data_9HDM
# 
_entry.id   9HDM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9HDM         pdb_00009hdm 10.2210/pdb9hdm/pdb 
WWPDB D_1292140682 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HDM 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-12 
_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              nico.fessner@pharmazie.uni-freiburg.de 
_pdbx_contact_author.name_first         'Nico D.' 
_pdbx_contact_author.name_last          Fessner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8247-1356 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Friedrich, F.' 1 0000-0001-5420-6184 
'Genz, F.'      2 0009-0002-4868-2752 
'Einsle, O.'    3 0000-0001-8722-2893 
'Mueller, M.'   4 0000-0002-2742-4992 
'Fessner, N.D.' 5 0000-0001-8247-1356 
# 
_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            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Identification and Characterization of Pyrimidine Nucleoside 2'-Hydroxylase
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c07764 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Genz, F.'      1 ? 
primary 'Friedrich, F.' 2 ? 
primary 'Lonarz, C.'    3 ? 
primary 'Einsle, O.'    4 ? 
primary 'Jung, M.'      5 ? 
primary 'Muller, M.'    6 ? 
primary 'Fessner, N.D.' 7 ? 
# 
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 'Clavaminate synthase-like protein' 42508.672 2   ? ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION'                54.938    2   ? ? ? ? 
3 non-polymer syn THYMIDINE                           242.229   2   ? ? ? ? 
4 non-polymer nat 1,2-ETHANEDIOL                      62.068    1   ? ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                      35.453    1   ? ? ? ? 
6 non-polymer syn '(R,R)-2,3-BUTANEDIOL'              90.121    1   ? ? ? ? 
7 water       nat water                               18.015    654 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMAPIAQAVTVSLNDLKNGTVSLEALEEAFGPDSLGILVVKDVPAEFAELRHRLLSYSSYL
GNLPKSELDRLENEKAKYLTGWSLGKETLKNGQVDNLKGSYYANCAFYVDPSLSCAKPTEEFNPDNFPEYLSPNLWPQES
TLPGFKPTFEDLCRLIIDVAVLVARACDRFAEKQIAGYPAGYLEGVVKTSTTTKARLLHYFPEEATATDASKESNKEEEG
DEDDWCATHLDHGCLTGLTSAMFVDEAATPPVVNPSVNGSLPPLGELPTSPDPKAGLYIKSRTGQTVQVKIPRDCIAFQT
GEALERITGGKFKAVPHFVRGARAEMSAGRIARNTLAVFTQPNLGDEVDMEQHITFGEFARGIVAKNTVS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMAPIAQAVTVSLNDLKNGTVSLEALEEAFGPDSLGILVVKDVPAEFAELRHRLLSYSSYL
GNLPKSELDRLENEKAKYLTGWSLGKETLKNGQVDNLKGSYYANCAFYVDPSLSCAKPTEEFNPDNFPEYLSPNLWPQES
TLPGFKPTFEDLCRLIIDVAVLVARACDRFAEKQIAGYPAGYLEGVVKTSTTTKARLLHYFPEEATATDASKESNKEEEG
DEDDWCATHLDHGCLTGLTSAMFVDEAATPPVVNPSVNGSLPPLGELPTSPDPKAGLYIKSRTGQTVQVKIPRDCIAFQT
GEALERITGGKFKAVPHFVRGARAEMSAGRIARNTLAVFTQPNLGDEVDMEQHITFGEFARGIVAKNTVS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION'   MN  
3 THYMIDINE              THM 
4 1,2-ETHANEDIOL         EDO 
5 'CHLORIDE ION'         CL  
6 '(R,R)-2,3-BUTANEDIOL' BU3 
7 water                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ALA n 
1 23  PRO n 
1 24  ILE n 
1 25  ALA n 
1 26  GLN n 
1 27  ALA n 
1 28  VAL n 
1 29  THR n 
1 30  VAL n 
1 31  SER n 
1 32  LEU n 
1 33  ASN n 
1 34  ASP n 
1 35  LEU n 
1 36  LYS n 
1 37  ASN n 
1 38  GLY n 
1 39  THR n 
1 40  VAL n 
1 41  SER n 
1 42  LEU n 
1 43  GLU n 
1 44  ALA n 
1 45  LEU n 
1 46  GLU n 
1 47  GLU n 
1 48  ALA n 
1 49  PHE n 
1 50  GLY n 
1 51  PRO n 
1 52  ASP n 
1 53  SER n 
1 54  LEU n 
1 55  GLY n 
1 56  ILE n 
1 57  LEU n 
1 58  VAL n 
1 59  VAL n 
1 60  LYS n 
1 61  ASP n 
1 62  VAL n 
1 63  PRO n 
1 64  ALA n 
1 65  GLU n 
1 66  PHE n 
1 67  ALA n 
1 68  GLU n 
1 69  LEU n 
1 70  ARG n 
1 71  HIS n 
1 72  ARG n 
1 73  LEU n 
1 74  LEU n 
1 75  SER n 
1 76  TYR n 
1 77  SER n 
1 78  SER n 
1 79  TYR n 
1 80  LEU n 
1 81  GLY n 
1 82  ASN n 
1 83  LEU n 
1 84  PRO n 
1 85  LYS n 
1 86  SER n 
1 87  GLU n 
1 88  LEU n 
1 89  ASP n 
1 90  ARG n 
1 91  LEU n 
1 92  GLU n 
1 93  ASN n 
1 94  GLU n 
1 95  LYS n 
1 96  ALA n 
1 97  LYS n 
1 98  TYR n 
1 99  LEU n 
1 100 THR n 
1 101 GLY n 
1 102 TRP n 
1 103 SER n 
1 104 LEU n 
1 105 GLY n 
1 106 LYS n 
1 107 GLU n 
1 108 THR n 
1 109 LEU n 
1 110 LYS n 
1 111 ASN n 
1 112 GLY n 
1 113 GLN n 
1 114 VAL n 
1 115 ASP n 
1 116 ASN n 
1 117 LEU n 
1 118 LYS n 
1 119 GLY n 
1 120 SER n 
1 121 TYR n 
1 122 TYR n 
1 123 ALA n 
1 124 ASN n 
1 125 CYS n 
1 126 ALA n 
1 127 PHE n 
1 128 TYR n 
1 129 VAL n 
1 130 ASP n 
1 131 PRO n 
1 132 SER n 
1 133 LEU n 
1 134 SER n 
1 135 CYS n 
1 136 ALA n 
1 137 LYS n 
1 138 PRO n 
1 139 THR n 
1 140 GLU n 
1 141 GLU n 
1 142 PHE n 
1 143 ASN n 
1 144 PRO n 
1 145 ASP n 
1 146 ASN n 
1 147 PHE n 
1 148 PRO n 
1 149 GLU n 
1 150 TYR n 
1 151 LEU n 
1 152 SER n 
1 153 PRO n 
1 154 ASN n 
1 155 LEU n 
1 156 TRP n 
1 157 PRO n 
1 158 GLN n 
1 159 GLU n 
1 160 SER n 
1 161 THR n 
1 162 LEU n 
1 163 PRO n 
1 164 GLY n 
1 165 PHE n 
1 166 LYS n 
1 167 PRO n 
1 168 THR n 
1 169 PHE n 
1 170 GLU n 
1 171 ASP n 
1 172 LEU n 
1 173 CYS n 
1 174 ARG n 
1 175 LEU n 
1 176 ILE n 
1 177 ILE n 
1 178 ASP n 
1 179 VAL n 
1 180 ALA n 
1 181 VAL n 
1 182 LEU n 
1 183 VAL n 
1 184 ALA n 
1 185 ARG n 
1 186 ALA n 
1 187 CYS n 
1 188 ASP n 
1 189 ARG n 
1 190 PHE n 
1 191 ALA n 
1 192 GLU n 
1 193 LYS n 
1 194 GLN n 
1 195 ILE n 
1 196 ALA n 
1 197 GLY n 
1 198 TYR n 
1 199 PRO n 
1 200 ALA n 
1 201 GLY n 
1 202 TYR n 
1 203 LEU n 
1 204 GLU n 
1 205 GLY n 
1 206 VAL n 
1 207 VAL n 
1 208 LYS n 
1 209 THR n 
1 210 SER n 
1 211 THR n 
1 212 THR n 
1 213 THR n 
1 214 LYS n 
1 215 ALA n 
1 216 ARG n 
1 217 LEU n 
1 218 LEU n 
1 219 HIS n 
1 220 TYR n 
1 221 PHE n 
1 222 PRO n 
1 223 GLU n 
1 224 GLU n 
1 225 ALA n 
1 226 THR n 
1 227 ALA n 
1 228 THR n 
1 229 ASP n 
1 230 ALA n 
1 231 SER n 
1 232 LYS n 
1 233 GLU n 
1 234 SER n 
1 235 ASN n 
1 236 LYS n 
1 237 GLU n 
1 238 GLU n 
1 239 GLU n 
1 240 GLY n 
1 241 ASP n 
1 242 GLU n 
1 243 ASP n 
1 244 ASP n 
1 245 TRP n 
1 246 CYS n 
1 247 ALA n 
1 248 THR n 
1 249 HIS n 
1 250 LEU n 
1 251 ASP n 
1 252 HIS n 
1 253 GLY n 
1 254 CYS n 
1 255 LEU n 
1 256 THR n 
1 257 GLY n 
1 258 LEU n 
1 259 THR n 
1 260 SER n 
1 261 ALA n 
1 262 MET n 
1 263 PHE n 
1 264 VAL n 
1 265 ASP n 
1 266 GLU n 
1 267 ALA n 
1 268 ALA n 
1 269 THR n 
1 270 PRO n 
1 271 PRO n 
1 272 VAL n 
1 273 VAL n 
1 274 ASN n 
1 275 PRO n 
1 276 SER n 
1 277 VAL n 
1 278 ASN n 
1 279 GLY n 
1 280 SER n 
1 281 LEU n 
1 282 PRO n 
1 283 PRO n 
1 284 LEU n 
1 285 GLY n 
1 286 GLU n 
1 287 LEU n 
1 288 PRO n 
1 289 THR n 
1 290 SER n 
1 291 PRO n 
1 292 ASP n 
1 293 PRO n 
1 294 LYS n 
1 295 ALA n 
1 296 GLY n 
1 297 LEU n 
1 298 TYR n 
1 299 ILE n 
1 300 LYS n 
1 301 SER n 
1 302 ARG n 
1 303 THR n 
1 304 GLY n 
1 305 GLN n 
1 306 THR n 
1 307 VAL n 
1 308 GLN n 
1 309 VAL n 
1 310 LYS n 
1 311 ILE n 
1 312 PRO n 
1 313 ARG n 
1 314 ASP n 
1 315 CYS n 
1 316 ILE n 
1 317 ALA n 
1 318 PHE n 
1 319 GLN n 
1 320 THR n 
1 321 GLY n 
1 322 GLU n 
1 323 ALA n 
1 324 LEU n 
1 325 GLU n 
1 326 ARG n 
1 327 ILE n 
1 328 THR n 
1 329 GLY n 
1 330 GLY n 
1 331 LYS n 
1 332 PHE n 
1 333 LYS n 
1 334 ALA n 
1 335 VAL n 
1 336 PRO n 
1 337 HIS n 
1 338 PHE n 
1 339 VAL n 
1 340 ARG n 
1 341 GLY n 
1 342 ALA n 
1 343 ARG n 
1 344 ALA n 
1 345 GLU n 
1 346 MET n 
1 347 SER n 
1 348 ALA n 
1 349 GLY n 
1 350 ARG n 
1 351 ILE n 
1 352 ALA n 
1 353 ARG n 
1 354 ASN n 
1 355 THR n 
1 356 LEU n 
1 357 ALA n 
1 358 VAL n 
1 359 PHE n 
1 360 THR n 
1 361 GLN n 
1 362 PRO n 
1 363 ASN n 
1 364 LEU n 
1 365 GLY n 
1 366 ASP n 
1 367 GLU n 
1 368 VAL n 
1 369 ASP n 
1 370 MET n 
1 371 GLU n 
1 372 GLN n 
1 373 HIS n 
1 374 ILE n 
1 375 THR n 
1 376 PHE n 
1 377 GLY n 
1 378 GLU n 
1 379 PHE n 
1 380 ALA n 
1 381 ARG n 
1 382 GLY n 
1 383 ILE n 
1 384 VAL n 
1 385 ALA n 
1 386 LYS n 
1 387 ASN n 
1 388 THR n 
1 389 VAL n 
1 390 SER 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                   390 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 NCU02560 
_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      'Neurospora crassa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5141 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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 
BU3 non-polymer               . '(R,R)-2,3-BUTANEDIOL' ?                                   'C4 H10 O2'      90.121  
CL  non-polymer               . 'CHLORIDE ION'         ?                                   'Cl -1'          35.453  
CYS 'L-peptide linking'       y CYSTEINE               ?                                   'C3 H7 N O2 S'   121.158 
EDO non-polymer               . 1,2-ETHANEDIOL         'ETHYLENE GLYCOL'                   'C2 H6 O2'       62.068  
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 
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 
MN  non-polymer               . 'MANGANESE (II) ION'   ?                                   'Mn 2'           54.938  
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 
THM 'DNA OH 5 prime terminus' . THYMIDINE              
;DEOXYTHYMIDINE; 2'-DEOXYTHYMIDINE
;
'C10 H14 N2 O5'  242.229 
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   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  -7  GLY GLY A . n 
A 1 14  LEU 14  -6  -6  LEU LEU A . n 
A 1 15  VAL 15  -5  -5  VAL VAL A . n 
A 1 16  PRO 16  -4  -4  PRO PRO A . n 
A 1 17  ARG 17  -3  -3  ARG ARG A . n 
A 1 18  GLY 18  -2  -2  GLY GLY A . n 
A 1 19  SER 19  -1  -1  SER SER A . n 
A 1 20  HIS 20  0   0   HIS HIS A . n 
A 1 21  MET 21  1   1   MET MET A . n 
A 1 22  ALA 22  2   2   ALA ALA A . n 
A 1 23  PRO 23  3   3   PRO PRO A . n 
A 1 24  ILE 24  4   4   ILE ILE A . n 
A 1 25  ALA 25  5   5   ALA ALA A . n 
A 1 26  GLN 26  6   6   GLN GLN A . n 
A 1 27  ALA 27  7   7   ALA ALA A . n 
A 1 28  VAL 28  8   8   VAL VAL A . n 
A 1 29  THR 29  9   9   THR THR A . n 
A 1 30  VAL 30  10  10  VAL VAL A . n 
A 1 31  SER 31  11  11  SER SER A . n 
A 1 32  LEU 32  12  12  LEU LEU A . n 
A 1 33  ASN 33  13  13  ASN ASN A . n 
A 1 34  ASP 34  14  14  ASP ASP A . n 
A 1 35  LEU 35  15  15  LEU LEU A . n 
A 1 36  LYS 36  16  16  LYS LYS A . n 
A 1 37  ASN 37  17  17  ASN ASN A . n 
A 1 38  GLY 38  18  18  GLY GLY A . n 
A 1 39  THR 39  19  19  THR THR A . n 
A 1 40  VAL 40  20  20  VAL VAL A . n 
A 1 41  SER 41  21  21  SER SER A . n 
A 1 42  LEU 42  22  22  LEU LEU A . n 
A 1 43  GLU 43  23  23  GLU GLU A . n 
A 1 44  ALA 44  24  24  ALA ALA A . n 
A 1 45  LEU 45  25  25  LEU LEU A . n 
A 1 46  GLU 46  26  26  GLU GLU A . n 
A 1 47  GLU 47  27  27  GLU GLU A . n 
A 1 48  ALA 48  28  28  ALA ALA A . n 
A 1 49  PHE 49  29  29  PHE PHE A . n 
A 1 50  GLY 50  30  30  GLY GLY A . n 
A 1 51  PRO 51  31  31  PRO PRO A . n 
A 1 52  ASP 52  32  32  ASP ASP A . n 
A 1 53  SER 53  33  33  SER SER A . n 
A 1 54  LEU 54  34  34  LEU LEU A . n 
A 1 55  GLY 55  35  35  GLY GLY A . n 
A 1 56  ILE 56  36  36  ILE ILE A . n 
A 1 57  LEU 57  37  37  LEU LEU A . n 
A 1 58  VAL 58  38  38  VAL VAL A . n 
A 1 59  VAL 59  39  39  VAL VAL A . n 
A 1 60  LYS 60  40  40  LYS LYS A . n 
A 1 61  ASP 61  41  41  ASP ASP A . n 
A 1 62  VAL 62  42  42  VAL VAL A . n 
A 1 63  PRO 63  43  43  PRO PRO A . n 
A 1 64  ALA 64  44  44  ALA ALA A . n 
A 1 65  GLU 65  45  45  GLU GLU A . n 
A 1 66  PHE 66  46  46  PHE PHE A . n 
A 1 67  ALA 67  47  47  ALA ALA A . n 
A 1 68  GLU 68  48  48  GLU GLU A . n 
A 1 69  LEU 69  49  49  LEU LEU A . n 
A 1 70  ARG 70  50  50  ARG ARG A . n 
A 1 71  HIS 71  51  51  HIS HIS A . n 
A 1 72  ARG 72  52  52  ARG ARG A . n 
A 1 73  LEU 73  53  53  LEU LEU A . n 
A 1 74  LEU 74  54  54  LEU LEU A . n 
A 1 75  SER 75  55  55  SER SER A . n 
A 1 76  TYR 76  56  56  TYR TYR A . n 
A 1 77  SER 77  57  57  SER SER A . n 
A 1 78  SER 78  58  58  SER SER A . n 
A 1 79  TYR 79  59  59  TYR TYR A . n 
A 1 80  LEU 80  60  60  LEU LEU A . n 
A 1 81  GLY 81  61  61  GLY GLY A . n 
A 1 82  ASN 82  62  62  ASN ASN A . n 
A 1 83  LEU 83  63  63  LEU LEU A . n 
A 1 84  PRO 84  64  64  PRO PRO A . n 
A 1 85  LYS 85  65  65  LYS LYS A . n 
A 1 86  SER 86  66  66  SER SER A . n 
A 1 87  GLU 87  67  67  GLU GLU A . n 
A 1 88  LEU 88  68  68  LEU LEU A . n 
A 1 89  ASP 89  69  69  ASP ASP A . n 
A 1 90  ARG 90  70  70  ARG ARG A . n 
A 1 91  LEU 91  71  71  LEU LEU A . n 
A 1 92  GLU 92  72  72  GLU GLU A . n 
A 1 93  ASN 93  73  73  ASN ASN A . n 
A 1 94  GLU 94  74  74  GLU GLU A . n 
A 1 95  LYS 95  75  75  LYS LYS A . n 
A 1 96  ALA 96  76  76  ALA ALA A . n 
A 1 97  LYS 97  77  77  LYS LYS A . n 
A 1 98  TYR 98  78  78  TYR TYR A . n 
A 1 99  LEU 99  79  79  LEU LEU A . n 
A 1 100 THR 100 80  80  THR THR A . n 
A 1 101 GLY 101 81  81  GLY GLY A . n 
A 1 102 TRP 102 82  82  TRP TRP A . n 
A 1 103 SER 103 83  83  SER SER A . n 
A 1 104 LEU 104 84  84  LEU LEU A . n 
A 1 105 GLY 105 85  85  GLY GLY A . n 
A 1 106 LYS 106 86  86  LYS LYS A . n 
A 1 107 GLU 107 87  87  GLU GLU A . n 
A 1 108 THR 108 88  88  THR THR A . n 
A 1 109 LEU 109 89  89  LEU LEU A . n 
A 1 110 LYS 110 90  ?   ?   ?   A . n 
A 1 111 ASN 111 91  ?   ?   ?   A . n 
A 1 112 GLY 112 92  ?   ?   ?   A . n 
A 1 113 GLN 113 93  ?   ?   ?   A . n 
A 1 114 VAL 114 94  ?   ?   ?   A . n 
