -0.4528 ? -0.2918 ? -0.2443 ? 
-0.0611 ? 
# 
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.beg_PDB_ins_code 
_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.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 553 ? ? ? A 672 ? ? '{ A|553 - A|672 }' 
2 'X-RAY DIFFRACTION' 2 ? ? A 673 ? ? ? A 932 ? ? '{ A|673 - A|932 }' 
# 
_phasing.method   MR 
# 
_pdbx_entry_details.entry_id                 7ZW8 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
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 PRO 551 ? A PRO 1   
2  1 Y 1 A MET 552 ? A MET 2   
3  1 Y 1 A TYR 553 ? A TYR 3   
4  1 Y 1 A ILE 563 ? A ILE 13  
5  1 Y 1 A ASN 564 ? A ASN 14  
6  1 Y 1 A GLY 565 ? A GLY 15  
7  1 Y 1 A ASN 566 ? A ASN 16  
8  1 Y 1 A ASN 567 ? A ASN 17  
9  1 Y 1 A TYR 568 ? A TYR 18  
10 1 Y 1 A SER 746 ? A SER 138 
11 1 Y 1 A PHE 747 ? A PHE 139 
12 1 Y 1 A ILE 748 ? A ILE 140 
13 1 Y 1 A CYS 749 ? A CYS 141 
14 1 Y 1 A SER 750 ? A SER 142 
15 1 Y 1 A LYS 751 ? A LYS 143 
16 1 Y 1 A THR 752 ? A THR 144 
17 1 Y 1 A GLU 753 ? A GLU 145 
18 1 Y 1 A PRO 754 ? A PRO 146 
19 1 Y 1 A ALA 755 ? A ALA 147 
20 1 Y 1 A ILE 756 ? A ILE 148 
21 1 Y 1 A MET 757 ? A MET 149 
22 1 Y 1 A GLU 758 ? A GLU 150 
23 1 Y 1 A ASP 759 ? A ASP 151 
24 1 Y 1 A ASN 933 ? A ASN 325 
25 1 Y 1 A HIS 934 ? A HIS 326 
26 1 Y 1 A ILE 935 ? A ILE 327 
# 
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 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
K3R C1   C N N 183 
K3R C3   C Y N 184 
K3R C4   C Y N 185 
K3R C5   C Y N 186 
K3R C7   C Y N 187 
K3R C8   C Y N 188 
K3R C11  C N N 189 
K3R C15  C Y N 190 
K3R C17  C Y N 191 
K3R C19  C Y N 192 
K3R C23  C Y N 193 
K3R C24  C Y N 194 
K3R O25  O N N 195 
K3R C27  C N N 196 
K3R C30  C N N 197 
K3R C31  C N N 198 
K3R C32  C N N 199 
K3R C33  C N N 200 
K3R C34  C Y N 201 
K3R C35  C Y N 202 
K3R C37  C Y N 203 
K3R C38  C Y N 204 
K3R N2   N Y N 205 
K3R N6   N Y N 206 
K3R C9   C Y N 207 
K3R C10  C Y N 208 
K3R N12  N N N 209 
K3R C13  C Y N 210 
K3R C14  C Y N 211 
K3R N16  N Y N 212 
K3R N18  N Y N 213 
K3R C20  C Y N 214 
K3R N21  N Y N 215 
K3R C22  C Y N 216 
K3R C26  C N N 217 
K3R C28  C N N 218 
K3R N29  N N N 219 
K3R N36  N Y N 220 
K3R H1   H N N 221 
K3R H2   H N N 222 
K3R H3   H N N 223 
K3R H4   H N N 224 
K3R H5   H N N 225 
K3R H6   H N N 226 
K3R H7   H N N 227 
K3R H8   H N N 228 
K3R H9   H N N 229 
K3R H10  H N N 230 
K3R H11  H N N 231 
K3R H12  H N N 232 
K3R H13  H N N 233 
K3R H14  H N N 234 
K3R H15  H N N 235 
K3R H16  H N N 236 
K3R H17  H N N 237 
K3R H18  H N N 238 
K3R H19  H N N 239 
K3R H20  H N N 240 
K3R H21  H N N 241 
K3R H22  H N N 242 
K3R H23  H N N 243 
K3R H24  H N N 244 
K3R H25  H N N 245 
K3R H26  H N N 246 
K3R H27  H N N 247 
K3R H28  H N N 248 
K3R H29  H N N 249 
K3R H30  H N N 250 
K3R H31  H N N 251 
K3R H32  H N N 252 
LEU N    N N N 253 
LEU CA   C N S 254 
LEU C    C N N 255 
LEU O    O N N 256 
LEU CB   C N N 257 
LEU CG   C N N 258 
LEU CD1  C N N 259 
LEU CD2  C N N 260 
LEU OXT  O N N 261 
LEU H    H N N 262 
LEU H2   H N N 263 
LEU HA   H N N 264 
LEU HB2  H N N 265 
LEU HB3  H N N 266 
LEU HG   H N N 267 
LEU HD11 H N N 268 
LEU HD12 H N N 269 
LEU HD13 H N N 270 
LEU HD21 H N N 271 
LEU HD22 H N N 272 
LEU HD23 H N N 273 
LEU HXT  H N N 274 
LYS N    N N N 275 
LYS CA   C N S 276 
LYS C    C N N 277 
LYS O    O N N 278 
LYS CB   C N N 279 
LYS CG   C N N 280 
LYS CD   C N N 281 
LYS CE   C N N 282 
LYS NZ   N N N 283 
LYS OXT  O N N 284 
LYS H    H N N 285 
LYS H2   H N N 286 
LYS HA   H N N 287 
LYS HB2  H N N 288 
LYS HB3  H N N 289 
LYS HG2  H N N 290 
LYS HG3  H N N 291 
LYS HD2  H N N 292 
LYS HD3  H N N 293 
LYS HE2  H N N 294 
LYS HE3  H N N 295 
LYS HZ1  H N N 296 
LYS HZ2  H N N 297 
LYS HZ3  H N N 298 
LYS HXT  H N N 299 
MET N    N N N 300 
MET CA   C N S 301 
MET C    C N N 302 
MET O    O N N 303 
MET CB   C N N 304 
MET CG   C N N 305 
MET SD   S N N 306 
MET CE   C N N 307 
MET OXT  O N N 308 
MET H    H N N 309 
MET H2   H N N 310 
MET HA   H N N 311 
MET HB2  H N N 312 
MET HB3  H N N 313 
MET HG2  H N N 314 
MET HG3  H N N 315 
MET HE1  H N N 316 
MET HE2  H N N 317 
MET HE3  H N N 318 
MET HXT  H N N 319 
PHE N    N N N 320 
PHE CA   C N S 321 
PHE C    C N N 322 
PHE O    O N N 323 
PHE CB   C N N 324 
PHE CG   C Y N 325 
PHE CD1  C Y N 326 
PHE CD2  C Y N 327 
PHE CE1  C Y N 328 
PHE CE2  C Y N 329 
PHE CZ   C Y N 330 
PHE OXT  O N N 331 
PHE H    H N N 332 
PHE H2   H N N 333 
PHE HA   H N N 334 
PHE HB2  H N N 335 
PHE HB3  H N N 336 
PHE HD1  H N N 337 
PHE HD2  H N N 338 
PHE HE1  H N N 339 
PHE HE2  H N N 340 
PHE HZ   H N N 341 
PHE HXT  H N N 342 
PRO N    N N N 343 
PRO CA   C N S 344 
PRO C    C N N 345 
PRO O    O N N 346 
PRO CB   C N N 347 
PRO CG   C N N 348 
PRO CD   C N N 349 
PRO OXT  O N N 350 
PRO H    H N N 351 
PRO HA   H N N 352 
PRO HB2  H N N 353 
PRO HB3  H N N 354 
PRO HG2  H N N 355 
PRO HG3  H N N 356 
PRO HD2  H N N 357 
PRO HD3  H N N 358 
PRO HXT  H N N 359 
SER N    N N N 360 
SER CA   C N S 361 
SER C    C N N 362 
SER O    O N N 363 
SER CB   C N N 364 
SER OG   O N N 365 
SER OXT  O N N 366 
SER H    H N N 367 
SER H2   H N N 368 
SER HA   H N N 369 
SER HB2  H N N 370 
SER HB3  H N N 371 
SER HG   H N N 372 
SER HXT  H N N 373 
THR N    N N N 374 
THR CA   C N S 375 
THR C    C N N 376 
THR O    O N N 377 
THR CB   C N R 378 
THR OG1  O N N 379 
THR CG2  C N N 380 
THR OXT  O N N 381 
THR H    H N N 382 
THR H2   H N N 383 
THR HA   H N N 384 
THR HB   H N N 385 
THR HG1  H N N 386 
THR HG21 H N N 387 
THR HG22 H N N 388 
THR HG23 H N N 389 
THR HXT  H N N 390 
TRP N    N N N 391 
TRP CA   C N S 392 
TRP C    C N N 393 
TRP O    O N N 394 
TRP CB   C N N 395 
TRP CG   C Y N 396 
TRP CD1  C Y N 397 
TRP CD2  C Y N 398 
TRP NE1  N Y N 399 
TRP CE2  C Y N 400 
TRP CE3  C Y N 401 
TRP CZ2  C Y N 402 
TRP CZ3  C Y N 403 
TRP CH2  C Y N 404 
TRP OXT  O N N 405 
TRP H    H N N 406 
TRP H2   H N N 407 
TRP HA   H N N 408 
TRP HB2  H N N 409 
TRP HB3  H N N 410 
TRP HD1  H N N 411 
TRP HE1  H N N 412 
TRP HE3  H N N 413 
TRP HZ2  H N N 414 
TRP HZ3  H N N 415 
TRP HH2  H N N 416 
TRP HXT  H N N 417 
TYR N    N N N 418 
TYR CA   C N S 419 
TYR C    C N N 420 
TYR O    O N N 421 
TYR CB   C N N 422 
TYR CG   C Y N 423 
TYR CD1  C Y N 424 
TYR CD2  C Y N 425 
TYR CE1  C Y N 426 
TYR CE2  C Y N 427 
TYR CZ   C Y N 428 
TYR OH   O N N 429 
TYR OXT  O N N 430 
TYR H    H N N 431 
TYR H2   H N N 432 
TYR HA   H N N 433 
TYR HB2  H N N 434 
TYR HB3  H N N 435 
TYR HD1  H N N 436 
TYR HD2  H N N 437 
TYR HE1  H N N 438 
TYR HE2  H N N 439 
TYR HH   H N N 440 
TYR HXT  H N N 441 
VAL N    N N N 442 
VAL CA   C N S 443 
VAL C    C N N 444 
VAL O    O N N 445 
VAL CB   C N N 446 
VAL CG1  C N N 447 
VAL CG2  C N N 448 
VAL OXT  O N N 449 
VAL H    H N N 450 
VAL H2   H N N 451 
VAL HA   H N N 452 
VAL HB   H N N 453 
VAL HG11 H N N 454 
VAL HG12 H N N 455 
VAL HG13 H N N 456 
VAL HG21 H N N 457 
VAL HG22 H N N 458 
VAL HG23 H N N 459 
VAL HXT  H N N 460 
# 
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 
K3R N6  N2   sing Y N 173 
K3R N6  C5   doub Y N 174 
K3R C1  N2   sing N N 175 
K3R N2  C3   sing Y N 176 
K3R C5  C4   sing Y N 177 
K3R C3  C4   doub Y N 178 
K3R C4  C7   sing N N 179 
K3R C7  C38  doub Y N 180 
K3R C7  C8   sing Y N 181 
K3R C38 C37  sing Y N 182 
K3R C8  C9   doub Y N 183 
K3R C37 C10  doub Y N 184 
K3R C9  C10  sing Y N 185 
K3R C10 C11  sing N N 186 
K3R C31 C30  sing N N 187 
K3R C31 C32  sing N N 188 
K3R C27 C26  sing N N 189 
K3R C27 C28  sing N N 190 
K3R C30 N29  sing N N 191 
K3R N29 C33  sing N N 192 
K3R N29 C28  sing N N 193 
K3R N21 C20  sing Y N 194 
K3R N21 C22  doub Y N 195 
K3R C20 C19  doub Y N 196 
K3R C22 C23  sing Y N 197 
K3R C22 N36  sing Y N 198 
K3R C23 C24  doub Y N 199 
K3R C19 N36  sing Y N 200 
K3R C19 C15  sing N N 201 
K3R N36 C35  sing Y N 202 
K3R C26 O25  sing N N 203 
K3R C24 O25  sing N N 204 
K3R C24 C34  sing Y N 205 
K3R C33 C32  sing N N 206 
K3R N16 C15  doub Y N 207 
K3R N16 C17  sing Y N 208 
K3R C15 C14  sing Y N 209 
K3R C35 C34  doub Y N 210 
K3R C17 N18  doub Y N 211 
K3R C14 C13  doub Y N 212 
K3R N18 C13  sing Y N 213 
K3R C13 N12  sing N N 214 
K3R N12 C11  sing N N 215 
K3R C1  H1   sing N N 216 
K3R C1  H2   sing N N 217 
K3R C1  H3   sing N N 218 
K3R C3  H4   sing N N 219 
K3R C5  H5   sing N N 220 
K3R C8  H6   sing N N 221 
K3R C11 H7   sing N N 222 
K3R C11 H8   sing N N 223 
K3R C17 H9   sing N N 224 
K3R C23 H10  sing N N 225 
K3R C27 H11  sing N N 226 
K3R C27 H12  sing N N 227 
K3R C30 H13  sing N N 228 
K3R C30 H14  sing N N 229 
K3R C31 H15  sing N N 230 
K3R C31 H16  sing N N 231 
K3R C32 H17  sing N N 232 
K3R C32 H18  sing N N 233 
K3R C33 H19  sing N N 234 
K3R C33 H20  sing N N 235 
K3R C34 H21  sing N N 236 
K3R C35 H22  sing N N 237 
K3R C37 H23  sing N N 238 
K3R C38 H24  sing N N 239 
K3R C9  H25  sing N N 240 
K3R N12 H26  sing N N 241 
K3R C14 H27  sing N N 242 
K3R C20 H28  sing N N 243 
K3R C26 H29  sing N N 244 
K3R C26 H30  sing N N 245 
K3R C28 H31  sing N N 246 
K3R C28 H32  sing N N 247 
LEU N   CA   sing N N 248 
LEU N   H    sing N N 249 
LEU N   H2   sing N N 250 
LEU CA  C    sing N N 251 
LEU CA  CB   sing N N 252 
LEU CA  HA   sing N N 253 
LEU C   O    doub N N 254 
LEU C   OXT  sing N N 255 
LEU CB  CG   sing N N 256 
LEU CB  HB2  sing N N 257 
LEU CB  HB3  sing N N 258 
LEU CG  CD1  sing N N 259 
LEU CG  CD2  sing N N 260 
LEU CG  HG   sing N N 261 
LEU CD1 HD11 sing N N 262 
LEU CD1 HD12 sing N N 263 
LEU CD1 HD13 sing N N 264 
LEU CD2 HD21 sing N N 265 
LEU CD2 HD22 sing N N 266 
LEU CD2 HD23 sing N N 267 
LEU OXT HXT  sing N N 268 
LYS N   CA   sing N N 269 
LYS N   H    sing N N 270 
LYS N   H2   sing N N 271 
LYS CA  C    sing N N 272 
LYS CA  CB   sing N N 273 
LYS CA  HA   sing N N 274 
LYS C   O    doub N N 275 
LYS C   OXT  sing N N 276 
LYS CB  CG   sing N N 277 
LYS CB  HB2  sing N N 278 
LYS CB  HB3  sing N N 279 
LYS CG  CD   sing N N 280 
LYS CG  HG2  sing N N 281 
LYS CG  HG3  sing N N 282 
LYS CD  CE   sing N N 283 
LYS CD  HD2  sing N N 284 
LYS CD  HD3  sing N N 285 
LYS CE  NZ   sing N N 286 
LYS CE  HE2  sing N N 287 
LYS CE  HE3  sing N N 288 
LYS NZ  HZ1  sing N N 289 
LYS NZ  HZ2  sing N N 290 
LYS NZ  HZ3  sing N N 291 
LYS OXT HXT  sing N N 292 
MET N   CA   sing N N 293 
MET N   H    sing N N 294 
MET N   H2   sing N N 295 
MET CA  C    sing N N 296 
MET CA  CB   sing N N 297 
MET CA  HA   sing N N 298 
MET C   O    doub N N 299 
MET C   OXT  sing N N 300 
MET CB  CG   sing N N 301 
MET CB  HB2  sing N N 302 
MET CB  HB3  sing N N 303 
MET CG  SD   sing N N 304 
MET CG  HG2  sing N N 305 
MET CG  HG3  sing N N 306 
MET SD  CE   sing N N 307 
MET CE  HE1  sing N N 308 
MET CE  HE2  sing N N 309 
MET CE  HE3  sing N N 310 
MET OXT HXT  sing N N 311 
PHE N   CA   sing N N 312 
PHE N   H    sing N N 313 
PHE N   H2   sing N N 314 
PHE CA  C    sing N N 315 
PHE CA  CB   sing N N 316 
PHE CA  HA   sing N N 317 
PHE C   O    doub N N 318 
PHE C   OXT  sing N N 319 
PHE CB  CG   sing N N 320 
PHE CB  HB2  sing N N 321 
PHE CB  HB3  sing N N 322 
PHE CG  CD1  doub Y N 323 
PHE CG  CD2  sing Y N 324 
PHE CD1 CE1  sing Y N 325 
PHE CD1 HD1  sing N N 326 
PHE CD2 CE2  doub Y N 327 
PHE CD2 HD2  sing N N 328 
PHE CE1 CZ   doub Y N 329 
PHE CE1 HE1  sing N N 330 
PHE CE2 CZ   sing Y N 331 
PHE CE2 HE2  sing N N 332 
PHE CZ  HZ   sing N N 333 
PHE OXT HXT  sing N N 334 
PRO N   CA   sing N N 335 
PRO N   CD   sing N N 336 
PRO N   H    sing N N 337 
PRO CA  C    sing N N 338 
PRO CA  CB   sing N N 339 
PRO CA  HA   sing N N 340 
PRO C   O    doub N N 341 
PRO C   OXT  sing N N 342 
PRO CB  CG   sing N N 343 
PRO CB  HB2  sing N N 344 
PRO CB  HB3  sing N N 345 
PRO CG  CD   sing N N 346 
PRO CG  HG2  sing N N 347 
PRO CG  HG3  sing N N 348 
PRO CD  HD2  sing N N 349 
PRO CD  HD3  sing N N 350 
PRO OXT HXT  sing N N 351 
SER N   CA   sing N N 352 
SER N   H    sing N N 353 
SER N   H2   sing N N 354 
SER CA  C    sing N N 355 
SER CA  CB   sing N N 356 
SER CA  HA   sing N N 357 
SER C   O    doub N N 358 
SER C   OXT  sing N N 359 
SER CB  OG   sing N N 360 
SER CB  HB2  sing N N 361 
SER CB  HB3  sing N N 362 
SER OG  HG   sing N N 363 
SER OXT HXT  sing N N 364 
THR N   CA   sing N N 365 
THR N   H    sing N N 366 
THR N   H2   sing N N 367 
THR CA  C    sing N N 368 
THR CA  CB   sing N N 369 
THR CA  HA   sing N N 370 
THR C   O    doub N N 371 
THR C   OXT  sing N N 372 
THR CB  OG1  sing N N 373 
THR CB  CG2  sing N N 374 
THR CB  HB   sing N N 375 
THR OG1 HG1  sing N N 376 
THR CG2 HG21 sing N N 377 
THR CG2 HG22 sing N N 378 
THR CG2 HG23 sing N N 379 
THR OXT HXT  sing N N 380 
TRP N   CA   sing N N 381 
TRP N   H    sing N N 382 
TRP N   H2   sing N N 383 
TRP CA  C    sing N N 384 
TRP CA  CB   sing N N 385 
TRP CA  HA   sing N N 386 
TRP C   O    doub N N 387 
TRP C   OXT  sing N N 388 
TRP CB  CG   sing N N 389 
TRP CB  HB2  sing N N 390 
TRP CB  HB3  sing N N 391 
TRP CG  CD1  doub Y N 392 
TRP CG  CD2  sing Y N 393 
TRP CD1 NE1  sing Y N 394 
TRP CD1 HD1  sing N N 395 
TRP CD2 CE2  doub Y N 396 
TRP CD2 CE3  sing Y N 397 
TRP NE1 CE2  sing Y N 398 
TRP NE1 HE1  sing N N 399 
TRP CE2 CZ2  sing Y N 400 
TRP CE3 CZ3  doub Y N 401 
TRP CE3 HE3  sing N N 402 
TRP CZ2 CH2  doub Y N 403 
TRP CZ2 HZ2  sing N N 404 
TRP CZ3 CH2  sing Y N 405 
TRP CZ3 HZ3  sing N N 406 
TRP CH2 HH2  sing N N 407 
TRP OXT HXT  sing N N 408 
TYR N   CA   sing N N 409 
TYR N   H    sing N N 410 
TYR N   H2   sing N N 411 
TYR CA  C    sing N N 412 
TYR CA  CB   sing N N 413 
TYR CA  HA   sing N N 414 
TYR C   O    doub N N 415 
TYR C   OXT  sing N N 416 
TYR CB  CG   sing N N 417 
TYR CB  HB2  sing N N 418 
TYR CB  HB3  sing N N 419 
TYR CG  CD1  doub Y N 420 
TYR CG  CD2  sing Y N 421 
TYR CD1 CE1  sing Y N 422 
TYR CD1 HD1  sing N N 423 
TYR CD2 CE2  doub Y N 424 
TYR CD2 HD2  sing N N 425 
TYR CE1 CZ   doub Y N 426 
TYR CE1 HE1  sing N N 427 
TYR CE2 CZ   sing Y N 428 
TYR CE2 HE2  sing N N 429 
TYR CZ  OH   sing N N 430 
TYR OH  HH   sing N N 431 
TYR OXT HXT  sing N N 432 
VAL N   CA   sing N N 433 
VAL N   H    sing N N 434 
VAL N   H2   sing N N 435 
VAL CA  C    sing N N 436 
VAL CA  CB   sing N N 437 
VAL CA  HA   sing N N 438 
VAL C   O    doub N N 439 
VAL C   OXT  sing N N 440 
VAL CB  CG1  sing N N 441 
VAL CB  CG2  sing N N 442 
VAL CB  HB   sing N N 443 
VAL CG1 HG11 sing N N 444 
VAL CG1 HG12 sing N N 445 
VAL CG1 HG13 sing N N 446 
VAL CG2 HG21 sing N N 447 
VAL CG2 HG22 sing N N 448 
VAL CG2 HG23 sing N N 449 
VAL OXT HXT  sing N N 450 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        K3R 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   K3R 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3G0E 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7ZW8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.021713 
_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]   0.012299 
_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]   0.010411 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . GLU A 1 4   ? 27.513  13.285  -10.760 1.00 77.97  ? 554  GLU A N   1 
ATOM   2    C CA  . GLU A 1 4   ? 27.332  14.321  -11.778 1.00 78.30  ? 554  GLU A CA  1 
ATOM   3    C C   . GLU A 1 4   ? 26.023  14.126  -12.551 1.00 76.59  ? 554  GLU A C   1 
ATOM   4    O O   . GLU A 1 4   ? 25.605  12.984  -12.759 1.00 76.10  ? 554  GLU A O   1 
ATOM   5    C CB  . GLU A 1 4   ? 28.509  14.304  -12.775 1.00 83.05  ? 554  GLU A CB  1 
ATOM   6    C CG  . GLU A 1 4   ? 28.668  15.601  -13.561 1.00 92.13  ? 554  GLU A CG  1 
ATOM   7    C CD  . GLU A 1 4   ? 29.371  15.481  -14.903 1.00 103.27 ? 554  GLU A CD  1 
ATOM   8    O OE1 . GLU A 1 4   ? 29.609  16.534  -15.545 1.00 104.93 ? 554  GLU A OE1 1 
ATOM   9    O OE2 . GLU A 1 4   ? 29.676  14.336  -15.318 1.00 106.72 ? 554  GLU A OE2 1 
ATOM   10   N N   . VAL A 1 5   ? 25.378  15.241  -12.978 1.00 75.08  ? 555  VAL A N   1 
ATOM   11   C CA  . VAL A 1 5   ? 24.168  15.184  -13.805 1.00 73.92  ? 555  VAL A CA  1 
ATOM   12   C C   . VAL A 1 5   ? 24.627  14.728  -15.189 1.00 73.38  ? 555  VAL A C   1 
ATOM   13   O O   . VAL A 1 5   ? 25.625  15.234  -15.701 1.00 74.13  ? 555  VAL A O   1 
ATOM   14   C CB  . VAL A 1 5   ? 23.381  16.526  -13.837 1.00 73.89  ? 555  VAL A CB  1 
ATOM   15   C CG1 . VAL A 1 5   ? 22.401  16.584  -15.010 1.00 74.03  ? 555  VAL A CG1 1 
ATOM   16   C CG2 . VAL A 1 5   ? 22.649  16.744  -12.525 1.00 74.10  ? 555  VAL A CG2 1 
ATOM   17   N N   . GLN A 1 6   ? 23.948  13.734  -15.765 1.00 72.04  ? 556  GLN A N   1 
ATOM   18   C CA  . GLN A 1 6   ? 24.354  13.164  -17.040 1.00 71.19  ? 556  GLN A CA  1 
ATOM   19   C C   . GLN A 1 6   ? 23.833  13.906  -18.227 1.00 70.15  ? 556  GLN A C   1 
ATOM   20   O O   . GLN A 1 6   ? 24.537  14.029  -19.222 1.00 70.39  ? 556  GLN A O   1 
ATOM   21   C CB  . GLN A 1 6   ? 23.939  11.692  -17.118 1.00 72.47  ? 556  GLN A CB  1 
ATOM   22   C CG  . GLN A 1 6   ? 24.440  10.873  -15.933 1.00 76.73  ? 556  GLN A CG  1 
ATOM   23   C CD  . GLN A 1 6   ? 25.945  10.823  -15.882 1.00 82.94  ? 556  GLN A CD  1 
ATOM   24   O OE1 . GLN A 1 6   ? 26.620  10.597  -16.890 1.00 85.73  ? 556  GLN A OE1 1 
ATOM   25   N NE2 . GLN A 1 6   ? 26.506  11.040  -14.709 1.00 83.84  ? 556  GLN A NE2 1 
ATOM   26   N N   . TRP A 1 7   ? 22.586  14.360  -18.159 1.00 68.87  ? 557  TRP A N   1 
ATOM   27   C CA  . TRP A 1 7   ? 21.961  15.041  -19.291 1.00 67.87  ? 557  TRP A CA  1 
ATOM   28   C C   . TRP A 1 7   ? 22.546  16.431  -19.441 1.00 68.54  ? 557  TRP A C   1 
ATOM   29   O O   . TRP A 1 7   ? 22.649  17.176  -18.467 1.00 69.31  ? 557  TRP A O   1 
ATOM   30   C CB  . TRP A 1 7   ? 20.424  15.086  -19.164 1.00 66.30  ? 557  TRP A CB  1 
ATOM   31   C CG  . TRP A 1 7   ? 19.859  13.894  -18.466 1.00 64.54  ? 557  TRP A CG  1 
ATOM   32   C CD1 . TRP A 1 7   ? 20.118  12.587  -18.743 1.00 64.45  ? 557  TRP A CD1 1 
ATOM   33   C CD2 . TRP A 1 7   ? 18.987  13.900  -17.326 1.00 63.54  ? 557  TRP A CD2 1 
ATOM   34   N NE1 . TRP A 1 7   ? 19.485  11.777  -17.828 1.00 64.34  ? 557  TRP A NE1 1 
ATOM   35   C CE2 . TRP A 1 7   ? 18.778  12.556  -16.952 1.00 63.81  ? 557  TRP A CE2 1 
ATOM   36   C CE3 . TRP A 1 7   ? 18.341  14.906  -16.604 1.00 63.28  ? 557  TRP A CE3 1 
ATOM   37   C CZ2 . TRP A 1 7   ? 17.972  12.197  -15.875 1.00 63.63  ? 557  TRP A CZ2 1 
ATOM   38   C CZ3 . TRP A 1 7   ? 17.523  14.544  -15.555 1.00 63.43  ? 557  TRP A CZ3 1 
ATOM   39   C CH2 . TRP A 1 7   ? 17.355  13.206  -15.193 1.00 63.43  ? 557  TRP A CH2 1 
ATOM   40   N N   . LYS A 1 8   ? 22.976  16.753  -20.647 1.00 68.17  ? 558  LYS A N   1 
ATOM   41   C CA  . LYS A 1 8   ? 23.574  18.042  -20.927 1.00 68.36  ? 558  LYS A CA  1 
ATOM   42   C C   . LYS A 1 8   ? 22.603  18.948  -21.620 1.00 67.62  ? 558  LYS A C   1 
ATOM   43   O O   . LYS A 1 8   ? 21.818  18.525  -22.464 1.00 66.25  ? 558  LYS A O   1 
ATOM   44   C CB  . LYS A 1 8   ? 24.852  17.889  -21.786 1.00 71.15  ? 558  LYS A CB  1 
ATOM   45   C CG  . LYS A 1 8   ? 25.883  16.931  -21.195 1.00 75.69  ? 558  LYS A CG  1 
ATOM   46   C CD  . LYS A 1 8   ? 26.424  17.447  -19.873 1.00 81.28  ? 558  LYS A CD  1 
ATOM   47   C CE  . LYS A 1 8   ? 27.263  16.409  -19.190 1.00 86.70  ? 558  LYS A CE  1 
ATOM   48   N NZ  . LYS A 1 8   ? 27.280  16.600  -17.719 1.00 90.32  ? 558  LYS A NZ  1 
ATOM   49   N N   . VAL A 1 9   ? 22.661  20.212  -21.256 1.00 68.48  ? 559  VAL A N   1 
ATOM   50   C CA  . VAL A 1 9   ? 21.869  21.235  -21.900 1.00 69.63  ? 559  VAL A CA  1 
ATOM   51   C C   . VAL A 1 9   ? 22.882  22.223  -22.455 1.00 71.81  ? 559  VAL A C   1 
ATOM   52   O O   . VAL A 1 9   ? 23.712  22.720  -21.696 1.00 71.61  ? 559  VAL A O   1 
ATOM   53   C CB  . VAL A 1 9   ? 20.857  21.879  -20.936 1.00 69.24  ? 559  VAL A CB  1 
ATOM   54   C CG1 . VAL A 1 9   ? 20.221  23.123  -21.559 1.00 69.23  ? 559  VAL A CG1 1 
ATOM   55   C CG2 . VAL A 1 9   ? 19.796  20.864  -20.531 1.00 68.98  ? 559  VAL A CG2 1 
ATOM   56   N N   . VAL A 1 10  ? 22.836  22.488  -23.763 1.00 73.73  ? 560  VAL A N   1 
ATOM   57   C CA  . VAL A 1 10  ? 23.852  23.391  -24.383 1.00 76.81  ? 560  VAL A CA  1 
ATOM   58   C C   . VAL A 1 10  ? 23.219  24.757  -24.669 1.00 80.49  ? 560  VAL A C   1 
ATOM   59   O O   . VAL A 1 10  ? 21.982  24.819  -24.804 1.00 80.81  ? 560  VAL A O   1 
ATOM   60   C CB  . VAL A 1 10  ? 24.492  22.770  -25.640 1.00 77.52  ? 560  VAL A CB  1 
ATOM   61   C CG1 . VAL A 1 10  ? 24.685  21.271  -25.493 1.00 77.85  ? 560  VAL A CG1 1 
ATOM   62   C CG2 . VAL A 1 10  ? 23.719  23.092  -26.909 1.00 77.88  ? 560  VAL A CG2 1 
ATOM   63   N N   . GLU A 1 11  ? 24.033  25.816  -24.699 1.00 82.88  ? 561  GLU A N   1 
ATOM   64   C CA  . GLU A 1 11  ? 23.519  27.168  -25.042 1.00 86.44  ? 561  GLU A CA  1 
ATOM   65   C C   . GLU A 1 11  ? 23.197  27.211  -26.539 1.00 90.49  ? 561  GLU A C   1 
ATOM   66   O O   . GLU A 1 11  ? 23.945  26.590  -27.319 1.00 91.18  ? 561  GLU A O   1 
ATOM   67   C CB  . GLU A 1 11  ? 24.541  28.239  -24.659 1.00 87.63  ? 561  GLU A CB  1 
ATOM   68   C CG  . GLU A 1 11  ? 24.857  28.269  -23.175 1.00 89.33  ? 561  GLU A CG  1 
ATOM   69   C CD  . GLU A 1 11  ? 24.640  29.617  -22.511 1.00 89.85  ? 561  GLU A CD  1 
ATOM   70   O OE1 . GLU A 1 11  ? 24.169  30.544  -23.199 1.00 88.90  ? 561  GLU A OE1 1 
ATOM   71   O OE2 . GLU A 1 11  ? 24.941  29.736  -21.307 1.00 90.56  ? 561  GLU A OE2 1 
ATOM   72   N N   . GLU A 1 12  ? 22.134  27.925  -26.921 1.00 92.74  ? 562  GLU A N   1 
ATOM   73   C CA  . GLU A 1 12  ? 21.744  28.034  -28.353 1.00 95.56  ? 562  GLU A CA  1 
ATOM   74   C C   . GLU A 1 12  ? 22.856  28.753  -29.125 1.00 96.76  ? 562  GLU A C   1 
ATOM   75   O O   . GLU A 1 12  ? 23.570  28.057  -29.874 1.00 97.52  ? 562  GLU A O   1 
ATOM   76   C CB  . GLU A 1 12  ? 20.412  28.776  -28.487 1.00 99.81  ? 562  GLU A CB  1 
ATOM   77   C CG  . GLU A 1 12  ? 19.224  27.854  -28.688 1.00 106.72 ? 562  GLU A CG  1 
ATOM   78   C CD  . GLU A 1 12  ? 18.890  27.562  -30.141 1.00 116.15 ? 562  GLU A CD  1 
ATOM   79   O OE1 . GLU A 1 12  ? 18.850  28.518  -30.940 1.00 118.10 ? 562  GLU A OE1 1 
ATOM   80   O OE2 . GLU A 1 12  ? 18.671  26.379  -30.469 1.00 118.61 ? 562  GLU A OE2 1 
ATOM   81   N N   . VAL A 1 19  ? 28.901  25.543  -25.536 1.00 81.08  ? 569  VAL A N   1 
ATOM   82   C CA  . VAL A 1 19  ? 28.941  26.064  -24.137 1.00 82.17  ? 569  VAL A CA  1 
ATOM   83   C C   . VAL A 1 19  ? 27.809  25.381  -23.364 1.00 81.33  ? 569  VAL A C   1 
ATOM   84   O O   . VAL A 1 19  ? 26.681  25.346  -23.888 1.00 82.03  ? 569  VAL A O   1 
ATOM   85   C CB  . VAL A 1 19  ? 28.865  27.603  -24.095 1.00 84.23  ? 569  VAL A CB  1 
ATOM   86   C CG1 . VAL A 1 19  ? 28.074  28.173  -25.263 1.00 85.45  ? 569  VAL A CG1 1 
ATOM   87   C CG2 . VAL A 1 19  ? 28.348  28.132  -22.766 1.00 84.71  ? 569  VAL A CG2 1 
ATOM   88   N N   . TYR A 1 20  ? 28.105  24.830  -22.185 1.00 79.37  ? 570  TYR A N   1 
ATOM   89   C CA  . TYR A 1 20  ? 27.079  24.041  -21.456 1.00 77.77  ? 570  TYR A CA  1 
ATOM   90   C C   . TYR A 1 20  ? 26.414  24.849  -20.342 1.00 75.41  ? 570  TYR A C   1 
ATOM   91   O O   . TYR A 1 20  ? 27.123  25.586  -19.631 1.00 75.90  ? 570  TYR A O   1 
ATOM   92   C CB  . TYR A 1 20  ? 27.692  22.747  -20.913 1.00 78.07  ? 570  TYR A CB  1 
ATOM   93   C CG  . TYR A 1 20  ? 28.098  21.754  -21.973 1.00 79.60  ? 570  TYR A CG  1 
ATOM   94   C CD1 . TYR A 1 20  ? 29.347  21.814  -22.569 1.00 80.75  ? 570  TYR A CD1 1 
ATOM   95   C CD2 . TYR A 1 20  ? 27.234  20.753  -22.381 1.00 80.51  ? 570  TYR A CD2 1 
ATOM   96   C CE1 . TYR A 1 20  ? 29.727  20.908  -23.545 1.00 81.73  ? 570  TYR A CE1 1 
ATOM   97   C CE2 . TYR A 1 20  ? 27.599  19.837  -23.353 1.00 81.43  ? 570  TYR A CE2 1 
ATOM   98   C CZ  . TYR A 1 20  ? 28.850  19.914  -23.938 1.00 82.73  ? 570  TYR A CZ  1 
ATOM   99   O OH  . TYR A 1 20  ? 29.214  19.014  -24.898 1.00 84.55  ? 570  TYR A OH  1 
ATOM   100  N N   . ILE A 1 21  ? 25.094  24.711  -20.200 1.00 73.01  ? 571  ILE A N   1 
ATOM   101  C CA  . ILE A 1 21  ? 24.354  25.364  -19.134 1.00 71.32  ? 571  ILE A CA  1 
ATOM   102  C C   . ILE A 1 21  ? 24.521  24.527  -17.858 1.00 70.33  ? 571  ILE A C   1 
ATOM   103  O O   . ILE A 1 21  ? 24.314  23.323  -17.874 1.00 68.69  ? 571  ILE A O   1 
ATOM   104  C CB  . ILE A 1 21  ? 22.853  25.537  -19.523 1.00 71.00  ? 571  ILE A CB  1 
ATOM   105  C CG1 . ILE A 1 21  ? 22.681  26.584  -20.635 1.00 71.51  ? 571  ILE A CG1 1 
ATOM   106  C CG2 . ILE A 1 21  ? 22.003  25.903  -18.305 1.00 71.23  ? 571  ILE A CG2 1 
ATOM   107  C CD1 . ILE A 1 21  ? 21.295  26.696  -21.195 1.00 72.35  ? 571  ILE A CD1 1 
ATOM   108  N N   . ASP A 1 22  ? 24.919  25.167  -16.769 1.00 70.95  ? 572  ASP A N   1 
ATOM   109  C CA  . ASP A 1 22  ? 25.063  24.498  -15.482 1.00 71.97  ? 572  ASP A CA  1 
ATOM   110  C C   . ASP A 1 22  ? 23.638  24.268  -14.948 1.00 71.63  ? 572  ASP A C   1 
ATOM   111  O O   . ASP A 1 22  ? 22.870  25.235  -14.785 1.00 71.56  ? 572  ASP A O   1 
ATOM   112  C CB  . ASP A 1 22  ? 25.850  25.421  -14.536 1.00 75.35  ? 572  ASP A CB  1 
ATOM   113  C CG  . ASP A 1 22  ? 26.164  24.845  -13.172 1.00 83.26  ? 572  ASP A CG  1 
ATOM   114  O OD1 . ASP A 1 22  ? 26.149  23.590  -13.028 1.00 84.14  ? 572  ASP A OD1 1 
ATOM   115  O OD2 . ASP A 1 22  ? 26.425  25.642  -12.242 1.00 87.34  ? 572  ASP A OD2 1 
ATOM   116  N N   . PRO A 1 23  ? 23.262  22.993  -14.696 1.00 70.56  ? 573  PRO A N   1 
ATOM   117  C CA  . PRO A 1 23  ? 21.886  22.718  -14.256 1.00 70.06  ? 573  PRO A CA  1 
ATOM   118  C C   . PRO A 1 23  ? 21.508  23.356  -12.939 1.00 70.13  ? 573  PRO A C   1 
ATOM   119  O O   . PRO A 1 23  ? 20.339  23.644  -12.753 1.00 70.69  ? 573  PRO A O   1 
ATOM   120  C CB  . PRO A 1 23  ? 21.792  21.185  -14.224 1.00 70.40  ? 573  PRO A CB  1 
ATOM   121  C CG  . PRO A 1 23  ? 23.170  20.691  -14.293 1.00 70.55  ? 573  PRO A CG  1 
ATOM   122  C CD  . PRO A 1 23  ? 24.045  21.756  -14.872 1.00 69.27  ? 573  PRO A CD  1 
ATOM   123  N N   . THR A 1 24  ? 22.468  23.620  -12.053 1.00 69.99  ? 574  THR A N   1 
ATOM   124  C CA  . THR A 1 24  ? 22.161  24.282  -10.777 1.00 71.00  ? 574  THR A CA  1 
ATOM   125  C C   . THR A 1 24  ? 21.642  25.720  -11.014 1.00 72.52  ? 574  THR A C   1 
ATOM   126  O O   . THR A 1 24  ? 20.949  26.263  -10.156 1.00 72.91  ? 574  THR A O   1 
ATOM   127  C CB  . THR A 1 24  ? 23.399  24.340  -9.886  1.00 71.66  ? 574  THR A CB  1 
ATOM   128  O OG1 . THR A 1 24  ? 24.397  25.112  -10.549 1.00 72.86  ? 574  THR A OG1 1 
ATOM   129  C CG2 . THR A 1 24  ? 23.931  22.968  -9.507  1.00 71.32  ? 574  THR A CG2 1 
ATOM   130  N N   . GLN A 1 25  ? 22.037  26.338  -12.165 1.00 72.79  ? 575  GLN A N   1 
ATOM   131  C CA  . GLN A 1 25  ? 21.654  27.661  -12.632 1.00 72.97  ? 575  GLN A CA  1 
ATOM   132  C C   . GLN A 1 25  ? 20.249  27.687  -13.231 1.00 72.75  ? 575  GLN A C   1 
ATOM   133  O O   . GLN A 1 25  ? 19.686  28.767  -13.342 1.00 73.55  ? 575  GLN A O   1 
ATOM   134  C CB  . GLN A 1 25  ? 22.657  28.167  -13.665 1.00 75.23  ? 575  GLN A CB  1 
ATOM   135  C CG  . GLN A 1 25  ? 23.978  28.632  -13.075 1.00 80.71  ? 575  GLN A CG  1 
ATOM   136  C CD  . GLN A 1 25  ? 24.876  29.140  -14.180 1.00 88.13  ? 575  GLN A CD  1 
ATOM   137  O OE1 . GLN A 1 25  ? 24.921  28.575  -15.293 1.00 90.16  ? 575  GLN A OE1 1 
ATOM   138  N NE2 . GLN A 1 25  ? 25.607  30.227  -13.905 1.00 89.38  ? 575  GLN A NE2 1 
ATOM   139  N N   . LEU A 1 26  ? 19.671  26.532  -13.615 1.00 71.88  ? 576  LEU A N   1 
ATOM   140  C CA  . LEU A 1 26  ? 18.304  26.502  -14.137 1.00 72.16  ? 576  LEU A CA  1 
ATOM   141  C C   . LEU A 1 26  ? 17.308  26.809  -13.004 1.00 72.93  ? 576  LEU A C   1 
ATOM   142  O O   . LEU A 1 26  ? 17.634  26.641  -11.825 1.00 73.72  ? 576  LEU A O   1 
ATOM   143  C CB  . LEU A 1 26  ? 18.001  25.130  -14.760 1.00 72.33  ? 576  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 26  ? 18.661  24.869  -16.107 1.00 72.94  ? 576  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 26  ? 18.503  23.418  -16.518 1.00 73.14  ? 576  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 26  ? 18.135  25.814  -17.157 1.00 73.06  ? 576  LEU A CD2 1 
ATOM   147  N N   . PRO A 1 27  ? 16.090  27.283  -13.318 1.00 72.50  ? 577  PRO A N   1 
ATOM   148  C CA  . PRO A 1 27  ? 15.137  27.608  -12.236 1.00 72.01  ? 577  PRO A CA  1 
ATOM   149  C C   . PRO A 1 27  ? 14.269  26.438  -11.730 1.00 72.19  ? 577  PRO A C   1 
ATOM   150  O O   . PRO A 1 27  ? 13.995  25.459  -12.453 1.00 71.27  ? 577  PRO A O   1 
ATOM   151  C CB  . PRO A 1 27  ? 14.262  28.672  -12.877 1.00 72.41  ? 577  PRO A CB  1 
ATOM   152  C CG  . PRO A 1 27  ? 14.227  28.287  -14.333 1.00 72.86  ? 577  PRO A CG  1 
ATOM   153  C CD  . PRO A 1 27  ? 15.521  27.576  -14.652 1.00 71.60  ? 577  PRO A CD  1 
ATOM   154  N N   . TYR A 1 28  ? 13.825  26.546  -10.463 1.00 72.40  ? 578  TYR A N   1 
ATOM   155  C CA  . TYR A 1 28  ? 12.864  25.588  -9.929  1.00 72.95  ? 578  TYR A CA  1 
ATOM   156  C C   . TYR A 1 28  ? 11.555  26.335  -9.673  1.00 72.92  ? 578  TYR A C   1 
ATOM   157  O O   . TYR A 1 28  ? 11.408  27.036  -8.671  1.00 72.44  ? 578  TYR A O   1 
ATOM   158  C CB  . TYR A 1 28  ? 13.327  24.843  -8.670  1.00 73.18  ? 578  TYR A CB  1 
ATOM   159  C CG  . TYR A 1 28  ? 12.223  23.957  -8.129  1.00 73.90  ? 578  TYR A CG  1 
ATOM   160  C CD1 . TYR A 1 28  ? 11.623  22.997  -8.929  1.00 75.05  ? 578  TYR A CD1 1 
ATOM   161  C CD2 . TYR A 1 28  ? 11.716  24.146  -6.855  1.00 74.77  ? 578  TYR A CD2 1 
ATOM   162  C CE1 . TYR A 1 28  ? 10.564  22.229  -8.463  1.00 76.03  ? 578  TYR A CE1 1 
ATOM   163  C CE2 . TYR A 1 28  ? 10.681  23.363  -6.366  1.00 75.64  ? 578  TYR A CE2 1 
ATOM   164  C CZ  . TYR A 1 28  ? 10.098  22.411  -7.177  1.00 76.62  ? 578  TYR A CZ  1 
ATOM   165  O OH  . TYR A 1 28  ? 9.050   21.653  -6.714  1.00 77.92  ? 578  TYR A OH  1 
ATOM   166  N N   . ASP A 1 29  ? 10.618  26.167  -10.593 1.00 73.46  ? 579  ASP A N   1 
ATOM   167  C CA  . ASP A 1 29  ? 9.290   26.754  -10.542 1.00 74.40  ? 579  ASP A CA  1 
ATOM   168  C C   . ASP A 1 29  ? 8.517   26.080  -9.404  1.00 73.93  ? 579  ASP A C   1 
ATOM   169  O O   . ASP A 1 29  ? 8.317   24.868  -9.410  1.00 72.77  ? 579  ASP A O   1 
ATOM   170  C CB  . ASP A 1 29  ? 8.602   26.500  -11.891 1.00 77.76  ? 579  ASP A CB  1 
ATOM   171  C CG  . ASP A 1 29  ? 7.419   27.393  -12.203 1.00 85.23  ? 579  ASP A CG  1 
ATOM   172  O OD1 . ASP A 1 29  ? 6.891   28.051  -11.256 1.00 86.35  ? 579  ASP A OD1 1 
ATOM   173  O OD2 . ASP A 1 29  ? 6.992   27.415  -13.385 1.00 88.56  ? 579  ASP A OD2 1 
ATOM   174  N N   . HIS A 1 30  ? 8.098   26.869  -8.424  1.00 74.71  ? 580  HIS A N   1 
ATOM   175  C CA  . HIS A 1 30  ? 7.374   26.328  -7.276  1.00 76.19  ? 580  HIS A CA  1 
ATOM   176  C C   . HIS A 1 30  ? 5.922   25.945  -7.601  1.00 74.58  ? 580  HIS A C   1 
ATOM   177  O O   . HIS A 1 30  ? 5.219   25.457  -6.722  1.00 74.76  ? 580  HIS A O   1 
ATOM   178  C CB  . HIS A 1 30  ? 7.488   27.254  -6.068  1.00 80.33  ? 580  HIS A CB  1 
ATOM   179  C CG  . HIS A 1 30  ? 8.922   27.589  -5.789  1.00 87.72  ? 580  HIS A CG  1 
ATOM   180  N ND1 . HIS A 1 30  ? 9.450   28.845  -6.099  1.00 90.97  ? 580  HIS A ND1 1 
ATOM   181  C CD2 . HIS A 1 30  ? 9.929   26.775  -5.387  1.00 90.05  ? 580  HIS A CD2 1 
ATOM   182  C CE1 . HIS A 1 30  ? 10.739  28.773  -5.803  1.00 92.17  ? 580  HIS A CE1 1 
ATOM   183  N NE2 . HIS A 1 30  ? 11.080  27.540  -5.389  1.00 92.16  ? 580  HIS A NE2 1 
ATOM   184  N N   . LYS A 1 31  ? 5.511   26.053  -8.877  1.00 72.75  ? 581  LYS A N   1 
ATOM   185  C CA  . LYS A 1 31  ? 4.229   25.551  -9.327  1.00 71.50  ? 581  LYS A CA  1 
ATOM   186  C C   . LYS A 1 31  ? 4.208   23.989  -9.241  1.00 69.91  ? 581  LYS A C   1 
ATOM   187  O O   . LYS A 1 31  ? 3.130   23.409  -9.159  1.00 70.87  ? 581  LYS A O   1 
ATOM   188  C CB  . LYS A 1 31  ? 3.931   26.038  -10.761 1.00 73.33  ? 581  LYS A CB  1 
ATOM   189  C CG  . LYS A 1 31  ? 4.649   25.284  -11.876 1.00 77.70  ? 581  LYS A CG  1 
ATOM   190  C CD  . LYS A 1 31  ? 4.084   25.635  -13.250 1.00 81.96  ? 581  LYS A CD  1 
ATOM   191  C CE  . LYS A 1 31  ? 4.696   24.774  -14.323 1.00 86.22  ? 581  LYS A CE  1 
ATOM   192  N NZ  . LYS A 1 31  ? 4.311   25.236  -15.679 1.00 88.90  ? 581  LYS A NZ  1 
ATOM   193  N N   . TRP A 1 32  ? 5.384   23.326  -9.246  1.00 67.36  ? 582  TRP A N   1 
ATOM   194  C CA  . TRP A 1 32  ? 5.521   21.867  -9.145  1.00 65.84  ? 582  TRP A CA  1 
ATOM   195  C C   . TRP A 1 32  ? 5.418   21.356  -7.712  1.00 65.60  ? 582  TRP A C   1 
ATOM   196  O O   . TRP A 1 32  ? 5.189   20.161  -7.512  1.00 65.70  ? 582  TRP A O   1 
ATOM   197  C CB  . TRP A 1 32  ? 6.878   21.403  -9.701  1.00 64.71  ? 582  TRP A CB  1 
ATOM   198  C CG  . TRP A 1 32  ? 7.068   21.664  -11.163 1.00 63.80  ? 582  TRP A CG  1 
ATOM   199  C CD1 . TRP A 1 32  ? 7.966   22.517  -11.733 1.00 64.26  ? 582  TRP A CD1 1 
ATOM   200  C CD2 . TRP A 1 32  ? 6.350   21.054  -12.241 1.00 63.02  ? 582  TRP A CD2 1 
ATOM   201  N NE1 . TRP A 1 32  ? 7.876   22.446  -13.102 1.00 64.36  ? 582  TRP A NE1 1 
ATOM   202  C CE2 . TRP A 1 32  ? 6.875   21.573  -13.441 1.00 63.70  ? 582  TRP A CE2 1 
ATOM   203  C CE3 . TRP A 1 32  ? 5.333   20.095  -12.311 1.00 63.10  ? 582  TRP A CE3 1 
ATOM   204  C CZ2 . TRP A 1 32  ? 6.402   21.182  -14.693 1.00 63.88  ? 582  TRP A CZ2 1 
ATOM   205  C CZ3 . TRP A 1 32  ? 4.841   19.734  -13.548 1.00 63.80  ? 582  TRP A CZ3 1 
ATOM   206  C CH2 . TRP A 1 32  ? 5.380   20.264  -14.722 1.00 63.90  ? 582  TRP A CH2 1 
ATOM   207  N N   . GLU A 1 33  ? 5.614   22.236  -6.715  1.00 64.91  ? 583  GLU A N   1 
ATOM   208  C CA  . GLU A 1 33  ? 5.581   21.838  -5.314  1.00 64.45  ? 583  GLU A CA  1 
ATOM   209  C C   . GLU A 1 33  ? 4.299   21.136  -4.921  1.00 64.54  ? 583  GLU A C   1 
ATOM   210  O O   . GLU A 1 33  ? 3.216   21.646  -5.177  1.00 64.28  ? 583  GLU A O   1 
ATOM   211  C CB  . GLU A 1 33  ? 5.876   23.019  -4.398  1.00 64.82  ? 583  GLU A CB  1 
ATOM   212  C CG  . GLU A 1 33  ? 6.408   22.595  -3.048  1.00 66.53  ? 583  GLU A CG  1 
ATOM   213  C CD  . GLU A 1 33  ? 7.726   21.844  -3.055  1.00 67.80  ? 583  GLU A CD  1 
ATOM   214  O OE1 . GLU A 1 33  ? 8.578   22.125  -3.931  1.00 66.43  ? 583  GLU A OE1 1 
ATOM   215  O OE2 . GLU A 1 33  ? 7.921   20.991  -2.157  1.00 68.65  ? 583  GLU A OE2 1 
ATOM   216  N N   . PHE A 1 34  ? 4.443   19.919  -4.380  1.00 64.89  ? 584  PHE A N   1 
ATOM   217  C CA  . PHE A 1 34  ? 3.348   19.064  -3.958  1.00 65.86  ? 584  PHE A CA  1 
ATOM   218  C C   . PHE A 1 34  ? 3.620   18.552  -2.540  1.00 68.73  ? 584  PHE A C   1 
ATOM   219  O O   . PHE A 1 34  ? 4.751   18.185  -2.221  1.00 69.40  ? 584  PHE A O   1 
ATOM   220  C CB  . PHE A 1 34  ? 3.210   17.870  -4.930  1.00 64.55  ? 584  PHE A CB  1 
ATOM   221  C CG  . PHE A 1 34  ? 2.073   16.900  -4.672  1.00 63.58  ? 584  PHE A CG  1 
ATOM   222  C CD1 . PHE A 1 34  ? 0.760   17.260  -4.928  1.00 63.47  ? 584  PHE A CD1 1 
ATOM   223  C CD2 . PHE A 1 34  ? 2.324   15.622  -4.220  1.00 64.00  ? 584  PHE A CD2 1 
ATOM   224  C CE1 . PHE A 1 34  ? -0.276  16.375  -4.711  1.00 63.98  ? 584  PHE A CE1 1 
ATOM   225  C CE2 . PHE A 1 34  ? 1.281   14.731  -4.005  1.00 64.66  ? 584  PHE A CE2 1 
ATOM   226  C CZ  . PHE A 1 34  ? -0.013  15.110  -4.260  1.00 64.20  ? 584  PHE A CZ  1 
ATOM   227  N N   . PRO A 1 35  ? 2.589   18.507  -1.677  1.00 69.92  ? 585  PRO A N   1 
ATOM   228  C CA  . PRO A 1 35  ? 2.801   17.999  -0.325  1.00 71.11  ? 585  PRO A CA  1 
ATOM   229  C C   . PRO A 1 35  ? 2.961   16.475  -0.268  1.00 72.90  ? 585  PRO A C   1 
ATOM   230  O O   . PRO A 1 35  ? 2.113   15.705  -0.708  1.00 73.13  ? 585  PRO A O   1 
ATOM   231  C CB  . PRO A 1 35  ? 1.555   18.479  0.418   1.00 71.84  ? 585  PRO A CB  1 
ATOM   232  C CG  . PRO A 1 35  ? 0.514   18.540  -0.631  1.00 71.71  ? 585  PRO A CG  1 
ATOM   233  C CD  . PRO A 1 35  ? 1.196   18.957  -1.879  1.00 69.57  ? 585  PRO A CD  1 
ATOM   234  N N   . ARG A 1 36  ? 4.083   16.063  0.296   1.00 73.80  ? 586  ARG A N   1 
ATOM   235  C CA  . ARG A 1 36  ? 4.559   14.710  0.544   1.00 74.70  ? 586  ARG A CA  1 
ATOM   236  C C   . ARG A 1 36  ? 3.515   13.846  1.253   1.00 76.01  ? 586  ARG A C   1 
ATOM   237  O O   . ARG A 1 36  ? 3.415   12.648  0.974   1.00 76.62  ? 586  ARG A O   1 
ATOM   238  C CB  . ARG A 1 36  ? 5.738   14.896  1.491   1.00 75.94  ? 586  ARG A CB  1 
ATOM   239  C CG  . ARG A 1 36  ? 6.729   13.764  1.647   1.00 77.32  ? 586  ARG A CG  1 
ATOM   240  C CD  . ARG A 1 36  ? 7.830   14.296  2.564   1.00 77.10  ? 586  ARG A CD  1 
ATOM   241  N NE  . ARG A 1 36  ? 8.464   15.489  1.989   1.00 75.45  ? 586  ARG A NE  1 
ATOM   242  C CZ  . ARG A 1 36  ? 9.608   15.477  1.319   1.00 72.38  ? 586  ARG A CZ  1 
ATOM   243  N NH1 . ARG A 1 36  ? 10.304  14.355  1.203   1.00 69.33  ? 586  ARG A NH1 1 
ATOM   244  N NH2 . ARG A 1 36  ? 10.098  16.598  0.819   1.00 71.56  ? 586  ARG A NH2 1 
ATOM   245  N N   . ASN A 1 37  ? 2.751   14.434  2.195   1.00 76.25  ? 587  ASN A N   1 
ATOM   246  C CA  . ASN A 1 37  ? 1.753   13.658  2.934   1.00 76.88  ? 587  ASN A CA  1 
ATOM   247  C C   . ASN A 1 37  ? 0.536   13.255  2.080   1.00 77.01  ? 587  ASN A C   1 
ATOM   248  O O   . ASN A 1 37  ? -0.300  12.488  2.562   1.00 77.46  ? 587  ASN A O   1 
ATOM   249  C CB  . ASN A 1 37  ? 1.340   14.329  4.238   1.00 78.40  ? 587  ASN A CB  1 
ATOM   250  C CG  . ASN A 1 37  ? 0.457   15.540  4.101   1.00 83.13  ? 587  ASN A CG  1 
ATOM   251  O OD1 . ASN A 1 37  ? 0.456   16.248  3.078   1.00 84.97  ? 587  ASN A OD1 1 
ATOM   252  N ND2 . ASN A 1 37  ? -0.302  15.817  5.161   1.00 84.31  ? 587  ASN A ND2 1 
ATOM   253  N N   . ARG A 1 38  ? 0.452   13.733  0.819   1.00 76.47  ? 588  ARG A N   1 
ATOM   254  C CA  . ARG A 1 38  ? -0.572  13.297  -0.128  1.00 76.65  ? 588  ARG A CA  1 
ATOM   255  C C   . ARG A 1 38  ? 0.010   12.270  -1.123  1.00 75.86  ? 588  ARG A C   1 
ATOM   256  O O   . ARG A 1 38  ? -0.474  12.162  -2.239  1.00 76.19  ? 588  ARG A O   1 
ATOM   257  C CB  . ARG A 1 38  ? -1.184  14.464  -0.895  1.00 79.45  ? 588  ARG A CB  1 
ATOM   258  C CG  . ARG A 1 38  ? -1.726  15.558  -0.013  1.00 85.62  ? 588  ARG A CG  1 
ATOM   259  C CD  . ARG A 1 38  ? -2.558  16.520  -0.826  1.00 92.01  ? 588  ARG A CD  1 
ATOM   260  N NE  . ARG A 1 38  ? -2.869  17.725  -0.057  1.00 98.92  ? 588  ARG A NE  1 
ATOM   261  C CZ  . ARG A 1 38  ? -3.012  18.937  -0.589  1.00 104.04 ? 588  ARG A CZ  1 
ATOM   262  N NH1 . ARG A 1 38  ? -2.859  19.119  -1.900  1.00 104.46 ? 588  ARG A NH1 1 
ATOM   263  N NH2 . ARG A 1 38  ? -3.291  19.981  0.186   1.00 104.85 ? 588  ARG A NH2 1 
ATOM   264  N N   . LEU A 1 39  ? 1.047   11.531  -0.725  1.00 74.83  ? 589  LEU A N   1 
ATOM   265  C CA  . LEU A 1 39  ? 1.640   10.454  -1.509  1.00 74.19  ? 589  LEU A CA  1 
ATOM   266  C C   . LEU A 1 39  ? 1.520   9.197   -0.672  1.00 74.47  ? 589  LEU A C   1 
ATOM   267  O O   . LEU A 1 39  ? 1.817   9.220   0.529   1.00 74.79  ? 589  LEU A O   1 
ATOM   268  C CB  . LEU A 1 39  ? 3.137   10.685  -1.743  1.00 73.41  ? 589  LEU A CB  1 
ATOM   269  C CG  . LEU A 1 39  ? 3.532   11.709  -2.754  1.00 73.48  ? 589  LEU A CG  1 
ATOM   270  C CD1 . LEU A 1 39  ? 5.001   11.974  -2.669  1.00 73.16  ? 589  LEU A CD1 1 
ATOM   271  C CD2 . LEU A 1 39  ? 3.107   11.289  -4.156  1.00 73.85  ? 589  LEU A CD2 1 
ATOM   272  N N   . SER A 1 40  ? 1.132   8.096   -1.294  1.00 74.30  ? 590  SER A N   1 
ATOM   273  C CA  . SER A 1 40  ? 1.073   6.809   -0.606  1.00 74.58  ? 590  SER A CA  1 
ATOM   274  C C   . SER A 1 40  ? 1.961   5.886   -1.415  1.00 74.45  ? 590  SER A C   1 
ATOM   275  O O   . SER A 1 40  ? 1.675   5.644   -2.586  1.00 74.74  ? 590  SER A O   1 
ATOM   276  C CB  . SER A 1 40  ? -0.355  6.280   -0.558  1.00 76.32  ? 590  SER A CB  1 
ATOM   277  O OG  . SER A 1 40  ? -0.354  5.036   0.124   1.00 79.88  ? 590  SER A OG  1 
ATOM   278  N N   . PHE A 1 41  ? 3.069   5.422   -0.836  1.00 74.26  ? 591  PHE A N   1 
ATOM   279  C CA  . PHE A 1 41  ? 4.038   4.622   -1.589  1.00 74.75  ? 591  PHE A CA  1 
ATOM   280  C C   . PHE A 1 41  ? 3.615   3.182   -1.800  1.00 75.97  ? 591  PHE A C   1 
ATOM   281  O O   . PHE A 1 41  ? 2.783   2.646   -1.076  1.00 76.91  ? 591  PHE A O   1 
ATOM   282  C CB  . PHE A 1 41  ? 5.440   4.711   -0.975  1.00 74.18  ? 591  PHE A CB  1 
ATOM   283  C CG  . PHE A 1 41  ? 5.969   6.120   -1.029  1.00 74.48  ? 591  PHE A CG  1 
ATOM   284  C CD1 . PHE A 1 41  ? 6.607   6.592   -2.161  1.00 75.01  ? 591  PHE A CD1 1 
ATOM   285  C CD2 . PHE A 1 41  ? 5.759   6.999   0.024   1.00 75.12  ? 591  PHE A CD2 1 
ATOM   286  C CE1 . PHE A 1 41  ? 7.047   7.907   -2.227  1.00 75.69  ? 591  PHE A CE1 1 
ATOM   287  C CE2 . PHE A 1 41  ? 6.202   8.311   -0.046  1.00 75.70  ? 591  PHE A CE2 1 
ATOM   288  C CZ  . PHE A 1 41  ? 6.858   8.752   -1.161  1.00 75.48  ? 591  PHE A CZ  1 
ATOM   289  N N   . GLY A 1 42  ? 4.164   2.586   -2.838  1.00 76.01  ? 592  GLY A N   1 
ATOM   290  C CA  . GLY A 1 42  ? 3.876   1.211   -3.195  1.00 76.25  ? 592  GLY A CA  1 
ATOM   291  C C   . GLY A 1 42  ? 5.154   0.447   -3.448  1.00 76.15  ? 592  GLY A C   1 
ATOM   292  O O   . GLY A 1 42  ? 6.154   0.631   -2.744  1.00 76.33  ? 592  GLY A O   1 
ATOM   293  N N   . LYS A 1 43  ? 5.124   -0.419  -4.452  1.00 75.50  ? 593  LYS A N   1 
ATOM   294  C CA  . LYS A 1 43  ? 6.261   -1.253  -4.780  1.00 75.28  ? 593  LYS A CA  1 
ATOM   295  C C   . LYS A 1 43  ? 7.412   -0.475  -5.424  1.00 74.13  ? 593  LYS A C   1 
ATOM   296  O O   . LYS A 1 43  ? 7.198   0.561   -6.048  1.00 73.17  ? 593  LYS A O   1 
ATOM   297  C CB  . LYS A 1 43  ? 5.795   -2.399  -5.690  1.00 78.31  ? 593  LYS A CB  1 
ATOM   298  C CG  . LYS A 1 43  ? 4.889   -3.387  -4.954  1.00 85.74  ? 593  LYS A CG  1 
ATOM   299  C CD  . LYS A 1 43  ? 4.211   -4.412  -5.897  1.00 92.86  ? 593  LYS A CD  1 
ATOM   300  C CE  . LYS A 1 43  ? 3.105   -5.185  -5.192  1.00 97.50  ? 593  LYS A CE  1 
ATOM   301  N NZ  . LYS A 1 43  ? 2.493   -6.237  -6.059  1.00 99.78  ? 593  LYS A NZ  1 
ATOM   302  N N   . THR A 1 44  ? 8.640   -0.993  -5.282  1.00 73.46  ? 594  THR A N   1 
ATOM   303  C CA  . THR A 1 44  ? 9.800   -0.402  -5.950  1.00 72.60  ? 594  THR A CA  1 
ATOM   304  C C   . THR A 1 44  ? 9.775   -0.915  -7.395  1.00 71.35  ? 594  THR A C   1 
ATOM   305  O O   . THR A 1 44  ? 9.622   -2.122  -7.621  1.00 71.29  ? 594  THR A O   1 
ATOM   306  C CB  . THR A 1 44  ? 11.082  -0.847  -5.259  1.00 73.25  ? 594  THR A CB  1 
ATOM   307  O OG1 . THR A 1 44  ? 11.092  -0.295  -3.951  1.00 73.91  ? 594  THR A OG1 1 
ATOM   308  C CG2 . THR A 1 44  ? 12.325  -0.430  -6.022  1.00 73.29  ? 594  THR A CG2 1 
ATOM   309  N N   . LEU A 1 45  ? 9.869   -0.000  -8.352  1.00 69.95  ? 595  LEU A N   1 
ATOM   310  C CA  . LEU A 1 45  ? 9.831   -0.265  -9.786  1.00 69.51  ? 595  LEU A CA  1 
ATOM   311  C C   . LEU A 1 45  ? 11.240  -0.503  -10.368 1.00 70.08  ? 595  LEU A C   1 
ATOM   312  O O   . LEU A 1 45  ? 11.403  -1.247  -11.344 1.00 71.43  ? 595  LEU A O   1 
ATOM   313  C CB  . LEU A 1 45  ? 9.177   0.926   -10.494 1.00 69.09  ? 595  LEU A CB  1 
ATOM   314  C CG  . LEU A 1 45  ? 7.749   1.277   -10.071 1.00 69.64  ? 595  LEU A CG  1 
ATOM   315  C CD1 . LEU A 1 45  ? 7.298   2.561   -10.730 1.00 69.78  ? 595  LEU A CD1 1 
ATOM   316  C CD2 . LEU A 1 45  ? 6.783   0.147   -10.412 1.00 69.97  ? 595  LEU A CD2 1 
ATOM   317  N N   . GLY A 1 46  ? 12.236  0.149   -9.783  1.00 68.80  ? 596  GLY A N   1 
ATOM   318  C CA  . GLY A 1 46  ? 13.633  0.056   -10.187 1.00 67.60  ? 596  GLY A CA  1 
ATOM   319  C C   . GLY A 1 46  ? 14.502  0.584   -9.073  1.00 66.56  ? 596  GLY A C   1 
ATOM   320  O O   . GLY A 1 46  ? 14.110  1.520   -8.378  1.00 66.20  ? 596  GLY A O   1 
ATOM   321  N N   . ALA A 1 47  ? 15.667  -0.013  -8.874  1.00 66.80  ? 597  ALA A N   1 
ATOM   322  C CA  . ALA A 1 47  ? 16.541  0.367   -7.764  1.00 67.74  ? 597  ALA A CA  1 
ATOM   323  C C   . ALA A 1 47  ? 17.995  0.083   -8.010  1.00 69.37  ? 597  ALA A C   1 
ATOM   324  O O   . ALA A 1 47  ? 18.375  -1.004  -8.457  1.00 70.04  ? 597  ALA A O   1 
ATOM   325  C CB  . ALA A 1 47  ? 16.099  -0.325  -6.471  1.00 66.89  ? 597  ALA A CB  1 
ATOM   326  N N   . GLY A 1 48  ? 18.806  1.045   -7.637  1.00 69.95  ? 598  GLY A N   1 
ATOM   327  C CA  . GLY A 1 48  ? 20.248  0.923   -7.724  1.00 71.21  ? 598  GLY A CA  1 
ATOM   328  C C   . GLY A 1 48  ? 20.857  0.993   -6.348  1.00 72.30  ? 598  GLY A C   1 
ATOM   329  O O   . GLY A 1 48  ? 20.165  0.776   -5.351  1.00 72.35  ? 598  GLY A O   1 
ATOM   330  N N   . ALA A 1 49  ? 22.148  1.319   -6.273  1.00 73.06  ? 599  ALA A N   1 
ATOM   331  C CA  . ALA A 1 49  ? 22.832  1.404   -4.982  1.00 73.84  ? 599  ALA A CA  1 
ATOM   332  C C   . ALA A 1 49  ? 22.433  2.666   -4.192  1.00 74.13  ? 599  ALA A C   1 
ATOM   333  O O   . ALA A 1 49  ? 22.348  2.637   -2.957  1.00 74.74  ? 599  ALA A O   1 
ATOM   334  C CB  . ALA A 1 49  ? 24.331  1.388   -5.202  1.00 74.04  ? 599  ALA A CB  1 
ATOM   335  N N   . PHE A 1 50  ? 22.177  3.766   -4.909  1.00 73.24  ? 600  PHE A N   1 
ATOM   336  C CA  . PHE A 1 50  ? 21.887  5.037   -4.269  1.00 72.63  ? 600  PHE A CA  1 
ATOM   337  C C   . PHE A 1 50  ? 20.525  5.621   -4.526  1.00 70.26  ? 600  PHE A C   1 
ATOM   338  O O   . PHE A 1 50  ? 20.166  6.595   -3.863  1.00 70.49  ? 600  PHE A O   1 
ATOM   339  C CB  . PHE A 1 50  ? 22.945  6.058   -4.676  1.00 73.78  ? 600  PHE A CB  1 
ATOM   340  C CG  . PHE A 1 50  ? 24.320  5.631   -4.252  1.00 75.98  ? 600  PHE A CG  1 
ATOM   341  C CD1 . PHE A 1 50  ? 24.612  5.406   -2.914  1.00 77.66  ? 600  PHE A CD1 1 
ATOM   342  C CD2 . PHE A 1 50  ? 25.318  5.429   -5.188  1.00 77.41  ? 600  PHE A CD2 1 
ATOM   343  C CE1 . PHE A 1 50  ? 25.876  4.995   -2.523  1.00 78.55  ? 600  PHE A CE1 1 
ATOM   344  C CE2 . PHE A 1 50  ? 26.590  5.032   -4.793  1.00 78.54  ? 600  PHE A CE2 1 
ATOM   345  C CZ  . PHE A 1 50  ? 26.857  4.810   -3.465  1.00 78.51  ? 600  PHE A CZ  1 
ATOM   346  N N   . GLY A 1 51  ? 19.796  5.081   -5.490  1.00 67.74  ? 601  GLY A N   1 
ATOM   347  C CA  . GLY A 1 51  ? 18.486  5.609   -5.815  1.00 66.01  ? 601  GLY A CA  1 
ATOM   348  C C   . GLY A 1 51  ? 17.463  4.558   -6.162  1.00 64.49  ? 601  GLY A C   1 
ATOM   349  O O   . GLY A 1 51  ? 17.784  3.382   -6.372  1.00 64.27  ? 601  GLY A O   1 
ATOM   350  N N   . LYS A 1 52  ? 16.216  4.993   -6.224  1.00 63.00  ? 602  LYS A N   1 
ATOM   351  C CA  . LYS A 1 52  ? 15.128  4.130   -6.608  1.00 61.91  ? 602  LYS A CA  1 
ATOM   352  C C   . LYS A 1 52  ? 13.949  4.899   -7.198  1.00 59.92  ? 602  LYS A C   1 
ATOM   353  O O   . LYS A 1 52  ? 13.811  6.096   -6.982  1.00 58.80  ? 602  LYS A O   1 
ATOM   354  C CB  . LYS A 1 52  ? 14.684  3.263   -5.423  1.00 64.41  ? 602  LYS A CB  1 
ATOM   355  C CG  . LYS A 1 52  ? 14.116  4.040   -4.255  1.00 68.66  ? 602  LYS A CG  1 
ATOM   356  C CD  . LYS A 1 52  ? 13.643  3.070   -3.203  1.00 73.18  ? 602  LYS A CD  1 
ATOM   357  C CE  . LYS A 1 52  ? 13.368  3.751   -1.884  1.00 77.70  ? 602  LYS A CE  1 
ATOM   358  N NZ  . LYS A 1 52  ? 13.074  2.752   -0.812  1.00 80.25  ? 602  LYS A NZ  1 
ATOM   359  N N   . VAL A 1 53  ? 13.124  4.189   -7.979  1.00 59.67  ? 603  VAL A N   1 
ATOM   360  C CA  . VAL A 1 53  ? 11.861  4.660   -8.524  1.00 59.89  ? 603  VAL A CA  1 
ATOM   361  C C   . VAL A 1 53  ? 10.820  3.741   -7.924  1.00 60.43  ? 603  VAL A C   1 
ATOM   362  O O   . VAL A 1 53  ? 10.919  2.531   -8.047  1.00 59.99  ? 603  VAL A O   1 
ATOM   363  C CB  . VAL A 1 53  ? 11.790  4.663   -10.053 1.00 60.32  ? 603  VAL A CB  1 
ATOM   364  C CG1 . VAL A 1 53  ? 10.428  5.171   -10.517 1.00 60.82  ? 603  VAL A CG1 1 
ATOM   365  C CG2 . VAL A 1 53  ? 12.906  5.510   -10.642 1.00 60.52  ? 603  VAL A CG2 1 
ATOM   366  N N   . VAL A 1 54  ? 9.878   4.317   -7.202  1.00 61.19  ? 604  VAL A N   1 
ATOM   367  C CA  . VAL A 1 54  ? 8.835   3.617   -6.468  1.00 62.22  ? 604  VAL A CA  1 
ATOM   368  C C   . VAL A 1 54  ? 7.483   4.013   -7.039  1.00 63.45  ? 604  VAL A C   1 
ATOM   369  O O   . VAL A 1 54  ? 7.260   5.181   -7.335  1.00 63.32  ? 604  VAL A O   1 
ATOM   370  C CB  . VAL A 1 54  ? 8.903   4.034   -4.961  1.00 63.63  ? 604  VAL A CB  1 
ATOM   371  C CG1 . VAL A 1 54  ? 7.984   3.166   -4.094  1.00 64.83  ? 604  VAL A CG1 1 
ATOM   372  C CG2 . VAL A 1 54  ? 10.335  3.994   -4.411  1.00 64.15  ? 604  VAL A CG2 1 
ATOM   373  N N   . GLU A 1 55  ? 6.574   3.063   -7.192  1.00 64.65  ? 605  GLU A N   1 
ATOM   374  C CA  . GLU A 1 55  ? 5.202   3.353   -7.612  1.00 66.48  ? 605  GLU A CA  1 
ATOM   375  C C   . GLU A 1 55  ? 4.511   4.058   -6.422  1.00 67.11  ? 605  GLU A C   1 
ATOM   376  O O   . GLU A 1 55  ? 4.843   3.789   -5.268  1.00 67.11  ? 605  GLU A O   1 
ATOM   377  C CB  . GLU A 1 55  ? 4.479   2.029   -7.940  1.00 71.09  ? 605  GLU A CB  1 
ATOM   378  C CG  . GLU A 1 55  ? 3.015   2.151   -8.345  1.00 79.82  ? 605  GLU A CG  1 
ATOM   379  C CD  . GLU A 1 55  ? 2.335   0.821   -8.619  1.00 91.84  ? 605  GLU A CD  1 
ATOM   380  O OE1 . GLU A 1 55  ? 1.086   0.767   -8.527  1.00 95.01  ? 605  GLU A OE1 1 
ATOM   381  O OE2 . GLU A 1 55  ? 3.046   -0.169  -8.922  1.00 95.46  ? 605  GLU A OE2 1 
ATOM   382  N N   . ALA A 1 56  ? 3.578   4.973   -6.689  1.00 67.61  ? 606  ALA A N   1 
ATOM   383  C CA  . ALA A 1 56  ? 2.875   5.686   -5.617  1.00 68.34  ? 606  ALA A CA  1 
ATOM   384  C C   . ALA A 1 56  ? 1.484   6.154   -6.072  1.00 69.31  ? 606  ALA A C   1 
ATOM   385  O O   . ALA A 1 56  ? 1.186   6.138   -7.267  1.00 69.41  ? 606  ALA A O   1 
ATOM   386  C CB  . ALA A 1 56  ? 3.718   6.868   -5.122  1.00 67.80  ? 606  ALA A CB  1 
ATOM   387  N N   . THR A 1 57  ? 0.610   6.492   -5.116  1.00 69.62  ? 607  THR A N   1 
ATOM   388  C CA  . THR A 1 57  ? -0.688  7.066   -5.418  1.00 70.39  ? 607  THR A CA  1 
ATOM   389  C C   . THR A 1 57  ? -0.598  8.504   -4.901  1.00 71.07  ? 607  THR A C   1 
ATOM   390  O O   . THR A 1 57  ? -0.360  8.718   -3.717  1.00 71.04  ? 607  THR A O   1 
ATOM   391  C CB  . THR A 1 57  ? -1.871  6.277   -4.783  1.00 71.32  ? 607  THR A CB  1 
ATOM   392  O OG1 . THR A 1 57  ? -1.880  4.916   -5.240  1.00 72.48  ? 607  THR A OG1 1 
ATOM   393  C CG2 . THR A 1 57  ? -3.212  6.896   -5.118  1.00 71.36  ? 607  THR A CG2 1 
ATOM   394  N N   . ALA A 1 58  ? -0.702  9.481   -5.797  1.00 71.76  ? 608  ALA A N   1 
ATOM   395  C CA  . ALA A 1 58  ? -0.680  10.889  -5.418  1.00 72.87  ? 608  ALA A CA  1 
ATOM   396  C C   . ALA A 1 58  ? -2.137  11.375  -5.371  1.00 74.54  ? 608  ALA A C   1 
ATOM   397  O O   . ALA A 1 58  ? -2.912  11.098  -6.291  1.00 75.00  ? 608  ALA A O   1 
ATOM   398  C CB  . ALA A 1 58  ? 0.111   11.688  -6.441  1.00 72.78  ? 608  ALA A CB  1 
ATOM   399  N N   . TYR A 1 59  ? -2.526  12.042  -4.291  1.00 75.50  ? 609  TYR A N   1 
ATOM   400  C CA  . TYR A 1 59  ? -3.897  12.522  -4.126  1.00 77.35  ? 609  TYR A CA  1 
ATOM   401  C C   . TYR A 1 59  ? -4.056  14.014  -4.460  1.00 77.82  ? 609  TYR A C   1 
ATOM   402  O O   . TYR A 1 59  ? -3.494  14.879  -3.780  1.00 77.80  ? 609  TYR A O   1 
ATOM   403  C CB  . TYR A 1 59  ? -4.397  12.219  -2.708  1.00 78.63  ? 609  TYR A CB  1 
ATOM   404  C CG  . TYR A 1 59  ? -4.451  10.734  -2.428  1.00 81.33  ? 609  TYR A CG  1 
ATOM   405  C CD1 . TYR A 1 59  ? -3.314  10.036  -2.041  1.00 83.10  ? 609  TYR A CD1 1 
ATOM   406  C CD2 . TYR A 1 59  ? -5.632  10.023  -2.575  1.00 83.11  ? 609  TYR A CD2 1 
ATOM   407  C CE1 . TYR A 1 59  ? -3.344  8.660   -1.843  1.00 84.57  ? 609  TYR A CE1 1 
ATOM   408  C CE2 . TYR A 1 59  ? -5.680  8.650   -2.359  1.00 84.75  ? 609  TYR A CE2 1 
ATOM   409  C CZ  . TYR A 1 59  ? -4.532  7.969   -1.992  1.00 86.11  ? 609  TYR A CZ  1 
ATOM   410  O OH  . TYR A 1 59  ? -4.580  6.602   -1.790  1.00 88.44  ? 609  TYR A OH  1 
ATOM   411  N N   . GLY A 1 60  ? -4.814  14.295  -5.511  1.00 78.10  ? 610  GLY A N   1 
ATOM   412  C CA  . GLY A 1 60  ? -5.072  15.656  -5.957  1.00 79.41  ? 610  GLY A CA  1 
ATOM   413  C C   . GLY A 1 60  ? -3.886  16.328  -6.614  1.00 81.10  ? 610  GLY A C   1 
ATOM   414  O O   . GLY A 1 60  ? -3.621  17.503  -6.360  1.00 80.82  ? 610  GLY A O   1 
ATOM   415  N N   . LEU A 1 61  ? -3.169  15.590  -7.482  1.00 82.87  ? 611  LEU A N   1 
ATOM   416  C CA  . LEU A 1 61  ? -2.000  16.117  -8.173  1.00 84.69  ? 611  LEU A CA  1 
ATOM   417  C C   . LEU A 1 61  ? -2.390  16.967  -9.403  1.00 87.54  ? 611  LEU A C   1 
ATOM   418  O O   . LEU A 1 61  ? -2.149  18.172  -9.384  1.00 87.88  ? 611  LEU A O   1 
ATOM   419  C CB  . LEU A 1 61  ? -1.007  14.987  -8.499  1.00 84.36  ? 611  LEU A CB  1 
ATOM   420  C CG  . LEU A 1 61  ? 0.317   15.367  -9.184  1.00 85.32  ? 611  LEU A CG  1 
ATOM   421  C CD1 . LEU A 1 61  ? 1.021   16.501  -8.481  1.00 85.65  ? 611  LEU A CD1 1 
ATOM   422  C CD2 . LEU A 1 61  ? 1.244   14.192  -9.237  1.00 85.69  ? 611  LEU A CD2 1 
ATOM   423  N N   . ILE A 1 62  ? -2.995  16.342  -10.417 1.00 89.59  ? 612  ILE A N   1 
ATOM   424  C CA  . ILE A 1 62  ? -3.479  17.109  -11.605 1.00 92.43  ? 612  ILE A CA  1 
ATOM   425  C C   . ILE A 1 62  ? -4.898  17.591  -11.292 1.00 95.74  ? 612  ILE A C   1 
ATOM   426  O O   . ILE A 1 62  ? -5.086  18.816  -11.159 1.00 96.24  ? 612  ILE A O   1 
ATOM   427  C CB  . ILE A 1 62  ? -3.425  16.244  -12.880 1.00 92.90  ? 612  ILE A CB  1 
ATOM   428  C CG1 . ILE A 1 62  ? -2.044  15.612  -13.074 1.00 93.75  ? 612  ILE A CG1 1 
ATOM   429  C CG2 . ILE A 1 62  ? -3.849  17.050  -14.097 1.00 93.24  ? 612  ILE A CG2 1 
ATOM   430  C CD1 . ILE A 1 62  ? -0.928  16.615  -13.247 1.00 95.03  ? 612  ILE A CD1 1 
ATOM   431  N N   . LYS A 1 63  ? -5.854  16.664  -11.174 1.00 97.48  ? 613  LYS A N   1 
ATOM   432  C CA  . LYS A 1 63  ? -7.238  17.042  -10.777 1.00 99.32  ? 613  LYS A CA  1 
ATOM   433  C C   . LYS A 1 63  ? -7.220  17.417  -9.293  1.00 100.75 ? 613  LYS A C   1 
ATOM   434  O O   . LYS A 1 63  ? -6.349  16.897  -8.579  1.00 100.80 ? 613  LYS A O   1 
ATOM   435  C CB  . LYS A 1 63  ? -8.217  15.909  -11.092 1.00 101.92 ? 613  LYS A CB  1 
ATOM   436  C CG  . LYS A 1 63  ? -7.968  15.189  -12.410 1.00 106.34 ? 613  LYS A CG  1 
ATOM   437  C CD  . LYS A 1 63  ? -9.234  14.920  -13.193 1.00 110.50 ? 613  LYS A CD  1 
ATOM   438  C CE  . LYS A 1 63  ? -10.489 15.307  -12.442 1.00 113.90 ? 613  LYS A CE  1 
ATOM   439  N NZ  . LYS A 1 63  ? -11.706 14.756  -13.084 1.00 115.67 ? 613  LYS A NZ  1 
ATOM   440  N N   . SER A 1 64  ? -8.146  18.269  -8.844  1.00 101.84 ? 614  SER A N   1 
ATOM   441  C CA  . SER A 1 64  ? -8.101  18.768  -7.442  1.00 103.14 ? 614  SER A CA  1 
ATOM   442  C C   . SER A 1 64  ? -8.253  17.646  -6.408  1.00 103.45 ? 614  SER A C   1 
ATOM   443  O O   . SER A 1 64  ? -7.529  17.696  -5.396  1.00 104.03 ? 614  SER A O   1 
ATOM   444  C CB  . SER A 1 64  ? -9.132  19.846  -7.226  1.00 105.09 ? 614  SER A CB  1 
ATOM   445  O OG  . SER A 1 64  ? -9.555  19.875  -5.871  1.00 107.96 ? 614  SER A OG  1 
ATOM   446  N N   . ASP A 1 65  ? -9.173  16.700  -6.617  1.00 102.66 ? 615  ASP A N   1 
ATOM   447  C CA  . ASP A 1 65  ? -9.416  15.662  -5.575  1.00 102.43 ? 615  ASP A CA  1 
ATOM   448  C C   . ASP A 1 65  ? -9.192  14.245  -6.116  1.00 100.78 ? 615  ASP A C   1 