A 1 115 ASP 115 95  95  ASP ASP A . n 
A 1 116 ASN 116 96  96  ASN ASN A . n 
A 1 117 LEU 117 97  97  LEU LEU A . n 
A 1 118 LYS 118 98  98  LYS LYS A . n 
A 1 119 GLY 119 99  99  GLY GLY A . n 
A 1 120 SER 120 100 100 SER SER A . n 
A 1 121 TYR 121 101 101 TYR TYR A . n 
A 1 122 TYR 122 102 102 TYR TYR A . n 
A 1 123 ALA 123 103 103 ALA ALA A . n 
A 1 124 ASN 124 104 104 ASN ASN A . n 
A 1 125 CYS 125 105 105 CYS CYS A . n 
A 1 126 ALA 126 106 106 ALA ALA A . n 
A 1 127 PHE 127 107 107 PHE PHE A . n 
A 1 128 TYR 128 108 108 TYR TYR A . n 
A 1 129 VAL 129 109 109 VAL VAL A . n 
A 1 130 ASP 130 110 110 ASP ASP A . n 
A 1 131 PRO 131 111 111 PRO PRO A . n 
A 1 132 SER 132 112 112 SER SER A . n 
A 1 133 LEU 133 113 113 LEU LEU A . n 
A 1 134 SER 134 114 114 SER SER A . n 
A 1 135 CYS 135 115 115 CYS CYS A . n 
A 1 136 ALA 136 116 116 ALA ALA A . n 
A 1 137 LYS 137 117 117 LYS LYS A . n 
A 1 138 PRO 138 118 118 PRO PRO A . n 
A 1 139 THR 139 119 119 THR THR A . n 
A 1 140 GLU 140 120 120 GLU GLU A . n 
A 1 141 GLU 141 121 121 GLU GLU A . n 
A 1 142 PHE 142 122 122 PHE PHE A . n 
A 1 143 ASN 143 123 123 ASN ASN A . n 
A 1 144 PRO 144 124 124 PRO PRO A . n 
A 1 145 ASP 145 125 125 ASP ASP A . n 
A 1 146 ASN 146 126 126 ASN ASN A . n 
A 1 147 PHE 147 127 127 PHE PHE A . n 
A 1 148 PRO 148 128 128 PRO PRO A . n 
A 1 149 GLU 149 129 129 GLU GLU A . n 
A 1 150 TYR 150 130 130 TYR TYR A . n 
A 1 151 LEU 151 131 131 LEU LEU A . n 
A 1 152 SER 152 132 132 SER SER A . n 
A 1 153 PRO 153 133 133 PRO PRO A . n 
A 1 154 ASN 154 134 134 ASN ASN A . n 
A 1 155 LEU 155 135 135 LEU LEU A . n 
A 1 156 TRP 156 136 136 TRP TRP A . n 
A 1 157 PRO 157 137 137 PRO PRO A . n 
A 1 158 GLN 158 138 138 GLN GLN A . n 
A 1 159 GLU 159 139 139 GLU GLU A . n 
A 1 160 SER 160 140 140 SER SER A . n 
A 1 161 THR 161 141 141 THR THR A . n 
A 1 162 LEU 162 142 142 LEU LEU A . n 
A 1 163 PRO 163 143 143 PRO PRO A . n 
A 1 164 GLY 164 144 144 GLY GLY A . n 
A 1 165 PHE 165 145 145 PHE PHE A . n 
A 1 166 LYS 166 146 146 LYS LYS A . n 
A 1 167 PRO 167 147 147 PRO PRO A . n 
A 1 168 THR 168 148 148 THR THR A . n 
A 1 169 PHE 169 149 149 PHE PHE A . n 
A 1 170 GLU 170 150 150 GLU GLU A . n 
A 1 171 ASP 171 151 151 ASP ASP A . n 
A 1 172 LEU 172 152 152 LEU LEU A . n 
A 1 173 CYS 173 153 153 CYS CYS A . n 
A 1 174 ARG 174 154 154 ARG ARG A . n 
A 1 175 LEU 175 155 155 LEU LEU A . n 
A 1 176 ILE 176 156 156 ILE ILE A . n 
A 1 177 ILE 177 157 157 ILE ILE A . n 
A 1 178 ASP 178 158 158 ASP ASP A . n 
A 1 179 VAL 179 159 159 VAL VAL A . n 
A 1 180 ALA 180 160 160 ALA ALA A . n 
A 1 181 VAL 181 161 161 VAL VAL A . n 
A 1 182 LEU 182 162 162 LEU LEU A . n 
A 1 183 VAL 183 163 163 VAL VAL A . n 
A 1 184 ALA 184 164 164 ALA ALA A . n 
A 1 185 ARG 185 165 165 ARG ARG A . n 
A 1 186 ALA 186 166 166 ALA ALA A . n 
A 1 187 CYS 187 167 167 CYS CYS A . n 
A 1 188 ASP 188 168 168 ASP ASP A . n 
A 1 189 ARG 189 169 169 ARG ARG A . n 
A 1 190 PHE 190 170 170 PHE PHE A . n 
A 1 191 ALA 191 171 171 ALA ALA A . n 
A 1 192 GLU 192 172 172 GLU GLU A . n 
A 1 193 LYS 193 173 173 LYS LYS A . n 
A 1 194 GLN 194 174 174 GLN GLN A . n 
A 1 195 ILE 195 175 175 ILE ILE A . n 
A 1 196 ALA 196 176 176 ALA ALA A . n 
A 1 197 GLY 197 177 177 GLY GLY A . n 
A 1 198 TYR 198 178 178 TYR TYR A . n 
A 1 199 PRO 199 179 179 PRO PRO A . n 
A 1 200 ALA 200 180 180 ALA ALA A . n 
A 1 201 GLY 201 181 181 GLY GLY A . n 
A 1 202 TYR 202 182 182 TYR TYR A . n 
A 1 203 LEU 203 183 183 LEU LEU A . n 
A 1 204 GLU 204 184 184 GLU GLU A . n 
A 1 205 GLY 205 185 185 GLY GLY A . n 
A 1 206 VAL 206 186 186 VAL VAL A . n 
A 1 207 VAL 207 187 187 VAL VAL A . n 
A 1 208 LYS 208 188 188 LYS LYS A . n 
A 1 209 THR 209 189 189 THR THR A . n 
A 1 210 SER 210 190 190 SER SER A . n 
A 1 211 THR 211 191 191 THR THR A . n 
A 1 212 THR 212 192 192 THR THR A . n 
A 1 213 THR 213 193 193 THR THR A . n 
A 1 214 LYS 214 194 194 LYS LYS A . n 
A 1 215 ALA 215 195 195 ALA ALA A . n 
A 1 216 ARG 216 196 196 ARG ARG A . n 
A 1 217 LEU 217 197 197 LEU LEU A . n 
A 1 218 LEU 218 198 198 LEU LEU A . n 
A 1 219 HIS 219 199 199 HIS HIS A . n 
A 1 220 TYR 220 200 200 TYR TYR A . n 
A 1 221 PHE 221 201 201 PHE PHE A . n 
A 1 222 PRO 222 202 202 PRO PRO A . n 
A 1 223 GLU 223 203 203 GLU GLU A . n 
A 1 224 GLU 224 204 204 GLU GLU A . n 
A 1 225 ALA 225 205 205 ALA ALA A . n 
A 1 226 THR 226 206 ?   ?   ?   A . n 
A 1 227 ALA 227 207 ?   ?   ?   A . n 
A 1 228 THR 228 208 ?   ?   ?   A . n 
A 1 229 ASP 229 209 ?   ?   ?   A . n 
A 1 230 ALA 230 210 ?   ?   ?   A . n 
A 1 231 SER 231 211 ?   ?   ?   A . n 
A 1 232 LYS 232 212 ?   ?   ?   A . n 
A 1 233 GLU 233 213 ?   ?   ?   A . n 
A 1 234 SER 234 214 ?   ?   ?   A . n 
A 1 235 ASN 235 215 ?   ?   ?   A . n 
A 1 236 LYS 236 216 ?   ?   ?   A . n 
A 1 237 GLU 237 217 ?   ?   ?   A . n 
A 1 238 GLU 238 218 ?   ?   ?   A . n 
A 1 239 GLU 239 219 ?   ?   ?   A . n 
A 1 240 GLY 240 220 ?   ?   ?   A . n 
A 1 241 ASP 241 221 ?   ?   ?   A . n 
A 1 242 GLU 242 222 ?   ?   ?   A . n 
A 1 243 ASP 243 223 ?   ?   ?   A . n 
A 1 244 ASP 244 224 ?   ?   ?   A . n 
A 1 245 TRP 245 225 ?   ?   ?   A . n 
A 1 246 CYS 246 226 226 CYS CYS A . n 
A 1 247 ALA 247 227 227 ALA ALA A . n 
A 1 248 THR 248 228 228 THR THR A . n 
A 1 249 HIS 249 229 229 HIS HIS A . n 
A 1 250 LEU 250 230 230 LEU LEU A . n 
A 1 251 ASP 251 231 231 ASP ASP A . n 
A 1 252 HIS 252 232 232 HIS HIS A . n 
A 1 253 GLY 253 233 233 GLY GLY A . n 
A 1 254 CYS 254 234 234 CYS CYS A . n 
A 1 255 LEU 255 235 235 LEU LEU A . n 
A 1 256 THR 256 236 236 THR THR A . n 
A 1 257 GLY 257 237 237 GLY GLY A . n 
A 1 258 LEU 258 238 238 LEU LEU A . n 
A 1 259 THR 259 239 239 THR THR A . n 
A 1 260 SER 260 240 240 SER SER A . n 
A 1 261 ALA 261 241 241 ALA ALA A . n 
A 1 262 MET 262 242 242 MET MET A . n 
A 1 263 PHE 263 243 243 PHE PHE A . n 
A 1 264 VAL 264 244 244 VAL VAL A . n 
A 1 265 ASP 265 245 245 ASP ASP A . n 
A 1 266 GLU 266 246 246 GLU GLU A . n 
A 1 267 ALA 267 247 247 ALA ALA A . n 
A 1 268 ALA 268 248 248 ALA ALA A . n 
A 1 269 THR 269 249 249 THR THR A . n 
A 1 270 PRO 270 250 250 PRO PRO A . n 
A 1 271 PRO 271 251 251 PRO PRO A . n 
A 1 272 VAL 272 252 252 VAL VAL A . n 
A 1 273 VAL 273 253 253 VAL VAL A . n 
A 1 274 ASN 274 254 254 ASN ASN A . n 
A 1 275 PRO 275 255 ?   ?   ?   A . n 
A 1 276 SER 276 256 ?   ?   ?   A . n 
A 1 277 VAL 277 257 ?   ?   ?   A . n 
A 1 278 ASN 278 258 ?   ?   ?   A . n 
A 1 279 GLY 279 259 259 GLY GLY A . n 
A 1 280 SER 280 260 260 SER SER A . n 
A 1 281 LEU 281 261 261 LEU LEU A . n 
A 1 282 PRO 282 262 262 PRO PRO A . n 
A 1 283 PRO 283 263 263 PRO PRO A . n 
A 1 284 LEU 284 264 264 LEU LEU A . n 
A 1 285 GLY 285 265 265 GLY GLY A . n 
A 1 286 GLU 286 266 266 GLU GLU A . n 
A 1 287 LEU 287 267 267 LEU LEU A . n 
A 1 288 PRO 288 268 268 PRO PRO A . n 
A 1 289 THR 289 269 269 THR THR A . n 
A 1 290 SER 290 270 270 SER SER A . n 
A 1 291 PRO 291 271 271 PRO PRO A . n 
A 1 292 ASP 292 272 272 ASP ASP A . n 
A 1 293 PRO 293 273 273 PRO PRO A . n 
A 1 294 LYS 294 274 274 LYS LYS A . n 
A 1 295 ALA 295 275 275 ALA ALA A . n 
A 1 296 GLY 296 276 276 GLY GLY A . n 
A 1 297 LEU 297 277 277 LEU LEU A . n 
A 1 298 TYR 298 278 278 TYR TYR A . n 
A 1 299 ILE 299 279 279 ILE ILE A . n 
A 1 300 LYS 300 280 280 LYS LYS A . n 
A 1 301 SER 301 281 281 SER SER A . n 
A 1 302 ARG 302 282 282 ARG ARG A . n 
A 1 303 THR 303 283 283 THR THR A . n 
A 1 304 GLY 304 284 284 GLY GLY A . n 
A 1 305 GLN 305 285 285 GLN GLN A . n 
A 1 306 THR 306 286 286 THR THR A . n 
A 1 307 VAL 307 287 287 VAL VAL A . n 
A 1 308 GLN 308 288 288 GLN GLN A . n 
A 1 309 VAL 309 289 289 VAL VAL A . n 
A 1 310 LYS 310 290 290 LYS LYS A . n 
A 1 311 ILE 311 291 291 ILE ILE A . n 
A 1 312 PRO 312 292 292 PRO PRO A . n 
A 1 313 ARG 313 293 293 ARG ARG A . n 
A 1 314 ASP 314 294 294 ASP ASP A . n 
A 1 315 CYS 315 295 295 CYS CYS A . n 
A 1 316 ILE 316 296 296 ILE ILE A . n 
A 1 317 ALA 317 297 297 ALA ALA A . n 
A 1 318 PHE 318 298 298 PHE PHE A . n 
A 1 319 GLN 319 299 299 GLN GLN A . n 
A 1 320 THR 320 300 300 THR THR A . n 
A 1 321 GLY 321 301 301 GLY GLY A . n 
A 1 322 GLU 322 302 302 GLU GLU A . n 
A 1 323 ALA 323 303 303 ALA ALA A . n 
A 1 324 LEU 324 304 304 LEU LEU A . n 
A 1 325 GLU 325 305 305 GLU GLU A . n 
A 1 326 ARG 326 306 306 ARG ARG A . n 
A 1 327 ILE 327 307 307 ILE ILE A . n 
A 1 328 THR 328 308 308 THR THR A . n 
A 1 329 GLY 329 309 309 GLY GLY A . n 
A 1 330 GLY 330 310 310 GLY GLY A . n 
A 1 331 LYS 331 311 311 LYS LYS A . n 
A 1 332 PHE 332 312 312 PHE PHE A . n 
A 1 333 LYS 333 313 313 LYS LYS A . n 
A 1 334 ALA 334 314 314 ALA ALA A . n 
A 1 335 VAL 335 315 315 VAL VAL A . n 
A 1 336 PRO 336 316 316 PRO PRO A . n 
A 1 337 HIS 337 317 317 HIS HIS A . n 
A 1 338 PHE 338 318 318 PHE PHE A . n 
A 1 339 VAL 339 319 319 VAL VAL A . n 
A 1 340 ARG 340 320 320 ARG ARG A . n 
A 1 341 GLY 341 321 321 GLY GLY A . n 
A 1 342 ALA 342 322 322 ALA ALA A . n 
A 1 343 ARG 343 323 323 ARG ARG A . n 
A 1 344 ALA 344 324 324 ALA ALA A . n 
A 1 345 GLU 345 325 325 GLU GLU A . n 
A 1 346 MET 346 326 326 MET MET A . n 
A 1 347 SER 347 327 327 SER SER A . n 
A 1 348 ALA 348 328 328 ALA ALA A . n 
A 1 349 GLY 349 329 329 GLY GLY A . n 
A 1 350 ARG 350 330 330 ARG ARG A . n 
A 1 351 ILE 351 331 331 ILE ILE A . n 
A 1 352 ALA 352 332 332 ALA ALA A . n 
A 1 353 ARG 353 333 333 ARG ARG A . n 
A 1 354 ASN 354 334 334 ASN ASN A . n 
A 1 355 THR 355 335 335 THR THR A . n 
A 1 356 LEU 356 336 336 LEU LEU A . n 
A 1 357 ALA 357 337 337 ALA ALA A . n 
A 1 358 VAL 358 338 338 VAL VAL A . n 
A 1 359 PHE 359 339 339 PHE PHE A . n 
A 1 360 THR 360 340 340 THR THR A . n 
A 1 361 GLN 361 341 341 GLN GLN A . n 
A 1 362 PRO 362 342 342 PRO PRO A . n 
A 1 363 ASN 363 343 343 ASN ASN A . n 
A 1 364 LEU 364 344 344 LEU LEU A . n 
A 1 365 GLY 365 345 345 GLY GLY A . n 
A 1 366 ASP 366 346 346 ASP ASP A . n 
A 1 367 GLU 367 347 347 GLU GLU A . n 
A 1 368 VAL 368 348 348 VAL VAL A . n 
A 1 369 ASP 369 349 349 ASP ASP A . n 
A 1 370 MET 370 350 350 MET MET A . n 
A 1 371 GLU 371 351 351 GLU GLU A . n 
A 1 372 GLN 372 352 352 GLN GLN A . n 
A 1 373 HIS 373 353 353 HIS HIS A . n 
A 1 374 ILE 374 354 354 ILE ILE A . n 
A 1 375 THR 375 355 355 THR THR A . n 
A 1 376 PHE 376 356 356 PHE PHE A . n 
A 1 377 GLY 377 357 357 GLY GLY A . n 
A 1 378 GLU 378 358 358 GLU GLU A . n 
A 1 379 PHE 379 359 359 PHE PHE A . n 
A 1 380 ALA 380 360 360 ALA ALA A . n 
A 1 381 ARG 381 361 361 ARG ARG A . n 
A 1 382 GLY 382 362 362 GLY GLY A . n 
A 1 383 ILE 383 363 363 ILE ILE A . n 
A 1 384 VAL 384 364 364 VAL VAL A . n 
A 1 385 ALA 385 365 365 ALA ALA A . n 
A 1 386 LYS 386 366 366 LYS LYS A . n 
A 1 387 ASN 387 367 367 ASN ASN A . n 
A 1 388 THR 388 368 ?   ?   ?   A . n 
A 1 389 VAL 389 369 ?   ?   ?   A . n 
A 1 390 SER 390 370 ?   ?   ?   A . n 
B 1 1   MET 1   -19 ?   ?   ?   B . n 
B 1 2   GLY 2   -18 ?   ?   ?   B . n 
B 1 3   SER 3   -17 ?   ?   ?   B . n 
B 1 4   SER 4   -16 ?   ?   ?   B . n 
B 1 5   HIS 5   -15 ?   ?   ?   B . n 
B 1 6   HIS 6   -14 ?   ?   ?   B . n 
B 1 7   HIS 7   -13 ?   ?   ?   B . n 
B 1 8   HIS 8   -12 ?   ?   ?   B . n 
B 1 9   HIS 9   -11 ?   ?   ?   B . n 
B 1 10  HIS 10  -10 ?   ?   ?   B . n 
B 1 11  SER 11  -9  ?   ?   ?   B . n 
B 1 12  SER 12  -8  ?   ?   ?   B . n 
B 1 13  GLY 13  -7  ?   ?   ?   B . n 
B 1 14  LEU 14  -6  ?   ?   ?   B . n 
B 1 15  VAL 15  -5  ?   ?   ?   B . n 
B 1 16  PRO 16  -4  ?   ?   ?   B . n 
B 1 17  ARG 17  -3  ?   ?   ?   B . n 
B 1 18  GLY 18  -2  ?   ?   ?   B . n 
B 1 19  SER 19  -1  ?   ?   ?   B . n 
B 1 20  HIS 20  0   ?   ?   ?   B . n 
B 1 21  MET 21  1   1   MET MET B . n 
B 1 22  ALA 22  2   2   ALA ALA B . n 
B 1 23  PRO 23  3   3   PRO PRO B . n 
B 1 24  ILE 24  4   4   ILE ILE B . n 
B 1 25  ALA 25  5   5   ALA ALA B . n 
B 1 26  GLN 26  6   6   GLN GLN B . n 
B 1 27  ALA 27  7   7   ALA ALA B . n 
B 1 28  VAL 28  8   8   VAL VAL B . n 
B 1 29  THR 29  9   9   THR THR B . n 
B 1 30  VAL 30  10  10  VAL VAL B . n 
B 1 31  SER 31  11  11  SER SER B . n 
B 1 32  LEU 32  12  12  LEU LEU B . n 
B 1 33  ASN 33  13  13  ASN ASN B . n 
B 1 34  ASP 34  14  14  ASP ASP B . n 
B 1 35  LEU 35  15  15  LEU LEU B . n 
B 1 36  LYS 36  16  16  LYS LYS B . n 
B 1 37  ASN 37  17  17  ASN ASN B . n 
B 1 38  GLY 38  18  18  GLY GLY B . n 
B 1 39  THR 39  19  19  THR THR B . n 
B 1 40  VAL 40  20  20  VAL VAL B . n 
B 1 41  SER 41  21  21  SER SER B . n 
B 1 42  LEU 42  22  22  LEU LEU B . n 
B 1 43  GLU 43  23  23  GLU GLU B . n 
B 1 44  ALA 44  24  24  ALA ALA B . n 
B 1 45  LEU 45  25  25  LEU LEU B . n 
B 1 46  GLU 46  26  26  GLU GLU B . n 
B 1 47  GLU 47  27  27  GLU GLU B . n 
B 1 48  ALA 48  28  28  ALA ALA B . n 
B 1 49  PHE 49  29  29  PHE PHE B . n 
B 1 50  GLY 50  30  30  GLY GLY B . n 
B 1 51  PRO 51  31  31  PRO PRO B . n 
B 1 52  ASP 52  32  32  ASP ASP B . n 
B 1 53  SER 53  33  33  SER SER B . n 
B 1 54  LEU 54  34  34  LEU LEU B . n 
B 1 55  GLY 55  35  35  GLY GLY B . n 
B 1 56  ILE 56  36  36  ILE ILE B . n 
B 1 57  LEU 57  37  37  LEU LEU B . n 
B 1 58  VAL 58  38  38  VAL VAL B . n 
B 1 59  VAL 59  39  39  VAL VAL B . n 
B 1 60  LYS 60  40  40  LYS LYS B . n 
B 1 61  ASP 61  41  41  ASP ASP B . n 