ATOM   449  O O   . ASP A 1 65  ? -9.573  13.294  -5.407  1.00 101.10 ? 615  ASP A O   1 
ATOM   450  C CB  . ASP A 1 65  ? -10.808 15.817  -4.958  1.00 105.45 ? 615  ASP A CB  1 
ATOM   451  C CG  . ASP A 1 65  ? -10.995 17.134  -4.227  1.00 113.07 ? 615  ASP A CG  1 
ATOM   452  O OD1 . ASP A 1 65  ? -10.423 17.280  -3.129  1.00 114.27 ? 615  ASP A OD1 1 
ATOM   453  O OD2 . ASP A 1 65  ? -11.705 18.006  -4.765  1.00 116.56 ? 615  ASP A OD2 1 
ATOM   454  N N   . ALA A 1 66  ? -8.599  14.095  -7.303  1.00 98.46  ? 616  ALA A N   1 
ATOM   455  C CA  . ALA A 1 66  ? -8.485  12.742  -7.900  1.00 96.17  ? 616  ALA A CA  1 
ATOM   456  C C   . ALA A 1 66  ? -7.176  12.049  -7.515  1.00 93.38  ? 616  ALA A C   1 
ATOM   457  O O   . ALA A 1 66  ? -6.119  12.705  -7.587  1.00 93.84  ? 616  ALA A O   1 
ATOM   458  C CB  . ALA A 1 66  ? -8.649  12.812  -9.397  1.00 96.16  ? 616  ALA A CB  1 
ATOM   459  N N   . ALA A 1 67  ? -7.248  10.770  -7.132  1.00 90.16  ? 617  ALA A N   1 
ATOM   460  C CA  . ALA A 1 67  ? -6.054  10.000  -6.824  1.00 87.48  ? 617  ALA A CA  1 
ATOM   461  C C   . ALA A 1 67  ? -5.546  9.421   -8.137  1.00 84.31  ? 617  ALA A C   1 
ATOM   462  O O   . ALA A 1 67  ? -6.353  8.982   -8.961  1.00 84.58  ? 617  ALA A O   1 
ATOM   463  C CB  . ALA A 1 67  ? -6.398  8.865   -5.880  1.00 87.54  ? 617  ALA A CB  1 
ATOM   464  N N   . MET A 1 68  ? -4.223  9.420   -8.346  1.00 80.97  ? 618  MET A N   1 
ATOM   465  C CA  . MET A 1 68  ? -3.659  8.868   -9.577  1.00 78.01  ? 618  MET A CA  1 
ATOM   466  C C   . MET A 1 68  ? -2.339  8.172   -9.336  1.00 74.28  ? 618  MET A C   1 
ATOM   467  O O   . MET A 1 68  ? -1.591  8.539   -8.428  1.00 74.87  ? 618  MET A O   1 
ATOM   468  C CB  . MET A 1 68  ? -3.515  9.942   -10.662 1.00 79.02  ? 618  MET A CB  1 
ATOM   469  C CG  . MET A 1 68  ? -2.408  10.953  -10.392 1.00 82.03  ? 618  MET A CG  1 
ATOM   470  S SD  . MET A 1 68  ? -2.091  12.009  -11.819 1.00 86.68  ? 618  MET A SD  1 
ATOM   471  C CE  . MET A 1 68  ? -1.724  10.744  -13.066 1.00 82.98  ? 618  MET A CE  1 
ATOM   472  N N   . THR A 1 69  ? -2.057  7.164   -10.135 1.00 70.58  ? 619  THR A N   1 
ATOM   473  C CA  . THR A 1 69  ? -0.816  6.424   -10.009 1.00 67.45  ? 619  THR A CA  1 
ATOM   474  C C   . THR A 1 69  ? 0.323   7.233   -10.620 1.00 63.93  ? 619  THR A C   1 
ATOM   475  O O   . THR A 1 69  ? 0.213   7.737   -11.735 1.00 63.77  ? 619  THR A O   1 
ATOM   476  C CB  . THR A 1 69  ? -0.957  5.044   -10.617 1.00 68.25  ? 619  THR A CB  1 
ATOM   477  O OG1 . THR A 1 69  ? -2.094  4.412   -10.022 1.00 69.77  ? 619  THR A OG1 1 
ATOM   478  C CG2 . THR A 1 69  ? 0.298   4.188   -10.425 1.00 68.10  ? 619  THR A CG2 1 
ATOM   479  N N   . VAL A 1 70  ? 1.411   7.361   -9.875  1.00 60.90  ? 620  VAL A N   1 
ATOM   480  C CA  . VAL A 1 70  ? 2.614   8.070   -10.281 1.00 58.48  ? 620  VAL A CA  1 
ATOM   481  C C   . VAL A 1 70  ? 3.846   7.217   -9.951  1.00 56.66  ? 620  VAL A C   1 
ATOM   482  O O   . VAL A 1 70  ? 3.719   6.204   -9.267  1.00 57.12  ? 620  VAL A O   1 
ATOM   483  C CB  . VAL A 1 70  ? 2.684   9.459   -9.580  1.00 58.31  ? 620  VAL A CB  1 
ATOM   484  C CG1 . VAL A 1 70  ? 1.727   10.467  -10.217 1.00 58.47  ? 620  VAL A CG1 1 
ATOM   485  C CG2 . VAL A 1 70  ? 2.453   9.337   -8.076  1.00 58.38  ? 620  VAL A CG2 1 
ATOM   486  N N   . ALA A 1 71  ? 5.026   7.614   -10.451 1.00 54.87  ? 621  ALA A N   1 
ATOM   487  C CA  . ALA A 1 71  ? 6.336   7.015   -10.182 1.00 53.87  ? 621  ALA A CA  1 
ATOM   488  C C   . ALA A 1 71  ? 7.149   8.082   -9.468  1.00 53.73  ? 621  ALA A C   1 
ATOM   489  O O   . ALA A 1 71  ? 7.202   9.212   -9.927  1.00 53.67  ? 621  ALA A O   1 
ATOM   490  C CB  . ALA A 1 71  ? 7.033   6.646   -11.486 1.00 53.27  ? 621  ALA A CB  1 
ATOM   491  N N   . VAL A 1 72  ? 7.750   7.745   -8.342  1.00 53.67  ? 622  VAL A N   1 
ATOM   492  C CA  . VAL A 1 72  ? 8.551   8.674   -7.560  1.00 53.81  ? 622  VAL A CA  1 
ATOM   493  C C   . VAL A 1 72  ? 10.043  8.328   -7.630  1.00 53.74  ? 622  VAL A C   1 
ATOM   494  O O   . VAL A 1 72  ? 10.462  7.255   -7.202  1.00 52.77  ? 622  VAL A O   1 
ATOM   495  C CB  . VAL A 1 72  ? 8.060   8.799   -6.080  1.00 54.74  ? 622  VAL A CB  1 
ATOM   496  C CG1 . VAL A 1 72  ? 8.773   9.936   -5.355  1.00 55.19  ? 622  VAL A CG1 1 
ATOM   497  C CG2 . VAL A 1 72  ? 6.549   9.006   -6.007  1.00 55.40  ? 622  VAL A CG2 1 
ATOM   498  N N   . LYS A 1 73  ? 10.841  9.264   -8.174  1.00 54.95  ? 623  LYS A N   1 
ATOM   499  C CA  . LYS A 1 73  ? 12.299  9.192   -8.236  1.00 55.86  ? 623  LYS A CA  1 
ATOM   500  C C   . LYS A 1 73  ? 12.778  9.789   -6.938  1.00 57.38  ? 623  LYS A C   1 
ATOM   501  O O   . LYS A 1 73  ? 12.384  10.896  -6.562  1.00 57.24  ? 623  LYS A O   1 
ATOM   502  C CB  . LYS A 1 73  ? 12.849  10.035  -9.386  1.00 57.45  ? 623  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 73  ? 13.960  9.365   -10.160 1.00 62.91  ? 623  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 73  ? 15.322  9.465   -9.504  1.00 68.40  ? 623  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 73  ? 16.311  8.443   -10.051 1.00 72.11  ? 623  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 73  ? 16.759  8.787   -11.429 1.00 73.98  ? 623  LYS A NZ  1 
ATOM   507  N N   . MET A 1 74  ? 13.618  9.055   -6.243  1.00 58.94  ? 624  MET A N   1 
ATOM   508  C CA  . MET A 1 74  ? 14.171  9.503   -4.970  1.00 60.54  ? 624  MET A CA  1 
ATOM   509  C C   . MET A 1 74  ? 15.495  8.784   -4.713  1.00 61.35  ? 624  MET A C   1 
ATOM   510  O O   . MET A 1 74  ? 15.846  7.855   -5.435  1.00 60.94  ? 624  MET A O   1 
ATOM   511  C CB  . MET A 1 74  ? 13.170  9.173   -3.862  1.00 62.03  ? 624  MET A CB  1 
ATOM   512  C CG  . MET A 1 74  ? 12.917  7.696   -3.756  1.00 65.64  ? 624  MET A CG  1 
ATOM   513  S SD  . MET A 1 74  ? 11.804  7.339   -2.411  1.00 76.89  ? 624  MET A SD  1 
ATOM   514  C CE  . MET A 1 74  ? 10.320  7.519   -3.217  1.00 75.73  ? 624  MET A CE  1 
ATOM   515  N N   . LEU A 1 75  ? 16.204  9.180   -3.665  1.00 62.80  ? 625  LEU A N   1 
ATOM   516  C CA  . LEU A 1 75  ? 17.447  8.531   -3.286  1.00 64.50  ? 625  LEU A CA  1 
ATOM   517  C C   . LEU A 1 75  ? 17.255  7.683   -2.046  1.00 66.72  ? 625  LEU A C   1 
ATOM   518  O O   . LEU A 1 75  ? 16.304  7.896   -1.297  1.00 66.80  ? 625  LEU A O   1 
ATOM   519  C CB  . LEU A 1 75  ? 18.545  9.564   -3.042  1.00 64.23  ? 625  LEU A CB  1 
ATOM   520  C CG  . LEU A 1 75  ? 18.947  10.418  -4.229  1.00 65.53  ? 625  LEU A CG  1 
ATOM   521  C CD1 . LEU A 1 75  ? 20.059  11.366  -3.833  1.00 66.51  ? 625  LEU A CD1 1 
ATOM   522  C CD2 . LEU A 1 75  ? 19.395  9.577   -5.389  1.00 65.39  ? 625  LEU A CD2 1 
ATOM   523  N N   . LYS A 1 76  ? 18.169  6.726   -1.822  1.00 68.30  ? 626  LYS A N   1 
ATOM   524  C CA  . LYS A 1 76  ? 18.160  5.872   -0.638  1.00 70.62  ? 626  LYS A CA  1 
ATOM   525  C C   . LYS A 1 76  ? 18.905  6.599   0.509   1.00 73.27  ? 626  LYS A C   1 
ATOM   526  O O   . LYS A 1 76  ? 19.715  7.489   0.242   1.00 73.00  ? 626  LYS A O   1 
ATOM   527  C CB  . LYS A 1 76  ? 18.823  4.513   -0.964  1.00 71.73  ? 626  LYS A CB  1 
ATOM   528  C CG  . LYS A 1 76  ? 18.307  3.877   -2.253  1.00 74.24  ? 626  LYS A CG  1 
ATOM   529  C CD  . LYS A 1 76  ? 17.817  2.471   -2.080  1.00 77.94  ? 626  LYS A CD  1 
ATOM   530  C CE  . LYS A 1 76  ? 18.876  1.438   -2.382  1.00 82.54  ? 626  LYS A CE  1 
ATOM   531  N NZ  . LYS A 1 76  ? 18.284  0.078   -2.605  1.00 85.26  ? 626  LYS A NZ  1 
ATOM   532  N N   . PRO A 1 77  ? 18.653  6.257   1.792   1.00 75.82  ? 627  PRO A N   1 
ATOM   533  C CA  . PRO A 1 77  ? 19.359  6.952   2.890   1.00 77.80  ? 627  PRO A CA  1 
ATOM   534  C C   . PRO A 1 77  ? 20.899  6.920   2.783   1.00 80.46  ? 627  PRO A C   1 
ATOM   535  O O   . PRO A 1 77  ? 21.581  7.775   3.366   1.00 80.80  ? 627  PRO A O   1 
ATOM   536  C CB  . PRO A 1 77  ? 18.845  6.233   4.155   1.00 78.13  ? 627  PRO A CB  1 
ATOM   537  C CG  . PRO A 1 77  ? 18.231  4.937   3.669   1.00 77.63  ? 627  PRO A CG  1 
ATOM   538  C CD  . PRO A 1 77  ? 17.691  5.263   2.318   1.00 75.77  ? 627  PRO A CD  1 
ATOM   539  N N   . SER A 1 78  ? 21.443  5.968   1.986   1.00 81.84  ? 628  SER A N   1 
ATOM   540  C CA  . SER A 1 78  ? 22.879  5.793   1.744   1.00 83.66  ? 628  SER A CA  1 
ATOM   541  C C   . SER A 1 78  ? 23.496  6.846   0.777   1.00 85.17  ? 628  SER A C   1 
ATOM   542  O O   . SER A 1 78  ? 24.711  6.830   0.550   1.00 85.94  ? 628  SER A O   1 
ATOM   543  C CB  . SER A 1 78  ? 23.151  4.384   1.218   1.00 85.21  ? 628  SER A CB  1 
ATOM   544  O OG  . SER A 1 78  ? 22.557  4.157   -0.053  1.00 88.09  ? 628  SER A OG  1 
ATOM   545  N N   . ALA A 1 79  ? 22.679  7.736   0.202   1.00 85.21  ? 629  ALA A N   1 
ATOM   546  C CA  . ALA A 1 79  ? 23.188  8.743   -0.725  1.00 85.67  ? 629  ALA A CA  1 
ATOM   547  C C   . ALA A 1 79  ? 23.858  9.926   -0.008  1.00 86.05  ? 629  ALA A C   1 
ATOM   548  O O   . ALA A 1 79  ? 23.314  10.445  0.965   1.00 86.50  ? 629  ALA A O   1 
ATOM   549  C CB  . ALA A 1 79  ? 22.070  9.230   -1.623  1.00 85.62  ? 629  ALA A CB  1 
ATOM   550  N N   . HIS A 1 80  ? 25.038  10.352  -0.498  1.00 85.66  ? 630  HIS A N   1 
ATOM   551  C CA  . HIS A 1 80  ? 25.782  11.498  0.036   1.00 85.46  ? 630  HIS A CA  1 
ATOM   552  C C   . HIS A 1 80  ? 25.171  12.837  -0.437  1.00 84.13  ? 630  HIS A C   1 
ATOM   553  O O   . HIS A 1 80  ? 24.210  12.857  -1.209  1.00 84.41  ? 630  HIS A O   1 
ATOM   554  C CB  . HIS A 1 80  ? 27.275  11.400  -0.350  1.00 87.43  ? 630  HIS A CB  1 
ATOM   555  C CG  . HIS A 1 80  ? 28.124  10.776  0.721   1.00 92.85  ? 630  HIS A CG  1 
ATOM   556  N ND1 . HIS A 1 80  ? 27.777  9.561   1.310   1.00 95.19  ? 630  HIS A ND1 1 
ATOM   557  C CD2 . HIS A 1 80  ? 29.285  11.212  1.274   1.00 94.53  ? 630  HIS A CD2 1 
ATOM   558  C CE1 . HIS A 1 80  ? 28.730  9.310   2.198   1.00 95.88  ? 630  HIS A CE1 1 
ATOM   559  N NE2 . HIS A 1 80  ? 29.664  10.266  2.207   1.00 95.71  ? 630  HIS A NE2 1 
ATOM   560  N N   . LEU A 1 81  ? 25.723  13.952  0.036   1.00 82.52  ? 631  LEU A N   1 
ATOM   561  C CA  . LEU A 1 81  ? 25.254  15.285  -0.305  1.00 81.30  ? 631  LEU A CA  1 
ATOM   562  C C   . LEU A 1 81  ? 25.329  15.585  -1.793  1.00 79.78  ? 631  LEU A C   1 
ATOM   563  O O   . LEU A 1 81  ? 24.361  16.105  -2.352  1.00 79.77  ? 631  LEU A O   1 
ATOM   564  C CB  . LEU A 1 81  ? 26.022  16.347  0.530   1.00 81.39  ? 631  LEU A CB  1 
ATOM   565  C CG  . LEU A 1 81  ? 25.689  17.809  0.257   1.00 82.40  ? 631  LEU A CG  1 
ATOM   566  C CD1 . LEU A 1 81  ? 24.181  18.086  0.375   1.00 83.31  ? 631  LEU A CD1 1 
ATOM   567  C CD2 . LEU A 1 81  ? 26.433  18.687  1.166   1.00 82.49  ? 631  LEU A CD2 1 
ATOM   568  N N   . THR A 1 82  ? 26.447  15.227  -2.450  1.00 78.38  ? 632  THR A N   1 
ATOM   569  C CA  . THR A 1 82  ? 26.592  15.525  -3.880  1.00 77.46  ? 632  THR A CA  1 
ATOM   570  C C   . THR A 1 82  ? 25.529  14.821  -4.733  1.00 75.40  ? 632  THR A C   1 
ATOM   571  O O   . THR A 1 82  ? 25.268  15.277  -5.837  1.00 75.80  ? 632  THR A O   1 
ATOM   572  C CB  . THR A 1 82  ? 28.021  15.290  -4.411  1.00 79.31  ? 632  THR A CB  1 
ATOM   573  O OG1 . THR A 1 82  ? 28.205  13.926  -4.791  1.00 81.24  ? 632  THR A OG1 1 
ATOM   574  C CG2 . THR A 1 82  ? 29.094  15.721  -3.439  1.00 79.78  ? 632  THR A CG2 1 
ATOM   575  N N   . GLU A 1 83  ? 24.921  13.733  -4.233  1.00 73.04  ? 633  GLU A N   1 
ATOM   576  C CA  . GLU A 1 83  ? 23.885  13.037  -4.979  1.00 71.41  ? 633  GLU A CA  1 
ATOM   577  C C   . GLU A 1 83  ? 22.545  13.731  -4.838  1.00 69.34  ? 633  GLU A C   1 
ATOM   578  O O   . GLU A 1 83  ? 21.795  13.835  -5.810  1.00 68.52  ? 633  GLU A O   1 
ATOM   579  C CB  . GLU A 1 83  ? 23.804  11.567  -4.572  1.00 74.03  ? 633  GLU A CB  1 
ATOM   580  C CG  . GLU A 1 83  ? 24.888  10.732  -5.228  1.00 81.01  ? 633  GLU A CG  1 
ATOM   581  C CD  . GLU A 1 83  ? 26.128  10.573  -4.374  1.00 92.40  ? 633  GLU A CD  1 
ATOM   582  O OE1 . GLU A 1 83  ? 25.976  10.252  -3.173  1.00 95.35  ? 633  GLU A OE1 1 
ATOM   583  O OE2 . GLU A 1 83  ? 27.251  10.762  -4.900  1.00 95.75  ? 633  GLU A OE2 1 
ATOM   584  N N   . ARG A 1 84  ? 22.250  14.220  -3.626  1.00 68.35  ? 634  ARG A N   1 
ATOM   585  C CA  . ARG A 1 84  ? 21.034  14.959  -3.321  1.00 67.81  ? 634  ARG A CA  1 
ATOM   586  C C   . ARG A 1 84  ? 20.991  16.259  -4.149  1.00 66.96  ? 634  ARG A C   1 
ATOM   587  O O   . ARG A 1 84  ? 19.931  16.642  -4.661  1.00 67.13  ? 634  ARG A O   1 
ATOM   588  C CB  . ARG A 1 84  ? 20.972  15.262  -1.816  1.00 69.14  ? 634  ARG A CB  1 
ATOM   589  C CG  . ARG A 1 84  ? 21.031  14.007  -0.962  1.00 72.88  ? 634  ARG A CG  1 
ATOM   590  C CD  . ARG A 1 84  ? 20.588  14.266  0.467   1.00 76.94  ? 634  ARG A CD  1 
ATOM   591  N NE  . ARG A 1 84  ? 21.592  14.993  1.248   1.00 82.07  ? 634  ARG A NE  1 
ATOM   592  C CZ  . ARG A 1 84  ? 22.524  14.408  2.000   1.00 85.35  ? 634  ARG A CZ  1 
ATOM   593  N NH1 . ARG A 1 84  ? 22.601  13.082  2.064   1.00 85.95  ? 634  ARG A NH1 1 
ATOM   594  N NH2 . ARG A 1 84  ? 23.392  15.145  2.686   1.00 84.30  ? 634  ARG A NH2 1 
ATOM   595  N N   . GLU A 1 85  ? 22.148  16.911  -4.315  1.00 65.57  ? 635  GLU A N   1 
ATOM   596  C CA  . GLU A 1 85  ? 22.248  18.101  -5.138  1.00 65.43  ? 635  GLU A CA  1 
ATOM   597  C C   . GLU A 1 85  ? 22.001  17.721  -6.587  1.00 64.02  ? 635  GLU A C   1 
ATOM   598  O O   . GLU A 1 85  ? 21.218  18.387  -7.250  1.00 64.99  ? 635  GLU A O   1 
ATOM   599  C CB  . GLU A 1 85  ? 23.631  18.750  -4.987  1.00 69.50  ? 635  GLU A CB  1 
ATOM   600  C CG  . GLU A 1 85  ? 23.942  19.205  -3.566  1.00 77.33  ? 635  GLU A CG  1 
ATOM   601  C CD  . GLU A 1 85  ? 22.951  20.221  -3.030  1.00 87.15  ? 635  GLU A CD  1 
ATOM   602  O OE1 . GLU A 1 85  ? 22.799  21.289  -3.668  1.00 88.52  ? 635  GLU A OE1 1 
ATOM   603  O OE2 . GLU A 1 85  ? 22.314  19.944  -1.984  1.00 90.55  ? 635  GLU A OE2 1 
ATOM   604  N N   . ALA A 1 86  ? 22.593  16.612  -7.063  1.00 61.82  ? 636  ALA A N   1 
ATOM   605  C CA  . ALA A 1 86  ? 22.396  16.157  -8.435  1.00 60.46  ? 636  ALA A CA  1 
ATOM   606  C C   . ALA A 1 86  ? 20.938  15.772  -8.726  1.00 58.72  ? 636  ALA A C   1 
ATOM   607  O O   . ALA A 1 86  ? 20.487  16.031  -9.829  1.00 59.61  ? 636  ALA A O   1 
ATOM   608  C CB  . ALA A 1 86  ? 23.331  15.013  -8.761  1.00 60.89  ? 636  ALA A CB  1 
ATOM   609  N N   . LEU A 1 87  ? 20.171  15.272  -7.739  1.00 56.14  ? 637  LEU A N   1 
ATOM   610  C CA  . LEU A 1 87  ? 18.751  14.985  -7.944  1.00 54.56  ? 637  LEU A CA  1 
ATOM   611  C C   . LEU A 1 87  ? 17.921  16.284  -8.127  1.00 54.55  ? 637  LEU A C   1 
ATOM   612  O O   . LEU A 1 87  ? 17.021  16.359  -8.982  1.00 54.21  ? 637  LEU A O   1 
ATOM   613  C CB  . LEU A 1 87  ? 18.197  14.156  -6.803  1.00 53.48  ? 637  LEU A CB  1 
ATOM   614  C CG  . LEU A 1 87  ? 16.748  13.745  -6.931  1.00 53.96  ? 637  LEU A CG  1 
ATOM   615  C CD1 . LEU A 1 87  ? 16.506  12.922  -8.200  1.00 53.39  ? 637  LEU A CD1 1 
ATOM   616  C CD2 . LEU A 1 87  ? 16.288  13.016  -5.671  1.00 55.02  ? 637  LEU A CD2 1 
ATOM   617  N N   . MET A 1 88  ? 18.287  17.327  -7.376  1.00 54.50  ? 638  MET A N   1 
ATOM   618  C CA  . MET A 1 88  ? 17.671  18.654  -7.476  1.00 54.41  ? 638  MET A CA  1 
ATOM   619  C C   . MET A 1 88  ? 17.954  19.215  -8.880  1.00 53.72  ? 638  MET A C   1 
ATOM   620  O O   . MET A 1 88  ? 17.047  19.694  -9.555  1.00 52.71  ? 638  MET A O   1 
ATOM   621  C CB  . MET A 1 88  ? 18.239  19.575  -6.380  1.00 55.54  ? 638  MET A CB  1 
ATOM   622  C CG  . MET A 1 88  ? 17.510  20.900  -6.244  1.00 59.23  ? 638  MET A CG  1 
ATOM   623  S SD  . MET A 1 88  ? 15.747  20.712  -5.904  1.00 66.70  ? 638  MET A SD  1 
ATOM   624  C CE  . MET A 1 88  ? 15.083  21.706  -7.235  1.00 65.64  ? 638  MET A CE  1 
ATOM   625  N N   . SER A 1 89  ? 19.198  19.045  -9.357  1.00 53.88  ? 639  SER A N   1 
ATOM   626  C CA  . SER A 1 89  ? 19.623  19.478  -10.680 1.00 54.51  ? 639  SER A CA  1 
ATOM   627  C C   . SER A 1 89  ? 18.912  18.723  -11.785 1.00 54.57  ? 639  SER A C   1 
ATOM   628  O O   . SER A 1 89  ? 18.608  19.299  -12.822 1.00 55.04  ? 639  SER A O   1 
ATOM   629  C CB  . SER A 1 89  ? 21.126  19.316  -10.810 1.00 56.99  ? 639  SER A CB  1 
ATOM   630  O OG  . SER A 1 89  ? 21.760  20.461  -10.262 1.00 61.45  ? 639  SER A OG  1 
ATOM   631  N N   . GLU A 1 90  ? 18.590  17.450  -11.549 1.00 53.72  ? 640  GLU A N   1 
ATOM   632  C CA  . GLU A 1 90  ? 17.848  16.652  -12.502 1.00 53.24  ? 640  GLU A CA  1 
ATOM   633  C C   . GLU A 1 90  ? 16.398  17.165  -12.573 1.00 52.38  ? 640  GLU A C   1 
ATOM   634  O O   . GLU A 1 90  ? 15.845  17.303  -13.656 1.00 52.59  ? 640  GLU A O   1 
ATOM   635  C CB  . GLU A 1 90  ? 17.938  15.166  -12.105 1.00 55.98  ? 640  GLU A CB  1 
ATOM   636  C CG  . GLU A 1 90  ? 19.344  14.628  -12.352 1.00 64.21  ? 640  GLU A CG  1 
ATOM   637  C CD  . GLU A 1 90  ? 19.629  13.156  -12.074 1.00 75.97  ? 640  GLU A CD  1 
ATOM   638  O OE1 . GLU A 1 90  ? 18.949  12.555  -11.206 1.00 77.46  ? 640  GLU A OE1 1 
ATOM   639  O OE2 . GLU A 1 90  ? 20.544  12.605  -12.736 1.00 80.00  ? 640  GLU A OE2 1 
ATOM   640  N N   . LEU A 1 91  ? 15.800  17.488  -11.431 1.00 51.57  ? 641  LEU A N   1 
ATOM   641  C CA  . LEU A 1 91  ? 14.457  18.032  -11.372 1.00 51.91  ? 641  LEU A CA  1 
ATOM   642  C C   . LEU A 1 91  ? 14.367  19.360  -12.145 1.00 53.15  ? 641  LEU A C   1 
ATOM   643  O O   . LEU A 1 91  ? 13.369  19.610  -12.823 1.00 54.27  ? 641  LEU A O   1 
ATOM   644  C CB  . LEU A 1 91  ? 14.108  18.248  -9.905  1.00 52.03  ? 641  LEU A CB  1 
ATOM   645  C CG  . LEU A 1 91  ? 12.852  19.038  -9.573  1.00 53.50  ? 641  LEU A CG  1 
ATOM   646  C CD1 . LEU A 1 91  ? 11.611  18.431  -10.257 1.00 54.04  ? 641  LEU A CD1 1 
ATOM   647  C CD2 . LEU A 1 91  ? 12.663  19.049  -8.080  1.00 54.55  ? 641  LEU A CD2 1 
ATOM   648  N N   . LYS A 1 92  ? 15.422  20.179  -12.088 1.00 52.81  ? 642  LYS A N   1 
ATOM   649  C CA  . LYS A 1 92  ? 15.469  21.467  -12.789 1.00 52.73  ? 642  LYS A CA  1 
ATOM   650  C C   . LYS A 1 92  ? 15.591  21.275  -14.302 1.00 52.94  ? 642  LYS A C   1 
ATOM   651  O O   . LYS A 1 92  ? 15.037  22.066  -15.057 1.00 53.36  ? 642  LYS A O   1 
ATOM   652  C CB  . LYS A 1 92  ? 16.639  22.306  -12.273 1.00 53.22  ? 642  LYS A CB  1 
ATOM   653  C CG  . LYS A 1 92  ? 16.491  22.734  -10.833 1.00 54.47  ? 642  LYS A CG  1 
ATOM   654  C CD  . LYS A 1 92  ? 17.672  23.551  -10.444 1.00 57.28  ? 642  LYS A CD  1 
ATOM   655  C CE  . LYS A 1 92  ? 17.678  23.898  -8.990  1.00 60.82  ? 642  LYS A CE  1 
ATOM   656  N NZ  . LYS A 1 92  ? 18.934  24.618  -8.652  1.00 64.56  ? 642  LYS A NZ  1 
ATOM   657  N N   . VAL A 1 93  ? 16.297  20.242  -14.739 1.00 52.92  ? 643  VAL A N   1 
ATOM   658  C CA  . VAL A 1 93  ? 16.406  19.927  -16.168 1.00 53.68  ? 643  VAL A CA  1 
ATOM   659  C C   . VAL A 1 93  ? 15.041  19.438  -16.659 1.00 53.89  ? 643  VAL A C   1 
ATOM   660  O O   . VAL A 1 93  ? 14.543  19.918  -17.683 1.00 53.70  ? 643  VAL A O   1 
ATOM   661  C CB  . VAL A 1 93  ? 17.504  18.885  -16.480 1.00 54.52  ? 643  VAL A CB  1 
ATOM   662  C CG1 . VAL A 1 93  ? 17.378  18.376  -17.911 1.00 56.01  ? 643  VAL A CG1 1 
ATOM   663  C CG2 . VAL A 1 93  ? 18.911  19.440  -16.224 1.00 54.21  ? 643  VAL A CG2 1 
ATOM   664  N N   . LEU A 1 94  ? 14.417  18.513  -15.917 1.00 53.85  ? 644  LEU A N   1 
ATOM   665  C CA  . LEU A 1 94  ? 13.096  17.994  -16.268 1.00 54.14  ? 644  LEU A CA  1 
ATOM   666  C C   . LEU A 1 94  ? 12.056  19.105  -16.358 1.00 55.36  ? 644  LEU A C   1 
ATOM   667  O O   . LEU A 1 94  ? 11.229  19.118  -17.271 1.00 55.45  ? 644  LEU A O   1 
ATOM   668  C CB  . LEU A 1 94  ? 12.660  16.925  -15.272 1.00 53.60  ? 644  LEU A CB  1 
ATOM   669  C CG  . LEU A 1 94  ? 13.389  15.571  -15.347 1.00 55.33  ? 644  LEU A CG  1 
ATOM   670  C CD1 . LEU A 1 94  ? 12.599  14.507  -14.579 1.00 55.85  ? 644  LEU A CD1 1 
ATOM   671  C CD2 . LEU A 1 94  ? 13.604  15.072  -16.835 1.00 55.31  ? 644  LEU A CD2 1 
ATOM   672  N N   . SER A 1 95  ? 12.133  20.056  -15.423 1.00 55.94  ? 645  SER A N   1 
ATOM   673  C CA  . SER A 1 95  ? 11.258  21.215  -15.392 1.00 56.77  ? 645  SER A CA  1 
ATOM   674  C C   . SER A 1 95  ? 11.521  22.144  -16.621 1.00 57.38  ? 645  SER A C   1 
ATOM   675  O O   . SER A 1 95  ? 10.572  22.620  -17.264 1.00 57.65  ? 645  SER A O   1 
ATOM   676  C CB  . SER A 1 95  ? 11.461  21.959  -14.085 1.00 58.24  ? 645  SER A CB  1 
ATOM   677  O OG  . SER A 1 95  ? 10.637  23.109  -14.057 1.00 62.88  ? 645  SER A OG  1 
ATOM   678  N N   . TYR A 1 96  ? 12.812  22.355  -16.963 1.00 57.02  ? 646  TYR A N   1 
ATOM   679  C CA  . TYR A 1 96  ? 13.241  23.122  -18.122 1.00 57.54  ? 646  TYR A CA  1 
ATOM   680  C C   . TYR A 1 96  ? 12.765  22.464  -19.414 1.00 59.12  ? 646  TYR A C   1 
ATOM   681  O O   . TYR A 1 96  ? 12.410  23.169  -20.364 1.00 60.34  ? 646  TYR A O   1 
ATOM   682  C CB  . TYR A 1 96  ? 14.784  23.288  -18.130 1.00 57.34  ? 646  TYR A CB  1 
ATOM   683  C CG  . TYR A 1 96  ? 15.405  23.548  -19.491 1.00 58.26  ? 646  TYR A CG  1 
ATOM   684  C CD1 . TYR A 1 96  ? 15.431  24.828  -20.035 1.00 59.27  ? 646  TYR A CD1 1 
ATOM   685  C CD2 . TYR A 1 96  ? 15.932  22.506  -20.249 1.00 58.88  ? 646  TYR A CD2 1 
ATOM   686  C CE1 . TYR A 1 96  ? 16.004  25.073  -21.277 1.00 59.98  ? 646  TYR A CE1 1 
ATOM   687  C CE2 . TYR A 1 96  ? 16.435  22.725  -21.524 1.00 59.85  ? 646  TYR A CE2 1 
ATOM   688  C CZ  . TYR A 1 96  ? 16.490  24.016  -22.029 1.00 61.40  ? 646  TYR A CZ  1 
ATOM   689  O OH  . TYR A 1 96  ? 17.035  24.238  -23.282 1.00 63.40  ? 646  TYR A OH  1 
ATOM   690  N N   . LEU A 1 97  ? 12.842  21.128  -19.503 1.00 59.36  ? 647  LEU A N   1 
ATOM   691  C CA  . LEU A 1 97  ? 12.486  20.440  -20.739 1.00 59.85  ? 647  LEU A CA  1 
ATOM   692  C C   . LEU A 1 97  ? 11.062  20.676  -21.142 1.00 60.65  ? 647  LEU A C   1 
ATOM   693  O O   . LEU A 1 97  ? 10.803  20.923  -22.314 1.00 61.66  ? 647  LEU A O   1 
ATOM   694  C CB  . LEU A 1 97  ? 12.812  18.942  -20.691 1.00 59.79  ? 647  LEU A CB  1 
ATOM   695  C CG  . LEU A 1 97  ? 14.290  18.634  -20.665 1.00 60.16  ? 647  LEU A CG  1 
ATOM   696  C CD1 . LEU A 1 97  ? 14.544  17.190  -20.325 1.00 60.14  ? 647  LEU A CD1 1 
ATOM   697  C CD2 . LEU A 1 97  ? 14.963  19.049  -21.955 1.00 60.32  ? 647  LEU A CD2 1 
ATOM   698  N N   . GLY A 1 98  ? 10.163  20.727  -20.170 1.00 60.05  ? 648  GLY A N   1 
ATOM   699  C CA  . GLY A 1 98  ? 8.756   20.899  -20.483 1.00 59.65  ? 648  GLY A CA  1 
ATOM   700  C C   . GLY A 1 98  ? 8.157   19.563  -20.888 1.00 59.25  ? 648  GLY A C   1 
ATOM   701  O O   . GLY A 1 98  ? 8.811   18.525  -20.830 1.00 58.84  ? 648  GLY A O   1 
ATOM   702  N N   . ASN A 1 99  ? 6.921   19.592  -21.337 1.00 59.06  ? 649  ASN A N   1 
ATOM   703  C CA  . ASN A 1 99  ? 6.148   18.419  -21.640 1.00 59.44  ? 649  ASN A CA  1 
ATOM   704  C C   . ASN A 1 99  ? 6.172   17.962  -23.091 1.00 59.40  ? 649  ASN A C   1 
ATOM   705  O O   . ASN A 1 99  ? 6.050   18.769  -24.005 1.00 59.77  ? 649  ASN A O   1 
ATOM   706  C CB  . ASN A 1 99  ? 4.711   18.699  -21.221 1.00 61.04  ? 649  ASN A CB  1 
ATOM   707  C CG  . ASN A 1 99  ? 3.821   17.494  -21.167 1.00 65.26  ? 649  ASN A CG  1 
ATOM   708  O OD1 . ASN A 1 99  ? 3.289   17.035  -22.195 1.00 67.50  ? 649  ASN A OD1 1 
ATOM   709  N ND2 . ASN A 1 99  ? 3.595   16.994  -19.953 1.00 65.08  ? 649  ASN A ND2 1 
ATOM   710  N N   . HIS A 1 100 ? 6.219   16.649  -23.290 1.00 58.64  ? 650  HIS A N   1 
ATOM   711  C CA  . HIS A 1 100 ? 6.093   16.040  -24.600 1.00 58.59  ? 650  HIS A CA  1 
ATOM   712  C C   . HIS A 1 100 ? 5.491   14.648  -24.437 1.00 59.22  ? 650  HIS A C   1 
ATOM   713  O O   . HIS A 1 100 ? 5.847   13.937  -23.528 1.00 59.28  ? 650  HIS A O   1 
ATOM   714  C CB  . HIS A 1 100 ? 7.431   15.967  -25.309 1.00 59.10  ? 650  HIS A CB  1 
ATOM   715  C CG  . HIS A 1 100 ? 7.339   15.394  -26.679 1.00 61.60  ? 650  HIS A CG  1 
ATOM   716  N ND1 . HIS A 1 100 ? 7.135   16.189  -27.773 1.00 64.30  ? 650  HIS A ND1 1 
ATOM   717  C CD2 . HIS A 1 100 ? 7.444   14.113  -27.086 1.00 63.35  ? 650  HIS A CD2 1 
ATOM   718  C CE1 . HIS A 1 100 ? 7.097   15.372  -28.809 1.00 65.15  ? 650  HIS A CE1 1 
ATOM   719  N NE2 . HIS A 1 100 ? 7.243   14.106  -28.433 1.00 64.76  ? 650  HIS A NE2 1 
ATOM   720  N N   . MET A 1 101 ? 4.585   14.256  -25.310 1.00 60.20  ? 651  MET A N   1 
ATOM   721  C CA  . MET A 1 101 ? 3.960   12.934  -25.283 1.00 61.29  ? 651  MET A CA  1 
ATOM   722  C C   . MET A 1 101 ? 4.976   11.753  -25.143 1.00 60.69  ? 651  MET A C   1 
ATOM   723  O O   . MET A 1 101 ? 4.747   10.815  -24.393 1.00 60.42  ? 651  MET A O   1 
ATOM   724  C CB  . MET A 1 101 ? 3.102   12.777  -26.554 1.00 63.08  ? 651  MET A CB  1 
ATOM   725  C CG  . MET A 1 101 ? 2.460   11.418  -26.711 1.00 68.57  ? 651  MET A CG  1 
ATOM   726  S SD  . MET A 1 101 ? 1.402   10.933  -25.317 1.00 82.75  ? 651  MET A SD  1 
ATOM   727  C CE  . MET A 1 101 ? 0.146   12.231  -25.386 1.00 82.97  ? 651  MET A CE  1 
ATOM   728  N N   . ASN A 1 102 ? 6.109   11.839  -25.829 1.00 59.94  ? 652  ASN A N   1 
ATOM   729  C CA  . ASN A 1 102 ? 7.089   10.773  -25.879 1.00 59.22  ? 652  ASN A CA  1 
ATOM   730  C C   . ASN A 1 102 ? 8.248   10.875  -24.894 1.00 57.61  ? 652  ASN A C   1 
ATOM   731  O O   . ASN A 1 102 ? 9.306   10.322  -25.147 1.00 57.53  ? 652  ASN A O   1 
ATOM   732  C CB  . ASN A 1 102 ? 7.604   10.614  -27.303 1.00 61.18  ? 652  ASN A CB  1 
ATOM   733  C CG  . ASN A 1 102 ? 6.488   10.251  -28.248 1.00 64.59  ? 652  ASN A CG  1 
ATOM   734  O OD1 . ASN A 1 102 ? 6.264   10.908  -29.272 1.00 65.93  ? 652  ASN A OD1 1 
ATOM   735  N ND2 . ASN A 1 102 ? 5.743   9.205   -27.904 1.00 65.21  ? 652  ASN A ND2 1 
ATOM   736  N N   . ILE A 1 103 ? 8.042   11.523  -23.753 1.00 56.64  ? 653  ILE A N   1 
ATOM   737  C CA  . ILE A 1 103 ? 8.987   11.506  -22.635 1.00 55.32  ? 653  ILE A CA  1 
ATOM   738  C C   . ILE A 1 103 ? 8.216   11.171  -21.333 1.00 53.04  ? 653  ILE A C   1 
ATOM   739  O O   . ILE A 1 103 ? 6.994   11.397  -21.255 1.00 51.82  ? 653  ILE A O   1 
ATOM   740  C CB  . ILE A 1 103 ? 9.921   12.736  -22.484 1.00 56.61  ? 653  ILE A CB  1 
ATOM   741  C CG1 . ILE A 1 103 ? 9.233   13.905  -21.803 1.00 58.44  ? 653  ILE A CG1 1 
ATOM   742  C CG2 . ILE A 1 103 ? 10.575  13.168  -23.802 1.00 57.39  ? 653  ILE A CG2 1 
ATOM   743  C CD1 . ILE A 1 103 ? 10.171  14.749  -20.898 1.00 60.51  ? 653  ILE A CD1 1 
ATOM   744  N N   . VAL A 1 104 ? 8.916   10.601  -20.321 1.00 52.16  ? 654  VAL A N   1 
ATOM   745  C CA  . VAL A 1 104 ? 8.291   10.355  -19.024 1.00 52.06  ? 654  VAL A CA  1 
ATOM   746  C C   . VAL A 1 104 ? 8.257   11.728  -18.362 1.00 52.46  ? 654  VAL A C   1 
ATOM   747  O O   . VAL A 1 104 ? 9.311   12.262  -18.006 1.00 53.21  ? 654  VAL A O   1 
ATOM   748  C CB  . VAL A 1 104 ? 9.048   9.335   -18.159 1.00 52.09  ? 654  VAL A CB  1 
ATOM   749  C CG1 . VAL A 1 104 ? 8.407   9.244   -16.784 1.00 52.33  ? 654  VAL A CG1 1 
ATOM   750  C CG2 . VAL A 1 104 ? 9.078   7.971   -18.833 1.00 52.23  ? 654  VAL A CG2 1 
ATOM   751  N N   . ASN A 1 105 ? 7.067   12.358  -18.335 1.00 51.62  ? 655  ASN A N   1 
ATOM   752  C CA  . ASN A 1 105 ? 6.893   13.732  -17.871 1.00 51.02  ? 655  ASN A CA  1 
ATOM   753  C C   . ASN A 1 105 ? 6.791   13.929  -16.396 1.00 50.61  ? 655  ASN A C   1 
ATOM   754  O O   . ASN A 1 105 ? 6.126   13.172  -15.712 1.00 50.57  ? 655  ASN A O   1 
ATOM   755  C CB  . ASN A 1 105 ? 5.675   14.385  -18.525 1.00 51.04  ? 655  ASN A CB  1 
ATOM   756  C CG  . ASN A 1 105 ? 5.898   14.629  -19.979 1.00 53.54  ? 655  ASN A CG  1 
ATOM   757  O OD1 . ASN A 1 105 ? 6.763   15.417  -20.382 1.00 56.78  ? 655  ASN A OD1 1 
ATOM   758  N ND2 . ASN A 1 105 ? 5.116   13.999  -20.792 1.00 52.09  ? 655  ASN A ND2 1 
ATOM   759  N N   . LEU A 1 106 ? 7.378   15.044  -15.944 1.00 50.55  ? 656  LEU A N   1 
ATOM   760  C CA  . LEU A 1 106 ? 7.372   15.566  -14.588 1.00 50.27  ? 656  LEU A CA  1 
ATOM   761  C C   . LEU A 1 106 ? 5.958   16.039  -14.270 1.00 50.65  ? 656  LEU A C   1 
ATOM   762  O O   . LEU A 1 106 ? 5.399   16.800  -15.046 1.00 50.04  ? 656  LEU A O   1 
ATOM   763  C CB  . LEU A 1 106 ? 8.344   16.764  -14.516 1.00 49.52  ? 656  LEU A CB  1 
ATOM   764  C CG  . LEU A 1 106 ? 8.376   17.495  -13.194 1.00 50.43  ? 656  LEU A CG  1 
ATOM   765  C CD1 . LEU A 1 106 ? 8.947   16.631  -12.118 1.00 50.42  ? 656  LEU A CD1 1 
ATOM   766  C CD2 . LEU A 1 106 ? 9.169   18.754  -13.294 1.00 51.44  ? 656  LEU A CD2 1 
ATOM   767  N N   . LEU A 1 107 ? 5.376   15.569  -13.139 1.00 51.75  ? 657  LEU A N   1 
ATOM   768  C CA  . LEU A 1 107 ? 4.028   15.937  -12.664 1.00 52.98  ? 657  LEU A CA  1 
ATOM   769  C C   . LEU A 1 107 ? 4.045   16.834  -11.427 1.00 54.36  ? 657  LEU A C   1 
ATOM   770  O O   . LEU A 1 107 ? 3.134   17.651  -11.224 1.00 54.35  ? 657  LEU A O   1 
ATOM   771  C CB  . LEU A 1 107 ? 3.175   14.699  -12.397 1.00 52.99  ? 657  LEU A CB  1 
ATOM   772  C CG  . LEU A 1 107 ? 2.912   13.823  -13.634 1.00 54.29  ? 657  LEU A CG  1 
ATOM   773  C CD1 . LEU A 1 107 ? 2.196   12.536  -13.249 1.00 54.60  ? 657  LEU A CD1 1 
ATOM   774  C CD2 . LEU A 1 107 ? 2.131   14.614  -14.706 1.00 54.09  ? 657  LEU A CD2 1 
ATOM   775  N N   . GLY A 1 108 ? 5.081   16.673  -10.615 1.00 55.05  ? 658  GLY A N   1 
ATOM   776  C CA  . GLY A 1 108 ? 5.266   17.450  -9.403  1.00 55.80  ? 658  GLY A CA  1 
ATOM   777  C C   . GLY A 1 108 ? 6.560   17.114  -8.705  1.00 56.74  ? 658  GLY A C   1 
ATOM   778  O O   . GLY A 1 108 ? 7.351   16.303  -9.190  1.00 56.52  ? 658  GLY A O   1 
ATOM   779  N N   . ALA A 1 109 ? 6.796   17.747  -7.552  1.00 57.61  ? 659  ALA A N   1 
ATOM   780  C CA  . ALA A 1 109 ? 7.999   17.504  -6.766  1.00 58.21  ? 659  ALA A CA  1 
ATOM   781  C C   . ALA A 1 109 ? 7.794   17.905  -5.320  1.00 59.46  ? 659  ALA A C   1 
ATOM   782  O O   . ALA A 1 109 ? 7.063   18.861  -5.045  1.00 59.52  ? 659  ALA A O   1 
ATOM   783  C CB  . ALA A 1 109 ? 9.173   18.273  -7.351  1.00 57.68  ? 659  ALA A CB  1 
ATOM   784  N N   . CYS A 1 110 ? 8.475   17.199  -4.395  1.00 59.94  ? 660  CYS A N   1 
ATOM   785  C CA  . CYS A 1 110 ? 8.482   17.536  -2.968  1.00 60.71  ? 660  CYS A CA  1 
ATOM   786  C C   . CYS A 1 110 ? 9.914   17.891  -2.581  1.00 62.88  ? 660  CYS A C   1 
ATOM   787  O O   . CYS A 1 110 ? 10.775  17.017  -2.450  1.00 62.41  ? 660  CYS A O   1 
ATOM   788  C CB  . CYS A 1 110 ? 7.951   16.398  -2.105  1.00 60.44  ? 660  CYS A CB  1 
ATOM   789  S SG  . CYS A 1 110 ? 6.502   15.562  -2.785  1.00 63.04  ? 660  CYS A SG  1 
ATOM   790  N N   . THR A 1 111 ? 10.175  19.174  -2.431  1.00 65.22  ? 661  THR A N   1 
ATOM   791  C CA  . THR A 1 111 ? 11.491  19.690  -2.058  1.00 68.01  ? 661  THR A CA  1 
ATOM   792  C C   . THR A 1 111 ? 11.493  20.343  -0.659  1.00 71.08  ? 661  THR A C   1 
ATOM   793  O O   . THR A 1 111 ? 12.564  20.649  -0.130  1.00 72.07  ? 661  THR A O   1 
ATOM   794  C CB  . THR A 1 111 ? 12.027  20.649  -3.146  1.00 68.96  ? 661  THR A CB  1 
ATOM   795  O OG1 . THR A 1 111 ? 11.274  21.869  -3.110  1.00 69.97  ? 661  THR A OG1 1 
ATOM   796  C CG2 . THR A 1 111 ? 11.988  20.029  -4.564  1.00 68.69  ? 661  THR A CG2 1 
ATOM   797  N N   . ILE A 1 112 ? 10.325  20.529  -0.040  1.00 72.65  ? 662  ILE A N   1 
ATOM   798  C CA  . ILE A 1 112 ? 10.244  21.140  1.294   1.00 74.66  ? 662  ILE A CA  1 
ATOM   799  C C   . ILE A 1 112 ? 9.928   20.078  2.351   1.00 76.16  ? 662  ILE A C   1 
ATOM   800  O O   . ILE A 1 112 ? 9.205   19.114  2.074   1.00 76.55  ? 662  ILE A O   1 
ATOM   801  C CB  . ILE A 1 112 ? 9.186   22.286  1.300   1.00 75.61  ? 662  ILE A CB  1 
ATOM   802  C CG1 . ILE A 1 112 ? 9.402   23.252  0.128   1.00 77.01  ? 662  ILE A CG1 1 
ATOM   803  C CG2 . ILE A 1 112 ? 9.177   23.061  2.618   1.00 76.48  ? 662  ILE A CG2 1 
ATOM   804  C CD1 . ILE A 1 112 ? 8.223   24.084  -0.154  1.00 78.79  ? 662  ILE A CD1 1 
ATOM   805  N N   . GLY A 1 113 ? 10.475  20.256  3.545   1.00 76.69  ? 663  GLY A N   1 
ATOM   806  C CA  . GLY A 1 113 ? 10.196  19.373  4.671   1.00 77.60  ? 663  GLY A CA  1 
ATOM   807  C C   . GLY A 1 113 ? 10.631  17.937  4.489   1.00 78.02  ? 663  GLY A C   1 
ATOM   808  O O   . GLY A 1 113 ? 9.901   17.009  4.859   1.00 78.47  ? 663  GLY A O   1 
ATOM   809  N N   . GLY A 1 114 ? 11.820  17.757  3.918   1.00 77.26  ? 664  GLY A N   1 
ATOM   810  C CA  . GLY A 1 114 ? 12.357  16.423  3.698   1.00 76.32  ? 664  GLY A CA  1 
ATOM   811  C C   . GLY A 1 114 ? 13.148  16.278  2.419   1.00 74.82  ? 664  GLY A C   1 
ATOM   812  O O   . GLY A 1 114 ? 13.316  17.241  1.659   1.00 74.94  ? 664  GLY A O   1 
ATOM   813  N N   . PRO A 1 115 ? 13.575  15.028  2.141   1.00 72.98  ? 665  PRO A N   1 
ATOM   814  C CA  . PRO A 1 115 ? 14.357  14.752  0.921   1.00 70.83  ? 665  PRO A CA  1 
ATOM   815  C C   . PRO A 1 115 ? 13.615  15.029  -0.380  1.00 68.01  ? 665  PRO A C   1 
ATOM   816  O O   . PRO A 1 115 ? 12.398  14.982  -0.406  1.00 68.39  ? 665  PRO A O   1 
ATOM   817  C CB  . PRO A 1 115 ? 14.702  13.264  1.052   1.00 72.04  ? 665  PRO A CB  1 
ATOM   818  C CG  . PRO A 1 115 ? 14.584  12.963  2.506   1.00 73.39  ? 665  PRO A CG  1 
ATOM   819  C CD  . PRO A 1 115 ? 13.452  13.827  2.988   1.00 72.30  ? 665  PRO A CD  1 
ATOM   820  N N   . THR A 1 116 ? 14.347  15.308  -1.462  1.00 65.19  ? 666  THR A N   1 
ATOM   821  C CA  . THR A 1 116 ? 13.737  15.585  -2.759  1.00 62.84  ? 666  THR A CA  1 
ATOM   822  C C   . THR A 1 116 ? 13.047  14.344  -3.341  1.00 61.37  ? 666  THR A C   1 
ATOM   823  O O   . THR A 1 116 ? 13.656  13.280  -3.453  1.00 61.32  ? 666  THR A O   1 
ATOM   824  C CB  . THR A 1 116 ? 14.783  16.152  -3.734  1.00 62.65  ? 666  THR A CB  1 
ATOM   825  O OG1 . THR A 1 116 ? 15.453  17.251  -3.111  1.00 65.06  ? 666  THR A OG1 1 
ATOM   826  C CG2 . THR A 1 116 ? 14.182  16.584  -5.063  1.00 61.31  ? 666  THR A CG2 1 
ATOM   827  N N   . LEU A 1 117 ? 11.774  14.504  -3.714  1.00 59.66  ? 667  LEU A N   1 
ATOM   828  C CA  . LEU A 1 117 ? 10.962  13.476  -4.338  1.00 58.51  ? 667  LEU A CA  1 
ATOM   829  C C   . LEU A 1 117 ? 10.542  14.025  -5.693  1.00 57.83  ? 667  LEU A C   1 
ATOM   830  O O   . LEU A 1 117 ? 9.889   15.065  -5.743  1.00 58.91  ? 667  LEU A O   1 
ATOM   831  C CB  . LEU A 1 117 ? 9.694   13.221  -3.498  1.00 58.42  ? 667  LEU A CB  1 
ATOM   832  C CG  . LEU A 1 117 ? 9.854   12.695  -2.060  1.00 59.21  ? 667  LEU A CG  1 
ATOM   833  C CD1 . LEU A 1 117 ? 8.525   12.274  -1.508  1.00 59.08  ? 667  LEU A CD1 1 
ATOM   834  C CD2 . LEU A 1 117 ? 10.769  11.492  -1.998  1.00 59.93  ? 667  LEU A CD2 1 
ATOM   835  N N   . VAL A 1 118 ? 10.925  13.361  -6.788  1.00 55.87  ? 668  VAL A N   1 
ATOM   836  C CA  . VAL A 1 118 ? 10.571  13.795  -8.143  1.00 53.87  ? 668  VAL A CA  1 
ATOM   837  C C   . VAL A 1 118 ? 9.380   12.961  -8.609  1.00 51.45  ? 668  VAL A C   1 
ATOM   838  O O   . VAL A 1 118 ? 9.523   11.753  -8.776  1.00 50.43  ? 668  VAL A O   1 
ATOM   839  C CB  . VAL A 1 118 ? 11.791  13.621  -9.100  1.00 54.05  ? 668  VAL A CB  1 
ATOM   840  C CG1 . VAL A 1 118 ? 11.437  14.036  -10.531 1.00 53.73  ? 668  VAL A CG1 1 
ATOM   841  C CG2 . VAL A 1 118 ? 13.016  14.380  -8.576  1.00 54.16  ? 668  VAL A CG2 1 
ATOM   842  N N   . ILE A 1 119 ? 8.210   13.575  -8.770  1.00 50.75  ? 669  ILE A N   1 
ATOM   843  C CA  . ILE A 1 119 ? 7.016   12.835  -9.187  1.00 51.46  ? 669  ILE A CA  1 
ATOM   844  C C   . ILE A 1 119 ? 6.811   12.945  -10.677 1.00 52.10  ? 669  ILE A C   1 
ATOM   845  O O   . ILE A 1 119 ? 6.729   14.061  -11.188 1.00 52.38  ? 669  ILE A O   1 
ATOM   846  C CB  . ILE A 1 119 ? 5.757   13.313  -8.469  1.00 52.35  ? 669  ILE A CB  1 
ATOM   847  C CG1 . ILE A 1 119 ? 5.953   13.373  -6.939  1.00 53.05  ? 669  ILE A CG1 1 
ATOM   848  C CG2 . ILE A 1 119 ? 4.591   12.436  -8.862  1.00 53.07  ? 669  ILE A CG2 1 
ATOM   849  C CD1 . ILE A 1 119 ? 5.200   14.486  -6.291  1.00 53.73  ? 669  ILE A CD1 1 
ATOM   850  N N   . THR A 1 120 ? 6.735   11.792  -11.376 1.00 51.85  ? 670  THR A N   1 
ATOM   851  C CA  . THR A 1 120 ? 6.563   11.727  -12.821 1.00 52.54  ? 670  THR A CA  1 
ATOM   852  C C   . THR A 1 120 ? 5.433   10.734  -13.225 1.00 53.97  ? 670  THR A C   1 
ATOM   853  O O   . THR A 1 120 ? 4.913   10.008  -12.382 1.00 53.68  ? 670  THR A O   1 
ATOM   854  C CB  . THR A 1 120 ? 7.903   11.342  -13.504 1.00 52.76  ? 670  THR A CB  1 
ATOM   855  O OG1 . THR A 1 120 ? 8.101   9.914   -13.435 1.00 53.45  ? 670  THR A OG1 1 
ATOM   856  C CG2 . THR A 1 120 ? 9.099   12.121  -12.982 1.00 52.34  ? 670  THR A CG2 1 
ATOM   857  N N   . GLU A 1 121 ? 5.090   10.682  -14.526 1.00 54.91  ? 671  GLU A N   1 
ATOM   858  C CA  . GLU A 1 121 ? 4.107   9.747   -15.056 1.00 56.22  ? 671  GLU A CA  1 
ATOM   859  C C   . GLU A 1 121 ? 4.487   8.301   -14.777 1.00 57.97  ? 671  GLU A C   1 
ATOM   860  O O   . GLU A 1 121 ? 5.677   7.960   -14.824 1.00 58.32  ? 671  GLU A O   1 
ATOM   861  C CB  . GLU A 1 121 ? 4.004   9.926   -16.568 1.00 57.18  ? 671  GLU A CB  1 
ATOM   862  C CG  . GLU A 1 121 ? 3.338   11.233  -16.899 1.00 61.91  ? 671  GLU A CG  1 
ATOM   863  C CD  . GLU A 1 121 ? 3.396   11.644  -18.353 1.00 66.41  ? 671  GLU A CD  1 
ATOM   864  O OE1 . GLU A 1 121 ? 4.382   11.294  -19.042 1.00 66.70  ? 671  GLU A OE1 1 
ATOM   865  O OE2 . GLU A 1 121 ? 2.467   12.361  -18.787 1.00 68.26  ? 671  GLU A OE2 1 
ATOM   866  N N   . TYR A 1 122 ? 3.477   7.443   -14.536 1.00 58.49  ? 672  TYR A N   1 
ATOM   867  C CA  . TYR A 1 122 ? 3.697   6.020   -14.355 1.00 59.66  ? 672  TYR A CA  1 
ATOM   868  C C   . TYR A 1 122 ? 3.360   5.321   -15.678 1.00 61.22  ? 672  TYR A C   1 
ATOM   869  O O   . TYR A 1 122 ? 2.272   5.507   -16.207 1.00 61.95  ? 672  TYR A O   1 
ATOM   870  C CB  . TYR A 1 122 ? 2.795   5.503   -13.247 1.00 60.30  ? 672  TYR A CB  1 
ATOM   871  C CG  . TYR A 1 122 ? 2.850   4.009   -13.056 1.00 62.23  ? 672  TYR A CG  1 
ATOM   872  C CD1 . TYR A 1 122 ? 3.855   3.421   -12.301 1.00 63.32  ? 672  TYR A CD1 1 
ATOM   873  C CD2 . TYR A 1 122 ? 1.856   3.186   -13.572 1.00 64.18  ? 672  TYR A CD2 1 
ATOM   874  C CE1 . TYR A 1 122 ? 3.886   2.046   -12.086 1.00 64.64  ? 672  TYR A CE1 1 
ATOM   875  C CE2 . TYR A 1 122 ? 1.883   1.808   -13.378 1.00 65.44  ? 672  TYR A CE2 1 
ATOM   876  C CZ  . TYR A 1 122 ? 2.904   1.240   -12.638 1.00 66.32  ? 672  TYR A CZ  1 
ATOM   877  O OH  . TYR A 1 122 ? 2.926   -0.124  -12.463 1.00 68.18  ? 672  TYR A OH  1 
ATOM   878  N N   . CYS A 1 123 ? 4.294   4.548   -16.234 1.00 61.63  ? 673  CYS A N   1 
ATOM   879  C CA  . CYS A 1 123 ? 4.071   3.820   -17.477 1.00 62.41  ? 673  CYS A CA  1 
ATOM   880  C C   . CYS A 1 123 ? 3.852   2.331   -17.133 1.00 63.98  ? 673  CYS A C   1 
ATOM   881  O O   . CYS A 1 123 ? 4.799   1.635   -16.779 1.00 63.89  ? 673  CYS A O   1 
ATOM   882  C CB  . CYS A 1 123 ? 5.242   4.028   -18.430 1.00 62.44  ? 673  CYS A CB  1 
ATOM   883  S SG  . CYS A 1 123 ? 5.744   5.768   -18.622 1.00 65.86  ? 673  CYS A SG  1 
ATOM   884  N N   . CYS A 1 124 ? 2.599   1.857   -17.206 1.00 65.35  ? 674  CYS A N   1 
ATOM   885  C CA  . CYS A 1 124 ? 2.214   0.497   -16.786 1.00 67.39  ? 674  CYS A CA  1 
ATOM   886  C C   . CYS A 1 124 ? 3.050   -0.682  -17.381 1.00 66.97  ? 674  CYS A C   1 
ATOM   887  O O   . CYS A 1 124 ? 3.233   -1.668  -16.662 1.00 67.07  ? 674  CYS A O   1 
ATOM   888  C CB  . CYS A 1 124 ? 0.718   0.253   -16.985 1.00 70.30  ? 674  CYS A CB  1 
ATOM   889  S SG  . CYS A 1 124 ? 0.174   0.271   -18.719 1.00 80.89  ? 674  CYS A SG  1 
ATOM   890  N N   . TYR A 1 125 ? 3.548   -0.608  -18.633 1.00 66.39  ? 675  TYR A N   1 
ATOM   891  C CA  . TYR A 1 125 ? 4.290   -1.753  -19.207 1.00 66.61  ? 675  TYR A CA  1 
ATOM   892  C C   . TYR A 1 125 ? 5.778   -1.836  -18.774 1.00 64.24  ? 675  TYR A C   1 
ATOM   893  O O   . TYR A 1 125 ? 6.415   -2.878  -18.980 1.00 63.90  ? 675  TYR A O   1 
ATOM   894  C CB  . TYR A 1 125 ? 4.141   -1.837  -20.751 1.00 68.20  ? 675  TYR A CB  1 
ATOM   895  C CG  . TYR A 1 125 ? 2.698   -2.049  -21.176 1.00 70.84  ? 675  TYR A CG  1 
ATOM   896  C CD1 . TYR A 1 125 ? 2.088   -3.285  -21.035 1.00 72.88  ? 675  TYR A CD1 1 
ATOM   897  C CD2 . TYR A 1 125 ? 1.918   -0.988  -21.611 1.00 72.59  ? 675  TYR A CD2 1 
ATOM   898  C CE1 . TYR A 1 125 ? 0.747   -3.474  -21.373 1.00 74.84  ? 675  TYR A CE1 1 
ATOM   899  C CE2 . TYR A 1 125 ? 0.580   -1.156  -21.932 1.00 74.34  ? 675  TYR A CE2 1 
ATOM   900  C CZ  . TYR A 1 125 ? -0.012  -2.402  -21.811 1.00 76.34  ? 675  TYR A CZ  1 
ATOM   901  O OH  . TYR A 1 125 ? -1.358  -2.557  -22.127 1.00 78.47  ? 675  TYR A OH  1 
ATOM   902  N N   . GLY A 1 126 ? 6.291   -0.787  -18.121 1.00 62.24  ? 676  GLY A N   1 
ATOM   903  C CA  . GLY A 1 126 ? 7.677   -0.752  -17.669 1.00 60.12  ? 676  GLY A CA  1 
ATOM   904  C C   . GLY A 1 126 ? 8.627   -0.467  -18.803 1.00 58.53  ? 676  GLY A C   1 
ATOM   905  O O   . GLY A 1 126 ? 8.217   0.137   -19.790 1.00 58.18  ? 676  GLY A O   1 
ATOM   906  N N   . ASP A 1 127 ? 9.894   -0.906  -18.694 1.00 58.45  ? 677  ASP A N   1 
ATOM   907  C CA  . ASP A 1 127 ? 10.889  -0.666  -19.751 1.00 59.51  ? 677  ASP A CA  1 
ATOM   908  C C   . ASP A 1 127 ? 10.674  -1.512  -21.002 1.00 60.38  ? 677  ASP A C   1 
ATOM   909  O O   . ASP A 1 127 ? 10.236  -2.664  -20.935 1.00 60.97  ? 677  ASP A O   1 
ATOM   910  C CB  . ASP A 1 127 ? 12.345  -0.796  -19.258 1.00 62.06  ? 677  ASP A CB  1 
ATOM   911  C CG  . ASP A 1 127 ? 12.793  -2.218  -18.938 1.00 68.64  ? 677  ASP A CG  1 
ATOM   912  O OD1 . ASP A 1 127 ? 12.195  -2.837  -18.029 1.00 69.82  ? 677  ASP A OD1 1 
ATOM   913  O OD2 . ASP A 1 127 ? 13.773  -2.696  -19.569 1.00 71.27  ? 677  ASP A OD2 1 
ATOM   914  N N   . LEU A 1 128 ? 11.002  -0.919  -22.147 1.00 59.96  ? 678  LEU A N   1 
ATOM   915  C CA  . LEU A 1 128 ? 10.832  -1.501  -23.456 1.00 59.78  ? 678  LEU A CA  1 
ATOM   916  C C   . LEU A 1 128 ? 11.724  -2.695  -23.694 1.00 60.59  ? 678  LEU A C   1 
ATOM   917  O O   . LEU A 1 128 ? 11.250  -3.670  -24.238 1.00 60.99  ? 678  LEU A O   1 
ATOM   918  C CB  . LEU A 1 128 ? 11.032  -0.423  -24.516 1.00 59.50  ? 678  LEU A CB  1 
ATOM   919  C CG  . LEU A 1 128 ? 10.668  -0.791  -25.922 1.00 60.80  ? 678  LEU A CG  1 
ATOM   920  C CD1 . LEU A 1 128 ? 9.231   -1.300  -26.009 1.00 61.15  ? 678  LEU A CD1 1 
ATOM   921  C CD2 . LEU A 1 128 ? 10.919  0.370   -26.861 1.00 61.33  ? 678  LEU A CD2 1 
ATOM   922  N N   . LEU A 1 129 ? 12.970  -2.689  -23.207 1.00 61.21  ? 679  LEU A N   1 
ATOM   923  C CA  . LEU A 1 129 ? 13.866  -3.837  -23.368 1.00 61.80  ? 679  LEU A CA  1 
ATOM   924  C C   . LEU A 1 129 ? 13.262  -5.118  -22.767 1.00 63.79  ? 679  LEU A C   1 
ATOM   925  O O   . LEU A 1 129 ? 13.210  -6.127  -23.463 1.00 65.00  ? 679  LEU A O   1 
ATOM   926  C CB  . LEU A 1 129 ? 15.267  -3.569  -22.808 1.00 60.70  ? 679  LEU A CB  1 
ATOM   927  C CG  . LEU A 1 129 ? 16.242  -4.728  -22.984 1.00 60.31  ? 679  LEU A CG  1 
ATOM   928  C CD1 . LEU A 1 129 ? 16.555  -4.949  -24.439 1.00 60.46  ? 679  LEU A CD1 1 
ATOM   929  C CD2 . LEU A 1 129 ? 17.506  -4.498  -22.223 1.00 60.08  ? 679  LEU A CD2 1 
ATOM   930  N N   . ASN A 1 130 ? 12.739  -5.064  -21.528 1.00 63.94  ? 680  ASN A N   1 
ATOM   931  C CA  . ASN A 1 130 ? 12.090  -6.236  -20.948 1.00 64.62  ? 680  ASN A CA  1 
ATOM   932  C C   . ASN A 1 130 ? 10.787  -6.535  -21.635 1.00 65.48  ? 680  ASN A C   1 
ATOM   933  O O   . ASN A 1 130 ? 10.416  -7.703  -21.709 1.00 66.60  ? 680  ASN A O   1 
ATOM   934  C CB  . ASN A 1 130 ? 11.881  -6.104  -19.458 1.00 66.54  ? 680  ASN A CB  1 
ATOM   935  C CG  . ASN A 1 130 ? 13.099  -6.521  -18.681 1.00 71.45  ? 680  ASN A CG  1 
ATOM   936  O OD1 . ASN A 1 130 ? 13.480  -7.720  -18.661 1.00 73.73  ? 680  ASN A OD1 1 
ATOM   937  N ND2 . ASN A 1 130 ? 13.747  -5.547  -18.034 1.00 71.09  ? 680  ASN A ND2 1 
ATOM   938  N N   . PHE A 1 131 ? 10.091  -5.512  -22.167 1.00 64.72  ? 681  PHE A N   1 
ATOM   939  C CA  . PHE A 1 131 ? 8.848   -5.738  -22.886 1.00 64.76  ? 681  PHE A CA  1 
ATOM   940  C C   . PHE A 1 131 ? 9.114   -6.511  -24.196 1.00 64.85  ? 681  PHE A C   1 
ATOM   941  O O   . PHE A 1 131 ? 8.391   -7.448  -24.520 1.00 64.59  ? 681  PHE A O   1 
ATOM   942  C CB  . PHE A 1 131 ? 8.132   -4.408  -23.163 1.00 64.47  ? 681  PHE A CB  1 
ATOM   943  C CG  . PHE A 1 131 ? 6.852   -4.604  -23.931 1.00 64.87  ? 681  PHE A CG  1 
ATOM   944  C CD1 . PHE A 1 131 ? 5.677   -4.918  -23.277 1.00 65.99  ? 681  PHE A CD1 1 
ATOM   945  C CD2 . PHE A 1 131 ? 6.837   -4.528  -25.312 1.00 65.37  ? 681  PHE A CD2 1 
ATOM   946  C CE1 . PHE A 1 131 ? 4.499   -5.128  -23.993 1.00 67.06  ? 681  PHE A CE1 1 
ATOM   947  C CE2 . PHE A 1 131 ? 5.675   -4.763  -26.023 1.00 66.40  ? 681  PHE A CE2 1 
ATOM   948  C CZ  . PHE A 1 131 ? 4.507   -5.053  -25.364 1.00 66.54  ? 681  PHE A CZ  1 
ATOM   949  N N   . LEU A 1 132 ? 10.164  -6.116  -24.937 1.00 64.82  ? 682  LEU A N   1 
ATOM   950  C CA  . LEU A 1 132 ? 10.538  -6.782  -26.175 1.00 65.05  ? 682  LEU A CA  1 
ATOM   951  C C   . LEU A 1 132 ? 11.023  -8.201  -25.901 1.00 66.30  ? 682  LEU A C   1 
ATOM   952  O O   . LEU A 1 132 ? 10.804  -9.066  -26.733 1.00 66.44  ? 682  LEU A O   1 
ATOM   953  C CB  . LEU A 1 132 ? 11.641  -6.016  -26.904 1.00 64.33  ? 682  LEU A CB  1 
ATOM   954  C CG  . LEU A 1 132 ? 11.264  -4.671  -27.486 1.00 64.83  ? 682  LEU A CG  1 
ATOM   955  C CD1 . LEU A 1 132 ? 12.501  -3.922  -27.957 1.00 64.83  ? 682  LEU A CD1 1 
ATOM   956  C CD2 . LEU A 1 132 ? 10.265  -4.819  -28.591 1.00 64.94  ? 682  LEU A CD2 1 
ATOM   957  N N   . ARG A 1 133 ? 11.705  -8.436  -24.768 1.00 67.32  ? 683  ARG A N   1 
ATOM   958  C CA  . ARG A 1 133 ? 12.251  -9.752  -24.440 1.00 68.96  ? 683  ARG A CA  1 
ATOM   959  C C   . ARG A 1 133 ? 11.192  -10.745 -24.053 1.00 72.52  ? 683  ARG A C   1 
ATOM   960  O O   . ARG A 1 133 ? 11.288  -11.922 -24.414 1.00 71.99  ? 683  ARG A O   1 
ATOM   961  C CB  . ARG A 1 133 ? 13.337  -9.656  -23.374 1.00 68.20  ? 683  ARG A CB  1 
ATOM   962  C CG  . ARG A 1 133 ? 14.629  -9.147  -23.956 1.00 68.64  ? 683  ARG A CG  1 
ATOM   963  C CD  . ARG A 1 133 ? 15.686  -8.948  -22.909 1.00 70.77  ? 683  ARG A CD  1 
ATOM   964  N NE  . ARG A 1 133 ? 16.919  -8.533  -23.560 1.00 73.67  ? 683  ARG A NE  1 
ATOM   965  C CZ  . ARG A 1 133 ? 18.089  -8.382  -22.957 1.00 77.26  ? 683  ARG A CZ  1 
ATOM   966  N NH1 . ARG A 1 133 ? 18.208  -8.613  -21.657 1.00 79.64  ? 683  ARG A NH1 1 
ATOM   967  N NH2 . ARG A 1 133 ? 19.153  -7.995  -23.650 1.00 76.31  ? 683  ARG A NH2 1 
ATOM   968  N N   . ARG A 1 134 ? 10.169  -10.278 -23.340 1.00 75.56  ? 684  ARG A N   1 
ATOM   969  C CA  . ARG A 1 134 ? 9.062   -11.146 -22.982 1.00 79.10  ? 684  ARG A CA  1 
ATOM   970  C C   . ARG A 1 134 ? 8.243   -11.547 -24.247 1.00 81.59  ? 684  ARG A C   1 
ATOM   971  O O   . ARG A 1 134 ? 7.654   -12.628 -24.279 1.00 82.28  ? 684  ARG A O   1 
ATOM   972  C CB  . ARG A 1 134 ? 8.179   -10.453 -21.945 1.00 82.48  ? 684  ARG A CB  1 
ATOM   973  C CG  . ARG A 1 134 ? 8.861   -10.229 -20.606 1.00 89.75  ? 684  ARG A CG  1 
ATOM   974  C CD  . ARG A 1 134 ? 7.860   -10.393 -19.476 1.00 97.36  ? 684  ARG A CD  1 
ATOM   975  N NE  . ARG A 1 134 ? 8.348   -9.870  -18.196 1.00 103.79 ? 684  ARG A NE  1 
ATOM   976  C CZ  . ARG A 1 134 ? 7.784   -10.132 -17.016 1.00 107.31 ? 684  ARG A CZ  1 
ATOM   977  N NH1 . ARG A 1 134 ? 6.711   -10.914 -16.943 1.00 105.96 ? 684  ARG A NH1 1 
ATOM   978  N NH2 . ARG A 1 134 ? 8.292   -9.616  -15.901 1.00 108.28 ? 684  ARG A NH2 1 
ATOM   979  N N   . LYS A 1 135 ? 8.239   -10.696 -25.293 1.00 83.02  ? 685  LYS A N   1 
ATOM   980  C CA  . LYS A 1 135 ? 7.508   -10.943 -26.533 1.00 84.99  ? 685  LYS A CA  1 
ATOM   981  C C   . LYS A 1 135 ? 8.234   -11.875 -27.507 1.00 87.39  ? 685  LYS A C   1 
ATOM   982  O O   . LYS A 1 135 ? 7.811   -11.988 -28.657 1.00 88.08  ? 685  LYS A O   1 
ATOM   983  C CB  . LYS A 1 135 ? 7.106   -9.626  -27.227 1.00 87.30  ? 685  LYS A CB  1 
ATOM   984  C CG  . LYS A 1 135 ? 6.119   -8.756  -26.433 1.00 91.34  ? 685  LYS A CG  1 
ATOM   985  C CD  . LYS A 1 135 ? 4.869   -9.503  -25.997 1.00 96.06  ? 685  LYS A CD  1 
ATOM   986  C CE  . LYS A 1 135 ? 3.886   -8.604  -25.282 1.00 100.80 ? 685  LYS A CE  1 
ATOM   987  N NZ  . LYS A 1 135 ? 3.466   -9.162  -23.956 1.00 103.45 ? 685  LYS A NZ  1 
ATOM   988  N N   . ARG A 1 136 ? 9.305   -12.552 -27.052 1.00 88.47  ? 686  ARG A N   1 
ATOM   989  C CA  . ARG A 1 136 ? 10.024  -13.579 -27.801 1.00 89.90  ? 686  ARG A CA  1 
ATOM   990  C C   . ARG A 1 136 ? 9.402   -14.935 -27.434 1.00 93.29  ? 686  ARG A C   1 
ATOM   991  O O   . ARG A 1 136 ? 8.813   -15.077 -26.351 1.00 94.11  ? 686  ARG A O   1 
ATOM   992  C CB  . ARG A 1 136 ? 11.490  -13.636 -27.365 1.00 88.96  ? 686  ARG A CB  1 
ATOM   993  C CG  . ARG A 1 136 ? 12.395  -12.610 -27.990 1.00 87.57  ? 686  ARG A CG  1 
ATOM   994  C CD  . ARG A 1 136 ? 13.756  -12.740 -27.348 1.00 86.27  ? 686  ARG A CD  1 
ATOM   995  N NE  . ARG A 1 136 ? 14.685  -11.745 -27.867 1.00 84.23  ? 686  ARG A NE  1 
ATOM   996  C CZ  . ARG A 1 136 ? 15.864  -12.020 -28.409 1.00 81.97  ? 686  ARG A CZ  1 
ATOM   997  N NH1 . ARG A 1 136 ? 16.289  -13.276 -28.494 1.00 80.68  ? 686  ARG A NH1 1 
ATOM   998  N NH2 . ARG A 1 136 ? 16.628  -11.047 -28.867 1.00 79.84  ? 686  ARG A NH2 1 
ATOM   999  N N   . ASP A 1 137 ? 9.574   -15.946 -28.315 1.00 94.98  ? 687  ASP A N   1 
ATOM   1000 C CA  . ASP A 1 137 ? 9.103   -17.332 -28.131 1.00 96.75  ? 687  ASP A CA  1 
ATOM   1001 C C   . ASP A 1 137 ? 7.566   -17.459 -28.093 1.00 98.07  ? 687  ASP A C   1 
ATOM   1002 O O   . ASP A 1 137 ? 6.854   -16.473 -27.865 1.00 98.58  ? 687  ASP A O   1 
ATOM   1003 C CB  . ASP A 1 137 ? 9.753   -18.001 -26.892 1.00 98.65  ? 687  ASP A CB  1 
ATOM   1004 C CG  . ASP A 1 137 ? 11.276  -18.133 -26.932 1.00 102.86 ? 687  ASP A CG  1 
ATOM   1005 O OD1 . ASP A 1 137 ? 11.964  -17.105 -27.146 1.00 101.69 ? 687  ASP A OD1 1 
ATOM   1006 O OD2 . ASP A 1 137 ? 11.778  -19.261 -26.729 1.00 106.67 ? 687  ASP A OD2 1 
ATOM   1007 N N   . ASP A 1 152 ? 1.580   -8.607  -21.147 1.00 120.95 ? 760  ASP A N   1 
ATOM   1008 C CA  . ASP A 1 152 ? 0.591   -8.286  -22.169 1.00 121.40 ? 760  ASP A CA  1 
ATOM   1009 C C   . ASP A 1 152 ? 0.260   -9.505  -23.018 1.00 121.27 ? 760  ASP A C   1 
ATOM   1010 O O   . ASP A 1 152 ? 1.135   -10.090 -23.654 1.00 121.79 ? 760  ASP A O   1 
ATOM   1011 C CB  . ASP A 1 152 ? 1.085   -7.146  -23.060 1.00 123.53 ? 760  ASP A CB  1 
ATOM   1012 C CG  . ASP A 1 152 ? 0.035   -6.686  -24.047 1.00 128.10 ? 760  ASP A CG  1 
ATOM   1013 O OD1 . ASP A 1 152 ? -1.031  -7.331  -24.120 1.00 128.55 ? 760  ASP A OD1 1 
ATOM   1014 O OD2 . ASP A 1 152 ? 0.276   -5.684  -24.751 1.00 130.07 ? 760  ASP A OD2 1 
ATOM   1015 N N   . GLU A 1 153 ? -1.014  -9.877  -23.020 1.00 120.30 ? 761  GLU A N   1 
ATOM   1016 C CA  . GLU A 1 153 ? -1.504  -11.029 -23.771 1.00 119.55 ? 761  GLU A CA  1 
ATOM   1017 C C   . GLU A 1 153 ? -1.345  -10.890 -25.287 1.00 118.17 ? 761  GLU A C   1 
ATOM   1018 O O   . GLU A 1 153 ? -1.030  -11.857 -25.977 1.00 118.45 ? 761  GLU A O   1 
ATOM   1019 C CB  . GLU A 1 153 ? -2.969  -11.291 -23.419 1.00 122.03 ? 761  GLU A CB  1 
ATOM   1020 C CG  . GLU A 1 153 ? -3.249  -11.269 -21.924 1.00 127.11 ? 761  GLU A CG  1 
ATOM   1021 C CD  . GLU A 1 153 ? -4.729  -11.355 -21.603 1.00 133.87 ? 761  GLU A CD  1 
ATOM   1022 O OE1 . GLU A 1 153 ? -5.495  -11.854 -22.453 1.00 134.43 ? 761  GLU A OE1 1 
ATOM   1023 O OE2 . GLU A 1 153 ? -5.124  -10.924 -20.499 1.00 136.28 ? 761  GLU A OE2 1 
ATOM   1024 N N   . LEU A 1 154 ? -1.576  -9.686  -25.796 1.00 116.43 ? 762  LEU A N   1 
ATOM   1025 C CA  . LEU A 1 154 ? -1.499  -9.412  -27.230 1.00 114.86 ? 762  LEU A CA  1 
ATOM   1026 C C   . LEU A 1 154 ? -0.115  -9.590  -27.862 1.00 112.57 ? 762  LEU A C   1 
ATOM   1027 O O   . LEU A 1 154 ? 0.908   -9.277  -27.258 1.00 112.58 ? 762  LEU A O   1 
ATOM   1028 C CB  . LEU A 1 154 ? -2.013  -7.999  -27.513 1.00 115.31 ? 762  LEU A CB  1 
ATOM   1029 C CG  . LEU A 1 154 ? -2.148  -7.585  -28.979 1.00 117.05 ? 762  LEU A CG  1 
ATOM   1030 C CD1 . LEU A 1 154 ? -3.197  -8.441  -29.671 1.00 117.62 ? 762  LEU A CD1 1 
ATOM   1031 C CD2 . LEU A 1 154 ? -2.495  -6.108  -29.091 1.00 117.57 ? 762  LEU A CD2 1 
ATOM   1032 N N   . ALA A 1 155 ? -0.108  -10.112 -29.085 1.00 110.38 ? 763  ALA A N   1 
ATOM   1033 C CA  . ALA A 1 155 ? 1.113   -10.326 -29.855 1.00 108.49 ? 763  ALA A CA  1 
ATOM   1034 C C   . ALA A 1 155 ? 1.665   -9.012  -30.399 1.00 106.07 ? 763  ALA A C   1 
ATOM   1035 O O   . ALA A 1 155 ? 0.937   -8.032  -30.532 1.00 105.97 ? 763  ALA A O   1 
ATOM   1036 C CB  . ALA A 1 155 ? 0.863   -11.306 -30.989 1.00 108.62 ? 763  ALA A CB  1 
ATOM   1037 N N   . LEU A 1 156 ? 2.954   -9.002  -30.718 1.00 104.05 ? 764  LEU A N   1 
ATOM   1038 C CA  . LEU A 1 156 ? 3.615   -7.809  -31.235 1.00 102.51 ? 764  LEU A CA  1 
ATOM   1039 C C   . LEU A 1 156 ? 3.942   -7.958  -32.716 1.00 101.35 ? 764  LEU A C   1 
ATOM   1040 O O   . LEU A 1 156 ? 4.500   -8.967  -33.135 1.00 101.66 ? 764  LEU A O   1 
ATOM   1041 C CB  . LEU A 1 156 ? 4.891   -7.541  -30.438 1.00 102.23 ? 764  LEU A CB  1 
ATOM   1042 C CG  . LEU A 1 156 ? 5.697   -6.284  -30.760 1.00 102.84 ? 764  LEU A CG  1 
ATOM   1043 C CD1 . LEU A 1 156 ? 4.863   -5.037  -30.522 1.00 103.05 ? 764  LEU A CD1 1 
ATOM   1044 C CD2 . LEU A 1 156 ? 6.955   -6.254  -29.910 1.00 103.24 ? 764  LEU A CD2 1 
ATOM   1045 N N   . ASP A 1 157 ? 3.583   -6.953  -33.509 1.00 99.78  ? 765  ASP A N   1 
ATOM   1046 C CA  . ASP A 1 157 ? 3.833   -6.991  -34.947 1.00 98.73  ? 765  ASP A CA  1 
ATOM   1047 C C   . ASP A 1 157 ? 4.716   -5.851  -35.451 1.00 96.66  ? 765  ASP A C   1 
ATOM   1048 O O   . ASP A 1 157 ? 5.108   -4.970  -34.692 1.00 96.99  ? 765  ASP A O   1 
ATOM   1049 C CB  . ASP A 1 157 ? 2.511   -7.016  -35.716 1.00 101.38 ? 765  ASP A CB  1 
ATOM   1050 C CG  . ASP A 1 157 ? 1.636   -5.819  -35.410 1.00 107.35 ? 765  ASP A CG  1 
ATOM   1051 O OD1 . ASP A 1 157 ? 2.184   -4.714  -35.211 1.00 107.97 ? 765  ASP A OD1 1 
ATOM   1052 O OD2 . ASP A 1 157 ? 0.400   -5.984  -35.366 1.00 109.70 ? 765  ASP A OD2 1 
ATOM   1053 N N   . LEU A 1 158 ? 5.014   -5.877  -36.745 1.00 94.68  ? 766  LEU A N   1 
ATOM   1054 C CA  . LEU A 1 158 ? 5.865   -4.873  -37.377 1.00 93.81  ? 766  LEU A CA  1 
ATOM   1055 C C   . LEU A 1 158 ? 5.308   -3.461  -37.215 1.00 92.73  ? 766  LEU A C   1 
ATOM   1056 O O   . LEU A 1 158 ? 6.070   -2.507  -37.079 1.00 92.90  ? 766  LEU A O   1 
ATOM   1057 C CB  . LEU A 1 158 ? 6.052   -5.197  -38.863 1.00 94.33  ? 766  LEU A CB  1 
ATOM   1058 C CG  . LEU A 1 158 ? 6.947   -4.234  -39.636 1.00 96.26  ? 766  LEU A CG  1 
ATOM   1059 C CD1 . LEU A 1 158 ? 8.421   -4.609  -39.485 1.00 97.03  ? 766  LEU A CD1 1 
ATOM   1060 C CD2 . LEU A 1 158 ? 6.531   -4.151  -41.095 1.00 96.62  ? 766  LEU A CD2 1 
ATOM   1061 N N   . GLU A 1 159 ? 3.977   -3.329  -37.202 1.00 91.44  ? 767  GLU A N   1 
ATOM   1062 C CA  . GLU A 1 159 ? 3.295   -2.047  -37.028 1.00 90.49  ? 767  GLU A CA  1 
ATOM   1063 C C   . GLU A 1 159 ? 3.577   -1.421  -35.645 1.00 88.01  ? 767  GLU A C   1 
ATOM   1064 O O   . GLU A 1 159 ? 3.547   -0.193  -35.500 1.00 88.30  ? 767  GLU A O   1 
ATOM   1065 C CB  . GLU A 1 159 ? 1.788   -2.225  -37.283 1.00 94.09  ? 767  GLU A CB  1 
ATOM   1066 C CG  . GLU A 1 159 ? 0.959   -0.958  -37.204 1.00 101.54 ? 767  GLU A CG  1 
ATOM   1067 C CD  . GLU A 1 159 ? -0.408  -1.082  -37.854 1.00 113.41 ? 767  GLU A CD  1 
ATOM   1068 O OE1 . GLU A 1 159 ? -1.310  -0.289  -37.492 1.00 114.99 ? 767  GLU A OE1 1 
ATOM   1069 O OE2 . GLU A 1 159 ? -0.578  -1.969  -38.726 1.00 118.28 ? 767  GLU A OE2 1 
ATOM   1070 N N   . ASP A 1 160 ? 3.890   -2.261  -34.644 1.00 85.14  ? 768  ASP A N   1 
ATOM   1071 C CA  . ASP A 1 160 ? 4.214   -1.794  -33.315 1.00 82.63  ? 768  ASP A CA  1 
ATOM   1072 C C   . ASP A 1 160 ? 5.625   -1.297  -33.321 1.00 80.03  ? 768  ASP A C   1 
ATOM   1073 O O   . ASP A 1 160 ? 5.855   -0.161  -32.939 1.00 80.09  ? 768  ASP A O   1 
ATOM   1074 C CB  . ASP A 1 160 ? 4.032   -2.911  -32.286 1.00 84.38  ? 768  ASP A CB  1 
ATOM   1075 C CG  . ASP A 1 160 ? 2.591   -3.348  -32.166 1.00 90.46  ? 768  ASP A CG  1 
ATOM   1076 O OD1 . ASP A 1 160 ? 1.705   -2.461  -32.086 1.00 91.19  ? 768  ASP A OD1 1 
ATOM   1077 O OD2 . ASP A 1 160 ? 2.341   -4.579  -32.173 1.00 93.08  ? 768  ASP A OD2 1 
ATOM   1078 N N   . LEU A 1 161 ? 6.566   -2.103  -33.824 1.00 77.73  ? 769  LEU A N   1 
ATOM   1079 C CA  . LEU A 1 161 ? 7.983   -1.756  -33.879 1.00 75.86  ? 769  LEU A CA  1 
ATOM   1080 C C   . LEU A 1 161 ? 8.256   -0.472  -34.658 1.00 74.38  ? 769  LEU A C   1 
ATOM   1081 O O   . LEU A 1 161 ? 9.122   0.312   -34.282 1.00 74.34  ? 769  LEU A O   1 
ATOM   1082 C CB  . LEU A 1 161 ? 8.774   -2.911  -34.479 1.00 75.86  ? 769  LEU A CB  1 
ATOM   1083 C CG  . LEU A 1 161 ? 8.584   -4.276  -33.824 1.00 77.06  ? 769  LEU A CG  1 
ATOM   1084 C CD1 . LEU A 1 161 ? 9.400   -5.320  -34.532 1.00 77.44  ? 769  LEU A CD1 1 
ATOM   1085 C CD2 . LEU A 1 161 ? 8.968   -4.247  -32.354 1.00 77.40  ? 769  LEU A CD2 1 
ATOM   1086 N N   . LEU A 1 162 ? 7.526   -0.260  -35.738 1.00 73.23  ? 770  LEU A N   1 
ATOM   1087 C CA  . LEU A 1 162 ? 7.652   0.948   -36.543 1.00 72.35  ? 770  LEU A CA  1 
ATOM   1088 C C   . LEU A 1 162 ? 7.158   2.159   -35.779 1.00 70.36  ? 770  LEU A C   1 
ATOM   1089 O O   . LEU A 1 162 ? 7.701   3.240   -35.948 1.00 70.79  ? 770  LEU A O   1 
ATOM   1090 C CB  . LEU A 1 162 ? 6.830   0.812   -37.828 1.00 73.20  ? 770  LEU A CB  1 
ATOM   1091 C CG  . LEU A 1 162 ? 7.372   -0.132  -38.875 1.00 74.93  ? 770  LEU A CG  1 
ATOM   1092 C CD1 . LEU A 1 162 ? 6.438   -0.195  -40.036 1.00 75.57  ? 770  LEU A CD1 1 
ATOM   1093 C CD2 . LEU A 1 162 ? 8.762   0.290   -39.337 1.00 75.49  ? 770  LEU A CD2 1 
ATOM   1094 N N   . SER A 1 163 ? 6.114   1.984   -34.964 1.00 68.31  ? 771  SER A N   1 
ATOM   1095 C CA  . SER A 1 163 ? 5.493   3.013   -34.143 1.00 66.56  ? 771  SER A CA  1 
ATOM   1096 C C   . SER A 1 163 ? 6.429   3.382   -33.000 1.00 65.41  ? 771  SER A C   1 
ATOM   1097 O O   . SER A 1 163 ? 6.583   4.550   -32.701 1.00 65.85  ? 771  SER A O   1 
ATOM   1098 C CB  . SER A 1 163 ? 4.153   2.499   -33.617 1.00 66.98  ? 771  SER A CB  1 
ATOM   1099 O OG  . SER A 1 163 ? 3.598   3.278   -32.573 1.00 68.72  ? 771  SER A OG  1 
ATOM   1100 N N   . PHE A 1 164 ? 7.080   2.386   -32.369 1.00 63.84  ? 772  PHE A N   1 
ATOM   1101 C CA  . PHE A 1 164 ? 8.027   2.637   -31.301 1.00 62.11  ? 772  PHE A CA  1 
ATOM   1102 C C   . PHE A 1 164 ? 9.224   3.418   -31.845 1.00 63.07  ? 772  PHE A C   1 
ATOM   1103 O O   . PHE A 1 164 ? 9.692   4.349   -31.203 1.00 63.29  ? 772  PHE A O   1 
ATOM   1104 C CB  . PHE A 1 164 ? 8.493   1.330   -30.687 1.00 60.63  ? 772  PHE A CB  1 
ATOM   1105 C CG  . PHE A 1 164 ? 7.443   0.479   -30.022 1.00 60.32  ? 772  PHE A CG  1 
ATOM   1106 C CD1 . PHE A 1 164 ? 6.224   1.008   -29.666 1.00 60.86  ? 772  PHE A CD1 1 
ATOM   1107 C CD2 . PHE A 1 164 ? 7.684   -0.855  -29.750 1.00 60.82  ? 772  PHE A CD2 1 
ATOM   1108 C CE1 . PHE A 1 164 ? 5.275   0.225   -29.040 1.00 62.13  ? 772  PHE A CE1 1 
ATOM   1109 C CE2 . PHE A 1 164 ? 6.730   -1.642  -29.129 1.00 61.39  ? 772  PHE A CE2 1 
ATOM   1110 C CZ  . PHE A 1 164 ? 5.534   -1.102  -28.778 1.00 61.69  ? 772  PHE A CZ  1 
ATOM   1111 N N   . SER A 1 165 ? 9.681   3.080   -33.050 1.00 63.65  ? 773  SER A N   1 
ATOM   1112 C CA  . SER A 1 165 ? 10.785  3.760   -33.708 1.00 64.66  ? 773  SER A CA  1 
ATOM   1113 C C   . SER A 1 165 ? 10.427  5.205   -33.964 1.00 65.29  ? 773  SER A C   1 
ATOM   1114 O O   . SER A 1 165 ? 11.241  6.093   -33.726 1.00 65.86  ? 773  SER A O   1 
ATOM   1115 C CB  . SER A 1 165 ? 11.091  3.095   -35.041 1.00 67.11  ? 773  SER A CB  1 
ATOM   1116 O OG  . SER A 1 165 ? 11.165  1.687   -34.910 1.00 72.05  ? 773  SER A OG  1 
ATOM   1117 N N   . TYR A 1 166 ? 9.209   5.440   -34.437 1.00 64.98  ? 774  TYR A N   1 
ATOM   1118 C CA  . TYR A 1 166 ? 8.682   6.751   -34.749 1.00 65.45  ? 774  TYR A CA  1 
ATOM   1119 C C   . TYR A 1 166 ? 8.541   7.621   -33.476 1.00 64.51  ? 774  TYR A C   1 
ATOM   1120 O O   . TYR A 1 166 ? 8.928   8.796   -33.479 1.00 64.31  ? 774  TYR A O   1 
ATOM   1121 C CB  . TYR A 1 166 ? 7.318   6.546   -35.420 1.00 66.43  ? 774  TYR A CB  1 
ATOM   1122 C CG  . TYR A 1 166 ? 6.627   7.818   -35.823 1.00 68.71  ? 774  TYR A CG  1 
ATOM   1123 C CD1 . TYR A 1 166 ? 7.284   8.777   -36.581 1.00 70.34  ? 774  TYR A CD1 1 
ATOM   1124 C CD2 . TYR A 1 166 ? 5.297   8.036   -35.506 1.00 70.50  ? 774  TYR A CD2 1 
ATOM   1125 C CE1 . TYR A 1 166 ? 6.643   9.938   -36.986 1.00 72.19  ? 774  TYR A CE1 1 
ATOM   1126 C CE2 . TYR A 1 166 ? 4.637   9.181   -35.924 1.00 72.35  ? 774  TYR A CE2 1 
ATOM   1127 C CZ  . TYR A 1 166 ? 5.311   10.132  -36.670 1.00 74.14  ? 774  TYR A CZ  1 
ATOM   1128 O OH  . TYR A 1 166 ? 4.656   11.280  -37.077 1.00 77.09  ? 774  TYR A OH  1 
ATOM   1129 N N   . GLN A 1 167 ? 8.000   7.031   -32.396 1.00 63.17  ? 775  GLN A N   1 
ATOM   1130 C CA  . GLN A 1 167 ? 7.776   7.751   -31.165 1.00 62.62  ? 775  GLN A CA  1 
ATOM   1131 C C   . GLN A 1 167 ? 9.074   8.065   -30.447 1.00 61.51  ? 775  GLN A C   1 
ATOM   1132 O O   . GLN A 1 167 ? 9.206   9.172   -29.913 1.00 61.54  ? 775  GLN A O   1 
ATOM   1133 C CB  . GLN A 1 167 ? 6.843   6.970   -30.254 1.00 64.39  ? 775  GLN A CB  1 
ATOM   1134 C CG  . GLN A 1 167 ? 5.476   6.677   -30.841 1.00 66.60  ? 775  GLN A CG  1 
ATOM   1135 C CD  . GLN A 1 167 ? 4.655   5.917   -29.833 1.00 68.71  ? 775  GLN A CD  1 
ATOM   1136 O OE1 . GLN A 1 167 ? 4.206   6.475   -28.831 1.00 71.77  ? 775  GLN A OE1 1 
ATOM   1137 N NE2 . GLN A 1 167 ? 4.473   4.632   -30.043 1.00 66.65  ? 775  GLN A NE2 1 
ATOM   1138 N N   . VAL A 1 168 ? 10.054  7.120   -30.445 1.00 59.80  ? 776  VAL A N   1 
ATOM   1139 C CA  . VAL A 1 168 ? 11.351  7.390   -29.807 1.00 58.55  ? 776  VAL A CA  1 
ATOM   1140 C C   . VAL A 1 168 ? 12.049  8.539   -30.551 1.00 58.09  ? 776  VAL A C   1 
ATOM   1141 O O   . VAL A 1 168 ? 12.529  9.463   -29.916 1.00 57.37  ? 776  VAL A O   1 
ATOM   1142 C CB  . VAL A 1 168 ? 12.256  6.133   -29.631 1.00 58.48  ? 776  VAL A CB  1 
ATOM   1143 C CG1 . VAL A 1 168 ? 13.662  6.516   -29.179 1.00 58.74  ? 776  VAL A CG1 1 
ATOM   1144 C CG2 . VAL A 1 168 ? 11.640  5.129   -28.660 1.00 58.36  ? 776  VAL A CG2 1 
ATOM   1145 N N   . ALA A 1 169 ? 11.965  8.551   -31.887 1.00 58.52  ? 777  ALA A N   1 
ATOM   1146 C CA  . ALA A 1 169 ? 12.525  9.619   -32.718 1.00 59.43  ? 777  ALA A CA  1 
ATOM   1147 C C   . ALA A 1 169 ? 11.855  10.972  -32.481 1.00 60.48  ? 777  ALA A C   1 
ATOM   1148 O O   . ALA A 1 169 ? 12.537  11.993  -32.518 1.00 61.04  ? 777  ALA A O   1 
ATOM   1149 C CB  . ALA A 1 169 ? 12.436  9.245   -34.190 1.00 59.63  ? 777  ALA A CB  1 
ATOM   1150 N N   . LYS A 1 170 ? 10.528  11.000  -32.246 1.00 60.57  ? 778  LYS A N   1 
ATOM   1151 C CA  . LYS A 1 170 ? 9.833   12.259  -31.959 1.00 60.49  ? 778  LYS A CA  1 
ATOM   1152 C C   . LYS A 1 170 ? 10.295  12.810  -30.612 1.00 59.57  ? 778  LYS A C   1 
ATOM   1153 O O   . LYS A 1 170 ? 10.523  14.026  -30.485 1.00 60.03  ? 778  LYS A O   1 
ATOM   1154 C CB  . LYS A 1 170 ? 8.301   12.085  -31.984 1.00 63.15  ? 778  LYS A CB  1 
ATOM   1155 C CG  . LYS A 1 170 ? 7.753   11.777  -33.373 1.00 68.36  ? 778  LYS A CG  1 
ATOM   1156 C CD  . LYS A 1 170 ? 6.222   11.835  -33.454 1.00 74.72  ? 778  LYS A CD  1 
ATOM   1157 C CE  . LYS A 1 170 ? 5.526   10.725  -32.694 1.00 80.35  ? 778  LYS A CE  1 
ATOM   1158 N NZ  . LYS A 1 170 ? 4.669   11.246  -31.585 1.00 83.41  ? 778  LYS A NZ  1 
ATOM   1159 N N   . GLY A 1 171 ? 10.420  11.909  -29.626 1.00 57.91  ? 779  GLY A N   1 
ATOM   1160 C CA  . GLY A 1 171 ? 10.880  12.224  -28.282 1.00 56.96  ? 779  GLY A CA  1 
ATOM   1161 C C   . GLY A 1 171 ? 12.314  12.709  -28.295 1.00 56.47  ? 779  GLY A C   1 
ATOM   1162 O O   . GLY A 1 171 ? 12.663  13.689  -27.618 1.00 57.11  ? 779  GLY A O   1 
ATOM   1163 N N   . MET A 1 172 ? 13.142  12.076  -29.114 1.00 55.59  ? 780  MET A N   1 
ATOM   1164 C CA  . MET A 1 172 ? 14.519  12.480  -29.263 1.00 55.74  ? 780  MET A CA  1 
ATOM   1165 C C   . MET A 1 172 ? 14.643  13.823  -29.964 1.00 57.48  ? 780  MET A C   1 
ATOM   1166 O O   . MET A 1 172 ? 15.365  14.694  -29.458 1.00 57.67  ? 780  MET A O   1 
ATOM   1167 C CB  . MET A 1 172 ? 15.351  11.391  -29.899 1.00 55.09  ? 780  MET A CB  1 
ATOM   1168 C CG  . MET A 1 172 ? 15.635  10.239  -28.954 1.00 56.10  ? 780  MET A CG  1 
ATOM   1169 S SD  . MET A 1 172 ? 16.297  10.746  -27.325 1.00 60.05  ? 780  MET A SD  1 
ATOM   1170 C CE  . MET A 1 172 ? 17.856  11.305  -27.771 1.00 53.98  ? 780  MET A CE  1 
ATOM   1171 N N   . ALA A 1 173 ? 13.848  14.059  -31.034 1.00 57.81  ? 781  ALA A N   1 
ATOM   1172 C CA  . ALA A 1 173 ? 13.861  15.374  -31.685 1.00 58.14  ? 781  ALA A CA  1 
ATOM   1173 C C   . ALA A 1 173 ? 13.326  16.459  -30.749 1.00 58.82  ? 781  ALA A C   1 
ATOM   1174 O O   . ALA A 1 173 ? 13.747  17.609  -30.858 1.00 59.65  ? 781  ALA A O   1 
ATOM   1175 C CB  . ALA A 1 173 ? 13.086  15.357  -32.998 1.00 57.73  ? 781  ALA A CB  1 
ATOM   1176 N N   . PHE A 1 174 ? 12.460  16.106  -29.784 1.00 58.47  ? 782  PHE A N   1 
ATOM   1177 C CA  . PHE A 1 174 ? 11.956  17.092  -28.817 1.00 57.96  ? 782  PHE A CA  1 
ATOM   1178 C C   . PHE A 1 174 ? 13.097  17.510  -27.888 1.00 58.80  ? 782  PHE A C   1 
ATOM   1179 O O   . PHE A 1 174 ? 13.253  18.701  -27.601 1.00 60.18  ? 782  PHE A O   1 
ATOM   1180 C CB  . PHE A 1 174 ? 10.797  16.504  -28.002 1.00 56.87  ? 782  PHE A CB  1 
ATOM   1181 C CG  . PHE A 1 174 ? 10.376  17.413  -26.882 1.00 56.37  ? 782  PHE A CG  1 
ATOM   1182 C CD1 . PHE A 1 174 ? 9.676   18.587  -27.145 1.00 56.34  ? 782  PHE A CD1 1 
ATOM   1183 C CD2 . PHE A 1 174 ? 10.729  17.136  -25.576 1.00 56.22  ? 782  PHE A CD2 1 
ATOM   1184 C CE1 . PHE A 1 174 ? 9.294   19.422  -26.121 1.00 56.16  ? 782  PHE A CE1 1 
ATOM   1185 C CE2 . PHE A 1 174 ? 10.368  17.998  -24.554 1.00 56.44  ? 782  PHE A CE2 1 
ATOM   1186 C CZ  . PHE A 1 174 ? 9.652   19.130  -24.837 1.00 56.07  ? 782  PHE A CZ  1 
ATOM   1187 N N   . LEU A 1 175 ? 13.891  16.530  -27.421 1.00 58.04  ? 783  LEU A N   1 
ATOM   1188 C CA  . LEU A 1 175 ? 15.044  16.769  -26.566 1.00 57.86  ? 783  LEU A CA  1 
ATOM   1189 C C   . LEU A 1 175 ? 16.054  17.631  -27.303 1.00 59.92  ? 783  LEU A C   1 
ATOM   1190 O O   . LEU A 1 175 ? 16.479  18.655  -26.767 1.00 60.76  ? 783  LEU A O   1 
ATOM   1191 C CB  . LEU A 1 175 ? 15.705  15.440  -26.119 1.00 56.27  ? 783  LEU A CB  1 
ATOM   1192 C CG  . LEU A 1 175 ? 14.953  14.622  -25.047 1.00 55.22  ? 783  LEU A CG  1 
ATOM   1193 C CD1 . LEU A 1 175 ? 15.770  13.450  -24.613 1.00 54.81  ? 783  LEU A CD1 1 
ATOM   1194 C CD2 . LEU A 1 175 ? 14.543  15.489  -23.823 1.00 54.84  ? 783  LEU A CD2 1 
ATOM   1195 N N   . ALA A 1 176 ? 16.362  17.285  -28.564 1.00 60.34  ? 784  ALA A N   1 
ATOM   1196 C CA  . ALA A 1 176 ? 17.293  18.027  -29.396 1.00 61.40  ? 784  ALA A CA  1 
ATOM   1197 C C   . ALA A 1 176 ? 16.812  19.449  -29.590 1.00 63.46  ? 784  ALA A C   1 
ATOM   1198 O O   . ALA A 1 176 ? 17.616  20.383  -29.463 1.00 63.87  ? 784  ALA A O   1 
ATOM   1199 C CB  . ALA A 1 176 ? 17.437  17.345  -30.725 1.00 61.87  ? 784  ALA A CB  1 
ATOM   1200 N N   . SER A 1 177 ? 15.478  19.640  -29.750 1.00 63.95  ? 785  SER A N   1 
ATOM   1201 C CA  . SER A 1 177 ? 14.914  20.981  -29.876 1.00 64.19  ? 785  SER A CA  1 
ATOM   1202 C C   . SER A 1 177 ? 15.106  21.811  -28.618 1.00 64.65  ? 785  SER A C   1 
ATOM   1203 O O   . SER A 1 177 ? 15.174  23.033  -28.699 1.00 66.16  ? 785  SER A O   1 
ATOM   1204 C CB  . SER A 1 177 ? 13.456  20.937  -30.309 1.00 66.05  ? 785  SER A CB  1 
ATOM   1205 O OG  . SER A 1 177 ? 12.573  20.729  -29.223 1.00 70.47  ? 785  SER A OG  1 
ATOM   1206 N N   . LYS A 1 178 ? 15.217  21.168  -27.450 1.00 63.30  ? 786  LYS A N   1 
ATOM   1207 C CA  . LYS A 1 178 ? 15.499  21.871  -26.201 1.00 61.65  ? 786  LYS A CA  1 
ATOM   1208 C C   . LYS A 1 178 ? 17.015  21.956  -25.912 1.00 61.08  ? 786  LYS A C   1 
ATOM   1209 O O   . LYS A 1 178 ? 17.393  22.292  -24.803 1.00 60.91  ? 786  LYS A O   1 
ATOM   1210 C CB  . LYS A 1 178 ? 14.767  21.187  -25.030 1.00 61.97  ? 786  LYS A CB  1 
ATOM   1211 C CG  . LYS A 1 178 ? 13.248  21.378  -25.036 1.00 64.94  ? 786  LYS A CG  1 
ATOM   1212 C CD  . LYS A 1 178 ? 12.862  22.829  -24.999 1.00 69.94  ? 786  LYS A CD  1 
ATOM   1213 C CE  . LYS A 1 178 ? 11.495  23.088  -24.448 1.00 75.31  ? 786  LYS A CE  1 
ATOM   1214 N NZ  . LYS A 1 178 ? 11.526  24.122  -23.362 1.00 77.51  ? 786  LYS A NZ  1 
ATOM   1215 N N   . ASN A 1 179 ? 17.881  21.655  -26.908 1.00 61.27  ? 787  ASN A N   1 
ATOM   1216 C CA  . ASN A 1 179 ? 19.345  21.636  -26.813 1.00 61.51  ? 787  ASN A CA  1 
ATOM   1217 C C   . ASN A 1 179 ? 19.814  20.657  -25.748 1.00 61.11  ? 787  ASN A C   1 
ATOM   1218 O O   . ASN A 1 179 ? 20.767  20.931  -25.015 1.00 60.20  ? 787  ASN A O   1 
ATOM   1219 C CB  . ASN A 1 179 ? 19.923  23.028  -26.573 1.00 63.24  ? 787  ASN A CB  1 
ATOM   1220 C CG  . ASN A 1 179 ? 19.595  23.975  -27.677 1.00 67.35  ? 787  ASN A CG  1 
ATOM   1221 O OD1 . ASN A 1 179 ? 19.722  23.644  -28.871 1.00 68.80  ? 787  ASN A OD1 1 
ATOM   1222 N ND2 . ASN A 1 179 ? 19.146  25.160  -27.291 1.00 68.63  ? 787  ASN A ND2 1 
ATOM   1223 N N   . CYS A 1 180 ? 19.139  19.492  -25.686 1.00 61.33  ? 788  CYS A N   1 
ATOM   1224 C CA  . CYS A 1 180 ? 19.439  18.483  -24.699 1.00 61.53  ? 788  CYS A CA  1 
ATOM   1225 C C   . CYS A 1 180 ? 20.026  17.196  -25.295 1.00 61.04  ? 788  CYS A C   1 
ATOM   1226 O O   . CYS A 1 180 ? 19.448  16.578  -26.182 1.00 61.49  ? 788  CYS A O   1 
ATOM   1227 C CB  . CYS A 1 180 ? 18.227  18.203  -23.818 1.00 62.03  ? 788  CYS A CB  1 
ATOM   1228 S SG  . CYS A 1 180 ? 18.505  16.908  -22.582 1.00 65.73  ? 788  CYS A SG  1 
ATOM   1229 N N   . ILE A 1 181 ? 21.175  16.801  -24.768 1.00 59.73  ? 789  ILE A N   1 
ATOM   1230 C CA  . ILE A 1 181 ? 21.819  15.583  -25.156 1.00 59.50  ? 789  ILE A CA  1 
ATOM   1231 C C   . ILE A 1 181 ? 21.522  14.580  -24.044 1.00 57.97  ? 789  ILE A C   1 
ATOM   1232 O O   . ILE A 1 181 ? 21.941  14.788  -22.910 1.00 58.08  ? 789  ILE A O   1 
ATOM   1233 C CB  . ILE A 1 181 ? 23.338  15.806  -25.329 1.00 60.87  ? 789  ILE A CB  1 
ATOM   1234 C CG1 . ILE A 1 181 ? 23.614  16.852  -26.399 1.00 62.47  ? 789  ILE A CG1 1 
ATOM   1235 C CG2 . ILE A 1 181 ? 24.064  14.485  -25.653 1.00 61.35  ? 789  ILE A CG2 1 
ATOM   1236 C CD1 . ILE A 1 181 ? 24.806  17.716  -26.061 1.00 64.02  ? 789  ILE A CD1 1 
ATOM   1237 N N   . HIS A 1 182 ? 20.776  13.529  -24.358 1.00 56.44  ? 790  HIS A N   1 
ATOM   1238 C CA  . HIS A 1 182 ? 20.423  12.482  -23.403 1.00 56.11  ? 790  HIS A CA  1 
ATOM   1239 C C   . HIS A 1 182 ? 21.668  11.750  -22.853 1.00 55.87  ? 790  HIS A C   1 
ATOM   1240 O O   . HIS A 1 182 ? 21.854  11.726  -21.651 1.00 55.72  ? 790  HIS A O   1 
ATOM   1241 C CB  . HIS A 1 182 ? 19.412  11.518  -24.040 1.00 56.36  ? 790  HIS A CB  1 
ATOM   1242 C CG  . HIS A 1 182 ? 18.840  10.502  -23.092 1.00 56.72  ? 790  HIS A CG  1 
ATOM   1243 N ND1 . HIS A 1 182 ? 19.609  9.467   -22.598 1.00 57.41  ? 790  HIS A ND1 1 
ATOM   1244 C CD2 . HIS A 1 182 ? 17.572  10.359  -22.637 1.00 56.56  ? 790  HIS A CD2 1 
ATOM   1245 C CE1 . HIS A 1 182 ? 18.789  8.732   -21.866 1.00 57.63  ? 790  HIS A CE1 1 
ATOM   1246 N NE2 . HIS A 1 182 ? 17.563  9.241   -21.846 1.00 57.36  ? 790  HIS A NE2 1 
ATOM   1247 N N   . ARG A 1 183 ? 22.529  11.203  -23.729 1.00 56.01  ? 791  ARG A N   1 
ATOM   1248 C CA  . ARG A 1 183 ? 23.791  10.525  -23.375 1.00 56.90  ? 791  ARG A CA  1 
ATOM   1249 C C   . ARG A 1 183 ? 23.653  9.056   -22.971 1.00 56.73  ? 791  ARG A C   1 
ATOM   1250 O O   . ARG A 1 183 ? 24.671  8.381   -22.808 1.00 57.13  ? 791  ARG A O   1 
ATOM   1251 C CB  . ARG A 1 183 ? 24.589  11.268  -22.313 1.00 59.29  ? 791  ARG A CB  1 
ATOM   1252 C CG  . ARG A 1 183 ? 25.432  12.406  -22.857 1.00 65.26  ? 791  ARG A CG  1 
ATOM   1253 C CD  . ARG A 1 183 ? 26.099  13.230  -21.765 1.00 70.53  ? 791  ARG A CD  1 
ATOM   1254 N NE  . ARG A 1 183 ? 26.557  12.408  -20.640 1.00 76.10  ? 791  ARG A NE  1 
ATOM   1255 C CZ  . ARG A 1 183 ? 27.699  12.589  -19.992 1.00 80.39  ? 791  ARG A CZ  1 
ATOM   1256 N NH1 . ARG A 1 183 ? 28.518  13.576  -20.340 1.00 81.36  ? 791  ARG A NH1 1 
ATOM   1257 N NH2 . ARG A 1 183 ? 28.032  11.789  -18.987 1.00 80.72  ? 791  ARG A NH2 1 
ATOM   1258 N N   . ASP A 1 184 ? 22.420  8.553   -22.812 1.00 55.82  ? 792  ASP A N   1 
ATOM   1259 C CA  . ASP A 1 184 ? 22.210  7.144   -22.500 1.00 54.71  ? 792  ASP A CA  1 
ATOM   1260 C C   . ASP A 1 184 ? 20.924  6.629   -23.151 1.00 54.88  ? 792  ASP A C   1 
ATOM   1261 O O   . ASP A 1 184 ? 20.083  6.016   -22.485 1.00 55.63  ? 792  ASP A O   1 
ATOM   1262 C CB  . ASP A 1 184 ? 22.258  6.831   -21.006 1.00 54.96  ? 792  ASP A CB  1 
ATOM   1263 C CG  . ASP A 1 184 ? 22.461  5.349   -20.679 1.00 60.97  ? 792  ASP A CG  1 
ATOM   1264 O OD1 . ASP A 1 184 ? 22.696  4.547   -21.628 1.00 60.66  ? 792  ASP A OD1 1 
ATOM   1265 O OD2 . ASP A 1 184 ? 22.359  4.983   -19.478 1.00 63.77  ? 792  ASP A OD2 1 
ATOM   1266 N N   . LEU A 1 185 ? 20.779  6.869   -24.465 1.00 53.49  ? 793  LEU A N   1 
ATOM   1267 C CA  . LEU A 1 185 ? 19.609  6.390   -25.174 1.00 52.88  ? 793  LEU A CA  1 
ATOM   1268 C C   . LEU A 1 185 ? 19.829  4.946   -25.516 1.00 52.31  ? 793  LEU A C   1 
ATOM   1269 O O   . LEU A 1 185 ? 20.806  4.598   -26.166 1.00 52.65  ? 793  LEU A O   1 
ATOM   1270 C CB  . LEU A 1 185 ? 19.377  7.202   -26.430 1.00 53.19  ? 793  LEU A CB  1 
ATOM   1271 C CG  . LEU A 1 185 ? 18.227  6.780   -27.299 1.00 54.15  ? 793  LEU A CG  1 
ATOM   1272 C CD1 . LEU A 1 185 ? 16.902  6.907   -26.552 1.00 54.12  ? 793  LEU A CD1 1 
ATOM   1273 C CD2 . LEU A 1 185 ? 18.252  7.586   -28.571 1.00 54.67  ? 793  LEU A CD2 1 
ATOM   1274 N N   . ALA A 1 186 ? 18.925  4.100   -25.045 1.00 51.14  ? 794  ALA A N   1 
ATOM   1275 C CA  . ALA A 1 186 ? 18.938  2.657   -25.211 1.00 49.44  ? 794  ALA A CA  1 
ATOM   1276 C C   . ALA A 1 186 ? 17.553  2.161   -24.877 1.00 48.97  ? 794  ALA A C   1 
ATOM   1277 O O   . ALA A 1 186 ? 16.830  2.849   -24.177 1.00 49.29  ? 794  ALA A O   1 
ATOM   1278 C CB  . ALA A 1 186 ? 19.937  2.052   -24.239 1.00 49.28  ? 794  ALA A CB  1 
ATOM   1279 N N   . ALA A 1 187 ? 17.185  0.933   -25.293 1.00 48.92  ? 795  ALA A N   1 
ATOM   1280 C CA  . ALA A 1 187 ? 15.866  0.374   -24.971 1.00 48.25  ? 795  ALA A CA  1 
ATOM   1281 C C   . ALA A 1 187 ? 15.593  0.247   -23.468 1.00 47.45  ? 795  ALA A C   1 
ATOM   1282 O O   . ALA A 1 187 ? 14.449  0.362   -23.052 1.00 46.79  ? 795  ALA A O   1 
ATOM   1283 C CB  . ALA A 1 187 ? 15.653  -0.952  -25.677 1.00 47.83  ? 795  ALA A CB  1 
ATOM   1284 N N   . ARG A 1 188 ? 16.635  0.029   -22.650 1.00 47.60  ? 796  ARG A N   1 
ATOM   1285 C CA  . ARG A 1 188 ? 16.453  -0.103  -21.193 1.00 47.94  ? 796  ARG A CA  1 
ATOM   1286 C C   . ARG A 1 188 ? 16.033  1.233   -20.534 1.00 49.05  ? 796  ARG A C   1 
ATOM   1287 O O   . ARG A 1 188 ? 15.591  1.211   -19.385 1.00 50.74  ? 796  ARG A O   1 
ATOM   1288 C CB  . ARG A 1 188 ? 17.734  -0.630  -20.536 1.00 47.79  ? 796  ARG A CB  1 
ATOM   1289 C CG  . ARG A 1 188 ? 18.907  0.326   -20.754 1.00 47.86  ? 796  ARG A CG  1 
ATOM   1290 C CD  . ARG A 1 188 ? 20.245  -0.133  -20.191 1.00 48.39  ? 796  ARG A CD  1 
ATOM   1291 N NE  . ARG A 1 188 ? 21.287  0.799   -20.618 1.00 51.38  ? 796  ARG A NE  1 
ATOM   1292 C CZ  . ARG A 1 188 ? 21.994  0.678   -21.737 1.00 53.65  ? 796  ARG A CZ  1 
ATOM   1293 N NH1 . ARG A 1 188 ? 21.825  -0.371  -22.526 1.00 53.87  ? 796  ARG A NH1 1 
ATOM   1294 N NH2 . ARG A 1 188 ? 22.856  1.623   -22.089 1.00 52.10  ? 796  ARG A NH2 1 
ATOM   1295 N N   . ASN A 1 189 ? 16.162  2.383   -21.248 1.00 47.55  ? 797  ASN A N   1 
ATOM   1296 C CA  . ASN A 1 189 ? 15.748  3.702   -20.743 1.00 47.15  ? 797  ASN A CA  1 
ATOM   1297 C C   . ASN A 1 189 ? 14.521  4.247   -21.474 1.00 49.35  ? 797  ASN A C   1 
ATOM   1298 O O   . ASN A 1 189 ? 14.331  5.453   -21.536 1.00 50.51  ? 797  ASN A O   1 
ATOM   1299 C CB  . ASN A 1 189 ? 16.884  4.736   -20.808 1.00 45.12  ? 797  ASN A CB  1 
ATOM   1300 C CG  . ASN A 1 189 ? 17.934  4.512   -19.778 1.00 45.35  ? 797  ASN A CG  1 
ATOM   1301 O OD1 . ASN A 1 189 ? 17.646  4.134   -18.639 1.00 47.30  ? 797  ASN A OD1 1 
ATOM   1302 N ND2 . ASN A 1 189 ? 19.175  4.654   -20.169 1.00 44.21  ? 797  ASN A ND2 1 
ATOM   1303 N N   . ILE A 1 190 ? 13.710  3.379   -22.050 1.00 50.22  ? 798  ILE A N   1 
ATOM   1304 C CA  . ILE A 1 190 ? 12.504  3.786   -22.756 1.00 51.11  ? 798  ILE A CA  1 
ATOM   1305 C C   . ILE A 1 190 ? 11.370  3.029   -22.094 1.00 52.84  ? 798  ILE A C   1 
ATOM   1306 O O   . ILE A 1 190 ? 11.493  1.822   -21.909 1.00 52.43  ? 798  ILE A O   1 
ATOM   1307 C CB  . ILE A 1 190 ? 12.612  3.496   -24.281 1.00 50.31  ? 798  ILE A CB  1 
ATOM   1308 C CG1 . ILE A 1 190 ? 13.690  4.411   -24.894 1.00 50.52  ? 798  ILE A CG1 1 
ATOM   1309 C CG2 . ILE A 1 190 ? 11.251  3.752   -24.952 1.00 50.53  ? 798  ILE A CG2 1 
ATOM   1310 C CD1 . ILE A 1 190 ? 14.232  3.999   -26.126 1.00 51.16  ? 798  ILE A CD1 1 
ATOM   1311 N N   . LEU A 1 191 ? 10.332  3.744   -21.630 1.00 53.52  ? 799  LEU A N   1 
ATOM   1312 C CA  . LEU A 1 191 ? 9.214   3.072   -20.988 1.00 55.09  ? 799  LEU A CA  1 
ATOM   1313 C C   . LEU A 1 191 ? 8.006   2.952   -21.955 1.00 56.76  ? 799  LEU A C   1 
ATOM   1314 O O   . LEU A 1 191 ? 7.886   3.711   -22.910 1.00 56.67  ? 799  LEU A O   1 
ATOM   1315 C CB  . LEU A 1 191 ? 8.820   3.772   -19.676 1.00 55.11  ? 799  LEU A CB  1 
ATOM   1316 C CG  . LEU A 1 191 ? 9.930   3.958   -18.627 1.00 55.45  ? 799  LEU A CG  1 
ATOM   1317 C CD1 . LEU A 1 191 ? 9.407   4.657   -17.425 1.00 55.19  ? 799  LEU A CD1 1 
ATOM   1318 C CD2 . LEU A 1 191 ? 10.463  2.657   -18.174 1.00 55.61  ? 799  LEU A CD2 1 
ATOM   1319 N N   . LEU A 1 192 ? 7.135   1.982   -21.713 1.00 57.86  ? 800  LEU A N   1 
ATOM   1320 C CA  . LEU A 1 192 ? 5.948   1.793   -22.530 1.00 59.73  ? 800  LEU A CA  1 
ATOM   1321 C C   . LEU A 1 192 ? 4.741   1.926   -21.640 1.00 60.73  ? 800  LEU A C   1 
ATOM   1322 O O   . LEU A 1 192 ? 4.728   1.358   -20.555 1.00 59.65  ? 800  LEU A O   1 
ATOM   1323 C CB  . LEU A 1 192 ? 5.960   0.391   -23.170 1.00 60.52  ? 800  LEU A CB  1 
ATOM   1324 C CG  . LEU A 1 192 ? 5.017   0.222   -24.335 1.00 62.15  ? 800  LEU A CG  1 
ATOM   1325 C CD1 . LEU A 1 192 ? 5.650   0.750   -25.571 1.00 62.09  ? 800  LEU A CD1 1 
ATOM   1326 C CD2 . LEU A 1 192 ? 4.609   -1.242  -24.505 1.00 63.23  ? 800  LEU A CD2 1 
ATOM   1327 N N   . THR A 1 193 ? 3.728   2.643   -22.092 1.00 63.46  ? 801  THR A N   1 
ATOM   1328 C CA  . THR A 1 193 ? 2.515   2.806   -21.286 1.00 67.46  ? 801  THR A CA  1 
ATOM   1329 C C   . THR A 1 193 ? 1.232   2.453   -22.107 1.00 71.20  ? 801  THR A C   1 
ATOM   1330 O O   . THR A 1 193 ? 1.330   1.964   -23.244 1.00 70.95  ? 801  THR A O   1 
ATOM   1331 C CB  . THR A 1 193 ? 2.522   4.203   -20.630 1.00 68.76  ? 801  THR A CB  1 
ATOM   1332 O OG1 . THR A 1 193 ? 1.380   4.309   -19.768 1.00 69.83  ? 801  THR A OG1 1 
ATOM   1333 C CG2 . THR A 1 193 ? 2.560   5.324   -21.653 1.00 68.94  ? 801  THR A CG2 1 
ATOM   1334 N N   . HIS A 1 194 ? 0.033   2.642   -21.505 1.00 74.37  ? 802  HIS A N   1 
ATOM   1335 C CA  . HIS A 1 194 ? -1.265  2.363   -22.122 1.00 77.62  ? 802  HIS A CA  1 
ATOM   1336 C C   . HIS A 1 194 ? -1.373  3.006   -23.503 1.00 78.22  ? 802  HIS A C   1 
ATOM   1337 O O   . HIS A 1 194 ? -0.993  4.164   -23.687 1.00 79.16  ? 802  HIS A O   1 
ATOM   1338 C CB  . HIS A 1 194 ? -2.397  2.835   -21.206 1.00 81.20  ? 802  HIS A CB  1 
ATOM   1339 C CG  . HIS A 1 194 ? -2.532  2.010   -19.966 1.00 87.87  ? 802  HIS A CG  1 
ATOM   1340 N ND1 . HIS A 1 194 ? -3.055  0.719   -20.009 1.00 91.13  ? 802  HIS A ND1 1 
ATOM   1341 C CD2 . HIS A 1 194 ? -2.219  2.317   -18.684 1.00 89.98  ? 802  HIS A CD2 1 
ATOM   1342 C CE1 . HIS A 1 194 ? -3.049  0.289   -18.755 1.00 92.15  ? 802  HIS A CE1 1 
ATOM   1343 N NE2 . HIS A 1 194 ? -2.555  1.215   -17.920 1.00 91.95  ? 802  HIS A NE2 1 
ATOM   1344 N N   . GLY A 1 195 ? -1.790  2.217   -24.465 1.00 77.51  ? 803  GLY A N   1 
ATOM   1345 C CA  . GLY A 1 195 ? -1.858  2.672   -25.845 1.00 77.85  ? 803  GLY A CA  1 
ATOM   1346 C C   . GLY A 1 195 ? -0.593  2.373   -26.630 1.00 77.97  ? 803  GLY A C   1 
ATOM   1347 O O   . GLY A 1 195 ? -0.503  2.727   -27.812 1.00 78.55  ? 803  GLY A O   1 
ATOM   1348 N N   . ARG A 1 196 ? 0.382   1.685   -25.994 1.00 76.99  ? 804  ARG A N   1 
ATOM   1349 C CA  . ARG A 1 196 ? 1.679   1.383   -26.573 1.00 76.28  ? 804  ARG A CA  1 
ATOM   1350 C C   . ARG A 1 196 ? 2.396   2.686   -26.963 1.00 73.45  ? 804  ARG A C   1 
ATOM   1351 O O   . ARG A 1 196 ? 2.847   2.876   -28.088 1.00 73.75  ? 804  ARG A O   1 
ATOM   1352 C CB  . ARG A 1 196 ? 1.594   0.335   -27.685 1.00 79.49  ? 804  ARG A CB  1 
ATOM   1353 C CG  . ARG A 1 196 ? 1.407   -1.061  -27.066 1.00 86.28  ? 804  ARG A CG  1 
ATOM   1354 C CD  . ARG A 1 196 ? 1.510   -2.253  -28.018 1.00 91.35  ? 804  ARG A CD  1 
ATOM   1355 N NE  . ARG A 1 196 ? 1.277   -3.509  -27.298 1.00 95.78  ? 804  ARG A NE  1 
ATOM   1356 C CZ  . ARG A 1 196 ? 1.372   -4.719  -27.841 1.00 99.69  ? 804  ARG A CZ  1 
ATOM   1357 N NH1 . ARG A 1 196 ? 1.699   -4.856  -29.119 1.00 100.29 ? 804  ARG A NH1 1 
ATOM   1358 N NH2 . ARG A 1 196 ? 1.152   -5.802  -27.108 1.00 99.82  ? 804  ARG A NH2 1 
ATOM   1359 N N   . ILE A 1 197 ? 2.458   3.593   -26.001 1.00 70.46  ? 805  ILE A N   1 
ATOM   1360 C CA  . ILE A 1 197 ? 3.111   4.876   -26.151 1.00 68.10  ? 805  ILE A CA  1 
ATOM   1361 C C   . ILE A 1 197 ? 4.475   4.759   -25.510 1.00 64.90  ? 805  ILE A C   1 
ATOM   1362 O O   . ILE A 1 197 ? 4.563   4.388   -24.345 1.00 64.66  ? 805  ILE A O   1 
ATOM   1363 C CB  . ILE A 1 197 ? 2.250   5.963   -25.464 1.00 68.92  ? 805  ILE A CB  1 
ATOM   1364 C CG1 . ILE A 1 197 ? 0.815   5.981   -26.052 1.00 69.69  ? 805  ILE A CG1 1 
ATOM   1365 C CG2 . ILE A 1 197 ? 2.926   7.350   -25.518 1.00 69.33  ? 805  ILE A CG2 1 
ATOM   1366 C CD1 . ILE A 1 197 ? 0.763   6.179   -27.567 1.00 70.81  ? 805  ILE A CD1 1 
ATOM   1367 N N   . THR A 1 198 ? 5.539   4.981   -26.282 1.00 62.61  ? 806  THR A N   1 
ATOM   1368 C CA  . THR A 1 198 ? 6.890   4.909   -25.748 1.00 60.93  ? 806  THR A CA  1 
ATOM   1369 C C   . THR A 1 198 ? 7.309   6.265   -25.266 1.00 58.21  ? 806  THR A C   1 
ATOM   1370 O O   . THR A 1 198 ? 7.163   7.258   -25.978 1.00 57.97  ? 806  THR A O   1 
ATOM   1371 C CB  . THR A 1 198 ? 7.917   4.369   -26.756 1.00 62.83  ? 806  THR A CB  1 
ATOM   1372 O OG1 . THR A 1 198 ? 7.971   5.208   -27.905 1.00 64.97  ? 806  THR A OG1 1 
ATOM   1373 C CG2 . THR A 1 198 ? 7.669   2.955   -27.141 1.00 62.26  ? 806  THR A CG2 1 
ATOM   1374 N N   . LYS A 1 199 ? 7.803   6.308   -24.033 1.00 56.20  ? 807  LYS A N   1 
ATOM   1375 C CA  . LYS A 1 199 ? 8.275   7.526   -23.392 1.00 54.63  ? 807  LYS A CA  1 
ATOM   1376 C C   . LYS A 1 199 ? 9.735   7.364   -23.009 1.00 52.84  ? 807  LYS A C   1 
ATOM   1377 O O   . LYS A 1 199 ? 10.114  6.339   -22.476 1.00 53.34  ? 807  LYS A O   1 
ATOM   1378 C CB  . LYS A 1 199 ? 7.424   7.837   -22.158 1.00 55.15  ? 807  LYS A CB  1 
ATOM   1379 C CG  . LYS A 1 199 ? 5.952   8.001   -22.496 1.00 56.39  ? 807  LYS A CG  1 
ATOM   1380 C CD  . LYS A 1 199 ? 5.141   8.346   -21.271 1.00 58.08  ? 807  LYS A CD  1 
ATOM   1381 C CE  . LYS A 1 199 ? 3.878   9.060   -21.673 1.00 60.47  ? 807  LYS A CE  1 
ATOM   1382 N NZ  . LYS A 1 199 ? 4.091   10.518  -21.878 1.00 60.99  ? 807  LYS A NZ  1 
ATOM   1383 N N   . ILE A 1 200 ? 10.554  8.367   -23.291 1.00 51.02  ? 808  ILE A N   1 
ATOM   1384 C CA  . ILE A 1 200 ? 11.963  8.342   -22.960 1.00 49.68  ? 808  ILE A CA  1 
ATOM   1385 C C   . ILE A 1 200 ? 12.175  8.711   -21.503 1.00 48.14  ? 808  ILE A C   1 
ATOM   1386 O O   . ILE A 1 200 ? 11.553  9.647   -20.976 1.00 46.80  ? 808  ILE A O   1 
ATOM   1387 C CB  . ILE A 1 200 ? 12.762  9.295   -23.907 1.00 50.29  ? 808  ILE A CB  1 
ATOM   1388 C CG1 . ILE A 1 200 ? 12.742  8.794   -25.350 1.00 50.65  ? 808  ILE A CG1 1 
ATOM   1389 C CG2 . ILE A 1 200 ? 14.224  9.571   -23.425 1.00 50.58  ? 808  ILE A CG2 1 
ATOM   1390 C CD1 . ILE A 1 200 ? 12.877  9.849   -26.211 1.00 52.12  ? 808  ILE A CD1 1 
ATOM   1391 N N   A CYS A 1 201 ? 13.052  7.946   -20.852 0.50 47.44  ? 809  CYS A N   1 
ATOM   1392 N N   B CYS A 1 201 ? 13.078  7.987   -20.837 0.50 47.99  ? 809  CYS A N   1 
ATOM   1393 C CA  A CYS A 1 201 ? 13.393  8.114   -19.452 0.50 47.01  ? 809  CYS A CA  1 
ATOM   1394 C CA  B CYS A 1 201 ? 13.466  8.336   -19.479 0.50 48.04  ? 809  CYS A CA  1 
ATOM   1395 C C   A CYS A 1 201 ? 14.943  7.949   -19.252 0.50 47.45  ? 809  CYS A C   1 
ATOM   1396 C C   B CYS A 1 201 ? 14.976  8.021   -19.239 0.50 47.90  ? 809  CYS A C   1 
ATOM   1397 O O   A CYS A 1 201 ? 15.687  7.926   -20.233 0.50 46.83  ? 809  CYS A O   1 
ATOM   1398 O O   B CYS A 1 201 ? 15.732  7.965   -20.208 0.50 47.27  ? 809  CYS A O   1 
ATOM   1399 C CB  A CYS A 1 201 ? 12.599  7.090   -18.644 0.50 45.86  ? 809  CYS A CB  1 
ATOM   1400 C CB  B CYS A 1 201 ? 12.523  7.730   -18.434 0.50 48.25  ? 809  CYS A CB  1 
ATOM   1401 S SG  A CYS A 1 201 ? 12.528  7.438   -16.874 0.50 46.29  ? 809  CYS A SG  1 
ATOM   1402 S SG  B CYS A 1 201 ? 12.902  6.032   -17.951 0.50 51.28  ? 809  CYS A SG  1 
ATOM   1403 N N   . ASP A 1 202 ? 15.414  7.866   -17.985 1.00 48.15  ? 810  ASP A N   1 
ATOM   1404 C CA  . ASP A 1 202 ? 16.783  7.571   -17.620 1.00 49.00  ? 810  ASP A CA  1 
ATOM   1405 C C   . ASP A 1 202 ? 16.703  7.097   -16.196 1.00 49.48  ? 810  ASP A C   1 
ATOM   1406 O O   . ASP A 1 202 ? 16.445  7.906   -15.315 1.00 49.84  ? 810  ASP A O   1 
ATOM   1407 C CB  . ASP A 1 202 ? 17.719  8.800   -17.697 1.00 50.54  ? 810  ASP A CB  1 
ATOM   1408 C CG  . ASP A 1 202 ? 19.207  8.440   -17.610 1.00 57.02  ? 810  ASP A CG  1 
ATOM   1409 O OD1 . ASP A 1 202 ? 19.533  7.234   -17.362 1.00 59.11  ? 810  ASP A OD1 1 
ATOM   1410 O OD2 . ASP A 1 202 ? 20.050  9.350   -17.769 1.00 58.96  ? 810  ASP A OD2 1 
ATOM   1411 N N   . PHE A 1 203 ? 16.942  5.813   -15.951 1.00 49.50  ? 811  PHE A N   1 
ATOM   1412 C CA  . PHE A 1 203 ? 16.945  5.299   -14.585 1.00 49.75  ? 811  PHE A CA  1 
ATOM   1413 C C   . PHE A 1 203 ? 18.046  5.904   -13.760 1.00 50.94  ? 811  PHE A C   1 
ATOM   1414 O O   . PHE A 1 203 ? 17.842  6.078   -12.577 1.00 51.46  ? 811  PHE A O   1 
ATOM   1415 C CB  . PHE A 1 203 ? 17.020  3.776   -14.545 1.00 49.66  ? 811  PHE A CB  1 
ATOM   1416 C CG  . PHE A 1 203 ? 15.670  3.152   -14.766 1.00 50.38  ? 811  PHE A CG  1 
ATOM   1417 C CD1 . PHE A 1 203 ? 15.172  2.977   -16.043 1.00 51.23  ? 811  PHE A CD1 1 
ATOM   1418 C CD2 . PHE A 1 203 ? 14.882  2.779   -13.698 1.00 51.71  ? 811  PHE A CD2 1 
ATOM   1419 C CE1 . PHE A 1 203 ? 13.928  2.398   -16.248 1.00 52.30  ? 811  PHE A CE1 1 
ATOM   1420 C CE2 . PHE A 1 203 ? 13.627  2.206   -13.903 1.00 52.80  ? 811  PHE A CE2 1 
ATOM   1421 C CZ  . PHE A 1 203 ? 13.158  2.019   -15.176 1.00 52.26  ? 811  PHE A CZ  1 
ATOM   1422 N N   . GLY A 1 204 ? 19.196  6.247   -14.350 1.00 51.60  ? 812  GLY A N   1 
ATOM   1423 C CA  . GLY A 1 204 ? 20.293  6.844   -13.593 1.00 53.40  ? 812  GLY A CA  1 
ATOM   1424 C C   . GLY A 1 204 ? 20.693  6.056   -12.353 1.00 56.36  ? 812  GLY A C   1 
ATOM   1425 O O   . GLY A 1 204 ? 20.911  4.852   -12.454 1.00 56.73  ? 812  GLY A O   1 
ATOM   1426 N N   . LEU A 1 205 ? 20.721  6.695   -11.155 1.00 57.83  ? 813  LEU A N   1 
ATOM   1427 C CA  . LEU A 1 205 ? 21.044  5.965   -9.934  1.00 59.54  ? 813  LEU A CA  1 
ATOM   1428 C C   . LEU A 1 205 ? 19.997  4.894   -9.545  1.00 61.96  ? 813  LEU A C   1 
ATOM   1429 O O   . LEU A 1 205 ? 20.235  4.107   -8.629  1.00 62.77  ? 813  LEU A O   1 
ATOM   1430 C CB  . LEU A 1 205 ? 21.270  6.930   -8.777  1.00 60.07  ? 813  LEU A CB  1 
ATOM   1431 C CG  . LEU A 1 205 ? 22.550  7.784   -8.844  1.00 61.90  ? 813  LEU A CG  1 
ATOM   1432 C CD1 . LEU A 1 205 ? 22.698  8.626   -7.586  1.00 62.52  ? 813  LEU A CD1 1 
ATOM   1433 C CD2 . LEU A 1 205 ? 23.807  6.917   -9.021  1.00 61.93  ? 813  LEU A CD2 1 
ATOM   1434 N N   . ALA A 1 206 ? 18.842  4.860   -10.226 1.00 63.21  ? 814  ALA A N   1 
ATOM   1435 C CA  . ALA A 1 206 ? 17.816  3.861   -9.951  1.00 64.81  ? 814  ALA A CA  1 
ATOM   1436 C C   . ALA A 1 206 ? 18.058  2.563   -10.696 1.00 67.41  ? 814  ALA A C   1 
ATOM   1437 O O   . ALA A 1 206 ? 17.129  1.800   -10.871 1.00 67.98  ? 814  ALA A O   1 
ATOM   1438 C CB  . ALA A 1 206 ? 16.425  4.396   -10.248 1.00 64.38  ? 814  ALA A CB  1 
ATOM   1439 N N   . ARG A 1 207 ? 19.295  2.280   -11.092 1.00 69.18  ? 815  ARG A N   1 
ATOM   1440 C CA  . ARG A 1 207 ? 19.648  1.005   -11.684 1.00 71.74  ? 815  ARG A CA  1 
ATOM   1441 C C   . ARG A 1 207 ? 20.978  0.566   -11.126 1.00 75.59  ? 815  ARG A C   1 
ATOM   1442 O O   . ARG A 1 207 ? 21.872  1.384   -10.897 1.00 76.18  ? 815  ARG A O   1 
ATOM   1443 C CB  . ARG A 1 207 ? 19.570  0.983   -13.215 1.00 71.75  ? 815  ARG A CB  1 
ATOM   1444 C CG  . ARG A 1 207 ? 20.882  1.070   -13.983 1.00 71.90  ? 815  ARG A CG  1 
ATOM   1445 C CD  . ARG A 1 207 ? 20.887  0.327   -15.317 1.00 71.44  ? 815  ARG A CD  1 
ATOM   1446 N NE  . ARG A 1 207 ? 19.637  0.459   -16.067 1.00 71.85  ? 815  ARG A NE  1 
ATOM   1447 C CZ  . ARG A 1 207 ? 19.292  1.520   -16.786 1.00 72.28  ? 815  ARG A CZ  1 
ATOM   1448 N NH1 . ARG A 1 207 ? 20.096  2.574   -16.856 1.00 73.05  ? 815  ARG A NH1 1 
ATOM   1449 N NH2 . ARG A 1 207 ? 18.131  1.549   -17.417 1.00 71.43  ? 815  ARG A NH2 1 
ATOM   1450 N N   . ASP A 1 208 ? 21.079  -0.710  -10.841 1.00 77.99  ? 816  ASP A N   1 
ATOM   1451 C CA  . ASP A 1 208 ? 22.274  -1.318  -10.274 1.00 80.82  ? 816  ASP A CA  1 
ATOM   1452 C C   . ASP A 1 208 ? 23.311  -1.535  -11.403 1.00 82.13  ? 816  ASP A C   1 
ATOM   1453 O O   . ASP A 1 208 ? 23.474  -2.669  -11.855 1.00 82.32  ? 816  ASP A O   1 
ATOM   1454 C CB  . ASP A 1 208 ? 21.848  -2.664  -9.640  1.00 83.89  ? 816  ASP A CB  1 
ATOM   1455 C CG  . ASP A 1 208 ? 22.914  -3.389  -8.859  1.00 91.51  ? 816  ASP A CG  1 
ATOM   1456 O OD1 . ASP A 1 208 ? 24.025  -2.824  -8.700  1.00 93.14  ? 816  ASP A OD1 1 
ATOM   1457 O OD2 . ASP A 1 208 ? 22.643  -4.530  -8.404  1.00 94.23  ? 816  ASP A OD2 1 
ATOM   1458 N N   . ILE A 1 209 ? 23.995  -0.463  -11.870 1.00 82.76  ? 817  ILE A N   1 
ATOM   1459 C CA  . ILE A 1 209 ? 24.972  -0.600  -12.962 1.00 84.30  ? 817  ILE A CA  1 
ATOM   1460 C C   . ILE A 1 209 ? 26.153  -1.519  -12.569 1.00 86.41  ? 817  ILE A C   1 
ATOM   1461 O O   . ILE A 1 209 ? 26.740  -2.185  -13.435 1.00 86.66  ? 817  ILE A O   1 
ATOM   1462 C CB  . ILE A 1 209 ? 25.449  0.750   -13.558 1.00 84.41  ? 817  ILE A CB  1 
ATOM   1463 C CG1 . ILE A 1 209 ? 26.063  1.652   -12.491 1.00 85.50  ? 817  ILE A CG1 1 
ATOM   1464 C CG2 . ILE A 1 209 ? 24.349  1.454   -14.336 1.00 84.25  ? 817  ILE A CG2 1 
ATOM   1465 C CD1 . ILE A 1 209 ? 26.837  2.813   -13.085 1.00 86.90  ? 817  ILE A CD1 1 
ATOM   1466 N N   . LYS A 1 210 ? 26.446  -1.609  -11.254 1.00 87.31  ? 818  LYS A N   1 
ATOM   1467 C CA  . LYS A 1 210 ? 27.446  -2.524  -10.704 1.00 88.37  ? 818  LYS A CA  1 
ATOM   1468 C C   . LYS A 1 210 ? 27.125  -3.993  -11.127 1.00 88.85  ? 818  LYS A C   1 
ATOM   1469 O O   . LYS A 1 210 ? 28.019  -4.843  -11.111 1.00 89.27  ? 818  LYS A O   1 
ATOM   1470 C CB  . LYS A 1 210 ? 27.417  -2.413  -9.168  1.00 90.76  ? 818  LYS A CB  1 
ATOM   1471 C CG  . LYS A 1 210 ? 28.730  -2.660  -8.453  1.00 95.29  ? 818  LYS A CG  1 
ATOM   1472 C CD  . LYS A 1 210 ? 28.692  -1.963  -7.090  1.00 100.90 ? 818  LYS A CD  1 
ATOM   1473 C CE  . LYS A 1 210 ? 30.039  -1.917  -6.385  1.00 105.59 ? 818  LYS A CE  1 
ATOM   1474 N NZ  . LYS A 1 210 ? 30.029  -0.978  -5.225  1.00 107.72 ? 818  LYS A NZ  1 
ATOM   1475 N N   . ASN A 1 211 ? 25.862  -4.283  -11.519 1.00 88.23  ? 819  ASN A N   1 
ATOM   1476 C CA  . ASN A 1 211 ? 25.446  -5.616  -11.920 1.00 88.17  ? 819  ASN A CA  1 
ATOM   1477 C C   . ASN A 1 211 ? 24.716  -5.644  -13.261 1.00 86.56  ? 819  ASN A C   1 
ATOM   1478 O O   . ASN A 1 211 ? 23.786  -6.427  -13.433 1.00 86.57  ? 819  ASN A O   1 
ATOM   1479 C CB  . ASN A 1 211 ? 24.622  -6.263  -10.820 1.00 90.83  ? 819  ASN A CB  1 
ATOM   1480 C CG  . ASN A 1 211 ? 25.455  -6.591  -9.606  1.00 97.12  ? 819  ASN A CG  1 
ATOM   1481 O OD1 . ASN A 1 211 ? 26.488  -7.283  -9.689  1.00 99.80  ? 819  ASN A OD1 1 
ATOM   1482 N ND2 . ASN A 1 211 ? 25.039  -6.096  -8.447  1.00 98.31  ? 819  ASN A ND2 1 
ATOM   1483 N N   . ASP A 1 212 ? 25.163  -4.814  -14.220 1.00 84.99  ? 820  ASP A N   1 
ATOM   1484 C CA  . ASP A 1 212 ? 24.602  -4.739  -15.575 1.00 83.89  ? 820  ASP A CA  1 
ATOM   1485 C C   . ASP A 1 212 ? 25.792  -4.760  -16.537 1.00 83.03  ? 820  ASP A C   1 
ATOM   1486 O O   . ASP A 1 212 ? 26.543  -3.785  -16.605 1.00 83.38  ? 820  ASP A O   1 
ATOM   1487 C CB  . ASP A 1 212 ? 23.766  -3.442  -15.750 1.00 84.60  ? 820  ASP A CB  1 
ATOM   1488 C CG  . ASP A 1 212 ? 22.885  -3.387  -16.994 1.00 87.24  ? 820  ASP A CG  1 
ATOM   1489 O OD1 . ASP A 1 212 ? 23.384  -3.702  -18.090 1.00 87.69  ? 820  ASP A OD1 1 
ATOM   1490 O OD2 . ASP A 1 212 ? 21.700  -3.008  -16.870 1.00 88.17  ? 820  ASP A OD2 1 
ATOM   1491 N N   . SER A 1 213 ? 25.967  -5.859  -17.280 1.00 81.94  ? 821  SER A N   1 
ATOM   1492 C CA  . SER A 1 213 ? 27.101  -6.023  -18.203 1.00 81.55  ? 821  SER A CA  1 
ATOM   1493 C C   . SER A 1 213 ? 27.054  -5.129  -19.462 1.00 80.66  ? 821  SER A C   1 
ATOM   1494 O O   . SER A 1 213 ? 27.959  -5.182  -20.296 1.00 80.60  ? 821  SER A O   1 
ATOM   1495 C CB  . SER A 1 213 ? 27.292  -7.487  -18.590 1.00 83.10  ? 821  SER A CB  1 
ATOM   1496 O OG  . SER A 1 213 ? 26.221  -7.974  -19.379 1.00 85.97  ? 821  SER A OG  1 
ATOM   1497 N N   . ASN A 1 214 ? 26.013  -4.307  -19.597 1.00 79.83  ? 822  ASN A N   1 
ATOM   1498 C CA  . ASN A 1 214 ? 25.944  -3.339  -20.688 1.00 78.91  ? 822  ASN A CA  1 
ATOM   1499 C C   . ASN A 1 214 ? 26.786  -2.080  -20.340 1.00 78.50  ? 822  ASN A C   1 
ATOM   1500 O O   . ASN A 1 214 ? 27.199  -1.361  -21.247 1.00 78.16  ? 822  ASN A O   1 
ATOM   1501 C CB  . ASN A 1 214 ? 24.496  -3.038  -21.084 1.00 79.04  ? 822  ASN A CB  1 
ATOM   1502 C CG  . ASN A 1 214 ? 23.775  -4.266  -21.612 1.00 81.29  ? 822  ASN A CG  1 
ATOM   1503 O OD1 . ASN A 1 214 ? 24.172  -4.871  -22.609 1.00 82.07  ? 822  ASN A OD1 1 
ATOM   1504 N ND2 . ASN A 1 214 ? 22.702  -4.680  -20.950 1.00 81.72  ? 822  ASN A ND2 1 
ATOM   1505 N N   . TYR A 1 215 ? 27.109  -1.865  -19.040 1.00 78.47  ? 823  TYR A N   1 
ATOM   1506 C CA  . TYR A 1 215 ? 27.957  -0.774  -18.572 1.00 79.50  ? 823  TYR A CA  1 
ATOM   1507 C C   . TYR A 1 215 ? 29.301  -1.382  -18.224 1.00 83.89  ? 823  TYR A C   1 
ATOM   1508 O O   . TYR A 1 215 ? 29.401  -2.202  -17.295 1.00 84.49  ? 823  TYR A O   1 
ATOM   1509 C CB  . TYR A 1 215 ? 27.350  -0.091  -17.344 1.00 77.10  ? 823  TYR A CB  1 
ATOM   1510 C CG  . TYR A 1 215 ? 26.066  0.605   -17.686 1.00 74.98  ? 823  TYR A CG  1 
ATOM   1511 C CD1 . TYR A 1 215 ? 24.854  -0.070  -17.637 1.00 74.36  ? 823  TYR A CD1 1 
ATOM   1512 C CD2 . TYR A 1 215 ? 26.067  1.910   -18.158 1.00 74.50  ? 823  TYR A CD2 1 
ATOM   1513 C CE1 . TYR A 1 215 ? 23.671  0.549   -18.009 1.00 74.53  ? 823  TYR A CE1 1 
ATOM   1514 C CE2 . TYR A 1 215 ? 24.888  2.544   -18.522 1.00 74.46  ? 823  TYR A CE2 1 
ATOM   1515 C CZ  . TYR A 1 215 ? 23.688  1.865   -18.432 1.00 74.88  ? 823  TYR A CZ  1 
ATOM   1516 O OH  . TYR A 1 215 ? 22.519  2.478   -18.806 1.00 75.47  ? 823  TYR A OH  1 
ATOM   1517 N N   . VAL A 1 216 ? 30.319  -1.054  -19.006 1.00 86.25  ? 824  VAL A N   1 
ATOM   1518 C CA  . VAL A 1 216 ? 31.642  -1.609  -18.781 1.00 88.80  ? 824  VAL A CA  1 
ATOM   1519 C C   . VAL A 1 216 ? 32.521  -0.607  -18.059 1.00 91.57  ? 824  VAL A C   1 
ATOM   1520 O O   . VAL A 1 216 ? 32.376  0.598   -18.238 1.00 91.59  ? 824  VAL A O   1 
ATOM   1521 C CB  . VAL A 1 216 ? 32.304  -2.013  -20.108 1.00 89.32  ? 824  VAL A CB  1 
ATOM   1522 C CG1 . VAL A 1 216 ? 33.410  -3.026  -19.861 1.00 89.70  ? 824  VAL A CG1 1 
ATOM   1523 C CG2 . VAL A 1 216 ? 31.264  -2.593  -21.049 1.00 89.77  ? 824  VAL A CG2 1 
ATOM   1524 N N   . VAL A 1 217 ? 33.436  -1.109  -17.239 1.00 93.86  ? 825  VAL A N   1 
ATOM   1525 C CA  . VAL A 1 217 ? 34.322  -0.231  -16.501 1.00 96.49  ? 825  VAL A CA  1 
ATOM   1526 C C   . VAL A 1 217 ? 35.416  0.312   -17.407 1.00 98.48  ? 825  VAL A C   1 
ATOM   1527 O O   . VAL A 1 217 ? 36.126  -0.442  -18.067 1.00 98.75  ? 825  VAL A O   1 
ATOM   1528 C CB  . VAL A 1 217 ? 34.984  -0.969  -15.322 1.00 97.66  ? 825  VAL A CB  1 
ATOM   1529 C CG1 . VAL A 1 217 ? 35.887  -0.025  -14.546 1.00 98.08  ? 825  VAL A CG1 1 
ATOM   1530 C CG2 . VAL A 1 217 ? 33.928  -1.574  -14.411 1.00 98.36  ? 825  VAL A CG2 1 
ATOM   1531 N N   . LYS A 1 218 ? 35.548  1.632   -17.421 1.00 99.56  ? 826  LYS A N   1 
ATOM   1532 C CA  . LYS A 1 218 ? 36.574  2.308   -18.208 1.00 101.57 ? 826  LYS A CA  1 
ATOM   1533 C C   . LYS A 1 218 ? 37.825  2.563   -17.354 1.00 103.84 ? 826  LYS A C   1 
ATOM   1534 O O   . LYS A 1 218 ? 38.815  3.119   -17.829 1.00 104.49 ? 826  LYS A O   1 
ATOM   1535 C CB  . LYS A 1 218 ? 36.033  3.633   -18.743 1.00 103.24 ? 826  LYS A CB  1 
ATOM   1536 C CG  . LYS A 1 218 ? 36.630  4.073   -20.070 1.00 106.67 ? 826  LYS A CG  1 
ATOM   1537 C CD  . LYS A 1 218 ? 35.996  3.322   -21.230 1.00 110.09 ? 826  LYS A CD  1 
ATOM   1538 C CE  . LYS A 1 218 ? 36.385  3.925   -22.569 1.00 113.14 ? 826  LYS A CE  1 
ATOM   1539 N NZ  . LYS A 1 218 ? 37.825  3.715   -22.883 1.00 115.00 ? 826  LYS A NZ  1 
ATOM   1540 N N   . GLY A 1 219 ? 37.759  2.133   -16.095 1.00 104.55 ? 827  GLY A N   1 
ATOM   1541 C CA  . GLY A 1 219 ? 38.797  2.302   -15.098 1.00 105.28 ? 827  GLY A CA  1 
ATOM   1542 C C   . GLY A 1 219 ? 38.456  3.469   -14.190 1.00 105.87 ? 827  GLY A C   1 
ATOM   1543 O O   . GLY A 1 219 ? 39.000  3.590   -13.094 1.00 106.81 ? 827  GLY A O   1 
ATOM   1544 N N   . ASN A 1 220 ? 37.544  4.325   -14.642 1.00 105.02 ? 828  ASN A N   1 
ATOM   1545 C CA  . ASN A 1 220 ? 37.089  5.452   -13.841 1.00 105.08 ? 828  ASN A CA  1 
ATOM   1546 C C   . ASN A 1 220 ? 35.570  5.445   -13.677 1.00 103.59 ? 828  ASN A C   1 
ATOM   1547 O O   . ASN A 1 220 ? 35.043  5.913   -12.669 1.00 104.09 ? 828  ASN A O   1 
ATOM   1548 C CB  . ASN A 1 220 ? 37.560  6.776   -14.445 1.00 107.57 ? 828  ASN A CB  1 
ATOM   1549 C CG  . ASN A 1 220 ? 37.621  6.739   -15.957 1.00 112.79 ? 828  ASN A CG  1 
ATOM   1550 O OD1 . ASN A 1 220 ? 37.497  7.766   -16.616 1.00 114.16 ? 828  ASN A OD1 1 
ATOM   1551 N ND2 . ASN A 1 220 ? 37.804  5.548   -16.515 1.00 114.61 ? 828  ASN A ND2 1 
ATOM   1552 N N   . ALA A 1 221 ? 34.873  4.901   -14.671 1.00 101.18 ? 829  ALA A N   1 
ATOM   1553 C CA  . ALA A 1 221 ? 33.412  4.853   -14.645 1.00 99.00  ? 829  ALA A CA  1 
ATOM   1554 C C   . ALA A 1 221 ? 32.823  3.752   -15.526 1.00 95.84  ? 829  ALA A C   1 
ATOM   1555 O O   . ALA A 1 221 ? 33.500  3.214   -16.398 1.00 96.32  ? 829  ALA A O   1 
ATOM   1556 C CB  . ALA A 1 221 ? 32.837  6.206   -15.037 1.00 99.09  ? 829  ALA A CB  1 
ATOM   1557 N N   . ARG A 1 222 ? 31.558  3.423   -15.281 1.00 92.42  ? 830  ARG A N   1 
ATOM   1558 C CA  . ARG A 1 222 ? 30.849  2.410   -16.057 1.00 89.02  ? 830  ARG A CA  1 
ATOM   1559 C C   . ARG A 1 222 ? 30.064  3.077   -17.186 1.00 84.18  ? 830  ARG A C   1 
ATOM   1560 O O   . ARG A 1 222 ? 29.161  3.872   -16.944 1.00 83.45  ? 830  ARG A O   1 
ATOM   1561 C CB  . ARG A 1 222 ? 29.927  1.594   -15.154 1.00 90.84  ? 830  ARG A CB  1 
ATOM   1562 C CG  . ARG A 1 222 ? 30.669  0.849   -14.059 1.00 95.07  ? 830  ARG A CG  1 
ATOM   1563 C CD  . ARG A 1 222 ? 29.721  0.085   -13.153 1.00 99.86  ? 830  ARG A CD  1 
ATOM   1564 N NE  . ARG A 1 222 ? 30.441  -0.651  -12.118 1.00 104.43 ? 830  ARG A NE  1 
ATOM   1565 C CZ  . ARG A 1 222 ? 30.874  -1.900  -12.255 1.00 107.37 ? 830  ARG A CZ  1 
ATOM   1566 N NH1 . ARG A 1 222 ? 30.660  -2.557  -13.385 1.00 106.94 ? 830  ARG A NH1 1 
ATOM   1567 N NH2 . ARG A 1 222 ? 31.522  -2.492  -11.263 1.00 107.00 ? 830  ARG A NH2 1 
ATOM   1568 N N   . LEU A 1 223 ? 30.415  2.734   -18.419 1.00 80.85  ? 831  LEU A N   1 
ATOM   1569 C CA  . LEU A 1 223 ? 29.806  3.321   -19.610 1.00 78.33  ? 831  LEU A CA  1 
ATOM   1570 C C   . LEU A 1 223 ? 29.076  2.329   -20.521 1.00 75.69  ? 831  LEU A C   1 
ATOM   1571 O O   . LEU A 1 223 ? 29.546  1.208   -20.727 1.00 75.55  ? 831  LEU A O   1 
ATOM   1572 C CB  . LEU A 1 223 ? 30.900  3.991   -20.449 1.00 78.24  ? 831  LEU A CB  1 
ATOM   1573 C CG  . LEU A 1 223 ? 31.781  5.008   -19.766 1.00 79.00  ? 831  LEU A CG  1 
ATOM   1574 C CD1 . LEU A 1 223 ? 32.845  5.496   -20.720 1.00 79.45  ? 831  LEU A CD1 1 
ATOM   1575 C CD2 . LEU A 1 223 ? 30.957  6.168   -19.206 1.00 79.04  ? 831  LEU A CD2 1 
ATOM   1576 N N   . PRO A 1 224 ? 28.006  2.793   -21.210 1.00 73.34  ? 832  PRO A N   1 
ATOM   1577 C CA  . PRO A 1 224 ? 27.325  1.920   -22.179 1.00 71.37  ? 832  PRO A CA  1 
ATOM   1578 C C   . PRO A 1 224 ? 28.004  2.000   -23.545 1.00 69.84  ? 832  PRO A C   1 
ATOM   1579 O O   . PRO A 1 224 ? 27.433  2.495   -24.516 1.00 69.18  ? 832  PRO A O   1 
ATOM   1580 C CB  . PRO A 1 224 ? 25.904  2.474   -22.208 1.00 71.94  ? 832  PRO A CB  1 
ATOM   1581 C CG  . PRO A 1 224 ? 26.017  3.905   -21.751 1.00 72.92  ? 832  PRO A CG  1 
ATOM   1582 C CD  . PRO A 1 224 ? 27.369  4.125   -21.138 1.00 72.06  ? 832  PRO A CD  1 
ATOM   1583 N N   . VAL A 1 225 ? 29.240  1.479   -23.600 1.00 69.28  ? 833  VAL A N   1 
ATOM   1584 C CA  . VAL A 1 225 ? 30.158  1.474   -24.744 1.00 68.79  ? 833  VAL A CA  1 
ATOM   1585 C C   . VAL A 1 225 ? 29.535  1.016   -26.054 1.00 67.20  ? 833  VAL A C   1 
ATOM   1586 O O   . VAL A 1 225 ? 29.755  1.650   -27.093 1.00 67.82  ? 833  VAL A O   1 
ATOM   1587 C CB  . VAL A 1 225 ? 31.407  0.633   -24.401 1.00 69.87  ? 833  VAL A CB  1 
ATOM   1588 C CG1 . VAL A 1 225 ? 32.374  0.583   -25.577 1.00 70.32  ? 833  VAL A CG1 1 
ATOM   1589 C CG2 . VAL A 1 225 ? 32.094  1.186   -23.152 1.00 70.68  ? 833  VAL A CG2 1 
ATOM   1590 N N   . LYS A 1 226 ? 28.760  -0.069  -26.018 1.00 64.71  ? 834  LYS A N   1 
ATOM   1591 C CA  . LYS A 1 226 ? 28.134  -0.604  -27.228 1.00 63.29  ? 834  LYS A CA  1 
ATOM   1592 C C   . LYS A 1 226 ? 27.076  0.337   -27.858 1.00 61.50  ? 834  LYS A C   1 
ATOM   1593 O O   . LYS A 1 226 ? 26.743  0.166   -29.026 1.00 61.70  ? 834  LYS A O   1 
ATOM   1594 C CB  . LYS A 1 226 ? 27.566  -2.010  -26.968 1.00 64.74  ? 834  LYS A CB  1 
ATOM   1595 C CG  . LYS A 1 226 ? 28.676  -3.034  -26.768 1.00 67.77  ? 834  LYS A CG  1 
ATOM   1596 C CD  . LYS A 1 226 ? 28.181  -4.455  -26.678 1.00 70.85  ? 834  LYS A CD  1 
ATOM   1597 C CE  . LYS A 1 226 ? 29.297  -5.434  -26.955 1.00 73.81  ? 834  LYS A CE  1 
ATOM   1598 N NZ  . LYS A 1 226 ? 28.770  -6.784  -27.325 1.00 75.90  ? 834  LYS A NZ  1 
ATOM   1599 N N   . TRP A 1 227 ? 26.583  1.335   -27.098 1.00 59.47  ? 835  TRP A N   1 
ATOM   1600 C CA  . TRP A 1 227 ? 25.639  2.354   -27.571 1.00 58.11  ? 835  TRP A CA  1 
ATOM   1601 C C   . TRP A 1 227 ? 26.335  3.706   -27.868 1.00 59.35  ? 835  TRP A C   1 
ATOM   1602 O O   . TRP A 1 227 ? 25.682  4.635   -28.359 1.00 58.54  ? 835  TRP A O   1 
ATOM   1603 C CB  . TRP A 1 227 ? 24.544  2.598   -26.522 1.00 56.24  ? 835  TRP A CB  1 
ATOM   1604 C CG  . TRP A 1 227 ? 23.533  1.494   -26.410 1.00 54.58  ? 835  TRP A CG  1 
ATOM   1605 C CD1 . TRP A 1 227 ? 22.289  1.455   -26.971 1.00 54.47  ? 835  TRP A CD1 1 
ATOM   1606 C CD2 . TRP A 1 227 ? 23.695  0.256   -25.703 1.00 53.70  ? 835  TRP A CD2 1 
ATOM   1607 N NE1 . TRP A 1 227 ? 21.675  0.263   -26.675 1.00 54.19  ? 835  TRP A NE1 1 
ATOM   1608 C CE2 . TRP A 1 227 ? 22.523  -0.501  -25.914 1.00 53.80  ? 835  TRP A CE2 1 
ATOM   1609 C CE3 . TRP A 1 227 ? 24.726  -0.296  -24.931 1.00 53.86  ? 835  TRP A CE3 1 
ATOM   1610 C CZ2 . TRP A 1 227 ? 22.334  -1.747  -25.335 1.00 53.79  ? 835  TRP A CZ2 1 
ATOM   1611 C CZ3 . TRP A 1 227 ? 24.576  -1.579  -24.452 1.00 54.79  ? 835  TRP A CZ3 1 
ATOM   1612 C CH2 . TRP A 1 227 ? 23.378  -2.277  -24.629 1.00 54.32  ? 835  TRP A CH2 1 
ATOM   1613 N N   . MET A 1 228 ? 27.648  3.820   -27.549 1.00 60.95  ? 836  MET A N   1 
ATOM   1614 C CA  . MET A 1 228 ? 28.426  5.035   -27.693 1.00 63.07  ? 836  MET A CA  1 
ATOM   1615 C C   . MET A 1 228 ? 29.077  5.210   -29.043 1.00 65.06  ? 836  MET A C   1 
ATOM   1616 O O   . MET A 1 228 ? 29.704  4.289   -29.536 1.00 64.62  ? 836  MET A O   1 
ATOM   1617 C CB  . MET A 1 228 ? 29.478  5.143   -26.577 1.00 63.93  ? 836  MET A CB  1 
ATOM   1618 C CG  . MET A 1 228 ? 28.882  5.465   -25.234 1.00 66.45  ? 836  MET A CG  1 
ATOM   1619 S SD  . MET A 1 228 ? 29.988  5.076   -23.854 1.00 74.89  ? 836  MET A SD  1 
ATOM   1620 C CE  . MET A 1 228 ? 31.258  6.342   -24.082 1.00 73.93  ? 836  MET A CE  1 
ATOM   1621 N N   . ALA A 1 229 ? 28.968  6.433   -29.618 1.00 67.04  ? 837  ALA A N   1 
ATOM   1622 C CA  . ALA A 1 229 ? 29.594  6.822   -30.892 1.00 69.50  ? 837  ALA A CA  1 
ATOM   1623 C C   . ALA A 1 229 ? 31.120  6.836   -30.745 1.00 72.08  ? 837  ALA A C   1 
ATOM   1624 O O   . ALA A 1 229 ? 31.625  7.092   -29.650 1.00 72.61  ? 837  ALA A O   1 
ATOM   1625 C CB  . ALA A 1 229 ? 29.094  8.198   -31.324 1.00 69.75  ? 837  ALA A CB  1 
ATOM   1626 N N   . PRO A 1 230 ? 31.884  6.565   -31.817 1.00 74.00  ? 838  PRO A N   1 
ATOM   1627 C CA  . PRO A 1 230 ? 33.352  6.534   -31.692 1.00 75.95  ? 838  PRO A CA  1 
ATOM   1628 C C   . PRO A 1 230 ? 33.974  7.743   -31.031 1.00 78.73  ? 838  PRO A C   1 
ATOM   1629 O O   . PRO A 1 230 ? 34.802  7.563   -30.152 1.00 79.59  ? 838  PRO A O   1 
ATOM   1630 C CB  . PRO A 1 230 ? 33.821  6.377   -33.138 1.00 76.14  ? 838  PRO A CB  1 
ATOM   1631 C CG  . PRO A 1 230 ? 32.713  5.621   -33.782 1.00 75.78  ? 838  PRO A CG  1 
ATOM   1632 C CD  . PRO A 1 230 ? 31.470  6.225   -33.186 1.00 73.66  ? 838  PRO A CD  1 
ATOM   1633 N N   . GLU A 1 231 ? 33.506  8.955   -31.367 1.00 80.13  ? 839  GLU A N   1 
ATOM   1634 C CA  . GLU A 1 231 ? 34.026  10.196  -30.800 1.00 81.86  ? 839  GLU A CA  1 
ATOM   1635 C C   . GLU A 1 231 ? 33.712  10.380  -29.305 1.00 84.27  ? 839  GLU A C   1 
ATOM   1636 O O   . GLU A 1 231 ? 34.301  11.256  -28.662 1.00 84.86  ? 839  GLU A O   1 
ATOM   1637 C CB  . GLU A 1 231 ? 33.538  11.393  -31.616 1.00 83.49  ? 839  GLU A CB  1 
ATOM   1638 C CG  . GLU A 1 231 ? 32.057  11.696  -31.452 1.00 87.91  ? 839  GLU A CG  1 
ATOM   1639 C CD  . GLU A 1 231 ? 31.119  11.002  -32.424 1.00 92.95  ? 839  GLU A CD  1 
ATOM   1640 O OE1 . GLU A 1 231 ? 31.546  10.031  -33.097 1.00 93.15  ? 839  GLU A OE1 1 
ATOM   1641 O OE2 . GLU A 1 231 ? 29.946  11.436  -32.504 1.00 93.60  ? 839  GLU A OE2 1 
ATOM   1642 N N   . SER A 1 232 ? 32.778  9.583   -28.746 1.00 85.03  ? 840  SER A N   1 
ATOM   1643 C CA  . SER A 1 232 ? 32.498  9.640   -27.308 1.00 86.19  ? 840  SER A CA  1 
ATOM   1644 C C   . SER A 1 232 ? 33.461  8.676   -26.583 1.00 87.62  ? 840  SER A C   1 
ATOM   1645 O O   . SER A 1 232 ? 33.975  9.002   -25.517 1.00 87.79  ? 840  SER A O   1 
ATOM   1646 C CB  . SER A 1 232 ? 31.052  9.258   -27.014 1.00 87.14  ? 840  SER A CB  1 
ATOM   1647 O OG  . SER A 1 232 ? 30.150  10.198  -27.570 1.00 88.91  ? 840  SER A OG  1 
ATOM   1648 N N   . ILE A 1 233 ? 33.727  7.511   -27.172 1.00 88.61  ? 841  ILE A N   1 
ATOM   1649 C CA  . ILE A 1 233 ? 34.647  6.541   -26.587 1.00 90.46  ? 841  ILE A CA  1 
ATOM   1650 C C   . ILE A 1 233 ? 36.099  7.047   -26.648 1.00 92.65  ? 841  ILE A C   1 
ATOM   1651 O O   . ILE A 1 233 ? 36.822  6.995   -25.651 1.00 92.79  ? 841  ILE A O   1 
ATOM   1652 C CB  . ILE A 1 233 ? 34.474  5.198   -27.325 1.00 90.48  ? 841  ILE A CB  1 
ATOM   1653 C CG1 . ILE A 1 233 ? 33.122  4.573   -26.984 1.00 90.68  ? 841  ILE A CG1 1 
ATOM   1654 C CG2 . ILE A 1 233 ? 35.636  4.248   -27.052 1.00 90.83  ? 841  ILE A CG2 1 
ATOM   1655 C CD1 . ILE A 1 233 ? 32.728  3.571   -27.896 1.00 91.56  ? 841  ILE A CD1 1 
ATOM   1656 N N   . PHE A 1 234 ? 36.510  7.549   -27.814 1.00 93.96  ? 842  PHE A N   1 
ATOM   1657 C CA  . PHE A 1 234 ? 37.875  7.993   -28.009 1.00 95.82  ? 842  PHE A CA  1 
ATOM   1658 C C   . PHE A 1 234 ? 38.157  9.404   -27.527 1.00 96.87  ? 842  PHE A C   1 
ATOM   1659 O O   . PHE A 1 234 ? 39.309  9.687   -27.198 1.00 97.33  ? 842  PHE A O   1 
ATOM   1660 C CB  . PHE A 1 234 ? 38.293  7.839   -29.479 1.00 96.39  ? 842  PHE A CB  1 
ATOM   1661 C CG  . PHE A 1 234 ? 38.040  6.465   -30.053 1.00 97.99  ? 842  PHE A CG  1 
ATOM   1662 C CD1 . PHE A 1 234 ? 38.404  5.324   -29.354 1.00 99.07  ? 842  PHE A CD1 1 
ATOM   1663 C CD2 . PHE A 1 234 ? 37.502  6.314   -31.321 1.00 99.14  ? 842  PHE A CD2 1 
ATOM   1664 C CE1 . PHE A 1 234 ? 38.187  4.064   -29.891 1.00 99.85  ? 842  PHE A CE1 1 
ATOM   1665 C CE2 . PHE A 1 234 ? 37.282  5.051   -31.852 1.00 99.89  ? 842  PHE A CE2 1 
ATOM   1666 C CZ  . PHE A 1 234 ? 37.623  3.936   -31.133 1.00 99.82  ? 842  PHE A CZ  1 
ATOM   1667 N N   . ASN A 1 235 ? 37.152  10.303  -27.510 1.00 97.08  ? 843  ASN A N   1 
ATOM   1668 C CA  . ASN A 1 235 ? 37.420  11.698  -27.123 1.00 97.82  ? 843  ASN A CA  1 
ATOM   1669 C C   . ASN A 1 235 ? 36.520  12.289  -26.041 1.00 97.50  ? 843  ASN A C   1 
ATOM   1670 O O   . ASN A 1 235 ? 36.654  13.482  -25.754 1.00 97.41  ? 843  ASN A O   1 
ATOM   1671 C CB  . ASN A 1 235 ? 37.370  12.596  -28.351 1.00 99.81  ? 843  ASN A CB  1 
ATOM   1672 C CG  . ASN A 1 235 ? 38.346  12.198  -29.423 1.00 105.12 ? 843  ASN A CG  1 
ATOM   1673 O OD1 . ASN A 1 235 ? 39.546  12.540  -29.378 1.00 107.71 ? 843  ASN A OD1 1 
ATOM   1674 N ND2 . ASN A 1 235 ? 37.857  11.472  -30.419 1.00 105.87 ? 843  ASN A ND2 1 
ATOM   1675 N N   . CYS A 1 236 ? 35.606  11.487  -25.456 1.00 97.00  ? 844  CYS A N   1 
ATOM   1676 C CA  . CYS A 1 236 ? 34.632  11.952  -24.449 1.00 97.27  ? 844  CYS A CA  1 
ATOM   1677 C C   . CYS A 1 236 ? 33.721  13.069  -24.977 1.00 95.61  ? 844  CYS A C   1 
ATOM   1678 O O   . CYS A 1 236 ? 33.241  13.902  -24.213 1.00 95.27  ? 844  CYS A O   1 