B 1 62  VAL 62  42  42  VAL VAL B . n 
B 1 63  PRO 63  43  43  PRO PRO B . n 
B 1 64  ALA 64  44  44  ALA ALA B . n 
B 1 65  GLU 65  45  45  GLU GLU B . n 
B 1 66  PHE 66  46  46  PHE PHE B . n 
B 1 67  ALA 67  47  47  ALA ALA B . n 
B 1 68  GLU 68  48  48  GLU GLU B . n 
B 1 69  LEU 69  49  49  LEU LEU B . n 
B 1 70  ARG 70  50  50  ARG ARG B . n 
B 1 71  HIS 71  51  51  HIS HIS B . n 
B 1 72  ARG 72  52  52  ARG ARG B . n 
B 1 73  LEU 73  53  53  LEU LEU B . n 
B 1 74  LEU 74  54  54  LEU LEU B . n 
B 1 75  SER 75  55  55  SER SER B . n 
B 1 76  TYR 76  56  56  TYR TYR B . n 
B 1 77  SER 77  57  57  SER SER B . n 
B 1 78  SER 78  58  58  SER SER B . n 
B 1 79  TYR 79  59  59  TYR TYR B . n 
B 1 80  LEU 80  60  60  LEU LEU B . n 
B 1 81  GLY 81  61  61  GLY GLY B . n 
B 1 82  ASN 82  62  62  ASN ASN B . n 
B 1 83  LEU 83  63  63  LEU LEU B . n 
B 1 84  PRO 84  64  64  PRO PRO B . n 
B 1 85  LYS 85  65  65  LYS LYS B . n 
B 1 86  SER 86  66  66  SER SER B . n 
B 1 87  GLU 87  67  67  GLU GLU B . n 
B 1 88  LEU 88  68  68  LEU LEU B . n 
B 1 89  ASP 89  69  69  ASP ASP B . n 
B 1 90  ARG 90  70  70  ARG ARG B . n 
B 1 91  LEU 91  71  71  LEU LEU B . n 
B 1 92  GLU 92  72  72  GLU GLU B . n 
B 1 93  ASN 93  73  73  ASN ASN B . n 
B 1 94  GLU 94  74  74  GLU GLU B . n 
B 1 95  LYS 95  75  75  LYS LYS B . n 
B 1 96  ALA 96  76  76  ALA ALA B . n 
B 1 97  LYS 97  77  77  LYS LYS B . n 
B 1 98  TYR 98  78  78  TYR TYR B . n 
B 1 99  LEU 99  79  79  LEU LEU B . n 
B 1 100 THR 100 80  80  THR THR B . n 
B 1 101 GLY 101 81  81  GLY GLY B . n 
B 1 102 TRP 102 82  82  TRP TRP B . n 
B 1 103 SER 103 83  83  SER SER B . n 
B 1 104 LEU 104 84  84  LEU LEU B . n 
B 1 105 GLY 105 85  85  GLY GLY B . n 
B 1 106 LYS 106 86  86  LYS LYS B . n 
B 1 107 GLU 107 87  87  GLU GLU B . n 
B 1 108 THR 108 88  88  THR THR B . n 
B 1 109 LEU 109 89  ?   ?   ?   B . n 
B 1 110 LYS 110 90  ?   ?   ?   B . n 
B 1 111 ASN 111 91  ?   ?   ?   B . n 
B 1 112 GLY 112 92  ?   ?   ?   B . n 
B 1 113 GLN 113 93  ?   ?   ?   B . n 
B 1 114 VAL 114 94  ?   ?   ?   B . n 
B 1 115 ASP 115 95  ?   ?   ?   B . n 
B 1 116 ASN 116 96  96  ASN ASN B . n 
B 1 117 LEU 117 97  97  LEU LEU B . n 
B 1 118 LYS 118 98  98  LYS LYS B . n 
B 1 119 GLY 119 99  99  GLY GLY B . n 
B 1 120 SER 120 100 100 SER SER B . n 
B 1 121 TYR 121 101 101 TYR TYR B . n 
B 1 122 TYR 122 102 102 TYR TYR B . n 
B 1 123 ALA 123 103 103 ALA ALA B . n 
B 1 124 ASN 124 104 104 ASN ASN B . n 
B 1 125 CYS 125 105 105 CYS CYS B . n 
B 1 126 ALA 126 106 106 ALA ALA B . n 
B 1 127 PHE 127 107 107 PHE PHE B . n 
B 1 128 TYR 128 108 108 TYR TYR B . n 
B 1 129 VAL 129 109 109 VAL VAL B . n 
B 1 130 ASP 130 110 110 ASP ASP B . n 
B 1 131 PRO 131 111 111 PRO PRO B . n 
B 1 132 SER 132 112 112 SER SER B . n 
B 1 133 LEU 133 113 113 LEU LEU B . n 
B 1 134 SER 134 114 114 SER SER B . n 
B 1 135 CYS 135 115 115 CYS CYS B . n 
B 1 136 ALA 136 116 116 ALA ALA B . n 
B 1 137 LYS 137 117 117 LYS LYS B . n 
B 1 138 PRO 138 118 118 PRO PRO B . n 
B 1 139 THR 139 119 119 THR THR B . n 
B 1 140 GLU 140 120 120 GLU GLU B . n 
B 1 141 GLU 141 121 121 GLU GLU B . n 
B 1 142 PHE 142 122 122 PHE PHE B . n 
B 1 143 ASN 143 123 123 ASN ASN B . n 
B 1 144 PRO 144 124 124 PRO PRO B . n 
B 1 145 ASP 145 125 125 ASP ASP B . n 
B 1 146 ASN 146 126 126 ASN ASN B . n 
B 1 147 PHE 147 127 127 PHE PHE B . n 
B 1 148 PRO 148 128 128 PRO PRO B . n 
B 1 149 GLU 149 129 129 GLU GLU B . n 
B 1 150 TYR 150 130 130 TYR TYR B . n 
B 1 151 LEU 151 131 131 LEU LEU B . n 
B 1 152 SER 152 132 132 SER SER B . n 
B 1 153 PRO 153 133 133 PRO PRO B . n 
B 1 154 ASN 154 134 134 ASN ASN B . n 
B 1 155 LEU 155 135 135 LEU LEU B . n 
B 1 156 TRP 156 136 136 TRP TRP B . n 
B 1 157 PRO 157 137 137 PRO PRO B . n 
B 1 158 GLN 158 138 138 GLN GLN B . n 
B 1 159 GLU 159 139 139 GLU GLU B . n 
B 1 160 SER 160 140 140 SER SER B . n 
B 1 161 THR 161 141 141 THR THR B . n 
B 1 162 LEU 162 142 142 LEU LEU B . n 
B 1 163 PRO 163 143 143 PRO PRO B . n 
B 1 164 GLY 164 144 144 GLY GLY B . n 
B 1 165 PHE 165 145 145 PHE PHE B . n 
B 1 166 LYS 166 146 146 LYS LYS B . n 
B 1 167 PRO 167 147 147 PRO PRO B . n 
B 1 168 THR 168 148 148 THR THR B . n 
B 1 169 PHE 169 149 149 PHE PHE B . n 
B 1 170 GLU 170 150 150 GLU GLU B . n 
B 1 171 ASP 171 151 151 ASP ASP B . n 
B 1 172 LEU 172 152 152 LEU LEU B . n 
B 1 173 CYS 173 153 153 CYS CYS B . n 
B 1 174 ARG 174 154 154 ARG ARG B . n 
B 1 175 LEU 175 155 155 LEU LEU B . n 
B 1 176 ILE 176 156 156 ILE ILE B . n 
B 1 177 ILE 177 157 157 ILE ILE B . n 
B 1 178 ASP 178 158 158 ASP ASP B . n 
B 1 179 VAL 179 159 159 VAL VAL B . n 
B 1 180 ALA 180 160 160 ALA ALA B . n 
B 1 181 VAL 181 161 161 VAL VAL B . n 
B 1 182 LEU 182 162 162 LEU LEU B . n 
B 1 183 VAL 183 163 163 VAL VAL B . n 
B 1 184 ALA 184 164 164 ALA ALA B . n 
B 1 185 ARG 185 165 165 ARG ARG B . n 
B 1 186 ALA 186 166 166 ALA ALA B . n 
B 1 187 CYS 187 167 167 CYS CYS B . n 
B 1 188 ASP 188 168 168 ASP ASP B . n 
B 1 189 ARG 189 169 169 ARG ARG B . n 
B 1 190 PHE 190 170 170 PHE PHE B . n 
B 1 191 ALA 191 171 171 ALA ALA B . n 
B 1 192 GLU 192 172 172 GLU GLU B . n 
B 1 193 LYS 193 173 173 LYS LYS B . n 
B 1 194 GLN 194 174 174 GLN GLN B . n 
B 1 195 ILE 195 175 175 ILE ILE B . n 
B 1 196 ALA 196 176 176 ALA ALA B . n 
B 1 197 GLY 197 177 177 GLY GLY B . n 
B 1 198 TYR 198 178 178 TYR TYR B . n 
B 1 199 PRO 199 179 179 PRO PRO B . n 
B 1 200 ALA 200 180 180 ALA ALA B . n 
B 1 201 GLY 201 181 181 GLY GLY B . n 
B 1 202 TYR 202 182 182 TYR TYR B . n 
B 1 203 LEU 203 183 183 LEU LEU B . n 
B 1 204 GLU 204 184 184 GLU GLU B . n 
B 1 205 GLY 205 185 185 GLY GLY B . n 
B 1 206 VAL 206 186 186 VAL VAL B . n 
B 1 207 VAL 207 187 187 VAL VAL B . n 
B 1 208 LYS 208 188 188 LYS LYS B . n 
B 1 209 THR 209 189 189 THR THR B . n 
B 1 210 SER 210 190 190 SER SER B . n 
B 1 211 THR 211 191 191 THR THR B . n 
B 1 212 THR 212 192 192 THR THR B . n 
B 1 213 THR 213 193 193 THR THR B . n 
B 1 214 LYS 214 194 194 LYS LYS B . n 
B 1 215 ALA 215 195 195 ALA ALA B . n 
B 1 216 ARG 216 196 196 ARG ARG B . n 
B 1 217 LEU 217 197 197 LEU LEU B . n 
B 1 218 LEU 218 198 198 LEU LEU B . n 
B 1 219 HIS 219 199 199 HIS HIS B . n 
B 1 220 TYR 220 200 200 TYR TYR B . n 
B 1 221 PHE 221 201 201 PHE PHE B . n 
B 1 222 PRO 222 202 202 PRO PRO B . n 
B 1 223 GLU 223 203 203 GLU GLU B . n 
B 1 224 GLU 224 204 ?   ?   ?   B . n 
B 1 225 ALA 225 205 ?   ?   ?   B . n 
B 1 226 THR 226 206 ?   ?   ?   B . n 
B 1 227 ALA 227 207 ?   ?   ?   B . n 
B 1 228 THR 228 208 ?   ?   ?   B . n 
B 1 229 ASP 229 209 ?   ?   ?   B . n 
B 1 230 ALA 230 210 ?   ?   ?   B . n 
B 1 231 SER 231 211 ?   ?   ?   B . n 
B 1 232 LYS 232 212 ?   ?   ?   B . n 
B 1 233 GLU 233 213 ?   ?   ?   B . n 
B 1 234 SER 234 214 ?   ?   ?   B . n 
B 1 235 ASN 235 215 ?   ?   ?   B . n 
B 1 236 LYS 236 216 ?   ?   ?   B . n 
B 1 237 GLU 237 217 ?   ?   ?   B . n 
B 1 238 GLU 238 218 ?   ?   ?   B . n 
B 1 239 GLU 239 219 ?   ?   ?   B . n 
B 1 240 GLY 240 220 ?   ?   ?   B . n 
B 1 241 ASP 241 221 ?   ?   ?   B . n 
B 1 242 GLU 242 222 ?   ?   ?   B . n 
B 1 243 ASP 243 223 ?   ?   ?   B . n 
B 1 244 ASP 244 224 ?   ?   ?   B . n 
B 1 245 TRP 245 225 ?   ?   ?   B . n 
B 1 246 CYS 246 226 226 CYS CYS B . n 
B 1 247 ALA 247 227 227 ALA ALA B . n 
B 1 248 THR 248 228 228 THR THR B . n 
B 1 249 HIS 249 229 229 HIS HIS B . n 
B 1 250 LEU 250 230 230 LEU LEU B . n 
B 1 251 ASP 251 231 231 ASP ASP B . n 
B 1 252 HIS 252 232 232 HIS HIS B . n 
B 1 253 GLY 253 233 233 GLY GLY B . n 
B 1 254 CYS 254 234 234 CYS CYS B . n 
B 1 255 LEU 255 235 235 LEU LEU B . n 
B 1 256 THR 256 236 236 THR THR B . n 
B 1 257 GLY 257 237 237 GLY GLY B . n 
B 1 258 LEU 258 238 238 LEU LEU B . n 
B 1 259 THR 259 239 239 THR THR B . n 
B 1 260 SER 260 240 240 SER SER B . n 
B 1 261 ALA 261 241 241 ALA ALA B . n 
B 1 262 MET 262 242 242 MET MET B . n 
B 1 263 PHE 263 243 243 PHE PHE B . n 
B 1 264 VAL 264 244 244 VAL VAL B . n 
B 1 265 ASP 265 245 245 ASP ASP B . n 
B 1 266 GLU 266 246 246 GLU GLU B . n 
B 1 267 ALA 267 247 247 ALA ALA B . n 
B 1 268 ALA 268 248 248 ALA ALA B . n 
B 1 269 THR 269 249 249 THR THR B . n 
B 1 270 PRO 270 250 250 PRO PRO B . n 
B 1 271 PRO 271 251 251 PRO PRO B . n 
B 1 272 VAL 272 252 252 VAL VAL B . n 
B 1 273 VAL 273 253 253 VAL VAL B . n 
B 1 274 ASN 274 254 254 ASN ASN B . n 
B 1 275 PRO 275 255 255 PRO PRO B . n 
B 1 276 SER 276 256 256 SER SER B . n 
B 1 277 VAL 277 257 257 VAL VAL B . n 
B 1 278 ASN 278 258 258 ASN ASN B . n 
B 1 279 GLY 279 259 259 GLY GLY B . n 
B 1 280 SER 280 260 260 SER SER B . n 
B 1 281 LEU 281 261 261 LEU LEU B . n 
B 1 282 PRO 282 262 262 PRO PRO B . n 
B 1 283 PRO 283 263 263 PRO PRO B . n 
B 1 284 LEU 284 264 264 LEU LEU B . n 
B 1 285 GLY 285 265 265 GLY GLY B . n 
B 1 286 GLU 286 266 266 GLU GLU B . n 
B 1 287 LEU 287 267 267 LEU LEU B . n 
B 1 288 PRO 288 268 268 PRO PRO B . n 
B 1 289 THR 289 269 269 THR THR B . n 
B 1 290 SER 290 270 270 SER SER B . n 
B 1 291 PRO 291 271 271 PRO PRO B . n 
B 1 292 ASP 292 272 272 ASP ASP B . n 
B 1 293 PRO 293 273 273 PRO PRO B . n 
B 1 294 LYS 294 274 274 LYS LYS B . n 
B 1 295 ALA 295 275 275 ALA ALA B . n 
B 1 296 GLY 296 276 276 GLY GLY B . n 
B 1 297 LEU 297 277 277 LEU LEU B . n 
B 1 298 TYR 298 278 278 TYR TYR B . n 
B 1 299 ILE 299 279 279 ILE ILE B . n 
B 1 300 LYS 300 280 280 LYS LYS B . n 
B 1 301 SER 301 281 281 SER SER B . n 
B 1 302 ARG 302 282 282 ARG ARG B . n 
B 1 303 THR 303 283 283 THR THR B . n 
B 1 304 GLY 304 284 284 GLY GLY B . n 
B 1 305 GLN 305 285 285 GLN GLN B . n 
B 1 306 THR 306 286 286 THR THR B . n 
B 1 307 VAL 307 287 287 VAL VAL B . n 
B 1 308 GLN 308 288 288 GLN GLN B . n 
B 1 309 VAL 309 289 289 VAL VAL B . n 
B 1 310 LYS 310 290 290 LYS LYS B . n 
B 1 311 ILE 311 291 291 ILE ILE B . n 
B 1 312 PRO 312 292 292 PRO PRO B . n 
B 1 313 ARG 313 293 293 ARG ARG B . n 
B 1 314 ASP 314 294 294 ASP ASP B . n 
B 1 315 CYS 315 295 295 CYS CYS B . n 
B 1 316 ILE 316 296 296 ILE ILE B . n 
B 1 317 ALA 317 297 297 ALA ALA B . n 
B 1 318 PHE 318 298 298 PHE PHE B . n 
B 1 319 GLN 319 299 299 GLN GLN B . n 
B 1 320 THR 320 300 300 THR THR B . n 
B 1 321 GLY 321 301 301 GLY GLY B . n 
B 1 322 GLU 322 302 302 GLU GLU B . n 
B 1 323 ALA 323 303 303 ALA ALA B . n 
B 1 324 LEU 324 304 304 LEU LEU B . n 
B 1 325 GLU 325 305 305 GLU GLU B . n 
B 1 326 ARG 326 306 306 ARG ARG B . n 
B 1 327 ILE 327 307 307 ILE ILE B . n 
B 1 328 THR 328 308 308 THR THR B . n 
B 1 329 GLY 329 309 309 GLY GLY B . n 
B 1 330 GLY 330 310 310 GLY GLY B . n 
B 1 331 LYS 331 311 311 LYS LYS B . n 
B 1 332 PHE 332 312 312 PHE PHE B . n 
B 1 333 LYS 333 313 313 LYS LYS B . n 
B 1 334 ALA 334 314 314 ALA ALA B . n 
B 1 335 VAL 335 315 315 VAL VAL B . n 
B 1 336 PRO 336 316 316 PRO PRO B . n 
B 1 337 HIS 337 317 317 HIS HIS B . n 
B 1 338 PHE 338 318 318 PHE PHE B . n 
B 1 339 VAL 339 319 319 VAL VAL B . n 
B 1 340 ARG 340 320 320 ARG ARG B . n 
B 1 341 GLY 341 321 321 GLY GLY B . n 
B 1 342 ALA 342 322 322 ALA ALA B . n 
B 1 343 ARG 343 323 323 ARG ARG B . n 
B 1 344 ALA 344 324 324 ALA ALA B . n 
B 1 345 GLU 345 325 325 GLU GLU B . n 
B 1 346 MET 346 326 326 MET MET B . n 
B 1 347 SER 347 327 327 SER SER B . n 
B 1 348 ALA 348 328 328 ALA ALA B . n 
B 1 349 GLY 349 329 329 GLY GLY B . n 
B 1 350 ARG 350 330 330 ARG ARG B . n 
B 1 351 ILE 351 331 331 ILE ILE B . n 
B 1 352 ALA 352 332 332 ALA ALA B . n 
B 1 353 ARG 353 333 333 ARG ARG B . n 
B 1 354 ASN 354 334 334 ASN ASN B . n 
B 1 355 THR 355 335 335 THR THR B . n 
B 1 356 LEU 356 336 336 LEU LEU B . n 
B 1 357 ALA 357 337 337 ALA ALA B . n 
B 1 358 VAL 358 338 338 VAL VAL B . n 
B 1 359 PHE 359 339 339 PHE PHE B . n 
B 1 360 THR 360 340 340 THR THR B . n 
B 1 361 GLN 361 341 341 GLN GLN B . n 
B 1 362 PRO 362 342 342 PRO PRO B . n 
B 1 363 ASN 363 343 343 ASN ASN B . n 
B 1 364 LEU 364 344 344 LEU LEU B . n 
B 1 365 GLY 365 345 345 GLY GLY B . n 
B 1 366 ASP 366 346 346 ASP ASP B . n 
B 1 367 GLU 367 347 347 GLU GLU B . n 
B 1 368 VAL 368 348 348 VAL VAL B . n 
B 1 369 ASP 369 349 349 ASP ASP B . n 
B 1 370 MET 370 350 350 MET MET B . n 
B 1 371 GLU 371 351 351 GLU GLU B . n 
B 1 372 GLN 372 352 352 GLN GLN B . n 
B 1 373 HIS 373 353 353 HIS HIS B . n 
B 1 374 ILE 374 354 354 ILE ILE B . n 
B 1 375 THR 375 355 355 THR THR B . n 
B 1 376 PHE 376 356 356 PHE PHE B . n 
B 1 377 GLY 377 357 357 GLY GLY B . n 
B 1 378 GLU 378 358 358 GLU GLU B . n 
B 1 379 PHE 379 359 359 PHE PHE B . n 
B 1 380 ALA 380 360 360 ALA ALA B . n 
B 1 381 ARG 381 361 361 ARG ARG B . n 
B 1 382 GLY 382 362 362 GLY GLY B . n 
B 1 383 ILE 383 363 363 ILE ILE B . n 
B 1 384 VAL 384 364 364 VAL VAL B . n 
B 1 385 ALA 385 365 365 ALA ALA B . n 
B 1 386 LYS 386 366 366 LYS LYS B . n 
B 1 387 ASN 387 367 367 ASN ASN B . n 
B 1 388 THR 388 368 368 THR THR B . n 
B 1 389 VAL 389 369 369 VAL VAL B . n 
B 1 390 SER 390 370 370 SER SER B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        THM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   THM 
_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        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 MN  1   401 2   MN  MN  A . 
D 3 THM 1   402 401 THM THY A . 
E 4 EDO 1   403 402 EDO EDO A . 
F 2 MN  1   401 1   MN  MN  B . 
G 5 CL  1   402 1   CL  CL  B . 
H 3 THM 1   403 401 THM THY B . 
I 6 BU3 1   404 402 BU3 BU3 B . 
J 7 HOH 1   501 201 HOH HOH A . 
J 7 HOH 2   502 575 HOH HOH A . 
J 7 HOH 3   503 719 HOH HOH A . 
J 7 HOH 4   504 355 HOH HOH A . 
J 7 HOH 5   505 641 HOH HOH A . 
J 7 HOH 6   506 715 HOH HOH A . 
J 7 HOH 7   507 354 HOH HOH A . 
J 7 HOH 8   508 704 HOH HOH A . 
J 7 HOH 9   509 306 HOH HOH A . 
J 7 HOH 10  510 498 HOH HOH A . 
J 7 HOH 11  511 384 HOH HOH A . 
J 7 HOH 12  512 434 HOH HOH A . 
J 7 HOH 13  513 506 HOH HOH A . 
J 7 HOH 14  514 148 HOH HOH A . 
J 7 HOH 15  515 309 HOH HOH A . 
J 7 HOH 16  516 175 HOH HOH A . 
J 7 HOH 17  517 429 HOH HOH A . 
J 7 HOH 18  518 442 HOH HOH A . 
J 7 HOH 19  519 526 HOH HOH A . 
J 7 HOH 20  520 710 HOH HOH A . 
J 7 HOH 21  521 711 HOH HOH A . 
J 7 HOH 22  522 338 HOH HOH A . 
J 7 HOH 23  523 642 HOH HOH A . 
J 7 HOH 24  524 193 HOH HOH A . 
J 7 HOH 25  525 29  HOH HOH A . 
J 7 HOH 26  526 314 HOH HOH A . 
J 7 HOH 27  527 370 HOH HOH A . 
J 7 HOH 28  528 278 HOH HOH A . 
J 7 HOH 29  529 570 HOH HOH A . 
J 7 HOH 30  530 231 HOH HOH A . 
J 7 HOH 31  531 283 HOH HOH A . 
J 7 HOH 32  532 216 HOH HOH A . 
J 7 HOH 33  533 439 HOH HOH A . 
J 7 HOH 34  534 234 HOH HOH A . 
J 7 HOH 35  535 123 HOH HOH A . 
J 7 HOH 36  536 271 HOH HOH A . 
J 7 HOH 37  537 502 HOH HOH A . 
J 7 HOH 38  538 724 HOH HOH A . 
J 7 HOH 39  539 647 HOH HOH A . 
J 7 HOH 40  540 594 HOH HOH A . 
J 7 HOH 41  541 76  HOH HOH A . 
J 7 HOH 42  542 713 HOH HOH A . 
J 7 HOH 43  543 645 HOH HOH A . 
J 7 HOH 44  544 103 HOH HOH A . 
J 7 HOH 45  545 160 HOH HOH A . 
J 7 HOH 46  546 98  HOH HOH A . 
J 7 HOH 47  547 589 HOH HOH A . 
J 7 HOH 48  548 694 HOH HOH A . 
J 7 HOH 49  549 366 HOH HOH A . 
J 7 HOH 50  550 244 HOH HOH A . 
J 7 HOH 51  551 344 HOH HOH A . 
J 7 HOH 52  552 182 HOH HOH A . 
J 7 HOH 53  553 53  HOH HOH A . 
J 7 HOH 54  554 391 HOH HOH A . 
J 7 HOH 55  555 507 HOH HOH A . 
J 7 HOH 56  556 503 HOH HOH A . 
J 7 HOH 57  557 96  HOH HOH A . 
J 7 HOH 58  558 418 HOH HOH A . 
J 7 HOH 59  559 92  HOH HOH A . 
J 7 HOH 60  560 210 HOH HOH A . 
J 7 HOH 61  561 281 HOH HOH A . 
J 7 HOH 62  562 339 HOH HOH A . 
J 7 HOH 63  563 49  HOH HOH A . 
J 7 HOH 64  564 378 HOH HOH A . 
J 7 HOH 65  565 73  HOH HOH A . 
J 7 HOH 66  566 268 HOH HOH A . 
J 7 HOH 67  567 453 HOH HOH A . 
J 7 HOH 68  568 93  HOH HOH A . 
J 7 HOH 69  569 448 HOH HOH A . 
J 7 HOH 70  570 242 HOH HOH A . 
J 7 HOH 71  571 144 HOH HOH A . 
J 7 HOH 72  572 139 HOH HOH A . 
J 7 HOH 73  573 252 HOH HOH A . 
J 7 HOH 74  574 492 HOH HOH A . 
J 7 HOH 75  575 668 HOH HOH A . 
J 7 HOH 76  576 142 HOH HOH A . 
J 7 HOH 77  577 436 HOH HOH A . 
J 7 HOH 78  578 198 HOH HOH A . 
J 7 HOH 79  579 166 HOH HOH A . 
J 7 HOH 80  580 174 HOH HOH A . 
J 7 HOH 81  581 723 HOH HOH A . 
J 7 HOH 82  582 361 HOH HOH A . 
J 7 HOH 83  583 591 HOH HOH A . 
J 7 HOH 84  584 40  HOH HOH A . 
J 7 HOH 85  585 405 HOH HOH A . 
J 7 HOH 86  586 41  HOH HOH A . 
J 7 HOH 87  587 18  HOH HOH A . 
J 7 HOH 88  588 545 HOH HOH A . 
J 7 HOH 89  589 81  HOH HOH A . 
J 7 HOH 90  590 518 HOH HOH A . 
J 7 HOH 91  591 336 HOH HOH A . 
J 7 HOH 92  592 667 HOH HOH A . 
J 7 HOH 93  593 196 HOH HOH A . 
J 7 HOH 94  594 47  HOH HOH A . 
J 7 HOH 95  595 727 HOH HOH A . 
J 7 HOH 96  596 307 HOH HOH A . 
J 7 HOH 97  597 331 HOH HOH A . 
J 7 HOH 98  598 12  HOH HOH A . 
J 7 HOH 99  599 273 HOH HOH A . 
J 7 HOH 100 600 15  HOH HOH A . 
J 7 HOH 101 601 107 HOH HOH A . 
J 7 HOH 102 602 345 HOH HOH A . 
J 7 HOH 103 603 221 HOH HOH A . 
J 7 HOH 104 604 558 HOH HOH A . 
J 7 HOH 105 605 438 HOH HOH A . 
J 7 HOH 106 606 531 HOH HOH A . 
J 7 HOH 107 607 125 HOH HOH A . 
J 7 HOH 108 608 487 HOH HOH A . 
J 7 HOH 109 609 126 HOH HOH A . 
J 7 HOH 110 610 350 HOH HOH A . 
J 7 HOH 111 611 33  HOH HOH A . 
J 7 HOH 112 612 322 HOH HOH A . 
J 7 HOH 113 613 42  HOH HOH A . 
J 7 HOH 114 614 51  HOH HOH A . 
J 7 HOH 115 615 421 HOH HOH A . 
J 7 HOH 116 616 110 HOH HOH A . 
J 7 HOH 117 617 35  HOH HOH A . 
J 7 HOH 118 618 519 HOH HOH A . 
J 7 HOH 119 619 183 HOH HOH A . 
J 7 HOH 120 620 192 HOH HOH A . 
J 7 HOH 121 621 333 HOH HOH A . 
J 7 HOH 122 622 16  HOH HOH A . 
J 7 HOH 123 623 91  HOH HOH A . 
J 7 HOH 124 624 122 HOH HOH A . 
J 7 HOH 125 625 679 HOH HOH A . 
J 7 HOH 126 626 145 HOH HOH A . 
J 7 HOH 127 627 8   HOH HOH A . 
J 7 HOH 128 628 540 HOH HOH A . 
J 7 HOH 129 629 14  HOH HOH A . 
J 7 HOH 130 630 102 HOH HOH A . 
J 7 HOH 131 631 692 HOH HOH A . 
J 7 HOH 132 632 241 HOH HOH A . 
J 7 HOH 133 633 316 HOH HOH A . 
J 7 HOH 134 634 106 HOH HOH A . 
J 7 HOH 135 635 27  HOH HOH A . 
J 7 HOH 136 636 184 HOH HOH A . 
J 7 HOH 137 637 178 HOH HOH A . 
J 7 HOH 138 638 75  HOH HOH A . 
J 7 HOH 139 639 64  HOH HOH A . 
J 7 HOH 140 640 291 HOH HOH A . 
J 7 HOH 141 641 121 HOH HOH A . 
J 7 HOH 142 642 57  HOH HOH A . 
J 7 HOH 143 643 222 HOH HOH A . 
J 7 HOH 144 644 245 HOH HOH A . 
J 7 HOH 145 645 417 HOH HOH A . 
J 7 HOH 146 646 32  HOH HOH A . 
J 7 HOH 147 647 269 HOH HOH A . 
J 7 HOH 148 648 90  HOH HOH A . 
J 7 HOH 149 649 177 HOH HOH A . 
J 7 HOH 150 650 207 HOH HOH A . 
J 7 HOH 151 651 615 HOH HOH A . 
J 7 HOH 152 652 115 HOH HOH A . 
J 7 HOH 153 653 264 HOH HOH A . 
J 7 HOH 154 654 512 HOH HOH A . 
J 7 HOH 155 655 4   HOH HOH A . 
J 7 HOH 156 656 581 HOH HOH A . 
J 7 HOH 157 657 5   HOH HOH A . 
J 7 HOH 158 658 324 HOH HOH A . 
J 7 HOH 159 659 299 HOH HOH A . 
J 7 HOH 160 660 325 HOH HOH A . 
J 7 HOH 161 661 392 HOH HOH A . 
J 7 HOH 162 662 99  HOH HOH A . 
J 7 HOH 163 663 640 HOH HOH A . 
J 7 HOH 164 664 706 HOH HOH A . 
J 7 HOH 165 665 718 HOH HOH A . 
J 7 HOH 166 666 131 HOH HOH A . 
J 7 HOH 167 667 85  HOH HOH A . 
J 7 HOH 168 668 290 HOH HOH A . 
J 7 HOH 169 669 630 HOH HOH A . 
J 7 HOH 170 670 433 HOH HOH A . 
J 7 HOH 171 671 675 HOH HOH A . 
J 7 HOH 172 672 97  HOH HOH A . 
J 7 HOH 173 673 151 HOH HOH A . 
J 7 HOH 174 674 527 HOH HOH A . 
J 7 HOH 175 675 105 HOH HOH A . 
J 7 HOH 176 676 660 HOH HOH A . 
J 7 HOH 177 677 332 HOH HOH A . 
J 7 HOH 178 678 371 HOH HOH A . 
J 7 HOH 179 679 66  HOH HOH A . 
J 7 HOH 180 680 308 HOH HOH A . 
J 7 HOH 181 681 326 HOH HOH A . 
J 7 HOH 182 682 397 HOH HOH A . 
J 7 HOH 183 683 693 HOH HOH A . 
J 7 HOH 184 684 34  HOH HOH A . 
J 7 HOH 185 685 229 HOH HOH A . 
J 7 HOH 186 686 544 HOH HOH A . 
J 7 HOH 187 687 197 HOH HOH A . 
J 7 HOH 188 688 255 HOH HOH A . 
J 7 HOH 189 689 351 HOH HOH A . 
J 7 HOH 190 690 136 HOH HOH A . 
J 7 HOH 191 691 678 HOH HOH A . 
J 7 HOH 192 692 549 HOH HOH A . 
J 7 HOH 193 693 179 HOH HOH A . 
J 7 HOH 194 694 373 HOH HOH A . 
J 7 HOH 195 695 327 HOH HOH A . 
J 7 HOH 196 696 132 HOH HOH A . 
J 7 HOH 197 697 95  HOH HOH A . 
J 7 HOH 198 698 260 HOH HOH A . 
J 7 HOH 199 699 613 HOH HOH A . 
J 7 HOH 200 700 101 HOH HOH A . 
J 7 HOH 201 701 656 HOH HOH A . 
J 7 HOH 202 702 353 HOH HOH A . 
J 7 HOH 203 703 450 HOH HOH A . 
J 7 HOH 204 704 223 HOH HOH A . 
J 7 HOH 205 705 109 HOH HOH A . 
J 7 HOH 206 706 432 HOH HOH A . 
J 7 HOH 207 707 293 HOH HOH A . 
J 7 HOH 208 708 552 HOH HOH A . 
J 7 HOH 209 709 427 HOH HOH A . 
J 7 HOH 210 710 600 HOH HOH A . 
J 7 HOH 211 711 171 HOH HOH A . 
J 7 HOH 212 712 2   HOH HOH A . 
J 7 HOH 213 713 697 HOH HOH A . 
J 7 HOH 214 714 146 HOH HOH A . 
J 7 HOH 215 715 460 HOH HOH A . 
J 7 HOH 216 716 119 HOH HOH A . 
J 7 HOH 217 717 225 HOH HOH A . 
J 7 HOH 218 718 661 HOH HOH A . 
J 7 HOH 219 719 514 HOH HOH A . 
J 7 HOH 220 720 219 HOH HOH A . 
J 7 HOH 221 721 446 HOH HOH A . 
J 7 HOH 222 722 305 HOH HOH A . 
J 7 HOH 223 723 561 HOH HOH A . 
J 7 HOH 224 724 261 HOH HOH A . 
J 7 HOH 225 725 522 HOH HOH A . 
J 7 HOH 226 726 389 HOH HOH A . 
J 7 HOH 227 727 635 HOH HOH A . 
J 7 HOH 228 728 249 HOH HOH A . 
J 7 HOH 229 729 359 HOH HOH A . 
J 7 HOH 230 730 725 HOH HOH A . 
J 7 HOH 231 731 163 HOH HOH A . 
J 7 HOH 232 732 698 HOH HOH A . 
J 7 HOH 233 733 504 HOH HOH A . 
J 7 HOH 234 734 130 HOH HOH A . 
J 7 HOH 235 735 455 HOH HOH A . 
J 7 HOH 236 736 682 HOH HOH A . 
J 7 HOH 237 737 25  HOH HOH A . 
J 7 HOH 238 738 386 HOH HOH A . 
J 7 HOH 239 739 251 HOH HOH A . 
J 7 HOH 240 740 557 HOH HOH A . 
J 7 HOH 241 741 628 HOH HOH A . 
J 7 HOH 242 742 240 HOH HOH A . 
J 7 HOH 243 743 651 HOH HOH A . 
J 7 HOH 244 744 74  HOH HOH A . 
J 7 HOH 245 745 31  HOH HOH A . 
J 7 HOH 246 746 663 HOH HOH A . 
J 7 HOH 247 747 562 HOH HOH A . 
J 7 HOH 248 748 534 HOH HOH A . 
J 7 HOH 249 749 426 HOH HOH A . 
J 7 HOH 250 750 465 HOH HOH A . 
J 7 HOH 251 751 390 HOH HOH A . 
J 7 HOH 252 752 621 HOH HOH A . 
J 7 HOH 253 753 152 HOH HOH A . 
J 7 HOH 254 754 565 HOH HOH A . 
J 7 HOH 255 755 295 HOH HOH A . 
J 7 HOH 256 756 63  HOH HOH A . 
J 7 HOH 257 757 468 HOH HOH A . 
J 7 HOH 258 758 548 HOH HOH A . 
J 7 HOH 259 759 187 HOH HOH A . 
J 7 HOH 260 760 329 HOH HOH A . 
J 7 HOH 261 761 239 HOH HOH A . 
J 7 HOH 262 762 463 HOH HOH A . 
J 7 HOH 263 763 580 HOH HOH A . 
J 7 HOH 264 764 586 HOH HOH A . 
J 7 HOH 265 765 665 HOH HOH A . 
J 7 HOH 266 766 352 HOH HOH A . 
J 7 HOH 267 767 320 HOH HOH A . 
J 7 HOH 268 768 596 HOH HOH A . 
J 7 HOH 269 769 608 HOH HOH A . 
J 7 HOH 270 770 451 HOH HOH A . 
J 7 HOH 271 771 343 HOH HOH A . 
J 7 HOH 272 772 597 HOH HOH A . 
J 7 HOH 273 773 701 HOH HOH A . 
J 7 HOH 274 774 257 HOH HOH A . 
J 7 HOH 275 775 564 HOH HOH A . 
J 7 HOH 276 776 695 HOH HOH A . 
J 7 HOH 277 777 479 HOH HOH A . 
J 7 HOH 278 778 720 HOH HOH A . 
J 7 HOH 279 779 717 HOH HOH A . 
J 7 HOH 280 780 369 HOH HOH A . 
J 7 HOH 281 781 574 HOH HOH A . 
J 7 HOH 282 782 469 HOH HOH A . 
J 7 HOH 283 783 578 HOH HOH A . 
J 7 HOH 284 784 590 HOH HOH A . 
J 7 HOH 285 785 277 HOH HOH A . 