ATOM   1679 C CB  . CYS A 1 236 ? 35.302  12.342  -23.135 1.00 99.73  ? 844  CYS A CB  1 
ATOM   1680 S SG  . CYS A 1 236 ? 36.435  11.089  -22.482 1.00 107.99 ? 844  CYS A SG  1 
ATOM   1681 N N   . VAL A 1 237 ? 33.478  13.062  -26.285 1.00 94.36  ? 845  VAL A N   1 
ATOM   1682 C CA  . VAL A 1 237 ? 32.649  14.036  -26.962 1.00 93.52  ? 845  VAL A CA  1 
ATOM   1683 C C   . VAL A 1 237 ? 31.215  13.520  -27.093 1.00 91.77  ? 845  VAL A C   1 
ATOM   1684 O O   . VAL A 1 237 ? 30.955  12.549  -27.801 1.00 91.79  ? 845  VAL A O   1 
ATOM   1685 C CB  . VAL A 1 237 ? 33.278  14.393  -28.335 1.00 94.50  ? 845  VAL A CB  1 
ATOM   1686 C CG1 . VAL A 1 237 ? 32.319  15.196  -29.206 1.00 95.12  ? 845  VAL A CG1 1 
ATOM   1687 C CG2 . VAL A 1 237 ? 34.593  15.138  -28.146 1.00 95.04  ? 845  VAL A CG2 1 
ATOM   1688 N N   . TYR A 1 238 ? 30.292  14.157  -26.379 1.00 90.00  ? 846  TYR A N   1 
ATOM   1689 C CA  . TYR A 1 238 ? 28.882  13.822  -26.460 1.00 88.36  ? 846  TYR A CA  1 
ATOM   1690 C C   . TYR A 1 238 ? 28.188  15.014  -27.105 1.00 86.59  ? 846  TYR A C   1 
ATOM   1691 O O   . TYR A 1 238 ? 28.148  16.119  -26.545 1.00 86.63  ? 846  TYR A O   1 
ATOM   1692 C CB  . TYR A 1 238 ? 28.292  13.561  -25.081 1.00 88.40  ? 846  TYR A CB  1 
ATOM   1693 C CG  . TYR A 1 238 ? 28.871  12.367  -24.360 1.00 89.32  ? 846  TYR A CG  1 
ATOM   1694 C CD1 . TYR A 1 238 ? 28.381  11.090  -24.584 1.00 90.15  ? 846  TYR A CD1 1 
ATOM   1695 C CD2 . TYR A 1 238 ? 29.830  12.529  -23.372 1.00 90.39  ? 846  TYR A CD2 1 
ATOM   1696 C CE1 . TYR A 1 238 ? 28.859  9.999   -23.871 1.00 91.31  ? 846  TYR A CE1 1 
ATOM   1697 C CE2 . TYR A 1 238 ? 30.323  11.445  -22.660 1.00 91.42  ? 846  TYR A CE2 1 
ATOM   1698 C CZ  . TYR A 1 238 ? 29.838  10.180  -22.915 1.00 92.70  ? 846  TYR A CZ  1 
ATOM   1699 O OH  . TYR A 1 238 ? 30.330  9.108   -22.210 1.00 95.07  ? 846  TYR A OH  1 
ATOM   1700 N N   . THR A 1 239 ? 27.692  14.801  -28.314 1.00 84.72  ? 847  THR A N   1 
ATOM   1701 C CA  . THR A 1 239 ? 27.009  15.830  -29.098 1.00 83.02  ? 847  THR A CA  1 
ATOM   1702 C C   . THR A 1 239 ? 25.602  15.347  -29.478 1.00 79.76  ? 847  THR A C   1 
ATOM   1703 O O   . THR A 1 239 ? 25.265  14.189  -29.212 1.00 79.01  ? 847  THR A O   1 
ATOM   1704 C CB  . THR A 1 239 ? 27.865  16.144  -30.348 1.00 85.13  ? 847  THR A CB  1 
ATOM   1705 O OG1 . THR A 1 239 ? 28.157  14.924  -31.052 1.00 86.64  ? 847  THR A OG1 1 
ATOM   1706 C CG2 . THR A 1 239 ? 29.139  16.862  -29.996 1.00 85.46  ? 847  THR A CG2 1 
ATOM   1707 N N   . PHE A 1 240 ? 24.773  16.206  -30.123 1.00 77.49  ? 848  PHE A N   1 
ATOM   1708 C CA  . PHE A 1 240 ? 23.450  15.762  -30.582 1.00 75.95  ? 848  PHE A CA  1 
ATOM   1709 C C   . PHE A 1 240 ? 23.589  14.574  -31.564 1.00 74.99  ? 848  PHE A C   1 
ATOM   1710 O O   . PHE A 1 240 ? 22.764  13.669  -31.574 1.00 74.81  ? 848  PHE A O   1 
ATOM   1711 C CB  . PHE A 1 240 ? 22.695  16.925  -31.223 1.00 75.29  ? 848  PHE A CB  1 
ATOM   1712 C CG  . PHE A 1 240 ? 22.503  18.071  -30.260 1.00 75.61  ? 848  PHE A CG  1 
ATOM   1713 C CD1 . PHE A 1 240 ? 21.523  18.022  -29.288 1.00 75.85  ? 848  PHE A CD1 1 
ATOM   1714 C CD2 . PHE A 1 240 ? 23.313  19.192  -30.318 1.00 76.66  ? 848  PHE A CD2 1 
ATOM   1715 C CE1 . PHE A 1 240 ? 21.363  19.056  -28.391 1.00 76.55  ? 848  PHE A CE1 1 
ATOM   1716 C CE2 . PHE A 1 240 ? 23.142  20.236  -29.420 1.00 77.21  ? 848  PHE A CE2 1 
ATOM   1717 C CZ  . PHE A 1 240 ? 22.178  20.153  -28.454 1.00 76.84  ? 848  PHE A CZ  1 
ATOM   1718 N N   . GLU A 1 241 ? 24.696  14.568  -32.328 1.00 73.95  ? 849  GLU A N   1 
ATOM   1719 C CA  . GLU A 1 241 ? 25.074  13.568  -33.298 1.00 72.92  ? 849  GLU A CA  1 
ATOM   1720 C C   . GLU A 1 241 ? 25.407  12.249  -32.630 1.00 70.87  ? 849  GLU A C   1 
ATOM   1721 O O   . GLU A 1 241 ? 25.053  11.186  -33.156 1.00 70.65  ? 849  GLU A O   1 
ATOM   1722 C CB  . GLU A 1 241 ? 26.271  14.077  -34.109 1.00 75.77  ? 849  GLU A CB  1 
ATOM   1723 C CG  . GLU A 1 241 ? 25.868  15.055  -35.191 1.00 81.69  ? 849  GLU A CG  1 
ATOM   1724 C CD  . GLU A 1 241 ? 26.208  16.498  -34.892 1.00 91.85  ? 849  GLU A CD  1 
ATOM   1725 O OE1 . GLU A 1 241 ? 26.408  16.829  -33.699 1.00 94.12  ? 849  GLU A OE1 1 
ATOM   1726 O OE2 . GLU A 1 241 ? 26.274  17.302  -35.855 1.00 94.75  ? 849  GLU A OE2 1 
ATOM   1727 N N   . SER A 1 242 ? 26.097  12.299  -31.480 1.00 69.00  ? 850  SER A N   1 
ATOM   1728 C CA  . SER A 1 242 ? 26.444  11.066  -30.767 1.00 67.34  ? 850  SER A CA  1 
ATOM   1729 C C   . SER A 1 242 ? 25.177  10.364  -30.280 1.00 65.28  ? 850  SER A C   1 
ATOM   1730 O O   . SER A 1 242 ? 25.092  9.141   -30.371 1.00 64.62  ? 850  SER A O   1 
ATOM   1731 C CB  . SER A 1 242 ? 27.432  11.338  -29.637 1.00 68.26  ? 850  SER A CB  1 
ATOM   1732 O OG  . SER A 1 242 ? 26.808  11.985  -28.546 1.00 70.97  ? 850  SER A OG  1 
ATOM   1733 N N   . ASP A 1 243 ? 24.159  11.156  -29.860 1.00 64.09  ? 851  ASP A N   1 
ATOM   1734 C CA  . ASP A 1 243 ? 22.845  10.675  -29.448 1.00 63.66  ? 851  ASP A CA  1 
ATOM   1735 C C   . ASP A 1 243 ? 22.183  9.931   -30.625 1.00 63.16  ? 851  ASP A C   1 
ATOM   1736 O O   . ASP A 1 243 ? 21.572  8.893   -30.434 1.00 62.58  ? 851  ASP A O   1 
ATOM   1737 C CB  . ASP A 1 243 ? 21.962  11.870  -29.045 1.00 64.39  ? 851  ASP A CB  1 
ATOM   1738 C CG  . ASP A 1 243 ? 21.696  12.014  -27.562 1.00 68.65  ? 851  ASP A CG  1 
ATOM   1739 O OD1 . ASP A 1 243 ? 22.443  11.404  -26.756 1.00 69.59  ? 851  ASP A OD1 1 
ATOM   1740 O OD2 . ASP A 1 243 ? 20.762  12.757  -27.200 1.00 70.57  ? 851  ASP A OD2 1 
ATOM   1741 N N   . VAL A 1 244 ? 22.309  10.483  -31.844 1.00 63.09  ? 852  VAL A N   1 
ATOM   1742 C CA  . VAL A 1 244 ? 21.773  9.894   -33.063 1.00 62.80  ? 852  VAL A CA  1 
ATOM   1743 C C   . VAL A 1 244 ? 22.406  8.540   -33.314 1.00 63.09  ? 852  VAL A C   1 
ATOM   1744 O O   . VAL A 1 244 ? 21.680  7.618   -33.675 1.00 63.99  ? 852  VAL A O   1 
ATOM   1745 C CB  . VAL A 1 244 ? 21.895  10.865  -34.255 1.00 62.68  ? 852  VAL A CB  1 
ATOM   1746 C CG1 . VAL A 1 244 ? 21.592  10.168  -35.582 1.00 62.74  ? 852  VAL A CG1 1 
ATOM   1747 C CG2 . VAL A 1 244 ? 20.988  12.080  -34.050 1.00 62.64  ? 852  VAL A CG2 1 
ATOM   1748 N N   . TRP A 1 245 ? 23.720  8.373   -33.016 1.00 62.79  ? 853  TRP A N   1 
ATOM   1749 C CA  . TRP A 1 245 ? 24.396  7.066   -33.113 1.00 63.50  ? 853  TRP A CA  1 
ATOM   1750 C C   . TRP A 1 245 ? 23.700  6.038   -32.210 1.00 62.57  ? 853  TRP A C   1 
ATOM   1751 O O   . TRP A 1 245 ? 23.428  4.925   -32.654 1.00 62.59  ? 853  TRP A O   1 
ATOM   1752 C CB  . TRP A 1 245 ? 25.889  7.175   -32.727 1.00 64.29  ? 853  TRP A CB  1 
ATOM   1753 C CG  . TRP A 1 245 ? 26.602  5.856   -32.631 1.00 65.87  ? 853  TRP A CG  1 
ATOM   1754 C CD1 . TRP A 1 245 ? 26.448  4.896   -31.671 1.00 66.87  ? 853  TRP A CD1 1 
ATOM   1755 C CD2 . TRP A 1 245 ? 27.597  5.359   -33.536 1.00 66.82  ? 853  TRP A CD2 1 
ATOM   1756 N NE1 . TRP A 1 245 ? 27.229  3.801   -31.970 1.00 67.41  ? 853  TRP A NE1 1 
ATOM   1757 C CE2 . TRP A 1 245 ? 27.967  4.074   -33.091 1.00 67.32  ? 853  TRP A CE2 1 
ATOM   1758 C CE3 . TRP A 1 245 ? 28.229  5.887   -34.666 1.00 67.67  ? 853  TRP A CE3 1 
ATOM   1759 C CZ2 . TRP A 1 245 ? 28.946  3.327   -33.721 1.00 68.32  ? 853  TRP A CZ2 1 
ATOM   1760 C CZ3 . TRP A 1 245 ? 29.178  5.129   -35.304 1.00 68.37  ? 853  TRP A CZ3 1 
ATOM   1761 C CH2 . TRP A 1 245 ? 29.529  3.865   -34.832 1.00 68.62  ? 853  TRP A CH2 1 
ATOM   1762 N N   . SER A 1 246 ? 23.432  6.420   -30.942 1.00 61.69  ? 854  SER A N   1 
ATOM   1763 C CA  . SER A 1 246 ? 22.783  5.601   -29.928 1.00 61.32  ? 854  SER A CA  1 
ATOM   1764 C C   . SER A 1 246 ? 21.392  5.175   -30.342 1.00 61.65  ? 854  SER A C   1 
ATOM   1765 O O   . SER A 1 246 ? 20.997  4.036   -30.061 1.00 61.79  ? 854  SER A O   1 
ATOM   1766 C CB  . SER A 1 246 ? 22.726  6.352   -28.611 1.00 61.60  ? 854  SER A CB  1 
ATOM   1767 O OG  . SER A 1 246 ? 24.052  6.517   -28.145 1.00 63.85  ? 854  SER A OG  1 
ATOM   1768 N N   . TYR A 1 247 ? 20.656  6.081   -31.028 1.00 61.15  ? 855  TYR A N   1 
ATOM   1769 C CA  . TYR A 1 247 ? 19.335  5.787   -31.581 1.00 61.06  ? 855  TYR A CA  1 
ATOM   1770 C C   . TYR A 1 247 ? 19.435  4.663   -32.610 1.00 61.80  ? 855  TYR A C   1 
ATOM   1771 O O   . TYR A 1 247 ? 18.537  3.833   -32.681 1.00 62.71  ? 855  TYR A O   1 
ATOM   1772 C CB  . TYR A 1 247 ? 18.716  7.038   -32.232 1.00 60.25  ? 855  TYR A CB  1 
ATOM   1773 C CG  . TYR A 1 247 ? 17.378  6.771   -32.888 1.00 60.41  ? 855  TYR A CG  1 
ATOM   1774 C CD1 . TYR A 1 247 ? 16.237  6.574   -32.127 1.00 60.88  ? 855  TYR A CD1 1 
ATOM   1775 C CD2 . TYR A 1 247 ? 17.262  6.682   -34.273 1.00 61.31  ? 855  TYR A CD2 1 
ATOM   1776 C CE1 . TYR A 1 247 ? 15.004  6.334   -32.723 1.00 61.87  ? 855  TYR A CE1 1 
ATOM   1777 C CE2 . TYR A 1 247 ? 16.041  6.401   -34.881 1.00 61.87  ? 855  TYR A CE2 1 
ATOM   1778 C CZ  . TYR A 1 247 ? 14.912  6.241   -34.100 1.00 62.82  ? 855  TYR A CZ  1 
ATOM   1779 O OH  . TYR A 1 247 ? 13.695  6.007   -34.681 1.00 64.19  ? 855  TYR A OH  1 
ATOM   1780 N N   . GLY A 1 248 ? 20.512  4.656   -33.401 1.00 61.14  ? 856  GLY A N   1 
ATOM   1781 C CA  . GLY A 1 248 ? 20.786  3.628   -34.390 1.00 61.01  ? 856  GLY A CA  1 
ATOM   1782 C C   . GLY A 1 248 ? 20.962  2.285   -33.720 1.00 61.33  ? 856  GLY A C   1 
ATOM   1783 O O   . GLY A 1 248 ? 20.406  1.291   -34.188 1.00 62.58  ? 856  GLY A O   1 
ATOM   1784 N N   . ILE A 1 249 ? 21.699  2.243   -32.591 1.00 60.34  ? 857  ILE A N   1 
ATOM   1785 C CA  . ILE A 1 249 ? 21.885  1.010   -31.801 1.00 59.53  ? 857  ILE A CA  1 
ATOM   1786 C C   . ILE A 1 249 ? 20.537  0.555   -31.206 1.00 58.03  ? 857  ILE A C   1 
ATOM   1787 O O   . ILE A 1 249 ? 20.245  -0.631  -31.178 1.00 57.83  ? 857  ILE A O   1 
ATOM   1788 C CB  . ILE A 1 249 ? 22.985  1.188   -30.710 1.00 59.91  ? 857  ILE A CB  1 
ATOM   1789 C CG1 . ILE A 1 249 ? 24.265  1.776   -31.314 1.00 61.37  ? 857  ILE A CG1 1 
ATOM   1790 C CG2 . ILE A 1 249 ? 23.282  -0.131  -30.006 1.00 59.46  ? 857  ILE A CG2 1 
ATOM   1791 C CD1 . ILE A 1 249 ? 24.926  0.800   -32.415 1.00 63.18  ? 857  ILE A CD1 1 
ATOM   1792 N N   . PHE A 1 250 ? 19.698  1.517   -30.802 1.00 57.22  ? 858  PHE A N   1 
ATOM   1793 C CA  . PHE A 1 250 ? 18.355  1.279   -30.273 1.00 56.16  ? 858  PHE A CA  1 
ATOM   1794 C C   . PHE A 1 250 ? 17.498  0.616   -31.340 1.00 56.12  ? 858  PHE A C   1 
ATOM   1795 O O   . PHE A 1 250 ? 16.820  -0.366  -31.056 1.00 55.54  ? 858  PHE A O   1 
ATOM   1796 C CB  . PHE A 1 250 ? 17.700  2.592   -29.761 1.00 54.44  ? 858  PHE A CB  1 
ATOM   1797 C CG  . PHE A 1 250 ? 16.194  2.497   -29.661 1.00 53.93  ? 858  PHE A CG  1 
ATOM   1798 C CD1 . PHE A 1 250 ? 15.597  1.685   -28.706 1.00 54.34  ? 858  PHE A CD1 1 
ATOM   1799 C CD2 . PHE A 1 250 ? 15.384  3.118   -30.596 1.00 54.15  ? 858  PHE A CD2 1 
ATOM   1800 C CE1 . PHE A 1 250 ? 14.231  1.508   -28.679 1.00 54.85  ? 858  PHE A CE1 1 
ATOM   1801 C CE2 . PHE A 1 250 ? 14.013  2.959   -30.557 1.00 54.90  ? 858  PHE A CE2 1 
ATOM   1802 C CZ  . PHE A 1 250 ? 13.441  2.170   -29.585 1.00 55.07  ? 858  PHE A CZ  1 
ATOM   1803 N N   . LEU A 1 251 ? 17.532  1.126   -32.581 1.00 56.87  ? 859  LEU A N   1 
ATOM   1804 C CA  . LEU A 1 251 ? 16.753  0.523   -33.679 1.00 57.98  ? 859  LEU A CA  1 
ATOM   1805 C C   . LEU A 1 251 ? 17.157  -0.924  -33.869 1.00 58.64  ? 859  LEU A C   1 
ATOM   1806 O O   . LEU A 1 251 ? 16.290  -1.776  -33.967 1.00 58.76  ? 859  LEU A O   1 
ATOM   1807 C CB  . LEU A 1 251 ? 16.951  1.269   -35.006 1.00 58.46  ? 859  LEU A CB  1 
ATOM   1808 C CG  . LEU A 1 251 ? 16.291  2.632   -35.198 1.00 60.30  ? 859  LEU A CG  1 
ATOM   1809 C CD1 . LEU A 1 251 ? 16.338  3.011   -36.667 1.00 60.74  ? 859  LEU A CD1 1 
ATOM   1810 C CD2 . LEU A 1 251 ? 14.821  2.631   -34.721 1.00 61.32  ? 859  LEU A CD2 1 
ATOM   1811 N N   . TRP A 1 252 ? 18.481  -1.208  -33.793 1.00 58.86  ? 860  TRP A N   1 
ATOM   1812 C CA  . TRP A 1 252 ? 18.998  -2.561  -33.879 1.00 59.61  ? 860  TRP A CA  1 
ATOM   1813 C C   . TRP A 1 252 ? 18.399  -3.432  -32.763 1.00 60.02  ? 860  TRP A C   1 
ATOM   1814 O O   . TRP A 1 252 ? 17.889  -4.506  -33.049 1.00 59.88  ? 860  TRP A O   1 
ATOM   1815 C CB  . TRP A 1 252 ? 20.533  -2.570  -33.807 1.00 59.97  ? 860  TRP A CB  1 
ATOM   1816 C CG  . TRP A 1 252 ? 21.104  -3.902  -34.167 1.00 60.85  ? 860  TRP A CG  1 
ATOM   1817 C CD1 . TRP A 1 252 ? 21.515  -4.301  -35.406 1.00 62.22  ? 860  TRP A CD1 1 
ATOM   1818 C CD2 . TRP A 1 252 ? 21.221  -5.049  -33.315 1.00 61.01  ? 860  TRP A CD2 1 
ATOM   1819 N NE1 . TRP A 1 252 ? 21.894  -5.619  -35.377 1.00 62.97  ? 860  TRP A NE1 1 
ATOM   1820 C CE2 . TRP A 1 252 ? 21.723  -6.107  -34.104 1.00 62.59  ? 860  TRP A CE2 1 
ATOM   1821 C CE3 . TRP A 1 252 ? 21.008  -5.272  -31.948 1.00 61.39  ? 860  TRP A CE3 1 
ATOM   1822 C CZ2 . TRP A 1 252 ? 22.000  -7.373  -33.573 1.00 63.10  ? 860  TRP A CZ2 1 
ATOM   1823 C CZ3 . TRP A 1 252 ? 21.258  -6.528  -31.431 1.00 62.87  ? 860  TRP A CZ3 1 
ATOM   1824 C CH2 . TRP A 1 252 ? 21.765  -7.560  -32.235 1.00 63.13  ? 860  TRP A CH2 1 
ATOM   1825 N N   . GLU A 1 253 ? 18.429  -2.943  -31.505 1.00 60.33  ? 861  GLU A N   1 
ATOM   1826 C CA  . GLU A 1 253 ? 17.889  -3.640  -30.334 1.00 60.98  ? 861  GLU A CA  1 
ATOM   1827 C C   . GLU A 1 253 ? 16.413  -3.946  -30.528 1.00 61.31  ? 861  GLU A C   1 
ATOM   1828 O O   . GLU A 1 253 ? 15.977  -5.044  -30.231 1.00 60.77  ? 861  GLU A O   1 
ATOM   1829 C CB  . GLU A 1 253 ? 17.964  -2.742  -29.089 1.00 62.61  ? 861  GLU A CB  1 
ATOM   1830 C CG  . GLU A 1 253 ? 19.304  -2.463  -28.463 1.00 65.52  ? 861  GLU A CG  1 
ATOM   1831 C CD  . GLU A 1 253 ? 18.992  -1.663  -27.207 1.00 68.36  ? 861  GLU A CD  1 
ATOM   1832 O OE1 . GLU A 1 253 ? 18.679  -2.295  -26.173 1.00 66.67  ? 861  GLU A OE1 1 
ATOM   1833 O OE2 . GLU A 1 253 ? 18.966  -0.411  -27.280 1.00 68.38  ? 861  GLU A OE2 1 
ATOM   1834 N N   . LEU A 1 254 ? 15.640  -2.925  -30.952 1.00 61.77  ? 862  LEU A N   1 
ATOM   1835 C CA  . LEU A 1 254 ? 14.208  -2.961  -31.151 1.00 62.60  ? 862  LEU A CA  1 
ATOM   1836 C C   . LEU A 1 254 ? 13.806  -3.970  -32.227 1.00 64.19  ? 862  LEU A C   1 
ATOM   1837 O O   . LEU A 1 254 ? 12.941  -4.806  -31.978 1.00 64.61  ? 862  LEU A O   1 
ATOM   1838 C CB  . LEU A 1 254 ? 13.746  -1.540  -31.495 1.00 62.34  ? 862  LEU A CB  1 
ATOM   1839 C CG  . LEU A 1 254 ? 12.327  -1.336  -31.961 1.00 63.19  ? 862  LEU A CG  1 
ATOM   1840 C CD1 . LEU A 1 254 ? 11.334  -1.782  -30.912 1.00 63.32  ? 862  LEU A CD1 1 
ATOM   1841 C CD2 . LEU A 1 254 ? 12.107  0.121   -32.263 1.00 64.08  ? 862  LEU A CD2 1 
ATOM   1842 N N   . PHE A 1 255 ? 14.460  -3.933  -33.394 1.00 64.73  ? 863  PHE A N   1 
ATOM   1843 C CA  . PHE A 1 255 ? 14.130  -4.838  -34.482 1.00 66.07  ? 863  PHE A CA  1 
ATOM   1844 C C   . PHE A 1 255 ? 14.652  -6.267  -34.307 1.00 67.13  ? 863  PHE A C   1 
ATOM   1845 O O   . PHE A 1 255 ? 14.260  -7.151  -35.055 1.00 67.74  ? 863  PHE A O   1 
ATOM   1846 C CB  . PHE A 1 255 ? 14.566  -4.240  -35.803 1.00 66.30  ? 863  PHE A CB  1 
ATOM   1847 C CG  . PHE A 1 255 ? 13.530  -3.234  -36.227 1.00 67.33  ? 863  PHE A CG  1 
ATOM   1848 C CD1 . PHE A 1 255 ? 12.288  -3.645  -36.683 1.00 68.18  ? 863  PHE A CD1 1 
ATOM   1849 C CD2 . PHE A 1 255 ? 13.769  -1.877  -36.106 1.00 68.02  ? 863  PHE A CD2 1 
ATOM   1850 C CE1 . PHE A 1 255 ? 11.323  -2.715  -37.051 1.00 68.74  ? 863  PHE A CE1 1 
ATOM   1851 C CE2 . PHE A 1 255 ? 12.795  -0.952  -36.460 1.00 68.85  ? 863  PHE A CE2 1 
ATOM   1852 C CZ  . PHE A 1 255 ? 11.585  -1.379  -36.948 1.00 68.49  ? 863  PHE A CZ  1 
ATOM   1853 N N   . SER A 1 256 ? 15.532  -6.493  -33.339 1.00 67.26  ? 864  SER A N   1 
ATOM   1854 C CA  . SER A 1 256 ? 15.999  -7.821  -32.987 1.00 67.50  ? 864  SER A CA  1 
ATOM   1855 C C   . SER A 1 256 ? 15.290  -8.332  -31.713 1.00 69.63  ? 864  SER A C   1 
ATOM   1856 O O   . SER A 1 256 ? 15.710  -9.337  -31.149 1.00 70.25  ? 864  SER A O   1 
ATOM   1857 C CB  . SER A 1 256 ? 17.502  -7.820  -32.798 1.00 67.26  ? 864  SER A CB  1 
ATOM   1858 O OG  . SER A 1 256 ? 17.880  -7.010  -31.705 1.00 68.46  ? 864  SER A OG  1 
ATOM   1859 N N   . LEU A 1 257 ? 14.184  -7.661  -31.291 1.00 70.59  ? 865  LEU A N   1 
ATOM   1860 C CA  . LEU A 1 257 ? 13.332  -7.968  -30.151 1.00 71.48  ? 865  LEU A CA  1 
ATOM   1861 C C   . LEU A 1 257 ? 14.081  -8.067  -28.829 1.00 71.73  ? 865  LEU A C   1 
ATOM   1862 O O   . LEU A 1 257 ? 13.836  -8.983  -28.049 1.00 72.52  ? 865  LEU A O   1 
ATOM   1863 C CB  . LEU A 1 257 ? 12.480  -9.218  -30.416 1.00 72.22  ? 865  LEU A CB  1 
ATOM   1864 C CG  . LEU A 1 257 ? 11.527  -9.105  -31.617 1.00 74.33  ? 865  LEU A CG  1 
ATOM   1865 C CD1 . LEU A 1 257 ? 10.723  -10.353 -31.773 1.00 75.27  ? 865  LEU A CD1 1 
ATOM   1866 C CD2 . LEU A 1 257 ? 10.578  -7.914  -31.478 1.00 75.01  ? 865  LEU A CD2 1 
ATOM   1867 N N   . GLY A 1 258 ? 14.947  -7.095  -28.568 1.00 71.05  ? 866  GLY A N   1 
ATOM   1868 C CA  . GLY A 1 258 ? 15.669  -6.992  -27.308 1.00 70.81  ? 866  GLY A CA  1 
ATOM   1869 C C   . GLY A 1 258 ? 17.023  -7.657  -27.232 1.00 70.51  ? 866  GLY A C   1 
ATOM   1870 O O   . GLY A 1 258 ? 17.522  -7.892  -26.136 1.00 70.83  ? 866  GLY A O   1 
ATOM   1871 N N   . SER A 1 259 ? 17.645  -7.951  -28.367 1.00 69.82  ? 867  SER A N   1 
ATOM   1872 C CA  . SER A 1 259 ? 18.973  -8.570  -28.370 1.00 69.48  ? 867  SER A CA  1 
ATOM   1873 C C   . SER A 1 259 ? 20.051  -7.549  -27.989 1.00 67.69  ? 867  SER A C   1 
ATOM   1874 O O   . SER A 1 259 ? 19.915  -6.364  -28.316 1.00 68.04  ? 867  SER A O   1 
ATOM   1875 C CB  . SER A 1 259 ? 19.252  -9.210  -29.731 1.00 72.79  ? 867  SER A CB  1 
ATOM   1876 O OG  . SER A 1 259 ? 20.589  -9.663  -29.872 1.00 77.94  ? 867  SER A OG  1 
ATOM   1877 N N   . SER A 1 260 ? 21.068  -7.979  -27.232 1.00 65.70  ? 868  SER A N   1 
ATOM   1878 C CA  . SER A 1 260 ? 22.178  -7.108  -26.849 1.00 65.08  ? 868  SER A CA  1 
ATOM   1879 C C   . SER A 1 260 ? 23.007  -6.831  -28.091 1.00 64.67  ? 868  SER A C   1 
ATOM   1880 O O   . SER A 1 260 ? 23.234  -7.720  -28.914 1.00 64.58  ? 868  SER A O   1 
ATOM   1881 C CB  . SER A 1 260 ? 23.073  -7.764  -25.798 1.00 66.56  ? 868  SER A CB  1 
ATOM   1882 O OG  . SER A 1 260 ? 22.559  -7.671  -24.480 1.00 69.08  ? 868  SER A OG  1 
ATOM   1883 N N   . PRO A 1 261 ? 23.487  -5.595  -28.248 1.00 64.25  ? 869  PRO A N   1 
ATOM   1884 C CA  . PRO A 1 261 ? 24.260  -5.260  -29.456 1.00 64.42  ? 869  PRO A CA  1 
ATOM   1885 C C   . PRO A 1 261 ? 25.604  -5.970  -29.536 1.00 65.02  ? 869  PRO A C   1 
ATOM   1886 O O   . PRO A 1 261 ? 26.119  -6.445  -28.521 1.00 64.97  ? 869  PRO A O   1 
ATOM   1887 C CB  . PRO A 1 261 ? 24.384  -3.736  -29.402 1.00 64.75  ? 869  PRO A CB  1 
ATOM   1888 C CG  . PRO A 1 261 ? 23.448  -3.310  -28.346 1.00 64.99  ? 869  PRO A CG  1 
ATOM   1889 C CD  . PRO A 1 261 ? 23.310  -4.427  -27.382 1.00 63.08  ? 869  PRO A CD  1 
ATOM   1890 N N   . TYR A 1 262 ? 26.116  -6.132  -30.774 1.00 65.80  ? 870  TYR A N   1 
ATOM   1891 C CA  . TYR A 1 262 ? 27.386  -6.812  -31.081 1.00 66.76  ? 870  TYR A CA  1 
ATOM   1892 C C   . TYR A 1 262 ? 27.462  -8.179  -30.377 1.00 67.83  ? 870  TYR A C   1 
ATOM   1893 O O   . TYR A 1 262 ? 28.328  -8.385  -29.521 1.00 67.60  ? 870  TYR A O   1 
ATOM   1894 C CB  . TYR A 1 262 ? 28.563  -5.906  -30.674 1.00 66.59  ? 870  TYR A CB  1 
ATOM   1895 C CG  . TYR A 1 262 ? 28.489  -4.548  -31.338 1.00 67.88  ? 870  TYR A CG  1 
ATOM   1896 C CD1 . TYR A 1 262 ? 28.956  -4.363  -32.627 1.00 69.26  ? 870  TYR A CD1 1 
ATOM   1897 C CD2 . TYR A 1 262 ? 27.892  -3.468  -30.700 1.00 68.96  ? 870  TYR A CD2 1 
ATOM   1898 C CE1 . TYR A 1 262 ? 28.880  -3.129  -33.253 1.00 70.46  ? 870  TYR A CE1 1 
ATOM   1899 C CE2 . TYR A 1 262 ? 27.797  -2.229  -31.323 1.00 70.35  ? 870  TYR A CE2 1 
ATOM   1900 C CZ  . TYR A 1 262 ? 28.293  -2.066  -32.606 1.00 71.45  ? 870  TYR A CZ  1 
ATOM   1901 O OH  . TYR A 1 262 ? 28.232  -0.866  -33.271 1.00 73.18  ? 870  TYR A OH  1 
ATOM   1902 N N   . PRO A 1 263 ? 26.496  -9.086  -30.647 1.00 68.65  ? 871  PRO A N   1 
ATOM   1903 C CA  . PRO A 1 263 ? 26.486  -10.380 -29.938 1.00 69.68  ? 871  PRO A CA  1 
ATOM   1904 C C   . PRO A 1 263 ? 27.818  -11.112 -29.923 1.00 72.68  ? 871  PRO A C   1 
ATOM   1905 O O   . PRO A 1 263 ? 28.573  -11.072 -30.909 1.00 72.96  ? 871  PRO A O   1 
ATOM   1906 C CB  . PRO A 1 263 ? 25.440  -11.193 -30.687 1.00 69.57  ? 871  PRO A CB  1 
ATOM   1907 C CG  . PRO A 1 263 ? 24.587  -10.193 -31.368 1.00 69.57  ? 871  PRO A CG  1 
ATOM   1908 C CD  . PRO A 1 263 ? 25.403  -8.992  -31.636 1.00 67.91  ? 871  PRO A CD  1 
ATOM   1909 N N   . GLY A 1 264 ? 28.121  -11.709 -28.775 1.00 74.31  ? 872  GLY A N   1 
ATOM   1910 C CA  . GLY A 1 264 ? 29.341  -12.472 -28.580 1.00 76.54  ? 872  GLY A CA  1 
ATOM   1911 C C   . GLY A 1 264 ? 30.642  -11.718 -28.744 1.00 78.82  ? 872  GLY A C   1 
ATOM   1912 O O   . GLY A 1 264 ? 31.703  -12.341 -28.752 1.00 79.67  ? 872  GLY A O   1 
ATOM   1913 N N   . MET A 1 265 ? 30.586  -10.388 -28.889 1.00 79.55  ? 873  MET A N   1 
ATOM   1914 C CA  . MET A 1 265 ? 31.787  -9.582  -29.017 1.00 81.05  ? 873  MET A CA  1 
ATOM   1915 C C   . MET A 1 265 ? 31.972  -8.819  -27.722 1.00 83.42  ? 873  MET A C   1 
ATOM   1916 O O   . MET A 1 265 ? 31.263  -7.842  -27.483 1.00 83.79  ? 873  MET A O   1 
ATOM   1917 C CB  . MET A 1 265 ? 31.649  -8.566  -30.150 1.00 81.37  ? 873  MET A CB  1 
ATOM   1918 C CG  . MET A 1 265 ? 31.744  -9.144  -31.519 1.00 83.62  ? 873  MET A CG  1 
ATOM   1919 S SD  . MET A 1 265 ? 31.829  -7.820  -32.754 1.00 90.08  ? 873  MET A SD  1 
ATOM   1920 C CE  . MET A 1 265 ? 33.427  -7.099  -32.342 1.00 92.18  ? 873  MET A CE  1 
ATOM   1921 N N   . PRO A 1 266 ? 32.911  -9.232  -26.857 1.00 84.60  ? 874  PRO A N   1 
ATOM   1922 C CA  . PRO A 1 266 ? 33.116  -8.484  -25.600 1.00 85.28  ? 874  PRO A CA  1 
ATOM   1923 C C   . PRO A 1 266 ? 33.806  -7.154  -25.862 1.00 86.24  ? 874  PRO A C   1 
ATOM   1924 O O   . PRO A 1 266 ? 34.602  -7.038  -26.800 1.00 86.13  ? 874  PRO A O   1 
ATOM   1925 C CB  . PRO A 1 266 ? 33.993  -9.425  -24.777 1.00 85.79  ? 874  PRO A CB  1 
ATOM   1926 C CG  . PRO A 1 266 ? 34.791  -10.169 -25.816 1.00 85.94  ? 874  PRO A CG  1 
ATOM   1927 C CD  . PRO A 1 266 ? 33.849  -10.365 -26.984 1.00 84.02  ? 874  PRO A CD  1 
ATOM   1928 N N   . VAL A 1 267 ? 33.490  -6.146  -25.047 1.00 87.20  ? 875  VAL A N   1 
ATOM   1929 C CA  . VAL A 1 267 ? 34.092  -4.829  -25.210 1.00 88.97  ? 875  VAL A CA  1 
ATOM   1930 C C   . VAL A 1 267 ? 35.570  -4.862  -24.777 1.00 91.11  ? 875  VAL A C   1 
ATOM   1931 O O   . VAL A 1 267 ? 35.874  -4.964  -23.586 1.00 91.45  ? 875  VAL A O   1 
ATOM   1932 C CB  . VAL A 1 267 ? 33.293  -3.731  -24.470 1.00 89.28  ? 875  VAL A CB  1 
ATOM   1933 C CG1 . VAL A 1 267 ? 34.034  -2.403  -24.517 1.00 89.91  ? 875  VAL A CG1 1 
ATOM   1934 C CG2 . VAL A 1 267 ? 31.894  -3.586  -25.048 1.00 89.08  ? 875  VAL A CG2 1 
ATOM   1935 N N   . ASP A 1 268 ? 36.483  -4.811  -25.751 1.00 92.20  ? 876  ASP A N   1 
ATOM   1936 C CA  . ASP A 1 268 ? 37.916  -4.882  -25.487 1.00 94.02  ? 876  ASP A CA  1 
ATOM   1937 C C   . ASP A 1 268 ? 38.732  -4.182  -26.619 1.00 95.81  ? 876  ASP A C   1 
ATOM   1938 O O   . ASP A 1 268 ? 38.132  -3.494  -27.454 1.00 95.94  ? 876  ASP A O   1 
ATOM   1939 C CB  . ASP A 1 268 ? 38.331  -6.363  -25.267 1.00 95.86  ? 876  ASP A CB  1 
ATOM   1940 C CG  . ASP A 1 268 ? 38.201  -7.263  -26.488 1.00 101.39 ? 876  ASP A CG  1 
ATOM   1941 O OD1 . ASP A 1 268 ? 37.659  -6.801  -27.517 1.00 102.48 ? 876  ASP A OD1 1 
ATOM   1942 O OD2 . ASP A 1 268 ? 38.631  -8.437  -26.410 1.00 104.02 ? 876  ASP A OD2 1 
ATOM   1943 N N   . SER A 1 269 ? 40.080  -4.381  -26.668 1.00 96.72  ? 877  SER A N   1 
ATOM   1944 C CA  . SER A 1 269 ? 40.948  -3.811  -27.703 1.00 98.05  ? 877  SER A CA  1 
ATOM   1945 C C   . SER A 1 269 ? 40.511  -4.226  -29.132 1.00 98.58  ? 877  SER A C   1 
ATOM   1946 O O   . SER A 1 269 ? 40.589  -3.418  -30.061 1.00 98.85  ? 877  SER A O   1 
ATOM   1947 C CB  . SER A 1 269 ? 42.420  -4.142  -27.425 1.00 100.16 ? 877  SER A CB  1 
ATOM   1948 O OG  . SER A 1 269 ? 42.983  -3.576  -26.246 1.00 102.86 ? 877  SER A OG  1 
ATOM   1949 N N   . LYS A 1 270 ? 40.027  -5.466  -29.294 1.00 98.47  ? 878  LYS A N   1 
ATOM   1950 C CA  . LYS A 1 270 ? 39.533  -5.942  -30.585 1.00 98.64  ? 878  LYS A CA  1 
ATOM   1951 C C   . LYS A 1 270 ? 38.279  -5.135  -30.988 1.00 98.68  ? 878  LYS A C   1 
ATOM   1952 O O   . LYS A 1 270 ? 38.210  -4.638  -32.111 1.00 98.59  ? 878  LYS A O   1 
ATOM   1953 C CB  . LYS A 1 270 ? 39.201  -7.439  -30.501 1.00 100.06 ? 878  LYS A CB  1 
ATOM   1954 C CG  . LYS A 1 270 ? 38.991  -8.109  -31.847 1.00 103.77 ? 878  LYS A CG  1 
ATOM   1955 C CD  . LYS A 1 270 ? 38.468  -9.528  -31.657 1.00 107.71 ? 878  LYS A CD  1 
ATOM   1956 C CE  . LYS A 1 270 ? 38.705  -10.401 -32.861 1.00 111.80 ? 878  LYS A CE  1 
ATOM   1957 N NZ  . LYS A 1 270 ? 40.112  -10.890 -32.928 1.00 114.54 ? 878  LYS A NZ  1 
ATOM   1958 N N   . PHE A 1 271 ? 37.324  -4.963  -30.050 1.00 98.41  ? 879  PHE A N   1 
ATOM   1959 C CA  . PHE A 1 271 ? 36.077  -4.249  -30.301 1.00 98.76  ? 879  PHE A CA  1 
ATOM   1960 C C   . PHE A 1 271 ? 36.310  -2.801  -30.717 1.00 98.94  ? 879  PHE A C   1 
ATOM   1961 O O   . PHE A 1 271 ? 35.687  -2.314  -31.662 1.00 98.80  ? 879  PHE A O   1 
ATOM   1962 C CB  . PHE A 1 271 ? 35.139  -4.340  -29.086 1.00 98.72  ? 879  PHE A CB  1 
ATOM   1963 C CG  . PHE A 1 271 ? 33.884  -3.515  -29.242 1.00 99.45  ? 879  PHE A CG  1 
ATOM   1964 C CD1 . PHE A 1 271 ? 32.867  -3.925  -30.085 1.00 100.15 ? 879  PHE A CD1 1 
ATOM   1965 C CD2 . PHE A 1 271 ? 33.746  -2.302  -28.586 1.00 100.16 ? 879  PHE A CD2 1 
ATOM   1966 C CE1 . PHE A 1 271 ? 31.724  -3.154  -30.245 1.00 100.75 ? 879  PHE A CE1 1 
ATOM   1967 C CE2 . PHE A 1 271 ? 32.607  -1.533  -28.756 1.00 100.85 ? 879  PHE A CE2 1 
ATOM   1968 C CZ  . PHE A 1 271 ? 31.600  -1.968  -29.578 1.00 100.58 ? 879  PHE A CZ  1 
ATOM   1969 N N   . TYR A 1 272 ? 37.206  -2.125  -30.017 1.00 99.01  ? 880  TYR A N   1 
ATOM   1970 C CA  . TYR A 1 272 ? 37.528  -0.745  -30.318 1.00 99.82  ? 880  TYR A CA  1 
ATOM   1971 C C   . TYR A 1 272 ? 38.189  -0.591  -31.689 1.00 100.71 ? 880  TYR A C   1 
ATOM   1972 O O   . TYR A 1 272 ? 37.909  0.379   -32.390 1.00 100.60 ? 880  TYR A O   1 
ATOM   1973 C CB  . TYR A 1 272 ? 38.410  -0.168  -29.215 1.00 99.73  ? 880  TYR A CB  1 
ATOM   1974 C CG  . TYR A 1 272 ? 37.681  -0.013  -27.899 1.00 100.15 ? 880  TYR A CG  1 
ATOM   1975 C CD1 . TYR A 1 272 ? 36.511  0.721   -27.814 1.00 100.86 ? 880  TYR A CD1 1 
ATOM   1976 C CD2 . TYR A 1 272 ? 38.208  -0.531  -26.725 1.00 100.90 ? 880  TYR A CD2 1 
ATOM   1977 C CE1 . TYR A 1 272 ? 35.849  0.883   -26.605 1.00 101.67 ? 880  TYR A CE1 1 
ATOM   1978 C CE2 . TYR A 1 272 ? 37.550  -0.385  -25.513 1.00 101.59 ? 880  TYR A CE2 1 
ATOM   1979 C CZ  . TYR A 1 272 ? 36.383  0.346   -25.451 1.00 102.50 ? 880  TYR A CZ  1 
ATOM   1980 O OH  . TYR A 1 272 ? 35.745  0.527   -24.248 1.00 103.90 ? 880  TYR A OH  1 
ATOM   1981 N N   . LYS A 1 273 ? 39.048  -1.548  -32.078 1.00 101.47 ? 881  LYS A N   1 
ATOM   1982 C CA  . LYS A 1 273 ? 39.736  -1.511  -33.370 1.00 102.47 ? 881  LYS A CA  1 
ATOM   1983 C C   . LYS A 1 273 ? 38.757  -1.614  -34.532 1.00 103.41 ? 881  LYS A C   1 
ATOM   1984 O O   . LYS A 1 273 ? 38.850  -0.816  -35.467 1.00 103.36 ? 881  LYS A O   1 
ATOM   1985 C CB  . LYS A 1 273 ? 40.805  -2.613  -33.476 1.00 104.09 ? 881  LYS A CB  1 
ATOM   1986 C CG  . LYS A 1 273 ? 42.192  -2.157  -33.064 1.00 107.97 ? 881  LYS A CG  1 
ATOM   1987 C CD  . LYS A 1 273 ? 43.265  -3.179  -33.400 1.00 111.95 ? 881  LYS A CD  1 
ATOM   1988 C CE  . LYS A 1 273 ? 44.548  -2.814  -32.695 1.00 116.13 ? 881  LYS A CE  1 
ATOM   1989 N NZ  . LYS A 1 273 ? 45.727  -3.522  -33.265 1.00 118.96 ? 881  LYS A NZ  1 
ATOM   1990 N N   . MET A 1 274 ? 37.818  -2.583  -34.479 1.00 103.91 ? 882  MET A N   1 
ATOM   1991 C CA  . MET A 1 274 ? 36.847  -2.729  -35.556 1.00 105.01 ? 882  MET A CA  1 
ATOM   1992 C C   . MET A 1 274 ? 35.908  -1.555  -35.615 1.00 105.20 ? 882  MET A C   1 
ATOM   1993 O O   . MET A 1 274 ? 35.614  -1.085  -36.711 1.00 105.40 ? 882  MET A O   1 
ATOM   1994 C CB  . MET A 1 274 ? 36.089  -4.068  -35.542 1.00 106.76 ? 882  MET A CB  1 
ATOM   1995 C CG  . MET A 1 274 ? 36.020  -4.761  -34.209 1.00 110.87 ? 882  MET A CG  1 
ATOM   1996 S SD  . MET A 1 274 ? 36.420  -6.527  -34.380 1.00 120.70 ? 882  MET A SD  1 
ATOM   1997 C CE  . MET A 1 274 ? 38.100  -6.420  -35.065 1.00 117.77 ? 882  MET A CE  1 
ATOM   1998 N N   . ILE A 1 275 ? 35.510  -1.014  -34.453 1.00 104.95 ? 883  ILE A N   1 
ATOM   1999 C CA  . ILE A 1 275 ? 34.650  0.164   -34.431 1.00 105.24 ? 883  ILE A CA  1 
ATOM   2000 C C   . ILE A 1 275 ? 35.371  1.371   -35.052 1.00 105.61 ? 883  ILE A C   1 
ATOM   2001 O O   . ILE A 1 275 ? 34.773  2.080   -35.860 1.00 106.24 ? 883  ILE A O   1 
ATOM   2002 C CB  . ILE A 1 275 ? 34.064  0.435   -33.018 1.00 105.62 ? 883  ILE A CB  1 
ATOM   2003 C CG1 . ILE A 1 275 ? 33.053  -0.663  -32.635 1.00 106.40 ? 883  ILE A CG1 1 
ATOM   2004 C CG2 . ILE A 1 275 ? 33.412  1.816   -32.931 1.00 106.14 ? 883  ILE A CG2 1 
ATOM   2005 C CD1 . ILE A 1 275 ? 31.878  -0.804  -33.588 1.00 107.43 ? 883  ILE A CD1 1 
ATOM   2006 N N   . LYS A 1 276 ? 36.671  1.550   -34.752 1.00 105.08 ? 884  LYS A N   1 
ATOM   2007 C CA  . LYS A 1 276 ? 37.477  2.635   -35.325 1.00 104.98 ? 884  LYS A CA  1 
ATOM   2008 C C   . LYS A 1 276 ? 37.643  2.438   -36.854 1.00 104.59 ? 884  LYS A C   1 
ATOM   2009 O O   . LYS A 1 276 ? 37.594  3.405   -37.610 1.00 104.80 ? 884  LYS A O   1 
ATOM   2010 C CB  . LYS A 1 276 ? 38.848  2.688   -34.633 1.00 106.77 ? 884  LYS A CB  1 
ATOM   2011 C CG  . LYS A 1 276 ? 39.532  4.035   -34.710 1.00 111.09 ? 884  LYS A CG  1 
ATOM   2012 C CD  . LYS A 1 276 ? 40.972  3.983   -34.181 1.00 115.93 ? 884  LYS A CD  1 
ATOM   2013 C CE  . LYS A 1 276 ? 41.624  5.356   -34.179 1.00 119.76 ? 884  LYS A CE  1 
ATOM   2014 N NZ  . LYS A 1 276 ? 43.095  5.295   -34.457 1.00 121.83 ? 884  LYS A NZ  1 
ATOM   2015 N N   . GLU A 1 277 ? 37.793  1.178   -37.298 1.00 103.89 ? 885  GLU A N   1 
ATOM   2016 C CA  . GLU A 1 277 ? 37.938  0.785   -38.706 1.00 103.71 ? 885  GLU A CA  1 
ATOM   2017 C C   . GLU A 1 277 ? 36.652  0.959   -39.546 1.00 102.44 ? 885  GLU A C   1 
ATOM   2018 O O   . GLU A 1 277 ? 36.743  1.078   -40.767 1.00 102.59 ? 885  GLU A O   1 
ATOM   2019 C CB  . GLU A 1 277 ? 38.392  -0.685  -38.803 1.00 106.88 ? 885  GLU A CB  1 
ATOM   2020 C CG  . GLU A 1 277 ? 39.807  -0.896  -39.330 1.00 112.54 ? 885  GLU A CG  1 
ATOM   2021 C CD  . GLU A 1 277 ? 40.160  -2.337  -39.672 1.00 119.94 ? 885  GLU A CD  1 
ATOM   2022 O OE1 . GLU A 1 277 ? 39.312  -3.232  -39.445 1.00 120.43 ? 885  GLU A OE1 1 
ATOM   2023 O OE2 . GLU A 1 277 ? 41.288  -2.571  -40.168 1.00 123.10 ? 885  GLU A OE2 1 
ATOM   2024 N N   . GLY A 1 278 ? 35.477  0.910   -38.912 1.00 100.67 ? 886  GLY A N   1 
ATOM   2025 C CA  . GLY A 1 278 ? 34.216  1.052   -39.633 1.00 99.25  ? 886  GLY A CA  1 
ATOM   2026 C C   . GLY A 1 278 ? 33.358  -0.203  -39.664 1.00 97.72  ? 886  GLY A C   1 
ATOM   2027 O O   . GLY A 1 278 ? 32.496  -0.349  -40.538 1.00 97.91  ? 886  GLY A O   1 
ATOM   2028 N N   . PHE A 1 279 ? 33.586  -1.126  -38.722 1.00 95.80  ? 887  PHE A N   1 
ATOM   2029 C CA  . PHE A 1 279 ? 32.782  -2.334  -38.622 1.00 94.74  ? 887  PHE A CA  1 
ATOM   2030 C C   . PHE A 1 279 ? 31.425  -1.943  -38.013 1.00 93.00  ? 887  PHE A C   1 
ATOM   2031 O O   . PHE A 1 279 ? 31.363  -1.172  -37.045 1.00 92.98  ? 887  PHE A O   1 
ATOM   2032 C CB  . PHE A 1 279 ? 33.497  -3.391  -37.754 1.00 95.22  ? 887  PHE A CB  1 
ATOM   2033 C CG  . PHE A 1 279 ? 32.595  -4.369  -37.033 1.00 96.86  ? 887  PHE A CG  1 
ATOM   2034 C CD1 . PHE A 1 279 ? 31.977  -5.406  -37.718 1.00 98.10  ? 887  PHE A CD1 1 
ATOM   2035 C CD2 . PHE A 1 279 ? 32.328  -4.225  -35.679 1.00 98.14  ? 887  PHE A CD2 1 
ATOM   2036 C CE1 . PHE A 1 279 ? 31.110  -6.278  -37.064 1.00 98.95  ? 887  PHE A CE1 1 
ATOM   2037 C CE2 . PHE A 1 279 ? 31.456  -5.094  -35.029 1.00 99.02  ? 887  PHE A CE2 1 
ATOM   2038 C CZ  . PHE A 1 279 ? 30.857  -6.119  -35.723 1.00 98.83  ? 887  PHE A CZ  1 
ATOM   2039 N N   . ARG A 1 280 ? 30.340  -2.485  -38.575 1.00 90.71  ? 888  ARG A N   1 
ATOM   2040 C CA  . ARG A 1 280 ? 28.991  -2.209  -38.094 1.00 88.42  ? 888  ARG A CA  1 
ATOM   2041 C C   . ARG A 1 280 ? 28.221  -3.498  -37.974 1.00 86.91  ? 888  ARG A C   1 
ATOM   2042 O O   . ARG A 1 280 ? 28.523  -4.455  -38.666 1.00 87.51  ? 888  ARG A O   1 
ATOM   2043 C CB  . ARG A 1 280 ? 28.251  -1.290  -39.079 1.00 88.37  ? 888  ARG A CB  1 
ATOM   2044 C CG  . ARG A 1 280 ? 28.921  0.044   -39.325 1.00 89.98  ? 888  ARG A CG  1 
ATOM   2045 C CD  . ARG A 1 280 ? 29.015  0.896   -38.075 1.00 91.74  ? 888  ARG A CD  1 
ATOM   2046 N NE  . ARG A 1 280 ? 29.610  2.200   -38.367 1.00 92.95  ? 888  ARG A NE  1 
ATOM   2047 C CZ  . ARG A 1 280 ? 30.835  2.565   -38.007 1.00 93.80  ? 888  ARG A CZ  1 
ATOM   2048 N NH1 . ARG A 1 280 ? 31.608  1.733   -37.319 1.00 92.97  ? 888  ARG A NH1 1 
ATOM   2049 N NH2 . ARG A 1 280 ? 31.291  3.775   -38.312 1.00 93.07  ? 888  ARG A NH2 1 
ATOM   2050 N N   . MET A 1 281 ? 27.179  -3.509  -37.162 1.00 85.49  ? 889  MET A N   1 
ATOM   2051 C CA  . MET A 1 281 ? 26.314  -4.668  -37.030 1.00 84.65  ? 889  MET A CA  1 
ATOM   2052 C C   . MET A 1 281 ? 25.550  -4.969  -38.322 1.00 85.25  ? 889  MET A C   1 
ATOM   2053 O O   . MET A 1 281 ? 25.362  -4.103  -39.179 1.00 84.53  ? 889  MET A O   1 
ATOM   2054 C CB  . MET A 1 281 ? 25.316  -4.469  -35.879 1.00 83.64  ? 889  MET A CB  1 
ATOM   2055 C CG  . MET A 1 281 ? 25.926  -4.666  -34.536 1.00 82.63  ? 889  MET A CG  1 
ATOM   2056 S SD  . MET A 1 281 ? 24.711  -4.610  -33.223 1.00 77.63  ? 889  MET A SD  1 
ATOM   2057 C CE  . MET A 1 281 ? 24.217  -2.892  -33.323 1.00 71.45  ? 889  MET A CE  1 
ATOM   2058 N N   . LEU A 1 282 ? 25.109  -6.225  -38.439 1.00 86.41  ? 890  LEU A N   1 
ATOM   2059 C CA  . LEU A 1 282 ? 24.293  -6.742  -39.530 1.00 87.87  ? 890  LEU A CA  1 
ATOM   2060 C C   . LEU A 1 282 ? 22.831  -6.364  -39.289 1.00 88.88  ? 890  LEU A C   1 
ATOM   2061 O O   . LEU A 1 282 ? 22.436  -6.164  -38.137 1.00 89.41  ? 890  LEU A O   1 
ATOM   2062 C CB  . LEU A 1 282 ? 24.391  -8.276  -39.513 1.00 88.29  ? 890  LEU A CB  1 
ATOM   2063 C CG  . LEU A 1 282 ? 25.767  -8.863  -39.797 1.00 89.57  ? 890  LEU A CG  1 
ATOM   2064 C CD1 . LEU A 1 282 ? 25.796  -10.370 -39.488 1.00 89.70  ? 890  LEU A CD1 1 
ATOM   2065 C CD2 . LEU A 1 282 ? 26.193  -8.563  -41.230 1.00 90.12  ? 890  LEU A CD2 1 
ATOM   2066 N N   . SER A 1 283 ? 22.011  -6.349  -40.344 1.00 89.11  ? 891  SER A N   1 
ATOM   2067 C CA  . SER A 1 283 ? 20.589  -6.056  -40.187 1.00 89.98  ? 891  SER A CA  1 
ATOM   2068 C C   . SER A 1 283 ? 19.893  -7.114  -39.383 1.00 91.37  ? 891  SER A C   1 
ATOM   2069 O O   . SER A 1 283 ? 20.046  -8.295  -39.666 1.00 91.52  ? 891  SER A O   1 
ATOM   2070 C CB  . SER A 1 283 ? 19.895  -5.967  -41.539 1.00 90.49  ? 891  SER A CB  1 
ATOM   2071 O OG  . SER A 1 283 ? 18.539  -5.569  -41.398 1.00 91.48  ? 891  SER A OG  1 
ATOM   2072 N N   . PRO A 1 284 ? 19.083  -6.716  -38.394 1.00 92.37  ? 892  PRO A N   1 
ATOM   2073 C CA  . PRO A 1 284 ? 18.298  -7.716  -37.659 1.00 93.19  ? 892  PRO A CA  1 
ATOM   2074 C C   . PRO A 1 284 ? 17.237  -8.362  -38.573 1.00 94.55  ? 892  PRO A C   1 
ATOM   2075 O O   . PRO A 1 284 ? 16.887  -7.819  -39.622 1.00 94.58  ? 892  PRO A O   1 
ATOM   2076 C CB  . PRO A 1 284 ? 17.676  -6.910  -36.509 1.00 93.56  ? 892  PRO A CB  1 
ATOM   2077 C CG  . PRO A 1 284 ? 18.360  -5.564  -36.533 1.00 93.71  ? 892  PRO A CG  1 
ATOM   2078 C CD  . PRO A 1 284 ? 18.780  -5.348  -37.941 1.00 91.94  ? 892  PRO A CD  1 
ATOM   2079 N N   . GLU A 1 285 ? 16.748  -9.540  -38.188 1.00 95.50  ? 893  GLU A N   1 
ATOM   2080 C CA  . GLU A 1 285 ? 15.770  -10.311 -38.959 1.00 96.78  ? 893  GLU A CA  1 
ATOM   2081 C C   . GLU A 1 285 ? 14.459  -9.578  -39.281 1.00 96.58  ? 893  GLU A C   1 
ATOM   2082 O O   . GLU A 1 285 ? 13.995  -9.634  -40.416 1.00 96.77  ? 893  GLU A O   1 
ATOM   2083 C CB  . GLU A 1 285 ? 15.455  -11.625 -38.224 1.00 100.82 ? 893  GLU A CB  1 
ATOM   2084 C CG  . GLU A 1 285 ? 15.688  -12.896 -39.027 1.00 107.46 ? 893  GLU A CG  1 
ATOM   2085 C CD  . GLU A 1 285 ? 15.340  -14.159 -38.260 1.00 116.97 ? 893  GLU A CD  1 
ATOM   2086 O OE1 . GLU A 1 285 ? 15.372  -14.118 -37.006 1.00 118.90 ? 893  GLU A OE1 1 
ATOM   2087 O OE2 . GLU A 1 285 ? 15.036  -15.189 -38.908 1.00 120.03 ? 893  GLU A OE2 1 
ATOM   2088 N N   . HIS A 1 286 ? 13.864  -8.903  -38.297 1.00 95.99  ? 894  HIS A N   1 
ATOM   2089 C CA  . HIS A 1 286 ? 12.581  -8.232  -38.494 1.00 96.13  ? 894  HIS A CA  1 
ATOM   2090 C C   . HIS A 1 286 ? 12.670  -6.800  -39.037 1.00 94.86  ? 894  HIS A C   1 
ATOM   2091 O O   . HIS A 1 286 ? 11.653  -6.096  -39.061 1.00 94.71  ? 894  HIS A O   1 
ATOM   2092 C CB  . HIS A 1 286 ? 11.778  -8.246  -37.184 1.00 98.27  ? 894  HIS A CB  1 
ATOM   2093 C CG  . HIS A 1 286 ? 11.657  -9.610  -36.577 1.00 103.10 ? 894  HIS A CG  1 
ATOM   2094 N ND1 . HIS A 1 286 ? 12.443  -9.994  -35.498 1.00 105.69 ? 894  HIS A ND1 1 
ATOM   2095 C CD2 . HIS A 1 286 ? 10.868  -10.649 -36.935 1.00 104.74 ? 894  HIS A CD2 1 
ATOM   2096 C CE1 . HIS A 1 286 ? 12.096  -11.242 -35.228 1.00 106.28 ? 894  HIS A CE1 1 
ATOM   2097 N NE2 . HIS A 1 286 ? 11.151  -11.679 -36.065 1.00 106.26 ? 894  HIS A NE2 1 
ATOM   2098 N N   . ALA A 1 287 ? 13.860  -6.369  -39.479 1.00 93.54  ? 895  ALA A N   1 
ATOM   2099 C CA  . ALA A 1 287 ? 14.033  -5.003  -39.950 1.00 92.86  ? 895  ALA A CA  1 
ATOM   2100 C C   . ALA A 1 287 ? 13.722  -4.761  -41.422 1.00 92.15  ? 895  ALA A C   1 
ATOM   2101 O O   . ALA A 1 287 ? 14.418  -5.263  -42.298 1.00 92.47  ? 895  ALA A O   1 
ATOM   2102 C CB  . ALA A 1 287 ? 15.441  -4.524  -39.641 1.00 92.91  ? 895  ALA A CB  1 
ATOM   2103 N N   . PRO A 1 288 ? 12.751  -3.885  -41.715 1.00 91.19  ? 896  PRO A N   1 
ATOM   2104 C CA  . PRO A 1 288 ? 12.516  -3.492  -43.116 1.00 90.85  ? 896  PRO A CA  1 
ATOM   2105 C C   . PRO A 1 288 ? 13.767  -2.813  -43.698 1.00 91.21  ? 896  PRO A C   1 
ATOM   2106 O O   . PRO A 1 288 ? 14.477  -2.126  -42.977 1.00 91.31  ? 896  PRO A O   1 
ATOM   2107 C CB  . PRO A 1 288 ? 11.352  -2.497  -43.007 1.00 91.07  ? 896  PRO A CB  1 
ATOM   2108 C CG  . PRO A 1 288 ? 10.732  -2.758  -41.665 1.00 91.26  ? 896  PRO A CG  1 
ATOM   2109 C CD  . PRO A 1 288 ? 11.867  -3.154  -40.791 1.00 90.20  ? 896  PRO A CD  1 
ATOM   2110 N N   . ALA A 1 289 ? 14.065  -3.032  -44.979 1.00 91.45  ? 897  ALA A N   1 
ATOM   2111 C CA  . ALA A 1 289 ? 15.263  -2.472  -45.620 1.00 91.79  ? 897  ALA A CA  1 
ATOM   2112 C C   . ALA A 1 289 ? 15.491  -0.969  -45.379 1.00 91.79  ? 897  ALA A C   1 
ATOM   2113 O O   . ALA A 1 289 ? 16.610  -0.572  -45.056 1.00 92.32  ? 897  ALA A O   1 
ATOM   2114 C CB  . ALA A 1 289 ? 15.255  -2.769  -47.105 1.00 91.90  ? 897  ALA A CB  1 
ATOM   2115 N N   . GLU A 1 290 ? 14.435  -0.147  -45.483 1.00 90.91  ? 898  GLU A N   1 
ATOM   2116 C CA  . GLU A 1 290 ? 14.535  1.300   -45.256 1.00 90.32  ? 898  GLU A CA  1 
ATOM   2117 C C   . GLU A 1 290 ? 14.969  1.654   -43.828 1.00 88.65  ? 898  GLU A C   1 
ATOM   2118 O O   . GLU A 1 290 ? 15.605  2.686   -43.618 1.00 88.15  ? 898  GLU A O   1 
ATOM   2119 C CB  . GLU A 1 290 ? 13.212  1.991   -45.599 1.00 93.41  ? 898  GLU A CB  1 
ATOM   2120 C CG  . GLU A 1 290 ? 12.732  1.741   -47.017 1.00 99.73  ? 898  GLU A CG  1 
ATOM   2121 C CD  . GLU A 1 290 ? 11.823  0.540   -47.199 1.00 108.72 ? 898  GLU A CD  1 
ATOM   2122 O OE1 . GLU A 1 290 ? 11.455  -0.090  -46.180 1.00 109.48 ? 898  GLU A OE1 1 
ATOM   2123 O OE2 . GLU A 1 290 ? 11.478  0.230   -48.365 1.00 113.13 ? 898  GLU A OE2 1 
ATOM   2124 N N   . MET A 1 291 ? 14.639  0.773   -42.864 1.00 87.55  ? 899  MET A N   1 
ATOM   2125 C CA  . MET A 1 291 ? 14.974  0.884   -41.454 1.00 86.93  ? 899  MET A CA  1 
ATOM   2126 C C   . MET A 1 291 ? 16.434  0.545   -41.196 1.00 86.44  ? 899  MET A C   1 
ATOM   2127 O O   . MET A 1 291 ? 17.059  1.171   -40.331 1.00 86.42  ? 899  MET A O   1 
ATOM   2128 C CB  . MET A 1 291 ? 14.054  -0.003  -40.615 1.00 87.60  ? 899  MET A CB  1 
ATOM   2129 C CG  . MET A 1 291 ? 12.695  0.622   -40.382 1.00 90.20  ? 899  MET A CG  1 
ATOM   2130 S SD  . MET A 1 291 ? 12.795  2.113   -39.362 1.00 95.07  ? 899  MET A SD  1 
ATOM   2131 C CE  . MET A 1 291 ? 11.314  2.872   -39.811 1.00 95.56  ? 899  MET A CE  1 
ATOM   2132 N N   . TYR A 1 292 ? 17.003  -0.424  -41.953 1.00 85.77  ? 900  TYR A N   1 
ATOM   2133 C CA  . TYR A 1 292 ? 18.428  -0.732  -41.801 1.00 85.09  ? 900  TYR A CA  1 
ATOM   2134 C C   . TYR A 1 292 ? 19.269  0.402   -42.397 1.00 84.10  ? 900  TYR A C   1 
ATOM   2135 O O   . TYR A 1 292 ? 20.327  0.710   -41.863 1.00 83.76  ? 900  TYR A O   1 
ATOM   2136 C CB  . TYR A 1 292 ? 18.797  -2.089  -42.395 1.00 85.29  ? 900  TYR A CB  1 
ATOM   2137 C CG  . TYR A 1 292 ? 20.225  -2.503  -42.097 1.00 86.42  ? 900  TYR A CG  1 
ATOM   2138 C CD1 . TYR A 1 292 ? 20.727  -2.463  -40.804 1.00 87.48  ? 900  TYR A CD1 1 
ATOM   2139 C CD2 . TYR A 1 292 ? 21.061  -2.973  -43.104 1.00 87.18  ? 900  TYR A CD2 1 
ATOM   2140 C CE1 . TYR A 1 292 ? 22.044  -2.822  -40.527 1.00 88.52  ? 900  TYR A CE1 1 
ATOM   2141 C CE2 . TYR A 1 292 ? 22.365  -3.377  -42.832 1.00 88.16  ? 900  TYR A CE2 1 
ATOM   2142 C CZ  . TYR A 1 292 ? 22.854  -3.305  -41.540 1.00 89.29  ? 900  TYR A CZ  1 
ATOM   2143 O OH  . TYR A 1 292 ? 24.144  -3.694  -41.260 1.00 90.51  ? 900  TYR A OH  1 
ATOM   2144 N N   . ASP A 1 293 ? 18.765  1.080   -43.451 1.00 83.68  ? 901  ASP A N   1 
ATOM   2145 C CA  . ASP A 1 293 ? 19.435  2.230   -44.041 1.00 84.16  ? 901  ASP A CA  1 
ATOM   2146 C C   . ASP A 1 293 ? 19.518  3.346   -42.992 1.00 82.71  ? 901  ASP A C   1 
ATOM   2147 O O   . ASP A 1 293 ? 20.577  3.963   -42.849 1.00 82.98  ? 901  ASP A O   1 
ATOM   2148 C CB  . ASP A 1 293 ? 18.693  2.715   -45.299 1.00 88.40  ? 901  ASP A CB  1 
ATOM   2149 C CG  . ASP A 1 293 ? 18.827  1.803   -46.513 1.00 98.48  ? 901  ASP A CG  1 
ATOM   2150 O OD1 . ASP A 1 293 ? 19.434  0.704   -46.378 1.00 100.01 ? 901  ASP A OD1 1 
ATOM   2151 O OD2 . ASP A 1 293 ? 18.330  2.187   -47.611 1.00 102.99 ? 901  ASP A OD2 1 
ATOM   2152 N N   . ILE A 1 294 ? 18.426  3.551   -42.199 1.00 80.98  ? 902  ILE A N   1 
ATOM   2153 C CA  . ILE A 1 294 ? 18.397  4.527   -41.099 1.00 79.36  ? 902  ILE A CA  1 
ATOM   2154 C C   . ILE A 1 294 ? 19.489  4.200   -40.100 1.00 78.19  ? 902  ILE A C   1 
ATOM   2155 O O   . ILE A 1 294 ? 20.311  5.071   -39.843 1.00 78.67  ? 902  ILE A O   1 
ATOM   2156 C CB  . ILE A 1 294 ? 17.011  4.726   -40.418 1.00 79.25  ? 902  ILE A CB  1 
ATOM   2157 C CG1 . ILE A 1 294 ? 15.983  5.327   -41.410 1.00 79.44  ? 902  ILE A CG1 1 
ATOM   2158 C CG2 . ILE A 1 294 ? 17.143  5.617   -39.157 1.00 79.40  ? 902  ILE A CG2 1 
ATOM   2159 C CD1 . ILE A 1 294 ? 14.582  5.645   -40.829 1.00 80.11  ? 902  ILE A CD1 1 
ATOM   2160 N N   . MET A 1 295 ? 19.594  2.932   -39.636 1.00 76.84  ? 903  MET A N   1 
ATOM   2161 C CA  . MET A 1 295 ? 20.667  2.512   -38.722 1.00 76.77  ? 903  MET A CA  1 
ATOM   2162 C C   . MET A 1 295 ? 22.040  2.848   -39.301 1.00 78.15  ? 903  MET A C   1 
ATOM   2163 O O   . MET A 1 295 ? 22.795  3.597   -38.681 1.00 78.31  ? 903  MET A O   1 
ATOM   2164 C CB  . MET A 1 295 ? 20.613  1.005   -38.413 1.00 76.03  ? 903  MET A CB  1 
ATOM   2165 C CG  . MET A 1 295 ? 19.357  0.567   -37.763 1.00 76.02  ? 903  MET A CG  1 
ATOM   2166 S SD  . MET A 1 295 ? 19.331  -1.229  -37.536 1.00 71.54  ? 903  MET A SD  1 
ATOM   2167 C CE  . MET A 1 295 ? 17.642  -1.540  -37.866 1.00 68.64  ? 903  MET A CE  1 
ATOM   2168 N N   . LYS A 1 296 ? 22.316  2.375   -40.537 1.00 79.06  ? 904  LYS A N   1 
ATOM   2169 C CA  . LYS A 1 296 ? 23.552  2.618   -41.261 1.00 80.18  ? 904  LYS A CA  1 
ATOM   2170 C C   . LYS A 1 296 ? 23.917  4.111   -41.293 1.00 81.52  ? 904  LYS A C   1 
ATOM   2171 O O   . LYS A 1 296 ? 25.064  4.439   -41.025 1.00 82.16  ? 904  LYS A O   1 
ATOM   2172 C CB  . LYS A 1 296 ? 23.437  2.061   -42.680 1.00 82.07  ? 904  LYS A CB  1 
ATOM   2173 C CG  . LYS A 1 296 ? 23.535  0.537   -42.778 1.00 85.58  ? 904  LYS A CG  1 
ATOM   2174 C CD  . LYS A 1 296 ? 23.385  0.045   -44.223 1.00 89.19  ? 904  LYS A CD  1 
ATOM   2175 C CE  . LYS A 1 296 ? 24.539  0.521   -45.088 1.00 93.91  ? 904  LYS A CE  1 
ATOM   2176 N NZ  . LYS A 1 296 ? 24.426  0.085   -46.519 1.00 96.49  ? 904  LYS A NZ  1 
ATOM   2177 N N   . THR A 1 297 ? 22.946  5.015   -41.530 1.00 81.89  ? 905  THR A N   1 
ATOM   2178 C CA  . THR A 1 297 ? 23.240  6.457   -41.538 1.00 82.82  ? 905  THR A CA  1 
ATOM   2179 C C   . THR A 1 297 ? 23.531  7.017   -40.134 1.00 83.03  ? 905  THR A C   1 
ATOM   2180 O O   . THR A 1 297 ? 24.328  7.945   -40.014 1.00 83.09  ? 905  THR A O   1 
ATOM   2181 C CB  . THR A 1 297 ? 22.174  7.258   -42.273 1.00 84.43  ? 905  THR A CB  1 
ATOM   2182 O OG1 . THR A 1 297 ? 20.889  6.973   -41.711 1.00 86.07  ? 905  THR A OG1 1 
ATOM   2183 C CG2 . THR A 1 297 ? 22.186  6.986   -43.767 1.00 84.44  ? 905  THR A CG2 1 
ATOM   2184 N N   . CYS A 1 298 ? 22.908  6.464   -39.077 1.00 83.07  ? 906  CYS A N   1 
ATOM   2185 C CA  . CYS A 1 298 ? 23.203  6.888   -37.688 1.00 82.93  ? 906  CYS A CA  1 
ATOM   2186 C C   . CYS A 1 298 ? 24.634  6.476   -37.300 1.00 83.44  ? 906  CYS A C   1 
ATOM   2187 O O   . CYS A 1 298 ? 25.249  7.112   -36.445 1.00 82.99  ? 906  CYS A O   1 
ATOM   2188 C CB  . CYS A 1 298 ? 22.200  6.288   -36.707 1.00 82.33  ? 906  CYS A CB  1 
ATOM   2189 S SG  . CYS A 1 298 ? 20.483  6.783   -36.983 1.00 82.81  ? 906  CYS A SG  1 
ATOM   2190 N N   . TRP A 1 299 ? 25.133  5.373   -37.907 1.00 83.87  ? 907  TRP A N   1 
ATOM   2191 C CA  . TRP A 1 299 ? 26.433  4.791   -37.639 1.00 84.66  ? 907  TRP A CA  1 
ATOM   2192 C C   . TRP A 1 299 ? 27.558  5.317   -38.528 1.00 85.45  ? 907  TRP A C   1 
ATOM   2193 O O   . TRP A 1 299 ? 28.670  4.817   -38.451 1.00 85.25  ? 907  TRP A O   1 
ATOM   2194 C CB  . TRP A 1 299 ? 26.352  3.254   -37.699 1.00 84.53  ? 907  TRP A CB  1 
ATOM   2195 C CG  . TRP A 1 299 ? 25.382  2.635   -36.733 1.00 85.01  ? 907  TRP A CG  1 
ATOM   2196 C CD1 . TRP A 1 299 ? 24.915  3.172   -35.566 1.00 85.91  ? 907  TRP A CD1 1 
ATOM   2197 C CD2 . TRP A 1 299 ? 24.811  1.324   -36.826 1.00 85.25  ? 907  TRP A CD2 1 
ATOM   2198 N NE1 . TRP A 1 299 ? 24.055  2.295   -34.954 1.00 86.25  ? 907  TRP A NE1 1 
ATOM   2199 C CE2 . TRP A 1 299 ? 23.985  1.145   -35.700 1.00 86.01  ? 907  TRP A CE2 1 
ATOM   2200 C CE3 . TRP A 1 299 ? 24.907  0.287   -37.761 1.00 85.75  ? 907  TRP A CE3 1 
ATOM   2201 C CZ2 . TRP A 1 299 ? 23.263  -0.030  -35.485 1.00 86.52  ? 907  TRP A CZ2 1 
ATOM   2202 C CZ3 . TRP A 1 299 ? 24.202  -0.874  -37.536 1.00 86.53  ? 907  TRP A CZ3 1 
ATOM   2203 C CH2 . TRP A 1 299 ? 23.377  -1.016  -36.419 1.00 86.61  ? 907  TRP A CH2 1 
ATOM   2204 N N   . ASP A 1 300 ? 27.312  6.358   -39.328 1.00 86.31  ? 908  ASP A N   1 
ATOM   2205 C CA  . ASP A 1 300 ? 28.355  6.978   -40.153 1.00 87.65  ? 908  ASP A CA  1 
ATOM   2206 C C   . ASP A 1 300 ? 29.489  7.489   -39.227 1.00 88.80  ? 908  ASP A C   1 
ATOM   2207 O O   . ASP A 1 300 ? 29.201  8.090   -38.191 1.00 88.57  ? 908  ASP A O   1 
ATOM   2208 C CB  . ASP A 1 300 ? 27.752  8.164   -40.928 1.00 89.57  ? 908  ASP A CB  1 
ATOM   2209 C CG  . ASP A 1 300 ? 28.463  8.525   -42.217 1.00 93.87  ? 908  ASP A CG  1 
ATOM   2210 O OD1 . ASP A 1 300 ? 29.704  8.722   -42.181 1.00 93.88  ? 908  ASP A OD1 1 
ATOM   2211 O OD2 . ASP A 1 300 ? 27.779  8.629   -43.258 1.00 96.27  ? 908  ASP A OD2 1 
ATOM   2212 N N   . ALA A 1 301 ? 30.754  7.174   -39.561 1.00 89.83  ? 909  ALA A N   1 
ATOM   2213 C CA  . ALA A 1 301 ? 31.921  7.583   -38.767 1.00 90.72  ? 909  ALA A CA  1 
ATOM   2214 C C   . ALA A 1 301 ? 32.009  9.110   -38.631 1.00 91.04  ? 909  ALA A C   1 
ATOM   2215 O O   . ALA A 1 301 ? 32.385  9.603   -37.572 1.00 91.24  ? 909  ALA A O   1 
ATOM   2216 C CB  . ALA A 1 301 ? 33.195  7.029   -39.388 1.00 91.02  ? 909  ALA A CB  1 
ATOM   2217 N N   . ASP A 1 302 ? 31.628  9.851   -39.684 1.00 91.10  ? 910  ASP A N   1 
ATOM   2218 C CA  . ASP A 1 302 ? 31.612  11.309  -39.642 1.00 92.21  ? 910  ASP A CA  1 
ATOM   2219 C C   . ASP A 1 302 ? 30.248  11.767  -39.108 1.00 92.48  ? 910  ASP A C   1 
ATOM   2220 O O   . ASP A 1 302 ? 29.209  11.509  -39.720 1.00 92.54  ? 910  ASP A O   1 
ATOM   2221 C CB  . ASP A 1 302 ? 31.927  11.901  -41.031 1.00 94.68  ? 910  ASP A CB  1 
ATOM   2222 C CG  . ASP A 1 302 ? 31.821  13.416  -41.178 1.00 100.24 ? 910  ASP A CG  1 
ATOM   2223 O OD1 . ASP A 1 302 ? 31.814  14.127  -40.136 1.00 100.31 ? 910  ASP A OD1 1 
ATOM   2224 O OD2 . ASP A 1 302 ? 31.764  13.896  -42.340 1.00 103.51 ? 910  ASP A OD2 1 
ATOM   2225 N N   . PRO A 1 303 ? 30.249  12.431  -37.941 1.00 92.44  ? 911  PRO A N   1 
ATOM   2226 C CA  . PRO A 1 303 ? 28.984  12.854  -37.332 1.00 92.30  ? 911  PRO A CA  1 
ATOM   2227 C C   . PRO A 1 303 ? 28.148  13.768  -38.192 1.00 92.68  ? 911  PRO A C   1 
ATOM   2228 O O   . PRO A 1 303 ? 26.924  13.685  -38.153 1.00 92.84  ? 911  PRO A O   1 
ATOM   2229 C CB  . PRO A 1 303 ? 29.428  13.579  -36.062 1.00 93.10  ? 911  PRO A CB  1 
ATOM   2230 C CG  . PRO A 1 303 ? 30.778  13.068  -35.774 1.00 93.81  ? 911  PRO A CG  1 
ATOM   2231 C CD  . PRO A 1 303 ? 31.402  12.779  -37.089 1.00 92.22  ? 911  PRO A CD  1 
ATOM   2232 N N   . LEU A 1 304 ? 28.802  14.647  -38.961 1.00 92.76  ? 912  LEU A N   1 
ATOM   2233 C CA  . LEU A 1 304 ? 28.112  15.603  -39.819 1.00 93.12  ? 912  LEU A CA  1 
ATOM   2234 C C   . LEU A 1 304 ? 27.308  14.950  -40.956 1.00 92.53  ? 912  LEU A C   1 
ATOM   2235 O O   . LEU A 1 304 ? 26.367  15.566  -41.453 1.00 93.36  ? 912  LEU A O   1 
ATOM   2236 C CB  . LEU A 1 304 ? 29.093  16.658  -40.355 1.00 93.83  ? 912  LEU A CB  1 
ATOM   2237 C CG  . LEU A 1 304 ? 29.787  17.528  -39.291 1.00 95.68  ? 912  LEU A CG  1 
ATOM   2238 C CD1 . LEU A 1 304 ? 30.655  18.588  -39.945 1.00 96.08  ? 912  LEU A CD1 1 
ATOM   2239 C CD2 . LEU A 1 304 ? 28.766  18.199  -38.343 1.00 96.55  ? 912  LEU A CD2 1 
ATOM   2240 N N   . LYS A 1 305 ? 27.621  13.695  -41.311 1.00 90.99  ? 913  LYS A N   1 
ATOM   2241 C CA  . LYS A 1 305 ? 26.894  12.945  -42.338 1.00 89.80  ? 913  LYS A CA  1 
ATOM   2242 C C   . LYS A 1 305 ? 25.729  12.087  -41.778 1.00 87.98  ? 913  LYS A C   1 
ATOM   2243 O O   . LYS A 1 305 ? 25.068  11.399  -42.557 1.00 88.36  ? 913  LYS A O   1 
ATOM   2244 C CB  . LYS A 1 305 ? 27.854  12.042  -43.125 1.00 91.34  ? 913  LYS A CB  1 
ATOM   2245 C CG  . LYS A 1 305 ? 28.898  12.790  -43.931 1.00 95.71  ? 913  LYS A CG  1 
ATOM   2246 C CD  . LYS A 1 305 ? 29.846  11.791  -44.581 1.00 101.16 ? 913  LYS A CD  1 
ATOM   2247 C CE  . LYS A 1 305 ? 30.713  12.399  -45.650 1.00 105.20 ? 913  LYS A CE  1 
ATOM   2248 N NZ  . LYS A 1 305 ? 31.297  11.350  -46.516 1.00 107.58 ? 913  LYS A NZ  1 
ATOM   2249 N N   . ARG A 1 306 ? 25.506  12.084  -40.443 1.00 85.72  ? 914  ARG A N   1 
ATOM   2250 C CA  . ARG A 1 306 ? 24.416  11.311  -39.818 1.00 83.71  ? 914  ARG A CA  1 
ATOM   2251 C C   . ARG A 1 306 ? 23.116  12.117  -39.859 1.00 82.81  ? 914  ARG A C   1 
ATOM   2252 O O   . ARG A 1 306 ? 23.165  13.351  -39.797 1.00 83.23  ? 914  ARG A O   1 
ATOM   2253 C CB  . ARG A 1 306 ? 24.743  10.998  -38.359 1.00 83.20  ? 914  ARG A CB  1 
ATOM   2254 C CG  . ARG A 1 306 ? 26.013  10.231  -38.152 1.00 83.73  ? 914  ARG A CG  1 
ATOM   2255 C CD  . ARG A 1 306 ? 26.336  10.187  -36.678 1.00 84.52  ? 914  ARG A CD  1 
ATOM   2256 N NE  . ARG A 1 306 ? 27.670  9.646   -36.446 1.00 85.50  ? 914  ARG A NE  1 
ATOM   2257 C CZ  . ARG A 1 306 ? 28.390  9.861   -35.352 1.00 86.89  ? 914  ARG A CZ  1 
ATOM   2258 N NH1 . ARG A 1 306 ? 27.910  10.614  -34.370 1.00 84.38  ? 914  ARG A NH1 1 
ATOM   2259 N NH2 . ARG A 1 306 ? 29.603  9.335   -35.236 1.00 88.03  ? 914  ARG A NH2 1 
ATOM   2260 N N   . PRO A 1 307 ? 21.938  11.468  -39.926 1.00 81.46  ? 915  PRO A N   1 
ATOM   2261 C CA  . PRO A 1 307 ? 20.697  12.246  -39.967 1.00 80.95  ? 915  PRO A CA  1 
ATOM   2262 C C   . PRO A 1 307 ? 20.398  12.900  -38.629 1.00 81.27  ? 915  PRO A C   1 
ATOM   2263 O O   . PRO A 1 307 ? 20.845  12.428  -37.581 1.00 81.88  ? 915  PRO A O   1 
ATOM   2264 C CB  . PRO A 1 307 ? 19.636  11.197  -40.313 1.00 81.33  ? 915  PRO A CB  1 
ATOM   2265 C CG  . PRO A 1 307 ? 20.181  9.941   -39.801 1.00 81.57  ? 915  PRO A CG  1 
ATOM   2266 C CD  . PRO A 1 307 ? 21.664  10.020  -39.987 1.00 80.36  ? 915  PRO A CD  1 
ATOM   2267 N N   . THR A 1 308 ? 19.666  14.014  -38.665 1.00 80.26  ? 916  THR A N   1 
ATOM   2268 C CA  . THR A 1 308 ? 19.221  14.643  -37.440 1.00 79.27  ? 916  THR A CA  1 
ATOM   2269 C C   . THR A 1 308 ? 17.943  13.903  -37.035 1.00 77.61  ? 916  THR A C   1 
ATOM   2270 O O   . THR A 1 308 ? 17.328  13.228  -37.877 1.00 77.80  ? 916  THR A O   1 
ATOM   2271 C CB  . THR A 1 308 ? 18.997  16.138  -37.652 1.00 81.11  ? 916  THR A CB  1 
ATOM   2272 O OG1 . THR A 1 308 ? 17.841  16.343  -38.474 1.00 82.14  ? 916  THR A OG1 1 
ATOM   2273 C CG2 . THR A 1 308 ? 20.222  16.824  -38.235 1.00 81.65  ? 916  THR A CG2 1 
ATOM   2274 N N   . PHE A 1 309 ? 17.504  14.063  -35.774 1.00 75.64  ? 917  PHE A N   1 
ATOM   2275 C CA  . PHE A 1 309 ? 16.263  13.432  -35.329 1.00 74.50  ? 917  PHE A CA  1 
ATOM   2276 C C   . PHE A 1 309 ? 15.067  13.965  -36.127 1.00 75.66  ? 917  PHE A C   1 
ATOM   2277 O O   . PHE A 1 309 ? 14.196  13.188  -36.496 1.00 75.32  ? 917  PHE A O   1 
ATOM   2278 C CB  . PHE A 1 309 ? 16.063  13.593  -33.806 1.00 72.62  ? 917  PHE A CB  1 
ATOM   2279 C CG  . PHE A 1 309 ? 16.887  12.622  -32.995 1.00 71.15  ? 917  PHE A CG  1 
ATOM   2280 C CD1 . PHE A 1 309 ? 16.767  11.257  -33.188 1.00 71.09  ? 917  PHE A CD1 1 
ATOM   2281 C CD2 . PHE A 1 309 ? 17.804  13.074  -32.066 1.00 70.80  ? 917  PHE A CD2 1 
ATOM   2282 C CE1 . PHE A 1 309 ? 17.542  10.369  -32.460 1.00 71.32  ? 917  PHE A CE1 1 
ATOM   2283 C CE2 . PHE A 1 309 ? 18.580  12.181  -31.342 1.00 70.98  ? 917  PHE A CE2 1 
ATOM   2284 C CZ  . PHE A 1 309 ? 18.450  10.835  -31.546 1.00 70.83  ? 917  PHE A CZ  1 
ATOM   2285 N N   . LYS A 1 310 ? 15.085  15.269  -36.474 1.00 76.89  ? 918  LYS A N   1 
ATOM   2286 C CA  . LYS A 1 310 ? 14.045  15.920  -37.264 1.00 78.54  ? 918  LYS A CA  1 
ATOM   2287 C C   . LYS A 1 310 ? 13.975  15.298  -38.666 1.00 79.45  ? 918  LYS A C   1 
ATOM   2288 O O   . LYS A 1 310 ? 12.881  15.121  -39.192 1.00 80.17  ? 918  LYS A O   1 
ATOM   2289 C CB  . LYS A 1 310 ? 14.249  17.458  -37.295 1.00 81.05  ? 918  LYS A CB  1 
ATOM   2290 C CG  . LYS A 1 310 ? 13.071  18.232  -37.862 1.00 87.21  ? 918  LYS A CG  1 
ATOM   2291 C CD  . LYS A 1 310 ? 12.992  19.663  -37.298 1.00 94.13  ? 918  LYS A CD  1 
ATOM   2292 C CE  . LYS A 1 310 ? 11.731  20.390  -37.723 1.00 99.29  ? 918  LYS A CE  1 
ATOM   2293 N NZ  . LYS A 1 310 ? 11.463  21.604  -36.896 1.00 102.30 ? 918  LYS A NZ  1 