J 7 HOH 286 786 262 HOH HOH A . 
J 7 HOH 287 787 480 HOH HOH A . 
J 7 HOH 288 788 477 HOH HOH A . 
J 7 HOH 289 789 424 HOH HOH A . 
J 7 HOH 290 790 676 HOH HOH A . 
J 7 HOH 291 791 285 HOH HOH A . 
J 7 HOH 292 792 662 HOH HOH A . 
J 7 HOH 293 793 364 HOH HOH A . 
J 7 HOH 294 794 447 HOH HOH A . 
J 7 HOH 295 795 603 HOH HOH A . 
J 7 HOH 296 796 340 HOH HOH A . 
J 7 HOH 297 797 443 HOH HOH A . 
J 7 HOH 298 798 318 HOH HOH A . 
J 7 HOH 299 799 341 HOH HOH A . 
J 7 HOH 300 800 563 HOH HOH A . 
J 7 HOH 301 801 566 HOH HOH A . 
J 7 HOH 302 802 475 HOH HOH A . 
J 7 HOH 303 803 543 HOH HOH A . 
J 7 HOH 304 804 435 HOH HOH A . 
J 7 HOH 305 805 547 HOH HOH A . 
J 7 HOH 306 806 80  HOH HOH A . 
J 7 HOH 307 807 186 HOH HOH A . 
J 7 HOH 308 808 683 HOH HOH A . 
J 7 HOH 309 809 471 HOH HOH A . 
J 7 HOH 310 810 616 HOH HOH A . 
J 7 HOH 311 811 624 HOH HOH A . 
J 7 HOH 312 812 579 HOH HOH A . 
J 7 HOH 313 813 620 HOH HOH A . 
J 7 HOH 314 814 716 HOH HOH A . 
J 7 HOH 315 815 672 HOH HOH A . 
J 7 HOH 316 816 398 HOH HOH A . 
J 7 HOH 317 817 576 HOH HOH A . 
J 7 HOH 318 818 577 HOH HOH A . 
J 7 HOH 319 819 688 HOH HOH A . 
J 7 HOH 320 820 674 HOH HOH A . 
J 7 HOH 321 821 680 HOH HOH A . 
K 7 HOH 1   501 569 HOH HOH B . 
K 7 HOH 2   502 685 HOH HOH B . 
K 7 HOH 3   503 699 HOH HOH B . 
K 7 HOH 4   504 414 HOH HOH B . 
K 7 HOH 5   505 707 HOH HOH B . 
K 7 HOH 6   506 637 HOH HOH B . 
K 7 HOH 7   507 619 HOH HOH B . 
K 7 HOH 8   508 602 HOH HOH B . 
K 7 HOH 9   509 61  HOH HOH B . 
K 7 HOH 10  510 356 HOH HOH B . 
K 7 HOH 11  511 79  HOH HOH B . 
K 7 HOH 12  512 517 HOH HOH B . 
K 7 HOH 13  513 440 HOH HOH B . 
K 7 HOH 14  514 646 HOH HOH B . 
K 7 HOH 15  515 496 HOH HOH B . 
K 7 HOH 16  516 59  HOH HOH B . 
K 7 HOH 17  517 501 HOH HOH B . 
K 7 HOH 18  518 233 HOH HOH B . 
K 7 HOH 19  519 265 HOH HOH B . 
K 7 HOH 20  520 154 HOH HOH B . 
K 7 HOH 21  521 246 HOH HOH B . 
K 7 HOH 22  522 158 HOH HOH B . 
K 7 HOH 23  523 266 HOH HOH B . 
K 7 HOH 24  524 236 HOH HOH B . 
K 7 HOH 25  525 220 HOH HOH B . 
K 7 HOH 26  526 224 HOH HOH B . 
K 7 HOH 27  527 294 HOH HOH B . 
K 7 HOH 28  528 117 HOH HOH B . 
K 7 HOH 29  529 55  HOH HOH B . 
K 7 HOH 30  530 321 HOH HOH B . 
K 7 HOH 31  531 286 HOH HOH B . 
K 7 HOH 32  532 170 HOH HOH B . 
K 7 HOH 33  533 729 HOH HOH B . 
K 7 HOH 34  534 653 HOH HOH B . 
K 7 HOH 35  535 247 HOH HOH B . 
K 7 HOH 36  536 22  HOH HOH B . 
K 7 HOH 37  537 508 HOH HOH B . 
K 7 HOH 38  538 347 HOH HOH B . 
K 7 HOH 39  539 208 HOH HOH B . 
K 7 HOH 40  540 72  HOH HOH B . 
K 7 HOH 41  541 36  HOH HOH B . 
K 7 HOH 42  542 572 HOH HOH B . 
K 7 HOH 43  543 538 HOH HOH B . 
K 7 HOH 44  544 360 HOH HOH B . 
K 7 HOH 45  545 342 HOH HOH B . 
K 7 HOH 46  546 304 HOH HOH B . 
K 7 HOH 47  547 705 HOH HOH B . 
K 7 HOH 48  548 452 HOH HOH B . 
K 7 HOH 49  549 362 HOH HOH B . 
K 7 HOH 50  550 189 HOH HOH B . 
K 7 HOH 51  551 684 HOH HOH B . 
K 7 HOH 52  552 393 HOH HOH B . 
K 7 HOH 53  553 731 HOH HOH B . 
K 7 HOH 54  554 449 HOH HOH B . 
K 7 HOH 55  555 505 HOH HOH B . 
K 7 HOH 56  556 228 HOH HOH B . 
K 7 HOH 57  557 282 HOH HOH B . 
K 7 HOH 58  558 430 HOH HOH B . 
K 7 HOH 59  559 587 HOH HOH B . 
K 7 HOH 60  560 56  HOH HOH B . 
K 7 HOH 61  561 298 HOH HOH B . 
K 7 HOH 62  562 703 HOH HOH B . 
K 7 HOH 63  563 493 HOH HOH B . 
K 7 HOH 64  564 54  HOH HOH B . 
K 7 HOH 65  565 128 HOH HOH B . 
K 7 HOH 66  566 289 HOH HOH B . 
K 7 HOH 67  567 150 HOH HOH B . 
K 7 HOH 68  568 733 HOH HOH B . 
K 7 HOH 69  569 394 HOH HOH B . 
K 7 HOH 70  570 204 HOH HOH B . 
K 7 HOH 71  571 118 HOH HOH B . 
K 7 HOH 72  572 669 HOH HOH B . 
K 7 HOH 73  573 330 HOH HOH B . 
K 7 HOH 74  574 86  HOH HOH B . 
K 7 HOH 75  575 605 HOH HOH B . 
K 7 HOH 76  576 490 HOH HOH B . 
K 7 HOH 77  577 652 HOH HOH B . 
K 7 HOH 78  578 108 HOH HOH B . 
K 7 HOH 79  579 312 HOH HOH B . 
K 7 HOH 80  580 24  HOH HOH B . 
K 7 HOH 81  581 88  HOH HOH B . 
K 7 HOH 82  582 214 HOH HOH B . 
K 7 HOH 83  583 20  HOH HOH B . 
K 7 HOH 84  584 500 HOH HOH B . 
K 7 HOH 85  585 172 HOH HOH B . 
K 7 HOH 86  586 114 HOH HOH B . 
K 7 HOH 87  587 218 HOH HOH B . 
K 7 HOH 88  588 494 HOH HOH B . 
K 7 HOH 89  589 30  HOH HOH B . 
K 7 HOH 90  590 46  HOH HOH B . 
K 7 HOH 91  591 267 HOH HOH B . 
K 7 HOH 92  592 230 HOH HOH B . 
K 7 HOH 93  593 658 HOH HOH B . 
K 7 HOH 94  594 374 HOH HOH B . 
K 7 HOH 95  595 87  HOH HOH B . 
K 7 HOH 96  596 375 HOH HOH B . 
K 7 HOH 97  597 372 HOH HOH B . 
K 7 HOH 98  598 194 HOH HOH B . 
K 7 HOH 99  599 147 HOH HOH B . 
K 7 HOH 100 600 7   HOH HOH B . 
K 7 HOH 101 601 461 HOH HOH B . 
K 7 HOH 102 602 37  HOH HOH B . 
K 7 HOH 103 603 165 HOH HOH B . 
K 7 HOH 104 604 301 HOH HOH B . 
K 7 HOH 105 605 26  HOH HOH B . 
K 7 HOH 106 606 631 HOH HOH B . 
K 7 HOH 107 607 206 HOH HOH B . 
K 7 HOH 108 608 670 HOH HOH B . 
K 7 HOH 109 609 60  HOH HOH B . 
K 7 HOH 110 610 459 HOH HOH B . 
K 7 HOH 111 611 190 HOH HOH B . 
K 7 HOH 112 612 357 HOH HOH B . 
K 7 HOH 113 613 45  HOH HOH B . 
K 7 HOH 114 614 404 HOH HOH B . 
K 7 HOH 115 615 250 HOH HOH B . 
K 7 HOH 116 616 636 HOH HOH B . 
K 7 HOH 117 617 419 HOH HOH B . 
K 7 HOH 118 618 141 HOH HOH B . 
K 7 HOH 119 619 489 HOH HOH B . 
K 7 HOH 120 620 135 HOH HOH B . 
K 7 HOH 121 621 237 HOH HOH B . 
K 7 HOH 122 622 28  HOH HOH B . 
K 7 HOH 123 623 19  HOH HOH B . 
K 7 HOH 124 624 69  HOH HOH B . 
K 7 HOH 125 625 11  HOH HOH B . 
K 7 HOH 126 626 185 HOH HOH B . 
K 7 HOH 127 627 161 HOH HOH B . 
K 7 HOH 128 628 488 HOH HOH B . 
K 7 HOH 129 629 358 HOH HOH B . 
K 7 HOH 130 630 437 HOH HOH B . 
K 7 HOH 131 631 140 HOH HOH B . 
K 7 HOH 132 632 9   HOH HOH B . 
K 7 HOH 133 633 209 HOH HOH B . 
K 7 HOH 134 634 113 HOH HOH B . 
K 7 HOH 135 635 48  HOH HOH B . 
K 7 HOH 136 636 413 HOH HOH B . 
K 7 HOH 137 637 520 HOH HOH B . 
K 7 HOH 138 638 127 HOH HOH B . 
K 7 HOH 139 639 155 HOH HOH B . 
K 7 HOH 140 640 23  HOH HOH B . 
K 7 HOH 141 641 70  HOH HOH B . 
K 7 HOH 142 642 388 HOH HOH B . 
K 7 HOH 143 643 509 HOH HOH B . 
K 7 HOH 144 644 243 HOH HOH B . 
K 7 HOH 145 645 328 HOH HOH B . 
K 7 HOH 146 646 254 HOH HOH B . 
K 7 HOH 147 647 52  HOH HOH B . 
K 7 HOH 148 648 454 HOH HOH B . 
K 7 HOH 149 649 525 HOH HOH B . 
K 7 HOH 150 650 708 HOH HOH B . 
K 7 HOH 151 651 62  HOH HOH B . 
K 7 HOH 152 652 556 HOH HOH B . 
K 7 HOH 153 653 133 HOH HOH B . 
K 7 HOH 154 654 431 HOH HOH B . 
K 7 HOH 155 655 164 HOH HOH B . 
K 7 HOH 156 656 687 HOH HOH B . 
K 7 HOH 157 657 510 HOH HOH B . 
K 7 HOH 158 658 94  HOH HOH B . 
K 7 HOH 159 659 38  HOH HOH B . 
K 7 HOH 160 660 632 HOH HOH B . 
K 7 HOH 161 661 313 HOH HOH B . 
K 7 HOH 162 662 302 HOH HOH B . 
K 7 HOH 163 663 712 HOH HOH B . 
K 7 HOH 164 664 495 HOH HOH B . 
K 7 HOH 165 665 149 HOH HOH B . 
K 7 HOH 166 666 116 HOH HOH B . 
K 7 HOH 167 667 279 HOH HOH B . 
K 7 HOH 168 668 401 HOH HOH B . 
K 7 HOH 169 669 167 HOH HOH B . 
K 7 HOH 170 670 365 HOH HOH B . 
K 7 HOH 171 671 732 HOH HOH B . 
K 7 HOH 172 672 491 HOH HOH B . 
K 7 HOH 173 673 406 HOH HOH B . 
K 7 HOH 174 674 134 HOH HOH B . 
K 7 HOH 175 675 153 HOH HOH B . 
K 7 HOH 176 676 513 HOH HOH B . 
K 7 HOH 177 677 120 HOH HOH B . 
K 7 HOH 178 678 516 HOH HOH B . 
K 7 HOH 179 679 275 HOH HOH B . 
K 7 HOH 180 680 89  HOH HOH B . 
K 7 HOH 181 681 408 HOH HOH B . 
K 7 HOH 182 682 633 HOH HOH B . 
K 7 HOH 183 683 714 HOH HOH B . 
K 7 HOH 184 684 634 HOH HOH B . 
K 7 HOH 185 685 78  HOH HOH B . 
K 7 HOH 186 686 270 HOH HOH B . 
K 7 HOH 187 687 284 HOH HOH B . 
K 7 HOH 188 688 195 HOH HOH B . 
K 7 HOH 189 689 205 HOH HOH B . 
K 7 HOH 190 690 659 HOH HOH B . 
K 7 HOH 191 691 227 HOH HOH B . 
K 7 HOH 192 692 44  HOH HOH B . 
K 7 HOH 193 693 523 HOH HOH B . 
K 7 HOH 194 694 317 HOH HOH B . 
K 7 HOH 195 695 535 HOH HOH B . 
K 7 HOH 196 696 410 HOH HOH B . 
K 7 HOH 197 697 532 HOH HOH B . 
K 7 HOH 198 698 84  HOH HOH B . 
K 7 HOH 199 699 112 HOH HOH B . 
K 7 HOH 200 700 162 HOH HOH B . 
K 7 HOH 201 701 529 HOH HOH B . 
K 7 HOH 202 702 297 HOH HOH B . 
K 7 HOH 203 703 555 HOH HOH B . 
K 7 HOH 204 704 625 HOH HOH B . 
K 7 HOH 205 705 387 HOH HOH B . 
K 7 HOH 206 706 67  HOH HOH B . 
K 7 HOH 207 707 607 HOH HOH B . 
K 7 HOH 208 708 65  HOH HOH B . 
K 7 HOH 209 709 168 HOH HOH B . 
K 7 HOH 210 710 700 HOH HOH B . 
K 7 HOH 211 711 296 HOH HOH B . 
K 7 HOH 212 712 124 HOH HOH B . 
K 7 HOH 213 713 111 HOH HOH B . 
K 7 HOH 214 714 259 HOH HOH B . 
K 7 HOH 215 715 226 HOH HOH B . 
K 7 HOH 216 716 648 HOH HOH B . 
K 7 HOH 217 717 77  HOH HOH B . 
K 7 HOH 218 718 311 HOH HOH B . 
K 7 HOH 219 719 43  HOH HOH B . 
K 7 HOH 220 720 611 HOH HOH B . 
K 7 HOH 221 721 258 HOH HOH B . 
K 7 HOH 222 722 691 HOH HOH B . 
K 7 HOH 223 723 528 HOH HOH B . 
K 7 HOH 224 724 288 HOH HOH B . 
K 7 HOH 225 725 380 HOH HOH B . 
K 7 HOH 226 726 58  HOH HOH B . 
K 7 HOH 227 727 213 HOH HOH B . 
K 7 HOH 228 728 176 HOH HOH B . 
K 7 HOH 229 729 310 HOH HOH B . 
K 7 HOH 230 730 381 HOH HOH B . 
K 7 HOH 231 731 524 HOH HOH B . 
K 7 HOH 232 732 129 HOH HOH B . 
K 7 HOH 233 733 156 HOH HOH B . 
K 7 HOH 234 734 188 HOH HOH B . 
K 7 HOH 235 735 407 HOH HOH B . 
K 7 HOH 236 736 521 HOH HOH B . 
K 7 HOH 237 737 137 HOH HOH B . 
K 7 HOH 238 738 627 HOH HOH B . 
K 7 HOH 239 739 559 HOH HOH B . 
K 7 HOH 240 740 643 HOH HOH B . 
K 7 HOH 241 741 412 HOH HOH B . 
K 7 HOH 242 742 441 HOH HOH B . 
K 7 HOH 243 743 650 HOH HOH B . 
K 7 HOH 244 744 68  HOH HOH B . 
K 7 HOH 245 745 180 HOH HOH B . 
K 7 HOH 246 746 348 HOH HOH B . 
K 7 HOH 247 747 497 HOH HOH B . 
K 7 HOH 248 748 248 HOH HOH B . 
K 7 HOH 249 749 654 HOH HOH B . 
K 7 HOH 250 750 253 HOH HOH B . 
K 7 HOH 251 751 655 HOH HOH B . 
K 7 HOH 252 752 536 HOH HOH B . 
K 7 HOH 253 753 690 HOH HOH B . 
K 7 HOH 254 754 598 HOH HOH B . 
K 7 HOH 255 755 726 HOH HOH B . 
K 7 HOH 256 756 458 HOH HOH B . 
K 7 HOH 257 757 199 HOH HOH B . 
K 7 HOH 258 758 203 HOH HOH B . 
K 7 HOH 259 759 367 HOH HOH B . 
K 7 HOH 260 760 657 HOH HOH B . 
K 7 HOH 261 761 399 HOH HOH B . 
K 7 HOH 262 762 385 HOH HOH B . 
K 7 HOH 263 763 584 HOH HOH B . 
K 7 HOH 264 764 274 HOH HOH B . 
K 7 HOH 265 765 400 HOH HOH B . 
K 7 HOH 266 766 614 HOH HOH B . 
K 7 HOH 267 767 416 HOH HOH B . 
K 7 HOH 268 768 604 HOH HOH B . 
K 7 HOH 269 769 601 HOH HOH B . 
K 7 HOH 270 770 550 HOH HOH B . 
K 7 HOH 271 771 593 HOH HOH B . 
K 7 HOH 272 772 730 HOH HOH B . 
K 7 HOH 273 773 466 HOH HOH B . 
K 7 HOH 274 774 595 HOH HOH B . 
K 7 HOH 275 775 709 HOH HOH B . 
K 7 HOH 276 776 315 HOH HOH B . 
K 7 HOH 277 777 368 HOH HOH B . 
K 7 HOH 278 778 546 HOH HOH B . 
K 7 HOH 279 779 212 HOH HOH B . 
K 7 HOH 280 780 425 HOH HOH B . 
K 7 HOH 281 781 467 HOH HOH B . 
K 7 HOH 282 782 280 HOH HOH B . 
K 7 HOH 283 783 472 HOH HOH B . 
K 7 HOH 284 784 395 HOH HOH B . 
K 7 HOH 285 785 481 HOH HOH B . 
K 7 HOH 286 786 334 HOH HOH B . 
K 7 HOH 287 787 721 HOH HOH B . 
K 7 HOH 288 788 671 HOH HOH B . 
K 7 HOH 289 789 256 HOH HOH B . 
K 7 HOH 290 790 173 HOH HOH B . 
K 7 HOH 291 791 623 HOH HOH B . 
K 7 HOH 292 792 722 HOH HOH B . 
K 7 HOH 293 793 217 HOH HOH B . 
K 7 HOH 294 794 363 HOH HOH B . 
K 7 HOH 295 795 104 HOH HOH B . 
K 7 HOH 296 796 191 HOH HOH B . 
K 7 HOH 297 797 473 HOH HOH B . 
K 7 HOH 298 798 728 HOH HOH B . 
K 7 HOH 299 799 202 HOH HOH B . 
K 7 HOH 300 800 303 HOH HOH B . 
K 7 HOH 301 801 200 HOH HOH B . 
K 7 HOH 302 802 689 HOH HOH B . 
K 7 HOH 303 803 476 HOH HOH B . 
K 7 HOH 304 804 215 HOH HOH B . 
K 7 HOH 305 805 415 HOH HOH B . 
K 7 HOH 306 806 470 HOH HOH B . 
K 7 HOH 307 807 238 HOH HOH B . 
K 7 HOH 308 808 263 HOH HOH B . 
K 7 HOH 309 809 143 HOH HOH B . 
K 7 HOH 310 810 644 HOH HOH B . 
K 7 HOH 311 811 702 HOH HOH B . 
K 7 HOH 312 812 292 HOH HOH B . 
K 7 HOH 313 813 585 HOH HOH B . 
K 7 HOH 314 814 696 HOH HOH B . 
K 7 HOH 315 815 272 HOH HOH B . 
K 7 HOH 316 816 606 HOH HOH B . 
K 7 HOH 317 817 539 HOH HOH B . 
K 7 HOH 318 818 571 HOH HOH B . 
K 7 HOH 319 819 568 HOH HOH B . 
K 7 HOH 320 820 592 HOH HOH B . 
K 7 HOH 321 821 612 HOH HOH B . 
K 7 HOH 322 822 478 HOH HOH B . 
K 7 HOH 323 823 583 HOH HOH B . 
K 7 HOH 324 824 377 HOH HOH B . 
K 7 HOH 325 825 677 HOH HOH B . 
K 7 HOH 326 826 346 HOH HOH B . 
K 7 HOH 327 827 626 HOH HOH B . 
K 7 HOH 328 828 551 HOH HOH B . 
K 7 HOH 329 829 599 HOH HOH B . 
K 7 HOH 330 830 582 HOH HOH B . 
K 7 HOH 331 831 541 HOH HOH B . 
K 7 HOH 332 832 382 HOH HOH B . 
K 7 HOH 333 833 673 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HDM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.983 
_cell.length_a_esd                 ? 
_cell.length_b                     108.293 
_cell.length_b_esd                 ? 
_cell.length_c                     115.732 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9HDM 
_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                   9HDM 
_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             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.44 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'25 % (w/v) PEG 3350, 0.2 M MgCl2 x 6 H2O and 0.1 M HEPES at pH 7.5; Co-crystallized with 15 mM thymidine' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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         2024-02-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_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   0.9798 
_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                        'ESRF BEAMLINE BM07' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9798 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BM07 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HDM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_reflns.d_resolution_low                               115.73 
_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                                     106321 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.95 
_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                                0.090 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1406879 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.087 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_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_shell.d_res_high                                    1.55 
_reflns_shell.d_res_low                                     1.58 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           70054 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5222 
_reflns_shell.percent_possible_obs                          99.9 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_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                               13.4 
_reflns_shell.pdbx_chi_squared                              0.88 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               2.939 
_reflns_shell.pdbx_Rpim_I_all                               0.799 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.535 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.827 
_reflns_shell.pdbx_Rsym_value                               ? 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9HDM 
_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                            1.55 
_refine.ls_d_res_low                             40.96 
_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                     106195 
_refine.ls_number_reflns_R_free                  5425 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_percent_reflns_R_free                 5.11 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1758 
_refine.ls_R_factor_R_free                       0.2007 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1745 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.62 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        40.96 
_refine_hist.number_atoms_solvent             654 
_refine_hist.number_atoms_total               5965 
_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       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5264 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         47 
_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' ? 0.006  ? 5493 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.844  ? 7484 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.996 ? 2046 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056  ? 845  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 983  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.55 1.57  . . 167 3360 100.00 . . . . 0.3404 . . . . . . . . . . . 0.3881 
'X-RAY DIFFRACTION' 1.57 1.59  . . 178 3293 100.00 . . . . 0.3255 . . . . . . . . . . . 0.3821 
'X-RAY DIFFRACTION' 1.59 1.61  . . 183 3305 100.00 . . . . 0.2981 . . . . . . . . . . . 0.3144 
'X-RAY DIFFRACTION' 1.61 1.63  . . 192 3300 100.00 . . . . 0.2742 . . . . . . . . . . . 0.3072 
'X-RAY DIFFRACTION' 1.63 1.65  . . 175 3300 100.00 . . . . 0.2652 . . . . . . . . . . . 0.2776 
'X-RAY DIFFRACTION' 1.65 1.67  . . 181 3352 100.00 . . . . 0.2482 . . . . . . . . . . . 0.2646 
'X-RAY DIFFRACTION' 1.67 1.69  . . 190 3311 100.00 . . . . 0.2416 . . . . . . . . . . . 0.2548 
'X-RAY DIFFRACTION' 1.69 1.72  . . 192 3302 100.00 . . . . 0.2199 . . . . . . . . . . . 0.2635 
'X-RAY DIFFRACTION' 1.72 1.75  . . 186 3312 100.00 . . . . 0.2056 . . . . . . . . . . . 0.2376 
'X-RAY DIFFRACTION' 1.75 1.77  . . 203 3318 100.00 . . . . 0.2027 . . . . . . . . . . . 0.2111 
'X-RAY DIFFRACTION' 1.77 1.80  . . 184 3341 100.00 . . . . 0.2059 . . . . . . . . . . . 0.2291 
'X-RAY DIFFRACTION' 1.80 1.84  . . 148 3356 100.00 . . . . 0.1991 . . . . . . . . . . . 0.2330 
'X-RAY DIFFRACTION' 1.84 1.87  . . 187 3314 100.00 . . . . 0.2078 . . . . . . . . . . . 0.2412 
'X-RAY DIFFRACTION' 1.87 1.91  . . 159 3343 100.00 . . . . 0.2082 . . . . . . . . . . . 0.2452 
'X-RAY DIFFRACTION' 1.91 1.95  . . 185 3352 100.00 . . . . 0.1938 . . . . . . . . . . . 0.2026 
'X-RAY DIFFRACTION' 1.95 2.00  . . 180 3343 100.00 . . . . 0.1865 . . . . . . . . . . . 0.1986 
'X-RAY DIFFRACTION' 2.00 2.05  . . 197 3328 100.00 . . . . 0.1791 . . . . . . . . . . . 0.2151 
'X-RAY DIFFRACTION' 2.05 2.10  . . 183 3322 100.00 . . . . 0.1743 . . . . . . . . . . . 0.1936 
'X-RAY DIFFRACTION' 2.10 2.17  . . 212 3331 100.00 . . . . 0.1674 . . . . . . . . . . . 0.1974 
'X-RAY DIFFRACTION' 2.17 2.24  . . 162 3391 100.00 . . . . 0.1661 . . . . . . . . . . . 0.1877 
'X-RAY DIFFRACTION' 2.24 2.32  . . 180 3371 100.00 . . . . 0.1733 . . . . . . . . . . . 0.2153 
'X-RAY DIFFRACTION' 2.32 2.41  . . 187 3352 100.00 . . . . 0.1762 . . . . . . . . . . . 0.2072 
'X-RAY DIFFRACTION' 2.41 2.52  . . 182 3380 100.00 . . . . 0.1773 . . . . . . . . . . . 0.2006 
'X-RAY DIFFRACTION' 2.52 2.65  . . 150 3380 100.00 . . . . 0.1672 . . . . . . . . . . . 0.1956 
'X-RAY DIFFRACTION' 2.65 2.82  . . 186 3373 100.00 . . . . 0.1685 . . . . . . . . . . . 0.2013 
'X-RAY DIFFRACTION' 2.82 3.03  . . 188 3387 100.00 . . . . 0.1742 . . . . . . . . . . . 0.1907 
'X-RAY DIFFRACTION' 3.03 3.34  . . 157 3411 100.00 . . . . 0.1665 . . . . . . . . . . . 0.2031 
'X-RAY DIFFRACTION' 3.34 3.82  . . 196 3432 100.00 . . . . 0.1499 . . . . . . . . . . . 0.1595 
'X-RAY DIFFRACTION' 3.82 4.81  . . 166 3499 100.00 . . . . 0.1341 . . . . . . . . . . . 0.1620 
'X-RAY DIFFRACTION' 4.81 40.96 . . 189 3611 100.00 . . . . 0.1689 . . . . . . . . . . . 0.1968 
# 
_struct.entry_id                     9HDM 
_struct.title                        
;Crystal structure of Pyrimidine Nucleoside 2'-Hydroxylase (PDN2'H) from Neurospora crassa in complex with thymidine
;
_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        9HDM 
_struct_keywords.text            'alpha-ketoglutarate-dependent dioxygenase, nucleoside hydroxylase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 5 ? 
H N N 3 ? 
I N N 6 ? 
J N N 7 ? 
K N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q7SHQ5_NEUCR 
_struct_ref.pdbx_db_accession          Q7SHQ5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAPIAQAVTVSLNDLKNGTVSLEALEEAFGPDSLGILVVKDVPAEFAELRHRLLSYSSYLGNLPKSELDRLENEKAKYLT
GWSLGKETLKNGQVDNLKGSYYANCAFYVDPSLSCAKPTEEFNPDNFPEYLSPNLWPQESTLPGFKPTFEDLCRLIIDVA
VLVARACDRFAEKQIAGYPAGYLEGVVKTSTTTKARLLHYFPEEATATDASKESNKEEEGDEDDWCATHLDHGCLTGLTS
AMFVDEAATPPVVNPSVNGSLPPLGELPTSPDPKAGLYIKSRTGQTVQVKIPRDCIAFQTGEALERITGGKFKAVPHFVR
GARAEMSAGRIARNTLAVFTQPNLGDEVDMEQHITFGEFARGIVAKNTVS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9HDM A 21 ? 390 ? Q7SHQ5 1 ? 370 ? 1 370 
2 1 9HDM B 21 ? 390 ? Q7SHQ5 1 ? 370 ? 1 370 
# 
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 9HDM MET A 1  ? UNP Q7SHQ5 ? ? 'initiating methionine' -19 1  
1 9HDM GLY A 2  ? UNP Q7SHQ5 ? ? 'expression tag'        -18 2  
1 9HDM SER A 3  ? UNP Q7SHQ5 ? ? 'expression tag'        -17 3  
1 9HDM SER A 4  ? UNP Q7SHQ5 ? ? 'expression tag'        -16 4  
1 9HDM HIS A 5  ? UNP Q7SHQ5 ? ? 'expression tag'        -15 5  
1 9HDM HIS A 6  ? UNP Q7SHQ5 ? ? 'expression tag'        -14 6  
1 9HDM HIS A 7  ? UNP Q7SHQ5 ? ? 'expression tag'        -13 7  
1 9HDM HIS A 8  ? UNP Q7SHQ5 ? ? 'expression tag'        -12 8  
1 9HDM HIS A 9  ? UNP Q7SHQ5 ? ? 'expression tag'        -11 9  
1 9HDM HIS A 10 ? UNP Q7SHQ5 ? ? 'expression tag'        -10 10 
1 9HDM SER A 11 ? UNP Q7SHQ5 ? ? 'expression tag'        -9  11 
1 9HDM SER A 12 ? UNP Q7SHQ5 ? ? 'expression tag'        -8  12 
1 9HDM GLY A 13 ? UNP Q7SHQ5 ? ? 'expression tag'        -7  13 
1 9HDM LEU A 14 ? UNP Q7SHQ5 ? ? 'expression tag'        -6  14 
1 9HDM VAL A 15 ? UNP Q7SHQ5 ? ? 'expression tag'        -5  15 
1 9HDM PRO A 16 ? UNP Q7SHQ5 ? ? 'expression tag'        -4  16 
1 9HDM ARG A 17 ? UNP Q7SHQ5 ? ? 'expression tag'        -3  17 
1 9HDM GLY A 18 ? UNP Q7SHQ5 ? ? 'expression tag'        -2  18 
1 9HDM SER A 19 ? UNP Q7SHQ5 ? ? 'expression tag'        -1  19 
1 9HDM HIS A 20 ? UNP Q7SHQ5 ? ? 'expression tag'        0   20 
2 9HDM MET B 1  ? UNP Q7SHQ5 ? ? 'initiating methionine' -19 21 
2 9HDM GLY B 2  ? UNP Q7SHQ5 ? ? 'expression tag'        -18 22 
2 9HDM SER B 3  ? UNP Q7SHQ5 ? ? 'expression tag'        -17 23 
2 9HDM SER B 4  ? UNP Q7SHQ5 ? ? 'expression tag'        -16 24 
2 9HDM HIS B 5  ? UNP Q7SHQ5 ? ? 'expression tag'        -15 25 
2 9HDM HIS B 6  ? UNP Q7SHQ5 ? ? 'expression tag'        -14 26 
2 9HDM HIS B 7  ? UNP Q7SHQ5 ? ? 'expression tag'        -13 27 
2 9HDM HIS B 8  ? UNP Q7SHQ5 ? ? 'expression tag'        -12 28 
2 9HDM HIS B 9  ? UNP Q7SHQ5 ? ? 'expression tag'        -11 29 
2 9HDM HIS B 10 ? UNP Q7SHQ5 ? ? 'expression tag'        -10 30 
2 9HDM SER B 11 ? UNP Q7SHQ5 ? ? 'expression tag'        -9  31 
2 9HDM SER B 12 ? UNP Q7SHQ5 ? ? 'expression tag'        -8  32 
2 9HDM GLY B 13 ? UNP Q7SHQ5 ? ? 'expression tag'        -7  33 
2 9HDM LEU B 14 ? UNP Q7SHQ5 ? ? 'expression tag'        -6  34 
2 9HDM VAL B 15 ? UNP Q7SHQ5 ? ? 'expression tag'        -5  35 
2 9HDM PRO B 16 ? UNP Q7SHQ5 ? ? 'expression tag'        -4  36 
2 9HDM ARG B 17 ? UNP Q7SHQ5 ? ? 'expression tag'        -3  37 
2 9HDM GLY B 18 ? UNP Q7SHQ5 ? ? 'expression tag'        -2  38 
2 9HDM SER B 19 ? UNP Q7SHQ5 ? ? 'expression tag'        -1  39 
2 9HDM HIS B 20 ? UNP Q7SHQ5 ? ? 'expression tag'        0   40 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,J   
2 1 B,F,G,H,I,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 LEU A 32  ? ASN A 37  ? LEU A 12  ASN A 17  1 ? 6  
HELX_P HELX_P2  AA2 SER A 41  ? GLY A 50  ? SER A 21  GLY A 30  1 ? 10 
HELX_P HELX_P3  AA3 GLU A 65  ? ASN A 82  ? GLU A 45  ASN A 62  1 ? 18 
HELX_P HELX_P4  AA4 PRO A 84  ? ARG A 90  ? PRO A 64  ARG A 70  1 ? 7  
HELX_P HELX_P5  AA5 ALA A 126 ? VAL A 129 ? ALA A 106 VAL A 109 5 ? 4  
HELX_P HELX_P6  AA6 PHE A 147 ? SER A 152 ? PHE A 127 SER A 132 1 ? 6  
HELX_P HELX_P7  AA7 GLY A 164 ? ILE A 195 ? GLY A 144 ILE A 175 1 ? 32 
HELX_P HELX_P8  AA8 GLY A 201 ? THR A 209 ? GLY A 181 THR A 189 1 ? 9  
HELX_P HELX_P9  AA9 GLY A 321 ? THR A 328 ? GLY A 301 THR A 308 1 ? 8  
HELX_P HELX_P10 AB1 ARG A 343 ? ALA A 348 ? ARG A 323 ALA A 328 1 ? 6  
HELX_P HELX_P11 AB2 PHE A 376 ? ARG A 381 ? PHE A 356 ARG A 361 1 ? 6  
HELX_P HELX_P12 AB3 LEU B 32  ? ASN B 37  ? LEU B 12  ASN B 17  1 ? 6  
HELX_P HELX_P13 AB4 SER B 41  ? GLY B 50  ? SER B 21  GLY B 30  1 ? 10 
HELX_P HELX_P14 AB5 GLU B 65  ? ASN B 82  ? GLU B 45  ASN B 62  1 ? 18 
HELX_P HELX_P15 AB6 PRO B 84  ? ARG B 90  ? PRO B 64  ARG B 70  1 ? 7  
HELX_P HELX_P16 AB7 ALA B 126 ? VAL B 129 ? ALA B 106 VAL B 109 5 ? 4  
HELX_P HELX_P17 AB8 PHE B 147 ? SER B 152 ? PHE B 127 SER B 132 1 ? 6  
HELX_P HELX_P18 AB9 GLY B 164 ? ILE B 195 ? GLY B 144 ILE B 175 1 ? 32 
HELX_P HELX_P19 AC1 GLY B 201 ? THR B 209 ? GLY B 181 THR B 189 1 ? 9  
HELX_P HELX_P20 AC2 GLY B 321 ? THR B 328 ? GLY B 301 THR B 308 1 ? 8  
HELX_P HELX_P21 AC3 ARG B 343 ? ALA B 348 ? ARG B 323 ALA B 328 1 ? 6  
HELX_P HELX_P22 AC4 PHE B 376 ? ARG B 381 ? PHE B 356 ARG B 361 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 249 NE2 ? ? ? 1_555 C MN  . MN ? ? A HIS 229 A MN  401 1_555 ? ? ? ? ? ? ? 2.233 ? ? 
metalc2  metalc ? ? A ASP 251 OD1 ? ? ? 1_555 C MN  . MN ? ? A ASP 231 A MN  401 1_555 ? ? ? ? ? ? ? 2.220 ? ? 
metalc3  metalc ? ? A HIS 337 NE2 ? ? ? 1_555 C MN  . MN ? ? A HIS 317 A MN  401 1_555 ? ? ? ? ? ? ? 2.240 ? ? 
metalc4  metalc ? ? C MN  .   MN  ? ? ? 1_555 J HOH . O  ? ? A MN  401 A HOH 541 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc5  metalc ? ? C MN  .   MN  ? ? ? 1_555 J HOH . O  ? ? A MN  401 A HOH 745 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc6  metalc ? ? C MN  .   MN  ? ? ? 1_555 J HOH . O  ? ? A MN  401 A HOH 756 1_555 ? ? ? ? ? ? ? 2.230 ? ? 
metalc7  metalc ? ? B HIS 249 NE2 ? ? ? 1_555 F MN  . MN ? ? B HIS 229 B MN  401 1_555 ? ? ? ? ? ? ? 2.223 ? ? 
metalc8  metalc ? ? B ASP 251 OD1 ? ? ? 1_555 F MN  . MN ? ? B ASP 231 B MN  401 1_555 ? ? ? ? ? ? ? 2.241 ? ? 
metalc9  metalc ? ? B HIS 337 NE2 ? ? ? 1_555 F MN  . MN ? ? B HIS 317 B MN  401 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc10 metalc ? ? F MN  .   MN  ? ? ? 1_555 K HOH . O  ? ? B MN  401 B HOH 534 1_555 ? ? ? ? ? ? ? 2.239 ? ? 
metalc11 metalc ? ? F MN  .   MN  ? ? ? 1_555 K HOH . O  ? ? B MN  401 B HOH 744 1_555 ? ? ? ? ? ? ? 2.205 ? ? 
metalc12 metalc ? ? F MN  .   MN  ? ? ? 1_555 K HOH . O  ? ? B MN  401 B HOH 749 1_555 ? ? ? ? ? ? ? 2.242 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 249 ? A HIS 229 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 OD1 ? A ASP 251 ? A ASP 231 ? 1_555 93.0  ? 
2  NE2 ? A HIS 249 ? A HIS 229 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 NE2 ? A HIS 337 ? A HIS 317 ? 1_555 88.4  ? 
3  OD1 ? A ASP 251 ? A ASP 231 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 NE2 ? A HIS 337 ? A HIS 317 ? 1_555 92.0  ? 
4  NE2 ? A HIS 249 ? A HIS 229 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 541 ? 1_555 178.0 ? 
5  OD1 ? A ASP 251 ? A ASP 231 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 541 ? 1_555 88.8  ? 
6  NE2 ? A HIS 337 ? A HIS 317 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 541 ? 1_555 92.4  ? 
7  NE2 ? A HIS 249 ? A HIS 229 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 745 ? 1_555 92.8  ? 
8  OD1 ? A ASP 251 ? A ASP 231 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 745 ? 1_555 174.2 ? 
9  NE2 ? A HIS 337 ? A HIS 317 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 745 ? 1_555 88.0  ? 
10 O   ? J HOH .   ? A HOH 541 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 745 ? 1_555 85.4  ? 
11 NE2 ? A HIS 249 ? A HIS 229 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 756 ? 1_555 93.6  ? 
12 OD1 ? A ASP 251 ? A ASP 231 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 756 ? 1_555 94.8  ? 
13 NE2 ? A HIS 337 ? A HIS 317 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 756 ? 1_555 172.8 ? 
14 O   ? J HOH .   ? A HOH 541 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 756 ? 1_555 85.4  ? 
15 O   ? J HOH .   ? A HOH 745 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? J HOH .   ? A HOH 756 ? 1_555 85.0  ? 