ATOM   2294 N N   . GLN A 1 311 ? 15.120  14.920  -39.247 1.00 79.39  ? 919  GLN A N   1 
ATOM   2295 C CA  . GLN A 1 311 ? 15.131  14.231  -40.533 1.00 80.39  ? 919  GLN A CA  1 
ATOM   2296 C C   . GLN A 1 311 ? 14.672  12.768  -40.363 1.00 80.40  ? 919  GLN A C   1 
ATOM   2297 O O   . GLN A 1 311 ? 14.041  12.233  -41.275 1.00 81.12  ? 919  GLN A O   1 
ATOM   2298 C CB  . GLN A 1 311 ? 16.528  14.250  -41.171 1.00 82.75  ? 919  GLN A CB  1 
ATOM   2299 C CG  . GLN A 1 311 ? 17.033  15.639  -41.542 1.00 86.30  ? 919  GLN A CG  1 
ATOM   2300 C CD  . GLN A 1 311 ? 18.479  15.606  -41.990 1.00 91.01  ? 919  GLN A CD  1 
ATOM   2301 O OE1 . GLN A 1 311 ? 19.254  14.688  -41.665 1.00 92.39  ? 919  GLN A OE1 1 
ATOM   2302 N NE2 . GLN A 1 311 ? 18.878  16.614  -42.751 1.00 91.44  ? 919  GLN A NE2 1 
ATOM   2303 N N   . ILE A 1 312 ? 15.013  12.111  -39.234 1.00 79.49  ? 920  ILE A N   1 
ATOM   2304 C CA  . ILE A 1 312 ? 14.592  10.723  -38.958 1.00 79.37  ? 920  ILE A CA  1 
ATOM   2305 C C   . ILE A 1 312 ? 13.058  10.649  -38.853 1.00 79.96  ? 920  ILE A C   1 
ATOM   2306 O O   . ILE A 1 312 ? 12.445  9.746   -39.421 1.00 79.58  ? 920  ILE A O   1 
ATOM   2307 C CB  . ILE A 1 312 ? 15.279  10.118  -37.686 1.00 78.92  ? 920  ILE A CB  1 
ATOM   2308 C CG1 . ILE A 1 312 ? 16.792  9.929   -37.883 1.00 78.95  ? 920  ILE A CG1 1 
ATOM   2309 C CG2 . ILE A 1 312 ? 14.634  8.790   -37.275 1.00 78.94  ? 920  ILE A CG2 1 
ATOM   2310 C CD1 . ILE A 1 312 ? 17.535  9.944   -36.617 1.00 79.43  ? 920  ILE A CD1 1 
ATOM   2311 N N   . VAL A 1 313 ? 12.439  11.630  -38.172 1.00 80.71  ? 921  VAL A N   1 
ATOM   2312 C CA  . VAL A 1 313 ? 10.988  11.670  -37.994 1.00 82.06  ? 921  VAL A CA  1 
ATOM   2313 C C   . VAL A 1 313 ? 10.274  11.709  -39.353 1.00 84.49  ? 921  VAL A C   1 
ATOM   2314 O O   . VAL A 1 313 ? 9.309   10.969  -39.570 1.00 85.02  ? 921  VAL A O   1 
ATOM   2315 C CB  . VAL A 1 313 ? 10.529  12.827  -37.067 1.00 81.70  ? 921  VAL A CB  1 
ATOM   2316 C CG1 . VAL A 1 313 ? 9.012   12.939  -37.042 1.00 82.04  ? 921  VAL A CG1 1 
ATOM   2317 C CG2 . VAL A 1 313 ? 11.069  12.660  -35.662 1.00 81.38  ? 921  VAL A CG2 1 
ATOM   2318 N N   . GLN A 1 314 ? 10.787  12.520  -40.286 1.00 85.54  ? 922  GLN A N   1 
ATOM   2319 C CA  . GLN A 1 314 ? 10.197  12.618  -41.614 1.00 87.18  ? 922  GLN A CA  1 
ATOM   2320 C C   . GLN A 1 314 ? 10.341  11.299  -42.382 1.00 88.48  ? 922  GLN A C   1 
ATOM   2321 O O   . GLN A 1 314 ? 9.430   10.928  -43.119 1.00 88.60  ? 922  GLN A O   1 
ATOM   2322 C CB  . GLN A 1 314 ? 10.828  13.775  -42.383 1.00 89.64  ? 922  GLN A CB  1 
ATOM   2323 C CG  . GLN A 1 314 ? 10.587  15.123  -41.722 1.00 96.08  ? 922  GLN A CG  1 
ATOM   2324 C CD  . GLN A 1 314 ? 11.454  16.218  -42.317 1.00 104.05 ? 922  GLN A CD  1 
ATOM   2325 O OE1 . GLN A 1 314 ? 11.871  16.161  -43.501 1.00 106.26 ? 922  GLN A OE1 1 
ATOM   2326 N NE2 . GLN A 1 314 ? 11.743  17.242  -41.501 1.00 104.99 ? 922  GLN A NE2 1 
ATOM   2327 N N   . LEU A 1 315 ? 11.463  10.577  -42.186 1.00 89.21  ? 923  LEU A N   1 
ATOM   2328 C CA  . LEU A 1 315 ? 11.722  9.299   -42.845 1.00 90.33  ? 923  LEU A CA  1 
ATOM   2329 C C   . LEU A 1 315 ? 10.752  8.225   -42.379 1.00 92.14  ? 923  LEU A C   1 
ATOM   2330 O O   . LEU A 1 315 ? 10.193  7.524   -43.211 1.00 92.61  ? 923  LEU A O   1 
ATOM   2331 C CB  . LEU A 1 315 ? 13.162  8.840   -42.609 1.00 90.23  ? 923  LEU A CB  1 
ATOM   2332 C CG  . LEU A 1 315 ? 14.242  9.663   -43.276 1.00 91.29  ? 923  LEU A CG  1 
ATOM   2333 C CD1 . LEU A 1 315 ? 15.572  9.460   -42.587 1.00 91.93  ? 923  LEU A CD1 1 
ATOM   2334 C CD2 . LEU A 1 315 ? 14.353  9.328   -44.737 1.00 91.54  ? 923  LEU A CD2 1 
ATOM   2335 N N   . ILE A 1 316 ? 10.527  8.100   -41.066 1.00 93.27  ? 924  ILE A N   1 
ATOM   2336 C CA  . ILE A 1 316 ? 9.598   7.086   -40.546 1.00 94.67  ? 924  ILE A CA  1 
ATOM   2337 C C   . ILE A 1 316 ? 8.123   7.490   -40.799 1.00 97.08  ? 924  ILE A C   1 
ATOM   2338 O O   . ILE A 1 316 ? 7.269   6.622   -40.951 1.00 97.16  ? 924  ILE A O   1 
ATOM   2339 C CB  . ILE A 1 316 ? 9.889   6.705   -39.082 1.00 94.18  ? 924  ILE A CB  1 
ATOM   2340 C CG1 . ILE A 1 316 ? 11.385  6.445   -38.885 1.00 94.80  ? 924  ILE A CG1 1 
ATOM   2341 C CG2 . ILE A 1 316 ? 9.066   5.485   -38.675 1.00 94.32  ? 924  ILE A CG2 1 
ATOM   2342 C CD1 . ILE A 1 316 ? 11.796  6.335   -37.502 1.00 96.24  ? 924  ILE A CD1 1 
ATOM   2343 N N   . GLU A 1 317 ? 7.844   8.798   -40.933 1.00 98.83  ? 925  GLU A N   1 
ATOM   2344 C CA  . GLU A 1 317 ? 6.518   9.301   -41.290 1.00 100.98 ? 925  GLU A CA  1 
ATOM   2345 C C   . GLU A 1 317 ? 6.181   8.790   -42.715 1.00 102.87 ? 925  GLU A C   1 
ATOM   2346 O O   . GLU A 1 317 ? 5.060   8.354   -42.965 1.00 102.84 ? 925  GLU A O   1 
ATOM   2347 C CB  . GLU A 1 317 ? 6.523   10.840  -41.267 1.00 103.58 ? 925  GLU A CB  1 
ATOM   2348 C CG  . GLU A 1 317 ? 5.443   11.460  -40.401 1.00 109.46 ? 925  GLU A CG  1 
ATOM   2349 C CD  . GLU A 1 317 ? 5.810   12.787  -39.757 1.00 115.72 ? 925  GLU A CD  1 
ATOM   2350 O OE1 . GLU A 1 317 ? 5.048   13.243  -38.873 1.00 116.01 ? 925  GLU A OE1 1 
ATOM   2351 O OE2 . GLU A 1 317 ? 6.863   13.361  -40.117 1.00 118.25 ? 925  GLU A OE2 1 
ATOM   2352 N N   . LYS A 1 318 ? 7.178   8.804   -43.624 1.00 104.30 ? 926  LYS A N   1 
ATOM   2353 C CA  . LYS A 1 318 ? 7.039   8.314   -44.987 1.00 106.10 ? 926  LYS A CA  1 
ATOM   2354 C C   . LYS A 1 318 ? 6.838   6.801   -44.994 1.00 107.72 ? 926  LYS A C   1 
ATOM   2355 O O   . LYS A 1 318 ? 6.029   6.298   -45.759 1.00 108.02 ? 926  LYS A O   1 
ATOM   2356 C CB  . LYS A 1 318 ? 8.262   8.694   -45.828 1.00 108.53 ? 926  LYS A CB  1 
ATOM   2357 C CG  . LYS A 1 318 ? 7.942   8.685   -47.316 1.00 114.57 ? 926  LYS A CG  1 
ATOM   2358 C CD  . LYS A 1 318 ? 9.149   8.917   -48.212 1.00 120.43 ? 926  LYS A CD  1 
ATOM   2359 C CE  . LYS A 1 318 ? 8.747   8.788   -49.661 1.00 125.52 ? 926  LYS A CE  1 
ATOM   2360 N NZ  . LYS A 1 318 ? 9.773   9.335   -50.593 1.00 128.89 ? 926  LYS A NZ  1 
ATOM   2361 N N   . GLN A 1 319 ? 7.538   6.081   -44.122 1.00 108.90 ? 927  GLN A N   1 
ATOM   2362 C CA  . GLN A 1 319 ? 7.419   4.630   -44.016 1.00 110.56 ? 927  GLN A CA  1 
ATOM   2363 C C   . GLN A 1 319 ? 6.097   4.162   -43.425 1.00 112.35 ? 927  GLN A C   1 
ATOM   2364 O O   . GLN A 1 319 ? 5.662   3.044   -43.708 1.00 112.70 ? 927  GLN A O   1 
ATOM   2365 C CB  . GLN A 1 319 ? 8.589   4.053   -43.225 1.00 111.78 ? 927  GLN A CB  1 
ATOM   2366 C CG  . GLN A 1 319 ? 9.905   4.275   -43.925 1.00 114.98 ? 927  GLN A CG  1 
ATOM   2367 C CD  . GLN A 1 319 ? 10.957  3.377   -43.366 1.00 119.82 ? 927  GLN A CD  1 
ATOM   2368 O OE1 . GLN A 1 319 ? 10.772  2.158   -43.241 1.00 121.22 ? 927  GLN A OE1 1 
ATOM   2369 N NE2 . GLN A 1 319 ? 12.093  3.961   -43.026 1.00 120.94 ? 927  GLN A NE2 1 
ATOM   2370 N N   . ILE A 1 320 ? 5.468   4.992   -42.597 1.00 113.37 ? 928  ILE A N   1 
ATOM   2371 C CA  . ILE A 1 320 ? 4.185   4.646   -42.010 1.00 115.13 ? 928  ILE A CA  1 
ATOM   2372 C C   . ILE A 1 320 ? 3.072   4.861   -43.053 1.00 117.33 ? 928  ILE A C   1 
ATOM   2373 O O   . ILE A 1 320 ? 2.169   4.032   -43.158 1.00 117.56 ? 928  ILE A O   1 
ATOM   2374 C CB  . ILE A 1 320 ? 3.973   5.403   -40.675 1.00 115.48 ? 928  ILE A CB  1 
ATOM   2375 C CG1 . ILE A 1 320 ? 4.899   4.829   -39.578 1.00 116.01 ? 928  ILE A CG1 1 
ATOM   2376 C CG2 . ILE A 1 320 ? 2.508   5.369   -40.234 1.00 116.06 ? 928  ILE A CG2 1 
ATOM   2377 C CD1 . ILE A 1 320 ? 4.970   5.621   -38.328 1.00 116.79 ? 928  ILE A CD1 1 
ATOM   2378 N N   . SER A 1 321 ? 3.173   5.933   -43.871 1.00 118.70 ? 929  SER A N   1 
ATOM   2379 C CA  . SER A 1 321 ? 2.199   6.215   -44.935 1.00 120.38 ? 929  SER A CA  1 
ATOM   2380 C C   . SER A 1 321 ? 2.324   5.199   -46.072 1.00 122.42 ? 929  SER A C   1 
ATOM   2381 O O   . SER A 1 321 ? 1.316   4.789   -46.648 1.00 122.78 ? 929  SER A O   1 
ATOM   2382 C CB  . SER A 1 321 ? 2.352   7.642   -45.457 1.00 121.22 ? 929  SER A CB  1 
ATOM   2383 O OG  . SER A 1 321 ? 3.614   7.852   -46.068 1.00 122.90 ? 929  SER A OG  1 
ATOM   2384 N N   . GLU A 1 322 ? 3.555   4.779   -46.372 1.00 123.69 ? 930  GLU A N   1 
ATOM   2385 C CA  . GLU A 1 322 ? 3.748   3.726   -47.404 1.00 125.49 ? 930  GLU A CA  1 
ATOM   2386 C C   . GLU A 1 322 ? 3.036   2.457   -46.927 1.00 126.98 ? 930  GLU A C   1 
ATOM   2387 O O   . GLU A 1 322 ? 2.371   1.808   -47.756 1.00 127.19 ? 930  GLU A O   1 
ATOM   2388 C CB  . GLU A 1 322 ? 5.237   3.471   -47.640 1.00 128.13 ? 930  GLU A CB  1 
ATOM   2389 C CG  . GLU A 1 322 ? 5.829   4.336   -48.736 1.00 133.02 ? 930  GLU A CG  1 
ATOM   2390 C CD  . GLU A 1 322 ? 7.297   4.677   -48.553 1.00 138.69 ? 930  GLU A CD  1 
ATOM   2391 O OE1 . GLU A 1 322 ? 7.881   4.247   -47.539 1.00 139.76 ? 930  GLU A OE1 1 
ATOM   2392 O OE2 . GLU A 1 322 ? 7.854   5.371   -49.426 1.00 140.22 ? 930  GLU A OE2 1 
ATOM   2393 N N   . SER A 1 323 ? 3.169   2.128   -45.639 1.00 127.86 ? 931  SER A N   1 
ATOM   2394 C CA  . SER A 1 323 ? 2.490   0.935   -45.068 1.00 129.15 ? 931  SER A CA  1 
ATOM   2395 C C   . SER A 1 323 ? 0.969   1.106   -45.142 1.00 130.03 ? 931  SER A C   1 
ATOM   2396 O O   . SER A 1 323 ? 0.280   0.111   -45.441 1.00 130.19 ? 931  SER A O   1 
ATOM   2397 C CB  . SER A 1 323 ? 2.950   0.671   -43.657 1.00 130.86 ? 931  SER A CB  1 
ATOM   2398 O OG  . SER A 1 323 ? 1.994   1.133   -42.714 1.00 133.58 ? 931  SER A OG  1 
ATOM   2399 N N   . THR A 1 324 ? 0.469   2.316   -44.874 1.00 130.30 ? 932  THR A N   1 
ATOM   2400 C CA  . THR A 1 324 ? -0.998  2.569   -44.883 1.00 131.08 ? 932  THR A CA  1 
ATOM   2401 C C   . THR A 1 324 ? -1.406  3.185   -46.225 1.00 131.41 ? 932  THR A C   1 
ATOM   2402 O O   . THR A 1 324 ? -0.986  2.628   -47.259 1.00 131.50 ? 932  THR A O   1 
ATOM   2403 C CB  . THR A 1 324 ? -1.411  3.466   -43.710 1.00 132.88 ? 932  THR A CB  1 
ATOM   2404 O OG1 . THR A 1 324 ? -0.674  4.685   -43.802 1.00 134.17 ? 932  THR A OG1 1 
ATOM   2405 C CG2 . THR A 1 324 ? -1.171  2.822   -42.361 1.00 133.23 ? 932  THR A CG2 1 
HETATM 2406 C C1  . K3R B 2 .   ? 16.931  13.627  -20.652 1.00 48.42  ? 1001 K3R A C1  1 
HETATM 2407 C C3  . K3R B 2 .   ? 15.615  12.517  -18.839 1.00 48.95  ? 1001 K3R A C3  1 
HETATM 2408 C C4  . K3R B 2 .   ? 14.385  11.928  -18.690 1.00 48.75  ? 1001 K3R A C4  1 
HETATM 2409 C C5  . K3R B 2 .   ? 13.774  11.987  -19.969 1.00 49.02  ? 1001 K3R A C5  1 
HETATM 2410 C C7  . K3R B 2 .   ? 13.814  11.400  -17.403 1.00 48.26  ? 1001 K3R A C7  1 
HETATM 2411 C C8  . K3R B 2 .   ? 14.675  11.026  -16.361 1.00 47.43  ? 1001 K3R A C8  1 
HETATM 2412 C C11 . K3R B 2 .   ? 12.257  10.004  -13.641 1.00 49.69  ? 1001 K3R A C11 1 
HETATM 2413 C C15 . K3R B 2 .   ? 10.019  5.652   -14.174 1.00 54.59  ? 1001 K3R A C15 1 
HETATM 2414 C C17 . K3R B 2 .   ? 12.334  5.816   -14.079 1.00 53.37  ? 1001 K3R A C17 1 
HETATM 2415 C C19 . K3R B 2 .   ? 8.812   4.817   -14.319 1.00 56.30  ? 1001 K3R A C19 1 
HETATM 2416 C C23 . K3R B 2 .   ? 6.997   1.785   -14.368 1.00 58.85  ? 1001 K3R A C23 1 
HETATM 2417 C C24 . K3R B 2 .   ? 7.936   0.766   -14.249 1.00 60.12  ? 1001 K3R A C24 1 
HETATM 2418 O O25 . K3R B 2 .   ? 7.563   -0.554  -14.206 1.00 62.97  ? 1001 K3R A O25 1 
HETATM 2419 C C27 . K3R B 2 .   ? 6.035   -2.343  -14.861 1.00 68.57  ? 1001 K3R A C27 1 
HETATM 2420 C C30 . K3R B 2 .   ? 5.241   -5.291  -14.827 1.00 74.75  ? 1001 K3R A C30 1 
HETATM 2421 C C31 . K3R B 2 .   ? 5.475   -6.828  -14.907 1.00 75.10  ? 1001 K3R A C31 1 
HETATM 2422 C C32 . K3R B 2 .   ? 6.713   -7.015  -13.979 1.00 75.20  ? 1001 K3R A C32 1 
HETATM 2423 C C33 . K3R B 2 .   ? 7.531   -5.716  -14.200 1.00 74.83  ? 1001 K3R A C33 1 
HETATM 2424 C C34 . K3R B 2 .   ? 9.302   1.111   -14.148 1.00 58.65  ? 1001 K3R A C34 1 
HETATM 2425 C C35 . K3R B 2 .   ? 9.668   2.420   -14.156 1.00 58.06  ? 1001 K3R A C35 1 
HETATM 2426 C C37 . K3R B 2 .   ? 11.897  10.820  -16.021 1.00 48.24  ? 1001 K3R A C37 1 
HETATM 2427 C C38 . K3R B 2 .   ? 12.414  11.317  -17.218 1.00 48.23  ? 1001 K3R A C38 1 
HETATM 2428 N N2  . K3R B 2 .   ? 15.761  12.939  -20.118 1.00 48.72  ? 1001 K3R A N2  1 
HETATM 2429 N N6  . K3R B 2 .   ? 14.598  12.587  -20.818 1.00 48.96  ? 1001 K3R A N6  1 
HETATM 2430 C C9  . K3R B 2 .   ? 14.152  10.560  -15.170 1.00 47.47  ? 1001 K3R A C9  1 
HETATM 2431 C C10 . K3R B 2 .   ? 12.773  10.454  -14.995 1.00 48.38  ? 1001 K3R A C10 1 
HETATM 2432 N N12 . K3R B 2 .   ? 11.037  9.172   -13.694 1.00 51.46  ? 1001 K3R A N12 1 
HETATM 2433 C C13 . K3R B 2 .   ? 11.088  7.780   -13.844 1.00 51.91  ? 1001 K3R A C13 1 
HETATM 2434 C C14 . K3R B 2 .   ? 9.905   7.049   -13.979 1.00 52.87  ? 1001 K3R A C14 1 
HETATM 2435 N N16 . K3R B 2 .   ? 11.242  5.071   -14.183 1.00 54.12  ? 1001 K3R A N16 1 
HETATM 2436 N N18 . K3R B 2 .   ? 12.266  7.140   -13.905 1.00 52.14  ? 1001 K3R A N18 1 
HETATM 2437 C C20 . K3R B 2 .   ? 7.520   5.299   -14.453 1.00 56.63  ? 1001 K3R A C20 1 
HETATM 2438 N N21 . K3R B 2 .   ? 6.693   4.257   -14.483 1.00 57.04  ? 1001 K3R A N21 1 
HETATM 2439 C C22 . K3R B 2 .   ? 7.396   3.126   -14.374 1.00 57.64  ? 1001 K3R A C22 1 
HETATM 2440 C C26 . K3R B 2 .   ? 6.183   -0.951  -14.251 1.00 65.70  ? 1001 K3R A C26 1 
HETATM 2441 C C28 . K3R B 2 .   ? 6.654   -3.434  -13.991 1.00 71.35  ? 1001 K3R A C28 1 
HETATM 2442 N N29 . K3R B 2 .   ? 6.607   -4.702  -14.759 1.00 73.98  ? 1001 K3R A N29 1 
HETATM 2443 N N36 . K3R B 2 .   ? 8.734   3.424   -14.264 1.00 57.31  ? 1001 K3R A N36 1 
HETATM 2444 O O   . HOH C 3 .   ? 28.208  -1.766  -23.518 1.00 61.05  ? 1101 HOH A O   1 
HETATM 2445 O O   . HOH C 3 .   ? 14.296  24.499  -14.824 1.00 56.12  ? 1102 HOH A O   1 
HETATM 2446 O O   . HOH C 3 .   ? 25.403  -7.619  -21.792 1.00 64.83  ? 1103 HOH A O   1 
HETATM 2447 O O   . HOH C 3 .   ? 19.420  -3.070  -15.650 1.00 71.31  ? 1104 HOH A O   1 
HETATM 2448 O O   . HOH C 3 .   ? 14.609  18.541  -0.188  1.00 65.25  ? 1105 HOH A O   1 
HETATM 2449 O O   . HOH C 3 .   ? 15.502  11.715  -2.384  1.00 65.23  ? 1106 HOH A O   1 
HETATM 2450 O O   . HOH C 3 .   ? 18.933  -1.323  -23.680 1.00 54.19  ? 1107 HOH A O   1 
HETATM 2451 O O   . HOH C 3 .   ? 28.143  1.288   -31.032 1.00 64.50  ? 1108 HOH A O   1 
HETATM 2452 O O   . HOH C 3 .   ? 14.783  7.580   -13.039 1.00 51.10  ? 1109 HOH A O   1 
HETATM 2453 O O   . HOH C 3 .   ? 19.577  -4.849  -25.978 1.00 52.43  ? 1110 HOH A O   1 
HETATM 2454 O O   . HOH C 3 .   ? 0.876   8.703   -14.197 1.00 52.90  ? 1111 HOH A O   1 
HETATM 2455 O O   . HOH C 3 .   ? 1.867   14.896  -23.120 1.00 63.57  ? 1112 HOH A O   1 
HETATM 2456 O O   . HOH C 3 .   ? 23.261  4.444   -24.312 1.00 52.99  ? 1113 HOH A O   1 
HETATM 2457 O O   . HOH C 3 .   ? 21.690  4.078   -15.088 1.00 54.89  ? 1114 HOH A O   1 
HETATM 2458 O O   . HOH C 3 .   ? 22.464  8.514   -26.061 1.00 51.63  ? 1115 HOH A O   1 
HETATM 2459 O O   . HOH C 3 .   ? 21.195  9.657   -15.176 1.00 53.85  ? 1116 HOH A O   1 
HETATM 2460 O O   . HOH C 3 .   ? 24.710  20.706  -18.942 1.00 60.69  ? 1117 HOH A O   1 
HETATM 2461 O O   . HOH C 3 .   ? 14.605  9.959   -0.216  1.00 61.79  ? 1118 HOH A O   1 
HETATM 2462 O O   . HOH C 3 .   ? 20.643  -2.967  -22.028 1.00 45.01  ? 1119 HOH A O   1 
HETATM 2463 O O   . HOH C 3 .   ? 14.540  18.789  -33.387 1.00 63.46  ? 1120 HOH A O   1 
HETATM 2464 O O   . HOH C 3 .   ? 8.665   15.941  -31.683 1.00 77.13  ? 1121 HOH A O   1 
HETATM 2465 O O   . HOH C 3 .   ? 9.740   -3.566  -12.078 1.00 74.18  ? 1122 HOH A O   1 
HETATM 2466 O O   . HOH C 3 .   ? 15.284  -15.846 -27.437 1.00 62.00  ? 1123 HOH A O   1 
HETATM 2467 O O   . HOH C 3 .   ? 16.623  17.188  -34.812 1.00 72.51  ? 1124 HOH A O   1 
HETATM 2468 O O   . HOH C 3 .   ? 21.319  0.692   -48.682 1.00 84.32  ? 1125 HOH A O   1 
HETATM 2469 O O   . HOH C 3 .   ? 8.080   -7.080  -19.245 1.00 68.07  ? 1126 HOH A O   1 
HETATM 2470 O O   . HOH C 3 .   ? 21.080  -5.109  -23.904 1.00 56.50  ? 1127 HOH A O   1 
HETATM 2471 O O   . HOH C 3 .   ? 8.837   16.923  -18.235 1.00 60.13  ? 1128 HOH A O   1 
HETATM 2472 O O   . HOH C 3 .   ? 20.056  -3.450  -19.408 1.00 58.94  ? 1129 HOH A O   1 
HETATM 2473 O O   . HOH C 3 .   ? 19.743  9.607   -11.579 1.00 69.14  ? 1130 HOH A O   1 
HETATM 2474 O O   . HOH C 3 .   ? 25.060  18.466  -16.412 1.00 75.75  ? 1131 HOH A O   1 
HETATM 2475 O O   . HOH C 3 .   ? 9.138   1.056   -50.403 1.00 73.49  ? 1132 HOH A O   1 
HETATM 2476 O O   . HOH C 3 .   ? 19.114  26.498  -24.240 1.00 74.06  ? 1133 HOH A O   1 
HETATM 2477 O O   . HOH C 3 .   ? 8.920   -3.582  -3.342  1.00 66.32  ? 1134 HOH A O   1 
HETATM 2478 O O   . HOH C 3 .   ? -2.565  13.109  4.822   1.00 78.27  ? 1135 HOH A O   1 
HETATM 2479 O O   . HOH C 3 .   ? 25.528  -8.517  -36.135 1.00 87.38  ? 1136 HOH A O   1 
HETATM 2480 O O   . HOH C 3 .   ? 0.783   2.860   -5.358  1.00 75.13  ? 1137 HOH A O   1 
HETATM 2481 O O   . HOH C 3 .   ? -5.919  22.053  -0.835  1.00 73.69  ? 1138 HOH A O   1 
HETATM 2482 O O   . HOH C 3 .   ? 7.999   -9.243  -35.617 1.00 75.21  ? 1139 HOH A O   1 
HETATM 2483 O O   . HOH C 3 .   ? 9.887   18.790  -31.483 1.00 79.95  ? 1140 HOH A 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   . GLU A 4   ? 0.8645 1.0060 1.0919 -0.0234 -0.0815 0.0067  554 GLU A N   
2    C CA  . GLU A 4   ? 0.8784 0.9914 1.1054 -0.0334 -0.0559 -0.0064 554 GLU A CA  
3    C C   . GLU A 4   ? 0.8884 0.9539 1.0679 -0.0249 -0.0391 -0.0021 554 GLU A C   
4    O O   . GLU A 4   ? 0.8906 0.9453 1.0556 -0.0104 -0.0388 0.0105  554 GLU A O   
5    C CB  . GLU A 4   ? 0.9170 1.0408 1.1977 -0.0314 -0.0370 -0.0049 554 GLU A CB  
6    C CG  . GLU A 4   ? 1.0364 1.1392 1.3249 -0.0464 -0.0124 -0.0179 554 GLU A CG  
7    C CD  . GLU A 4   ? 1.1706 1.2637 1.4894 -0.0413 0.0179  -0.0127 554 GLU A CD  
8    O OE1 . GLU A 4   ? 1.1948 1.2701 1.5218 -0.0538 0.0406  -0.0200 554 GLU A OE1 
9    O OE2 . GLU A 4   ? 1.2074 1.3074 1.5402 -0.0249 0.0218  -0.0012 554 GLU A OE2 
10   N N   . VAL A 5   ? 0.8856 0.9232 1.0440 -0.0339 -0.0252 -0.0129 555 VAL A N   
11   C CA  . VAL A 5   ? 0.8971 0.8958 1.0158 -0.0253 -0.0116 -0.0090 555 VAL A CA  
12   C C   . VAL A 5   ? 0.8912 0.8762 1.0207 -0.0156 0.0089  -0.0008 555 VAL A C   
13   O O   . VAL A 5   ? 0.8882 0.8790 1.0495 -0.0209 0.0229  -0.0028 555 VAL A O   
14   C CB  . VAL A 5   ? 0.9119 0.8862 1.0095 -0.0338 -0.0033 -0.0197 555 VAL A CB  
15   C CG1 . VAL A 5   ? 0.9355 0.8749 1.0026 -0.0225 0.0116  -0.0129 555 VAL A CG1 
16   C CG2 . VAL A 5   ? 0.9185 0.9012 0.9959 -0.0408 -0.0199 -0.0292 555 VAL A CG2 
17   N N   . GLN A 6   ? 0.8880 0.8563 0.9929 -0.0030 0.0119  0.0065  556 GLN A N   
18   C CA  . GLN A 6   ? 0.8806 0.8352 0.9891 0.0060  0.0315  0.0112  556 GLN A CA  
19   C C   . GLN A 6   ? 0.8878 0.8116 0.9658 0.0066  0.0498  0.0103  556 GLN A C   
20   O O   . GLN A 6   ? 0.8912 0.8063 0.9770 0.0081  0.0711  0.0123  556 GLN A O   
21   C CB  . GLN A 6   ? 0.9019 0.8517 0.9999 0.0174  0.0272  0.0163  556 GLN A CB  
22   C CG  . GLN A 6   ? 0.9372 0.9145 1.0637 0.0205  0.0096  0.0232  556 GLN A CG  
23   C CD  . GLN A 6   ? 0.9891 0.9938 1.1684 0.0223  0.0139  0.0261  556 GLN A CD  
24   O OE1 . GLN A 6   ? 1.0209 1.0184 1.2180 0.0275  0.0356  0.0255  556 GLN A OE1 
25   N NE2 . GLN A 6   ? 0.9801 1.0195 1.1861 0.0176  -0.0066 0.0282  556 GLN A NE2 
26   N N   . TRP A 7   ? 0.8887 0.7966 0.9315 0.0070  0.0425  0.0088  557 TRP A N   
27   C CA  . TRP A 7   ? 0.8964 0.7761 0.9061 0.0113  0.0557  0.0118  557 TRP A CA  
28   C C   . TRP A 7   ? 0.9036 0.7737 0.9267 0.0034  0.0701  0.0129  557 TRP A C   
29   O O   . TRP A 7   ? 0.9036 0.7832 0.9467 -0.0065 0.0627  0.0065  557 TRP A O   
30   C CB  . TRP A 7   ? 0.8905 0.7615 0.8671 0.0163  0.0419  0.0106  557 TRP A CB  
31   C CG  . TRP A 7   ? 0.8636 0.7488 0.8398 0.0175  0.0261  0.0070  557 TRP A CG  
32   C CD1 . TRP A 7   ? 0.8606 0.7483 0.8397 0.0214  0.0273  0.0071  557 TRP A CD1 
33   C CD2 . TRP A 7   ? 0.8481 0.7436 0.8226 0.0141  0.0107  0.0031  557 TRP A CD2 
34   N NE1 . TRP A 7   ? 0.8558 0.7529 0.8360 0.0203  0.0133  0.0057  557 TRP A NE1 
35   C CE2 . TRP A 7   ? 0.8484 0.7519 0.8242 0.0155  0.0033  0.0035  557 TRP A CE2 
36   C CE3 . TRP A 7   ? 0.8455 0.7415 0.8173 0.0102  0.0057  -0.0012 557 TRP A CE3 
37   C CZ2 . TRP A 7   ? 0.8443 0.7569 0.8165 0.0120  -0.0083 0.0018  557 TRP A CZ2 
38   C CZ3 . TRP A 7   ? 0.8450 0.7520 0.8129 0.0073  -0.0057 -0.0054 557 TRP A CZ3 
39   C CH2 . TRP A 7   ? 0.8423 0.7582 0.8095 0.0077  -0.0124 -0.0030 557 TRP A CH2 
40   N N   . LYS A 8   ? 0.9095 0.7594 0.9213 0.0064  0.0926  0.0201  558 LYS A N   
41   C CA  . LYS A 8   ? 0.9128 0.7470 0.9376 -0.0018 0.1122  0.0236  558 LYS A CA  
42   C C   . LYS A 8   ? 0.9285 0.7287 0.9120 0.0063  0.1184  0.0340  558 LYS A C   
43   O O   . LYS A 8   ? 0.9293 0.7174 0.8704 0.0192  0.1157  0.0413  558 LYS A O   
44   C CB  . LYS A 8   ? 0.9413 0.7754 0.9867 -0.0050 0.1391  0.0273  558 LYS A CB  
45   C CG  . LYS A 8   ? 0.9704 0.8416 1.0639 -0.0087 0.1333  0.0193  558 LYS A CG  
46   C CD  . LYS A 8   ? 1.0156 0.9158 1.1569 -0.0232 0.1186  0.0096  558 LYS A CD  
47   C CE  . LYS A 8   ? 1.0569 0.9981 1.2391 -0.0219 0.1028  0.0054  558 LYS A CE  
48   N NZ  . LYS A 8   ? 1.0858 1.0559 1.2900 -0.0321 0.0757  -0.0037 558 LYS A NZ  
49   N N   . VAL A 9   ? 0.9397 0.7249 0.9372 -0.0013 0.1260  0.0341  559 VAL A N   
50   C CA  . VAL A 9   ? 0.9770 0.7258 0.9426 0.0082  0.1353  0.0478  559 VAL A CA  
51   C C   . VAL A 9   ? 1.0081 0.7313 0.9892 -0.0012 0.1673  0.0560  559 VAL A C   
52   O O   . VAL A 9   ? 0.9870 0.7196 1.0143 -0.0192 0.1740  0.0436  559 VAL A O   
53   C CB  . VAL A 9   ? 0.9715 0.7181 0.9412 0.0095  0.1194  0.0407  559 VAL A CB  
54   C CG1 . VAL A 9   ? 0.9921 0.6977 0.9406 0.0205  0.1332  0.0570  559 VAL A CG1 
55   C CG2 . VAL A 9   ? 0.9658 0.7363 0.9188 0.0186  0.0923  0.0348  559 VAL A CG2 
56   N N   . VAL A 10  ? 1.0549 0.7486 0.9980 0.0091  0.1877  0.0758  560 VAL A N   
57   C CA  . VAL A 10  ? 1.0996 0.7642 1.0546 -0.0003 0.2237  0.0867  560 VAL A CA  
58   C C   . VAL A 10  ? 1.1689 0.7866 1.1027 0.0076  0.2359  0.1050  560 VAL A C   
59   O O   . VAL A 10  ? 1.1854 0.7956 1.0895 0.0247  0.2161  0.1119  560 VAL A O   
60   C CB  . VAL A 10  ? 1.1179 0.7775 1.0499 0.0023  0.2481  0.0973  560 VAL A CB  
61   C CG1 . VAL A 10  ? 1.1033 0.8044 1.0501 0.0015  0.2340  0.0811  560 VAL A CG1 
62   C CG2 . VAL A 10  ? 1.1587 0.7832 1.0172 0.0223  0.2552  0.1221  560 VAL A CG2 
63   N N   . GLU A 11  ? 1.2020 0.7892 1.1580 -0.0051 0.2694  0.1122  561 GLU A N   
64   C CA  . GLU A 11  ? 1.2703 0.8051 1.2090 0.0028  0.2874  0.1330  561 GLU A CA  
65   C C   . GLU A 11  ? 1.3535 0.8535 1.2311 0.0197  0.3090  0.1663  561 GLU A C   
66   O O   . GLU A 11  ? 1.3630 0.8726 1.2289 0.0147  0.3251  0.1684  561 GLU A O   
67   C CB  . GLU A 11  ? 1.2735 0.7874 1.2687 -0.0223 0.3160  0.1231  561 GLU A CB  
68   C CG  . GLU A 11  ? 1.2637 0.8153 1.3150 -0.0421 0.2946  0.0876  561 GLU A CG  
69   C CD  . GLU A 11  ? 1.2671 0.7884 1.3586 -0.0595 0.3109  0.0752  561 GLU A CD  
70   O OE1 . GLU A 11  ? 1.2770 0.7421 1.3585 -0.0561 0.3428  0.0967  561 GLU A OE1 
71   O OE2 . GLU A 11  ? 1.2530 0.8044 1.3836 -0.0768 0.2927  0.0440  561 GLU A OE2 
72   N N   . GLU A 12  ? 1.4086 0.8679 1.2471 0.0404  0.3105  0.1927  562 GLU A N   
73   C CA  . GLU A 12  ? 1.4792 0.9021 1.2497 0.0598  0.3277  0.2292  562 GLU A CA  
74   C C   . GLU A 12  ? 1.5054 0.8923 1.2788 0.0445  0.3775  0.2440  562 GLU A C   
75   O O   . GLU A 12  ? 1.5140 0.9177 1.2736 0.0370  0.3911  0.2405  562 GLU A O   
76   C CB  . GLU A 12  ? 1.5548 0.9413 1.2964 0.0859  0.3188  0.2562  562 GLU A CB  
77   C CG  . GLU A 12  ? 1.6325 1.0568 1.3656 0.1040  0.2720  0.2455  562 GLU A CG  
78   C CD  . GLU A 12  ? 1.7765 1.2000 1.4365 0.1336  0.2529  0.2733  562 GLU A CD  
79   O OE1 . GLU A 12  ? 1.8269 1.2063 1.4539 0.1540  0.2652  0.3093  562 GLU A OE1 
80   O OE2 . GLU A 12  ? 1.8016 1.2679 1.4372 0.1361  0.2257  0.2593  562 GLU A OE2 
81   N N   . VAL A 19  ? 1.1041 0.7494 1.2271 -0.0751 0.3661  0.0849  569 VAL A N   
82   C CA  . VAL A 19  ? 1.0998 0.7550 1.2671 -0.0904 0.3467  0.0654  569 VAL A CA  
83   C C   . VAL A 19  ? 1.0937 0.7652 1.2311 -0.0748 0.3013  0.0577  569 VAL A C   
84   O O   . VAL A 19  ? 1.1316 0.7712 1.2137 -0.0557 0.2939  0.0734  569 VAL A O   
85   C CB  . VAL A 19  ? 1.1404 0.7423 1.3177 -0.1033 0.3777  0.0736  569 VAL A CB  
86   C CG1 . VAL A 19  ? 1.2009 0.7412 1.3048 -0.0812 0.3980  0.1087  569 VAL A CG1 
87   C CG2 . VAL A 19  ? 1.1358 0.7404 1.3425 -0.1150 0.3552  0.0512  569 VAL A CG2 
88   N N   . TYR A 20  ? 1.0389 0.7625 1.2142 -0.0824 0.2713  0.0348  570 TYR A N   
89   C CA  . TYR A 20  ? 1.0203 0.7636 1.1710 -0.0700 0.2317  0.0271  570 TYR A CA  
90   C C   . TYR A 20  ? 0.9893 0.7261 1.1499 -0.0786 0.2163  0.0122  570 TYR A C   
91   O O   . TYR A 20  ? 0.9778 0.7207 1.1854 -0.1014 0.2234  -0.0051 570 TYR A O   
92   C CB  . TYR A 20  ? 0.9959 0.7950 1.1756 -0.0711 0.2080  0.0139  570 TYR A CB  
93   C CG  . TYR A 20  ? 1.0145 0.8216 1.1884 -0.0614 0.2236  0.0244  570 TYR A CG  
94   C CD1 . TYR A 20  ? 1.0134 0.8260 1.2288 -0.0733 0.2551  0.0251  570 TYR A CD1 
95   C CD2 . TYR A 20  ? 1.0390 0.8495 1.1703 -0.0419 0.2087  0.0305  570 TYR A CD2 
96   C CE1 . TYR A 20  ? 1.0255 0.8440 1.2358 -0.0640 0.2737  0.0325  570 TYR A CE1 
97   C CE2 . TYR A 20  ? 1.0510 0.8664 1.1766 -0.0339 0.2251  0.0358  570 TYR A CE2 
98   C CZ  . TYR A 20  ? 1.0533 0.8725 1.2175 -0.0440 0.2582  0.0368  570 TYR A CZ  
99   O OH  . TYR A 20  ? 1.0774 0.8995 1.2356 -0.0355 0.2788  0.0402  570 TYR A OH  
100  N N   . ILE A 21  ? 0.9757 0.7036 1.0946 -0.0616 0.1950  0.0158  571 ILE A N   
101  C CA  . ILE A 21  ? 0.9551 0.6776 1.0770 -0.0660 0.1805  0.0008  571 ILE A CA  
102  C C   . ILE A 21  ? 0.9188 0.6931 1.0602 -0.0748 0.1490  -0.0210 571 ILE A C   
103  O O   . ILE A 21  ? 0.8946 0.6954 1.0198 -0.0631 0.1304  -0.0161 571 ILE A O   
104  C CB  . ILE A 21  ? 0.9775 0.6702 1.0499 -0.0414 0.1743  0.0166  571 ILE A CB  
105  C CG1 . ILE A 21  ? 1.0086 0.6467 1.0619 -0.0319 0.2043  0.0404  571 ILE A CG1 
106  C CG2 . ILE A 21  ? 0.9778 0.6752 1.0536 -0.0432 0.1566  -0.0017 571 ILE A CG2 
107  C CD1 . ILE A 21  ? 1.0423 0.6573 1.0495 -0.0043 0.1961  0.0605  571 ILE A CD1 
108  N N   . ASP A 22  ? 0.9116 0.6984 1.0858 -0.0960 0.1438  -0.0450 572 ASP A N   
109  C CA  . ASP A 22  ? 0.9048 0.7394 1.0903 -0.1045 0.1128  -0.0642 572 ASP A CA  
110  C C   . ASP A 22  ? 0.9171 0.7442 1.0605 -0.0900 0.0959  -0.0647 572 ASP A C   
111  O O   . ASP A 22  ? 0.9312 0.7247 1.0632 -0.0892 0.1059  -0.0701 572 ASP A O   
112  C CB  . ASP A 22  ? 0.9291 0.7772 1.1565 -0.1335 0.1130  -0.0924 572 ASP A CB  
113  C CG  . ASP A 22  ? 1.0081 0.9099 1.2454 -0.1442 0.0795  -0.1119 572 ASP A CG  
114  O OD1 . ASP A 22  ? 1.0113 0.9461 1.2397 -0.1309 0.0594  -0.0999 572 ASP A OD1 
115  O OD2 . ASP A 22  ? 1.0524 0.9618 1.3045 -0.1657 0.0737  -0.1389 572 ASP A OD2 
116  N N   . PRO A 23  ? 0.9005 0.7565 1.0241 -0.0780 0.0731  -0.0586 573 PRO A N   
117  C CA  . PRO A 23  ? 0.9080 0.7582 0.9959 -0.0651 0.0607  -0.0582 573 PRO A CA  
118  C C   . PRO A 23  ? 0.9079 0.7614 0.9952 -0.0782 0.0536  -0.0817 573 PRO A C   
119  O O   . PRO A 23  ? 0.9285 0.7636 0.9937 -0.0685 0.0555  -0.0828 573 PRO A O   
120  C CB  . PRO A 23  ? 0.9065 0.7869 0.9814 -0.0545 0.0414  -0.0482 573 PRO A CB  
121  C CG  . PRO A 23  ? 0.8883 0.7967 0.9956 -0.0631 0.0388  -0.0480 573 PRO A CG  
122  C CD  . PRO A 23  ? 0.8681 0.7594 1.0044 -0.0744 0.0619  -0.0504 573 PRO A CD  
123  N N   . THR A 24  ? 0.8899 0.7673 1.0021 -0.1001 0.0463  -0.1018 574 THR A N   
124  C CA  . THR A 24  ? 0.9041 0.7834 1.0102 -0.1154 0.0408  -0.1288 574 THR A CA  
125  C C   . THR A 24  ? 0.9386 0.7682 1.0487 -0.1179 0.0675  -0.1384 574 THR A C   
126  O O   . THR A 24  ? 0.9520 0.7702 1.0481 -0.1223 0.0693  -0.1576 574 THR A O   
127  C CB  . THR A 24  ? 0.8904 0.8085 1.0239 -0.1403 0.0258  -0.1502 574 THR A CB  
128  O OG1 . THR A 24  ? 0.8957 0.8017 1.0711 -0.1542 0.0446  -0.1547 574 THR A OG1 
129  C CG2 . THR A 24  ? 0.8695 0.8370 1.0033 -0.1354 -0.0014 -0.1387 574 THR A CG2 
130  N N   . GLN A 25  ? 0.9458 0.7441 1.0757 -0.1153 0.0906  -0.1245 575 GLN A N   
131  C CA  . GLN A 25  ? 0.9639 0.7082 1.1005 -0.1137 0.1194  -0.1246 575 GLN A CA  
132  C C   . GLN A 25  ? 0.9808 0.6961 1.0874 -0.0844 0.1248  -0.1037 575 GLN A C   
133  O O   . GLN A 25  ? 1.0040 0.6763 1.1141 -0.0793 0.1451  -0.1052 575 GLN A O   
134  C CB  . GLN A 25  ? 0.9900 0.7137 1.1545 -0.1205 0.1423  -0.1118 575 GLN A CB  
135  C CG  . GLN A 25  ? 1.0385 0.7808 1.2473 -0.1534 0.1455  -0.1381 575 GLN A CG  
136  C CD  . GLN A 25  ? 1.1306 0.8490 1.3687 -0.1594 0.1742  -0.1230 575 GLN A CD  
137  O OE1 . GLN A 25  ? 1.1622 0.8769 1.3865 -0.1412 0.1805  -0.0932 575 GLN A OE1 
138  N NE2 . GLN A 25  ? 1.1393 0.8392 1.4174 -0.1866 0.1947  -0.1445 575 GLN A NE2 
139  N N   . LEU A 26  ? 0.9705 0.7089 1.0517 -0.0653 0.1072  -0.0849 576 LEU A N   
140  C CA  . LEU A 26  ? 0.9877 0.7086 1.0456 -0.0390 0.1078  -0.0680 576 LEU A CA  
141  C C   . LEU A 26  ? 0.9983 0.7209 1.0517 -0.0394 0.1046  -0.0888 576 LEU A C   
142  O O   . LEU A 26  ? 1.0000 0.7463 1.0547 -0.0582 0.0951  -0.1132 576 LEU A O   
143  C CB  . LEU A 26  ? 0.9878 0.7365 1.0238 -0.0237 0.0895  -0.0486 576 LEU A CB  
144  C CG  . LEU A 26  ? 0.9999 0.7401 1.0314 -0.0172 0.0970  -0.0260 576 LEU A CG  
145  C CD1 . LEU A 26  ? 0.9992 0.7688 1.0111 -0.0073 0.0789  -0.0155 576 LEU A CD1 
146  C CD2 . LEU A 26  ? 1.0192 0.7159 1.0408 -0.0005 0.1158  -0.0057 576 LEU A CD2 
147  N N   . PRO A 27  ? 1.0023 0.7017 1.0506 -0.0182 0.1128  -0.0800 577 PRO A N   
148  C CA  . PRO A 27  ? 0.9957 0.6964 1.0440 -0.0182 0.1149  -0.1017 577 PRO A CA  
149  C C   . PRO A 27  ? 0.9909 0.7310 1.0211 -0.0111 0.0953  -0.1018 577 PRO A C   
150  O O   . PRO A 27  ? 0.9763 0.7361 0.9956 0.0016  0.0809  -0.0810 577 PRO A O   
151  C CB  . PRO A 27  ? 1.0108 0.6695 1.0708 0.0041  0.1345  -0.0894 577 PRO A CB  
152  C CG  . PRO A 27  ? 1.0212 0.6764 1.0709 0.0244  0.1288  -0.0538 577 PRO A CG  
153  C CD  . PRO A 27  ? 1.0017 0.6745 1.0444 0.0076  0.1207  -0.0499 577 PRO A CD  
154  N N   . TYR A 28  ? 0.9918 0.7413 1.0177 -0.0210 0.0974  -0.1271 578 TYR A N   
155  C CA  . TYR A 28  ? 0.9934 0.7738 1.0046 -0.0144 0.0860  -0.1272 578 TYR A CA  
156  C C   . TYR A 28  ? 0.9940 0.7585 1.0182 0.0005  0.1032  -0.1353 578 TYR A C   
157  O O   . TYR A 28  ? 0.9917 0.7437 1.0169 -0.0100 0.1185  -0.1618 578 TYR A O   
158  C CB  . TYR A 28  ? 0.9934 0.8043 0.9827 -0.0356 0.0737  -0.1444 578 TYR A CB  
159  C CG  . TYR A 28  ? 0.9993 0.8341 0.9743 -0.0288 0.0691  -0.1431 578 TYR A CG  
160  C CD1 . TYR A 28  ? 1.0079 0.8585 0.9852 -0.0133 0.0587  -0.1202 578 TYR A CD1 
161  C CD2 . TYR A 28  ? 1.0136 0.8531 0.9742 -0.0385 0.0787  -0.1664 578 TYR A CD2 
162  C CE1 . TYR A 28  ? 1.0152 0.8867 0.9868 -0.0091 0.0579  -0.1202 578 TYR A CE1 
163  C CE2 . TYR A 28  ? 1.0213 0.8811 0.9716 -0.0333 0.0796  -0.1644 578 TYR A CE2 
164  C CZ  . TYR A 28  ? 1.0253 0.9013 0.9846 -0.0190 0.0695  -0.1410 578 TYR A CZ  
165  O OH  . TYR A 28  ? 1.0363 0.9321 0.9920 -0.0161 0.0730  -0.1402 578 TYR A OH  
166  N N   . ASP A 29  ? 0.9962 0.7632 1.0316 0.0253  0.1003  -0.1134 579 ASP A N   
167  C CA  . ASP A 29  ? 1.0032 0.7633 1.0604 0.0454  0.1134  -0.1151 579 ASP A CA  
168  C C   . ASP A 29  ? 0.9892 0.7801 1.0398 0.0380  0.1138  -0.1331 579 ASP A C   
169  O O   . ASP A 29  ? 0.9674 0.7915 1.0059 0.0354  0.0974  -0.1247 579 ASP A O   
170  C CB  . ASP A 29  ? 1.0396 0.8066 1.1082 0.0725  0.1018  -0.0845 579 ASP A CB  
171  C CG  . ASP A 29  ? 1.1278 0.8822 1.2282 0.0999  0.1139  -0.0783 579 ASP A CG  
172  O OD1 . ASP A 29  ? 1.1393 0.8847 1.2571 0.0989  0.1339  -0.1005 579 ASP A OD1 
173  O OD2 . ASP A 29  ? 1.1671 0.9227 1.2749 0.1234  0.1032  -0.0513 579 ASP A OD2 
174  N N   . HIS A 30  ? 1.0014 0.7780 1.0591 0.0335  0.1357  -0.1585 580 HIS A N   
175  C CA  . HIS A 30  ? 1.0153 0.8169 1.0627 0.0252  0.1423  -0.1771 580 HIS A CA  
176  C C   . HIS A 30  ? 0.9771 0.8032 1.0536 0.0473  0.1439  -0.1660 580 HIS A C   
177  O O   . HIS A 30  ? 0.9732 0.8214 1.0460 0.0412  0.1529  -0.1792 580 HIS A O   
178  C CB  . HIS A 30  ? 1.0782 0.8566 1.1173 0.0102  0.1669  -0.2121 580 HIS A CB  
179  C CG  . HIS A 30  ? 1.1851 0.9474 1.2006 -0.0139 0.1610  -0.2247 580 HIS A CG  
180  N ND1 . HIS A 30  ? 1.2339 0.9546 1.2681 -0.0150 0.1751  -0.2329 580 HIS A ND1 
181  C CD2 . HIS A 30  ? 1.2181 1.0031 1.2003 -0.0354 0.1404  -0.2257 580 HIS A CD2 
182  C CE1 . HIS A 30  ? 1.2551 0.9782 1.2685 -0.0401 0.1634  -0.2431 580 HIS A CE1 
183  N NE2 . HIS A 30  ? 1.2519 1.0153 1.2345 -0.0514 0.1407  -0.2381 580 HIS A NE2 
184  N N   . LYS A 31  ? 0.9446 0.7716 1.0479 0.0713  0.1333  -0.1407 581 LYS A N   
185  C CA  . LYS A 31  ? 0.9075 0.7680 1.0411 0.0906  0.1270  -0.1290 581 LYS A CA  
186  C C   . LYS A 31  ? 0.8813 0.7802 0.9948 0.0759  0.1084  -0.1238 581 LYS A C   
187  O O   . LYS A 31  ? 0.8751 0.8063 1.0114 0.0810  0.1090  -0.1247 581 LYS A O   
188  C CB  . LYS A 31  ? 0.9245 0.7786 1.0830 0.1189  0.1147  -0.1018 581 LYS A CB  
189  C CG  . LYS A 31  ? 0.9865 0.8465 1.1194 0.1169  0.0882  -0.0788 581 LYS A CG  
190  C CD  . LYS A 31  ? 1.0328 0.8958 1.1853 0.1464  0.0743  -0.0520 581 LYS A CD  
191  C CE  . LYS A 31  ? 1.0948 0.9649 1.2162 0.1430  0.0505  -0.0328 581 LYS A CE  
192  N NZ  . LYS A 31  ? 1.1267 0.9958 1.2551 0.1711  0.0366  -0.0058 581 LYS A NZ  
193  N N   . TRP A 32  ? 0.8628 0.7576 0.9390 0.0579  0.0941  -0.1189 582 TRP A N   
194  C CA  . TRP A 32  ? 0.8411 0.7632 0.8975 0.0446  0.0788  -0.1126 582 TRP A CA  
195  C C   . TRP A 32  ? 0.8418 0.7741 0.8767 0.0251  0.0911  -0.1295 582 TRP A C   
196  O O   . TRP A 32  ? 0.8389 0.7930 0.8644 0.0166  0.0844  -0.1236 582 TRP A O   
197  C CB  . TRP A 32  ? 0.8391 0.7514 0.8681 0.0356  0.0612  -0.1001 582 TRP A CB  
198  C CG  . TRP A 32  ? 0.8274 0.7305 0.8661 0.0522  0.0493  -0.0808 582 TRP A CG  
199  C CD1 . TRP A 32  ? 0.8449 0.7183 0.8784 0.0556  0.0514  -0.0744 582 TRP A CD1 
200  C CD2 . TRP A 32  ? 0.8065 0.7303 0.8578 0.0661  0.0340  -0.0659 582 TRP A CD2 
201  N NE1 . TRP A 32  ? 0.8456 0.7181 0.8818 0.0718  0.0394  -0.0537 582 TRP A NE1 
202  C CE2 . TRP A 32  ? 0.8232 0.7278 0.8691 0.0788  0.0269  -0.0494 582 TRP A CE2 
203  C CE3 . TRP A 32  ? 0.7914 0.7487 0.8574 0.0670  0.0261  -0.0662 582 TRP A CE3 
204  C CZ2 . TRP A 32  ? 0.8200 0.7390 0.8682 0.0935  0.0099  -0.0335 582 TRP A CZ2 
205  C CZ3 . TRP A 32  ? 0.7914 0.7652 0.8674 0.0803  0.0084  -0.0533 582 TRP A CZ3 
206  C CH2 . TRP A 32  ? 0.8030 0.7583 0.8665 0.0937  -0.0009 -0.0373 582 TRP A CH2 
207  N N   . GLU A 33  ? 0.8430 0.7570 0.8662 0.0170  0.1101  -0.1506 583 GLU A N   
208  C CA  . GLU A 33  ? 0.8452 0.7670 0.8367 -0.0021 0.1221  -0.1669 583 GLU A CA  
209  C C   . GLU A 33  ? 0.8326 0.7804 0.8392 -0.0002 0.1346  -0.1674 583 GLU A C   
210  O O   . GLU A 33  ? 0.8129 0.7679 0.8616 0.0153  0.1482  -0.1720 583 GLU A O   
211  C CB  . GLU A 33  ? 0.8629 0.7603 0.8396 -0.0109 0.1419  -0.1941 583 GLU A CB  
212  C CG  . GLU A 33  ? 0.9003 0.8030 0.8246 -0.0347 0.1444  -0.2084 583 GLU A CG  
213  C CD  . GLU A 33  ? 0.9255 0.8342 0.8165 -0.0482 0.1174  -0.1955 583 GLU A CD  
214  O OE1 . GLU A 33  ? 0.9065 0.8054 0.8121 -0.0440 0.1020  -0.1857 583 GLU A OE1 
215  O OE2 . GLU A 33  ? 0.9449 0.8680 0.7954 -0.0621 0.1129  -0.1942 583 GLU A OE2 
216  N N   . PHE A 34  ? 0.8418 0.8046 0.8191 -0.0150 0.1291  -0.1599 584 PHE A N   
217  C CA  . PHE A 34  ? 0.8425 0.8287 0.8312 -0.0182 0.1426  -0.1585 584 PHE A CA  
218  C C   . PHE A 34  ? 0.8974 0.8811 0.8328 -0.0385 0.1556  -0.1651 584 PHE A C   
219  O O   . PHE A 34  ? 0.9234 0.8984 0.8151 -0.0494 0.1398  -0.1580 584 PHE A O   
220  C CB  . PHE A 34  ? 0.8139 0.8178 0.8209 -0.0155 0.1224  -0.1367 584 PHE A CB  
221  C CG  . PHE A 34  ? 0.7863 0.8150 0.8146 -0.0212 0.1355  -0.1348 584 PHE A CG  
222  C CD1 . PHE A 34  ? 0.7592 0.8106 0.8419 -0.0102 0.1491  -0.1435 584 PHE A CD1 
223  C CD2 . PHE A 34  ? 0.8008 0.8306 0.8004 -0.0368 0.1344  -0.1229 584 PHE A CD2 
224  C CE1 . PHE A 34  ? 0.7478 0.8254 0.8577 -0.0179 0.1624  -0.1436 584 PHE A CE1 
225  C CE2 . PHE A 34  ? 0.7948 0.8441 0.8177 -0.0444 0.1498  -0.1212 584 PHE A CE2 
226  C CZ  . PHE A 34  ? 0.7617 0.8364 0.8411 -0.0363 0.1638  -0.1329 584 PHE A CZ  
227  N N   . PRO A 35  ? 0.9083 0.9017 0.8468 -0.0431 0.1849  -0.1776 585 PRO A N   
228  C CA  . PRO A 35  ? 0.9443 0.9341 0.8236 -0.0621 0.1991  -0.1813 585 PRO A CA  
229  C C   . PRO A 35  ? 0.9710 0.9692 0.8299 -0.0713 0.1886  -0.1554 585 PRO A C   
230  O O   . PRO A 35  ? 0.9564 0.9700 0.8522 -0.0694 0.1944  -0.1452 585 PRO A O   
231  C CB  . PRO A 35  ? 0.9455 0.9421 0.8419 -0.0621 0.2380  -0.2024 585 PRO A CB  
232  C CG  . PRO A 35  ? 0.9112 0.9282 0.8852 -0.0447 0.2391  -0.1984 585 PRO A CG  
233  C CD  . PRO A 35  ? 0.8793 0.8888 0.8755 -0.0304 0.2074  -0.1883 585 PRO A CD  
234  N N   . ARG A 36  ? 1.0047 0.9925 0.8069 -0.0814 0.1727  -0.1455 586 ARG A N   
235  C CA  . ARG A 36  ? 1.0271 1.0146 0.7967 -0.0892 0.1613  -0.1190 586 ARG A CA  
236  C C   . ARG A 36  ? 1.0448 1.0372 0.8060 -0.0985 0.1906  -0.1121 586 ARG A C   
237  O O   . ARG A 36  ? 1.0500 1.0426 0.8186 -0.1010 0.1874  -0.0894 586 ARG A O   
238  C CB  . ARG A 36  ? 1.0674 1.0467 0.7713 -0.0982 0.1478  -0.1196 586 ARG A CB  
239  C CG  . ARG A 36  ? 1.0973 1.0750 0.7656 -0.1012 0.1254  -0.0902 586 ARG A CG  
240  C CD  . ARG A 36  ? 1.1136 1.0917 0.7240 -0.1091 0.1095  -0.0980 586 ARG A CD  
241  N NE  . ARG A 36  ? 1.0845 1.0625 0.7198 -0.1061 0.0950  -0.1199 586 ARG A NE  
242  C CZ  . ARG A 36  ? 1.0395 1.0209 0.6898 -0.1016 0.0657  -0.1111 586 ARG A CZ  
243  N NH1 . ARG A 36  ? 1.0021 0.9888 0.6432 -0.0982 0.0457  -0.0819 586 ARG A NH1 
244  N NH2 . ARG A 36  ? 1.0221 1.0002 0.6967 -0.1008 0.0586  -0.1313 586 ARG A NH2 
245  N N   . ASN A 37  ? 1.0525 1.0464 0.7984 -0.1047 0.2227  -0.1323 587 ASN A N   
246  C CA  . ASN A 37  ? 1.0620 1.0600 0.7991 -0.1153 0.2563  -0.1262 587 ASN A CA  
247  C C   . ASN A 37  ? 1.0309 1.0478 0.8474 -0.1108 0.2693  -0.1252 587 ASN A C   
248  O O   . ASN A 37  ? 1.0337 1.0555 0.8540 -0.1215 0.2975  -0.1183 587 ASN A O   
249  C CB  . ASN A 37  ? 1.0976 1.0913 0.7897 -0.1246 0.2901  -0.1486 587 ASN A CB  
250  C CG  . ASN A 37  ? 1.1376 1.1404 0.8807 -0.1165 0.3138  -0.1806 587 ASN A CG  
251  O OD1 . ASN A 37  ? 1.1404 1.1483 0.9399 -0.1015 0.2972  -0.1891 587 ASN A OD1 
252  N ND2 . ASN A 37  ? 1.1595 1.1625 0.8814 -0.1253 0.3555  -0.1979 587 ASN A ND2 
253  N N   . ARG A 38  ? 0.9995 1.0281 0.8778 -0.0961 0.2486  -0.1311 588 ARG A N   
254  C CA  . ARG A 38  ? 0.9689 1.0213 0.9222 -0.0914 0.2507  -0.1297 588 ARG A CA  
255  C C   . ARG A 38  ? 0.9567 1.0057 0.9199 -0.0910 0.2200  -0.1083 588 ARG A C   
256  O O   . ARG A 38  ? 0.9354 1.0031 0.9564 -0.0837 0.2074  -0.1102 588 ARG A O   
257  C CB  . ARG A 38  ? 0.9775 1.0483 0.9927 -0.0735 0.2486  -0.1492 588 ARG A CB  
258  C CG  . ARG A 38  ? 1.0565 1.1271 1.0695 -0.0711 0.2805  -0.1731 588 ARG A CG  
259  C CD  . ARG A 38  ? 1.1049 1.1969 1.1941 -0.0506 0.2814  -0.1875 588 ARG A CD  
260  N NE  . ARG A 38  ? 1.1968 1.2795 1.2822 -0.0450 0.3102  -0.2120 588 ARG A NE  
261  C CZ  . ARG A 38  ? 1.2495 1.3297 1.3737 -0.0245 0.3069  -0.2242 588 ARG A CZ  
262  N NH1 . ARG A 38  ? 1.2390 1.3268 1.4033 -0.0071 0.2745  -0.2116 588 ARG A NH1 
263  N NH2 . ARG A 38  ? 1.2659 1.3325 1.3855 -0.0209 0.3376  -0.2489 588 ARG A NH2 
264  N N   . LEU A 39  ? 0.9699 0.9962 0.8771 -0.0979 0.2079  -0.0887 589 LEU A N   
265  C CA  . LEU A 39  ? 0.9630 0.9807 0.8754 -0.0982 0.1852  -0.0683 589 LEU A CA  
266  C C   . LEU A 39  ? 0.9815 0.9845 0.8636 -0.1133 0.2047  -0.0484 589 LEU A C   
267  O O   . LEU A 39  ? 1.0091 0.9994 0.8332 -0.1198 0.2189  -0.0417 589 LEU A O   
268  C CB  . LEU A 39  ? 0.9710 0.9723 0.8461 -0.0904 0.1544  -0.0588 589 LEU A CB  
269  C CG  . LEU A 39  ? 0.9610 0.9682 0.8627 -0.0761 0.1323  -0.0709 589 LEU A CG  
270  C CD1 . LEU A 39  ? 0.9750 0.9677 0.8372 -0.0728 0.1096  -0.0636 589 LEU A CD1 
271  C CD2 . LEU A 39  ? 0.9442 0.9628 0.8989 -0.0697 0.1192  -0.0696 589 LEU A CD2 
272  N N   . SER A 40  ? 0.9679 0.9700 0.8849 -0.1193 0.2057  -0.0385 590 SER A N   
273  C CA  . SER A 40  ? 0.9870 0.9676 0.8791 -0.1332 0.2255  -0.0159 590 SER A CA  
274  C C   . SER A 40  ? 0.9912 0.9523 0.8854 -0.1291 0.2010  0.0019  590 SER A C   
275  O O   . SER A 40  ? 0.9742 0.9456 0.9200 -0.1278 0.1891  -0.0081 590 SER A O   
276  C CB  . SER A 40  ? 0.9874 0.9827 0.9299 -0.1482 0.2580  -0.0242 590 SER A CB  
277  O OG  . SER A 40  ? 1.0508 1.0182 0.9663 -0.1623 0.2804  0.0003  590 SER A OG  
278  N N   . PHE A 41  ? 1.0157 0.9511 0.8547 -0.1256 0.1918  0.0269  591 PHE A N   
279  C CA  . PHE A 41  ? 1.0268 0.9433 0.8699 -0.1181 0.1690  0.0433  591 PHE A CA  
280  C C   . PHE A 41  ? 1.0422 0.9359 0.9083 -0.1289 0.1866  0.0579  591 PHE A C   
281  O O   . PHE A 41  ? 1.0583 0.9433 0.9205 -0.1429 0.2178  0.0654  591 PHE A O   
282  C CB  . PHE A 41  ? 1.0429 0.9465 0.8291 -0.1071 0.1487  0.0641  591 PHE A CB  
283  C CG  . PHE A 41  ? 1.0436 0.9683 0.8181 -0.0986 0.1285  0.0450  591 PHE A CG  
284  C CD1 . PHE A 41  ? 1.0378 0.9708 0.8416 -0.0878 0.1032  0.0341  591 PHE A CD1 
285  C CD2 . PHE A 41  ? 1.0615 0.9957 0.7969 -0.1029 0.1388  0.0355  591 PHE A CD2 
286  C CE1 . PHE A 41  ? 1.0435 0.9916 0.8407 -0.0817 0.0889  0.0166  591 PHE A CE1 
287  C CE2 . PHE A 41  ? 1.0658 1.0152 0.7954 -0.0972 0.1235  0.0146  591 PHE A CE2 
288  C CZ  . PHE A 41  ? 1.0503 1.0055 0.8121 -0.0867 0.0988  0.0065  591 PHE A CZ  
289  N N   . GLY A 42  ? 1.0376 0.9203 0.9300 -0.1234 0.1692  0.0595  592 GLY A N   
290  C CA  . GLY A 42  ? 1.0407 0.8969 0.9597 -0.1337 0.1843  0.0691  592 GLY A CA  
291  C C   . GLY A 42  ? 1.0555 0.8806 0.9572 -0.1210 0.1688  0.0921  592 GLY A C   
292  O O   . GLY A 42  ? 1.0756 0.8934 0.9313 -0.1080 0.1568  0.1141  592 GLY A O   
293  N N   . LYS A 43  ? 1.0398 0.8484 0.9803 -0.1247 0.1690  0.0855  593 LYS A N   
294  C CA  . LYS A 43  ? 1.0501 0.8262 0.9841 -0.1123 0.1596  0.1050  593 LYS A CA  
295  C C   . LYS A 43  ? 1.0327 0.8254 0.9586 -0.0928 0.1272  0.0997  593 LYS A C   
296  O O   . LYS A 43  ? 1.0059 0.8302 0.9439 -0.0914 0.1122  0.0747  593 LYS A O   
297  C CB  . LYS A 43  ? 1.0812 0.8332 1.0611 -0.1248 0.1734  0.0927  593 LYS A CB  
298  C CG  . LYS A 43  ? 1.1817 0.9054 1.1706 -0.1444 0.2095  0.1051  593 LYS A CG  
299  C CD  . LYS A 43  ? 1.2597 0.9657 1.3027 -0.1635 0.2246  0.0825  593 LYS A CD  
300  C CE  . LYS A 43  ? 1.3197 1.0050 1.3799 -0.1879 0.2635  0.0894  593 LYS A CE  
301  N NZ  . LYS A 43  ? 1.3358 1.0036 1.4520 -0.2103 0.2789  0.0643  593 LYS A NZ  
302  N N   . THR A 44  ? 1.0369 0.8076 0.9465 -0.0770 0.1179  0.1247  594 THR A N   
303  C CA  . THR A 44  ? 1.0209 0.8059 0.9314 -0.0598 0.0910  0.1202  594 THR A CA  
304  C C   . THR A 44  ? 0.9958 0.7693 0.9459 -0.0614 0.0916  0.0994  594 THR A C   
305  O O   . THR A 44  ? 1.0004 0.7398 0.9686 -0.0663 0.1088  0.1052  594 THR A O   
306  C CB  . THR A 44  ? 1.0420 0.8125 0.9286 -0.0420 0.0816  0.1545  594 THR A CB  
307  O OG1 . THR A 44  ? 1.0602 0.8455 0.9026 -0.0420 0.0779  0.1702  594 THR A OG1 
308  C CG2 . THR A 44  ? 1.0337 0.8176 0.9336 -0.0253 0.0583  0.1500  594 THR A CG2 
309  N N   . LEU A 45  ? 0.9659 0.7653 0.9268 -0.0585 0.0751  0.0746  595 LEU A N   
310  C CA  . LEU A 45  ? 0.9525 0.7476 0.9408 -0.0602 0.0726  0.0512  595 LEU A CA  
311  C C   . LEU A 45  ? 0.9636 0.7456 0.9534 -0.0427 0.0634  0.0592  595 LEU A C   
312  O O   . LEU A 45  ? 0.9812 0.7430 0.9898 -0.0432 0.0699  0.0472  595 LEU A O   
313  C CB  . LEU A 45  ? 0.9335 0.7642 0.9273 -0.0639 0.0596  0.0243  595 LEU A CB  
314  C CG  . LEU A 45  ? 0.9304 0.7818 0.9338 -0.0790 0.0679  0.0123  595 LEU A CG  
315  C CD1 . LEU A 45  ? 0.9185 0.8052 0.9275 -0.0756 0.0521  -0.0082 595 LEU A CD1 
316  C CD2 . LEU A 45  ? 0.9292 0.7669 0.9624 -0.0972 0.0849  -0.0001 595 LEU A CD2 
317  N N   . GLY A 46  ? 0.9487 0.7447 0.9208 -0.0286 0.0493  0.0762  596 GLY A N   
318  C CA  . GLY A 46  ? 0.9322 0.7246 0.9118 -0.0113 0.0403  0.0853  596 GLY A CA  
319  C C   . GLY A 46  ? 0.9192 0.7300 0.8800 -0.0003 0.0256  0.1086  596 GLY A C   
320  O O   . GLY A 46  ? 0.9142 0.7481 0.8531 -0.0064 0.0177  0.1057  596 GLY A O   
321  N N   . ALA A 47  ? 0.9219 0.7240 0.8923 0.0159  0.0217  0.1307  597 ALA A N   
322  C CA  . ALA A 47  ? 0.9319 0.7560 0.8858 0.0266  0.0038  0.1544  597 ALA A CA  
323  C C   . ALA A 47  ? 0.9417 0.7723 0.9219 0.0464  -0.0066 0.1683  597 ALA A C   
324  O O   . ALA A 47  ? 0.9508 0.7538 0.9566 0.0573  0.0057  0.1783  597 ALA A O   
325  C CB  . ALA A 47  ? 0.9356 0.7439 0.8620 0.0252  0.0101  0.1822  597 ALA A CB  
326  N N   . GLY A 48  ? 0.9377 0.8055 0.9145 0.0507  -0.0280 0.1690  598 GLY A N   
327  C CA  . GLY A 48  ? 0.9373 0.8234 0.9449 0.0689  -0.0410 0.1823  598 GLY A CA  
328  C C   . GLY A 48  ? 0.9485 0.8610 0.9376 0.0770  -0.0641 0.2089  598 GLY A C   
329  O O   . GLY A 48  ? 0.9652 0.8690 0.9146 0.0714  -0.0640 0.2233  598 GLY A O   
330  N N   . ALA A 49  ? 0.9370 0.8851 0.9539 0.0891  -0.0841 0.2149  599 ALA A N   
331  C CA  . ALA A 49  ? 0.9409 0.9228 0.9419 0.0975  -0.1121 0.2393  599 ALA A CA  
332  C C   . ALA A 49  ? 0.9495 0.9601 0.9069 0.0777  -0.1277 0.2216  599 ALA A C   
333  O O   . ALA A 49  ? 0.9666 0.9905 0.8827 0.0774  -0.1437 0.2391  599 ALA A O   
334  C CB  . ALA A 49  ? 0.9138 0.9315 0.9679 0.1154  -0.1296 0.2476  599 ALA A CB  
335  N N   . PHE A 50  ? 0.9336 0.9513 0.8980 0.0618  -0.1217 0.1873  600 PHE A N   
336  C CA  . PHE A 50  ? 0.9287 0.9706 0.8605 0.0437  -0.1333 0.1665  600 PHE A CA  
337  C C   . PHE A 50  ? 0.9156 0.9340 0.8200 0.0265  -0.1133 0.1432  600 PHE A C   
338  O O   . PHE A 50  ? 0.9237 0.9565 0.7979 0.0125  -0.1192 0.1270  600 PHE A O   
339  C CB  . PHE A 50  ? 0.9189 0.9973 0.8872 0.0401  -0.1476 0.1472  600 PHE A CB  
340  C CG  . PHE A 50  ? 0.9238 1.0388 0.9241 0.0557  -0.1721 0.1680  600 PHE A CG  
341  C CD1 . PHE A 50  ? 0.9472 1.0872 0.9162 0.0600  -0.1978 0.1887  600 PHE A CD1 
342  C CD2 . PHE A 50  ? 0.9177 1.0440 0.9794 0.0673  -0.1693 0.1679  600 PHE A CD2 
343  C CE1 . PHE A 50  ? 0.9341 1.1136 0.9367 0.0770  -0.2243 0.2101  600 PHE A CE1 
344  C CE2 . PHE A 50  ? 0.9058 1.0716 1.0067 0.0835  -0.1923 0.1874  600 PHE A CE2 
345  C CZ  . PHE A 50  ? 0.9054 1.0991 0.9784 0.0892  -0.2215 0.2091  600 PHE A CZ  
346  N N   . GLY A 51  ? 0.8903 0.8755 0.8080 0.0274  -0.0905 0.1390  601 GLY A N   
347  C CA  . GLY A 51  ? 0.8798 0.8484 0.7800 0.0132  -0.0736 0.1175  601 GLY A CA  
348  C C   . GLY A 51  ? 0.8722 0.8066 0.7714 0.0129  -0.0525 0.1238  601 GLY A C   
349  O O   . GLY A 51  ? 0.8704 0.7859 0.7856 0.0238  -0.0470 0.1426  601 GLY A O   
350  N N   . LYS A 52  ? 0.8607 0.7875 0.7454 0.0001  -0.0396 0.1068  602 LYS A N   
351  C CA  . LYS A 52  ? 0.8542 0.7542 0.7438 -0.0047 -0.0196 0.1064  602 LYS A CA  
352  C C   . LYS A 52  ? 0.8266 0.7299 0.7202 -0.0161 -0.0103 0.0797  602 LYS A C   
353  O O   . LYS A 52  ? 0.8098 0.7313 0.6932 -0.0204 -0.0159 0.0654  602 LYS A O   
354  C CB  . LYS A 52  ? 0.8997 0.7853 0.7620 -0.0071 -0.0109 0.1299  602 LYS A CB  
355  C CG  . LYS A 52  ? 0.9617 0.8627 0.7844 -0.0175 -0.0112 0.1264  602 LYS A CG  
356  C CD  . LYS A 52  ? 1.0355 0.9175 0.8277 -0.0200 0.0021  0.1522  602 LYS A CD  
357  C CE  . LYS A 52  ? 1.1037 1.0017 0.8466 -0.0284 0.0008  0.1519  602 LYS A CE  
358  N NZ  . LYS A 52  ? 1.1556 1.0333 0.8603 -0.0292 0.0139  0.1829  602 LYS A NZ  
359  N N   . VAL A 53  ? 0.8232 0.7091 0.7348 -0.0204 0.0035  0.0723  603 VAL A N   
360  C CA  . VAL A 53  ? 0.8210 0.7128 0.7416 -0.0302 0.0113  0.0501  603 VAL A CA  
361  C C   . VAL A 53  ? 0.8328 0.7113 0.7519 -0.0413 0.0293  0.0561  603 VAL A C   
362  O O   . VAL A 53  ? 0.8322 0.6867 0.7604 -0.0417 0.0386  0.0676  603 VAL A O   
363  C CB  . VAL A 53  ? 0.8195 0.7087 0.7637 -0.0279 0.0094  0.0331  603 VAL A CB  
364  C CG1 . VAL A 53  ? 0.8180 0.7204 0.7726 -0.0364 0.0131  0.0127  603 VAL A CG1 
365  C CG2 . VAL A 53  ? 0.8188 0.7171 0.7637 -0.0176 -0.0034 0.0305  603 VAL A CG2 
366  N N   . VAL A 54  ? 0.8416 0.7335 0.7500 -0.0502 0.0370  0.0493  604 VAL A N   
367  C CA  . VAL A 54  ? 0.8584 0.7413 0.7644 -0.0628 0.0582  0.0547  604 VAL A CA  
368  C C   . VAL A 54  ? 0.8581 0.7588 0.7938 -0.0727 0.0663  0.0296  604 VAL A C   
369  O O   . VAL A 54  ? 0.8474 0.7705 0.7881 -0.0687 0.0573  0.0134  604 VAL A O   
370  C CB  . VAL A 54  ? 0.8884 0.7766 0.7528 -0.0647 0.0627  0.0679  604 VAL A CB  
371  C CG1 . VAL A 54  ? 0.9118 0.7847 0.7666 -0.0774 0.0891  0.0802  604 VAL A CG1 
372  C CG2 . VAL A 54  ? 0.9059 0.7906 0.7409 -0.0527 0.0452  0.0894  604 VAL A CG2 
373  N N   . GLU A 55  ? 0.8685 0.7602 0.8277 -0.0855 0.0834  0.0265  605 GLU A N   
374  C CA  . GLU A 55  ? 0.8720 0.7877 0.8662 -0.0963 0.0909  0.0032  605 GLU A CA  
375  C C   . GLU A 55  ? 0.8791 0.8107 0.8601 -0.1011 0.1060  0.0033  605 GLU A C   
376  O O   . GLU A 55  ? 0.8965 0.8120 0.8415 -0.1031 0.1180  0.0228  605 GLU A O   
377  C CB  . GLU A 55  ? 0.9250 0.8260 0.9501 -0.1126 0.1076  -0.0004 605 GLU A CB  
378  C CG  . GLU A 55  ? 1.0105 0.9418 1.0806 -0.1269 0.1157  -0.0248 605 GLU A CG  
379  C CD  . GLU A 55  ? 1.1561 1.0730 1.2604 -0.1472 0.1333  -0.0315 605 GLU A CD  
380  O OE1 . GLU A 55  ? 1.1742 1.1172 1.3186 -0.1627 0.1456  -0.0482 605 GLU A OE1 
381  O OE2 . GLU A 55  ? 1.2172 1.0970 1.3131 -0.1480 0.1361  -0.0211 605 GLU A OE2 
382  N N   . ALA A 56  ? 0.8660 0.8289 0.8739 -0.1015 0.1060  -0.0178 606 ALA A N   
383  C CA  . ALA A 56  ? 0.8729 0.8507 0.8729 -0.1054 0.1244  -0.0218 606 ALA A CA  
384  C C   . ALA A 56  ? 0.8555 0.8686 0.9092 -0.1094 0.1313  -0.0451 606 ALA A C   
385  O O   . ALA A 56  ? 0.8390 0.8688 0.9294 -0.1062 0.1144  -0.0580 606 ALA A O   
386  C CB  . ALA A 56  ? 0.8790 0.8571 0.8399 -0.0928 0.1129  -0.0203 606 ALA A CB  
387  N N   . THR A 57  ? 0.8532 0.8797 0.9124 -0.1166 0.1568  -0.0503 607 THR A N   
388  C CA  . THR A 57  ? 0.8313 0.8965 0.9467 -0.1172 0.1644  -0.0717 607 THR A CA  
389  C C   . THR A 57  ? 0.8429 0.9164 0.9409 -0.1031 0.1657  -0.0792 607 THR A C   
390  O O   . THR A 57  ? 0.8620 0.9203 0.9168 -0.1069 0.1844  -0.0735 607 THR A O   
391  C CB  . THR A 57  ? 0.8284 0.9046 0.9768 -0.1378 0.1985  -0.0752 607 THR A CB  
392  O OG1 . THR A 57  ? 0.8428 0.9041 1.0069 -0.1529 0.1995  -0.0692 607 THR A OG1 
393  C CG2 . THR A 57  ? 0.7901 0.9144 1.0070 -0.1366 0.2050  -0.0983 607 THR A CG2 
394  N N   . ALA A 58  ? 0.8358 0.9291 0.9616 -0.0867 0.1453  -0.0912 608 ALA A N   
395  C CA  . ALA A 58  ? 0.8510 0.9485 0.9691 -0.0727 0.1485  -0.1003 608 ALA A CA  
396  C C   . ALA A 58  ? 0.8393 0.9742 1.0188 -0.0702 0.1666  -0.1174 608 ALA A C   
397  O O   . ALA A 58  ? 0.8161 0.9817 1.0516 -0.0684 0.1554  -0.1238 608 ALA A O   
398  C CB  . ALA A 58  ? 0.8533 0.9452 0.9668 -0.0546 0.1180  -0.0994 608 ALA A CB  
399  N N   . TYR A 59  ? 0.8544 0.9892 1.0252 -0.0708 0.1950  -0.1262 609 TYR A N   
400  C CA  . TYR A 59  ? 0.8450 1.0159 1.0782 -0.0672 0.2176  -0.1430 609 TYR A CA  
401  C C   . TYR A 59  ? 0.8401 1.0196 1.0972 -0.0428 0.2116  -0.1547 609 TYR A C   
402  O O   . TYR A 59  ? 0.8624 1.0158 1.0777 -0.0381 0.2217  -0.1593 609 TYR A O   
403  C CB  . TYR A 59  ? 0.8693 1.0350 1.0832 -0.0845 0.2609  -0.1468 609 TYR A CB  
404  C CG  . TYR A 59  ? 0.9106 1.0676 1.1118 -0.1076 0.2718  -0.1330 609 TYR A CG  
405  C CD1 . TYR A 59  ? 0.9700 1.0875 1.1000 -0.1160 0.2639  -0.1130 609 TYR A CD1 
406  C CD2 . TYR A 59  ? 0.9014 1.0898 1.1667 -0.1207 0.2904  -0.1395 609 TYR A CD2 
407  C CE1 . TYR A 59  ? 0.9963 1.0998 1.1171 -0.1347 0.2748  -0.0974 609 TYR A CE1 
408  C CE2 . TYR A 59  ? 0.9295 1.1041 1.1865 -0.1432 0.3032  -0.1267 609 TYR A CE2 
409  C CZ  . TYR A 59  ? 0.9866 1.1155 1.1696 -0.1493 0.2962  -0.1045 609 TYR A CZ  
410  O OH  . TYR A 59  ? 1.0248 1.1342 1.2014 -0.1695 0.3110  -0.0893 609 TYR A OH  
411  N N   . GLY A 60  ? 0.8095 1.0247 1.1334 -0.0276 0.1946  -0.1591 610 GLY A N   
412  C CA  . GLY A 60  ? 0.8128 1.0363 1.1680 -0.0009 0.1883  -0.1657 610 GLY A CA  
413  C C   . GLY A 60  ? 0.8594 1.0498 1.1725 0.0131  0.1605  -0.1552 610 GLY A C   
414  O O   . GLY A 60  ? 0.8653 1.0358 1.1698 0.0276  0.1680  -0.1603 610 GLY A O   
415  N N   . LEU A 61  ? 0.8922 1.0749 1.1815 0.0082  0.1309  -0.1417 611 LEU A N   
416  C CA  . LEU A 61  ? 0.9383 1.0907 1.1890 0.0193  0.1067  -0.1308 611 LEU A CA  
417  C C   . LEU A 61  ? 0.9552 1.1250 1.2457 0.0458  0.0845  -0.1263 611 LEU A C   
418  O O   . LEU A 61  ? 0.9670 1.1172 1.2548 0.0630  0.0883  -0.1259 611 LEU A O   
419  C CB  . LEU A 61  ? 0.9549 1.0890 1.1616 0.0039  0.0894  -0.1188 611 LEU A CB  
420  C CG  . LEU A 61  ? 0.9902 1.0943 1.1572 0.0122  0.0672  -0.1074 611 LEU A CG  
421  C CD1 . LEU A 61  ? 1.0143 1.0887 1.1513 0.0167  0.0788  -0.1108 611 LEU A CD1 
422  C CD2 . LEU A 61  ? 1.0128 1.1005 1.1427 -0.0033 0.0573  -0.0975 611 LEU A CD2 
423  N N   . ILE A 62  ? 0.9567 1.1628 1.2846 0.0492  0.0624  -0.1234 612 ILE A N   
424  C CA  . ILE A 62  ? 0.9744 1.2015 1.3362 0.0760  0.0382  -0.1162 612 ILE A CA  
425  C C   . ILE A 62  ? 0.9759 1.2487 1.4132 0.0899  0.0494  -0.1260 612 ILE A C   
426  O O   . ILE A 62  ? 0.9755 1.2448 1.4363 0.1151  0.0545  -0.1232 612 ILE A O   
427  C CB  . ILE A 62  ? 0.9780 1.2205 1.3315 0.0741  0.0033  -0.1083 612 ILE A CB  
428  C CG1 . ILE A 62  ? 1.0254 1.2251 1.3114 0.0582  -0.0018 -0.1009 612 ILE A CG1 
429  C CG2 . ILE A 62  ? 0.9707 1.2288 1.3431 0.1040  -0.0230 -0.0963 612 ILE A CG2 
430  C CD1 . ILE A 62  ? 1.0718 1.2256 1.3134 0.0701  0.0003  -0.0897 612 ILE A CD1 
431  N N   . LYS A 63  ? 0.9697 1.2843 1.4498 0.0733  0.0562  -0.1378 613 LYS A N   
432  C CA  . LYS A 63  ? 0.9496 1.3140 1.5101 0.0838  0.0701  -0.1492 613 LYS A CA  
433  C C   . LYS A 63  ? 0.9762 1.3205 1.5312 0.0735  0.1164  -0.1616 613 LYS A C   
434  O O   . LYS A 63  ? 1.0009 1.3195 1.5096 0.0471  0.1343  -0.1646 613 LYS A O   
435  C CB  . LYS A 63  ? 0.9459 1.3669 1.5599 0.0672  0.0581  -0.1588 613 LYS A CB  
436  C CG  . LYS A 63  ? 0.9924 1.4387 1.6093 0.0739  0.0112  -0.1515 613 LYS A CG  
437  C CD  . LYS A 63  ? 0.9970 1.5130 1.6885 0.0616  -0.0016 -0.1665 613 LYS A CD  
438  C CE  . LYS A 63  ? 0.9902 1.5638 1.7737 0.0814  0.0076  -0.1740 613 LYS A CE  
439  N NZ  . LYS A 63  ? 0.9603 1.6100 1.8245 0.0691  -0.0091 -0.1900 613 LYS A NZ  
440  N N   . SER A 64  ? 0.9709 1.3265 1.5721 0.0955  0.1362  -0.1684 614 SER A N   
441  C CA  . SER A 64  ? 0.9943 1.3314 1.5931 0.0906  0.1827  -0.1838 614 SER A CA  
442  C C   . SER A 64  ? 1.0062 1.3419 1.5825 0.0564  0.2143  -0.1947 614 SER A C   
443  O O   . SER A 64  ? 1.0457 1.3408 1.5661 0.0450  0.2427  -0.2011 614 SER A O   
444  C CB  . SER A 64  ? 0.9777 1.3526 1.6628 0.1174  0.1993  -0.1929 614 SER A CB  
445  O OG  . SER A 64  ? 1.0221 1.3764 1.7035 0.1136  0.2476  -0.2109 614 SER A OG  
446  N N   . ASP A 65  ? 0.9679 1.3466 1.5861 0.0394  0.2107  -0.1970 615 ASP A N   
447  C CA  . ASP A 65  ? 0.9731 1.3467 1.5720 0.0074  0.2445  -0.2038 615 ASP A CA  
448  C C   . ASP A 65  ? 0.9557 1.3333 1.5401 -0.0182 0.2265  -0.1959 615 ASP A C   
449  O O   . ASP A 65  ? 0.9684 1.3370 1.5357 -0.0447 0.2549  -0.1974 615 ASP A O   
450  C CB  . ASP A 65  ? 0.9704 1.3889 1.6474 0.0067  0.2830  -0.2211 615 ASP A CB  