16 NE2 ? B HIS 249 ? B HIS 229 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 OD1 ? B ASP 251 ? B ASP 231 ? 1_555 94.9  ? 
17 NE2 ? B HIS 249 ? B HIS 229 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 NE2 ? B HIS 337 ? B HIS 317 ? 1_555 88.2  ? 
18 OD1 ? B ASP 251 ? B ASP 231 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 NE2 ? B HIS 337 ? B HIS 317 ? 1_555 91.7  ? 
19 NE2 ? B HIS 249 ? B HIS 229 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 534 ? 1_555 177.7 ? 
20 OD1 ? B ASP 251 ? B ASP 231 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 534 ? 1_555 86.7  ? 
21 NE2 ? B HIS 337 ? B HIS 317 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 534 ? 1_555 93.5  ? 
22 NE2 ? B HIS 249 ? B HIS 229 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 744 ? 1_555 91.2  ? 
23 OD1 ? B ASP 251 ? B ASP 231 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 744 ? 1_555 92.8  ? 
24 NE2 ? B HIS 337 ? B HIS 317 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 744 ? 1_555 175.5 ? 
25 O   ? K HOH .   ? B HOH 534 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 744 ? 1_555 87.0  ? 
26 NE2 ? B HIS 249 ? B HIS 229 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 749 ? 1_555 92.3  ? 
27 OD1 ? B ASP 251 ? B ASP 231 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 749 ? 1_555 172.5 ? 
28 NE2 ? B HIS 337 ? B HIS 317 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 749 ? 1_555 90.7  ? 
29 O   ? K HOH .   ? B HOH 534 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 749 ? 1_555 86.1  ? 
30 O   ? K HOH .   ? B HOH 744 ? 1_555 MN ? F MN . ? B MN 401 ? 1_555 O   ? K HOH .   ? B HOH 749 ? 1_555 84.9  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 8 ? 
AA6 ? 6 ? 
AA7 ? 3 ? 
AA8 ? 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 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA5 7 8 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 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 VAL A 28  ? SER A 31  ? VAL A 8   SER A 11  
AA1 2 ILE A 56  ? LYS A 60  ? ILE A 36  LYS A 40  
AA1 3 ILE A 316 ? THR A 320 ? ILE A 296 THR A 300 
AA1 4 LEU A 255 ? LEU A 258 ? LEU A 235 LEU A 238 
AA1 5 ILE A 351 ? THR A 360 ? ILE A 331 THR A 340 
AA1 6 LYS A 214 ? TYR A 220 ? LYS A 194 TYR A 200 
AA1 7 ASN A 116 ? ASN A 124 ? ASN A 96  ASN A 104 
AA1 8 GLY A 101 ? GLU A 107 ? GLY A 81  GLU A 87  
AA2 1 VAL A 28  ? SER A 31  ? VAL A 8   SER A 11  
AA2 2 ILE A 56  ? LYS A 60  ? ILE A 36  LYS A 40  
AA2 3 ILE A 316 ? THR A 320 ? ILE A 296 THR A 300 
AA2 4 LEU A 255 ? LEU A 258 ? LEU A 235 LEU A 238 
AA2 5 ILE A 351 ? THR A 360 ? ILE A 331 THR A 340 
AA2 6 MET A 262 ? ASP A 265 ? MET A 242 ASP A 245 
AA3 1 THR A 306 ? VAL A 309 ? THR A 286 VAL A 289 
AA3 2 GLY A 296 ? LYS A 300 ? GLY A 276 LYS A 280 
AA3 3 HIS A 337 ? ARG A 340 ? HIS A 317 ARG A 320 
AA4 1 GLU A 367 ? ASP A 369 ? GLU A 347 ASP A 349 
AA4 2 ILE A 374 ? THR A 375 ? ILE A 354 THR A 355 
AA5 1 VAL B 28  ? SER B 31  ? VAL B 8   SER B 11  
AA5 2 ILE B 56  ? LYS B 60  ? ILE B 36  LYS B 40  
AA5 3 ILE B 316 ? THR B 320 ? ILE B 296 THR B 300 
AA5 4 LEU B 255 ? LEU B 258 ? LEU B 235 LEU B 238 
AA5 5 ILE B 351 ? THR B 360 ? ILE B 331 THR B 340 
AA5 6 LYS B 214 ? TYR B 220 ? LYS B 194 TYR B 200 
AA5 7 LEU B 117 ? ASN B 124 ? LEU B 97  ASN B 104 
AA5 8 GLY B 101 ? LYS B 106 ? GLY B 81  LYS B 86  
AA6 1 VAL B 28  ? SER B 31  ? VAL B 8   SER B 11  
AA6 2 ILE B 56  ? LYS B 60  ? ILE B 36  LYS B 40  
AA6 3 ILE B 316 ? THR B 320 ? ILE B 296 THR B 300 
AA6 4 LEU B 255 ? LEU B 258 ? LEU B 235 LEU B 238 
AA6 5 ILE B 351 ? THR B 360 ? ILE B 331 THR B 340 
AA6 6 MET B 262 ? ASP B 265 ? MET B 242 ASP B 245 
AA7 1 THR B 306 ? VAL B 309 ? THR B 286 VAL B 289 
AA7 2 GLY B 296 ? LYS B 300 ? GLY B 276 LYS B 280 
AA7 3 HIS B 337 ? ARG B 340 ? HIS B 317 ARG B 320 
AA8 1 GLU B 367 ? ASP B 369 ? GLU B 347 ASP B 349 
AA8 2 ILE B 374 ? THR B 375 ? ILE B 354 THR B 355 
# 
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 VAL A 28  ? N VAL A 8   O VAL A 58  ? O VAL A 38  
AA1 2 3 N VAL A 59  ? N VAL A 39  O ILE A 316 ? O ILE A 296 
AA1 3 4 O GLN A 319 ? O GLN A 299 N THR A 256 ? N THR A 236 
AA1 4 5 N GLY A 257 ? N GLY A 237 O VAL A 358 ? O VAL A 338 
AA1 5 6 O ARG A 353 ? O ARG A 333 N TYR A 220 ? N TYR A 200 
AA1 6 7 O ALA A 215 ? O ALA A 195 N ALA A 123 ? N ALA A 103 
AA1 7 8 O TYR A 122 ? O TYR A 102 N GLY A 101 ? N GLY A 81  
AA2 1 2 N VAL A 28  ? N VAL A 8   O VAL A 58  ? O VAL A 38  
AA2 2 3 N VAL A 59  ? N VAL A 39  O ILE A 316 ? O ILE A 296 
AA2 3 4 O GLN A 319 ? O GLN A 299 N THR A 256 ? N THR A 236 
AA2 4 5 N GLY A 257 ? N GLY A 237 O VAL A 358 ? O VAL A 338 
AA2 5 6 O ASN A 354 ? O ASN A 334 N MET A 262 ? N MET A 242 
AA3 1 2 O VAL A 307 ? O VAL A 287 N ILE A 299 ? N ILE A 279 
AA3 2 3 N TYR A 298 ? N TYR A 278 O PHE A 338 ? O PHE A 318 
AA4 1 2 N VAL A 368 ? N VAL A 348 O ILE A 374 ? O ILE A 354 
AA5 1 2 N VAL B 28  ? N VAL B 8   O VAL B 58  ? O VAL B 38  
AA5 2 3 N VAL B 59  ? N VAL B 39  O ILE B 316 ? O ILE B 296 
AA5 3 4 O GLN B 319 ? O GLN B 299 N THR B 256 ? N THR B 236 
AA5 4 5 N GLY B 257 ? N GLY B 237 O VAL B 358 ? O VAL B 338 
AA5 5 6 O ARG B 353 ? O ARG B 333 N TYR B 220 ? N TYR B 200 
AA5 6 7 O HIS B 219 ? O HIS B 199 N GLY B 119 ? N GLY B 99  
AA5 7 8 O LYS B 118 ? O LYS B 98  N GLY B 105 ? N GLY B 85  
AA6 1 2 N VAL B 28  ? N VAL B 8   O VAL B 58  ? O VAL B 38  
AA6 2 3 N VAL B 59  ? N VAL B 39  O ILE B 316 ? O ILE B 296 
AA6 3 4 O GLN B 319 ? O GLN B 299 N THR B 256 ? N THR B 236 
AA6 4 5 N GLY B 257 ? N GLY B 237 O VAL B 358 ? O VAL B 338 
AA6 5 6 O ALA B 352 ? O ALA B 332 N VAL B 264 ? N VAL B 244 
AA7 1 2 O VAL B 307 ? O VAL B 287 N ILE B 299 ? N ILE B 279 
AA7 2 3 N GLY B 296 ? N GLY B 276 O ARG B 340 ? O ARG B 320 
AA8 1 2 N VAL B 368 ? N VAL B 348 O ILE B 374 ? O ILE B 354 
# 
_pdbx_entry_details.entry_id                   9HDM 
_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           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 573 ? ? O A HOH 692 ? ? 2.15 
2 1 O B HOH 709 ? ? O B HOH 716 ? ? 2.18 
3 1 O B HOH 537 ? ? O B HOH 800 ? ? 2.19 
# 
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 CYS A 115 ? ? 175.48 170.51  
2 1 CYS A 234 ? ? -96.71 -65.62  
3 1 CYS B 115 ? ? 175.60 170.97  
4 1 CYS B 234 ? ? -96.21 -65.46  
5 1 SER B 256 ? ? -65.04 -179.10 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -14.7004 
_pdbx_refine_tls.origin_y         21.0525 
_pdbx_refine_tls.origin_z         -34.6770 
_pdbx_refine_tls.T[1][1]          0.1757 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0090 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0129 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1633 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0191 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1914 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.5002 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.2574 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4594 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.3698 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.2327 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.7325 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0121 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0116 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0183 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0056 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0079 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0130 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0106 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0239 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0046 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 821 ? 5.85 . 
2 1 O ? B HOH 832 ? 5.91 . 
3 1 O ? B HOH 833 ? 6.07 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A LYS 90  ? A LYS 110 
14 1 Y 1 A ASN 91  ? A ASN 111 
15 1 Y 1 A GLY 92  ? A GLY 112 
16 1 Y 1 A GLN 93  ? A GLN 113 
17 1 Y 1 A VAL 94  ? A VAL 114 
18 1 Y 1 A THR 206 ? A THR 226 
19 1 Y 1 A ALA 207 ? A ALA 227 
20 1 Y 1 A THR 208 ? A THR 228 
21 1 Y 1 A ASP 209 ? A ASP 229 
22 1 Y 1 A ALA 210 ? A ALA 230 
23 1 Y 1 A SER 211 ? A SER 231 
24 1 Y 1 A LYS 212 ? A LYS 232 
25 1 Y 1 A GLU 213 ? A GLU 233 
26 1 Y 1 A SER 214 ? A SER 234 
27 1 Y 1 A ASN 215 ? A ASN 235 
28 1 Y 1 A LYS 216 ? A LYS 236 
29 1 Y 1 A GLU 217 ? A GLU 237 
30 1 Y 1 A GLU 218 ? A GLU 238 
31 1 Y 1 A GLU 219 ? A GLU 239 
32 1 Y 1 A GLY 220 ? A GLY 240 
33 1 Y 1 A ASP 221 ? A ASP 241 
34 1 Y 1 A GLU 222 ? A GLU 242 
35 1 Y 1 A ASP 223 ? A ASP 243 
36 1 Y 1 A ASP 224 ? A ASP 244 
37 1 Y 1 A TRP 225 ? A TRP 245 
38 1 Y 1 A PRO 255 ? A PRO 275 
39 1 Y 1 A SER 256 ? A SER 276 
40 1 Y 1 A VAL 257 ? A VAL 277 
41 1 Y 1 A ASN 258 ? A ASN 278 
42 1 Y 1 A THR 368 ? A THR 388 
43 1 Y 1 A VAL 369 ? A VAL 389 
44 1 Y 1 A SER 370 ? A SER 390 
45 1 Y 1 B MET -19 ? B MET 1   
46 1 Y 1 B GLY -18 ? B GLY 2   
47 1 Y 1 B SER -17 ? B SER 3   
48 1 Y 1 B SER -16 ? B SER 4   
49 1 Y 1 B HIS -15 ? B HIS 5   
50 1 Y 1 B HIS -14 ? B HIS 6   
51 1 Y 1 B HIS -13 ? B HIS 7   
52 1 Y 1 B HIS -12 ? B HIS 8   
53 1 Y 1 B HIS -11 ? B HIS 9   
54 1 Y 1 B HIS -10 ? B HIS 10  
55 1 Y 1 B SER -9  ? B SER 11  
56 1 Y 1 B SER -8  ? B SER 12  
57 1 Y 1 B GLY -7  ? B GLY 13  
58 1 Y 1 B LEU -6  ? B LEU 14  
59 1 Y 1 B VAL -5  ? B VAL 15  
60 1 Y 1 B PRO -4  ? B PRO 16  
61 1 Y 1 B ARG -3  ? B ARG 17  
62 1 Y 1 B GLY -2  ? B GLY 18  
63 1 Y 1 B SER -1  ? B SER 19  
64 1 Y 1 B HIS 0   ? B HIS 20  
65 1 Y 1 B LEU 89  ? B LEU 109 
66 1 Y 1 B LYS 90  ? B LYS 110 
67 1 Y 1 B ASN 91  ? B ASN 111 
68 1 Y 1 B GLY 92  ? B GLY 112 
69 1 Y 1 B GLN 93  ? B GLN 113 
70 1 Y 1 B VAL 94  ? B VAL 114 
71 1 Y 1 B ASP 95  ? B ASP 115 
72 1 Y 1 B GLU 204 ? B GLU 224 
73 1 Y 1 B ALA 205 ? B ALA 225 
74 1 Y 1 B THR 206 ? B THR 226 
75 1 Y 1 B ALA 207 ? B ALA 227 
76 1 Y 1 B THR 208 ? B THR 228 
77 1 Y 1 B ASP 209 ? B ASP 229 
78 1 Y 1 B ALA 210 ? B ALA 230 
79 1 Y 1 B SER 211 ? B SER 231 
80 1 Y 1 B LYS 212 ? B LYS 232 
81 1 Y 1 B GLU 213 ? B GLU 233 
82 1 Y 1 B SER 214 ? B SER 234 
83 1 Y 1 B ASN 215 ? B ASN 235 
84 1 Y 1 B LYS 216 ? B LYS 236 
85 1 Y 1 B GLU 217 ? B GLU 237 
86 1 Y 1 B GLU 218 ? B GLU 238 
87 1 Y 1 B GLU 219 ? B GLU 239 
88 1 Y 1 B GLY 220 ? B GLY 240 
89 1 Y 1 B ASP 221 ? B ASP 241 
90 1 Y 1 B GLU 222 ? B GLU 242 
91 1 Y 1 B ASP 223 ? B ASP 243 
92 1 Y 1 B ASP 224 ? B ASP 244 
93 1 Y 1 B TRP 225 ? B TRP 245 
# 
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  
BU3 O6     O  N N 74  
BU3 C3     C  N R 75  
BU3 C4     C  N N 76  
BU3 C2     C  N R 77  
BU3 O5     O  N N 78  
BU3 C1     C  N N 79  
BU3 HO6    H  N N 80  
BU3 H3     H  N N 81  
BU3 H41    H  N N 82  
BU3 H42    H  N N 83  
BU3 H43    H  N N 84  
BU3 H2     H  N N 85  
BU3 HO5    H  N N 86  
BU3 H11    H  N N 87  
BU3 H12    H  N N 88  
BU3 H13    H  N N 89  
CL  CL     CL N N 90  
CYS N      N  N N 91  
CYS CA     C  N R 92  
CYS C      C  N N 93  
CYS O      O  N N 94  
CYS CB     C  N N 95  
CYS SG     S  N N 96  
CYS OXT    O  N N 97  
CYS H      H  N N 98  
CYS H2     H  N N 99  
CYS HA     H  N N 100 
CYS HB2    H  N N 101 
CYS HB3    H  N N 102 
CYS HG     H  N N 103 
CYS HXT    H  N N 104 
EDO C1     C  N N 105 
EDO O1     O  N N 106 
EDO C2     C  N N 107 
EDO O2     O  N N 108 
EDO H11    H  N N 109 
EDO H12    H  N N 110 
EDO HO1    H  N N 111 
EDO H21    H  N N 112 
EDO H22    H  N N 113 
EDO HO2    H  N N 114 
GLN N      N  N N 115 
GLN CA     C  N S 116 
GLN C      C  N N 117 
GLN O      O  N N 118 
GLN CB     C  N N 119 
GLN CG     C  N N 120 
GLN CD     C  N N 121 
GLN OE1    O  N N 122 
GLN NE2    N  N N 123 
GLN OXT    O  N N 124 
GLN H      H  N N 125 
GLN H2     H  N N 126 
GLN HA     H  N N 127 
GLN HB2    H  N N 128 
GLN HB3    H  N N 129 
GLN HG2    H  N N 130 
GLN HG3    H  N N 131 
GLN HE21   H  N N 132 
GLN HE22   H  N N 133 
GLN HXT    H  N N 134 
GLU N      N  N N 135 
GLU CA     C  N S 136 
GLU C      C  N N 137 
GLU O      O  N N 138 
GLU CB     C  N N 139 
GLU CG     C  N N 140 
GLU CD     C  N N 141 
GLU OE1    O  N N 142 
GLU OE2    O  N N 143 
GLU OXT    O  N N 144 
GLU H      H  N N 145 
GLU H2     H  N N 146 
GLU HA     H  N N 147 
GLU HB2    H  N N 148 
GLU HB3    H  N N 149 
GLU HG2    H  N N 150 
GLU HG3    H  N N 151 
GLU HE2    H  N N 152 
GLU HXT    H  N N 153 
GLY N      N  N N 154 
GLY CA     C  N N 155 
GLY C      C  N N 156 
GLY O      O  N N 157 
GLY OXT    O  N N 158 
GLY H      H  N N 159 
GLY H2     H  N N 160 
GLY HA2    H  N N 161 
GLY HA3    H  N N 162 
GLY HXT    H  N N 163 
HIS N      N  N N 164 
HIS CA     C  N S 165 
HIS C      C  N N 166 
HIS O      O  N N 167 
HIS CB     C  N N 168 
HIS CG     C  Y N 169 
HIS ND1    N  Y N 170 
HIS CD2    C  Y N 171 
HIS CE1    C  Y N 172 
HIS NE2    N  Y N 173 
HIS OXT    O  N N 174 
HIS H      H  N N 175 
HIS H2     H  N N 176 
HIS HA     H  N N 177 
HIS HB2    H  N N 178 
HIS HB3    H  N N 179 
HIS HD1    H  N N 180 
HIS HD2    H  N N 181 
HIS HE1    H  N N 182 
HIS HE2    H  N N 183 
HIS HXT    H  N N 184 
HOH O      O  N N 185 
HOH H1     H  N N 186 
HOH H2     H  N N 187 
ILE N      N  N N 188 
ILE CA     C  N S 189 
ILE C      C  N N 190 
ILE O      O  N N 191 
ILE CB     C  N S 192 
ILE CG1    C  N N 193 
ILE CG2    C  N N 194 
ILE CD1    C  N N 195 
ILE OXT    O  N N 196 
ILE H      H  N N 197 
ILE H2     H  N N 198 
ILE HA     H  N N 199 
ILE HB     H  N N 200 
ILE HG12   H  N N 201 
ILE HG13   H  N N 202 
ILE HG21   H  N N 203 
ILE HG22   H  N N 204 
ILE HG23   H  N N 205 
ILE HD11   H  N N 206 
ILE HD12   H  N N 207 
ILE HD13   H  N N 208 
ILE HXT    H  N N 209 
LEU N      N  N N 210 
LEU CA     C  N S 211 
LEU C      C  N N 212 
LEU O      O  N N 213 
LEU CB     C  N N 214 
LEU CG     C  N N 215 
LEU CD1    C  N N 216 
LEU CD2    C  N N 217 
LEU OXT    O  N N 218 
LEU H      H  N N 219 