451  C CG  . ASP A 65  ? 1.0664 1.4742 1.7555 0.0300  0.3098  -0.2321 615 ASP A CG  
452  O OD1 . ASP A 65  ? 1.1168 1.4817 1.7434 0.0195  0.3431  -0.2388 615 ASP A OD1 
453  O OD2 . ASP A 65  ? 1.0757 1.5173 1.8357 0.0596  0.2970  -0.2341 615 ASP A OD2 
454  N N   . ALA A 66  ? 0.9217 1.3090 1.5102 -0.0105 0.1822  -0.1874 616 ALA A N   
455  C CA  . ALA A 66  ? 0.8953 1.2846 1.4742 -0.0341 0.1656  -0.1837 616 ALA A CA  
456  C C   . ALA A 66  ? 0.9105 1.2389 1.3986 -0.0495 0.1672  -0.1701 616 ALA A C   
457  O O   . ALA A 66  ? 0.9480 1.2384 1.3791 -0.0363 0.1571  -0.1607 616 ALA A O   
458  C CB  . ALA A 66  ? 0.8741 1.2955 1.4841 -0.0211 0.1188  -0.1824 616 ALA A CB  
459  N N   . ALA A 67  ? 0.8751 1.1954 1.3550 -0.0771 0.1802  -0.1685 617 ALA A N   
460  C CA  . ALA A 67  ? 0.8844 1.1516 1.2880 -0.0907 0.1801  -0.1531 617 ALA A CA  
461  C C   . ALA A 67  ? 0.8460 1.1112 1.2460 -0.0902 0.1420  -0.1496 617 ALA A C   
462  O O   . ALA A 67  ? 0.8178 1.1214 1.2745 -0.0971 0.1291  -0.1613 617 ALA A O   
463  C CB  . ALA A 67  ? 0.8897 1.1462 1.2903 -0.1187 0.2157  -0.1507 617 ALA A CB  
464  N N   . MET A 68  ? 0.8391 1.0626 1.1748 -0.0831 0.1242  -0.1357 618 MET A N   
465  C CA  . MET A 68  ? 0.8068 1.0242 1.1331 -0.0824 0.0921  -0.1334 618 MET A CA  
466  C C   . MET A 68  ? 0.7980 0.9642 1.0600 -0.0895 0.0921  -0.1175 618 MET A C   
467  O O   . MET A 68  ? 0.8308 0.9676 1.0461 -0.0864 0.1045  -0.1058 618 MET A O   
468  C CB  . MET A 68  ? 0.8123 1.0458 1.1443 -0.0567 0.0606  -0.1344 618 MET A CB  
469  C CG  . MET A 68  ? 0.8798 1.0779 1.1592 -0.0395 0.0589  -0.1222 618 MET A CG  
470  S SD  . MET A 68  ? 0.9382 1.1416 1.2137 -0.0123 0.0234  -0.1174 618 MET A SD  
471  C CE  . MET A 68  ? 0.8968 1.0973 1.1587 -0.0247 -0.0009 -0.1182 618 MET A CE  
472  N N   . THR A 69  ? 0.7544 0.9116 1.0156 -0.0990 0.0781  -0.1183 619 THR A N   
473  C CA  . THR A 69  ? 0.7476 0.8581 0.9571 -0.1034 0.0779  -0.1029 619 THR A CA  
474  C C   . THR A 69  ? 0.7212 0.8157 0.8921 -0.0832 0.0544  -0.0951 619 THR A C   
475  O O   . THR A 69  ? 0.7090 0.8216 0.8924 -0.0716 0.0313  -0.1027 619 THR A O   
476  C CB  . THR A 69  ? 0.7546 0.8570 0.9815 -0.1218 0.0775  -0.1092 619 THR A CB  
477  O OG1 . THR A 69  ? 0.7540 0.8734 1.0237 -0.1424 0.1025  -0.1175 619 THR A OG1 
478  C CG2 . THR A 69  ? 0.7851 0.8369 0.9654 -0.1245 0.0817  -0.0915 619 THR A CG2 
479  N N   . VAL A 70  ? 0.7093 0.7713 0.8332 -0.0794 0.0606  -0.0791 620 VAL A N   
480  C CA  . VAL A 70  ? 0.6961 0.7407 0.7850 -0.0637 0.0432  -0.0709 620 VAL A CA  
481  C C   . VAL A 70  ? 0.6974 0.7065 0.7491 -0.0678 0.0451  -0.0545 620 VAL A C   
482  O O   . VAL A 70  ? 0.7088 0.7042 0.7575 -0.0807 0.0613  -0.0469 620 VAL A O   
483  C CB  . VAL A 70  ? 0.6964 0.7456 0.7734 -0.0523 0.0476  -0.0711 620 VAL A CB  
484  C CG1 . VAL A 70  ? 0.6755 0.7556 0.7906 -0.0401 0.0405  -0.0838 620 VAL A CG1 
485  C CG2 . VAL A 70  ? 0.7049 0.7477 0.7656 -0.0628 0.0725  -0.0674 620 VAL A CG2 
486  N N   . ALA A 71  ? 0.6876 0.6822 0.7148 -0.0560 0.0298  -0.0476 621 ALA A N   
487  C CA  . ALA A 71  ? 0.6940 0.6610 0.6918 -0.0548 0.0282  -0.0315 621 ALA A CA  
488  C C   . ALA A 71  ? 0.7015 0.6670 0.6728 -0.0466 0.0242  -0.0252 621 ALA A C   
489  O O   . ALA A 71  ? 0.6966 0.6715 0.6713 -0.0377 0.0159  -0.0332 621 ALA A O   
490  C CB  . ALA A 71  ? 0.6891 0.6461 0.6889 -0.0488 0.0148  -0.0334 621 ALA A CB  
491  N N   . VAL A 72  ? 0.7136 0.6674 0.6583 -0.0502 0.0300  -0.0112 622 VAL A N   
492  C CA  . VAL A 72  ? 0.7237 0.6791 0.6417 -0.0461 0.0247  -0.0084 622 VAL A CA  
493  C C   . VAL A 72  ? 0.7313 0.6758 0.6348 -0.0401 0.0113  0.0062  622 VAL A C   
494  O O   . VAL A 72  ? 0.7264 0.6589 0.6198 -0.0414 0.0132  0.0233  622 VAL A O   
495  C CB  . VAL A 72  ? 0.7427 0.7012 0.6362 -0.0549 0.0398  -0.0068 622 VAL A CB  
496  C CG1 . VAL A 72  ? 0.7558 0.7189 0.6221 -0.0531 0.0333  -0.0120 622 VAL A CG1 
497  C CG2 . VAL A 72  ? 0.7387 0.7105 0.6559 -0.0608 0.0573  -0.0211 622 VAL A CG2 
498  N N   . LYS A 73  ? 0.7444 0.6930 0.6506 -0.0329 -0.0007 0.0003  623 LYS A N   
499  C CA  . LYS A 73  ? 0.7586 0.7046 0.6595 -0.0274 -0.0131 0.0106  623 LYS A CA  
500  C C   . LYS A 73  ? 0.7831 0.7389 0.6583 -0.0320 -0.0176 0.0118  623 LYS A C   
501  O O   . LYS A 73  ? 0.7814 0.7438 0.6496 -0.0362 -0.0142 -0.0035 623 LYS A O   
502  C CB  . LYS A 73  ? 0.7731 0.7200 0.6897 -0.0206 -0.0197 0.0017  623 LYS A CB  
503  C CG  . LYS A 73  ? 0.8407 0.7809 0.7686 -0.0138 -0.0254 0.0113  623 LYS A CG  
504  C CD  . LYS A 73  ? 0.9081 0.8575 0.8334 -0.0123 -0.0355 0.0211  623 LYS A CD  
505  C CE  . LYS A 73  ? 0.9514 0.8949 0.8935 -0.0038 -0.0375 0.0344  623 LYS A CE  
506  N NZ  . LYS A 73  ? 0.9713 0.9088 0.9308 0.0013  -0.0334 0.0266  623 LYS A NZ  
507  N N   . MET A 74  ? 0.8074 0.7639 0.6680 -0.0308 -0.0254 0.0295  624 MET A N   
508  C CA  . MET A 74  ? 0.8334 0.8034 0.6636 -0.0356 -0.0344 0.0316  624 MET A CA  
509  C C   . MET A 74  ? 0.8412 0.8185 0.6715 -0.0280 -0.0517 0.0525  624 MET A C   
510  O O   . MET A 74  ? 0.8317 0.7986 0.6851 -0.0188 -0.0513 0.0660  624 MET A O   
511  C CB  . MET A 74  ? 0.8645 0.8303 0.6620 -0.0436 -0.0207 0.0355  624 MET A CB  
512  C CG  . MET A 74  ? 0.9163 0.8662 0.7115 -0.0406 -0.0131 0.0595  624 MET A CG  
513  S SD  . MET A 74  ? 1.0746 1.0181 0.8289 -0.0518 0.0076  0.0657  624 MET A SD  
514  C CE  . MET A 74  ? 1.0495 0.9893 0.8388 -0.0579 0.0290  0.0449  624 MET A CE  
515  N N   . LEU A 75  ? 0.8613 0.8578 0.6669 -0.0316 -0.0667 0.0543  625 LEU A N   
516  C CA  . LEU A 75  ? 0.8772 0.8886 0.6850 -0.0227 -0.0869 0.0758  625 LEU A CA  
517  C C   . LEU A 75  ? 0.9202 0.9297 0.6851 -0.0214 -0.0895 0.1000  625 LEU A C   
518  O O   . LEU A 75  ? 0.9361 0.9389 0.6630 -0.0314 -0.0771 0.0942  625 LEU A O   
519  C CB  . LEU A 75  ? 0.8612 0.9028 0.6764 -0.0276 -0.1074 0.0615  625 LEU A CB  
520  C CG  . LEU A 75  ? 0.8634 0.9057 0.7208 -0.0288 -0.1040 0.0419  625 LEU A CG  
521  C CD1 . LEU A 75  ? 0.8621 0.9351 0.7297 -0.0366 -0.1232 0.0286  625 LEU A CD1 
522  C CD2 . LEU A 75  ? 0.8522 0.8836 0.7486 -0.0151 -0.0992 0.0555  625 LEU A CD2 
523  N N   . LYS A 76  ? 0.9364 0.9511 0.7077 -0.0076 -0.1040 0.1287  626 LYS A N   
524  C CA  . LYS A 76  ? 0.9809 0.9931 0.7092 -0.0026 -0.1093 0.1589  626 LYS A CA  
525  C C   . LYS A 76  ? 1.0142 1.0639 0.7057 -0.0078 -0.1368 0.1555  626 LYS A C   
526  O O   . LYS A 76  ? 0.9930 1.0713 0.7096 -0.0116 -0.1543 0.1350  626 LYS A O   
527  C CB  . LYS A 76  ? 0.9899 0.9893 0.7460 0.0178  -0.1130 0.1932  626 LYS A CB  
528  C CG  . LYS A 76  ? 1.0188 0.9846 0.8173 0.0211  -0.0888 0.1890  626 LYS A CG  
529  C CD  . LYS A 76  ? 1.0805 1.0090 0.8718 0.0283  -0.0706 0.2180  626 LYS A CD  
530  C CE  . LYS A 76  ? 1.1298 1.0507 0.9556 0.0504  -0.0780 0.2459  626 LYS A CE  
531  N NZ  . LYS A 76  ? 1.1778 1.0505 1.0111 0.0551  -0.0518 0.2660  626 LYS A NZ  
532  N N   . PRO A 77  ? 1.0666 1.1173 0.6970 -0.0095 -0.1407 0.1739  627 PRO A N   
533  C CA  . PRO A 77  ? 1.0925 1.1820 0.6815 -0.0162 -0.1696 0.1674  627 PRO A CA  
534  C C   . PRO A 77  ? 1.1005 1.2307 0.7258 -0.0037 -0.2067 0.1778  627 PRO A C   
535  O O   . PRO A 77  ? 1.0966 1.2666 0.7068 -0.0133 -0.2332 0.1605  627 PRO A O   
536  C CB  . PRO A 77  ? 1.1256 1.2025 0.6404 -0.0154 -0.1645 0.1957  627 PRO A CB  
537  C CG  . PRO A 77  ? 1.1278 1.1618 0.6599 -0.0028 -0.1388 0.2271  627 PRO A CG  
538  C CD  . PRO A 77  ? 1.0900 1.1064 0.6827 -0.0079 -0.1172 0.1998  627 PRO A CD  
539  N N   . SER A 78  ? 1.1030 1.2246 0.7818 0.0165  -0.2071 0.2025  628 SER A N   
540  C CA  . SER A 78  ? 1.0970 1.2570 0.8247 0.0318  -0.2374 0.2145  628 SER A CA  
541  C C   . SER A 78  ? 1.0883 1.2706 0.8771 0.0225  -0.2403 0.1788  628 SER A C   
542  O O   . SER A 78  ? 1.0696 1.2879 0.9078 0.0326  -0.2625 0.1841  628 SER A O   
543  C CB  . SER A 78  ? 1.1128 1.2496 0.8752 0.0580  -0.2307 0.2537  628 SER A CB  
544  O OG  . SER A 78  ? 1.1488 1.2462 0.9519 0.0578  -0.1983 0.2421  628 SER A OG  
545  N N   . ALA A 79  ? 1.0959 1.2570 0.8846 0.0047  -0.2167 0.1449  629 ALA A N   
546  C CA  . ALA A 79  ? 1.0799 1.2544 0.9206 -0.0041 -0.2150 0.1145  629 ALA A CA  
547  C C   . ALA A 79  ? 1.0739 1.2902 0.9055 -0.0224 -0.2386 0.0873  629 ALA A C   
548  O O   . ALA A 79  ? 1.0982 1.3150 0.8733 -0.0371 -0.2406 0.0735  629 ALA A O   
549  C CB  . ALA A 79  ? 1.0915 1.2258 0.9360 -0.0127 -0.1818 0.0934  629 ALA A CB  
550  N N   . HIS A 80  ? 1.0381 1.2894 0.9273 -0.0231 -0.2544 0.0774  630 HIS A N   
551  C CA  . HIS A 80  ? 1.0196 1.3129 0.9147 -0.0435 -0.2764 0.0475  630 HIS A CA  
552  C C   . HIS A 80  ? 1.0115 1.2794 0.9057 -0.0659 -0.2518 0.0075  630 HIS A C   
553  O O   . HIS A 80  ? 1.0314 1.2542 0.9214 -0.0631 -0.2210 0.0058  630 HIS A O   
554  C CB  . HIS A 80  ? 1.0042 1.3456 0.9720 -0.0365 -0.2988 0.0521  630 HIS A CB  
555  C CG  . HIS A 80  ? 1.0585 1.4514 1.0180 -0.0254 -0.3399 0.0757  630 HIS A CG  
556  N ND1 . HIS A 80  ? 1.1050 1.4852 1.0266 -0.0028 -0.3460 0.1164  630 HIS A ND1 
557  C CD2 . HIS A 80  ? 1.0496 1.5066 1.0356 -0.0336 -0.3767 0.0649  630 HIS A CD2 
558  C CE1 . HIS A 80  ? 1.0948 1.5309 1.0174 0.0045  -0.3872 0.1318  630 HIS A CE1 
559  N NE2 . HIS A 80  ? 1.0622 1.5496 1.0246 -0.0137 -0.4089 0.1008  630 HIS A NE2 
560  N N   . LEU A 81  ? 0.9796 1.2766 0.8790 -0.0878 -0.2659 -0.0244 631 LEU A N   
561  C CA  . LEU A 81  ? 0.9718 1.2439 0.8733 -0.1088 -0.2432 -0.0621 631 LEU A CA  
562  C C   . LEU A 81  ? 0.9418 1.1879 0.9015 -0.1043 -0.2170 -0.0642 631 LEU A C   
563  O O   . LEU A 81  ? 0.9597 1.1624 0.9087 -0.1068 -0.1882 -0.0751 631 LEU A O   
564  C CB  . LEU A 81  ? 0.9599 1.2714 0.8612 -0.1350 -0.2657 -0.0971 631 LEU A CB  
565  C CG  . LEU A 81  ? 0.9787 1.2637 0.8886 -0.1588 -0.2421 -0.1387 631 LEU A CG  
566  C CD1 . LEU A 81  ? 1.0249 1.2569 0.8835 -0.1582 -0.2112 -0.1459 631 LEU A CD1 
567  C CD2 . LEU A 81  ? 0.9686 1.2921 0.8734 -0.1857 -0.2655 -0.1738 631 LEU A CD2 
568  N N   . THR A 82  ? 0.8950 1.1679 0.9153 -0.0959 -0.2260 -0.0522 632 THR A N   
569  C CA  . THR A 82  ? 0.8749 1.1232 0.9451 -0.0924 -0.1991 -0.0539 632 THR A CA  
570  C C   . THR A 82  ? 0.8711 1.0711 0.9226 -0.0741 -0.1733 -0.0344 632 THR A C   
571  O O   . THR A 82  ? 0.8794 1.0498 0.9508 -0.0736 -0.1484 -0.0399 632 THR A O   
572  C CB  . THR A 82  ? 0.8613 1.1495 1.0026 -0.0879 -0.2097 -0.0467 632 THR A CB  
573  O OG1 . THR A 82  ? 0.8808 1.1712 1.0349 -0.0615 -0.2123 -0.0131 632 THR A OG1 
574  C CG2 . THR A 82  ? 0.8400 1.1883 1.0031 -0.1039 -0.2430 -0.0624 632 THR A CG2 
575  N N   . GLU A 83  ? 0.8567 1.0490 0.8697 -0.0602 -0.1791 -0.0120 633 GLU A N   
576  C CA  . GLU A 83  ? 0.8552 1.0052 0.8530 -0.0464 -0.1561 0.0027  633 GLU A CA  
577  C C   . GLU A 83  ? 0.8534 0.9713 0.8101 -0.0559 -0.1386 -0.0139 633 GLU A C   
578  O O   . GLU A 83  ? 0.8524 0.9381 0.8131 -0.0510 -0.1166 -0.0151 633 GLU A O   
579  C CB  . GLU A 83  ? 0.8926 1.0441 0.8761 -0.0283 -0.1652 0.0341  633 GLU A CB  
580  C CG  . GLU A 83  ? 0.9583 1.1257 0.9942 -0.0120 -0.1701 0.0527  633 GLU A CG  
581  C CD  . GLU A 83  ? 1.0788 1.2975 1.1344 -0.0089 -0.2022 0.0626  633 GLU A CD  
582  O OE1 . GLU A 83  ? 1.1259 1.3571 1.1397 -0.0071 -0.2215 0.0755  633 GLU A OE1 
583  O OE2 . GLU A 83  ? 1.0922 1.3409 1.2049 -0.0080 -0.2081 0.0583  633 GLU A OE2 
584  N N   . ARG A 84  ? 0.8502 0.9790 0.7678 -0.0689 -0.1485 -0.0275 634 ARG A N   
585  C CA  . ARG A 84  ? 0.8640 0.9665 0.7460 -0.0783 -0.1307 -0.0464 634 ARG A CA  
586  C C   . ARG A 84  ? 0.8499 0.9337 0.7605 -0.0870 -0.1132 -0.0703 634 ARG A C   
587  O O   . ARG A 84  ? 0.8645 0.9169 0.7690 -0.0837 -0.0915 -0.0755 634 ARG A O   
588  C CB  . ARG A 84  ? 0.8905 1.0118 0.7246 -0.0921 -0.1448 -0.0592 634 ARG A CB  
589  C CG  . ARG A 84  ? 0.9442 1.0812 0.7438 -0.0823 -0.1616 -0.0308 634 ARG A CG  
590  C CD  . ARG A 84  ? 1.0142 1.1594 0.7499 -0.0948 -0.1676 -0.0419 634 ARG A CD  
591  N NE  . ARG A 84  ? 1.0687 1.2515 0.7981 -0.1108 -0.1936 -0.0629 634 ARG A NE  
592  C CZ  . ARG A 84  ? 1.1010 1.3240 0.8179 -0.1077 -0.2268 -0.0466 634 ARG A CZ  
593  N NH1 . ARG A 84  ? 1.1101 1.3353 0.8202 -0.0871 -0.2354 -0.0062 634 ARG A NH1 
594  N NH2 . ARG A 84  ? 1.0760 1.3376 0.7896 -0.1249 -0.2522 -0.0706 634 ARG A NH2 
595  N N   . GLU A 85  ? 0.8140 0.9177 0.7597 -0.0972 -0.1220 -0.0827 635 GLU A N   
596  C CA  . GLU A 85  ? 0.8093 0.8917 0.7849 -0.1054 -0.1031 -0.1012 635 GLU A CA  
597  C C   . GLU A 85  ? 0.7922 0.8496 0.7909 -0.0887 -0.0855 -0.0826 635 GLU A C   
598  O O   . GLU A 85  ? 0.8162 0.8404 0.8125 -0.0862 -0.0648 -0.0882 635 GLU A O   
599  C CB  . GLU A 85  ? 0.8382 0.9505 0.8519 -0.1222 -0.1155 -0.1177 635 GLU A CB  
600  C CG  . GLU A 85  ? 0.9364 1.0769 0.9249 -0.1420 -0.1358 -0.1415 635 GLU A CG  
601  C CD  . GLU A 85  ? 1.0830 1.1922 1.0362 -0.1543 -0.1181 -0.1686 635 GLU A CD  
602  O OE1 . GLU A 85  ? 1.1028 1.1808 1.0796 -0.1610 -0.0949 -0.1847 635 GLU A OE1 
603  O OE2 . GLU A 85  ? 1.1416 1.2550 1.0437 -0.1560 -0.1249 -0.1724 635 GLU A OE2 
604  N N   . ALA A 86  ? 0.7532 0.8251 0.7704 -0.0757 -0.0935 -0.0602 636 ALA A N   
605  C CA  . ALA A 86  ? 0.7384 0.7874 0.7713 -0.0608 -0.0769 -0.0450 636 ALA A CA  
606  C C   . ALA A 86  ? 0.7370 0.7567 0.7375 -0.0506 -0.0654 -0.0385 636 ALA A C   
607  O O   . ALA A 86  ? 0.7548 0.7499 0.7600 -0.0439 -0.0493 -0.0368 636 ALA A O   
608  C CB  . ALA A 86  ? 0.7280 0.7980 0.7873 -0.0494 -0.0861 -0.0257 636 ALA A CB  
609  N N   . LEU A 87  ? 0.7140 0.7373 0.6817 -0.0508 -0.0726 -0.0363 637 LEU A N   
610  C CA  . LEU A 87  ? 0.7092 0.7100 0.6541 -0.0440 -0.0604 -0.0334 637 LEU A CA  
611  C C   . LEU A 87  ? 0.7170 0.6980 0.6577 -0.0485 -0.0456 -0.0516 637 LEU A C   
612  O O   . LEU A 87  ? 0.7184 0.6803 0.6610 -0.0394 -0.0336 -0.0489 637 LEU A O   
613  C CB  . LEU A 87  ? 0.7031 0.7123 0.6165 -0.0448 -0.0676 -0.0259 637 LEU A CB  
614  C CG  . LEU A 87  ? 0.7205 0.7118 0.6178 -0.0401 -0.0540 -0.0233 637 LEU A CG  
615  C CD1 . LEU A 87  ? 0.7115 0.6897 0.6274 -0.0284 -0.0480 -0.0110 637 LEU A CD1 
616  C CD2 . LEU A 87  ? 0.7427 0.7410 0.6068 -0.0437 -0.0571 -0.0156 637 LEU A CD2 
617  N N   . MET A 88  ? 0.7154 0.7015 0.6539 -0.0621 -0.0469 -0.0707 638 MET A N   
618  C CA  . MET A 88  ? 0.7213 0.6848 0.6613 -0.0662 -0.0306 -0.0892 638 MET A CA  
619  C C   . MET A 88  ? 0.7102 0.6531 0.6779 -0.0590 -0.0188 -0.0834 638 MET A C   
620  O O   . MET A 88  ? 0.7050 0.6248 0.6730 -0.0491 -0.0053 -0.0818 638 MET A O   
621  C CB  . MET A 88  ? 0.7346 0.7073 0.6686 -0.0854 -0.0345 -0.1138 638 MET A CB  
622  C CG  . MET A 88  ? 0.7906 0.7359 0.7240 -0.0901 -0.0146 -0.1358 638 MET A CG  
623  S SD  . MET A 88  ? 0.8976 0.8300 0.8067 -0.0788 -0.0004 -0.1360 638 MET A SD  
624  C CE  . MET A 88  ? 0.8860 0.7829 0.8252 -0.0640 0.0205  -0.1335 638 MET A CE  
625  N N   . SER A 89  ? 0.7009 0.6546 0.6916 -0.0619 -0.0241 -0.0771 639 SER A N   
626  C CA  . SER A 89  ? 0.7079 0.6427 0.7206 -0.0563 -0.0106 -0.0694 639 SER A CA  
627  C C   . SER A 89  ? 0.7162 0.6384 0.7189 -0.0382 -0.0061 -0.0509 639 SER A C   
628  O O   . SER A 89  ? 0.7298 0.6279 0.7336 -0.0301 0.0073  -0.0453 639 SER A O   
629  C CB  . SER A 89  ? 0.7224 0.6779 0.7651 -0.0647 -0.0159 -0.0682 639 SER A CB  
630  O OG  . SER A 89  ? 0.7723 0.7296 0.8331 -0.0833 -0.0128 -0.0885 639 SER A OG  
631  N N   . GLU A 90  ? 0.7045 0.6416 0.6952 -0.0321 -0.0172 -0.0417 640 GLU A N   
632  C CA  . GLU A 90  ? 0.7049 0.6322 0.6858 -0.0184 -0.0143 -0.0294 640 GLU A CA  
633  C C   . GLU A 90  ? 0.7030 0.6170 0.6703 -0.0124 -0.0090 -0.0337 640 GLU A C   
634  O O   . GLU A 90  ? 0.7112 0.6117 0.6754 -0.0016 -0.0036 -0.0273 640 GLU A O   
635  C CB  . GLU A 90  ? 0.7357 0.6790 0.7123 -0.0161 -0.0251 -0.0203 640 GLU A CB  
636  C CG  . GLU A 90  ? 0.8286 0.7843 0.8269 -0.0160 -0.0284 -0.0129 640 GLU A CG  
637  C CD  . GLU A 90  ? 0.9730 0.9397 0.9737 -0.0101 -0.0365 -0.0006 640 GLU A CD  
638  O OE1 . GLU A 90  ? 0.9965 0.9669 0.9798 -0.0108 -0.0434 0.0026  640 GLU A OE1 
639  O OE2 . GLU A 90  ? 1.0164 0.9857 1.0377 -0.0044 -0.0330 0.0065  640 GLU A OE2 
640  N N   . LEU A 91  ? 0.6934 0.6130 0.6529 -0.0189 -0.0101 -0.0449 641 LEU A N   
641  C CA  . LEU A 91  ? 0.7021 0.6130 0.6573 -0.0128 -0.0027 -0.0508 641 LEU A CA  
642  C C   . LEU A 91  ? 0.7221 0.6094 0.6879 -0.0059 0.0090  -0.0522 641 LEU A C   
643  O O   . LEU A 91  ? 0.7383 0.6177 0.7059 0.0076  0.0125  -0.0468 641 LEU A O   
644  C CB  . LEU A 91  ? 0.7043 0.6241 0.6486 -0.0234 -0.0016 -0.0654 641 LEU A CB  
645  C CG  . LEU A 91  ? 0.7251 0.6364 0.6710 -0.0190 0.0109  -0.0769 641 LEU A CG  
646  C CD1 . LEU A 91  ? 0.7279 0.6449 0.6806 -0.0057 0.0110  -0.0676 641 LEU A CD1 
647  C CD2 . LEU A 91  ? 0.7414 0.6622 0.6690 -0.0318 0.0139  -0.0923 641 LEU A CD2 
648  N N   . LYS A 92  ? 0.7181 0.5948 0.6935 -0.0149 0.0147  -0.0577 642 LYS A N   
649  C CA  . LYS A 92  ? 0.7232 0.5707 0.7094 -0.0099 0.0298  -0.0567 642 LYS A CA  
650  C C   . LYS A 92  ? 0.7310 0.5665 0.7140 0.0038  0.0322  -0.0361 642 LYS A C   
651  O O   . LYS A 92  ? 0.7442 0.5570 0.7263 0.0170  0.0412  -0.0273 642 LYS A O   
652  C CB  . LYS A 92  ? 0.7270 0.5674 0.7277 -0.0277 0.0368  -0.0705 642 LYS A CB  
653  C CG  . LYS A 92  ? 0.7413 0.5895 0.7389 -0.0424 0.0358  -0.0946 642 LYS A CG  
654  C CD  . LYS A 92  ? 0.7724 0.6164 0.7874 -0.0622 0.0407  -0.1108 642 LYS A CD  
655  C CE  . LYS A 92  ? 0.8168 0.6715 0.8227 -0.0799 0.0373  -0.1384 642 LYS A CE  
656  N NZ  . LYS A 92  ? 0.8563 0.7134 0.8833 -0.1024 0.0384  -0.1569 642 LYS A NZ  
657  N N   . VAL A 93  ? 0.7271 0.5769 0.7065 0.0019  0.0249  -0.0282 643 VAL A N   
658  C CA  . VAL A 93  ? 0.7437 0.5833 0.7126 0.0136  0.0282  -0.0116 643 VAL A CA  
659  C C   . VAL A 93  ? 0.7500 0.5946 0.7028 0.0284  0.0190  -0.0058 643 VAL A C   
660  O O   . VAL A 93  ? 0.7565 0.5859 0.6980 0.0423  0.0223  0.0057  643 VAL A O   
661  C CB  . VAL A 93  ? 0.7487 0.6021 0.7208 0.0081  0.0257  -0.0078 643 VAL A CB  
662  C CG1 . VAL A 93  ? 0.7774 0.6208 0.7299 0.0202  0.0295  0.0053  643 VAL A CG1 
663  C CG2 . VAL A 93  ? 0.7365 0.5901 0.7329 -0.0056 0.0349  -0.0124 643 VAL A CG2 
664  N N   . LEU A 94  ? 0.7422 0.6091 0.6948 0.0252  0.0075  -0.0131 644 LEU A N   
665  C CA  . LEU A 94  ? 0.7443 0.6222 0.6906 0.0354  -0.0014 -0.0115 644 LEU A CA  
666  C C   . LEU A 94  ? 0.7601 0.6301 0.7132 0.0477  0.0019  -0.0105 644 LEU A C   
667  O O   . LEU A 94  ? 0.7619 0.6351 0.7098 0.0620  -0.0048 -0.0023 644 LEU A O   
668  C CB  . LEU A 94  ? 0.7291 0.6286 0.6790 0.0266  -0.0087 -0.0201 644 LEU A CB  
669  C CG  . LEU A 94  ? 0.7500 0.6571 0.6950 0.0199  -0.0136 -0.0173 644 LEU A CG  
670  C CD1 . LEU A 94  ? 0.7508 0.6736 0.6976 0.0145  -0.0187 -0.0218 644 LEU A CD1 
671  C CD2 . LEU A 94  ? 0.7563 0.6557 0.6897 0.0275  -0.0144 -0.0102 644 LEU A CD2 
672  N N   . SER A 95  ? 0.7667 0.6267 0.7321 0.0427  0.0120  -0.0196 645 SER A N   
673  C CA  . SER A 95  ? 0.7773 0.6244 0.7554 0.0552  0.0200  -0.0200 645 SER A CA  
674  C C   . SER A 95  ? 0.7964 0.6148 0.7688 0.0697  0.0269  -0.0019 645 SER A C   
675  O O   . SER A 95  ? 0.8000 0.6150 0.7756 0.0895  0.0244  0.0094  645 SER A O   
676  C CB  . SER A 95  ? 0.7951 0.6335 0.7842 0.0428  0.0324  -0.0381 645 SER A CB  
677  O OG  . SER A 95  ? 0.8537 0.6762 0.8591 0.0561  0.0438  -0.0401 645 SER A OG  
678  N N   . TYR A 96  ? 0.8005 0.6004 0.7654 0.0603  0.0357  0.0026  646 TYR A N   
679  C CA  . TYR A 96  ? 0.8207 0.5903 0.7751 0.0707  0.0466  0.0217  646 TYR A CA  
680  C C   . TYR A 96  ? 0.8464 0.6251 0.7746 0.0863  0.0338  0.0391  646 TYR A C   
681  O O   . TYR A 96  ? 0.8728 0.6320 0.7880 0.1044  0.0367  0.0584  646 TYR A O   
682  C CB  . TYR A 96  ? 0.8220 0.5770 0.7796 0.0530  0.0605  0.0196  646 TYR A CB  
683  C CG  . TYR A 96  ? 0.8480 0.5790 0.7866 0.0602  0.0721  0.0409  646 TYR A CG  
684  C CD1 . TYR A 96  ? 0.8741 0.5654 0.8123 0.0692  0.0909  0.0560  646 TYR A CD1 
685  C CD2 . TYR A 96  ? 0.8579 0.6024 0.7768 0.0587  0.0671  0.0466  646 TYR A CD2 
686  C CE1 . TYR A 96  ? 0.8992 0.5656 0.8142 0.0754  0.1048  0.0781  646 TYR A CE1 
687  C CE2 . TYR A 96  ? 0.8858 0.6078 0.7804 0.0657  0.0803  0.0657  646 TYR A CE2 
688  C CZ  . TYR A 96  ? 0.9197 0.6029 0.8104 0.0735  0.0994  0.0825  646 TYR A CZ  
689  O OH  . TYR A 96  ? 0.9631 0.6213 0.8246 0.0795  0.1158  0.1038  646 TYR A OH  
690  N N   . LEU A 97  ? 0.8442 0.6494 0.7617 0.0792  0.0206  0.0330  647 LEU A N   
691  C CA  . LEU A 97  ? 0.8571 0.6706 0.7464 0.0901  0.0089  0.0439  647 LEU A CA  
692  C C   . LEU A 97  ? 0.8629 0.6899 0.7515 0.1089  -0.0063 0.0505  647 LEU A C   
693  O O   . LEU A 97  ? 0.8867 0.7068 0.7492 0.1245  -0.0117 0.0675  647 LEU A O   
694  C CB  . LEU A 97  ? 0.8511 0.6868 0.7340 0.0777  0.0003  0.0324  647 LEU A CB  
695  C CG  . LEU A 97  ? 0.8590 0.6844 0.7423 0.0644  0.0140  0.0307  647 LEU A CG  
696  C CD1 . LEU A 97  ? 0.8507 0.6966 0.7379 0.0540  0.0065  0.0192  647 LEU A CD1 
697  C CD2 . LEU A 97  ? 0.8780 0.6791 0.7349 0.0708  0.0274  0.0461  647 LEU A CD2 
698  N N   . GLY A 98  ? 0.8394 0.6852 0.7572 0.1088  -0.0116 0.0384  648 GLY A N   
699  C CA  . GLY A 98  ? 0.8234 0.6904 0.7524 0.1269  -0.0266 0.0428  648 GLY A CA  
700  C C   . GLY A 98  ? 0.8088 0.7117 0.7308 0.1224  -0.0471 0.0341  648 GLY A C   
701  O O   . GLY A 98  ? 0.8066 0.7128 0.7162 0.1059  -0.0467 0.0245  648 GLY A O   
702  N N   . ASN A 99  ? 0.7937 0.7236 0.7267 0.1375  -0.0648 0.0372  649 ASN A N   
703  C CA  . ASN A 99  ? 0.7846 0.7530 0.7209 0.1316  -0.0849 0.0248  649 ASN A CA  
704  C C   . ASN A 99  ? 0.7954 0.7701 0.6917 0.1375  -0.1024 0.0318  649 ASN A C   
705  O O   . ASN A 99  ? 0.8101 0.7763 0.6845 0.1576  -0.1094 0.0520  649 ASN A O   
706  C CB  . ASN A 99  ? 0.7785 0.7819 0.7590 0.1427  -0.0953 0.0201  649 ASN A CB  
707  C CG  . ASN A 99  ? 0.8106 0.8574 0.8116 0.1306  -0.1111 0.0015  649 ASN A CG  
708  O OD1 . ASN A 99  ? 0.8342 0.9066 0.8239 0.1351  -0.1340 0.0011  649 ASN A OD1 
709  N ND2 . ASN A 99  ? 0.7949 0.8514 0.8263 0.1145  -0.0988 -0.0147 649 ASN A ND2 
710  N N   . HIS A 100 ? 0.7837 0.7741 0.6702 0.1204  -0.1097 0.0148  650 HIS A N   
711  C CA  . HIS A 100 ? 0.7919 0.7936 0.6406 0.1220  -0.1274 0.0133  650 HIS A CA  
712  C C   . HIS A 100 ? 0.7836 0.8164 0.6500 0.1028  -0.1386 -0.0130 650 HIS A C   
713  O O   . HIS A 100 ? 0.7804 0.8060 0.6659 0.0852  -0.1243 -0.0255 650 HIS A O   
714  C CB  . HIS A 100 ? 0.8273 0.7917 0.6267 0.1187  -0.1125 0.0212  650 HIS A CB  
715  C CG  . HIS A 100 ? 0.8720 0.8448 0.6238 0.1202  -0.1279 0.0180  650 HIS A CG  
716  N ND1 . HIS A 100 ? 0.9212 0.8896 0.6324 0.1404  -0.1385 0.0392  650 HIS A ND1 
717  C CD2 . HIS A 100 ? 0.8961 0.8785 0.6324 0.1035  -0.1328 -0.0045 650 HIS A CD2 
718  C CE1 . HIS A 100 ? 0.9425 0.9220 0.6110 0.1346  -0.1516 0.0274  650 HIS A CE1 
719  N NE2 . HIS A 100 ? 0.9291 0.9174 0.6139 0.1118  -0.1484 -0.0012 650 HIS A NE2 
720  N N   . MET A 101 ? 0.7867 0.8537 0.6470 0.1057  -0.1643 -0.0209 651 MET A N   
721  C CA  . MET A 101 ? 0.7845 0.8810 0.6633 0.0852  -0.1751 -0.0487 651 MET A CA  
722  C C   . MET A 101 ? 0.7930 0.8595 0.6535 0.0627  -0.1558 -0.0641 651 MET A C   
723  O O   . MET A 101 ? 0.7769 0.8496 0.6693 0.0442  -0.1486 -0.0812 651 MET A O   
724  C CB  . MET A 101 ? 0.8017 0.9351 0.6598 0.0918  -0.2078 -0.0549 651 MET A CB  
725  C CG  . MET A 101 ? 0.8555 1.0195 0.7306 0.0678  -0.2204 -0.0877 651 MET A CG  
726  S SD  . MET A 101 ? 0.9957 1.1934 0.9552 0.0520  -0.2152 -0.1047 651 MET A SD  
727  C CE  . MET A 101 ? 0.9690 1.2158 0.9678 0.0803  -0.2398 -0.0879 651 MET A CE  
728  N N   . ASN A 102 ? 0.8110 0.8434 0.6230 0.0659  -0.1447 -0.0558 652 ASN A N   
729  C CA  . ASN A 102 ? 0.8165 0.8217 0.6120 0.0493  -0.1266 -0.0690 652 ASN A CA  
730  C C   . ASN A 102 ? 0.8022 0.7753 0.6113 0.0463  -0.0999 -0.0586 652 ASN A C   
731  O O   . ASN A 102 ? 0.8164 0.7633 0.6063 0.0405  -0.0835 -0.0615 652 ASN A O   
732  C CB  . ASN A 102 ? 0.8656 0.8573 0.6016 0.0522  -0.1289 -0.0716 652 ASN A CB  
733  C CG  . ASN A 102 ? 0.9018 0.9296 0.6227 0.0499  -0.1583 -0.0888 652 ASN A CG  
734  O OD1 . ASN A 102 ? 0.9290 0.9670 0.6089 0.0648  -0.1757 -0.0778 652 ASN A OD1 
735  N ND2 . ASN A 102 ? 0.8911 0.9403 0.6464 0.0306  -0.1651 -0.1154 652 ASN A ND2 
736  N N   . ILE A 103 ? 0.7767 0.7543 0.6209 0.0496  -0.0957 -0.0489 653 ILE A N   
737  C CA  . ILE A 103 ? 0.7614 0.7177 0.6229 0.0436  -0.0755 -0.0431 653 ILE A CA  
738  C C   . ILE A 103 ? 0.7128 0.6869 0.6156 0.0344  -0.0755 -0.0501 653 ILE A C   
739  O O   . ILE A 103 ? 0.6811 0.6832 0.6047 0.0370  -0.0881 -0.0549 653 ILE A O   
740  C CB  . ILE A 103 ? 0.7881 0.7222 0.6405 0.0544  -0.0632 -0.0240 653 ILE A CB  
741  C CG1 . ILE A 103 ? 0.8008 0.7444 0.6753 0.0642  -0.0668 -0.0152 653 ILE A CG1 
742  C CG2 . ILE A 103 ? 0.8182 0.7337 0.6284 0.0638  -0.0596 -0.0143 653 ILE A CG2 
743  C CD1 . ILE A 103 ? 0.8303 0.7531 0.7157 0.0635  -0.0499 -0.0063 653 ILE A CD1 
744  N N   . VAL A 104 ? 0.7024 0.6621 0.6175 0.0242  -0.0609 -0.0498 654 VAL A N   
745  C CA  . VAL A 104 ? 0.6870 0.6588 0.6322 0.0158  -0.0571 -0.0528 654 VAL A CA  
746  C C   . VAL A 104 ? 0.6893 0.6627 0.6412 0.0257  -0.0545 -0.0427 654 VAL A C   
747  O O   . VAL A 104 ? 0.7083 0.6629 0.6505 0.0280  -0.0458 -0.0337 654 VAL A O   
748  C CB  . VAL A 104 ? 0.6915 0.6465 0.6414 0.0042  -0.0440 -0.0517 654 VAL A CB  
749  C CG1 . VAL A 104 ? 0.6837 0.6492 0.6553 -0.0034 -0.0381 -0.0513 654 VAL A CG1 
750  C CG2 . VAL A 104 ? 0.6970 0.6438 0.6438 -0.0052 -0.0426 -0.0631 654 VAL A CG2 
751  N N   . ASN A 105 ? 0.6648 0.6610 0.6355 0.0325  -0.0622 -0.0454 655 ASN A N   
752  C CA  . ASN A 105 ? 0.6547 0.6497 0.6342 0.0444  -0.0582 -0.0380 655 ASN A CA  
753  C C   . ASN A 105 ? 0.6439 0.6389 0.6401 0.0369  -0.0447 -0.0414 655 ASN A C   
754  O O   . ASN A 105 ? 0.6330 0.6428 0.6458 0.0259  -0.0411 -0.0496 655 ASN A O   
755  C CB  . ASN A 105 ? 0.6410 0.6609 0.6373 0.0593  -0.0718 -0.0375 655 ASN A CB  
756  C CG  . ASN A 105 ? 0.6835 0.6989 0.6517 0.0715  -0.0854 -0.0289 655 ASN A CG  
757  O OD1 . ASN A 105 ? 0.7418 0.7302 0.6855 0.0806  -0.0793 -0.0154 655 ASN A OD1 
758  N ND2 . ASN A 105 ? 0.6560 0.6976 0.6256 0.0710  -0.1031 -0.0369 655 ASN A ND2 
759  N N   . LEU A 106 ? 0.6506 0.6283 0.6417 0.0426  -0.0361 -0.0360 656 LEU A N   
760  C CA  . LEU A 106 ? 0.6454 0.6199 0.6447 0.0370  -0.0228 -0.0413 656 LEU A CA  
761  C C   . LEU A 106 ? 0.6331 0.6290 0.6622 0.0441  -0.0199 -0.0484 656 LEU A C   
762  O O   . LEU A 106 ? 0.6194 0.6207 0.6613 0.0608  -0.0264 -0.0439 656 LEU A O   
763  C CB  . LEU A 106 ? 0.6480 0.5973 0.6363 0.0415  -0.0157 -0.0367 656 LEU A CB  
764  C CG  . LEU A 106 ? 0.6599 0.6035 0.6528 0.0352  -0.0022 -0.0465 656 LEU A CG  
765  C CD1 . LEU A 106 ? 0.6631 0.6106 0.6420 0.0181  -0.0001 -0.0508 656 LEU A CD1 
766  C CD2 . LEU A 106 ? 0.6825 0.6007 0.6713 0.0388  0.0050  -0.0451 656 LEU A CD2 
767  N N   . LEU A 107 ? 0.6389 0.6477 0.6798 0.0326  -0.0092 -0.0579 657 LEU A N   
768  C CA  . LEU A 107 ? 0.6353 0.6674 0.7104 0.0373  -0.0009 -0.0671 657 LEU A CA  
769  C C   . LEU A 107 ? 0.6568 0.6774 0.7310 0.0355  0.0194  -0.0756 657 LEU A C   
770  O O   . LEU A 107 ? 0.6436 0.6743 0.7470 0.0466  0.0289  -0.0823 657 LEU A O   
771  C CB  . LEU A 107 ? 0.6208 0.6783 0.7142 0.0241  0.0005  -0.0736 657 LEU A CB  
772  C CG  . LEU A 107 ? 0.6298 0.7026 0.7303 0.0238  -0.0190 -0.0720 657 LEU A CG  
773  C CD1 . LEU A 107 ? 0.6209 0.7125 0.7410 0.0057  -0.0132 -0.0807 657 LEU A CD1 
774  C CD2 . LEU A 107 ? 0.6117 0.7067 0.7366 0.0440  -0.0352 -0.0705 657 LEU A CD2 
775  N N   . GLY A 108 ? 0.6831 0.6840 0.7244 0.0221  0.0255  -0.0763 658 GLY A N   
776  C CA  . GLY A 108 ? 0.7007 0.6894 0.7302 0.0163  0.0429  -0.0876 658 GLY A CA  
777  C C   . GLY A 108 ? 0.7305 0.7039 0.7213 0.0015  0.0405  -0.0859 658 GLY A C   
778  O O   . GLY A 108 ? 0.7329 0.7038 0.7107 -0.0020 0.0269  -0.0741 658 GLY A O   
779  N N   . ALA A 109 ? 0.7504 0.7151 0.7232 -0.0070 0.0535  -0.0988 659 ALA A N   
780  C CA  . ALA A 109 ? 0.7728 0.7298 0.7090 -0.0212 0.0480  -0.0987 659 ALA A CA  
781  C C   . ALA A 109 ? 0.7970 0.7533 0.7089 -0.0329 0.0642  -0.1158 659 ALA A C   
782  O O   . ALA A 109 ? 0.7949 0.7460 0.7205 -0.0288 0.0816  -0.1323 659 ALA A O   
783  C CB  . ALA A 109 ? 0.7716 0.7126 0.7075 -0.0190 0.0384  -0.0978 659 ALA A CB  
784  N N   . CYS A 110 ? 0.8144 0.7750 0.6882 -0.0464 0.0586  -0.1116 660 CYS A N   
785  C CA  . CYS A 110 ? 0.8367 0.7969 0.6730 -0.0596 0.0708  -0.1276 660 CYS A CA  
786  C C   . CYS A 110 ? 0.8739 0.8315 0.6836 -0.0694 0.0536  -0.1320 660 CYS A C   
787  O O   . CYS A 110 ? 0.8710 0.8377 0.6627 -0.0730 0.0350  -0.1151 660 CYS A O   
788  C CB  . CYS A 110 ? 0.8391 0.8094 0.6480 -0.0673 0.0792  -0.1173 660 CYS A CB  
789  S SG  . CYS A 110 ? 0.8547 0.8350 0.7055 -0.0592 0.0927  -0.1070 660 CYS A SG  
790  N N   . THR A 111 ? 0.9064 0.8522 0.7194 -0.0734 0.0602  -0.1551 661 THR A N   
791  C CA  . THR A 111 ? 0.9474 0.8933 0.7433 -0.0859 0.0454  -0.1661 661 THR A CA  
792  C C   . THR A 111 ? 1.0002 0.9455 0.7551 -0.1029 0.0555  -0.1948 661 THR A C   
793  O O   . THR A 111 ? 1.0172 0.9699 0.7512 -0.1172 0.0401  -0.2065 661 THR A O   
794  C CB  . THR A 111 ? 0.9517 0.8811 0.7875 -0.0801 0.0436  -0.1702 661 THR A CB  
795  O OG1 . THR A 111 ? 0.9663 0.8737 0.8185 -0.0769 0.0675  -0.1919 661 THR A OG1 
796  C CG2 . THR A 111 ? 0.9376 0.8669 0.8053 -0.0636 0.0348  -0.1432 661 THR A CG2 
797  N N   . ILE A 112 ? 1.0261 0.9655 0.7690 -0.1026 0.0812  -0.2078 662 ILE A N   
798  C CA  . ILE A 112 ? 1.0675 1.0039 0.7653 -0.1192 0.0952  -0.2381 662 ILE A CA  
799  C C   . ILE A 112 ? 1.0994 1.0521 0.7424 -0.1263 0.0965  -0.2265 662 ILE A C   
800  O O   . ILE A 112 ? 1.0992 1.0574 0.7521 -0.1166 0.1027  -0.2025 662 ILE A O   
801  C CB  . ILE A 112 ? 1.0786 0.9923 0.8019 -0.1140 0.1298  -0.2653 662 ILE A CB  
802  C CG1 . ILE A 112 ? 1.0846 0.9774 0.8641 -0.1024 0.1301  -0.2679 662 ILE A CG1 
803  C CG2 . ILE A 112 ? 1.1078 1.0131 0.7851 -0.1327 0.1473  -0.3034 662 ILE A CG2 
804  C CD1 . ILE A 112 ? 1.1007 0.9746 0.9185 -0.0876 0.1607  -0.2801 662 ILE A CD1 
805  N N   . GLY A 113 ? 1.1232 1.0831 0.7076 -0.1439 0.0906  -0.2435 663 GLY A N   
806  C CA  . GLY A 113 ? 1.1520 1.1238 0.6725 -0.1513 0.0940  -0.2325 663 GLY A CA  
807  C C   . GLY A 113 ? 1.1554 1.1425 0.6665 -0.1440 0.0705  -0.1897 663 GLY A C   
808  O O   . GLY A 113 ? 1.1684 1.1551 0.6581 -0.1412 0.0850  -0.1694 663 GLY A O   
809  N N   . GLY A 114 ? 1.1353 1.1342 0.6661 -0.1411 0.0373  -0.1763 664 GLY A N   
810  C CA  . GLY A 114 ? 1.1201 1.1315 0.6483 -0.1321 0.0147  -0.1364 664 GLY A CA  
811  C C   . GLY A 114 ? 1.0803 1.0951 0.6673 -0.1210 -0.0059 -0.1225 664 GLY A C   
812  O O   . GLY A 114 ? 1.0706 1.0774 0.6993 -0.1205 -0.0032 -0.1416 664 GLY A O   
813  N N   . PRO A 115 ? 1.0531 1.0755 0.6441 -0.1110 -0.0225 -0.0873 665 PRO A N   
814  C CA  . PRO A 115 ? 1.0072 1.0324 0.6517 -0.0998 -0.0393 -0.0731 665 PRO A CA  
815  C C   . PRO A 115 ? 0.9602 0.9670 0.6569 -0.0906 -0.0218 -0.0775 665 PRO A C   
816  O O   . PRO A 115 ? 0.9684 0.9632 0.6668 -0.0888 0.0012  -0.0811 665 PRO A O   
817  C CB  . PRO A 115 ? 1.0244 1.0553 0.6575 -0.0900 -0.0522 -0.0354 665 PRO A CB  
818  C CG  . PRO A 115 ? 1.0612 1.1000 0.6272 -0.0981 -0.0540 -0.0297 665 PRO A CG  
819  C CD  . PRO A 115 ? 1.0589 1.0853 0.6028 -0.1093 -0.0252 -0.0587 665 PRO A CD  
820  N N   . THR A 116 ? 0.9102 0.9171 0.6495 -0.0845 -0.0328 -0.0764 666 THR A N   
821  C CA  . THR A 116 ? 0.8716 0.8622 0.6539 -0.0745 -0.0200 -0.0779 666 THR A CA  
822  C C   . THR A 116 ? 0.8510 0.8364 0.6442 -0.0642 -0.0147 -0.0552 666 THR A C   
823  O O   . THR A 116 ? 0.8493 0.8395 0.6412 -0.0598 -0.0271 -0.0336 666 THR A O   
824  C CB  . THR A 116 ? 0.8575 0.8480 0.6749 -0.0716 -0.0312 -0.0800 666 THR A CB  
825  O OG1 . THR A 116 ? 0.8886 0.8846 0.6986 -0.0849 -0.0358 -0.1030 666 THR A OG1 
826  C CG2 . THR A 116 ? 0.8348 0.8074 0.6874 -0.0608 -0.0187 -0.0809 666 THR A CG2 
827  N N   . LEU A 117 ? 0.8274 0.8039 0.6356 -0.0605 0.0039  -0.0617 667 LEU A N   
828  C CA  . LEU A 117 ? 0.8080 0.7813 0.6337 -0.0540 0.0105  -0.0472 667 LEU A CA  
829  C C   . LEU A 117 ? 0.7880 0.7564 0.6529 -0.0441 0.0123  -0.0538 667 LEU A C   
830  O O   . LEU A 117 ? 0.7986 0.7649 0.6748 -0.0421 0.0229  -0.0698 667 LEU A O   
831  C CB  . LEU A 117 ? 0.8112 0.7857 0.6226 -0.0600 0.0314  -0.0512 667 LEU A CB  
832  C CG  . LEU A 117 ? 0.8370 0.8136 0.5991 -0.0701 0.0351  -0.0433 667 LEU A CG  
833  C CD1 . LEU A 117 ? 0.8375 0.8127 0.5945 -0.0754 0.0607  -0.0434 667 LEU A CD1 
834  C CD2 . LEU A 117 ? 0.8512 0.8268 0.5992 -0.0675 0.0180  -0.0162 667 LEU A CD2 
835  N N   . VAL A 118 ? 0.7579 0.7233 0.6415 -0.0368 0.0026  -0.0412 668 VAL A N   
836  C CA  . VAL A 118 ? 0.7244 0.6859 0.6365 -0.0267 0.0019  -0.0446 668 VAL A CA  
837  C C   . VAL A 118 ? 0.6865 0.6535 0.6149 -0.0248 0.0074  -0.0423 668 VAL A C   
838  O O   . VAL A 118 ? 0.6746 0.6395 0.6019 -0.0274 0.0045  -0.0315 668 VAL A O   
839  C CB  . VAL A 118 ? 0.7266 0.6819 0.6451 -0.0215 -0.0104 -0.0353 668 VAL A CB  
840  C CG1 . VAL A 118 ? 0.7183 0.6677 0.6554 -0.0109 -0.0107 -0.0365 668 VAL A CG1 
841  C CG2 . VAL A 118 ? 0.7307 0.6861 0.6409 -0.0265 -0.0161 -0.0391 668 VAL A CG2 
842  N N   . ILE A 119 ? 0.6687 0.6437 0.6160 -0.0208 0.0159  -0.0530 669 ILE A N   
843  C CA  . ILE A 119 ? 0.6656 0.6535 0.6362 -0.0211 0.0198  -0.0541 669 ILE A CA  
844  C C   . ILE A 119 ? 0.6655 0.6575 0.6566 -0.0102 0.0074  -0.0538 669 ILE A C   
845  O O   . ILE A 119 ? 0.6664 0.6578 0.6660 0.0013  0.0045  -0.0571 669 ILE A O   
846  C CB  . ILE A 119 ? 0.6668 0.6690 0.6532 -0.0229 0.0365  -0.0660 669 ILE A CB  
847  C CG1 . ILE A 119 ? 0.6878 0.6844 0.6435 -0.0341 0.0513  -0.0682 669 ILE A CG1 
848  C CG2 . ILE A 119 ? 0.6595 0.6802 0.6769 -0.0263 0.0399  -0.0679 669 ILE A CG2 
849  C CD1 . ILE A 119 ? 0.6927 0.6939 0.6548 -0.0320 0.0679  -0.0847 669 ILE A CD1 
850  N N   . THR A 120 ? 0.6600 0.6537 0.6564 -0.0137 0.0009  -0.0499 670 THR A N   
851  C CA  . THR A 120 ? 0.6636 0.6620 0.6706 -0.0056 -0.0122 -0.0513 670 THR A CA  
852  C C   . THR A 120 ? 0.6671 0.6847 0.6989 -0.0130 -0.0137 -0.0594 670 THR A C   
853  O O   . THR A 120 ? 0.6586 0.6808 0.7002 -0.0254 -0.0015 -0.0617 670 THR A O   
854  C CB  . THR A 120 ? 0.6802 0.6585 0.6658 -0.0038 -0.0193 -0.0428 670 THR A CB  
855  O OG1 . THR A 120 ? 0.6918 0.6631 0.6758 -0.0139 -0.0167 -0.0406 670 THR A OG1 
856  C CG2 . THR A 120 ? 0.6855 0.6493 0.6539 -0.0013 -0.0171 -0.0363 670 THR A CG2 
857  N N   . GLU A 121 ? 0.6726 0.7011 0.7126 -0.0069 -0.0284 -0.0642 671 GLU A N   
858  C CA  . GLU A 121 ? 0.6741 0.7236 0.7385 -0.0162 -0.0336 -0.0761 671 GLU A CA  
859  C C   . GLU A 121 ? 0.7043 0.7353 0.7629 -0.0330 -0.0242 -0.0768 671 GLU A C   
860  O O   . GLU A 121 ? 0.7268 0.7300 0.7590 -0.0319 -0.0221 -0.0676 671 GLU A O   
861  C CB  . GLU A 121 ? 0.6846 0.7444 0.7437 -0.0067 -0.0542 -0.0804 671 GLU A CB  
862  C CG  . GLU A 121 ? 0.7327 0.8144 0.8053 0.0115  -0.0645 -0.0777 671 GLU A CG  
863  C CD  . GLU A 121 ? 0.7936 0.8812 0.8487 0.0254  -0.0855 -0.0751 671 GLU A CD  
864  O OE1 . GLU A 121 ? 0.8173 0.8803 0.8368 0.0244  -0.0872 -0.0715 671 GLU A OE1 
865  O OE2 . GLU A 121 ? 0.8000 0.9171 0.8764 0.0388  -0.0993 -0.0751 671 GLU A OE2 
866  N N   . TYR A 122 ? 0.6961 0.7424 0.7841 -0.0482 -0.0173 -0.0875 672 TYR A N   
867  C CA  . TYR A 122 ? 0.7181 0.7429 0.8059 -0.0647 -0.0058 -0.0885 672 TYR A CA  
868  C C   . TYR A 122 ? 0.7317 0.7644 0.8299 -0.0715 -0.0189 -0.1064 672 TYR A C   
869  O O   . TYR A 122 ? 0.7196 0.7880 0.8461 -0.0742 -0.0306 -0.1218 672 TYR A O   
870  C CB  . TYR A 122 ? 0.7150 0.7476 0.8286 -0.0802 0.0143  -0.0898 672 TYR A CB  
871  C CG  . TYR A 122 ? 0.7459 0.7534 0.8650 -0.0984 0.0297  -0.0897 672 TYR A CG  
872  C CD1 . TYR A 122 ? 0.7821 0.7513 0.8725 -0.0980 0.0426  -0.0697 672 TYR A CD1 
873  C CD2 . TYR A 122 ? 0.7532 0.7758 0.9097 -0.1163 0.0319  -0.1094 672 TYR A CD2 
874  C CE1 . TYR A 122 ? 0.8061 0.7465 0.9033 -0.1124 0.0594  -0.0662 672 TYR A CE1 
875  C CE2 . TYR A 122 ? 0.7762 0.7694 0.9408 -0.1345 0.0500  -0.1100 672 TYR A CE2 
876  C CZ  . TYR A 122 ? 0.8122 0.7612 0.9464 -0.1313 0.0649  -0.0869 672 TYR A CZ  
877  O OH  . TYR A 122 ? 0.8441 0.7587 0.9879 -0.1469 0.0847  -0.0846 672 TYR A OH  
878  N N   . CYS A 123 ? 0.6953 0.8649 0.7813 -0.0626 0.0495  -0.0695 673 CYS A N   
879  C CA  . CYS A 123 ? 0.6803 0.8751 0.8158 -0.0630 0.0401  -0.0872 673 CYS A CA  
880  C C   . CYS A 123 ? 0.6925 0.8786 0.8597 -0.0880 0.0617  -0.0837 673 CYS A C   
881  O O   . CYS A 123 ? 0.7122 0.8587 0.8566 -0.0965 0.0623  -0.0604 673 CYS A O   
882  C CB  . CYS A 123 ? 0.6925 0.8710 0.8090 -0.0498 0.0138  -0.0801 673 CYS A CB  
883  S SG  . CYS A 123 ? 0.7550 0.9240 0.8236 -0.0247 -0.0038 -0.0767 673 CYS A SG  
884  N N   . CYS A 124 ? 0.6798 0.9017 0.9013 -0.0994 0.0806  -0.1078 674 CYS A N   
885  C CA  . CYS A 124 ? 0.6976 0.9091 0.9537 -0.1264 0.1096  -0.1070 674 CYS A CA  
886  C C   . CYS A 124 ? 0.6968 0.8825 0.9654 -0.1352 0.1022  -0.0986 674 CYS A C   
887  O O   . CYS A 124 ? 0.7123 0.8603 0.9759 -0.1541 0.1257  -0.0803 674 CYS A O   
888  C CB  . CYS A 124 ? 0.6932 0.9571 1.0206 -0.1371 0.1291  -0.1429 674 CYS A CB  
889  S SG  . CYS A 124 ? 0.7845 1.1106 1.1785 -0.1227 0.0982  -0.1868 674 CYS A SG  
890  N N   . TYR A 125 ? 0.6804 0.8810 0.9611 -0.1211 0.0727  -0.1106 675 TYR A N   
891  C CA  . TYR A 125 ? 0.6855 0.8632 0.9822 -0.1295 0.0681  -0.1059 675 TYR A CA  
892  C C   . TYR A 125 ? 0.6911 0.8164 0.9335 -0.1239 0.0576  -0.0705 675 TYR A C   
893  O O   . TYR A 125 ? 0.6918 0.7910 0.9453 -0.1315 0.0580  -0.0625 675 TYR A O   
894  C CB  . TYR A 125 ? 0.6797 0.8955 1.0163 -0.1190 0.0451  -0.1377 675 TYR A CB  
895  C CG  . TYR A 125 ? 0.6732 0.9432 1.0751 -0.1258 0.0529  -0.1773 675 TYR A CG  
896  C CD1 . TYR A 125 ? 0.6786 0.9527 1.1380 -0.1520 0.0770  -0.1925 675 TYR A CD1 
897  C CD2 . TYR A 125 ? 0.6779 0.9941 1.0861 -0.1061 0.0380  -0.2002 675 TYR A CD2 
898  C CE1 . TYR A 125 ? 0.6614 0.9911 1.1910 -0.1603 0.0849  -0.2338 675 TYR A CE1 
899  C CE2 . TYR A 125 ? 0.6595 1.0315 1.1336 -0.1103 0.0426  -0.2398 675 TYR A CE2 
900  C CZ  . TYR A 125 ? 0.6600 1.0420 1.1986 -0.1386 0.0661  -0.2585 675 TYR A CZ  
901  O OH  . TYR A 125 ? 0.6411 1.0850 1.2555 -0.1443 0.0707  -0.3033 675 TYR A OH  
902  N N   . GLY A 126 ? 0.6884 0.7992 0.8772 -0.1113 0.0490  -0.0519 676 GLY A N   
903  C CA  . GLY A 126 ? 0.6907 0.7599 0.8337 -0.1046 0.0360  -0.0236 676 GLY A CA  
904  C C   . GLY A 126 ? 0.6677 0.7424 0.8137 -0.0906 0.0104  -0.0294 676 GLY A C   
905  O O   . GLY A 126 ? 0.6473 0.7543 0.8090 -0.0804 0.0004  -0.0510 676 GLY A O   
906  N N   . ASP A 127 ? 0.6824 0.7252 0.8131 -0.0884 0.0001  -0.0110 677 ASP A N   
907  C CA  . ASP A 127 ? 0.6932 0.7392 0.8287 -0.0767 -0.0196 -0.0166 677 ASP A CA  
908  C C   . ASP A 127 ? 0.6843 0.7464 0.8635 -0.0797 -0.0199 -0.0373 677 ASP A C   
909  O O   . ASP A 127 ? 0.6832 0.7401 0.8931 -0.0932 -0.0071 -0.0409 677 ASP A O   
910  C CB  . ASP A 127 ? 0.7434 0.7572 0.8573 -0.0722 -0.0315 0.0047  677 ASP A CB  
911  C CG  . ASP A 127 ? 0.8314 0.8164 0.9602 -0.0799 -0.0265 0.0176  677 ASP A CG  
912  O OD1 . ASP A 127 ? 0.8557 0.8218 0.9753 -0.0896 -0.0105 0.0297  677 ASP A OD1 
913  O OD2 . ASP A 127 ? 0.8608 0.8385 1.0086 -0.0755 -0.0367 0.0163  677 ASP A OD2 
914  N N   . LEU A 128 ? 0.6736 0.7518 0.8526 -0.0667 -0.0331 -0.0512 678 LEU A N   
915  C CA  . LEU A 128 ? 0.6552 0.7509 0.8652 -0.0648 -0.0368 -0.0742 678 LEU A CA  
916  C C   . LEU A 128 ? 0.6657 0.7389 0.8976 -0.0715 -0.0360 -0.0697 678 LEU A C   
917  O O   . LEU A 128 ? 0.6558 0.7374 0.9240 -0.0797 -0.0307 -0.0869 678 LEU A O   
918  C CB  . LEU A 128 ? 0.6547 0.7639 0.8421 -0.0459 -0.0493 -0.0854 678 LEU A CB  
919  C CG  . LEU A 128 ? 0.6576 0.7883 0.8640 -0.0387 -0.0555 -0.1124 678 LEU A CG  
920  C CD1 . LEU A 128 ? 0.6388 0.8034 0.8814 -0.0451 -0.0528 -0.1365 678 LEU A CD1 
921  C CD2 . LEU A 128 ? 0.6765 0.8089 0.8449 -0.0172 -0.0652 -0.1171 678 LEU A CD2 
922  N N   . LEU A 129 ? 0.6885 0.7338 0.9036 -0.0687 -0.0408 -0.0484 679 LEU A N   
923  C CA  . LEU A 129 ? 0.6957 0.7185 0.9340 -0.0721 -0.0410 -0.0436 679 LEU A CA  
924  C C   . LEU A 129 ? 0.7184 0.7245 0.9810 -0.0872 -0.0269 -0.0395 679 LEU A C   
925  O O   . LEU A 129 ? 0.7224 0.7272 1.0203 -0.0929 -0.0222 -0.0542 679 LEU A O   
926  C CB  . LEU A 129 ? 0.6951 0.6953 0.9158 -0.0645 -0.0511 -0.0232 679 LEU A CB  
927  C CG  . LEU A 129 ? 0.6881 0.6669 0.9364 -0.0641 -0.0533 -0.0194 679 LEU A CG  
928  C CD1 . LEU A 129 ? 0.6770 0.6699 0.9504 -0.0606 -0.0529 -0.0422 679 LEU A CD1 
929  C CD2 . LEU A 129 ? 0.6953 0.6564 0.9311 -0.0553 -0.0661 -0.0008 679 LEU A CD2 
930  N N   . ASN A 130 ? 0.7316 0.7235 0.9744 -0.0942 -0.0171 -0.0217 680 ASN A N   
931  C CA  . ASN A 130 ? 0.7412 0.7110 1.0031 -0.1102 0.0029  -0.0163 680 ASN A CA  
932  C C   . ASN A 130 ? 0.7277 0.7293 1.0307 -0.1230 0.0159  -0.0461 680 ASN A C   
933  O O   . ASN A 130 ? 0.7350 0.7223 1.0731 -0.1376 0.0319  -0.0528 680 ASN A O   
934  C CB  . ASN A 130 ? 0.7880 0.7295 1.0108 -0.1137 0.0136  0.0111  680 ASN A CB  
935  C CG  . ASN A 130 ? 0.8743 0.7722 1.0681 -0.1036 0.0035  0.0400  680 ASN A CG  
936  O OD1 . ASN A 130 ? 0.9088 0.7736 1.1191 -0.1059 0.0088  0.0483  680 ASN A OD1 
937  N ND2 . ASN A 130 ? 0.8843 0.7810 1.0360 -0.0908 -0.0126 0.0540  680 ASN A ND2 
938  N N   . PHE A 131 ? 0.7042 0.7486 1.0063 -0.1167 0.0086  -0.0663 681 PHE A N   
939  C CA  . PHE A 131 ? 0.6771 0.7603 1.0231 -0.1252 0.0151  -0.1002 681 PHE A CA  
940  C C   . PHE A 131 ? 0.6632 0.7557 1.0449 -0.1241 0.0066  -0.1254 681 PHE A C   
941  O O   . PHE A 131 ? 0.6405 0.7435 1.0702 -0.1390 0.0178  -0.1486 681 PHE A O   
942  C CB  . PHE A 131 ? 0.6644 0.7892 0.9960 -0.1122 0.0045  -0.1150 681 PHE A CB  
943  C CG  . PHE A 131 ? 0.6377 0.8092 1.0178 -0.1165 0.0054  -0.1540 681 PHE A CG  
944  C CD1 . PHE A 131 ? 0.6349 0.8231 1.0495 -0.1338 0.0263  -0.1647 681 PHE A CD1 
945  C CD2 . PHE A 131 ? 0.6307 0.8298 1.0234 -0.1030 -0.0142 -0.1820 681 PHE A CD2 
946  C CE1 . PHE A 131 ? 0.6133 0.8514 1.0833 -0.1380 0.0252  -0.2061 681 PHE A CE1 
947  C CE2 . PHE A 131 ? 0.6127 0.8580 1.0522 -0.1048 -0.0180 -0.2218 681 PHE A CE2 
948  C CZ  . PHE A 131 ? 0.5926 0.8605 1.0751 -0.1224 0.0004  -0.2354 681 PHE A CZ  
949  N N   . LEU A 132 ? 0.6719 0.7600 1.0311 -0.1073 -0.0112 -0.1227 682 LEU A N   
950  C CA  . LEU A 132 ? 0.6648 0.7583 1.0485 -0.1039 -0.0184 -0.1454 682 LEU A CA  
951  C C   . LEU A 132 ? 0.6826 0.7400 1.0965 -0.1177 -0.0057 -0.1383 682 LEU A C   
952  O O   . LEU A 132 ? 0.6693 0.7339 1.1211 -0.1237 -0.0038 -0.1648 682 LEU A O   
953  C CB  . LEU A 132 ? 0.6684 0.7587 1.0170 -0.0841 -0.0338 -0.1402 682 LEU A CB  
954  C CG  . LEU A 132 ? 0.6767 0.7949 0.9918 -0.0668 -0.0460 -0.1496 682 LEU A CG  
955  C CD1 . LEU A 132 ? 0.6943 0.7966 0.9725 -0.0514 -0.0529 -0.1375 682 LEU A CD1 
956  C CD2 . LEU A 132 ? 0.6592 0.8140 0.9944 -0.0619 -0.0535 -0.1868 682 LEU A CD2 
957  N N   . ARG A 133 ? 0.7156 0.7322 1.1102 -0.1204 0.0013  -0.1038 683 ARG A N   
958  C CA  . ARG A 133 ? 0.7436 0.7173 1.1594 -0.1287 0.0122  -0.0922 683 ARG A CA  
959  C C   . ARG A 133 ? 0.7803 0.7431 1.2322 -0.1511 0.0364  -0.1007 683 ARG A C   
960  O O   . ARG A 133 ? 0.7682 0.7101 1.2570 -0.1603 0.0461  -0.1115 683 ARG A O   
961  C CB  . ARG A 133 ? 0.7596 0.6933 1.1384 -0.1191 0.0075  -0.0535 683 ARG A CB  
962  C CG  . ARG A 133 ? 0.7673 0.7070 1.1339 -0.1007 -0.0125 -0.0522 683 ARG A CG  
963  C CD  . ARG A 133 ? 0.8143 0.7243 1.1505 -0.0894 -0.0221 -0.0201 683 ARG A CD  
964  N NE  . ARG A 133 ? 0.8466 0.7668 1.1856 -0.0747 -0.0379 -0.0248 683 ARG A NE  
965  C CZ  . ARG A 133 ? 0.9015 0.8054 1.2288 -0.0622 -0.0512 -0.0062 683 ARG A CZ  
966  N NH1 . ARG A 133 ? 0.9498 0.8232 1.2529 -0.0593 -0.0542 0.0207  683 ARG A NH1 
967  N NH2 . ARG A 133 ? 0.8805 0.7988 1.2202 -0.0518 -0.0612 -0.0159 683 ARG A NH2 
968  N N   . ARG A 134 ? 0.8164 0.7930 1.2616 -0.1610 0.0487  -0.0983 684 ARG A N   
969  C CA  . ARG A 134 ? 0.8498 0.8202 1.3355 -0.1856 0.0771  -0.1101 684 ARG A CA  
970  C C   . ARG A 134 ? 0.8456 0.8617 1.3928 -0.1947 0.0749  -0.1599 684 ARG A C   
971  O O   . ARG A 134 ? 0.8414 0.8465 1.4383 -0.2163 0.0968  -0.1769 684 ARG A O   
972  C CB  . ARG A 134 ? 0.8966 0.8759 1.3615 -0.1930 0.0923  -0.0983 684 ARG A CB  
973  C CG  . ARG A 134 ? 1.0256 0.9557 1.4288 -0.1860 0.0972  -0.0520 684 ARG A CG  
974  C CD  . ARG A 134 ? 1.1298 1.0423 1.5272 -0.2048 0.1310  -0.0405 684 ARG A CD  
975  N NE  . ARG A 134 ? 1.2469 1.1230 1.5738 -0.1943 0.1318  -0.0006 684 ARG A NE  
976  C CZ  . ARG A 134 ? 1.3119 1.1525 1.6130 -0.2070 0.1633  0.0205  684 ARG A CZ  
977  N NH1 . ARG A 134 ? 1.2814 1.1174 1.6272 -0.2332 0.2003  0.0060  684 ARG A NH1 
978  N NH2 . ARG A 134 ? 1.3586 1.1669 1.5885 -0.1938 0.1594  0.0547  684 ARG A NH2 
979  N N   . LYS A 135 ? 0.8497 0.9136 1.3912 -0.1774 0.0486  -0.1838 685 LYS A N   
980  C CA  . LYS A 135 ? 0.8435 0.9538 1.4319 -0.1795 0.0392  -0.2324 685 LYS A CA  
981  C C   . LYS A 135 ? 0.8720 0.9669 1.4817 -0.1777 0.0332  -0.2492 685 LYS A C   
982  O O   . LYS A 135 ? 0.8590 0.9919 1.4959 -0.1741 0.0198  -0.2904 685 LYS A O   
983  C CB  . LYS A 135 ? 0.8633 1.0261 1.4274 -0.1579 0.0137  -0.2500 685 LYS A CB  
984  C CG  . LYS A 135 ? 0.9092 1.0967 1.4648 -0.1595 0.0197  -0.2442 685 LYS A CG  
985  C CD  . LYS A 135 ? 0.9397 1.1504 1.5598 -0.1847 0.0421  -0.2707 685 LYS A CD  
986  C CE  . LYS A 135 ? 1.0064 1.2103 1.6132 -0.1945 0.0638  -0.2474 685 LYS A CE  
987  N NZ  . LYS A 135 ? 1.0060 1.2426 1.6819 -0.2189 0.0878  -0.2793 685 LYS A NZ  
988  N N   . ARG A 136 ? 0.9080 0.9479 1.5054 -0.1786 0.0419  -0.2194 686 ARG A N   
989  C CA  . ARG A 136 ? 0.9255 0.9425 1.5478 -0.1784 0.0414  -0.2326 686 ARG A CA  
990  C C   . ARG A 136 ? 0.9598 0.9480 1.6367 -0.2056 0.0695  -0.2429 686 ARG A C   
991  O O   . ARG A 136 ? 0.9760 0.9442 1.6554 -0.2217 0.0920  -0.2239 686 ARG A O   
992  C CB  . ARG A 136 ? 0.9411 0.9121 1.5269 -0.1636 0.0370  -0.1943 686 ARG A CB  
993  C CG  . ARG A 136 ? 0.9305 0.9212 1.4757 -0.1394 0.0138  -0.1900 686 ARG A CG  
994  C CD  . ARG A 136 ? 0.9359 0.8840 1.4581 -0.1281 0.0115  -0.1542 686 ARG A CD  
995  N NE  . ARG A 136 ? 0.9152 0.8803 1.4050 -0.1081 -0.0058 -0.1503 686 ARG A NE  
996  C CZ  . ARG A 136 ? 0.8891 0.8416 1.3838 -0.0964 -0.0108 -0.1510 686 ARG A CZ  
997  N NH1 . ARG A 136 ? 0.8714 0.7934 1.4008 -0.1001 -0.0028 -0.1546 686 ARG A NH1 
998  N NH2 . ARG A 136 ? 0.8658 0.8344 1.3332 -0.0814 -0.0213 -0.1490 686 ARG A NH2 
999  N N   . ASP A 137 ? 0.9699 0.9505 1.6882 -0.2110 0.0712  -0.2721 687 ASP A N   
1000 C CA  . ASP A 137 ? 0.9847 0.9314 1.7598 -0.2371 0.0993  -0.2859 687 ASP A CA  
1001 C C   . ASP A 137 ? 0.9709 0.9559 1.7995 -0.2628 0.1150  -0.3211 687 ASP A C   
1002 O O   . ASP A 137 ? 0.9670 0.9960 1.7827 -0.2601 0.1078  -0.3235 687 ASP A O   
1003 C CB  . ASP A 137 ? 1.0418 0.9112 1.7951 -0.2411 0.1222  -0.2357 687 ASP A CB  
1004 C CG  . ASP A 137 ? 1.1198 0.9510 1.8374 -0.2167 0.1072  -0.2069 687 ASP A CG  
1005 O OD1 . ASP A 137 ? 1.1093 0.9680 1.7865 -0.1940 0.0817  -0.1980 687 ASP A OD1 
1006 O OD2 . ASP A 137 ? 1.1827 0.9553 1.9150 -0.2200 0.1225  -0.1937 687 ASP A OD2 
1007 N N   . ASP A 152 ? 1.2558 1.4580 1.8816 -0.2506 0.1725  -0.2153 760 ASP A N   
1008 C CA  . ASP A 152 ? 1.2146 1.4886 1.9095 -0.2472 0.1529  -0.2693 760 ASP A CA  
1009 C C   . ASP A 152 ? 1.1865 1.4619 1.9594 -0.2754 0.1731  -0.3003 760 ASP A C   
1010 O O   . ASP A 152 ? 1.2161 1.4323 1.9792 -0.2887 0.1894  -0.2780 760 ASP A O   
1011 C CB  . ASP A 152 ? 1.2462 1.5399 1.9077 -0.2144 0.1049  -0.2753 760 ASP A CB  
1012 C CG  . ASP A 152 ? 1.2663 1.6357 1.9653 -0.1967 0.0770  -0.3219 760 ASP A CG  
1013 O OD1 . ASP A 152 ? 1.2317 1.6441 2.0086 -0.2110 0.0810  -0.3671 760 ASP A OD1 
1014 O OD2 . ASP A 152 ? 1.3023 1.6868 1.9528 -0.1672 0.0500  -0.3145 760 ASP A OD2 
1015 N N   . GLU A 153 ? 1.1244 1.4682 1.9781 -0.2835 0.1709  -0.3541 761 GLU A N   
1016 C CA  . GLU A 153 ? 1.0826 1.4370 2.0226 -0.3122 0.1894  -0.3931 761 GLU A CA  
1017 C C   . GLU A 153 ? 1.0363 1.4412 2.0123 -0.2958 0.1465  -0.4403 761 GLU A C   
1018 O O   . GLU A 153 ? 1.0087 1.4306 2.0612 -0.3179 0.1563  -0.4808 761 GLU A O   
1019 C CB  . GLU A 153 ? 1.0732 1.4687 2.0944 -0.3408 0.2268  -0.4261 761 GLU A CB  
1020 C CG  . GLU A 153 ? 1.1638 1.5202 2.1457 -0.3531 0.2687  -0.3854 761 GLU A CG  
1021 C CD  . GLU A 153 ? 1.2076 1.6065 2.2724 -0.3821 0.3103  -0.4197 761 GLU A CD  
1022 O OE1 . GLU A 153 ? 1.1778 1.5955 2.3343 -0.4119 0.3325  -0.4605 761 GLU A OE1 
1023 O OE2 . GLU A 153 ? 1.2411 1.6546 2.2824 -0.3761 0.3226  -0.4078 761 GLU A OE2 
1024 N N   . LEU A 154 ? 1.0256 1.4525 1.9458 -0.2577 0.1011  -0.4367 762 LEU A N   
1025 C CA  . LEU A 154 ? 0.9840 1.4562 1.9241 -0.2377 0.0601  -0.4800 762 LEU A CA  
1026 C C   . LEU A 154 ? 0.9927 1.4235 1.8611 -0.2145 0.0343  -0.4543 762 LEU A C   
1027 O O   . LEU A 154 ? 1.0338 1.4129 1.8308 -0.2055 0.0382  -0.4034 762 LEU A O   
1028 C CB  . LEU A 154 ? 0.9604 1.5088 1.9122 -0.2108 0.0284  -0.5140 762 LEU A CB  
1029 C CG  . LEU A 154 ? 0.9304 1.5394 1.9775 -0.2322 0.0477  -0.5582 762 LEU A CG  
1030 C CD1 . LEU A 154 ? 0.9334 1.5745 1.9612 -0.2141 0.0443  -0.5498 762 LEU A CD1 
1031 C CD2 . LEU A 154 ? 0.8872 1.5640 2.0157 -0.2315 0.0223  -0.6279 762 LEU A CD2 
1032 N N   . ALA A 155 ? 0.9487 1.4053 1.8400 -0.2052 0.0083  -0.4936 763 ALA A N   
1033 C CA  . ALA A 155 ? 0.9548 1.3785 1.7887 -0.1849 -0.0132 -0.4790 763 ALA A CA  
1034 C C   . ALA A 155 ? 0.9464 1.3811 1.7026 -0.1453 -0.0461 -0.4636 763 ALA A C   
1035 O O   . ALA A 155 ? 0.9291 1.4126 1.6847 -0.1266 -0.0651 -0.4825 763 ALA A O   
1036 C CB  . ALA A 155 ? 0.9322 1.3783 1.8167 -0.1898 -0.0262 -0.5297 763 ALA A CB  
1037 N N   . LEU A 156 ? 0.9579 1.3449 1.6507 -0.1323 -0.0511 -0.4298 764 LEU A N   
1038 C CA  . LEU A 156 ? 0.9662 1.3479 1.5809 -0.0983 -0.0750 -0.4100 764 LEU A CA  
1039 C C   . LEU A 156 ? 0.9504 1.3480 1.5525 -0.0781 -0.1011 -0.4433 764 LEU A C   
1040 O O   . LEU A 156 ? 0.9537 1.3311 1.5778 -0.0906 -0.0943 -0.4540 764 LEU A O   
1041 C CB  . LEU A 156 ? 1.0003 1.3189 1.5650 -0.1015 -0.0593 -0.3566 764 LEU A CB  
1042 C CG  . LEU A 156 ? 1.0390 1.3409 1.5275 -0.0752 -0.0721 -0.3256 764 LEU A CG  
1043 C CD1 . LEU A 156 ? 1.0393 1.3627 1.5133 -0.0675 -0.0736 -0.3167 764 LEU A CD1 
1044 C CD2 . LEU A 156 ? 1.0723 1.3191 1.5313 -0.0823 -0.0576 -0.2830 764 LEU A CD2 
1045 N N   . ASP A 157 ? 0.9320 1.3628 1.4963 -0.0456 -0.1303 -0.4604 765 ASP A N   
1046 C CA  . ASP A 157 ? 0.9238 1.3658 1.4616 -0.0222 -0.1556 -0.4907 765 ASP A CA  
1047 C C   . ASP A 157 ? 0.9404 1.3513 1.3810 0.0110  -0.1670 -0.4605 765 ASP A C   
1048 O O   . ASP A 157 ? 0.9666 1.3488 1.3698 0.0127  -0.1552 -0.4179 765 ASP A O   
1049 C CB  . ASP A 157 ? 0.9192 1.4294 1.5036 -0.0115 -0.1828 -0.5508 765 ASP A CB  
1050 C CG  . ASP A 157 ? 0.9812 1.5355 1.5622 0.0095  -0.2007 -0.5586 765 ASP A CG  
1051 O OD1 . ASP A 157 ? 1.0079 1.5394 1.5551 0.0117  -0.1880 -0.5168 765 ASP A OD1 
1052 O OD2 . ASP A 157 ? 0.9801 1.5935 1.5944 0.0252  -0.2291 -0.6093 765 ASP A OD2 
1053 N N   . LEU A 158 ? 0.9286 1.3407 1.3279 0.0356  -0.1866 -0.4822 766 LEU A N   
1054 C CA  . LEU A 158 ? 0.9601 1.3380 1.2662 0.0659  -0.1923 -0.4563 766 LEU A CA  
1055 C C   . LEU A 158 ? 0.9576 1.3473 1.2184 0.0932  -0.2068 -0.4433 766 LEU A C   
1056 O O   . LEU A 158 ? 0.9946 1.3448 1.1904 0.1065  -0.1983 -0.4056 766 LEU A O   
1057 C CB  . LEU A 158 ? 0.9783 1.3577 1.2480 0.0879  -0.2097 -0.4880 766 LEU A CB  
1058 C CG  . LEU A 158 ? 1.0504 1.3875 1.2194 0.1182  -0.2093 -0.4626 766 LEU A CG  
1059 C CD1 . LEU A 158 ? 1.0807 1.3671 1.2390 0.1007  -0.1798 -0.4341 766 LEU A CD1 
1060 C CD2 . LEU A 158 ? 1.0664 1.4208 1.1839 0.1541  -0.2383 -0.4999 766 LEU A CD2 
1061 N N   . GLU A 159 ? 0.9098 1.3540 1.2104 0.1009  -0.2272 -0.4760 767 GLU A N   
1062 C CA  . GLU A 159 ? 0.9035 1.3639 1.1710 0.1286  -0.2427 -0.4685 767 GLU A CA  
1063 C C   . GLU A 159 ? 0.8813 1.3150 1.1478 0.1116  -0.2173 -0.4233 767 GLU A C   
1064 O O   . GLU A 159 ? 0.9080 1.3268 1.1201 0.1352  -0.2218 -0.4008 767 GLU A O   
1065 C CB  . GLU A 159 ? 0.9044 1.4371 1.2335 0.1374  -0.2697 -0.5197 767 GLU A CB  
1066 C CG  . GLU A 159 ? 1.0008 1.5568 1.3003 0.1721  -0.2910 -0.5194 767 GLU A CG  
1067 C CD  . GLU A 159 ? 1.1157 1.7420 1.4512 0.1982  -0.3306 -0.5772 767 GLU A CD  
1068 O OE1 . GLU A 159 ? 1.1189 1.7811 1.4690 0.2176  -0.3455 -0.5862 767 GLU A OE1 
1069 O OE2 . GLU A 159 ? 1.1653 1.8124 1.5165 0.2005  -0.3479 -0.6162 767 GLU A OE2 
1070 N N   . ASP A 160 ? 0.8303 1.2531 1.1517 0.0723  -0.1904 -0.4099 768 ASP A N   
1071 C CA  . ASP A 160 ? 0.8085 1.2045 1.1266 0.0555  -0.1671 -0.3691 768 ASP A CA  
1072 C C   . ASP A 160 ? 0.8166 1.1547 1.0694 0.0601  -0.1554 -0.3289 768 ASP A C   
1073 O O   . ASP A 160 ? 0.8399 1.1576 1.0455 0.0736  -0.1533 -0.3021 768 ASP A O   
1074 C CB  . ASP A 160 ? 0.8052 1.2046 1.1963 0.0153  -0.1429 -0.3688 768 ASP A CB  
1075 C CG  . ASP A 160 ? 0.8377 1.2957 1.3038 0.0057  -0.1479 -0.4106 768 ASP A CG  
1076 O OD1 . ASP A 160 ? 0.8353 1.3250 1.3045 0.0196  -0.1563 -0.4174 768 ASP A OD1 
1077 O OD2 . ASP A 160 ? 0.8458 1.3188 1.3718 -0.0157 -0.1426 -0.4390 768 ASP A OD2 
1078 N N   . LEU A 161 ? 0.7962 1.1092 1.0481 0.0502  -0.1479 -0.3278 769 LEU A N   
1079 C CA  . LEU A 161 ? 0.8060 1.0682 1.0081 0.0521  -0.1345 -0.2942 769 LEU A CA  
1080 C C   . LEU A 161 ? 0.8198 1.0632 0.9431 0.0850  -0.1433 -0.2841 769 LEU A C   
1081 O O   . LEU A 161 ? 0.8444 1.0511 0.9292 0.0861  -0.1299 -0.2514 769 LEU A O   
1082 C CB  . LEU A 161 ? 0.8048 1.0519 1.0254 0.0403  -0.1274 -0.3046 769 LEU A CB  
1083 C CG  . LEU A 161 ? 0.7927 1.0477 1.0876 0.0088  -0.1161 -0.3138 769 LEU A CG  
1084 C CD1 . LEU A 161 ? 0.7989 1.0361 1.1073 0.0020  -0.1104 -0.3258 769 LEU A CD1 
1085 C CD2 . LEU A 161 ? 0.8004 1.0314 1.1092 -0.0117 -0.0975 -0.2771 769 LEU A CD2 
1086 N N   . LEU A 162 ? 0.8057 1.0723 0.9045 0.1123  -0.1655 -0.3128 770 LEU A N   
1087 C CA  . LEU A 162 ? 0.8297 1.0735 0.8457 0.1479  -0.1742 -0.3034 770 LEU A CA  
1088 C C   . LEU A 162 ? 0.8107 1.0540 0.8086 0.1589  -0.1760 -0.2842 770 LEU A C   
1089 O O   . LEU A 162 ? 0.8512 1.0545 0.7841 0.1764  -0.1688 -0.2589 770 LEU A O   
1090 C CB  . LEU A 162 ? 0.8384 1.1107 0.8320 0.1784  -0.2029 -0.3422 770 LEU A CB  
1091 C CG  . LEU A 162 ? 0.8658 1.1300 0.8513 0.1775  -0.2026 -0.3625 770 LEU A CG  
1092 C CD1 . LEU A 162 ? 0.8705 1.1679 0.8330 0.2098  -0.2357 -0.4040 770 LEU A CD1 
1093 C CD2 . LEU A 162 ? 0.9155 1.1193 0.8335 0.1823  -0.1788 -0.3318 770 LEU A CD2 
1094 N N   . SER A 163 ? 0.7512 1.0372 0.8072 0.1485  -0.1832 -0.2980 771 SER A N   
1095 C CA  . SER A 163 ? 0.7283 1.0214 0.7792 0.1570  -0.1844 -0.2852 771 SER A CA  
1096 C C   . SER A 163 ? 0.7295 0.9828 0.7732 0.1343  -0.1581 -0.2455 771 SER A C   
1097 O O   . SER A 163 ? 0.7583 0.9861 0.7576 0.1483  -0.1541 -0.2240 771 SER A O   
1098 C CB  . SER A 163 ? 0.6883 1.0418 0.8148 0.1469  -0.1944 -0.3157 771 SER A CB  
1099 O OG  . SER A 163 ? 0.7041 1.0659 0.8410 0.1456  -0.1881 -0.3030 771 SER A OG  
1100 N N   . PHE A 164 ? 0.6980 0.9436 0.7839 0.1009  -0.1410 -0.2367 772 PHE A N   
1101 C CA  . PHE A 164 ? 0.6896 0.9003 0.7699 0.0812  -0.1205 -0.2024 772 PHE A CA  
1102 C C   . PHE A 164 ? 0.7376 0.9016 0.7571 0.0934  -0.1126 -0.1806 772 PHE A C   
1103 O O   . PHE A 164 ? 0.7576 0.8954 0.7516 0.0928  -0.1027 -0.1567 772 PHE A O   
1104 C CB  . PHE A 164 ? 0.6543 0.8634 0.7860 0.0495  -0.1079 -0.1993 772 PHE A CB  
1105 C CG  . PHE A 164 ? 0.6178 0.8624 0.8118 0.0307  -0.1063 -0.2167 772 PHE A CG  
1106 C CD1 . PHE A 164 ? 0.6088 0.8867 0.8170 0.0375  -0.1122 -0.2294 772 PHE A CD1 
1107 C CD2 . PHE A 164 ? 0.6096 0.8515 0.8500 0.0057  -0.0960 -0.2205 772 PHE A CD2 
1108 C CE1 . PHE A 164 ? 0.5937 0.9033 0.8637 0.0171  -0.1048 -0.2464 772 PHE A CE1 
1109 C CE2 . PHE A 164 ? 0.5892 0.8569 0.8866 -0.0141 -0.0885 -0.2354 772 PHE A CE2 
1110 C CZ  . PHE A 164 ? 0.5761 0.8784 0.8894 -0.0097 -0.0915 -0.2488 772 PHE A CZ  
1111 N N   . SER A 165 ? 0.7562 0.9093 0.7527 0.1043  -0.1150 -0.1911 773 SER A N   
1112 C CA  . SER A 165 ? 0.8031 0.9108 0.7428 0.1152  -0.1023 -0.1735 773 SER A CA  
1113 C C   . SER A 165 ? 0.8384 0.9262 0.7162 0.1432  -0.1056 -0.1636 773 SER A C   
1114 O O   . SER A 165 ? 0.8702 0.9180 0.7143 0.1427  -0.0885 -0.1396 773 SER A O   
1115 C CB  . SER A 165 ? 0.8415 0.9447 0.7637 0.1250  -0.1044 -0.1916 773 SER A CB  
1116 O OG  . SER A 165 ? 0.8756 1.0037 0.8584 0.1040  -0.1065 -0.2093 773 SER A OG  
1117 N N   . TYR A 166 ? 0.8291 0.9447 0.6952 0.1682  -0.1277 -0.1836 774 TYR A N   
1118 C CA  . TYR A 166 ? 0.8602 0.9589 0.6676 0.2011  -0.1355 -0.1773 774 TYR A CA  
1119 C C   . TYR A 166 ? 0.8469 0.9393 0.6649 0.1923  -0.1270 -0.1579 774 TYR A C   
1120 O O   . TYR A 166 ? 0.8762 0.9256 0.6419 0.2059  -0.1161 -0.1372 774 TYR A O   
1121 C CB  . TYR A 166 ? 0.8559 1.0000 0.6680 0.2284  -0.1668 -0.2101 774 TYR A CB  
1122 C CG  . TYR A 166 ? 0.9093 1.0399 0.6613 0.2694  -0.1810 -0.2071 774 TYR A CG  
1123 C CD1 . TYR A 166 ? 0.9797 1.0488 0.6442 0.2940  -0.1701 -0.1853 774 TYR A CD1 
1124 C CD2 . TYR A 166 ? 0.9060 1.0840 0.6887 0.2855  -0.2045 -0.2277 774 TYR A CD2 
1125 C CE1 . TYR A 166 ? 1.0304 1.0792 0.6332 0.3355  -0.1831 -0.1807 774 TYR A CE1 
1126 C CE2 . TYR A 166 ? 0.9518 1.1175 0.6795 0.3281  -0.2207 -0.2266 774 TYR A CE2 
1127 C CZ  . TYR A 166 ? 1.0281 1.1263 0.6624 0.3544  -0.2108 -0.2017 774 TYR A CZ  
1128 O OH  . TYR A 166 ? 1.0923 1.1704 0.6664 0.3996  -0.2263 -0.1979 774 TYR A OH  
1129 N N   . GLN A 167 ? 0.7949 0.9266 0.6787 0.1690  -0.1294 -0.1650 775 GLN A N   
1130 C CA  . GLN A 167 ? 0.7847 0.9148 0.6795 0.1603  -0.1218 -0.1506 775 GLN A CA  
1131 C C   . GLN A 167 ? 0.7878 0.8765 0.6729 0.1383  -0.0995 -0.1227 775 GLN A C   
1132 O O   . GLN A 167 ? 0.8055 0.8692 0.6637 0.1434  -0.0918 -0.1074 775 GLN A O   
1133 C CB  . GLN A 167 ? 0.7679 0.9482 0.7306 0.1416  -0.1265 -0.1666 775 GLN A CB  
1134 C CG  . GLN A 167 ? 0.7705 1.0013 0.7588 0.1606  -0.1488 -0.2003 775 GLN A CG  
1135 C CD  . GLN A 167 ? 0.7582 1.0336 0.8188 0.1359  -0.1446 -0.2147 775 GLN A CD  
1136 O OE1 . GLN A 167 ? 0.7912 1.0734 0.8622 0.1319  -0.1370 -0.2081 775 GLN A OE1 
1137 N NE2 . GLN A 167 ? 0.7064 1.0086 0.8173 0.1173  -0.1457 -0.2342 775 GLN A NE2 
1138 N N   . VAL A 168 ? 0.7605 0.8421 0.6694 0.1152  -0.0900 -0.1184 776 VAL A N   
1139 C CA  . VAL A 168 ? 0.7571 0.8046 0.6628 0.0963  -0.0722 -0.0961 776 VAL A CA  
1140 C C   . VAL A 168 ? 0.7862 0.7875 0.6334 0.1131  -0.0601 -0.0841 776 VAL A C   
1141 O O   . VAL A 168 ? 0.7906 0.7659 0.6234 0.1085  -0.0489 -0.0692 776 VAL A O   
1142 C CB  . VAL A 168 ? 0.7412 0.7921 0.6885 0.0715  -0.0664 -0.0951 776 VAL A CB  
1143 C CG1 . VAL A 168 ? 0.7566 0.7752 0.7002 0.0578  -0.0513 -0.0768 776 VAL A CG1 
1144 C CG2 . VAL A 168 ? 0.7117 0.7949 0.7107 0.0529  -0.0723 -0.1005 776 VAL A CG2 
1145 N N   . ALA A 169 ? 0.8081 0.7981 0.6174 0.1346  -0.0623 -0.0921 777 ALA A N   
1146 C CA  . ALA A 169 ? 0.8585 0.7973 0.6023 0.1534  -0.0470 -0.0797 777 ALA A CA  
1147 C C   . ALA A 169 ? 0.8920 0.8110 0.5951 0.1752  -0.0491 -0.0713 777 ALA A C   
1148 O O   . ALA A 169 ? 0.9275 0.7980 0.5940 0.1769  -0.0286 -0.0544 777 ALA A O   
1149 C CB  . ALA A 169 ? 0.8767 0.8081 0.5810 0.1752  -0.0509 -0.0913 777 ALA A CB  
1150 N N   . LYS A 170 ? 0.8779 0.8331 0.5906 0.1917  -0.0719 -0.0845 778 LYS A N   
1151 C CA  . LYS A 170 ? 0.8933 0.8323 0.5727 0.2145  -0.0751 -0.0782 778 LYS A CA  
1152 C C   . LYS A 170 ? 0.8777 0.8052 0.5805 0.1902  -0.0603 -0.0645 778 LYS A C   
1153 O O   . LYS A 170 ? 0.9109 0.7949 0.5750 0.2000  -0.0474 -0.0509 778 LYS A O   
1154 C CB  . LYS A 170 ? 0.9046 0.8935 0.6014 0.2370  -0.1033 -0.0999 778 LYS A CB  
1155 C CG  . LYS A 170 ? 0.9775 0.9769 0.6429 0.2682  -0.1232 -0.1171 778 LYS A CG  
1156 C CD  . LYS A 170 ? 1.0363 1.0851 0.7177 0.2965  -0.1536 -0.1419 778 LYS A CD  
1157 C CE  . LYS A 170 ? 1.0555 1.1725 0.8250 0.2705  -0.1629 -0.1640 778 LYS A CE  
1158 N NZ  . LYS A 170 ? 1.0773 1.2164 0.8755 0.2713  -0.1640 -0.1659 778 LYS A NZ  
1159 N N   . GLY A 171 ? 0.8247 0.7881 0.5874 0.1600  -0.0622 -0.0687 779 GLY A N   
1160 C CA  . GLY A 171 ? 0.8064 0.7651 0.5926 0.1362  -0.0523 -0.0586 779 GLY A CA  
1161 C C   . GLY A 171 ? 0.8201 0.7339 0.5915 0.1219  -0.0316 -0.0439 779 GLY A C   
1162 O O   . GLY A 171 ? 0.8404 0.7285 0.6010 0.1170  -0.0211 -0.0357 779 GLY A O   
1163 N N   . MET A 172 ? 0.8117 0.7161 0.5844 0.1157  -0.0243 -0.0435 780 MET A N   
1164 C CA  . MET A 172 ? 0.8286 0.6944 0.5948 0.1019  -0.0019 -0.0335 780 MET A CA  
1165 C C   . MET A 172 ? 0.8888 0.7003 0.5949 0.1214  0.0163  -0.0240 780 MET A C   
1166 O O   . MET A 172 ? 0.9023 0.6824 0.6065 0.1097  0.0339  -0.0165 780 MET A O   
1167 C CB  . MET A 172 ? 0.8099 0.6834 0.6000 0.0895  0.0031  -0.0376 780 MET A CB  
1168 C CG  . MET A 172 ? 0.7896 0.7011 0.6409 0.0655  -0.0084 -0.0419 780 MET A CG  
1169 S SD  . MET A 172 ? 0.8308 0.7404 0.7104 0.0434  -0.0070 -0.0344 780 MET A SD  
1170 C CE  . MET A 172 ? 0.7654 0.6392 0.6463 0.0327  0.0175  -0.0315 780 MET A CE  
1171 N N   . ALA A 173 ? 0.9138 0.7132 0.5695 0.1530  0.0103  -0.0253 781 ALA A N   
1172 C CA  . ALA A 173 ? 0.9605 0.6998 0.5486 0.1766  0.0276  -0.0130 781 ALA A CA  
1173 C C   . ALA A 173 ? 0.9742 0.7028 0.5578 0.1818  0.0258  -0.0089 781 ALA A C   
1174 O O   . ALA A 173 ? 1.0157 0.6881 0.5624 0.1864  0.0484  0.0029  781 ALA A O   
1175 C CB  . ALA A 173 ? 0.9783 0.7076 0.5076 0.2145  0.0163  -0.0156 781 ALA A CB  
1176 N N   . PHE A 174 ? 0.9396 0.7189 0.5629 0.1783  0.0030  -0.0191 782 PHE A N   
1177 C CA  . PHE A 174 ? 0.9360 0.7081 0.5580 0.1820  0.0025  -0.0177 782 PHE A CA  
1178 C C   . PHE A 174 ? 0.9458 0.6968 0.5915 0.1505  0.0217  -0.0125 782 PHE A C   
1179 O O   . PHE A 174 ? 0.9853 0.6941 0.6070 0.1543  0.0365  -0.0068 782 PHE A O   
1180 C CB  . PHE A 174 ? 0.8884 0.7218 0.5506 0.1825  -0.0219 -0.0316 782 PHE A CB  
1181 C CG  . PHE A 174 ? 0.8823 0.7116 0.5479 0.1823  -0.0200 -0.0321 782 PHE A CG  
1182 C CD1 . PHE A 174 ? 0.9058 0.7053 0.5295 0.2137  -0.0194 -0.0302 782 PHE A CD1 
1183 C CD2 . PHE A 174 ? 0.8603 0.7102 0.5656 0.1528  -0.0181 -0.0344 782 PHE A CD2 
1184 C CE1 . PHE A 174 ? 0.9036 0.6985 0.5316 0.2138  -0.0163 -0.0327 782 PHE A CE1 
1185 C CE2 . PHE A 174 ? 0.8657 0.7097 0.5692 0.1531  -0.0153 -0.0368 782 PHE A CE2 
1186 C CZ  . PHE A 174 ? 0.8818 0.6993 0.5493 0.1825  -0.0135 -0.0368 782 PHE A CZ  
1187 N N   . LEU A 175 ? 0.9105 0.6902 0.6046 0.1210  0.0202  -0.0162 783 LEU A N   
1188 C CA  . LEU A 175 ? 0.9020 0.6706 0.6256 0.0921  0.0329  -0.0156 783 LEU A CA  
1189 C C   . LEU A 175 ? 0.9561 0.6669 0.6538 0.0898  0.0627  -0.0085 783 LEU A C   
1190 O O   . LEU A 175 ? 0.9781 0.6574 0.6730 0.0814  0.0775  -0.0083 783 LEU A O   
1191 C CB  . LEU A 175 ? 0.8504 0.6601 0.6275 0.0674  0.0226  -0.0206 783 LEU A CB  
1192 C CG  . LEU A 175 ? 0.8108 0.6692 0.6181 0.0611  -0.0002 -0.0258 783 LEU A CG  
1193 C CD1 . LEU A 175 ? 0.7822 0.6664 0.6341 0.0391  -0.0071 -0.0274 783 LEU A CD1 
1194 C CD2 . LEU A 175 ? 0.8086 0.6646 0.6106 0.0593  -0.0026 -0.0277 783 LEU A CD2 
1195 N N   . ALA A 176 ? 0.9751 0.6680 0.6496 0.0986  0.0741  -0.0038 784 ALA A N   
1196 C CA  . ALA A 176 ? 1.0182 0.6518 0.6629 0.0967  0.1086  0.0041  784 ALA A CA  
1197 C C   . ALA A 176 ? 1.0828 0.6586 0.6699 0.1181  0.1237  0.0139  784 ALA A C   
1198 O O   . ALA A 176 ? 1.1042 0.6334 0.6890 0.1042  0.1526  0.0168  784 ALA A O   
1199 C CB  . ALA A 176 ? 1.0354 0.6619 0.6535 0.1085  0.1154  0.0073  784 ALA A CB  
1200 N N   . SER A 177 ? 1.0994 0.6816 0.6487 0.1506  0.1027  0.0164  785 SER A N   
1201 C CA  . SER A 177 ? 1.1389 0.6667 0.6332 0.1761  0.1130  0.0257  785 SER A CA  
1202 C C   . SER A 177 ? 1.1378 0.6581 0.6606 0.1580  0.1190  0.0204  785 SER A C   
1203 O O   . SER A 177 ? 1.1897 0.6489 0.6754 0.1678  0.1406  0.0280  785 SER A O   
1204 C CB  . SER A 177 ? 1.1690 0.7143 0.6261 0.2169  0.0850  0.0253  785 SER A CB  
1205 O OG  . SER A 177 ? 1.1928 0.7936 0.6912 0.2152  0.0584  0.0127  785 SER A OG  
1206 N N   . LYS A 178 ? 1.0810 0.6585 0.6656 0.1326  0.1009  0.0072  786 LYS A N   
1207 C CA  . LYS A 178 ? 1.0519 0.6266 0.6639 0.1135  0.1043  -0.0014 786 LYS A CA  
1208 C C   . LYS A 178 ? 1.0355 0.5974 0.6877 0.0776  0.1252  -0.0077 786 LYS A C   
1209 O O   . LYS A 178 ? 1.0183 0.5916 0.7043 0.0577  0.1220  -0.0199 786 LYS A O   
1210 C CB  . LYS A 178 ? 1.0220 0.6622 0.6705 0.1086  0.0734  -0.0125 786 LYS A CB  
1211 C CG  . LYS A 178 ? 1.0641 0.7178 0.6855 0.1407  0.0565  -0.0127 786 LYS A CG  
1212 C CD  . LYS A 178 ? 1.1566 0.7587 0.7421 0.1577  0.0702  -0.0107 786 LYS A CD  
1213 C CE  . LYS A 178 ? 1.2188 0.8458 0.7970 0.1828  0.0521  -0.0173 786 LYS A CE  
1214 N NZ  . LYS A 178 ? 1.2514 0.8598 0.8338 0.1756  0.0601  -0.0257 786 LYS A NZ  
1215 N N   . ASN A 179 ? 1.0457 0.5862 0.6959 0.0701  0.1465  -0.0021 787 ASN A N   
1216 C CA  . ASN A 179 ? 1.0359 0.5693 0.7320 0.0371  0.1684  -0.0109 787 ASN A CA  
1217 C C   . ASN A 179 ? 0.9858 0.5861 0.7499 0.0133  0.1416  -0.0261 787 ASN A C   
1218 O O   . ASN A 179 ? 0.9573 0.5627 0.7675 -0.0123 0.1471  -0.0406 787 ASN A O   
1219 C CB  . ASN A 179 ? 1.0785 0.5539 0.7704 0.0251  0.1999  -0.0148 787 ASN A CB  
1220 C CG  . ASN A 179 ? 1.1803 0.5786 0.8000 0.0491  0.2311  0.0036  787 ASN A CG  
1221 O OD1 . ASN A 179 ? 1.2182 0.5931 0.8028 0.0607  0.2470  0.0165  787 ASN A OD1 
1222 N ND2 . ASN A 179 ? 1.2204 0.5753 0.8118 0.0593  0.2398  0.0051  787 ASN A ND2 
1223 N N   . CYS A 180 ? 0.9701 0.6204 0.7398 0.0229  0.1123  -0.0236 788 CYS A N   
1224 C CA  . CYS A 180 ? 0.9361 0.6432 0.7585 0.0057  0.0861  -0.0336 788 CYS A CA  
1225 C C   . CYS A 180 ? 0.9104 0.6456 0.7630 -0.0015 0.0822  -0.0335 788 CYS A C   
1226 O O   . CYS A 180 ? 0.9228 0.6619 0.7516 0.0144  0.0800  -0.0258 788 CYS A O   
1227 C CB  . CYS A 180 ? 0.9346 0.6750 0.7473 0.0173  0.0582  -0.0331 788 CYS A CB  
1228 S SG  . CYS A 180 ? 0.9449 0.7450 0.8077 -0.0003 0.0281  -0.0404 788 CYS A SG  
1229 N N   . ILE A 181 ? 0.8685 0.6250 0.7759 -0.0243 0.0795  -0.0448 789 ILE A N   
1230 C CA  . ILE A 181 ? 0.8439 0.6290 0.7880 -0.0315 0.0743  -0.0472 789 ILE A CA  
1231 C C   . ILE A 181 ? 0.7996 0.6325 0.7705 -0.0341 0.0394  -0.0492 789 ILE A C   
1232 O O   . ILE A 181 ? 0.7881 0.6349 0.7837 -0.0452 0.0258  -0.0580 789 ILE A O   
1233 C CB  . ILE A 181 ? 0.8479 0.6248 0.8400 -0.0530 0.0956  -0.0601 789 ILE A CB  
1234 C CG1 . ILE A 181 ? 0.8978 0.6183 0.8576 -0.0520 0.1373  -0.0560 789 ILE A CG1 
1235 C CG2 . ILE A 181 ? 0.8272 0.6382 0.8655 -0.0595 0.0882  -0.0650 789 ILE A CG2 
1236 C CD1 . ILE A 181 ? 0.9088 0.6121 0.9117 -0.0760 0.1609  -0.0723 789 ILE A CD1 
1237 N N   . HIS A 182 ? 0.7759 0.6303 0.7382 -0.0233 0.0257  -0.0418 790 HIS A N   
1238 C CA  . HIS A 182 ? 0.7527 0.6443 0.7348 -0.0253 -0.0019 -0.0406 790 HIS A CA  
1239 C C   . HIS A 182 ? 0.7252 0.6378 0.7600 -0.0399 -0.0130 -0.0481 790 HIS A C   
1240 O O   . HIS A 182 ? 0.7148 0.6412 0.7611 -0.0452 -0.0314 -0.0512 790 HIS A O   
1241 C CB  . HIS A 182 ? 0.7556 0.6622 0.7237 -0.0129 -0.0086 -0.0341 790 HIS A CB  
1242 C CG  . HIS A 182 ? 0.7457 0.6821 0.7273 -0.0151 -0.0306 -0.0309 790 HIS A CG  
1243 N ND1 . HIS A 182 ? 0.7365 0.6897 0.7553 -0.0249 -0.0428 -0.0311 790 HIS A ND1 
1244 C CD2 . HIS A 182 ? 0.7461 0.6948 0.7082 -0.0077 -0.0390 -0.0273 790 HIS A CD2 
1245 C CE1 . HIS A 182 ? 0.7356 0.7044 0.7499 -0.0236 -0.0562 -0.0251 790 HIS A CE1 
1246 N NE2 . HIS A 182 ? 0.7424 0.7109 0.7261 -0.0152 -0.0529 -0.0237 790 HIS A NE2 
1247 N N   . ARG A 183 ? 0.7165 0.6305 0.7812 -0.0444 -0.0020 -0.0523 791 ARG A N   
1248 C CA  . ARG A 183 ? 0.7016 0.6368 0.8235 -0.0553 -0.0113 -0.0622 791 ARG A CA  
1249 C C   . ARG A 183 ? 0.6845 0.6459 0.8251 -0.0511 -0.0351 -0.0566 791 ARG A C   
1250 O O   . ARG A 183 ? 0.6685 0.6464 0.8559 -0.0556 -0.0440 -0.0640 791 ARG A O   
1251 C CB  . ARG A 183 ? 0.7214 0.6622 0.8691 -0.0660 -0.0204 -0.0748 791 ARG A CB  
1252 C CG  . ARG A 183 ? 0.7989 0.7178 0.9628 -0.0777 0.0084  -0.0880 791 ARG A CG  
1253 C CD  . ARG A 183 ? 0.8544 0.7801 1.0452 -0.0893 -0.0019 -0.1053 791 ARG A CD  
1254 N NE  . ARG A 183 ? 0.9018 0.8644 1.1253 -0.0882 -0.0388 -0.1119 791 ARG A NE  
1255 C CZ  . ARG A 183 ? 0.9311 0.9154 1.2081 -0.0978 -0.0521 -0.1343 791 ARG A CZ  
1256 N NH1 . ARG A 183 ? 0.9348 0.9094 1.2470 -0.1136 -0.0280 -0.1543 791 ARG A NH1 
1257 N NH2 . ARG A 183 ? 0.9189 0.9334 1.2148 -0.0909 -0.0893 -0.1377 791 ARG A NH2 
1258 N N   . ASP A 184 ? 0.6830 0.6472 0.7908 -0.0424 -0.0441 -0.0448 792 ASP A N   
1259 C CA  . ASP A 184 ? 0.6583 0.6391 0.7813 -0.0398 -0.0609 -0.0384 792 ASP A CA  
1260 C C   . ASP A 184 ? 0.6692 0.6499 0.7661 -0.0324 -0.0559 -0.0322 792 ASP A C   
1261 O O   . ASP A 184 ? 0.6794 0.6680 0.7664 -0.0308 -0.0669 -0.0247 792 ASP A O   
1262 C CB  . ASP A 184 ? 0.6583 0.6481 0.7816 -0.0404 -0.0850 -0.0329 792 ASP A CB  
1263 C CG  . ASP A 184 ? 0.7241 0.7228 0.8697 -0.0376 -0.1004 -0.0259 792 ASP A CG  
1264 O OD1 . ASP A 184 ? 0.7110 0.7122 0.8816 -0.0370 -0.0929 -0.0285 792 ASP A OD1 
1265 O OD2 . ASP A 184 ? 0.7634 0.7625 0.8969 -0.0350 -0.1189 -0.0174 792 ASP A OD2 
1266 N N   . LEU A 185 ? 0.6585 0.6298 0.7440 -0.0275 -0.0382 -0.0370 793 LEU A N   
1267 C CA  . LEU A 185 ? 0.6562 0.6321 0.7210 -0.0186 -0.0369 -0.0366 793 LEU A CA  
1268 C C   . LEU A 185 ? 0.6339 0.6221 0.7313 -0.0212 -0.0418 -0.0396 793 LEU A C   
1269 O O   . LEU A 185 ? 0.6311 0.6163 0.7530 -0.0236 -0.0341 -0.0457 793 LEU A O   
1270 C CB  . LEU A 185 ? 0.6772 0.6354 0.7086 -0.0082 -0.0195 -0.0408 793 LEU A CB  
1271 C CG  . LEU A 185 ? 0.6940 0.6599 0.7035 0.0047  -0.0217 -0.0453 793 LEU A CG  
1272 C CD1 . LEU A 185 ? 0.6928 0.6742 0.6893 0.0093  -0.0345 -0.0431 793 LEU A CD1 
1273 C CD2 . LEU A 185 ? 0.7222 0.6637 0.6915 0.0183  -0.0052 -0.0480 793 LEU A CD2 
1274 N N   . ALA A 186 ? 0.6141 0.6146 0.7146 -0.0216 -0.0523 -0.0364 794 ALA A N   
1275 C CA  . ALA A 186 ? 0.5798 0.5880 0.7108 -0.0249 -0.0566 -0.0386 794 ALA A CA  
1276 C C   . ALA A 186 ? 0.5726 0.5916 0.6966 -0.0256 -0.0606 -0.0380 794 ALA A C   
1277 O O   . ALA A 186 ? 0.5834 0.6050 0.6846 -0.0248 -0.0625 -0.0328 794 ALA A O   
1278 C CB  . ALA A 186 ? 0.5691 0.5743 0.7290 -0.0307 -0.0671 -0.0305 794 ALA A CB  
1279 N N   . ALA A 187 ? 0.5616 0.5872 0.7099 -0.0286 -0.0604 -0.0448 795 ALA A N   
1280 C CA  . ALA A 187 ? 0.5477 0.5854 0.7000 -0.0328 -0.0607 -0.0478 795 ALA A CA  
1281 C C   . ALA A 187 ? 0.5419 0.5725 0.6887 -0.0405 -0.0628 -0.0311 795 ALA A C   
1282 O O   . ALA A 187 ? 0.5326 0.5737 0.6715 -0.0432 -0.0589 -0.0327 795 ALA A O   
1283 C CB  . ALA A 187 ? 0.5298 0.5724 0.7151 -0.0373 -0.0583 -0.0605 795 ALA A CB  
1284 N N   . ARG A 188 ? 0.5486 0.5621 0.6980 -0.0424 -0.0690 -0.0165 796 ARG A N   
1285 C CA  . ARG A 188 ? 0.5626 0.5636 0.6952 -0.0465 -0.0722 0.0009  796 ARG A CA  
1286 C C   . ARG A 188 ? 0.5871 0.5926 0.6840 -0.0437 -0.0730 0.0037  796 ARG A C   
1287 O O   . ARG A 188 ? 0.6184 0.6156 0.6940 -0.0468 -0.0721 0.0153  796 ARG A O   
1288 C CB  . ARG A 188 ? 0.5642 0.5467 0.7048 -0.0438 -0.0842 0.0136  796 ARG A CB  
1289 C CG  . ARG A 188 ? 0.5629 0.5504 0.7053 -0.0378 -0.0933 0.0084  796 ARG A CG  
1290 C CD  . ARG A 188 ? 0.5664 0.5447 0.7274 -0.0327 -0.1090 0.0146  796 ARG A CD  
1291 N NE  . ARG A 188 ? 0.5957 0.5850 0.7714 -0.0305 -0.1122 0.0027  796 ARG A NE  
1292 C CZ  . ARG A 188 ? 0.6113 0.6075 0.8197 -0.0304 -0.1047 -0.0103 796 ARG A CZ  
1293 N NH1 . ARG A 188 ? 0.6076 0.6021 0.8372 -0.0306 -0.0975 -0.0140 796 ARG A NH1 
1294 N NH2 . ARG A 188 ? 0.5852 0.5888 0.8057 -0.0312 -0.1016 -0.0213 796 ARG A NH2 
1295 N N   . ASN A 189 ? 0.5687 0.5828 0.6554 -0.0373 -0.0723 -0.0064 797 ASN A N   
1296 C CA  . ASN A 189 ? 0.5738 0.5891 0.6286 -0.0334 -0.0715 -0.0059 797 ASN A CA  
1297 C C   . ASN A 189 ? 0.5995 0.6304 0.6451 -0.0271 -0.0638 -0.0178 797 ASN A C   
1298 O O   . ASN A 189 ? 0.6228 0.6520 0.6444 -0.0195 -0.0623 -0.0207 797 ASN A O   
1299 C CB  . ASN A 189 ? 0.5538 0.5596 0.6011 -0.0301 -0.0758 -0.0072 797 ASN A CB  
1300 C CG  . ASN A 189 ? 0.5580 0.5549 0.6101 -0.0334 -0.0884 0.0011  797 ASN A CG  
1301 O OD1 . ASN A 189 ? 0.5896 0.5812 0.6264 -0.0351 -0.0943 0.0116  797 ASN A OD1 
1302 N ND2 . ASN A 189 ? 0.5370 0.5318 0.6111 -0.0334 -0.0926 -0.0043 797 ASN A ND2 
1303 N N   . ILE A 190 ? 0.5987 0.6445 0.6651 -0.0289 -0.0601 -0.0266 798 ILE A N   
1304 C CA  . ILE A 190 ? 0.6037 0.6708 0.6677 -0.0203 -0.0575 -0.0420 798 ILE A CA  
1305 C C   . ILE A 190 ? 0.6136 0.6969 0.6972 -0.0302 -0.0508 -0.0452 798 ILE A C   
1306 O O   . ILE A 190 ? 0.6017 0.6803 0.7102 -0.0421 -0.0470 -0.0421 798 ILE A O   
1307 C CB  . ILE A 190 ? 0.5877 0.6619 0.6621 -0.0117 -0.0600 -0.0568 798 ILE A CB  
1308 C CG1 . ILE A 190 ? 0.6058 0.6589 0.6550 -0.0025 -0.0595 -0.0525 798 ILE A CG1 
1309 C CG2 . ILE A 190 ? 0.5812 0.6825 0.6561 -0.0002 -0.0627 -0.0758 798 ILE A CG2 
1310 C CD1 . ILE A 190 ? 0.6134 0.6623 0.6683 0.0021  -0.0580 -0.0609 798 ILE A CD1 
1311 N N   . LEU A 191 ? 0.6209 0.7190 0.6938 -0.0263 -0.0466 -0.0501 799 LEU A N   
1312 C CA  . LEU A 191 ? 0.6275 0.7423 0.7233 -0.0378 -0.0348 -0.0554 799 LEU A CA  
1313 C C   . LEU A 191 ? 0.6253 0.7785 0.7530 -0.0314 -0.0361 -0.0828 799 LEU A C   
1314 O O   . LEU A 191 ? 0.6241 0.7886 0.7404 -0.0127 -0.0478 -0.0947 799 LEU A O   
1315 C CB  . LEU A 191 ? 0.6386 0.7474 0.7081 -0.0402 -0.0258 -0.0452 799 LEU A CB  
1316 C CG  . LEU A 191 ? 0.6659 0.7405 0.7006 -0.0441 -0.0284 -0.0221 799 LEU A CG  
1317 C CD1 . LEU A 191 ? 0.6735 0.7445 0.6791 -0.0448 -0.0193 -0.0167 799 LEU A CD1 
1318 C CD2 . LEU A 191 ? 0.6711 0.7256 0.7160 -0.0568 -0.0250 -0.0082 799 LEU A CD2 
1319 N N   . LEU A 192 ? 0.6200 0.7913 0.7871 -0.0461 -0.0241 -0.0937 800 LEU A N   
1320 C CA  . LEU A 192 ? 0.6157 0.8302 0.8235 -0.0418 -0.0269 -0.1250 800 LEU A CA  
1321 C C   . LEU A 192 ? 0.6137 0.8514 0.8424 -0.0501 -0.0101 -0.1336 800 LEU A C   
1322 O O   . LEU A 192 ? 0.6059 0.8245 0.8361 -0.0697 0.0107  -0.1185 800 LEU A O   
1323 C CB  . LEU A 192 ? 0.6094 0.8291 0.8610 -0.0555 -0.0249 -0.1383 800 LEU A CB  
1324 C CG  . LEU A 192 ? 0.6013 0.8668 0.8932 -0.0470 -0.0362 -0.1759 800 LEU A CG  
1325 C CD1 . LEU A 192 ? 0.6115 0.8753 0.8724 -0.0225 -0.0589 -0.1816 800 LEU A CD1 
1326 C CD2 . LEU A 192 ? 0.5926 0.8676 0.9422 -0.0694 -0.0249 -0.1934 800 LEU A CD2 
1327 N N   . THR A 193 ? 0.6300 0.9073 0.8738 -0.0343 -0.0179 -0.1579 801 THR A N   
1328 C CA  . THR A 193 ? 0.6616 0.9677 0.9339 -0.0416 0.0000  -0.1708 801 THR A CA  
1329 C C   . THR A 193 ? 0.6670 1.0326 1.0057 -0.0378 -0.0060 -0.2130 801 THR A C   
1330 O O   . THR A 193 ? 0.6527 1.0325 1.0108 -0.0314 -0.0240 -0.2306 801 THR A O   
1331 C CB  . THR A 193 ? 0.6968 0.9927 0.9230 -0.0256 -0.0008 -0.1582 801 THR A CB  
1332 O OG1 . THR A 193 ? 0.6919 1.0150 0.9463 -0.0336 0.0203  -0.1711 801 THR A OG1 
1333 C CG2 . THR A 193 ? 0.7049 1.0089 0.9056 0.0066  -0.0269 -0.1669 801 THR A CG2 
1334 N N   . HIS A 194 ? 0.6823 1.0840 1.0595 -0.0430 0.0102  -0.2319 802 HIS A N   
1335 C CA  . HIS A 194 ? 0.6776 1.1434 1.1283 -0.0404 0.0054  -0.2765 802 HIS A CA  
1336 C C   . HIS A 194 ? 0.6780 1.1721 1.1217 -0.0047 -0.0340 -0.2987 802 HIS A C   
1337 O O   . HIS A 194 ? 0.7137 1.1917 1.1022 0.0233  -0.0507 -0.2853 802 HIS A O   
1338 C CB  . HIS A 194 ? 0.7016 1.1996 1.1840 -0.0448 0.0277  -0.2904 802 HIS A CB  
1339 C CG  . HIS A 194 ? 0.7886 1.2638 1.2863 -0.0814 0.0709  -0.2758 802 HIS A CG  
1340 N ND1 . HIS A 194 ? 0.8020 1.2934 1.3671 -0.1108 0.0926  -0.2952 802 HIS A ND1 
1341 C CD2 . HIS A 194 ? 0.8451 1.2792 1.2946 -0.0917 0.0963  -0.2441 802 HIS A CD2 
1342 C CE1 . HIS A 194 ? 0.8313 1.2866 1.3832 -0.1372 0.1329  -0.2718 802 HIS A CE1 
1343 N NE2 . HIS A 194 ? 0.8640 1.2851 1.3444 -0.1258 0.1351  -0.2409 802 HIS A NE2 
1344 N N   . GLY A 195 ? 0.6409 1.1699 1.1342 -0.0058 -0.0478 -0.3310 803 GLY A N   
1345 C CA  . GLY A 195 ? 0.6421 1.1943 1.1217 0.0293  -0.0866 -0.3528 803 GLY A CA  
1346 C C   . GLY A 195 ? 0.6763 1.1831 1.1032 0.0343  -0.0998 -0.3324 803 GLY A C   
1347 O O   . GLY A 195 ? 0.6900 1.2046 1.0900 0.0642  -0.1294 -0.3454 803 GLY A O   
1348 N N   . ARG A 196 ? 0.6849 1.1440 1.0965 0.0064  -0.0776 -0.3015 804 ARG A N   
1349 C CA  . ARG A 196 ? 0.7056 1.1201 1.0727 0.0079  -0.0847 -0.2802 804 ARG A CA  
1350 C C   . ARG A 196 ? 0.7051 1.0893 0.9962 0.0381  -0.1003 -0.2582 804 ARG A C   
1351 O O   . ARG A 196 ? 0.7230 1.0980 0.9813 0.0589  -0.1192 -0.2623 804 ARG A O   
1352 C CB  . ARG A 196 ? 0.7272 1.1625 1.1306 0.0054  -0.0978 -0.3103 804 ARG A CB  
1353 C CG  . ARG A 196 ? 0.7890 1.2301 1.2593 -0.0326 -0.0727 -0.3199 804 ARG A CG  
1354 C CD  . ARG A 196 ? 0.8400 1.2861 1.3447 -0.0423 -0.0791 -0.3436 804 ARG A CD  
1355 N NE  . ARG A 196 ? 0.8790 1.3178 1.4424 -0.0800 -0.0493 -0.3465 804 ARG A NE  
1356 C CZ  . ARG A 196 ? 0.9147 1.3530 1.5202 -0.0964 -0.0463 -0.3670 804 ARG A CZ  
1357 N NH1 . ARG A 196 ? 0.9222 1.3709 1.5174 -0.0784 -0.0726 -0.3886 804 ARG A NH1 
1358 N NH2 . ARG A 196 ? 0.9050 1.3279 1.5597 -0.1306 -0.0150 -0.3660 804 ARG A NH2 
1359 N N   . ILE A 197 ? 0.6829 1.0492 0.9452 0.0398  -0.0895 -0.2358 805 ILE A N   
1360 C CA  . ILE A 197 ? 0.6868 1.0190 0.8817 0.0636  -0.0977 -0.2139 805 ILE A CA  
1361 C C   . ILE A 197 ? 0.6744 0.9548 0.8365 0.0453  -0.0832 -0.1788 805 ILE A C   
1362 O O   . ILE A 197 ? 0.6702 0.9413 0.8454 0.0223  -0.0650 -0.1651 805 ILE A O   
1363 C CB  . ILE A 197 ? 0.6936 1.0415 0.8837 0.0773  -0.0955 -0.2165 805 ILE A CB  
1364 C CG1 . ILE A 197 ? 0.6681 1.0765 0.9034 0.0968  -0.1121 -0.2563 805 ILE A CG1 
1365 C CG2 . ILE A 197 ? 0.7362 1.0413 0.8568 0.0996  -0.0999 -0.1927 805 ILE A CG2 
1366 C CD1 . ILE A 197 ? 0.6883 1.1039 0.8983 0.1302  -0.1422 -0.2727 805 ILE A CD1 
1367 N N   . THR A 198 ? 0.6697 0.9175 0.7917 0.0552  -0.0906 -0.1662 806 THR A N   
1368 C CA  . THR A 198 ? 0.6709 0.8751 0.7690 0.0400  -0.0796 -0.1374 806 THR A CA  
1369 C C   . THR A 198 ? 0.6612 0.8375 0.7129 0.0509  -0.0769 -0.1189 806 THR A C   
1370 O O   . THR A 198 ? 0.6716 0.8414 0.6898 0.0758  -0.0853 -0.1223 806 THR A O   
1371 C CB  . THR A 198 ? 0.7048 0.8892 0.7931 0.0409  -0.0840 -0.1355 806 THR A CB  
1372 O OG1 . THR A 198 ? 0.7476 0.9250 0.7960 0.0684  -0.0951 -0.1419 806 THR A OG1 
1373 C CG2 . THR A 198 ? 0.6751 0.8799 0.8104 0.0266  -0.0844 -0.1527 806 THR A CG2 
1374 N N   . LYS A 199 ? 0.6435 0.8009 0.6911 0.0334  -0.0654 -0.0999 807 LYS A N   
1375 C CA  . LYS A 199 ? 0.6456 0.7758 0.6542 0.0392  -0.0617 -0.0845 807 LYS A CA  
1376 C C   . LYS A 199 ? 0.6381 0.7349 0.6345 0.0253  -0.0581 -0.0652 807 LYS A C   
1377 O O   . LYS A 199 ? 0.6375 0.7336 0.6555 0.0076  -0.0552 -0.0587 807 LYS A O   
1378 C CB  . LYS A 199 ? 0.6459 0.7897 0.6599 0.0337  -0.0533 -0.0852 807 LYS A CB  
1379 C CG  . LYS A 199 ? 0.6407 0.8244 0.6775 0.0479  -0.0566 -0.1082 807 LYS A CG  
1380 C CD  . LYS A 199 ? 0.6547 0.8521 0.6998 0.0411  -0.0435 -0.1102 807 LYS A CD  
1381 C CE  . LYS A 199 ? 0.6696 0.9007 0.7273 0.0641  -0.0496 -0.1326 807 LYS A CE  
1382 N NZ  . LYS A 199 ? 0.7000 0.9056 0.7116 0.0886  -0.0561 -0.1264 807 LYS A NZ  
1383 N N   . ILE A 200 ? 0.6354 0.7038 0.5995 0.0340  -0.0578 -0.0572 808 ILE A N   
1384 C CA  . ILE A 200 ? 0.6285 0.6705 0.5885 0.0219  -0.0552 -0.0440 808 ILE A CA  
1385 C C   . ILE A 200 ? 0.6145 0.6483 0.5663 0.0114  -0.0535 -0.0346 808 ILE A C   
1386 O O   . ILE A 200 ? 0.6044 0.6374 0.5364 0.0184  -0.0508 -0.0366 808 ILE A O   
1387 C CB  . ILE A 200 ? 0.6547 0.6684 0.5878 0.0333  -0.0510 -0.0422 808 ILE A CB  
1388 C CG1 . ILE A 200 ? 0.6581 0.6747 0.5918 0.0435  -0.0521 -0.0502 808 ILE A CG1 
1389 C CG2 . ILE A 200 ? 0.6658 0.6551 0.6008 0.0199  -0.0465 -0.0329 808 ILE A CG2 
1390 C CD1 . ILE A 200 ? 0.6982 0.6887 0.5936 0.0609  -0.0459 -0.0493 808 ILE A CD1 
1391 N N   A CYS A 201 ? 0.6031 0.6305 0.5687 -0.0033 -0.0564 -0.0255 809 CYS A N   
1392 N N   B CYS A 201 ? 0.6107 0.6373 0.5755 -0.0032 -0.0564 -0.0254 809 CYS A N   
1393 C CA  A CYS A 201 ? 0.6047 0.6230 0.5582 -0.0119 -0.0586 -0.0168 809 CYS A CA  
1394 C CA  B CYS A 201 ? 0.6198 0.6356 0.5698 -0.0106 -0.0585 -0.0173 809 CYS A CA  
1395 C C   A CYS A 201 ? 0.6128 0.6152 0.5747 -0.0188 -0.0667 -0.0108 809 CYS A C   
1396 C C   B CYS A 201 ? 0.6192 0.6208 0.5799 -0.0186 -0.0667 -0.0110 809 CYS A C   
1397 O O   A CYS A 201 ? 0.6018 0.5994 0.5783 -0.0175 -0.0658 -0.0144 809 CYS A O   
1398 O O   B CYS A 201 ? 0.6076 0.6046 0.5837 -0.0176 -0.0659 -0.0143 809 CYS A O   
1399 C CB  A CYS A 201 ? 0.5834 0.6138 0.5452 -0.0203 -0.0553 -0.0122 809 CYS A CB  
1400 C CB  B CYS A 201 ? 0.6191 0.6465 0.5675 -0.0170 -0.0547 -0.0135 809 CYS A CB  
1401 S SG  A CYS A 201 ? 0.6037 0.6223 0.5328 -0.0256 -0.0541 -0.0027 809 CYS A SG  
1402 S SG  B CYS A 201 ? 0.6516 0.6760 0.6209 -0.0303 -0.0567 -0.0017 809 CYS A SG  
1403 N N   . ASP A 202 ? 0.6274 0.6228 0.5792 -0.0247 -0.0746 -0.0038 810 ASP A N   
1404 C CA  . ASP A 202 ? 0.6366 0.6239 0.6014 -0.0291 -0.0873 -0.0008 810 ASP A CA  
1405 C C   . ASP A 202 ? 0.6514 0.6335 0.5953 -0.0311 -0.0963 0.0094  810 ASP A C   
1406 O O   . ASP A 202 ? 0.6675 0.6449 0.5812 -0.0298 -0.0972 0.0077  810 ASP A O   
1407 C CB  . ASP A 202 ? 0.6592 0.6378 0.6234 -0.0290 -0.0893 -0.0106 810 ASP A CB  
1408 C CG  . ASP A 202 ? 0.7309 0.7097 0.7258 -0.0334 -0.1018 -0.0138 810 ASP A CG  
1409 O OD1 . ASP A 202 ? 0.7507 0.7340 0.7611 -0.0334 -0.1126 -0.0061 810 ASP A OD1 
1410 O OD2 . ASP A 202 ? 0.7532 0.7273 0.7599 -0.0364 -0.1002 -0.0252 810 ASP A OD2 
1411 N N   . PHE A 203 ? 0.6491 0.6278 0.6039 -0.0330 -0.1020 0.0201  811 PHE A N   
1412 C CA  . PHE A 203 ? 0.6669 0.6319 0.5916 -0.0320 -0.1100 0.0334  811 PHE A CA  
1413 C C   . PHE A 203 ? 0.6883 0.6479 0.5992 -0.0271 -0.1311 0.0297  811 PHE A C   
1414 O O   . PHE A 203 ? 0.7122 0.6612 0.5819 -0.0240 -0.1365 0.0353  811 PHE A O   
1415 C CB  . PHE A 203 ? 0.6652 0.6195 0.6023 -0.0331 -0.1104 0.0474  811 PHE A CB  
1416 C CG  . PHE A 203 ? 0.6730 0.6291 0.6122 -0.0403 -0.0881 0.0512  811 PHE A CG  
1417 C CD1 . PHE A 203 ? 0.6659 0.6398 0.6409 -0.0439 -0.0777 0.0395  811 PHE A CD1 
1418 C CD2 . PHE A 203 ? 0.7062 0.6471 0.6114 -0.0435 -0.0764 0.0638  811 PHE A CD2 
1419 C CE1 . PHE A 203 ? 0.6733 0.6550 0.6590 -0.0511 -0.0593 0.0373  811 PHE A CE1 
1420 C CE2 . PHE A 203 ? 0.7142 0.6604 0.6315 -0.0530 -0.0526 0.0632  811 PHE A CE2 
1421 C CZ  . PHE A 203 ? 0.6849 0.6542 0.6464 -0.0570 -0.0458 0.0483  811 PHE A CZ  
1422 N N   . GLY A 204 ? 0.6826 0.6505 0.6277 -0.0267 -0.1420 0.0178  812 GLY A N   
1423 C CA  . GLY A 204 ? 0.7053 0.6746 0.6489 -0.0231 -0.1638 0.0080  812 GLY A CA  
1424 C C   . GLY A 204 ? 0.7554 0.7139 0.6722 -0.0135 -0.1866 0.0197  812 GLY A C   
1425 O O   . GLY A 204 ? 0.7584 0.7101 0.6870 -0.0090 -0.1916 0.0325  812 GLY A O   
1426 N N   . LEU A 205 ? 0.7902 0.7428 0.6644 -0.0086 -0.1998 0.0161  813 LEU A N   
1427 C CA  . LEU A 205 ? 0.8306 0.7672 0.6646 0.0046  -0.2223 0.0290  813 LEU A CA  
1428 C C   . LEU A 205 ? 0.8835 0.7942 0.6767 0.0061  -0.2048 0.0561  813 LEU A C   
1429 O O   . LEU A 205 ? 0.9138 0.8018 0.6695 0.0186  -0.2193 0.0725  813 LEU A O   
1430 C CB  . LEU A 205 ? 0.8515 0.7872 0.6438 0.0103  -0.2398 0.0163  813 LEU A CB  
1431 C CG  . LEU A 205 ? 0.8529 0.8121 0.6867 0.0106  -0.2645 -0.0126 813 LEU A CG  
1432 C CD1 . LEU A 205 ? 0.8774 0.8341 0.6642 0.0176  -0.2849 -0.0267 813 LEU A CD1 
1433 C CD2 . LEU A 205 ? 0.8344 0.8054 0.7131 0.0206  -0.2914 -0.0147 813 LEU A CD2 
1434 N N   . ALA A 206 ? 0.8963 0.8088 0.6967 -0.0058 -0.1735 0.0600  814 ALA A N   
1435 C CA  . ALA A 206 ? 0.9321 0.8234 0.7071 -0.0088 -0.1520 0.0811  814 ALA A CA  
1436 C C   . ALA A 206 ? 0.9542 0.8394 0.7678 -0.0097 -0.1496 0.0915  814 ALA A C   
1437 O O   . ALA A 206 ? 0.9651 0.8391 0.7788 -0.0175 -0.1258 0.1024  814 ALA A O   
1438 C CB  . ALA A 206 ? 0.9244 0.8256 0.6964 -0.0203 -0.1214 0.0760  814 ALA A CB  
1439 N N   . ARG A 207 ? 0.9623 0.8548 0.8115 -0.0020 -0.1730 0.0861  815 ARG A N   
1440 C CA  . ARG A 207 ? 0.9864 0.8696 0.8698 0.0001  -0.1732 0.0953  815 ARG A CA  
1441 C C   . ARG A 207 ? 1.0378 0.9125 0.9218 0.0183  -0.2067 0.0990  815 ARG A C   
1442 O O   . ARG A 207 ? 1.0361 0.9301 0.9283 0.0248  -0.2305 0.0828  815 ARG A O   
1443 C CB  . ARG A 207 ? 0.9585 0.8656 0.9023 -0.0107 -0.1591 0.0806  815 ARG A CB  
1444 C CG  . ARG A 207 ? 0.9367 0.8631 0.9322 -0.0061 -0.1763 0.0653  815 ARG A CG  
1445 C CD  . ARG A 207 ? 0.9120 0.8454 0.9571 -0.0119 -0.1628 0.0601  815 ARG A CD  
1446 N NE  . ARG A 207 ? 0.9151 0.8549 0.9602 -0.0240 -0.1366 0.0564  815 ARG A NE  
1447 C CZ  . ARG A 207 ? 0.9122 0.8715 0.9627 -0.0294 -0.1265 0.0415  815 ARG A CZ  
1448 N NH1 . ARG A 207 ? 0.9163 0.8867 0.9726 -0.0273 -0.1355 0.0297  815 ARG A NH1 
1449 N NH2 . ARG A 207 ? 0.8992 0.8657 0.9492 -0.0362 -0.1075 0.0374  815 ARG A NH2 
1450 N N   . ASP A 208 ? 1.0814 0.9260 0.9558 0.0273  -0.2087 0.1191  816 ASP A N   
1451 C CA  . ASP A 208 ? 1.1225 0.9541 0.9942 0.0498  -0.2422 0.1257  816 ASP A CA  
1452 C C   . ASP A 208 ? 1.1028 0.9632 1.0546 0.0507  -0.2530 0.1072  816 ASP A C   
1453 O O   . ASP A 208 ? 1.1022 0.9464 1.0793 0.0548  -0.2486 0.1167  816 ASP A O   
1454 C CB  . ASP A 208 ? 1.1936 0.9725 1.0212 0.0588  -0.2328 0.1575  816 ASP A CB  
1455 C CG  . ASP A 208 ? 1.3062 1.0590 1.1118 0.0880  -0.2674 0.1711  816 ASP A CG  
1456 O OD1 . ASP A 208 ? 1.3103 1.0918 1.1367 0.1026  -0.3036 0.1529  816 ASP A OD1 
1457 O OD2 . ASP A 208 ? 1.3697 1.0719 1.1387 0.0972  -0.2583 0.1991  816 ASP A OD2 
1458 N N   . ILE A 209 ? 1.0839 0.9841 1.0763 0.0459  -0.2632 0.0803  817 ILE A N   
1459 C CA  . ILE A 209 ? 1.0689 0.9967 1.1374 0.0447  -0.2674 0.0609  817 ILE A CA  
1460 C C   . ILE A 209 ? 1.0896 1.0125 1.1811 0.0682  -0.2993 0.0635  817 ILE A C   
1461 O O   . ILE A 209 ? 1.0704 1.0027 1.2196 0.0698  -0.2969 0.0561  817 ILE A O   
1462 C CB  . ILE A 209 ? 1.0452 1.0106 1.1513 0.0327  -0.2654 0.0322  817 ILE A CB  
1463 C CG1 . ILE A 209 ? 1.0618 1.0388 1.1480 0.0413  -0.2941 0.0202  817 ILE A CG1 
1464 C CG2 . ILE A 209 ? 1.0455 1.0137 1.1420 0.0129  -0.2315 0.0295  817 ILE A CG2 
1465 C CD1 . ILE A 209 ? 1.0511 1.0628 1.1878 0.0294  -0.2927 -0.0111 817 ILE A CD1 
1466 N N   . LYS A 210 ? 1.1233 1.0288 1.1651 0.0889  -0.3291 0.0746  818 LYS A N   
1467 C CA  . LYS A 210 ? 1.1378 1.0323 1.1875 0.1177  -0.3636 0.0808  818 LYS A CA  
1468 C C   . LYS A 210 ? 1.1551 1.0117 1.2090 0.1221  -0.3467 0.1043  818 LYS A C   
1469 O O   . LYS A 210 ? 1.1508 1.0034 1.2375 0.1432  -0.3682 0.1046  818 LYS A O   
1470 C CB  . LYS A 210 ? 1.2036 1.0725 1.1724 0.1399  -0.3928 0.0955  818 LYS A CB  
1471 C CG  . LYS A 210 ? 1.2524 1.1335 1.2346 0.1727  -0.4439 0.0853  818 LYS A CG  
1472 C CD  . LYS A 210 ? 1.3499 1.2253 1.2585 0.1876  -0.4726 0.0847  818 LYS A CD  
1473 C CE  . LYS A 210 ? 1.3939 1.2954 1.3229 0.2198  -0.5296 0.0641  818 LYS A CE  
1474 N NZ  . LYS A 210 ? 1.4400 1.3466 1.3061 0.2299  -0.5576 0.0534  818 LYS A NZ  
1475 N N   . ASN A 211 ? 1.1650 0.9957 1.1916 0.1025  -0.3083 0.1208  819 ASN A N   
1476 C CA  . ASN A 211 ? 1.1747 0.9683 1.2069 0.1023  -0.2882 0.1398  819 ASN A CA  
1477 C C   . ASN A 211 ? 1.1338 0.9441 1.2109 0.0748  -0.2513 0.1276  819 ASN A C   
1478 O O   . ASN A 211 ? 1.1492 0.9288 1.2113 0.0641  -0.2240 0.1425  819 ASN A O   
1479 C CB  . ASN A 211 ? 1.2555 0.9904 1.2053 0.1096  -0.2792 0.1741  819 ASN A CB  
1480 C CG  . ASN A 211 ? 1.3601 1.0683 1.2616 0.1442  -0.3185 0.1894  819 ASN A CG  
1481 O OD1 . ASN A 211 ? 1.3843 1.0895 1.3180 0.1680  -0.3453 0.1883  819 ASN A OD1 
1482 N ND2 . ASN A 211 ? 1.4081 1.0971 1.2303 0.1502  -0.3246 0.2023  819 ASN A ND2 
1483 N N   . ASP A 212 ? 1.0800 0.9374 1.2119 0.0641  -0.2501 0.0992  820 ASP A N   
1484 C CA  . ASP A 212 ? 1.0469 0.9228 1.2179 0.0425  -0.2198 0.0844  820 ASP A CA  
1485 C C   . ASP A 212 ? 1.0022 0.9085 1.2438 0.0467  -0.2277 0.0610  820 ASP A C   
1486 O O   . ASP A 212 ? 0.9885 0.9272 1.2525 0.0467  -0.2393 0.0424  820 ASP A O   
1487 C CB  . ASP A 212 ? 1.0559 0.9535 1.2049 0.0244  -0.2036 0.0749  820 ASP A CB  
1488 C CG  . ASP A 212 ? 1.0786 0.9878 1.2484 0.0058  -0.1733 0.0641  820 ASP A CG  
1489 O OD1 . ASP A 212 ? 1.0639 0.9860 1.2817 0.0043  -0.1676 0.0497  820 ASP A OD1 
1490 O OD2 . ASP A 212 ? 1.1018 1.0087 1.2394 -0.0056 -0.1562 0.0682  820 ASP A OD2 
1491 N N   . SER A 213 ? 0.9797 0.8750 1.2587 0.0490  -0.2187 0.0600  821 SER A N   
1492 C CA  . SER A 213 ? 0.9430 0.8647 1.2909 0.0539  -0.2227 0.0374  821 SER A CA  
1493 C C   . SER A 213 ? 0.9109 0.8659 1.2880 0.0352  -0.1996 0.0130  821 SER A C   
1494 O O   . SER A 213 ? 0.8847 0.8612 1.3165 0.0366  -0.1965 -0.0070 821 SER A O   
1495 C CB  . SER A 213 ? 0.9616 0.8578 1.3380 0.0634  -0.2189 0.0428  821 SER A CB  
1496 O OG  . SER A 213 ? 1.0035 0.8865 1.3764 0.0459  -0.1885 0.0426  821 SER A OG  
1497 N N   . ASN A 214 ? 0.9124 0.8696 1.2513 0.0193  -0.1823 0.0148  822 ASN A N   
1498 C CA  . ASN A 214 ? 0.8881 0.8696 1.2406 0.0055  -0.1621 -0.0046 822 ASN A CA  
1499 C C   . ASN A 214 ? 0.8718 0.8769 1.2339 0.0054  -0.1729 -0.0170 822 ASN A C   
1500 O O   . ASN A 214 ? 0.8536 0.8761 1.2401 -0.0032 -0.1566 -0.0349 822 ASN A O   
1501 C CB  . ASN A 214 ? 0.9054 0.8800 1.2178 -0.0076 -0.1412 0.0001  822 ASN A CB  
1502 C CG  . ASN A 214 ? 0.9375 0.8955 1.2559 -0.0104 -0.1285 0.0035  822 ASN A CG  
1503 O OD1 . ASN A 214 ? 0.9339 0.8955 1.2889 -0.0100 -0.1198 -0.0097 822 ASN A OD1 
1504 N ND2 . ASN A 214 ? 0.9604 0.8992 1.2453 -0.0146 -0.1249 0.0192  822 ASN A ND2 
1505 N N   . TYR A 215 ? 0.8781 0.8815 1.2220 0.0154  -0.1997 -0.0089 823 TYR A N   
1506 C CA  . TYR A 215 ? 0.8783 0.9052 1.2370 0.0157  -0.2144 -0.0243 823 TYR A CA  
1507 C C   . TYR A 215 ? 0.9113 0.9534 1.3226 0.0326  -0.2415 -0.0346 823 TYR A C   
1508 O O   . TYR A 215 ? 0.9303 0.9560 1.3241 0.0511  -0.2672 -0.0192 823 TYR A O   
1509 C CB  . TYR A 215 ? 0.8709 0.8881 1.1706 0.0171  -0.2285 -0.0125 823 TYR A CB  
1510 C CG  . TYR A 215 ? 0.8616 0.8694 1.1178 0.0022  -0.2026 -0.0064 823 TYR A CG  
1511 C CD1 . TYR A 215 ? 0.8741 0.8592 1.0921 0.0002  -0.1905 0.0127  823 TYR A CD1 
1512 C CD2 . TYR A 215 ? 0.8503 0.8714 1.1091 -0.0099 -0.1880 -0.0216 823 TYR A CD2 
1513 C CE1 . TYR A 215 ? 0.8875 0.8702 1.0743 -0.0114 -0.1686 0.0144  823 TYR A CE1 
1514 C CE2 . TYR A 215 ? 0.8658 0.8779 1.0857 -0.0193 -0.1663 -0.0165 823 TYR A CE2 
1515 C CZ  . TYR A 215 ? 0.8878 0.8840 1.0734 -0.0191 -0.1586 0.0004  823 TYR A CZ  
1516 O OH  . TYR A 215 ? 0.9065 0.8998 1.0610 -0.0261 -0.1398 0.0019  823 TYR A OH  
1517 N N   . VAL A 216 ? 0.9100 0.9814 1.3858 0.0275  -0.2342 -0.0607 824 VAL A N   
1518 C CA  . VAL A 216 ? 0.9138 1.0070 1.4533 0.0440  -0.2584 -0.0758 824 VAL A CA  
1519 C C   . VAL A 216 ? 0.9286 1.0539 1.4966 0.0459  -0.2823 -0.0979 824 VAL A C   
1520 O O   . VAL A 216 ? 0.9252 1.0619 1.4928 0.0274  -0.2653 -0.1113 824 VAL A O   
1521 C CB  . VAL A 216 ? 0.8946 1.0002 1.4991 0.0403  -0.2349 -0.0924 824 VAL A CB  
1522 C CG1 . VAL A 216 ? 0.8751 0.9950 1.5382 0.0637  -0.2631 -0.1013 824 VAL A CG1 
1523 C CG2 . VAL A 216 ? 0.9210 0.9972 1.4926 0.0329  -0.2067 -0.0765 824 VAL A CG2 
1524 N N   . VAL A 217 ? 0.9461 1.0838 1.5364 0.0700  -0.3233 -0.1021 825 VAL A N   
1525 C CA  . VAL A 217 ? 0.9561 1.1297 1.5802 0.0760  -0.3545 -0.1278 825 VAL A CA  
1526 C C   . VAL A 217 ? 0.9352 1.1520 1.6548 0.0610  -0.3365 -0.1660 825 VAL A C   
1527 O O   . VAL A 217 ? 0.9082 1.1464 1.6975 0.0720  -0.3416 -0.1809 825 VAL A O   
1528 C CB  . VAL A 217 ? 0.9712 1.1464 1.5929 0.1114  -0.4069 -0.1229 825 VAL A CB  
1529 C CG1 . VAL A 217 ? 0.9538 1.1688 1.6040 0.1191  -0.4444 -0.1526 825 VAL A CG1 
1530 C CG2 . VAL A 217 ? 1.0303 1.1530 1.5538 0.1256  -0.4164 -0.0816 825 VAL A CG2 
1531 N N   . LYS A 218 ? 0.9442 1.1710 1.6676 0.0360  -0.3124 -0.1818 826 LYS A N   
1532 C CA  . LYS A 218 ? 0.9291 1.1913 1.7389 0.0177  -0.2885 -0.2182 826 LYS A CA  
1533 C C   . LYS A 218 ? 0.9166 1.2288 1.8000 0.0274  -0.3280 -0.2551 826 LYS A C   
1534 O O   . LYS A 218 ? 0.8882 1.2337 1.8482 0.0088  -0.3094 -0.2905 826 LYS A O   
1535 C CB  . LYS A 218 ? 0.9667 1.2115 1.7444 -0.0116 -0.2468 -0.2187 826 LYS A CB  
1536 C CG  . LYS A 218 ? 0.9834 1.2423 1.8271 -0.0349 -0.2015 -0.2445 826 LYS A CG  
1537 C CD  . LYS A 218 ? 1.0409 1.2741 1.8678 -0.0390 -0.1625 -0.2280 826 LYS A CD  
1538 C CE  . LYS A 218 ? 1.0648 1.3002 1.9340 -0.0628 -0.1113 -0.2488 826 LYS A CE  
1539 N NZ  . LYS A 218 ? 1.1045 1.3144 1.9507 -0.0645 -0.0748 -0.2350 826 LYS A NZ  
1540 N N   . GLY A 219 ? 0.9325 1.2485 1.7915 0.0567  -0.3811 -0.2477 827 GLY A N   
1541 C CA  . GLY A 219 ? 0.9076 1.2703 1.8222 0.0717  -0.4281 -0.2818 827 GLY A CA  
1542 C C   . GLY A 219 ? 0.9266 1.2923 1.8038 0.0604  -0.4405 -0.2932 827 GLY A C   
1543 O O   . GLY A 219 ? 0.9112 1.3171 1.8301 0.0715  -0.4818 -0.3255 827 GLY A O   
1544 N N   . ASN A 220 ? 0.9547 1.2799 1.7557 0.0393  -0.4063 -0.2696 828 ASN A N   
1545 C CA  . ASN A 220 ? 0.9708 1.2913 1.7303 0.0264  -0.4102 -0.2782 828 ASN A CA  
1546 C C   . ASN A 220 ? 1.0080 1.2741 1.6540 0.0230  -0.3916 -0.2359 828 ASN A C   
1547 O O   . ASN A 220 ? 1.0398 1.2933 1.6219 0.0290  -0.4131 -0.2300 828 ASN A O   
1548 C CB  . ASN A 220 ? 0.9721 1.3141 1.8011 -0.0074 -0.3726 -0.3139 828 ASN A CB  
1549 C CG  . ASN A 220 ? 1.0303 1.3607 1.8946 -0.0279 -0.3162 -0.3092 828 ASN A CG  
1550 O OD1 . ASN A 220 ? 1.0058 1.3695 1.9621 -0.0318 -0.3064 -0.3352 828 ASN A OD1 
1551 N ND2 . ASN A 220 ? 1.0933 1.3770 1.8842 -0.0395 -0.2785 -0.2772 828 ASN A ND2 
1552 N N   . ALA A 221 ? 0.9948 1.2311 1.6184 0.0140  -0.3521 -0.2094 829 ALA A N   
1553 C CA  . ALA A 221 ? 1.0139 1.2049 1.5427 0.0107  -0.3334 -0.1732 829 ALA A CA  
1554 C C   . ALA A 221 ? 0.9877 1.1543 1.4996 0.0165  -0.3149 -0.1444 829 ALA A C   
1555 O O   . ALA A 221 ? 0.9680 1.1496 1.5421 0.0162  -0.3039 -0.1544 829 ALA A O   
1556 C CB  . ALA A 221 ? 1.0240 1.2027 1.5382 -0.0161 -0.2942 -0.1794 829 ALA A CB  
1557 N N   . ARG A 222 ? 0.9830 1.1133 1.4151 0.0208  -0.3099 -0.1115 830 ARG A N   
1558 C CA  . ARG A 222 ? 0.9529 1.0593 1.3700 0.0233  -0.2904 -0.0872 830 ARG A CA  
1559 C C   . ARG A 222 ? 0.9000 0.9944 1.3043 0.0013  -0.2458 -0.0848 830 ARG A C   
1560 O O   . ARG A 222 ? 0.9135 0.9924 1.2647 -0.0070 -0.2347 -0.0760 830 ARG A O   
1561 C CB  . ARG A 222 ? 1.0105 1.0844 1.3566 0.0397  -0.3077 -0.0555 830 ARG A CB  
1562 C CG  . ARG A 222 ? 1.0604 1.1395 1.4123 0.0668  -0.3526 -0.0555 830 ARG A CG  
1563 C CD  . ARG A 222 ? 1.1621 1.2009 1.4313 0.0834  -0.3672 -0.0228 830 ARG A CD  
1564 N NE  . ARG A 222 ? 1.2204 1.2591 1.4883 0.1143  -0.4122 -0.0213 830 ARG A NE  
1565 C CZ  . ARG A 222 ? 1.2642 1.2805 1.5348 0.1348  -0.4228 -0.0036 830 ARG A CZ  
1566 N NH1 . ARG A 222 ? 1.2643 1.2575 1.5413 0.1250  -0.3906 0.0126  830 ARG A NH1 
1567 N NH2 . ARG A 222 ? 1.2616 1.2768 1.5271 0.1671  -0.4671 -0.0029 830 ARG A NH2 
1568 N N   . LEU A 223 ? 0.8390 0.9412 1.2919 -0.0061 -0.2212 -0.0947 831 LEU A N   
1569 C CA  . LEU A 223 ? 0.8153 0.9053 1.2555 -0.0229 -0.1805 -0.0946 831 LEU A CA  
1570 C C   . LEU A 223 ? 0.7932 0.8654 1.2174 -0.0211 -0.1619 -0.0791 831 LEU A C   
1571 O O   . LEU A 223 ? 0.7789 0.8551 1.2366 -0.0118 -0.1692 -0.0790 831 LEU A O   
1572 C CB  . LEU A 223 ? 0.7863 0.8961 1.2903 -0.0353 -0.1595 -0.1221 831 LEU A CB  
1573 C CG  . LEU A 223 ? 0.7771 0.9089 1.3156 -0.0419 -0.1717 -0.1460 831 LEU A CG  
1574 C CD1 . LEU A 223 ? 0.7535 0.9026 1.3628 -0.0567 -0.1430 -0.1733 831 LEU A CD1 
1575 C CD2 . LEU A 223 ? 0.8032 0.9171 1.2828 -0.0499 -0.1679 -0.1397 831 LEU A CD2 
1576 N N   . PRO A 224 ? 0.7840 0.8385 1.1640 -0.0299 -0.1362 -0.0706 832 PRO A N   
1577 C CA  . PRO A 224 ? 0.7667 0.8090 1.1362 -0.0290 -0.1190 -0.0624 832 PRO A CA  
1578 C C   . PRO A 224 ? 0.7332 0.7808 1.1395 -0.0349 -0.0919 -0.0793 832 PRO A C   
1579 O O   . PRO A 224 ? 0.7384 0.7738 1.1164 -0.0404 -0.0662 -0.0798 832 PRO A O   
1580 C CB  . PRO A 224 ? 0.7997 0.8261 1.1075 -0.0328 -0.1084 -0.0498 832 PRO A CB  
1581 C CG  . PRO A 224 ? 0.8172 0.8446 1.1089 -0.0389 -0.1069 -0.0556 832 PRO A CG  
1582 C CD  . PRO A 224 ? 0.7845 0.8299 1.1237 -0.0390 -0.1235 -0.0703 832 PRO A CD  
1583 N N   . VAL A 225 ? 0.6995 0.7649 1.1678 -0.0316 -0.0981 -0.0936 833 VAL A N   
1584 C CA  . VAL A 225 ? 0.6744 0.7488 1.1906 -0.0371 -0.0722 -0.1131 833 VAL A CA  
1585 C C   . VAL A 225 ? 0.6677 0.7254 1.1600 -0.0379 -0.0453 -0.1108 833 VAL A C   
1586 O O   . VAL A 225 ? 0.6792 0.7300 1.1677 -0.0457 -0.0135 -0.1208 833 VAL A O   
1587 C CB  . VAL A 225 ? 0.6554 0.7545 1.2447 -0.0281 -0.0913 -0.1270 833 VAL A CB  
1588 C CG1 . VAL A 225 ? 0.6389 0.7495 1.2833 -0.0341 -0.0610 -0.1493 833 VAL A CG1 
1589 C CG2 . VAL A 225 ? 0.6499 0.7704 1.2651 -0.0257 -0.1201 -0.1353 833 VAL A CG2 
1590 N N   . LYS A 226 ? 0.6456 0.6942 1.1188 -0.0300 -0.0567 -0.0987 834 LYS A N   
1591 C CA  . LYS A 226 ? 0.6385 0.6746 1.0916 -0.0297 -0.0359 -0.1009 834 LYS A CA  
1592 C C   . LYS A 226 ? 0.6419 0.6628 1.0321 -0.0340 -0.0180 -0.0960 834 LYS A C   
1593 O O   . LYS A 226 ? 0.6537 0.6658 1.0249 -0.0325 0.0015  -0.1027 834 LYS A O   
1594 C CB  . LYS A 226 ? 0.6582 0.6879 1.1137 -0.0221 -0.0521 -0.0923 834 LYS A CB  
1595 C CG  . LYS A 226 ? 0.6727 0.7115 1.1907 -0.0140 -0.0625 -0.1004 834 LYS A CG  
1596 C CD  . LYS A 226 ? 0.7153 0.7395 1.2370 -0.0066 -0.0731 -0.0926 834 LYS A CD  
1597 C CE  . LYS A 226 ? 0.7301 0.7604 1.3140 0.0029  -0.0745 -0.1058 834 LYS A CE  
1598 N NZ  . LYS A 226 ? 0.7622 0.7729 1.3489 0.0070  -0.0724 -0.1045 834 LYS A NZ  
1599 N N   . TRP A 227 ? 0.6283 0.6458 0.9854 -0.0368 -0.0256 -0.0859 835 TRP A N   
1600 C CA  . TRP A 227 ? 0.6354 0.6377 0.9347 -0.0376 -0.0113 -0.0810 835 TRP A CA  
1601 C C   . TRP A 227 ? 0.6553 0.6483 0.9515 -0.0444 0.0104  -0.0875 835 TRP A C   
1602 O O   . TRP A 227 ? 0.6680 0.6418 0.9144 -0.0428 0.0253  -0.0830 835 TRP A O   
1603 C CB  . TRP A 227 ? 0.6238 0.6255 0.8877 -0.0358 -0.0312 -0.0663 835 TRP A CB  
1604 C CG  . TRP A 227 ? 0.6051 0.6090 0.8598 -0.0316 -0.0429 -0.0598 835 TRP A CG  
1605 C CD1 . TRP A 227 ? 0.6165 0.6175 0.8358 -0.0280 -0.0383 -0.0595 835 TRP A CD1 
1606 C CD2 . TRP A 227 ? 0.5827 0.5908 0.8670 -0.0305 -0.0600 -0.0544 835 TRP A CD2 
1607 N NE1 . TRP A 227 ? 0.6073 0.6128 0.8390 -0.0283 -0.0489 -0.0568 835 TRP A NE1 
1608 C CE2 . TRP A 227 ? 0.5903 0.5957 0.8583 -0.0298 -0.0604 -0.0517 835 TRP A CE2 
1609 C CE3 . TRP A 227 ? 0.5702 0.5828 0.8935 -0.0284 -0.0754 -0.0525 835 TRP A CE3 
1610 C CZ2 . TRP A 227 ? 0.5855 0.5862 0.8721 -0.0297 -0.0711 -0.0446 835 TRP A CZ2 
1611 C CZ3 . TRP A 227 ? 0.5791 0.5857 0.9168 -0.0241 -0.0883 -0.0444 835 TRP A CZ3 
1612 C CH2 . TRP A 227 ? 0.5829 0.5805 0.9005 -0.0261 -0.0841 -0.0393 835 TRP A CH2 
1613 N N   . MET A 228 ? 0.6527 0.6586 1.0044 -0.0515 0.0122  -0.0991 836 MET A N   
1614 C CA  . MET A 228 ? 0.6782 0.6771 1.0411 -0.0620 0.0343  -0.1087 836 MET A CA  
1615 C C   . MET A 228 ? 0.7055 0.6904 1.0762 -0.0666 0.0737  -0.1201 836 MET A C   
1616 O O   . MET A 228 ? 0.6822 0.6799 1.0932 -0.0652 0.0789  -0.1306 836 MET A O   
1617 C CB  . MET A 228 ? 0.6600 0.6849 1.0842 -0.0681 0.0144  -0.1201 836 MET A CB  
1618 C CG  . MET A 228 ? 0.6984 0.7276 1.0986 -0.0651 -0.0172 -0.1095 836 MET A CG  
1619 S SD  . MET A 228 ? 0.7724 0.8360 1.2371 -0.0630 -0.0547 -0.1219 836 MET A SD  
1620 C CE  . MET A 228 ? 0.7387 0.8119 1.2585 -0.0807 -0.0304 -0.1498 836 MET A CE  
1621 N N   . ALA A 229 ? 0.7538 0.7088 1.0847 -0.0717 0.1040  -0.1182 837 ALA A N   
1622 C CA  . ALA A 229 ? 0.7945 0.7255 1.1207 -0.0771 0.1492  -0.1266 837 ALA A CA  
1623 C C   . ALA A 229 ? 0.7910 0.7443 1.2034 -0.0926 0.1637  -0.1486 837 ALA A C   
1624 O O   . ALA A 229 ? 0.7730 0.7513 1.2347 -0.1001 0.1422  -0.1568 837 ALA A O   
1625 C CB  . ALA A 229 ? 0.8343 0.7215 1.0943 -0.0777 0.1762  -0.1162 837 ALA A CB  
1626 N N   . PRO A 230 ? 0.8103 0.7573 1.2441 -0.0969 0.1997  -0.1612 838 PRO A N   
1627 C CA  . PRO A 230 ? 0.7945 0.7692 1.3220 -0.1117 0.2148  -0.1864 838 PRO A CA  
1628 C C   . PRO A 230 ? 0.8172 0.7934 1.3808 -0.1298 0.2253  -0.1974 838 PRO A C   
1629 O O   . PRO A 230 ? 0.7871 0.8050 1.4319 -0.1363 0.2031  -0.2164 838 PRO A O   
1630 C CB  . PRO A 230 ? 0.8070 0.7598 1.3261 -0.1140 0.2640  -0.1944 838 PRO A CB  
1631 C CG  . PRO A 230 ? 0.8331 0.7684 1.2779 -0.0947 0.2524  -0.1779 838 PRO A CG  
1632 C CD  . PRO A 230 ? 0.8348 0.7524 1.2116 -0.0872 0.2274  -0.1560 838 PRO A CD  
1633 N N   . GLU A 231 ? 0.8707 0.8014 1.3724 -0.1357 0.2541  -0.1858 839 GLU A N   
1634 C CA  . GLU A 231 ? 0.8849 0.8090 1.4163 -0.1548 0.2688  -0.1970 839 GLU A CA  
1635 C C   . GLU A 231 ? 0.9013 0.8531 1.4473 -0.1527 0.2181  -0.1969 839 GLU A C   
1636 O O   . GLU A 231 ? 0.8929 0.8510 1.4805 -0.1689 0.2219  -0.2133 839 GLU A O   
1637 C CB  . GLU A 231 ? 0.9539 0.8119 1.4066 -0.1587 0.3158  -0.1818 839 GLU A CB  
1638 C CG  . GLU A 231 ? 1.0525 0.8800 1.4076 -0.1398 0.2936  -0.1536 839 GLU A CG  
1639 C CD  . GLU A 231 ? 1.1486 0.9563 1.4266 -0.1171 0.2920  -0.1345 839 GLU A CD  
1640 O OE1 . GLU A 231 ? 1.1384 0.9619 1.4389 -0.1141 0.2995  -0.1424 839 GLU A OE1 
1641 O OE2 . GLU A 231 ? 1.1934 0.9718 1.3911 -0.1013 0.2820  -0.1141 839 GLU A OE2 
1642 N N   . SER A 232 ? 0.9181 0.8843 1.4285 -0.1338 0.1730  -0.1799 840 SER A N   
1643 C CA  . SER A 232 ? 0.9212 0.9128 1.4407 -0.1301 0.1258  -0.1792 840 SER A CA  
1644 C C   . SER A 232 ? 0.8929 0.9379 1.4982 -0.1281 0.0923  -0.1986 840 SER A C   
1645 O O   . SER A 232 ? 0.8720 0.9439 1.5199 -0.1324 0.0658  -0.2138 840 SER A O   
1646 C CB  . SER A 232 ? 0.9631 0.9424 1.4055 -0.1119 0.0981  -0.1522 840 SER A CB  
1647 O OG  . SER A 232 ? 1.0253 0.9604 1.3926 -0.1100 0.1210  -0.1367 840 SER A OG  
1648 N N   . ILE A 233 ? 0.8926 0.9518 1.5224 -0.1196 0.0928  -0.1998 841 ILE A N   
1649 C CA  . ILE A 233 ? 0.8739 0.9795 1.5835 -0.1132 0.0620  -0.2172 841 ILE A CA  
1650 C C   . ILE A 233 ? 0.8603 0.9945 1.6652 -0.1302 0.0816  -0.2523 841 ILE A C   
1651 O O   . ILE A 233 ? 0.8274 1.0020 1.6963 -0.1286 0.0477  -0.2721 841 ILE A O   
1652 C CB  . ILE A 233 ? 0.8755 0.9812 1.5810 -0.0995 0.0627  -0.2090 841 ILE A CB  
1653 C CG1 . ILE A 233 ? 0.9081 0.9970 1.5402 -0.0837 0.0345  -0.1803 841 ILE A CG1 
1654 C CG2 . ILE A 233 ? 0.8348 0.9835 1.6327 -0.0930 0.0444  -0.2310 841 ILE A CG2 
1655 C CD1 . ILE A 233 ? 0.9306 1.0071 1.5412 -0.0753 0.0464  -0.1727 841 ILE A CD1 
1656 N N   . PHE A 234 ? 0.8815 0.9942 1.6945 -0.1457 0.1367  -0.2610 842 PHE A N   
1657 C CA  . PHE A 234 ? 0.8645 1.0031 1.7732 -0.1649 0.1646  -0.2962 842 PHE A CA  
1658 C C   . PHE A 234 ? 0.8744 1.0062 1.7999 -0.1862 0.1783  -0.3111 842 PHE A C   
1659 O O   . PHE A 234 ? 0.8345 1.0058 1.8579 -0.2002 0.1799  -0.3465 842 PHE A O   
1660 C CB  . PHE A 234 ? 0.8771 0.9941 1.7912 -0.1734 0.2236  -0.3010 842 PHE A CB  
1661 C CG  . PHE A 234 ? 0.9003 1.0224 1.8005 -0.1538 0.2136  -0.2907 842 PHE A CG  
1662 C CD1 . PHE A 234 ? 0.8792 1.0473 1.8376 -0.1374 0.1667  -0.2997 842 PHE A CD1 
1663 C CD2 . PHE A 234 ? 0.9524 1.0316 1.7829 -0.1507 0.2521  -0.2744 842 PHE A CD2 
1664 C CE1 . PHE A 234 ? 0.8924 1.0608 1.8407 -0.1203 0.1601  -0.2916 842 PHE A CE1 
1665 C CE2 . PHE A 234 ? 0.9632 1.0477 1.7844 -0.1338 0.2428  -0.2691 842 PHE A CE2 
1666 C CZ  . PHE A 234 ? 0.9274 1.0556 1.8097 -0.1200 0.1983  -0.2779 842 PHE A CZ  
1667 N N   . ASN A 235 ? 0.9226 1.0062 1.7600 -0.1887 0.1891  -0.2876 843 ASN A N   
1668 C CA  . ASN A 235 ? 0.9319 1.0012 1.7837 -0.2101 0.2078  -0.3025 843 ASN A CA  
1669 C C   . ASN A 235 ? 0.9508 1.0088 1.7451 -0.2032 0.1708  -0.2885 843 ASN A C   
1670 O O   . ASN A 235 ? 0.9540 0.9937 1.7533 -0.2206 0.1883  -0.3002 843 ASN A O   
1671 C CB  . ASN A 235 ? 0.9902 0.9997 1.8025 -0.2266 0.2780  -0.2951 843 ASN A CB  
1672 C CG  . ASN A 235 ? 1.0364 1.0523 1.9056 -0.2375 0.3243  -0.3123 843 ASN A CG  
1673 O OD1 . ASN A 235 ? 1.0268 1.0706 1.9952 -0.2598 0.3479  -0.3479 843 ASN A OD1 
1674 N ND2 . ASN A 235 ? 1.0733 1.0651 1.8840 -0.2225 0.3398  -0.2905 843 ASN A ND2 
1675 N N   . CYS A 236 ? 0.9594 1.0254 1.7005 -0.1795 0.1241  -0.2648 844 CYS A N   
1676 C CA  . CYS A 236 ? 0.9875 1.0417 1.6667 -0.1710 0.0911  -0.2494 844 CYS A CA  
1677 C C   . CYS A 236 ? 1.0135 1.0077 1.6116 -0.1759 0.1266  -0.2296 844 CYS A C   
1678 O O   . CYS A 236 ? 1.0234 1.0046 1.5919 -0.1779 0.1147  -0.2284 844 CYS A O   
1679 C CB  . CYS A 236 ? 0.9859 1.0793 1.7239 -0.1773 0.0553  -0.2779 844 CYS A CB  
1680 S SG  . CYS A 236 ? 1.0373 1.2005 1.8653 -0.1640 0.0054  -0.3010 844 CYS A SG  
1681 N N   . VAL A 237 ? 1.0235 0.9798 1.5821 -0.1751 0.1689  -0.2143 845 VAL A N   
1682 C CA  . VAL A 237 ? 1.0608 0.9555 1.5371 -0.1744 0.2036  -0.1936 845 VAL A CA  
1683 C C   . VAL A 237 ? 1.0730 0.9525 1.4613 -0.1493 0.1809  -0.1622 845 VAL A C   
1684 O O   . VAL A 237 ? 1.0776 0.9616 1.4485 -0.1370 0.1801  -0.1515 845 VAL A O   
1685 C CB  . VAL A 237 ? 1.0848 0.9416 1.5641 -0.1869 0.2660  -0.1968 845 VAL A CB  
1686 C CG1 . VAL A 237 ? 1.1502 0.9361 1.5279 -0.1781 0.2999  -0.1698 845 VAL A CG1 
1687 C CG2 . VAL A 237 ? 1.0577 0.9261 1.6272 -0.2157 0.2942  -0.2304 845 VAL A CG2 
1688 N N   . TYR A 238 ? 1.0720 0.9367 1.4107 -0.1423 0.1623  -0.1508 846 TYR A N   
1689 C CA  . TYR A 238 ? 1.0812 0.9334 1.3429 -0.1202 0.1435  -0.1249 846 TYR A CA  
1690 C C   . TYR A 238 ? 1.1019 0.8953 1.2929 -0.1155 0.1758  -0.1108 846 TYR A C   
1691 O O   . TYR A 238 ? 1.1113 0.8840 1.2963 -0.1232 0.1822  -0.1157 846 TYR A O   
1692 C CB  . TYR A 238 ? 1.0722 0.9550 1.3316 -0.1133 0.0964  -0.1230 846 TYR A CB  
1693 C CG  . TYR A 238 ? 1.0481 0.9814 1.3641 -0.1125 0.0609  -0.1325 846 TYR A CG  
1694 C CD1 . TYR A 238 ? 1.0576 1.0063 1.3615 -0.0986 0.0434  -0.1192 846 TYR A CD1 
1695 C CD2 . TYR A 238 ? 1.0311 0.9950 1.4081 -0.1231 0.0409  -0.1549 846 TYR A CD2 
1696 C CE1 . TYR A 238 ? 1.0446 1.0316 1.3931 -0.0949 0.0105  -0.1247 846 TYR A CE1 
1697 C CE2 . TYR A 238 ? 1.0156 1.0219 1.4361 -0.1169 0.0041  -0.1615 846 TYR A CE2 
1698 C CZ  . TYR A 238 ? 1.0345 1.0490 1.4386 -0.1023 -0.0097 -0.1446 846 TYR A CZ  
1699 O OH  . TYR A 238 ? 1.0404 1.0889 1.4832 -0.0939 -0.0446 -0.1488 846 TYR A OH  
1700 N N   . THR A 239 ? 1.1061 0.8698 1.2430 -0.1016 0.1970  -0.0948 847 THR A N   
1701 C CA  . THR A 239 ? 1.1311 0.8333 1.1900 -0.0902 0.2271  -0.0784 847 THR A CA  
1702 C C   . THR A 239 ? 1.1137 0.8140 1.1029 -0.0618 0.2049  -0.0590 847 THR A C   
1703 O O   . THR A 239 ? 1.0835 0.8277 1.0908 -0.0556 0.1730  -0.0597 847 THR A O   
1704 C CB  . THR A 239 ? 1.1729 0.8339 1.2278 -0.0991 0.2803  -0.0801 847 THR A CB  
1705 O OG1 . THR A 239 ? 1.1778 0.8647 1.2494 -0.0950 0.2788  -0.0826 847 THR A OG1 
1706 C CG2 . THR A 239 ? 1.1558 0.8123 1.2791 -0.1287 0.3090  -0.1014 847 THR A CG2 
1707 N N   . PHE A 240 ? 1.1281 0.7770 1.0391 -0.0433 0.2218  -0.0429 848 PHE A N   
1708 C CA  . PHE A 240 ? 1.1280 0.7794 0.9783 -0.0144 0.1998  -0.0293 848 PHE A CA  
1709 C C   . PHE A 240 ? 1.1104 0.7784 0.9603 -0.0080 0.2008  -0.0309 848 PHE A C   
1710 O O   . PHE A 240 ? 1.0997 0.8006 0.9422 0.0058  0.1705  -0.0301 848 PHE A O   
1711 C CB  . PHE A 240 ? 1.1678 0.7577 0.9351 0.0076  0.2191  -0.0135 848 PHE A CB  
1712 C CG  . PHE A 240 ? 1.1775 0.7495 0.9459 0.0022  0.2184  -0.0136 848 PHE A CG  
1713 C CD1 . PHE A 240 ? 1.1689 0.7738 0.9394 0.0110  0.1816  -0.0142 848 PHE A CD1 
1714 C CD2 . PHE A 240 ? 1.2072 0.7285 0.9769 -0.0131 0.2573  -0.0150 848 PHE A CD2 
1715 C CE1 . PHE A 240 ? 1.1828 0.7717 0.9541 0.0062  0.1815  -0.0168 848 PHE A CE1 
1716 C CE2 . PHE A 240 ? 1.2186 0.7229 0.9920 -0.0188 0.2565  -0.0184 848 PHE A CE2 
1717 C CZ  . PHE A 240 ? 1.2022 0.7416 0.9757 -0.0085 0.2174  -0.0196 848 PHE A CZ  
1718 N N   . GLU A 241 ? 1.0990 0.7459 0.9647 -0.0209 0.2377  -0.0363 849 GLU A N   
1719 C CA  . GLU A 241 ? 1.0817 0.7383 0.9508 -0.0181 0.2472  -0.0410 849 GLU A CA  
1720 C C   . GLU A 241 ? 1.0090 0.7298 0.9541 -0.0292 0.2157  -0.0547 849 GLU A C   
1721 O O   . GLU A 241 ? 1.0014 0.7426 0.9404 -0.0183 0.2019  -0.0568 849 GLU A O   
1722 C CB  . GLU A 241 ? 1.1301 0.7454 1.0034 -0.0327 0.3009  -0.0448 849 GLU A CB  
1723 C CG  . GLU A 241 ? 1.2625 0.8034 1.0379 -0.0139 0.3363  -0.0271 849 GLU A CG  
1724 C CD  . GLU A 241 ? 1.4124 0.9019 1.1754 -0.0246 0.3672  -0.0207 849 GLU A CD  
1725 O OE1 . GLU A 241 ? 1.4124 0.9296 1.2342 -0.0421 0.3497  -0.0300 849 GLU A OE1 
1726 O OE2 . GLU A 241 ? 1.4969 0.9151 1.1881 -0.0149 0.4096  -0.0066 849 GLU A OE2 
1727 N N   . SER A 242 ? 0.9519 0.7027 0.9672 -0.0493 0.2035  -0.0650 850 SER A N   
1728 C CA  . SER A 242 ? 0.8898 0.6960 0.9726 -0.0564 0.1718  -0.0757 850 SER A CA  
1729 C C   . SER A 242 ? 0.8636 0.6943 0.9225 -0.0409 0.1319  -0.0668 850 SER A C   
1730 O O   . SER A 242 ? 0.8379 0.6974 0.9199 -0.0376 0.1143  -0.0704 850 SER A O   
1731 C CB  . SER A 242 ? 0.8688 0.6999 1.0248 -0.0770 0.1644  -0.0897 850 SER A CB  
1732 O OG  . SER A 242 ? 0.9070 0.7400 1.0497 -0.0766 0.1422  -0.0850 850 SER A OG  
1733 N N   . ASP A 243 ? 0.8689 0.6852 0.8810 -0.0311 0.1214  -0.0562 851 ASP A N   
1734 C CA  . ASP A 243 ? 0.8648 0.7018 0.8523 -0.0168 0.0898  -0.0492 851 ASP A CA  
1735 C C   . ASP A 243 ? 0.8703 0.7059 0.8234 0.0001  0.0903  -0.0486 851 ASP A C   
1736 O O   . ASP A 243 ? 0.8480 0.7146 0.8153 0.0042  0.0664  -0.0511 851 ASP A O   
1737 C CB  . ASP A 243 ? 0.8973 0.7119 0.8375 -0.0070 0.0878  -0.0404 851 ASP A CB  
1738 C CG  . ASP A 243 ? 0.9355 0.7733 0.8996 -0.0150 0.0637  -0.0410 851 ASP A CG  
1739 O OD1 . ASP A 243 ? 0.9203 0.7860 0.9376 -0.0296 0.0505  -0.0479 851 ASP A OD1 
1740 O OD2 . ASP A 243 ? 0.9756 0.8025 0.9033 -0.0048 0.0580  -0.0353 851 ASP A OD2 
1741 N N   . VAL A 244 ? 0.8983 0.6950 0.8038 0.0101  0.1188  -0.0460 852 VAL A N   
1742 C CA  . VAL A 244 ? 0.9103 0.7012 0.7744 0.0286  0.1204  -0.0480 852 VAL A CA  
1743 C C   . VAL A 244 ? 0.8873 0.7079 0.8019 0.0189  0.1170  -0.0604 852 VAL A C   
1744 O O   . VAL A 244 ? 0.8935 0.7355 0.8025 0.0294  0.0977  -0.0665 852 VAL A O   
1745 C CB  . VAL A 244 ? 0.9515 0.6855 0.7445 0.0426  0.1548  -0.0404 852 VAL A CB  
1746 C CG1 . VAL A 244 ? 0.9687 0.6958 0.7194 0.0607  0.1590  -0.0459 852 VAL A CG1 
1747 C CG2 . VAL A 244 ? 0.9800 0.6847 0.7154 0.0599  0.1508  -0.0276 852 VAL A CG2 
1748 N N   . TRP A 245 ? 0.8623 0.6887 0.8346 -0.0013 0.1325  -0.0668 853 TRP A N   
1749 C CA  . TRP A 245 ? 0.8423 0.6982 0.8720 -0.0097 0.1277  -0.0794 853 TRP A CA  
1750 C C   . TRP A 245 ? 0.8069 0.7018 0.8685 -0.0094 0.0889  -0.0797 853 TRP A C   
1751 O O   . TRP A 245 ? 0.7986 0.7090 0.8705 -0.0046 0.0794  -0.0874 853 TRP A O   
1752 C CB  . TRP A 245 ? 0.8282 0.6903 0.9241 -0.0300 0.1456  -0.0880 853 TRP A CB  
1753 C CG  . TRP A 245 ? 0.8151 0.7102 0.9776 -0.0362 0.1358  -0.1008 853 TRP A CG  
1754 C CD1 . TRP A 245 ? 0.8019 0.7308 1.0081 -0.0376 0.1014  -0.1014 853 TRP A CD1 
1755 C CD2 . TRP A 245 ? 0.8182 0.7113 1.0095 -0.0406 0.1632  -0.1148 853 TRP A CD2 
1756 N NE1 . TRP A 245 ? 0.7856 0.7320 1.0438 -0.0401 0.1033  -0.1141 853 TRP A NE1 
1757 C CE2 . TRP A 245 ? 0.7918 0.7200 1.0460 -0.0425 0.1407  -0.1240 853 TRP A CE2 
1758 C CE3 . TRP A 245 ? 0.8468 0.7088 1.0156 -0.0428 0.2075  -0.1200 853 TRP A CE3 
1759 C CZ2 . TRP A 245 ? 0.7862 0.7234 1.0864 -0.0459 0.1588  -0.1402 853 TRP A CZ2 
1760 C CZ3 . TRP A 245 ? 0.8379 0.7095 1.0502 -0.0477 0.2277  -0.1363 853 TRP A CZ3 
1761 C CH2 . TRP A 245 ? 0.8054 0.7165 1.0854 -0.0489 0.2024  -0.1473 853 TRP A CH2 
1762 N N   . SER A 246 ? 0.7872 0.6940 0.8629 -0.0152 0.0693  -0.0721 854 SER A N   
1763 C CA  . SER A 246 ? 0.7649 0.7008 0.8641 -0.0163 0.0376  -0.0691 854 SER A CA  
1764 C C   . SER A 246 ? 0.7788 0.7210 0.8427 -0.0031 0.0249  -0.0689 854 SER A C   
1765 O O   . SER A 246 ? 0.7645 0.7282 0.8549 -0.0048 0.0082  -0.0722 854 SER A O   
1766 C CB  . SER A 246 ? 0.7658 0.7051 0.8696 -0.0228 0.0249  -0.0612 854 SER A CB  
1767 O OG  . SER A 246 ? 0.7773 0.7208 0.9279 -0.0355 0.0297  -0.0669 854 SER A OG  
1768 N N   . TYR A 247 ? 0.7983 0.7208 0.8041 0.0112  0.0331  -0.0664 855 TYR A N   
1769 C CA  . TYR A 247 ? 0.8053 0.7371 0.7778 0.0274  0.0200  -0.0712 855 TYR A CA  
1770 C C   . TYR A 247 ? 0.8092 0.7488 0.7901 0.0312  0.0218  -0.0855 855 TYR A C   
1771 O O   . TYR A 247 ? 0.8101 0.7729 0.7996 0.0355  0.0043  -0.0951 855 TYR A O   
1772 C CB  . TYR A 247 ? 0.8267 0.7308 0.7319 0.0468  0.0284  -0.0661 855 TYR A CB  
1773 C CG  . TYR A 247 ? 0.8349 0.7529 0.7075 0.0677  0.0112  -0.0753 855 TYR A CG  
1774 C CD1 . TYR A 247 ? 0.8258 0.7740 0.7133 0.0695  -0.0117 -0.0780 855 TYR A CD1 
1775 C CD2 . TYR A 247 ? 0.8661 0.7689 0.6945 0.0861  0.0179  -0.0839 855 TYR A CD2 
1776 C CE1 . TYR A 247 ? 0.8383 0.8062 0.7064 0.0884  -0.0287 -0.0916 855 TYR A CE1 
1777 C CE2 . TYR A 247 ? 0.8756 0.7969 0.6783 0.1072  -0.0029 -0.0972 855 TYR A CE2 
1778 C CZ  . TYR A 247 ? 0.8678 0.8241 0.6949 0.1079  -0.0268 -0.1023 855 TYR A CZ  
1779 O OH  . TYR A 247 ? 0.8825 0.8630 0.6934 0.1287  -0.0483 -0.1198 855 TYR A OH  
1780 N N   . GLY A 248 ? 0.8073 0.7277 0.7881 0.0288  0.0451  -0.0891 856 GLY A N   
1781 C CA  . GLY A 248 ? 0.8015 0.7261 0.7905 0.0318  0.0508  -0.1043 856 GLY A CA  
1782 C C   . GLY A 248 ? 0.7737 0.7274 0.8290 0.0187  0.0349  -0.1110 856 GLY A C   
1783 O O   . GLY A 248 ? 0.7823 0.7505 0.8450 0.0228  0.0243  -0.1247 856 GLY A O   
1784 N N   . ILE A 249 ? 0.7432 0.7039 0.8456 0.0040  0.0314  -0.1020 857 ILE A N   
1785 C CA  . ILE A 249 ? 0.7071 0.6880 0.8668 -0.0057 0.0151  -0.1034 857 ILE A CA  
1786 C C   . ILE A 249 ? 0.6845 0.6808 0.8396 -0.0047 -0.0065 -0.1008 857 ILE A C   
1787 O O   . ILE A 249 ? 0.6687 0.6757 0.8531 -0.0080 -0.0150 -0.1082 857 ILE A O   
1788 C CB  . ILE A 249 ? 0.6967 0.6803 0.8992 -0.0166 0.0128  -0.0945 857 ILE A CB  
1789 C CG1 . ILE A 249 ? 0.7152 0.6873 0.9293 -0.0199 0.0380  -0.1010 857 ILE A CG1 
1790 C CG2 . ILE A 249 ? 0.6693 0.6662 0.9236 -0.0214 -0.0037 -0.0943 857 ILE A CG2 
1791 C CD1 . ILE A 249 ? 0.7300 0.7024 0.9681 -0.0179 0.0531  -0.1175 857 ILE A CD1 
1792 N N   . PHE A 250 ? 0.6863 0.6822 0.8057 -0.0001 -0.0122 -0.0924 858 PHE A N   
1793 C CA  . PHE A 250 ? 0.6687 0.6814 0.7838 0.0008  -0.0283 -0.0922 858 PHE A CA  
1794 C C   . PHE A 250 ? 0.6666 0.6914 0.7744 0.0094  -0.0319 -0.1118 858 PHE A C   
1795 O O   . PHE A 250 ? 0.6438 0.6855 0.7811 0.0030  -0.0415 -0.1197 858 PHE A O   
1796 C CB  . PHE A 250 ? 0.6605 0.6698 0.7380 0.0068  -0.0310 -0.0819 858 PHE A CB  
1797 C CG  . PHE A 250 ? 0.6506 0.6802 0.7183 0.0130  -0.0433 -0.0889 858 PHE A CG  
1798 C CD1 . PHE A 250 ? 0.6393 0.6858 0.7396 0.0014  -0.0520 -0.0874 858 PHE A CD1 
1799 C CD2 . PHE A 250 ? 0.6658 0.6975 0.6941 0.0314  -0.0454 -0.0991 858 PHE A CD2 
1800 C CE1 . PHE A 250 ? 0.6373 0.7066 0.7400 0.0044  -0.0597 -0.0984 858 PHE A CE1 
1801 C CE2 . PHE A 250 ? 0.6658 0.7237 0.6963 0.0379  -0.0587 -0.1110 858 PHE A CE2 
1802 C CZ  . PHE A 250 ? 0.6472 0.7259 0.7192 0.0227  -0.0644 -0.1118 858 PHE A CZ  
1803 N N   . LEU A 251 ? 0.6932 0.7072 0.7604 0.0242  -0.0235 -0.1212 859 LEU A N   
1804 C CA  . LEU A 251 ? 0.7071 0.7338 0.7620 0.0357  -0.0304 -0.1440 859 LEU A CA  
1805 C C   . LEU A 251 ? 0.6965 0.7313 0.8002 0.0243  -0.0297 -0.1577 859 LEU A C   
1806 O O   . LEU A 251 ? 0.6833 0.7389 0.8105 0.0218  -0.0416 -0.1743 859 LEU A O   
1807 C CB  . LEU A 251 ? 0.7408 0.7461 0.7345 0.0557  -0.0194 -0.1495 859 LEU A CB  
1808 C CG  . LEU A 251 ? 0.7887 0.7810 0.7213 0.0750  -0.0216 -0.1407 859 LEU A CG  
1809 C CD1 . LEU A 251 ? 0.8237 0.7932 0.6911 0.0984  -0.0134 -0.1499 859 LEU A CD1 
1810 C CD2 . LEU A 251 ? 0.7888 0.8127 0.7286 0.0813  -0.0459 -0.1483 859 LEU A CD2 
1811 N N   . TRP A 252 ? 0.6967 0.7159 0.8240 0.0160  -0.0156 -0.1510 860 TRP A N   
1812 C CA  . TRP A 252 ? 0.6885 0.7109 0.8653 0.0067  -0.0141 -0.1620 860 TRP A CA  
1813 C C   . TRP A 252 ? 0.6752 0.7098 0.8956 -0.0063 -0.0277 -0.1571 860 TRP A C   
1814 O O   . TRP A 252 ? 0.6616 0.7049 0.9086 -0.0104 -0.0319 -0.1743 860 TRP A O   
1815 C CB  . TRP A 252 ? 0.6902 0.6974 0.8908 0.0016  0.0017  -0.1543 860 TRP A CB  
1816 C CG  . TRP A 252 ? 0.6861 0.6938 0.9321 -0.0027 0.0054  -0.1690 860 TRP A CG  
1817 C CD1 . TRP A 252 ? 0.7075 0.7097 0.9470 0.0037  0.0193  -0.1894 860 TRP A CD1 
1818 C CD2 . TRP A 252 ? 0.6692 0.6795 0.9693 -0.0124 -0.0043 -0.1654 860 TRP A CD2 
1819 N NE1 . TRP A 252 ? 0.6990 0.7027 0.9908 -0.0021 0.0185  -0.2005 860 TRP A NE1 
1820 C CE2 . TRP A 252 ? 0.6809 0.6874 1.0100 -0.0114 0.0039  -0.1850 860 TRP A CE2 
1821 C CE3 . TRP A 252 ? 0.6667 0.6772 0.9887 -0.0203 -0.0175 -0.1464 860 TRP A CE3 
1822 C CZ2 . TRP A 252 ? 0.6714 0.6728 1.0534 -0.0176 -0.0012 -0.1854 860 TRP A CZ2 
1823 C CZ3 . TRP A 252 ? 0.6728 0.6758 1.0403 -0.0258 -0.0221 -0.1450 860 TRP A CZ3 
1824 C CH2 . TRP A 252 ? 0.6675 0.6651 1.0662 -0.0241 -0.0143 -0.1639 860 TRP A CH2 
1825 N N   . GLU A 253 ? 0.6786 0.7110 0.9026 -0.0128 -0.0326 -0.1348 861 GLU A N   
1826 C CA  . GLU A 253 ? 0.6759 0.7120 0.9291 -0.0243 -0.0413 -0.1251 861 GLU A CA  
1827 C C   . GLU A 253 ? 0.6738 0.7291 0.9268 -0.0258 -0.0473 -0.1406 861 GLU A C   
1828 O O   . GLU A 253 ? 0.6545 0.7116 0.9429 -0.0365 -0.0476 -0.1469 861 GLU A O   
1829 C CB  . GLU A 253 ? 0.7034 0.7350 0.9406 -0.0268 -0.0457 -0.1013 861 GLU A CB  
1830 C CG  . GLU A 253 ? 0.7412 0.7595 0.9889 -0.0279 -0.0451 -0.0860 861 GLU A CG  
1831 C CD  . GLU A 253 ? 0.7842 0.8016 1.0117 -0.0304 -0.0525 -0.0677 861 GLU A CD  
1832 O OE1 . GLU A 253 ? 0.7605 0.7735 0.9990 -0.0366 -0.0591 -0.0562 861 GLU A OE1 
1833 O OE2 . GLU A 253 ? 0.7946 0.8126 0.9911 -0.0258 -0.0499 -0.0653 861 GLU A OE2 
1834 N N   . LEU A 254 ? 0.6877 0.7566 0.9028 -0.0147 -0.0516 -0.1467 862 LEU A N   
1835 C CA  . LEU A 254 ? 0.6895 0.7842 0.9049 -0.0123 -0.0603 -0.1645 862 LEU A CA  
1836 C C   . LEU A 254 ? 0.6976 0.8063 0.9350 -0.0113 -0.0636 -0.1959 862 LEU A C   
1837 O O   . LEU A 254 ? 0.6843 0.8101 0.9603 -0.0227 -0.0663 -0.2109 862 LEU A O   
1838 C CB  . LEU A 254 ? 0.7013 0.8018 0.8656 0.0057  -0.0656 -0.1628 862 LEU A CB  
1839 C CG  . LEU A 254 ? 0.7040 0.8352 0.8618 0.0171  -0.0787 -0.1856 862 LEU A CG  
1840 C CD1 . LEU A 254 ? 0.6847 0.8378 0.8833 0.0017  -0.0804 -0.1874 862 LEU A CD1 
1841 C CD2 . LEU A 254 ? 0.7360 0.8621 0.8368 0.0390  -0.0831 -0.1785 862 LEU A CD2 
1842 N N   . PHE A 255 ? 0.7149 0.8148 0.9299 0.0007  -0.0609 -0.2074 863 PHE A N   
1843 C CA  . PHE A 255 ? 0.7228 0.8352 0.9522 0.0038  -0.0650 -0.2404 863 PHE A CA  
1844 C C   . PHE A 255 ? 0.7216 0.8234 1.0055 -0.0133 -0.0568 -0.2467 863 PHE A C   
1845 O O   . PHE A 255 ? 0.7181 0.8312 1.0245 -0.0148 -0.0600 -0.2769 863 PHE A O   
1846 C CB  . PHE A 255 ? 0.7470 0.8506 0.9217 0.0253  -0.0637 -0.2509 863 PHE A CB  
1847 C CG  . PHE A 255 ? 0.7699 0.8905 0.8977 0.0456  -0.0785 -0.2585 863 PHE A CG  
1848 C CD1 . PHE A 255 ? 0.7647 0.9198 0.9061 0.0518  -0.0975 -0.2907 863 PHE A CD1 
1849 C CD2 . PHE A 255 ? 0.8023 0.9050 0.8772 0.0589  -0.0744 -0.2351 863 PHE A CD2 
1850 C CE1 . PHE A 255 ? 0.7791 0.9526 0.8801 0.0747  -0.1149 -0.2991 863 PHE A CE1 
1851 C CE2 . PHE A 255 ? 0.8234 0.9382 0.8544 0.0810  -0.0892 -0.2409 863 PHE A CE2 
1852 C CZ  . PHE A 255 ? 0.8026 0.9538 0.8459 0.0906  -0.1108 -0.2729 863 PHE A CZ  
1853 N N   . SER A 256 ? 0.7238 0.8032 1.0285 -0.0242 -0.0477 -0.2200 864 SER A N   
1854 C CA  . SER A 256 ? 0.7154 0.7791 1.0703 -0.0378 -0.0409 -0.2209 864 SER A CA  
1855 C C   . SER A 256 ? 0.7330 0.7938 1.1186 -0.0544 -0.0405 -0.2073 864 SER A C   
1856 O O   . SER A 256 ? 0.7372 0.7750 1.1569 -0.0645 -0.0337 -0.1981 864 SER A O   
1857 C CB  . SER A 256 ? 0.7193 0.7587 1.0777 -0.0349 -0.0327 -0.2021 864 SER A CB  
1858 O OG  . SER A 256 ? 0.7417 0.7737 1.0859 -0.0357 -0.0347 -0.1715 864 SER A OG  
1859 N N   . LEU A 257 ? 0.7426 0.8248 1.1149 -0.0559 -0.0461 -0.2070 865 LEU A N   
1860 C CA  . LEU A 257 ? 0.7462 0.8288 1.1408 -0.0716 -0.0414 -0.1968 865 LEU A CA  
1861 C C   . LEU A 257 ? 0.7615 0.8113 1.1529 -0.0776 -0.0350 -0.1598 865 LEU A C   
1862 O O   . LEU A 257 ? 0.7691 0.7994 1.1870 -0.0917 -0.0252 -0.1511 865 LEU A O   
1863 C CB  . LEU A 257 ? 0.7358 0.8264 1.1818 -0.0872 -0.0353 -0.2249 865 LEU A CB  
1864 C CG  . LEU A 257 ? 0.7466 0.8781 1.1994 -0.0808 -0.0466 -0.2670 865 LEU A CG  
1865 C CD1 . LEU A 257 ? 0.7356 0.8762 1.2483 -0.1000 -0.0393 -0.2968 865 LEU A CD1 
1866 C CD2 . LEU A 257 ? 0.7533 0.9172 1.1794 -0.0711 -0.0571 -0.2685 865 LEU A CD2 
1867 N N   . GLY A 258 ? 0.7667 0.8093 1.1235 -0.0664 -0.0402 -0.1390 866 GLY A N   
1868 C CA  . GLY A 258 ? 0.7753 0.7923 1.1231 -0.0680 -0.0400 -0.1067 866 GLY A CA  
1869 C C   . GLY A 258 ? 0.7742 0.7657 1.1390 -0.0639 -0.0408 -0.0964 866 GLY A C   
1870 O O   . GLY A 258 ? 0.7865 0.7549 1.1496 -0.0643 -0.0432 -0.0721 866 GLY A O   
1871 N N   . SER A 259 ? 0.7593 0.7548 1.1390 -0.0578 -0.0395 -0.1152 867 SER A N   
1872 C CA  . SER A 259 ? 0.7537 0.7294 1.1570 -0.0522 -0.0397 -0.1092 867 SER A CA  
1873 C C   . SER A 259 ? 0.7363 0.7137 1.1219 -0.0429 -0.0463 -0.0935 867 SER A C   
1874 O O   . SER A 259 ? 0.7456 0.7390 1.1007 -0.0396 -0.0460 -0.0958 867 SER A O   
1875 C CB  . SER A 259 ? 0.7865 0.7668 1.2124 -0.0494 -0.0330 -0.1375 867 SER A CB  
1876 O OG  . SER A 259 ? 0.8479 0.8147 1.2988 -0.0418 -0.0317 -0.1354 867 SER A OG  
1877 N N   . SER A 260 ? 0.7103 0.6703 1.1155 -0.0380 -0.0528 -0.0781 868 SER A N   
1878 C CA  . SER A 260 ? 0.7019 0.6676 1.1032 -0.0300 -0.0607 -0.0688 868 SER A CA  
1879 C C   . SER A 260 ? 0.6872 0.6658 1.1043 -0.0256 -0.0504 -0.0893 868 SER A C   
1880 O O   . SER A 260 ? 0.6783 0.6532 1.1223 -0.0243 -0.0423 -0.1056 868 SER A O   
1881 C CB  . SER A 260 ? 0.7198 0.6667 1.1426 -0.0222 -0.0743 -0.0514 868 SER A CB  
1882 O OG  . SER A 260 ? 0.7661 0.6986 1.1600 -0.0233 -0.0841 -0.0279 868 SER A OG  
1883 N N   . PRO A 261 ? 0.6834 0.6743 1.0834 -0.0239 -0.0474 -0.0897 869 PRO A N   
1884 C CA  . PRO A 261 ? 0.6801 0.6783 1.0892 -0.0211 -0.0309 -0.1083 869 PRO A CA  
1885 C C   . PRO A 261 ? 0.6699 0.6681 1.1327 -0.0160 -0.0298 -0.1156 869 PRO A C   
1886 O O   . PRO A 261 ? 0.6614 0.6557 1.1514 -0.0117 -0.0465 -0.1037 869 PRO A O   
1887 C CB  . PRO A 261 ? 0.6931 0.6974 1.0698 -0.0223 -0.0257 -0.1033 869 PRO A CB  
1888 C CG  . PRO A 261 ? 0.7061 0.7095 1.0537 -0.0251 -0.0402 -0.0859 869 PRO A CG  
1889 C CD  . PRO A 261 ? 0.6773 0.6726 1.0470 -0.0253 -0.0552 -0.0747 869 PRO A CD  
1890 N N   . TYR A 262 ? 0.6743 0.6755 1.1505 -0.0143 -0.0103 -0.1363 870 TYR A N   
1891 C CA  . TYR A 262 ? 0.6666 0.6712 1.1987 -0.0089 -0.0039 -0.1493 870 TYR A CA  
1892 C C   . TYR A 262 ? 0.6715 0.6647 1.2409 -0.0029 -0.0214 -0.1432 870 TYR A C   
1893 O O   . TYR A 262 ? 0.6558 0.6513 1.2612 0.0046  -0.0367 -0.1351 870 TYR A O   
1894 C CB  . TYR A 262 ? 0.6511 0.6702 1.2088 -0.0087 -0.0026 -0.1484 870 TYR A CB  
1895 C CG  . TYR A 262 ? 0.6798 0.7009 1.1986 -0.0156 0.0190  -0.1521 870 TYR A CG  
1896 C CD1 . TYR A 262 ? 0.6989 0.7177 1.2151 -0.0166 0.0496  -0.1704 870 TYR A CD1 
1897 C CD2 . TYR A 262 ? 0.7073 0.7271 1.1857 -0.0201 0.0110  -0.1366 870 TYR A CD2 
1898 C CE1 . TYR A 262 ? 0.7312 0.7422 1.2038 -0.0213 0.0726  -0.1707 870 TYR A CE1 
1899 C CE2 . TYR A 262 ? 0.7397 0.7539 1.1793 -0.0247 0.0322  -0.1384 870 TYR A CE2 
1900 C CZ  . TYR A 262 ? 0.7575 0.7649 1.1924 -0.0250 0.0635  -0.1543 870 TYR A CZ  
1901 O OH  . TYR A 262 ? 0.7994 0.7920 1.1890 -0.0279 0.0883  -0.1537 870 TYR A OH  
1902 N N   . PRO A 263 ? 0.6904 0.6690 1.2489 -0.0056 -0.0210 -0.1463 871 PRO A N   
1903 C CA  . PRO A 263 ? 0.7004 0.6583 1.2891 -0.0008 -0.0337 -0.1376 871 PRO A CA  
1904 C C   . PRO A 263 ? 0.7197 0.6758 1.3661 0.0120  -0.0360 -0.1450 871 PRO A C   
1905 O O   . PRO A 263 ? 0.7102 0.6799 1.3819 0.0142  -0.0195 -0.1673 871 PRO A O   
1906 C CB  . PRO A 263 ? 0.7056 0.6525 1.2853 -0.0082 -0.0235 -0.1521 871 PRO A CB  
1907 C CG  . PRO A 263 ? 0.7158 0.6796 1.2482 -0.0155 -0.0156 -0.1601 871 PRO A CG  
1908 C CD  . PRO A 263 ? 0.6933 0.6729 1.2142 -0.0119 -0.0088 -0.1603 871 PRO A CD  
1909 N N   . GLY A 264 ? 0.7401 0.6792 1.4043 0.0220  -0.0562 -0.1259 872 GLY A N   
1910 C CA  . GLY A 264 ? 0.7507 0.6866 1.4709 0.0392  -0.0649 -0.1306 872 GLY A CA  
1911 C C   . GLY A 264 ? 0.7559 0.7254 1.5134 0.0459  -0.0657 -0.1436 872 GLY A C   
1912 O O   . GLY A 264 ? 0.7464 0.7206 1.5602 0.0610  -0.0712 -0.1539 872 GLY A O   
1913 N N   . MET A 265 ? 0.7661 0.7587 1.4976 0.0349  -0.0588 -0.1450 873 MET A N   
1914 C CA  . MET A 265 ? 0.7618 0.7858 1.5322 0.0371  -0.0554 -0.1591 873 MET A CA  
1915 C C   . MET A 265 ? 0.7919 0.8255 1.5523 0.0407  -0.0826 -0.1417 873 MET A C   
1916 O O   . MET A 265 ? 0.8133 0.8469 1.5235 0.0291  -0.0815 -0.1306 873 MET A O   
1917 C CB  . MET A 265 ? 0.7693 0.8063 1.5162 0.0216  -0.0236 -0.1746 873 MET A CB  
1918 C CG  . MET A 265 ? 0.7958 0.8281 1.5532 0.0201  0.0048  -0.1972 873 MET A CG  
1919 S SD  . MET A 265 ? 0.8862 0.9278 1.6087 0.0065  0.0432  -0.2123 873 MET A SD  
1920 C CE  . MET A 265 ? 0.8797 0.9520 1.6706 0.0064  0.0478  -0.2234 873 MET A CE  
1921 N N   . PRO A 266 ? 0.7887 0.8309 1.5949 0.0587  -0.1092 -0.1405 874 PRO A N   
1922 C CA  . PRO A 266 ? 0.7977 0.8511 1.5915 0.0641  -0.1384 -0.1274 874 PRO A CA  
1923 C C   . PRO A 266 ? 0.7902 0.8801 1.6065 0.0518  -0.1269 -0.1465 874 PRO A C   
1924 O O   . PRO A 266 ? 0.7653 0.8761 1.6312 0.0467  -0.1027 -0.1717 874 PRO A O   
1925 C CB  . PRO A 266 ? 0.7890 0.8417 1.6289 0.0912  -0.1706 -0.1255 874 PRO A CB  
1926 C CG  . PRO A 266 ? 0.7649 0.8290 1.6716 0.0962  -0.1516 -0.1510 874 PRO A CG  
1927 C CD  . PRO A 266 ? 0.7588 0.8027 1.6307 0.0775  -0.1156 -0.1536 874 PRO A CD  
1928 N N   . VAL A 267 ? 0.8131 0.9077 1.5923 0.0458  -0.1406 -0.1355 875 VAL A N   
1929 C CA  . VAL A 267 ? 0.8191 0.9429 1.6185 0.0323  -0.1287 -0.1533 875 VAL A CA  
1930 C C   . VAL A 267 ? 0.8059 0.9672 1.6886 0.0447  -0.1489 -0.1761 875 VAL A C   
1931 O O   . VAL A 267 ? 0.8060 0.9751 1.6936 0.0608  -0.1884 -0.1699 875 VAL A O   
1932 C CB  . VAL A 267 ? 0.8467 0.9627 1.5827 0.0222  -0.1367 -0.1372 875 VAL A CB  
1933 C CG1 . VAL A 267 ? 0.8356 0.9795 1.6011 0.0094  -0.1272 -0.1575 875 VAL A CG1 
1934 C CG2 . VAL A 267 ? 0.8772 0.9646 1.5427 0.0099  -0.1137 -0.1214 875 VAL A CG2 
1935 N N   . ASP A 268 ? 0.7900 0.9749 1.7382 0.0388  -0.1218 -0.2040 876 ASP A N   
1936 C CA  . ASP A 268 ? 0.7678 0.9951 1.8095 0.0496  -0.1368 -0.2321 876 ASP A CA  
1937 C C   . ASP A 268 ? 0.7624 1.0157 1.8621 0.0295  -0.0910 -0.2642 876 ASP A C   
1938 O O   . ASP A 268 ? 0.7870 1.0197 1.8387 0.0086  -0.0520 -0.2597 876 ASP A O   
1939 C CB  . ASP A 268 ? 0.7794 1.0035 1.8592 0.0781  -0.1624 -0.2306 876 ASP A CB  
1940 C CG  . ASP A 268 ? 0.8524 1.0582 1.9418 0.0768  -0.1295 -0.2357 876 ASP A CG  
1941 O OD1 . ASP A 268 ? 0.8811 1.0748 1.9378 0.0552  -0.0882 -0.2382 876 ASP A OD1 
1942 O OD2 . ASP A 268 ? 0.8750 1.0762 2.0011 0.0994  -0.1461 -0.2373 876 ASP A OD2 
1943 N N   . SER A 269 ? 0.7258 1.0222 1.9269 0.0370  -0.0941 -0.2965 877 SER A N   
1944 C CA  . SER A 269 ? 0.7130 1.0344 1.9780 0.0175  -0.0466 -0.3291 877 SER A CA  
1945 C C   . SER A 269 ? 0.7412 1.0315 1.9730 0.0082  0.0027  -0.3265 877 SER A C   
1946 O O   . SER A 269 ? 0.7497 1.0338 1.9722 -0.0142 0.0513  -0.3369 877 SER A O   
1947 C CB  . SER A 269 ? 0.6807 1.0574 2.0677 0.0308  -0.0628 -0.3658 877 SER A CB  
1948 O OG  . SER A 269 ? 0.6926 1.0780 2.1378 0.0400  -0.0412 -0.3841 877 SER A OG  
1949 N N   . LYS A 270 ? 0.7549 1.0222 1.9641 0.0258  -0.0095 -0.3127 878 LYS A N   
1950 C CA  . LYS A 270 ? 0.7789 1.0168 1.9521 0.0196  0.0307  -0.3122 878 LYS A CA  
1951 C C   . LYS A 270 ? 0.8268 1.0273 1.8954 0.0020  0.0511  -0.2892 878 LYS A C   
1952 O O   . LYS A 270 ? 0.8387 1.0257 1.8816 -0.0127 0.0967  -0.2975 878 LYS A O   
1953 C CB  . LYS A 270 ? 0.8037 1.0228 1.9752 0.0421  0.0075  -0.3024 878 LYS A CB  
1954 C CG  . LYS A 270 ? 0.8610 1.0600 2.0216 0.0391  0.0461  -0.3133 878 LYS A CG  
1955 C CD  . LYS A 270 ? 0.9245 1.0964 2.0718 0.0582  0.0221  -0.3004 878 LYS A CD  
1956 C CE  . LYS A 270 ? 0.9711 1.1348 2.1421 0.0611  0.0542  -0.3223 878 LYS A CE  
1957 N NZ  . LYS A 270 ? 0.9589 1.1578 2.2355 0.0752  0.0564  -0.3518 878 LYS A NZ  
1958 N N   . PHE A 271 ? 0.8492 1.0328 1.8572 0.0050  0.0179  -0.2613 879 PHE A N   
1959 C CA  . PHE A 271 ? 0.8955 1.0474 1.8094 -0.0076 0.0305  -0.2400 879 PHE A CA  
1960 C C   . PHE A 271 ? 0.9012 1.0553 1.8026 -0.0276 0.0634  -0.2479 879 PHE A C   
1961 O O   . PHE A 271 ? 0.9288 1.0561 1.7690 -0.0373 0.0962  -0.2427 879 PHE A O   
1962 C CB  . PHE A 271 ? 0.9160 1.0545 1.7805 0.0000  -0.0111 -0.2118 879 PHE A CB  
1963 C CG  . PHE A 271 ? 0.9631 1.0757 1.7401 -0.0119 -0.0008 -0.1926 879 PHE A CG  
1964 C CD1 . PHE A 271 ? 0.9988 1.0854 1.7209 -0.0131 0.0152  -0.1853 879 PHE A CD1 
1965 C CD2 . PHE A 271 ? 0.9787 1.0949 1.7320 -0.0208 -0.0071 -0.1855 879 PHE A CD2 
1966 C CE1 . PHE A 271 ? 1.0382 1.1053 1.6847 -0.0207 0.0221  -0.1704 879 PHE A CE1 
1967 C CE2 . PHE A 271 ? 1.0212 1.1137 1.6971 -0.0290 0.0025  -0.1691 879 PHE A CE2 
1968 C CZ  . PHE A 271 ? 1.0427 1.1121 1.6666 -0.0279 0.0161  -0.1614 879 PHE A CZ  
1969 N N   . TYR A 272 ? 0.8731 1.0571 1.8318 -0.0325 0.0542  -0.2614 880 TYR A N   
1970 C CA  . TYR A 272 ? 0.8835 1.0679 1.8411 -0.0532 0.0871  -0.2712 880 TYR A CA  
1971 C C   . TYR A 272 ? 0.8878 1.0682 1.8705 -0.0650 0.1438  -0.2924 880 TYR A C   
1972 O O   . TYR A 272 ? 0.9118 1.0648 1.8457 -0.0804 0.1834  -0.2888 880 TYR A O   
1973 C CB  . TYR A 272 ? 0.8471 1.0696 1.8728 -0.0559 0.0614  -0.2869 880 TYR A CB  
1974 C CG  . TYR A 272 ? 0.8685 1.0870 1.8497 -0.0471 0.0131  -0.2648 880 TYR A CG  
1975 C CD1 . TYR A 272 ? 0.9189 1.1034 1.8100 -0.0547 0.0176  -0.2404 880 TYR A CD1 
1976 C CD2 . TYR A 272 ? 0.8520 1.1009 1.8811 -0.0299 -0.0361 -0.2700 880 TYR A CD2 
1977 C CE1 . TYR A 272 ? 0.9439 1.1248 1.7944 -0.0474 -0.0225 -0.2218 880 TYR A CE1 
1978 C CE2 . TYR A 272 ? 0.8794 1.1207 1.8598 -0.0211 -0.0775 -0.2495 880 TYR A CE2 
1979 C CZ  . TYR A 272 ? 0.9311 1.1392 1.8241 -0.0315 -0.0685 -0.2262 880 TYR A CZ  
1980 O OH  . TYR A 272 ? 0.9672 1.1680 1.8124 -0.0237 -0.1054 -0.2077 880 TYR A OH  
1981 N N   . LYS A 273 ? 0.8660 1.0695 1.9200 -0.0564 0.1491  -0.3137 881 LYS A N   
1982 C CA  . LYS A 273 ? 0.8704 1.0712 1.9516 -0.0664 0.2052  -0.3362 881 LYS A CA  
1983 C C   . LYS A 273 ? 0.9312 1.0841 1.9137 -0.0669 0.2363  -0.3206 881 LYS A C   
1984 O O   . LYS A 273 ? 0.9502 1.0789 1.8982 -0.0812 0.2862  -0.3242 881 LYS A O   
1985 C CB  . LYS A 273 ? 0.8455 1.0831 2.0263 -0.0537 0.2005  -0.3635 881 LYS A CB  
1986 C CG  . LYS A 273 ? 0.8397 1.1276 2.1350 -0.0615 0.2044  -0.3961 881 LYS A CG  
1987 C CD  . LYS A 273 ? 0.8457 1.1684 2.2397 -0.0501 0.2132  -0.4273 881 LYS A CD  
1988 C CE  . LYS A 273 ? 0.8380 1.2202 2.3543 -0.0534 0.2022  -0.4612 881 LYS A CE  
1989 N NZ  . LYS A 273 ? 0.8263 1.2452 2.4486 -0.0492 0.2295  -0.4992 881 LYS A NZ  
1990 N N   . MET A 274 ? 0.9583 1.0958 1.8941 -0.0508 0.2075  -0.3041 882 MET A N   
1991 C CA  . MET A 274 ? 1.0155 1.1134 1.8611 -0.0490 0.2304  -0.2938 882 MET A CA  
1992 C C   . MET A 274 ? 1.0584 1.1250 1.8136 -0.0571 0.2382  -0.2719 882 MET A C   
1993 O O   . MET A 274 ? 1.0924 1.1274 1.7848 -0.0609 0.2771  -0.2713 882 MET A O   
1994 C CB  . MET A 274 ? 1.0462 1.1371 1.8732 -0.0324 0.2005  -0.2871 882 MET A CB  
1995 C CG  . MET A 274 ? 1.0788 1.1886 1.9451 -0.0212 0.1477  -0.2763 882 MET A CG  
1996 S SD  . MET A 274 ? 1.1807 1.2983 2.1069 -0.0028 0.1335  -0.2909 882 MET A SD  
1997 C CE  . MET A 274 ? 1.1013 1.2503 2.1230 -0.0066 0.1724  -0.3274 882 MET A CE  
1998 N N   . ILE A 275 ? 1.0553 1.1290 1.8033 -0.0588 0.2037  -0.2552 883 ILE A N   
1999 C CA  . ILE A 275 ? 1.0954 1.1401 1.7631 -0.0653 0.2103  -0.2356 883 ILE A CA  
2000 C C   . ILE A 275 ? 1.1047 1.1345 1.7735 -0.0818 0.2602  -0.2451 883 ILE A C   
2001 O O   . ILE A 275 ? 1.1532 1.1429 1.7407 -0.0832 0.2892  -0.2339 883 ILE A O   
2002 C CB  . ILE A 275 ? 1.0995 1.1545 1.7592 -0.0631 0.1639  -0.2174 883 ILE A CB  
2003 C CG1 . ILE A 275 ? 1.1184 1.1725 1.7517 -0.0484 0.1257  -0.2031 883 ILE A CG1 
2004 C CG2 . ILE A 275 ? 1.1377 1.1657 1.7293 -0.0710 0.1750  -0.2018 883 ILE A CG2 
2005 C CD1 . ILE A 275 ? 1.1678 1.1929 1.7213 -0.0427 0.1371  -0.1945 883 ILE A CD1 
2006 N N   . LYS A 276 ? 1.0570 1.1173 1.8185 -0.0932 0.2726  -0.2675 884 LYS A N   
2007 C CA  . LYS A 276 ? 1.0545 1.1019 1.8325 -0.1128 0.3260  -0.2808 884 LYS A CA  
2008 C C   . LYS A 276 ? 1.0717 1.0883 1.8139 -0.1133 0.3813  -0.2882 884 LYS A C   
2009 O O   . LYS A 276 ? 1.1062 1.0814 1.7943 -0.1235 0.4288  -0.2829 884 LYS A O   
2010 C CB  . LYS A 276 ? 1.0193 1.1167 1.9206 -0.1242 0.3222  -0.3095 884 LYS A CB  
2011 C CG  . LYS A 276 ? 1.0679 1.1567 1.9963 -0.1489 0.3671  -0.3227 884 LYS A CG  
2012 C CD  . LYS A 276 ? 1.0641 1.2115 2.1293 -0.1600 0.3638  -0.3593 884 LYS A CD  
2013 C CE  . LYS A 276 ? 1.1033 1.2444 2.2028 -0.1879 0.4047  -0.3749 884 LYS A CE  
2014 N NZ  . LYS A 276 ? 1.0730 1.2574 2.2985 -0.2039 0.4386  -0.4170 884 LYS A NZ  
2015 N N   . GLU A 277 ? 1.0501 1.0819 1.8155 -0.1006 0.3749  -0.2995 885 GLU A N   
2016 C CA  . GLU A 277 ? 1.0673 1.0739 1.7994 -0.0977 0.4216  -0.3097 885 GLU A CA  
2017 C C   . GLU A 277 ? 1.1122 1.0673 1.7126 -0.0857 0.4280  -0.2873 885 GLU A C   
2018 O O   . GLU A 277 ? 1.1431 1.0640 1.6907 -0.0848 0.4751  -0.2921 885 GLU A O   
2019 C CB  . GLU A 277 ? 1.0742 1.1141 1.8727 -0.0853 0.4048  -0.3296 885 GLU A CB  
2020 C CG  . GLU A 277 ? 1.1067 1.1712 1.9980 -0.0945 0.4475  -0.3627 885 GLU A CG  
2021 C CD  . GLU A 277 ? 1.1766 1.2633 2.1174 -0.0794 0.4384  -0.3823 885 GLU A CD  
2022 O OE1 . GLU A 277 ? 1.1952 1.2780 2.1027 -0.0626 0.3962  -0.3700 885 GLU A OE1 
2023 O OE2 . GLU A 277 ? 1.1846 1.2918 2.2008 -0.0851 0.4756  -0.4114 885 GLU A OE2 
2024 N N   . GLY A 278 ? 1.1078 1.0595 1.6578 -0.0750 0.3806  -0.2654 886 GLY A N   
2025 C CA  . GLY A 278 ? 1.1416 1.0533 1.5762 -0.0612 0.3790  -0.2478 886 GLY A CA  
2026 C C   . GLY A 278 ? 1.1232 1.0473 1.5423 -0.0445 0.3395  -0.2485 886 GLY A C   
2027 O O   . GLY A 278 ? 1.1622 1.0597 1.4983 -0.0316 0.3428  -0.2449 886 GLY A O   
2028 N N   . PHE A 279 ? 1.0597 1.0226 1.5577 -0.0437 0.3019  -0.2542 887 PHE A N   
2029 C CA  . PHE A 279 ? 1.0457 1.0173 1.5368 -0.0308 0.2658  -0.2543 887 PHE A CA  
2030 C C   . PHE A 279 ? 1.0471 1.0099 1.4767 -0.0261 0.2310  -0.2308 887 PHE A C   
2031 O O   . PHE A 279 ? 1.0427 1.0111 1.4792 -0.0327 0.2163  -0.2158 887 PHE A O   
2032 C CB  . PHE A 279 ? 1.0066 1.0141 1.5973 -0.0297 0.2389  -0.2643 887 PHE A CB  
2033 C CG  . PHE A 279 ? 1.0253 1.0395 1.6156 -0.0206 0.1927  -0.2540 887 PHE A CG  
2034 C CD1 . PHE A 279 ? 1.0514 1.0560 1.6198 -0.0117 0.1888  -0.2634 887 PHE A CD1 
2035 C CD2 . PHE A 279 ? 1.0313 1.0583 1.6393 -0.0216 0.1557  -0.2358 887 PHE A CD2 
2036 C CE1 . PHE A 279 ? 1.0611 1.0679 1.6306 -0.0064 0.1516  -0.2545 887 PHE A CE1 
2037 C CE2 . PHE A 279 ? 1.0447 1.0713 1.6462 -0.0147 0.1197  -0.2245 887 PHE A CE2 
2038 C CZ  . PHE A 279 ? 1.0512 1.0673 1.6365 -0.0083 0.1193  -0.2338 887 PHE A CZ  
2039 N N   . ARG A 280 ? 1.0403 0.9920 1.4142 -0.0149 0.2179  -0.2310 888 ARG A N   
2040 C CA  . ARG A 280 ? 1.0300 0.9779 1.3516 -0.0096 0.1864  -0.2136 888 ARG A CA  
2041 C C   . ARG A 280 ? 1.0018 0.9627 1.3378 -0.0035 0.1564  -0.2205 888 ARG A C   
2042 O O   . ARG A 280 ? 1.0006 0.9637 1.3609 -0.0002 0.1649  -0.2398 888 ARG A O   
2043 C CB  . ARG A 280 ? 1.0724 0.9891 1.2962 -0.0004 0.2045  -0.2086 888 ARG A CB  
2044 C CG  . ARG A 280 ? 1.1099 1.0016 1.3076 -0.0065 0.2406  -0.1999 888 ARG A CG  
2045 C CD  . ARG A 280 ? 1.1200 1.0207 1.3452 -0.0173 0.2264  -0.1829 888 ARG A CD  
2046 N NE  . ARG A 280 ? 1.1530 1.0252 1.3536 -0.0249 0.2642  -0.1767 888 ARG A NE  
2047 C CZ  . ARG A 280 ? 1.1389 1.0201 1.4050 -0.0414 0.2862  -0.1837 888 ARG A CZ  
2048 N NH1 . ARG A 280 ? 1.0845 1.0048 1.4431 -0.0485 0.2697  -0.1967 888 ARG A NH1 
2049 N NH2 . ARG A 280 ? 1.1482 0.9986 1.3897 -0.0502 0.3244  -0.1788 888 ARG A NH2 
2050 N N   . MET A 281 ? 0.9869 0.9542 1.3071 -0.0026 0.1248  -0.2066 889 MET A N   
2051 C CA  . MET A 281 ? 0.9693 0.9455 1.3016 0.0004  0.1000  -0.2134 889 MET A CA  
2052 C C   . MET A 281 ? 0.9970 0.9647 1.2774 0.0103  0.1065  -0.2327 889 MET A C   
2053 O O   . MET A 281 ? 1.0148 0.9670 1.2299 0.0184  0.1229  -0.2338 889 MET A O   
2054 C CB  . MET A 281 ? 0.9562 0.9404 1.2813 -0.0027 0.0701  -0.1943 889 MET A CB  
2055 C CG  . MET A 281 ? 0.9220 0.9153 1.3021 -0.0097 0.0551  -0.1794 889 MET A CG  
2056 S SD  . MET A 281 ? 0.8616 0.8598 1.2280 -0.0131 0.0246  -0.1586 889 MET A SD  
2057 C CE  . MET A 281 ? 0.8065 0.7999 1.1085 -0.0116 0.0313  -0.1474 889 MET A CE  
2058 N N   . LEU A 282 ? 0.9997 0.9752 1.3082 0.0108  0.0928  -0.2486 890 LEU A N   
2059 C CA  . LEU A 282 ? 1.0313 1.0051 1.3024 0.0195  0.0913  -0.2727 890 LEU A CA  
2060 C C   . LEU A 282 ? 1.0543 1.0372 1.2856 0.0228  0.0666  -0.2677 890 LEU A C   
2061 O O   . LEU A 282 ? 1.0511 1.0427 1.3033 0.0150  0.0495  -0.2483 890 LEU A O   
2062 C CB  . LEU A 282 ? 1.0148 0.9941 1.3456 0.0152  0.0846  -0.2922 890 LEU A CB  
2063 C CG  . LEU A 282 ? 1.0162 0.9901 1.3971 0.0144  0.1062  -0.3020 890 LEU A CG  
2064 C CD1 . LEU A 282 ? 0.9961 0.9711 1.4410 0.0108  0.0951  -0.3154 890 LEU A CD1 
2065 C CD2 . LEU A 282 ? 1.0421 1.0043 1.3777 0.0233  0.1363  -0.3219 890 LEU A CD2 
2066 N N   . SER A 283 ? 1.0751 1.0582 1.2525 0.0355  0.0632  -0.2879 891 SER A N   
2067 C CA  . SER A 283 ? 1.0909 1.0893 1.2386 0.0409  0.0376  -0.2896 891 SER A CA  
2068 C C   . SER A 283 ? 1.0815 1.0995 1.2905 0.0275  0.0171  -0.2965 891 SER A C   
2069 O O   . SER A 283 ? 1.0693 1.0886 1.3195 0.0219  0.0185  -0.3173 891 SER A O   
2070 C CB  . SER A 283 ? 1.1190 1.1172 1.2022 0.0604  0.0338  -0.3161 891 SER A CB  
2071 O OG  . SER A 283 ? 1.1333 1.1511 1.1915 0.0686  0.0070  -0.3202 891 SER A OG  
2072 N N   . PRO A 284 ? 1.0882 1.1190 1.3024 0.0221  0.0002  -0.2804 892 PRO A N   
2073 C CA  . PRO A 284 ? 1.0757 1.1217 1.3436 0.0081  -0.0147 -0.2878 892 PRO A CA  
2074 C C   . PRO A 284 ? 1.0874 1.1527 1.3523 0.0131  -0.0270 -0.3263 892 PRO A C   
2075 O O   . PRO A 284 ? 1.1043 1.1749 1.3142 0.0311  -0.0312 -0.3433 892 PRO A O   
2076 C CB  . PRO A 284 ? 1.0797 1.1341 1.3410 0.0036  -0.0254 -0.2623 892 PRO A CB  
2077 C CG  . PRO A 284 ? 1.1022 1.1427 1.3158 0.0134  -0.0159 -0.2397 892 PRO A CG  
2078 C CD  . PRO A 284 ? 1.0977 1.1275 1.2680 0.0284  -0.0036 -0.2569 892 PRO A CD  
2079 N N   . GLU A 285 ? 1.0772 1.1506 1.4006 -0.0023 -0.0326 -0.3413 893 GLU A N   
2080 C CA  . GLU A 285 ? 1.0815 1.1763 1.4195 -0.0022 -0.0443 -0.3833 893 GLU A CA  
2081 C C   . GLU A 285 ? 1.0794 1.2064 1.3837 0.0094  -0.0655 -0.3988 893 GLU A C   
2082 O O   . GLU A 285 ? 1.0869 1.2291 1.3607 0.0252  -0.0769 -0.4322 893 GLU A O   
2083 C CB  . GLU A 285 ? 1.1082 1.2004 1.5221 -0.0254 -0.0419 -0.3908 893 GLU A CB  
2084 C CG  . GLU A 285 ? 1.1837 1.2667 1.6327 -0.0297 -0.0351 -0.4242 893 GLU A CG  
2085 C CD  . GLU A 285 ? 1.2834 1.3556 1.8052 -0.0530 -0.0294 -0.4288 893 GLU A CD  
2086 O OE1 . GLU A 285 ? 1.3061 1.3647 1.8470 -0.0646 -0.0248 -0.3947 893 GLU A OE1 
2087 O OE2 . GLU A 285 ? 1.3100 1.3837 1.8668 -0.0595 -0.0284 -0.4668 893 GLU A OE2 
2088 N N   . HIS A 286 ? 1.0669 1.2049 1.3754 0.0041  -0.0718 -0.3765 894 HIS A N   
2089 C CA  . HIS A 286 ? 1.0646 1.2365 1.3515 0.0158  -0.0925 -0.3919 894 HIS A CA  
2090 C C   . HIS A 286 ? 1.0775 1.2442 1.2826 0.0434  -0.0985 -0.3783 894 HIS A C   
2091 O O   . HIS A 286 ? 1.0742 1.2662 1.2583 0.0569  -0.1168 -0.3857 894 HIS A O   
2092 C CB  . HIS A 286 ? 1.0720 1.2585 1.4034 -0.0026 -0.0937 -0.3772 894 HIS A CB  
2093 C CG  . HIS A 286 ? 1.1094 1.2924 1.5154 -0.0300 -0.0835 -0.3865 894 HIS A CG  
2094 N ND1 . HIS A 286 ? 1.1456 1.2945 1.5758 -0.0463 -0.0656 -0.3530 894 HIS A ND1 
2095 C CD2 . HIS A 286 ? 1.1049 1.3111 1.5636 -0.0422 -0.0884 -0.4259 894 HIS A CD2 
2096 C CE1 . HIS A 286 ? 1.1336 1.2800 1.6245 -0.0670 -0.0581 -0.3693 894 HIS A CE1 
2097 N NE2 . HIS A 286 ? 1.1144 1.2950 1.6281 -0.0675 -0.0697 -0.4141 894 HIS A NE2 
2098 N N   . ALA A 287 ? 1.0868 1.2197 1.2478 0.0522  -0.0816 -0.3591 895 ALA A N   
2099 C CA  . ALA A 287 ? 1.1098 1.2269 1.1914 0.0761  -0.0805 -0.3421 895 ALA A CA  
2100 C C   . ALA A 287 ? 1.1231 1.2403 1.1378 0.1048  -0.0904 -0.3691 895 ALA A C   
2101 O O   . ALA A 287 ? 1.1382 1.2385 1.1368 0.1084  -0.0782 -0.3831 895 ALA A O   
2102 C CB  . ALA A 287 ? 1.1275 1.2073 1.1951 0.0703  -0.0540 -0.3084 895 ALA A CB  
2103 N N   . PRO A 288 ? 1.1224 1.2539 1.0885 0.1289  -0.1115 -0.3742 896 PRO A N   
2104 C CA  . PRO A 288 ? 1.1482 1.2716 1.0321 0.1628  -0.1222 -0.3946 896 PRO A CA  
2105 C C   . PRO A 288 ? 1.1945 1.2639 1.0071 0.1728  -0.0911 -0.3684 896 PRO A C   
2106 O O   . PRO A 288 ? 1.2039 1.2479 1.0177 0.1615  -0.0695 -0.3322 896 PRO A O   
2107 C CB  . PRO A 288 ? 1.1558 1.2994 1.0049 0.1871  -0.1490 -0.3940 896 PRO A CB  
2108 C CG  . PRO A 288 ? 1.1187 1.2964 1.0523 0.1614  -0.1558 -0.3892 896 PRO A CG  
2109 C CD  . PRO A 288 ? 1.0991 1.2513 1.0769 0.1295  -0.1259 -0.3603 896 PRO A CD  
2110 N N   . ALA A 289 ? 1.2233 1.2749 0.9766 0.1924  -0.0867 -0.3886 897 ALA A N   
2111 C CA  . ALA A 289 ? 1.2678 1.2662 0.9538 0.2004  -0.0509 -0.3672 897 ALA A CA  
2112 C C   . ALA A 289 ? 1.3010 1.2624 0.9242 0.2130  -0.0366 -0.3275 897 ALA A C   
2113 O O   . ALA A 289 ? 1.3169 1.2459 0.9448 0.1975  -0.0021 -0.2997 897 ALA A O   
2114 C CB  . ALA A 289 ? 1.2984 1.2828 0.9106 0.2269  -0.0525 -0.3965 897 ALA A CB  
2115 N N   . GLU A 290 ? 1.3041 1.2725 0.8774 0.2401  -0.0634 -0.3267 898 GLU A N   
2116 C CA  . GLU A 290 ? 1.3298 1.2602 0.8418 0.2547  -0.0519 -0.2906 898 GLU A CA  
2117 C C   . GLU A 290 ? 1.2848 1.2183 0.8652 0.2238  -0.0381 -0.2609 898 GLU A C   
2118 O O   . GLU A 290 ? 1.3047 1.1964 0.8483 0.2242  -0.0127 -0.2296 898 GLU A O   
2119 C CB  . GLU A 290 ? 1.3833 1.3272 0.8388 0.2924  -0.0892 -0.3001 898 GLU A CB  
2120 C CG  . GLU A 290 ? 1.4897 1.4310 0.8685 0.3287  -0.1089 -0.3310 898 GLU A CG  
2121 C CD  . GLU A 290 ? 1.5613 1.5681 1.0015 0.3270  -0.1479 -0.3796 898 GLU A CD  
2122 O OE1 . GLU A 290 ? 1.5207 1.5745 1.0645 0.2975  -0.1591 -0.3877 898 GLU A OE1 
2123 O OE2 . GLU A 290 ? 1.6354 1.6445 1.0185 0.3551  -0.1662 -0.4106 898 GLU A OE2 
2124 N N   . MET A 291 ? 1.2231 1.2029 0.9006 0.1969  -0.0532 -0.2719 899 MET A N   
2125 C CA  . MET A 291 ? 1.1902 1.1777 0.9350 0.1680  -0.0447 -0.2482 899 MET A CA  
2126 C C   . MET A 291 ? 1.1808 1.1447 0.9588 0.1434  -0.0114 -0.2340 899 MET A C   
2127 O O   . MET A 291 ? 1.1802 1.1285 0.9747 0.1292  0.0044  -0.2074 899 MET A O   
2128 C CB  . MET A 291 ? 1.1543 1.1937 0.9804 0.1512  -0.0707 -0.2655 899 MET A CB  
2129 C CG  . MET A 291 ? 1.1826 1.2487 0.9957 0.1690  -0.0990 -0.2710 899 MET A CG  
2130 S SD  . MET A 291 ? 1.2606 1.3019 1.0498 0.1700  -0.0886 -0.2310 899 MET A SD  
2131 C CE  . MET A 291 ? 1.2763 1.3371 1.0175 0.2073  -0.1204 -0.2453 899 MET A CE  
2132 N N   . TYR A 292 ? 1.1689 1.1314 0.9584 0.1394  -0.0011 -0.2543 900 TYR A N   
2133 C CA  . TYR A 292 ? 1.1557 1.0981 0.9792 0.1194  0.0310  -0.2442 900 TYR A CA  
2134 C C   . TYR A 292 ? 1.1823 1.0764 0.9366 0.1296  0.0647  -0.2245 900 TYR A C   
2135 O O   . TYR A 292 ? 1.1727 1.0517 0.9582 0.1117  0.0901  -0.2069 900 TYR A O   
2136 C CB  . TYR A 292 ? 1.1428 1.0964 1.0015 0.1129  0.0345  -0.2724 900 TYR A CB  
2137 C CG  . TYR A 292 ? 1.1438 1.0851 1.0548 0.0924  0.0636  -0.2645 900 TYR A CG  
2138 C CD1 . TYR A 292 ? 1.1330 1.0825 1.1084 0.0714  0.0645  -0.2437 900 TYR A CD1 
2139 C CD2 . TYR A 292 ? 1.1634 1.0875 1.0616 0.0955  0.0885  -0.2808 900 TYR A CD2 
2140 C CE1 . TYR A 292 ? 1.1311 1.0739 1.1584 0.0561  0.0869  -0.2392 900 TYR A CE1 
2141 C CE2 . TYR A 292 ? 1.1585 1.0770 1.1140 0.0781  0.1140  -0.2772 900 TYR A CE2 
2142 C CZ  . TYR A 292 ? 1.1468 1.0764 1.1693 0.0591  0.1114  -0.2569 900 TYR A CZ  
2143 O OH  . TYR A 292 ? 1.1425 1.0709 1.2257 0.0452  0.1323  -0.2560 900 TYR A OH  
2144 N N   . ASP A 293 ? 1.2172 1.0855 0.8767 0.1593  0.0646  -0.2271 901 ASP A N   
2145 C CA  . ASP A 293 ? 1.2676 1.0804 0.8497 0.1710  0.0997  -0.2058 901 ASP A CA  
2146 C C   . ASP A 293 ? 1.2496 1.0502 0.8427 0.1615  0.1051  -0.1757 901 ASP A C   
2147 O O   . ASP A 293 ? 1.2636 1.0315 0.8577 0.1482  0.1414  -0.1580 901 ASP A O   
2148 C CB  . ASP A 293 ? 1.3680 1.1530 0.8378 0.2099  0.0923  -0.2131 901 ASP A CB  
2149 C CG  . ASP A 293 ? 1.5058 1.2902 0.9456 0.2216  0.0954  -0.2427 901 ASP A CG  
2150 O OD1 . ASP A 293 ? 1.4926 1.3009 1.0062 0.1983  0.1029  -0.2595 901 ASP A OD1 
2151 O OD2 . ASP A 293 ? 1.6054 1.3634 0.9443 0.2562  0.0897  -0.2497 901 ASP A OD2 
2152 N N   . ILE A 294 ? 1.2115 1.0422 0.8232 0.1654  0.0700  -0.1732 902 ILE A N   
2153 C CA  . ILE A 294 ? 1.1877 1.0121 0.8155 0.1559  0.0713  -0.1483 902 ILE A CA  
2154 C C   . ILE A 294 ? 1.1415 0.9767 0.8527 0.1217  0.0876  -0.1405 902 ILE A C   
2155 O O   . ILE A 294 ? 1.1599 0.9642 0.8649 0.1125  0.1151  -0.1225 902 ILE A O   
2156 C CB  . ILE A 294 ? 1.1720 1.0302 0.8090 0.1662  0.0325  -0.1503 902 ILE A CB  
2157 C CG1 . ILE A 294 ? 1.2090 1.0527 0.7567 0.2062  0.0153  -0.1566 902 ILE A CG1 
2158 C CG2 . ILE A 294 ? 1.1670 1.0198 0.8300 0.1518  0.0369  -0.1265 902 ILE A CG2 
2159 C CD1 . ILE A 294 ? 1.2032 1.0816 0.7591 0.2207  -0.0220 -0.1613 902 ILE A CD1 
2160 N N   . MET A 295 ? 1.0858 0.9606 0.8730 0.1041  0.0732  -0.1555 903 MET A N   
2161 C CA  . MET A 295 ? 1.0553 0.9408 0.9206 0.0764  0.0846  -0.1496 903 MET A CA  
2162 C C   . MET A 295 ? 1.0858 0.9389 0.9445 0.0696  0.1252  -0.1463 903 MET A C   
2163 O O   . MET A 295 ? 1.0850 0.9257 0.9648 0.0560  0.1423  -0.1319 903 MET A O   
2164 C CB  . MET A 295 ? 1.0106 0.9326 0.9458 0.0641  0.0666  -0.1670 903 MET A CB  
2165 C CG  . MET A 295 ? 0.9933 0.9473 0.9479 0.0651  0.0331  -0.1720 903 MET A CG  
2166 S SD  . MET A 295 ? 0.9008 0.8850 0.9325 0.0500  0.0198  -0.1924 903 MET A SD  
2167 C CE  . MET A 295 ? 0.8619 0.8726 0.8734 0.0638  -0.0085 -0.2145 903 MET A CE  
2168 N N   . LYS A 296 ? 1.1131 0.9518 0.9391 0.0798  0.1422  -0.1618 904 LYS A N   
2169 C CA  . LYS A 296 ? 1.1417 0.9485 0.9562 0.0746  0.1861  -0.1624 904 LYS A CA  
2170 C C   . LYS A 296 ? 1.1901 0.9523 0.9549 0.0758  0.2160  -0.1403 904 LYS A C   
2171 O O   . LYS A 296 ? 1.1883 0.9401 0.9931 0.0568  0.2469  -0.1362 904 LYS A O   
2172 C CB  . LYS A 296 ? 1.1893 0.9811 0.9479 0.0926  0.1969  -0.1815 904 LYS A CB  
2173 C CG  . LYS A 296 ? 1.2014 1.0288 1.0216 0.0856  0.1826  -0.2072 904 LYS A CG  
2174 C CD  . LYS A 296 ? 1.2733 1.0844 1.0312 0.1048  0.1931  -0.2293 904 LYS A CD  
2175 C CE  . LYS A 296 ? 1.3598 1.1282 1.0801 0.1043  0.2457  -0.2264 904 LYS A CE  
2176 N NZ  . LYS A 296 ? 1.4236 1.1708 1.0717 0.1248  0.2590  -0.2476 904 LYS A NZ  
2177 N N   . THR A 297 ? 1.2294 0.9670 0.9152 0.0973  0.2059  -0.1275 905 THR A N   
2178 C CA  . THR A 297 ? 1.2741 0.9623 0.9104 0.0992  0.2353  -0.1054 905 THR A CA  
2179 C C   . THR A 297 ? 1.2496 0.9537 0.9516 0.0767  0.2293  -0.0935 905 THR A C   
2180 O O   . THR A 297 ? 1.2614 0.9325 0.9632 0.0644  0.2636  -0.0827 905 THR A O   
2181 C CB  . THR A 297 ? 1.3429 0.9942 0.8710 0.1332  0.2269  -0.0949 905 THR A CB  
2182 O OG1 . THR A 297 ? 1.3455 1.0388 0.8859 0.1448  0.1767  -0.1001 905 THR A OG1 
2183 C CG2 . THR A 297 ? 1.3815 1.0000 0.8270 0.1565  0.2446  -0.1038 905 THR A CG2 
2184 N N   . CYS A 298 ? 1.2157 0.9680 0.9728 0.0706  0.1881  -0.0968 906 CYS A N   
2185 C CA  . CYS A 298 ? 1.1879 0.9577 1.0053 0.0504  0.1793  -0.0878 906 CYS A CA  
2186 C C   . CYS A 298 ? 1.1627 0.9469 1.0608 0.0245  0.1988  -0.0958 906 CYS A C   
2187 O O   . CYS A 298 ? 1.1437 0.9286 1.0810 0.0080  0.2052  -0.0904 906 CYS A O   
2188 C CB  . CYS A 298 ? 1.1545 0.9688 1.0050 0.0511  0.1344  -0.0896 906 CYS A CB  
2189 S SG  . CYS A 298 ? 1.1866 0.9971 0.9626 0.0807  0.1076  -0.0854 906 CYS A SG  
2190 N N   . TRP A 299 ? 1.1538 0.9529 1.0802 0.0224  0.2052  -0.1118 907 TRP A N   
2191 C CA  . TRP A 299 ? 1.1302 0.9487 1.1379 0.0025  0.2200  -0.1236 907 TRP A CA  
2192 C C   . TRP A 299 ? 1.1547 0.9394 1.1528 -0.0045 0.2721  -0.1282 907 TRP A C   
2193 O O   . TRP A 299 ? 1.1225 0.9256 1.1910 -0.0194 0.2878  -0.1421 907 TRP A O   
2194 C CB  . TRP A 299 ? 1.1017 0.9556 1.1543 0.0040  0.1977  -0.1394 907 TRP A CB  
2195 C CG  . TRP A 299 ? 1.0903 0.9759 1.1640 0.0061  0.1527  -0.1357 907 TRP A CG  
2196 C CD1 . TRP A 299 ? 1.0958 0.9913 1.1773 0.0019  0.1303  -0.1218 907 TRP A CD1 
2197 C CD2 . TRP A 299 ? 1.0787 0.9882 1.1722 0.0110  0.1290  -0.1476 907 TRP A CD2 
2198 N NE1 . TRP A 299 ? 1.0847 1.0071 1.1851 0.0041  0.0965  -0.1227 907 TRP A NE1 
2199 C CE2 . TRP A 299 ? 1.0752 1.0062 1.1866 0.0086  0.0953  -0.1385 907 TRP A CE2 
2200 C CE3 . TRP A 299 ? 1.0824 0.9951 1.1806 0.0164  0.1350  -0.1666 907 TRP A CE3 
2201 C CZ2 . TRP A 299 ? 1.0666 1.0196 1.2013 0.0099  0.0706  -0.1468 907 TRP A CZ2 
2202 C CZ3 . TRP A 299 ? 1.0758 1.0119 1.2001 0.0179  0.1075  -0.1763 907 TRP A CZ3 
2203 C CH2 . TRP A 299 ? 1.0644 1.0193 1.2071 0.0141  0.0769  -0.1659 907 TRP A CH2 
2204 N N   . ASP A 300 ? 1.2108 0.9443 1.1242 0.0061  0.3012  -0.1164 908 ASP A N   
2205 C CA  . ASP A 300 ? 1.2472 0.9392 1.1439 -0.0022 0.3584  -0.1181 908 ASP A CA  
2206 C C   . ASP A 300 ? 1.2276 0.9340 1.2125 -0.0306 0.3754  -0.1227 908 ASP A C   
2207 O O   . ASP A 300 ? 1.2144 0.9312 1.2195 -0.0370 0.3529  -0.1141 908 ASP A O   
2208 C CB  . ASP A 300 ? 1.3312 0.9577 1.1144 0.0159  0.3827  -0.0985 908 ASP A CB  
2209 C CG  . ASP A 300 ? 1.4226 0.9941 1.1501 0.0178  0.4424  -0.0987 908 ASP A CG  
2210 O OD1 . ASP A 300 ? 1.4051 0.9715 1.1905 -0.0070 0.4847  -0.1067 908 ASP A OD1 
2211 O OD2 . ASP A 300 ? 1.4997 1.0330 1.1252 0.0447  0.4477  -0.0921 908 ASP A OD2 
2212 N N   . ALA A 301 ? 1.2190 0.9320 1.2622 -0.0469 0.4117  -0.1399 909 ALA A N   
2213 C CA  . ALA A 301 ? 1.1916 0.9254 1.3300 -0.0737 0.4284  -0.1516 909 ALA A CA  
2214 C C   . ALA A 301 ? 1.2217 0.9101 1.3274 -0.0839 0.4586  -0.1386 909 ALA A C   
2215 O O   . ALA A 301 ? 1.1958 0.9065 1.3643 -0.1005 0.4459  -0.1430 909 ALA A O   
2216 C CB  . ALA A 301 ? 1.1730 0.9160 1.3692 -0.0864 0.4701  -0.1742 909 ALA A CB  
2217 N N   . ASP A 302 ? 1.2789 0.9006 1.2820 -0.0720 0.4967  -0.1226 910 ASP A N   
2218 C CA  . ASP A 302 ? 1.3255 0.8923 1.2859 -0.0787 0.5282  -0.1072 910 ASP A CA  
2219 C C   . ASP A 302 ? 1.3530 0.9109 1.2499 -0.0580 0.4834  -0.0864 910 ASP A C   
2220 O O   . ASP A 302 ? 1.3876 0.9288 1.1997 -0.0297 0.4644  -0.0740 910 ASP A O   
2221 C CB  . ASP A 302 ? 1.4104 0.9012 1.2860 -0.0741 0.5949  -0.0978 910 ASP A CB  
2222 C CG  . ASP A 302 ? 1.5274 0.9435 1.3376 -0.0763 0.6336  -0.0773 910 ASP A CG  
2223 O OD1 . ASP A 302 ? 1.5089 0.9363 1.3659 -0.0911 0.6190  -0.0773 910 ASP A OD1 
2224 O OD2 . ASP A 302 ? 1.6269 0.9695 1.3364 -0.0626 0.6801  -0.0616 910 ASP A OD2 
2225 N N   . PRO A 303 ? 1.3325 0.9053 1.2745 -0.0717 0.4652  -0.0857 911 PRO A N   
2226 C CA  . PRO A 303 ? 1.3487 0.9181 1.2403 -0.0535 0.4235  -0.0687 911 PRO A CA  
2227 C C   . PRO A 303 ? 1.4176 0.9147 1.1890 -0.0287 0.4435  -0.0451 911 PRO A C   
2228 O O   . PRO A 303 ? 1.4373 0.9375 1.1528 -0.0029 0.4055  -0.0335 911 PRO A O   
2229 C CB  . PRO A 303 ? 1.3296 0.9169 1.2911 -0.0767 0.4159  -0.0757 911 PRO A CB  
2230 C CG  . PRO A 303 ? 1.2891 0.9179 1.3572 -0.1034 0.4295  -0.1009 911 PRO A CG  
2231 C CD  . PRO A 303 ? 1.2861 0.8853 1.3326 -0.1039 0.4789  -0.1045 911 PRO A CD  
2232 N N   . LEU A 304 ? 1.4536 0.8846 1.1861 -0.0357 0.5036  -0.0383 912 LEU A N   
2233 C CA  . LEU A 304 ? 1.5262 0.8761 1.1359 -0.0096 0.5277  -0.0130 912 LEU A CA  
2234 C C   . LEU A 304 ? 1.5548 0.8902 1.0706 0.0261  0.5155  -0.0049 912 LEU A C   
2235 O O   . LEU A 304 ? 1.6162 0.9022 1.0290 0.0579  0.5100  0.0151  912 LEU A O   
2236 C CB  . LEU A 304 ? 1.5656 0.8416 1.1578 -0.0284 0.6012  -0.0072 912 LEU A CB  
2237 C CG  . LEU A 304 ? 1.5582 0.8407 1.2365 -0.0626 0.6150  -0.0176 912 LEU A CG  
2238 C CD1 . LEU A 304 ? 1.5974 0.7997 1.2535 -0.0813 0.6931  -0.0121 912 LEU A CD1 
2239 C CD2 . LEU A 304 ? 1.5740 0.8597 1.2346 -0.0501 0.5712  -0.0067 912 LEU A CD2 
2240 N N   . LYS A 305 ? 1.5074 0.8889 1.0607 0.0232  0.5059  -0.0225 913 LYS A N   
2241 C CA  . LYS A 305 ? 1.5193 0.8973 0.9954 0.0550  0.4894  -0.0219 913 LYS A CA  
2242 C C   . LYS A 305 ? 1.4692 0.9114 0.9623 0.0721  0.4186  -0.0287 913 LYS A C   
2243 O O   . LYS A 305 ? 1.4905 0.9381 0.9289 0.0980  0.3983  -0.0330 913 LYS A O   
2244 C CB  . LYS A 305 ? 1.5255 0.9147 1.0302 0.0432  0.5206  -0.0400 913 LYS A CB  
2245 C CG  . LYS A 305 ? 1.6139 0.9350 1.0876 0.0298  0.5967  -0.0344 913 LYS A CG  
2246 C CD  . LYS A 305 ? 1.6578 1.0043 1.1815 0.0152  0.6243  -0.0573 913 LYS A CD  
2247 C CE  . LYS A 305 ? 1.7521 1.0249 1.2201 0.0089  0.7032  -0.0518 913 LYS A CE  
2248 N NZ  . LYS A 305 ? 1.7731 1.0635 1.2509 0.0089  0.7230  -0.0722 913 LYS A NZ  
2249 N N   . ARG A 306 ? 1.3987 0.8897 0.9687 0.0569  0.3829  -0.0320 914 ARG A N   
2250 C CA  . ARG A 306 ? 1.3471 0.8958 0.9378 0.0693  0.3222  -0.0379 914 ARG A CA  
2251 C C   . ARG A 306 ? 1.3719 0.8936 0.8809 0.0997  0.3001  -0.0218 914 ARG A C   
2252 O O   . ARG A 306 ? 1.4083 0.8777 0.8763 0.1024  0.3241  -0.0052 914 ARG A O   
2253 C CB  . ARG A 306 ? 1.2865 0.8916 0.9830 0.0424  0.2967  -0.0462 914 ARG A CB  
2254 C CG  . ARG A 306 ? 1.2521 0.8904 1.0389 0.0155  0.3106  -0.0634 914 ARG A CG  
2255 C CD  . ARG A 306 ? 1.2176 0.9006 1.0930 -0.0061 0.2854  -0.0686 914 ARG A CD  
2256 N NE  . ARG A 306 ? 1.1917 0.9016 1.1554 -0.0303 0.3016  -0.0856 914 ARG A NE  
2257 C CZ  . ARG A 306 ? 1.1748 0.9109 1.2155 -0.0516 0.2954  -0.0933 914 ARG A CZ  
2258 N NH1 . ARG A 306 ? 1.1443 0.8806 1.1813 -0.0535 0.2753  -0.0850 914 ARG A NH1 
2259 N NH2 . ARG A 306 ? 1.1528 0.9165 1.2756 -0.0698 0.3085  -0.1118 914 ARG A NH2 
2260 N N   . PRO A 307 ? 1.3493 0.9065 0.8394 0.1225  0.2546  -0.0281 915 PRO A N   
2261 C CA  . PRO A 307 ? 1.3728 0.9101 0.7929 0.1537  0.2315  -0.0161 915 PRO A CA  
2262 C C   . PRO A 307 ? 1.3561 0.9105 0.8212 0.1415  0.2148  -0.0094 915 PRO A C   
2263 O O   . PRO A 307 ? 1.3194 0.9191 0.8725 0.1129  0.2042  -0.0178 915 PRO A O   
2264 C CB  . PRO A 307 ? 1.3636 0.9492 0.7772 0.1750  0.1871  -0.0327 915 PRO A CB  
2265 C CG  . PRO A 307 ? 1.3163 0.9587 0.8245 0.1463  0.1773  -0.0505 915 PRO A CG  
2266 C CD  . PRO A 307 ? 1.3006 0.9170 0.8356 0.1213  0.2232  -0.0485 915 PRO A CD  
2267 N N   . THR A 308 ? 1.3781 0.8927 0.7787 0.1652  0.2129  0.0058  916 THR A N   
2268 C CA  . THR A 308 ? 1.3486 0.8792 0.7840 0.1580  0.1949  0.0100  916 THR A CA  
2269 C C   . THR A 308 ? 1.3000 0.8931 0.7556 0.1731  0.1435  -0.0022 916 THR A C   
2270 O O   . THR A 308 ? 1.3082 0.9162 0.7314 0.1956  0.1251  -0.0114 916 THR A O   
2271 C CB  . THR A 308 ? 1.4206 0.8794 0.7817 0.1774  0.2171  0.0300  916 THR A CB  
2272 O OG1 . THR A 308 ? 1.4684 0.9084 0.7440 0.2221  0.1965  0.0353  916 THR A OG1 
2273 C CG2 . THR A 308 ? 1.4588 0.8489 0.7945 0.1625  0.2746  0.0413  916 THR A CG2 
2274 N N   . PHE A 309 ? 1.2467 0.8746 0.7528 0.1617  0.1217  -0.0040 917 PHE A N   
2275 C CA  . PHE A 309 ? 1.2055 0.8907 0.7346 0.1734  0.0788  -0.0160 917 PHE A CA  
2276 C C   . PHE A 309 ? 1.2511 0.9190 0.7047 0.2168  0.0617  -0.0146 917 PHE A C   
2277 O O   . PHE A 309 ? 1.2317 0.9414 0.6887 0.2327  0.0317  -0.0305 917 PHE A O   
2278 C CB  . PHE A 309 ? 1.1503 0.8690 0.7399 0.1532  0.0646  -0.0168 917 PHE A CB  
2279 C CG  . PHE A 309 ? 1.0923 0.8497 0.7613 0.1181  0.0632  -0.0243 917 PHE A CG  
2280 C CD1 . PHE A 309 ? 1.0651 0.8655 0.7706 0.1124  0.0465  -0.0373 917 PHE A CD1 
2281 C CD2 . PHE A 309 ? 1.0781 0.8271 0.7847 0.0926  0.0776  -0.0197 917 PHE A CD2 
2282 C CE1 . PHE A 309 ? 1.0356 0.8652 0.8091 0.0842  0.0449  -0.0421 917 PHE A CE1 
2283 C CE2 . PHE A 309 ? 1.0460 0.8295 0.8213 0.0656  0.0725  -0.0267 917 PHE A CE2 
2284 C CZ  . PHE A 309 ? 1.0212 0.8426 0.8275 0.0626  0.0566  -0.0362 917 PHE A CZ  
2285 N N   . LYS A 310 ? 1.3115 0.9145 0.6957 0.2370  0.0819  0.0031  918 LYS A N   
2286 C CA  . LYS A 310 ? 1.3683 0.9445 0.6714 0.2837  0.0664  0.0074  918 LYS A CA  
2287 C C   . LYS A 310 ? 1.4021 0.9687 0.6478 0.3082  0.0626  0.0008  918 LYS A C   
2288 O O   . LYS A 310 ? 1.4150 1.0033 0.6276 0.3436  0.0287  -0.0106 918 LYS A O   
2289 C CB  . LYS A 310 ? 1.4474 0.9451 0.6872 0.2987  0.0939  0.0308  918 LYS A CB  
2290 C CG  . LYS A 310 ? 1.5557 1.0337 0.7242 0.3496  0.0695  0.0348  918 LYS A CG  
2291 C CD  . LYS A 310 ? 1.6813 1.0898 0.8054 0.3620  0.0918  0.0560  918 LYS A CD  
2292 C CE  . LYS A 310 ? 1.7489 1.1725 0.8510 0.4031  0.0554  0.0518  918 LYS A CE  
2293 N NZ  . LYS A 310 ? 1.8312 1.1774 0.8783 0.4221  0.0773  0.0732  918 LYS A NZ  
2294 N N   . GLN A 311 ? 1.4128 0.9524 0.6514 0.2896  0.0954  0.0043  919 GLN A N   
2295 C CA  . GLN A 311 ? 1.4448 0.9779 0.6318 0.3096  0.0936  -0.0048 919 GLN A CA  
2296 C C   . GLN A 311 ? 1.3932 1.0097 0.6518 0.2985  0.0574  -0.0338 919 GLN A C   
2297 O O   . GLN A 311 ? 1.4104 1.0415 0.6304 0.3257  0.0347  -0.0496 919 GLN A O   
2298 C CB  . GLN A 311 ? 1.5001 0.9803 0.6639 0.2906  0.1446  0.0057  919 GLN A CB  
2299 C CG  . GLN A 311 ? 1.6015 0.9894 0.6882 0.3003  0.1887  0.0336  919 GLN A CG  
2300 C CD  . GLN A 311 ? 1.6742 1.0200 0.7639 0.2715  0.2440  0.0401  919 GLN A CD  
2301 O OE1 . GLN A 311 ? 1.6494 1.0403 0.8205 0.2373  0.2497  0.0248  919 GLN A OE1 
2302 N NE2 . GLN A 311 ? 1.7388 0.9949 0.7405 0.2854  0.2882  0.0627  919 GLN A NE2 
2303 N N   . ILE A 312 ? 1.3314 0.9985 0.6903 0.2596  0.0529  -0.0413 920 ILE A N   
2304 C CA  . ILE A 312 ? 1.2819 1.0213 0.7127 0.2459  0.0230  -0.0665 920 ILE A CA  
2305 C C   . ILE A 312 ? 1.2742 1.0579 0.7059 0.2721  -0.0202 -0.0824 920 ILE A C   
2306 O O   . ILE A 312 ? 1.2534 1.0763 0.6942 0.2828  -0.0454 -0.1065 920 ILE A O   
2307 C CB  . ILE A 312 ? 1.2316 1.0061 0.7608 0.2017  0.0290  -0.0669 920 ILE A CB  
2308 C CG1 . ILE A 312 ? 1.2363 0.9826 0.7809 0.1767  0.0662  -0.0603 920 ILE A CG1 
2309 C CG2 . ILE A 312 ? 1.1862 1.0285 0.7847 0.1905  -0.0020 -0.0896 920 ILE A CG2 
2310 C CD1 . ILE A 312 ? 1.2135 0.9737 0.8309 0.1423  0.0755  -0.0539 920 ILE A CD1 
2311 N N   . VAL A 313 ? 1.2883 1.0659 0.7123 0.2830  -0.0280 -0.0716 921 VAL A N   
2312 C CA  . VAL A 313 ? 1.2876 1.1098 0.7203 0.3080  -0.0667 -0.0881 921 VAL A CA  
2313 C C   . VAL A 313 ? 1.3461 1.1600 0.7041 0.3540  -0.0886 -0.1011 921 VAL A C   
2314 O O   . VAL A 313 ? 1.3240 1.1954 0.7109 0.3660  -0.1233 -0.1300 921 VAL A O   
2315 C CB  . VAL A 313 ? 1.2873 1.0976 0.7193 0.3142  -0.0670 -0.0738 921 VAL A CB  
2316 C CG1 . VAL A 313 ? 1.2740 1.1303 0.7128 0.3449  -0.1057 -0.0934 921 VAL A CG1 
2317 C CG2 . VAL A 313 ? 1.2524 1.0806 0.7591 0.2710  -0.0528 -0.0667 921 VAL A CG2 
2318 N N   . GLN A 314 ? 1.4157 1.1569 0.6776 0.3790  -0.0671 -0.0812 922 GLN A N   
2319 C CA  . GLN A 314 ? 1.4719 1.1946 0.6460 0.4272  -0.0870 -0.0904 922 GLN A CA  
2320 C C   . GLN A 314 ? 1.4724 1.2289 0.6604 0.4211  -0.0971 -0.1167 922 GLN A C   
2321 O O   . GLN A 314 ? 1.4719 1.2592 0.6354 0.4539  -0.1337 -0.1423 922 GLN A O   
2322 C CB  . GLN A 314 ? 1.5727 1.1982 0.6350 0.4518  -0.0534 -0.0586 922 GLN A CB  
2323 C CG  . GLN A 314 ? 1.6742 1.2603 0.7161 0.4629  -0.0446 -0.0347 922 GLN A CG  
2324 C CD  . GLN A 314 ? 1.8417 1.3239 0.7879 0.4736  0.0015  -0.0007 922 GLN A CD  
2325 O OE1 . GLN A 314 ? 1.9143 1.3470 0.7761 0.4934  0.0180  0.0056  922 GLN A OE1 
2326 N NE2 . GLN A 314 ? 1.8626 1.3071 0.8193 0.4599  0.0261  0.0210  922 GLN A NE2 
2327 N N   . LEU A 315 ? 1.4677 1.2218 0.7000 0.3799  -0.0668 -0.1137 923 LEU A N   
2328 C CA  . LEU A 315 ? 1.4655 1.2482 0.7183 0.3699  -0.0714 -0.1386 923 LEU A CA  
2329 C C   . LEU A 315 ? 1.4306 1.2985 0.7719 0.3596  -0.1110 -0.1732 923 LEU A C   
2330 O O   . LEU A 315 ? 1.4311 1.3276 0.7600 0.3784  -0.1368 -0.2028 923 LEU A O   
2331 C CB  . LEU A 315 ? 1.4590 1.2206 0.7487 0.3284  -0.0291 -0.1268 923 LEU A CB  
2332 C CG  . LEU A 315 ? 1.5276 1.2078 0.7332 0.3355  0.0159  -0.1014 923 LEU A CG  
2333 C CD1 . LEU A 315 ? 1.5192 1.1879 0.7860 0.2907  0.0561  -0.0888 923 LEU A CD1 
2334 C CD2 . LEU A 315 ? 1.5647 1.2221 0.6914 0.3628  0.0171  -0.1149 923 LEU A CD2 
2335 N N   . ILE A 316 ? 1.4031 1.3099 0.8309 0.3306  -0.1151 -0.1712 924 ILE A N   
2336 C CA  . ILE A 316 ? 1.3663 1.3493 0.8813 0.3173  -0.1461 -0.2025 924 ILE A CA  
2337 C C   . ILE A 316 ? 1.3904 1.4089 0.8894 0.3558  -0.1866 -0.2239 924 ILE A C   
2338 O O   . ILE A 316 ? 1.3552 1.4335 0.9031 0.3576  -0.2160 -0.2600 924 ILE A O   
2339 C CB  . ILE A 316 ? 1.3211 1.3292 0.9283 0.2730  -0.1333 -0.1929 924 ILE A CB  
2340 C CG1 . ILE A 316 ? 1.3372 1.3093 0.9554 0.2418  -0.0971 -0.1729 924 ILE A CG1 
2341 C CG2 . ILE A 316 ? 1.2710 1.3482 0.9646 0.2557  -0.1568 -0.2248 924 ILE A CG2 
2342 C CD1 . ILE A 316 ? 1.3285 1.3125 1.0156 0.2062  -0.0851 -0.1588 924 ILE A CD1 
2343 N N   . GLU A 317 ? 1.4485 1.4286 0.8781 0.3890  -0.1882 -0.2041 925 GLU A N   
2344 C CA  . GLU A 317 ? 1.4752 1.4824 0.8791 0.4336  -0.2276 -0.2229 925 GLU A CA  
2345 C C   . GLU A 317 ? 1.5148 1.5298 0.8640 0.4683  -0.2543 -0.2514 925 GLU A C   
2346 O O   . GLU A 317 ? 1.4825 1.5600 0.8650 0.4872  -0.2950 -0.2895 925 GLU A O   
2347 C CB  . GLU A 317 ? 1.5555 1.5006 0.8795 0.4648  -0.2177 -0.1904 925 GLU A CB  
2348 C CG  . GLU A 317 ? 1.6042 1.5845 0.9703 0.4748  -0.2374 -0.1945 925 GLU A CG  
2349 C CD  . GLU A 317 ? 1.7165 1.6360 1.0444 0.4774  -0.2108 -0.1570 925 GLU A CD  
2350 O OE1 . GLU A 317 ? 1.6965 1.6443 1.0672 0.4788  -0.2212 -0.1597 925 GLU A OE1 
2351 O OE2 . GLU A 317 ? 1.7969 1.6404 1.0556 0.4764  -0.1773 -0.1268 925 GLU A OE2 
2352 N N   . LYS A 318 ? 1.5796 1.5336 0.8497 0.4742  -0.2297 -0.2357 926 LYS A N   
2353 C CA  . LYS A 318 ? 1.6249 1.5759 0.8306 0.5055  -0.2489 -0.2600 926 LYS A CA  
2354 C C   . LYS A 318 ? 1.5923 1.6134 0.8871 0.4778  -0.2658 -0.3020 926 LYS A C   
2355 O O   . LYS A 318 ? 1.5857 1.6468 0.8717 0.5051  -0.3041 -0.3408 926 LYS A O   
2356 C CB  . LYS A 318 ? 1.7177 1.5822 0.8236 0.5107  -0.2078 -0.2303 926 LYS A CB  
2357 C CG  . LYS A 318 ? 1.8375 1.6792 0.8366 0.5599  -0.2287 -0.2474 926 LYS A CG  
2358 C CD  . LYS A 318 ? 1.9737 1.7284 0.8736 0.5625  -0.1820 -0.2195 926 LYS A CD  
2359 C CE  . LYS A 318 ? 2.0802 1.8161 0.8731 0.6107  -0.2043 -0.2403 926 LYS A CE  
2360 N NZ  . LYS A 318 ? 2.1946 1.8334 0.8692 0.6215  -0.1552 -0.2087 926 LYS A NZ  
2361 N N   . GLN A 319 ? 1.5733 1.6092 0.9552 0.4251  -0.2389 -0.2960 927 GLN A N   
2362 C CA  . GLN A 319 ? 1.5452 1.6390 1.0166 0.3948  -0.2489 -0.3319 927 GLN A CA  
2363 C C   . GLN A 319 ? 1.5112 1.6850 1.0726 0.3908  -0.2849 -0.3668 927 GLN A C   
2364 O O   . GLN A 319 ? 1.4796 1.7040 1.0984 0.3803  -0.3037 -0.4075 927 GLN A O   
2365 C CB  . GLN A 319 ? 1.5455 1.6241 1.0774 0.3436  -0.2090 -0.3113 927 GLN A CB  
2366 C CG  . GLN A 319 ? 1.6325 1.6433 1.0928 0.3437  -0.1724 -0.2870 927 GLN A CG  
2367 C CD  . GLN A 319 ? 1.6701 1.6812 1.2012 0.2977  -0.1427 -0.2809 927 GLN A CD  
2368 O OE1 . GLN A 319 ? 1.6491 1.7036 1.2530 0.2766  -0.1532 -0.3089 927 GLN A OE1 
2369 N NE2 . GLN A 319 ? 1.7068 1.6684 1.2201 0.2822  -0.1048 -0.2457 927 GLN A NE2 
2370 N N   . ILE A 320 ? 1.5148 1.6997 1.0931 0.3972  -0.2914 -0.3531 928 ILE A N   
2371 C CA  . ILE A 320 ? 1.4830 1.7435 1.1481 0.3938  -0.3210 -0.3861 928 ILE A CA  
2372 C C   . ILE A 320 ? 1.5115 1.8071 1.1394 0.4453  -0.3690 -0.4246 928 ILE A C   
2373 O O   . ILE A 320 ? 1.4664 1.8325 1.1677 0.4413  -0.3974 -0.4719 928 ILE A O   
2374 C CB  . ILE A 320 ? 1.4760 1.7357 1.1759 0.3796  -0.3068 -0.3584 928 ILE A CB  
2375 C CG1 . ILE A 320 ? 1.4661 1.7135 1.2281 0.3248  -0.2688 -0.3348 928 ILE A CG1 
2376 C CG2 . ILE A 320 ? 1.4367 1.7689 1.2043 0.3905  -0.3387 -0.3919 928 ILE A CG2 
2377 C CD1 . ILE A 320 ? 1.4768 1.7079 1.2528 0.3108  -0.2498 -0.3028 928 ILE A CD1 
2378 N N   . SER A 321 ? 1.5847 1.8287 1.0968 0.4943  -0.3778 -0.4060 929 SER A N   
2379 C CA  . SER A 321 ? 1.6158 1.8841 1.0740 0.5516  -0.4266 -0.4394 929 SER A CA  
2380 C C   . SER A 321 ? 1.6435 1.9261 1.0819 0.5584  -0.4433 -0.4762 929 SER A C   
2381 O O   . SER A 321 ? 1.6215 1.9643 1.0793 0.5856  -0.4897 -0.5258 929 SER A O   
2382 C CB  . SER A 321 ? 1.6929 1.8894 1.0234 0.6031  -0.4270 -0.4035 929 SER A CB  
2383 O OG  . SER A 321 ? 1.7744 1.8847 1.0105 0.6006  -0.3885 -0.3663 929 SER A OG  
2384 N N   . GLU A 322 ? 1.6863 1.9188 1.0946 0.5321  -0.4058 -0.4563 930 GLU A N   
2385 C CA  . GLU A 322 ? 1.7095 1.9535 1.1050 0.5330  -0.4160 -0.4916 930 GLU A CA  
2386 C C   . GLU A 322 ? 1.6580 1.9746 1.1923 0.4846  -0.4195 -0.5317 930 GLU A C   
2387 O O   . GLU A 322 ? 1.6571 1.9716 1.2041 0.4646  -0.4087 -0.5497 930 GLU A O   
2388 C CB  . GLU A 322 ? 1.7974 1.9596 1.1113 0.5236  -0.3708 -0.4563 930 GLU A CB  
2389 C CG  . GLU A 322 ? 1.9356 2.0191 1.0993 0.5735  -0.3646 -0.4240 930 GLU A CG  
2390 C CD  . GLU A 322 ? 2.0593 2.0645 1.1459 0.5631  -0.3160 -0.3942 930 GLU A CD  
2391 O OE1 . GLU A 322 ? 2.0476 2.0590 1.2037 0.5150  -0.2852 -0.3942 930 GLU A OE1 
2392 O OE2 . GLU A 322 ? 2.1453 2.0810 1.1013 0.6041  -0.3073 -0.3710 930 GLU A OE2 
2393 N N   . SER A 323 ? 1.6152 1.9914 1.2514 0.4660  -0.4314 -0.5450 931 SER A N   
2394 C CA  . SER A 323 ? 1.5656 2.0062 1.3353 0.4199  -0.4308 -0.5795 931 SER A CA  
2395 C C   . SER A 323 ? 1.5265 2.0477 1.3663 0.4361  -0.4719 -0.6219 931 SER A C   
2396 O O   . SER A 323 ? 1.4821 2.0682 1.3962 0.4284  -0.4971 -0.6775 931 SER A O   
2397 C CB  . SER A 323 ? 1.5760 1.9918 1.4042 0.3678  -0.3840 -0.5381 931 SER A CB  
2398 O OG  . SER A 323 ? 1.5498 2.0228 1.5028 0.3265  -0.3814 -0.5646 931 SER A OG  
2399 N N   . THR A 324 ? 1.5384 2.0559 1.3565 0.4596  -0.4784 -0.5986 932 THR A N   
2400 C CA  . THR A 324 ? 1.5015 2.0942 1.3846 0.4788  -0.5155 -0.6363 932 THR A CA  
2401 C C   . THR A 324 ? 1.5303 2.1335 1.3292 0.5481  -0.5674 -0.6618 932 THR A C   
2402 O O   . THR A 324 ? 1.5418 2.1521 1.3027 0.5684  -0.5923 -0.6947 932 THR A O   
2403 C CB  . THR A 324 ? 1.5162 2.1020 1.4305 0.4650  -0.4928 -0.5999 932 THR A CB  
2404 O OG1 . THR A 324 ? 1.5945 2.1103 1.3931 0.5026  -0.4875 -0.5531 932 THR A OG1 
2405 C CG2 . THR A 324 ? 1.5029 2.0723 1.4869 0.4011  -0.4434 -0.5721 932 THR A CG2 
# 