LEU H2     H  N N 220 
LEU HA     H  N N 221 
LEU HB2    H  N N 222 
LEU HB3    H  N N 223 
LEU HG     H  N N 224 
LEU HD11   H  N N 225 
LEU HD12   H  N N 226 
LEU HD13   H  N N 227 
LEU HD21   H  N N 228 
LEU HD22   H  N N 229 
LEU HD23   H  N N 230 
LEU HXT    H  N N 231 
LYS N      N  N N 232 
LYS CA     C  N S 233 
LYS C      C  N N 234 
LYS O      O  N N 235 
LYS CB     C  N N 236 
LYS CG     C  N N 237 
LYS CD     C  N N 238 
LYS CE     C  N N 239 
LYS NZ     N  N N 240 
LYS OXT    O  N N 241 
LYS H      H  N N 242 
LYS H2     H  N N 243 
LYS HA     H  N N 244 
LYS HB2    H  N N 245 
LYS HB3    H  N N 246 
LYS HG2    H  N N 247 
LYS HG3    H  N N 248 
LYS HD2    H  N N 249 
LYS HD3    H  N N 250 
LYS HE2    H  N N 251 
LYS HE3    H  N N 252 
LYS HZ1    H  N N 253 
LYS HZ2    H  N N 254 
LYS HZ3    H  N N 255 
LYS HXT    H  N N 256 
MET N      N  N N 257 
MET CA     C  N S 258 
MET C      C  N N 259 
MET O      O  N N 260 
MET CB     C  N N 261 
MET CG     C  N N 262 
MET SD     S  N N 263 
MET CE     C  N N 264 
MET OXT    O  N N 265 
MET H      H  N N 266 
MET H2     H  N N 267 
MET HA     H  N N 268 
MET HB2    H  N N 269 
MET HB3    H  N N 270 
MET HG2    H  N N 271 
MET HG3    H  N N 272 
MET HE1    H  N N 273 
MET HE2    H  N N 274 
MET HE3    H  N N 275 
MET HXT    H  N N 276 
MN  MN     MN N N 277 
PHE N      N  N N 278 
PHE CA     C  N S 279 
PHE C      C  N N 280 
PHE O      O  N N 281 
PHE CB     C  N N 282 
PHE CG     C  Y N 283 
PHE CD1    C  Y N 284 
PHE CD2    C  Y N 285 
PHE CE1    C  Y N 286 
PHE CE2    C  Y N 287 
PHE CZ     C  Y N 288 
PHE OXT    O  N N 289 
PHE H      H  N N 290 
PHE H2     H  N N 291 
PHE HA     H  N N 292 
PHE HB2    H  N N 293 
PHE HB3    H  N N 294 
PHE HD1    H  N N 295 
PHE HD2    H  N N 296 
PHE HE1    H  N N 297 
PHE HE2    H  N N 298 
PHE HZ     H  N N 299 
PHE HXT    H  N N 300 
PRO N      N  N N 301 
PRO CA     C  N S 302 
PRO C      C  N N 303 
PRO O      O  N N 304 
PRO CB     C  N N 305 
PRO CG     C  N N 306 
PRO CD     C  N N 307 
PRO OXT    O  N N 308 
PRO H      H  N N 309 
PRO HA     H  N N 310 
PRO HB2    H  N N 311 
PRO HB3    H  N N 312 
PRO HG2    H  N N 313 
PRO HG3    H  N N 314 
PRO HD2    H  N N 315 
PRO HD3    H  N N 316 
PRO HXT    H  N N 317 
SER N      N  N N 318 
SER CA     C  N S 319 
SER C      C  N N 320 
SER O      O  N N 321 
SER CB     C  N N 322 
SER OG     O  N N 323 
SER OXT    O  N N 324 
SER H      H  N N 325 
SER H2     H  N N 326 
SER HA     H  N N 327 
SER HB2    H  N N 328 
SER HB3    H  N N 329 
SER HG     H  N N 330 
SER HXT    H  N N 331 
THM "O5'"  O  N N 332 
THM "C5'"  C  N N 333 
THM "C4'"  C  N R 334 
THM "O4'"  O  N N 335 
THM "C3'"  C  N S 336 
THM "O3'"  O  N N 337 
THM "C2'"  C  N N 338 
THM "C1'"  C  N R 339 
THM N1     N  N N 340 
THM C2     C  N N 341 
THM O2     O  N N 342 
THM N3     N  N N 343 
THM C4     C  N N 344 
THM O4     O  N N 345 
THM C5     C  N N 346 
THM C5M    C  N N 347 
THM C6     C  N N 348 
THM "HO5'" H  N N 349 
THM "H5'1" H  N N 350 
THM "H5'2" H  N N 351 
THM "H4'"  H  N N 352 
THM "H3'"  H  N N 353 
THM "HO3'" H  N N 354 
THM "H2'1" H  N N 355 
THM "H2'2" H  N N 356 
THM "H1'"  H  N N 357 
THM HN3    H  N N 358 
THM HM51   H  N N 359 
THM HM52   H  N N 360 
THM HM53   H  N N 361 
THM H6     H  N N 362 
THR N      N  N N 363 
THR CA     C  N S 364 
THR C      C  N N 365 
THR O      O  N N 366 
THR CB     C  N R 367 
THR OG1    O  N N 368 
THR CG2    C  N N 369 
THR OXT    O  N N 370 
THR H      H  N N 371 
THR H2     H  N N 372 
THR HA     H  N N 373 
THR HB     H  N N 374 
THR HG1    H  N N 375 
THR HG21   H  N N 376 
THR HG22   H  N N 377 
THR HG23   H  N N 378 
THR HXT    H  N N 379 
TRP N      N  N N 380 
TRP CA     C  N S 381 
TRP C      C  N N 382 
TRP O      O  N N 383 
TRP CB     C  N N 384 
TRP CG     C  Y N 385 
TRP CD1    C  Y N 386 
TRP CD2    C  Y N 387 
TRP NE1    N  Y N 388 
TRP CE2    C  Y N 389 
TRP CE3    C  Y N 390 
TRP CZ2    C  Y N 391 
TRP CZ3    C  Y N 392 
TRP CH2    C  Y N 393 
TRP OXT    O  N N 394 
TRP H      H  N N 395 
TRP H2     H  N N 396 
TRP HA     H  N N 397 
TRP HB2    H  N N 398 
TRP HB3    H  N N 399 
TRP HD1    H  N N 400 
TRP HE1    H  N N 401 
TRP HE3    H  N N 402 
TRP HZ2    H  N N 403 
TRP HZ3    H  N N 404 
TRP HH2    H  N N 405 
TRP HXT    H  N N 406 
TYR N      N  N N 407 
TYR CA     C  N S 408 
TYR C      C  N N 409 
TYR O      O  N N 410 
TYR CB     C  N N 411 
TYR CG     C  Y N 412 
TYR CD1    C  Y N 413 
TYR CD2    C  Y N 414 
TYR CE1    C  Y N 415 
TYR CE2    C  Y N 416 
TYR CZ     C  Y N 417 
TYR OH     O  N N 418 
TYR OXT    O  N N 419 
TYR H      H  N N 420 
TYR H2     H  N N 421 
TYR HA     H  N N 422 
TYR HB2    H  N N 423 
TYR HB3    H  N N 424 
TYR HD1    H  N N 425 
TYR HD2    H  N N 426 
TYR HE1    H  N N 427 
TYR HE2    H  N N 428 
TYR HH     H  N N 429 
TYR HXT    H  N N 430 
VAL N      N  N N 431 
VAL CA     C  N S 432 
VAL C      C  N N 433 
VAL O      O  N N 434 
VAL CB     C  N N 435 
VAL CG1    C  N N 436 
VAL CG2    C  N N 437 
VAL OXT    O  N N 438 
VAL H      H  N N 439 
VAL H2     H  N N 440 
VAL HA     H  N N 441 
VAL HB     H  N N 442 
VAL HG11   H  N N 443 
VAL HG12   H  N N 444 
VAL HG13   H  N N 445 
VAL HG21   H  N N 446 
VAL HG22   H  N N 447 
VAL HG23   H  N N 448 
VAL HXT    H  N N 449 
# 
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  
BU3 O6    C3     sing N N 70  
BU3 O6    HO6    sing N N 71  
BU3 C3    C4     sing N N 72  
BU3 C3    C2     sing N N 73  
BU3 C3    H3     sing N N 74  
BU3 C4    H41    sing N N 75  
BU3 C4    H42    sing N N 76  
BU3 C4    H43    sing N N 77  
BU3 C2    O5     sing N N 78  
BU3 C2    C1     sing N N 79  
BU3 C2    H2     sing N N 80  
BU3 O5    HO5    sing N N 81  
BU3 C1    H11    sing N N 82  
BU3 C1    H12    sing N N 83  
BU3 C1    H13    sing N N 84  
CYS N     CA     sing N N 85  
CYS N     H      sing N N 86  
CYS N     H2     sing N N 87  
CYS CA    C      sing N N 88  
CYS CA    CB     sing N N 89  
CYS CA    HA     sing N N 90  
CYS C     O      doub N N 91  
CYS C     OXT    sing N N 92  
CYS CB    SG     sing N N 93  
CYS CB    HB2    sing N N 94  
CYS CB    HB3    sing N N 95  
CYS SG    HG     sing N N 96  
CYS OXT   HXT    sing N N 97  
EDO C1    O1     sing N N 98  
EDO C1    C2     sing N N 99  
EDO C1    H11    sing N N 100 
EDO C1    H12    sing N N 101 
EDO O1    HO1    sing N N 102 
EDO C2    O2     sing N N 103 
EDO C2    H21    sing N N 104 
EDO C2    H22    sing N N 105 
EDO O2    HO2    sing N N 106 
GLN N     CA     sing N N 107 
GLN N     H      sing N N 108 
GLN N     H2     sing N N 109 
GLN CA    C      sing N N 110 
GLN CA    CB     sing N N 111 
GLN CA    HA     sing N N 112 
GLN C     O      doub N N 113 
GLN C     OXT    sing N N 114 
GLN CB    CG     sing N N 115 
GLN CB    HB2    sing N N 116 
GLN CB    HB3    sing N N 117 
GLN CG    CD     sing N N 118 
GLN CG    HG2    sing N N 119 
GLN CG    HG3    sing N N 120 
GLN CD    OE1    doub N N 121 
GLN CD    NE2    sing N N 122 
GLN NE2   HE21   sing N N 123 
GLN NE2   HE22   sing N N 124 
GLN OXT   HXT    sing N N 125 
GLU N     CA     sing N N 126 
GLU N     H      sing N N 127 
GLU N     H2     sing N N 128 
GLU CA    C      sing N N 129 
GLU CA    CB     sing N N 130 
GLU CA    HA     sing N N 131 
GLU C     O      doub N N 132 
GLU C     OXT    sing N N 133 
GLU CB    CG     sing N N 134 
GLU CB    HB2    sing N N 135 
GLU CB    HB3    sing N N 136 
GLU CG    CD     sing N N 137 
GLU CG    HG2    sing N N 138 
GLU CG    HG3    sing N N 139 
GLU CD    OE1    doub N N 140 
GLU CD    OE2    sing N N 141 
GLU OE2   HE2    sing N N 142 
GLU OXT   HXT    sing N N 143 
GLY N     CA     sing N N 144 
GLY N     H      sing N N 145 
GLY N     H2     sing N N 146 
GLY CA    C      sing N N 147 
GLY CA    HA2    sing N N 148 
GLY CA    HA3    sing N N 149 
GLY C     O      doub N N 150 
GLY C     OXT    sing N N 151 
GLY OXT   HXT    sing N N 152 
HIS N     CA     sing N N 153 
HIS N     H      sing N N 154 
HIS N     H2     sing N N 155 
HIS CA    C      sing N N 156 
HIS CA    CB     sing N N 157 
HIS CA    HA     sing N N 158 
HIS C     O      doub N N 159 
HIS C     OXT    sing N N 160 
HIS CB    CG     sing N N 161 
HIS CB    HB2    sing N N 162 
HIS CB    HB3    sing N N 163 
HIS CG    ND1    sing Y N 164 
HIS CG    CD2    doub Y N 165 
HIS ND1   CE1    doub Y N 166 
HIS ND1   HD1    sing N N 167 
HIS CD2   NE2    sing Y N 168 
HIS CD2   HD2    sing N N 169 
HIS CE1   NE2    sing Y N 170 
HIS CE1   HE1    sing N N 171 
HIS NE2   HE2    sing N N 172 
HIS OXT   HXT    sing N N 173 
HOH O     H1     sing N N 174 
HOH O     H2     sing N N 175 
ILE N     CA     sing N N 176 
ILE N     H      sing N N 177 
ILE N     H2     sing N N 178 
ILE CA    C      sing N N 179 
ILE CA    CB     sing N N 180 
ILE CA    HA     sing N N 181 
ILE C     O      doub N N 182 
ILE C     OXT    sing N N 183 
ILE CB    CG1    sing N N 184 
ILE CB    CG2    sing N N 185 
ILE CB    HB     sing N N 186 
ILE CG1   CD1    sing N N 187 
ILE CG1   HG12   sing N N 188 
ILE CG1   HG13   sing N N 189 
ILE CG2   HG21   sing N N 190 
ILE CG2   HG22   sing N N 191 
ILE CG2   HG23   sing N N 192 
ILE CD1   HD11   sing N N 193 
ILE CD1   HD12   sing N N 194 
ILE CD1   HD13   sing N N 195 
ILE OXT   HXT    sing N N 196 
LEU N     CA     sing N N 197 
LEU N     H      sing N N 198 
LEU N     H2     sing N N 199 
LEU CA    C      sing N N 200 
LEU CA    CB     sing N N 201 
LEU CA    HA     sing N N 202 
LEU C     O      doub N N 203 
LEU C     OXT    sing N N 204 
LEU CB    CG     sing N N 205 
LEU CB    HB2    sing N N 206 
LEU CB    HB3    sing N N 207 
LEU CG    CD1    sing N N 208 
LEU CG    CD2    sing N N 209 
LEU CG    HG     sing N N 210 
LEU CD1   HD11   sing N N 211 
LEU CD1   HD12   sing N N 212 
LEU CD1   HD13   sing N N 213 
LEU CD2   HD21   sing N N 214 
LEU CD2   HD22   sing N N 215 
LEU CD2   HD23   sing N N 216 
LEU OXT   HXT    sing N N 217 
LYS N     CA     sing N N 218 
LYS N     H      sing N N 219 
LYS N     H2     sing N N 220 
LYS CA    C      sing N N 221 
LYS CA    CB     sing N N 222 
LYS CA    HA     sing N N 223 
LYS C     O      doub N N 224 
LYS C     OXT    sing N N 225 
LYS CB    CG     sing N N 226 
LYS CB    HB2    sing N N 227 
LYS CB    HB3    sing N N 228 
LYS CG    CD     sing N N 229 
LYS CG    HG2    sing N N 230 
LYS CG    HG3    sing N N 231 
LYS CD    CE     sing N N 232 
LYS CD    HD2    sing N N 233 
LYS CD    HD3    sing N N 234 
LYS CE    NZ     sing N N 235 
LYS CE    HE2    sing N N 236 
LYS CE    HE3    sing N N 237 
LYS NZ    HZ1    sing N N 238 
LYS NZ    HZ2    sing N N 239 
LYS NZ    HZ3    sing N N 240 
LYS OXT   HXT    sing N N 241 
MET N     CA     sing N N 242 
MET N     H      sing N N 243 
MET N     H2     sing N N 244 
MET CA    C      sing N N 245 
MET CA    CB     sing N N 246 
MET CA    HA     sing N N 247 
MET C     O      doub N N 248 
MET C     OXT    sing N N 249 
MET CB    CG     sing N N 250 
MET CB    HB2    sing N N 251 
MET CB    HB3    sing N N 252 
MET CG    SD     sing N N 253 
MET CG    HG2    sing N N 254 
MET CG    HG3    sing N N 255 
MET SD    CE     sing N N 256 
MET CE    HE1    sing N N 257 
MET CE    HE2    sing N N 258 
MET CE    HE3    sing N N 259 
MET OXT   HXT    sing N N 260 
PHE N     CA     sing N N 261 
PHE N     H      sing N N 262 
PHE N     H2     sing N N 263 
PHE CA    C      sing N N 264 
PHE CA    CB     sing N N 265 
PHE CA    HA     sing N N 266 
PHE C     O      doub N N 267 
PHE C     OXT    sing N N 268 
PHE CB    CG     sing N N 269 
PHE CB    HB2    sing N N 270 
PHE CB    HB3    sing N N 271 
PHE CG    CD1    doub Y N 272 
PHE CG    CD2    sing Y N 273 
PHE CD1   CE1    sing Y N 274 
PHE CD1   HD1    sing N N 275 
PHE CD2   CE2    doub Y N 276 
PHE CD2   HD2    sing N N 277 
PHE CE1   CZ     doub Y N 278 
PHE CE1   HE1    sing N N 279 
PHE CE2   CZ     sing Y N 280 
PHE CE2   HE2    sing N N 281 
PHE CZ    HZ     sing N N 282 
PHE OXT   HXT    sing N N 283 
PRO N     CA     sing N N 284 
PRO N     CD     sing N N 285 
PRO N     H      sing N N 286 
PRO CA    C      sing N N 287 
PRO CA    CB     sing N N 288 
PRO CA    HA     sing N N 289 
PRO C     O      doub N N 290 
PRO C     OXT    sing N N 291 
PRO CB    CG     sing N N 292 
PRO CB    HB2    sing N N 293 
PRO CB    HB3    sing N N 294 
PRO CG    CD     sing N N 295 
PRO CG    HG2    sing N N 296 
PRO CG    HG3    sing N N 297 
PRO CD    HD2    sing N N 298 
PRO CD    HD3    sing N N 299 
PRO OXT   HXT    sing N N 300 
SER N     CA     sing N N 301 
SER N     H      sing N N 302 
SER N     H2     sing N N 303 
SER CA    C      sing N N 304 
SER CA    CB     sing N N 305 
SER CA    HA     sing N N 306 
SER C     O      doub N N 307 
SER C     OXT    sing N N 308 
SER CB    OG     sing N N 309 
SER CB    HB2    sing N N 310 
SER CB    HB3    sing N N 311 
SER OG    HG     sing N N 312 
SER OXT   HXT    sing N N 313 
THM "O5'" "C5'"  sing N N 314 
THM "O5'" "HO5'" sing N N 315 
THM "C5'" "C4'"  sing N N 316 
THM "C5'" "H5'1" sing N N 317 
THM "C5'" "H5'2" sing N N 318 
THM "C4'" "O4'"  sing N N 319 
THM "C4'" "C3'"  sing N N 320 
THM "C4'" "H4'"  sing N N 321 
THM "O4'" "C1'"  sing N N 322 
THM "C3'" "O3'"  sing N N 323 
THM "C3'" "C2'"  sing N N 324 
THM "C3'" "H3'"  sing N N 325 
THM "O3'" "HO3'" sing N N 326 
THM "C2'" "C1'"  sing N N 327 
THM "C2'" "H2'1" sing N N 328 
THM "C2'" "H2'2" sing N N 329 
THM "C1'" N1     sing N N 330 
THM "C1'" "H1'"  sing N N 331 
THM N1    C2     sing N N 332 
THM N1    C6     sing N N 333 
THM C2    O2     doub N N 334 
THM C2    N3     sing N N 335 
THM N3    C4     sing N N 336 
THM N3    HN3    sing N N 337 
THM C4    O4     doub N N 338 
THM C4    C5     sing N N 339 
THM C5    C5M    sing N N 340 
THM C5    C6     doub N N 341 
THM C5M   HM51   sing N N 342 
THM C5M   HM52   sing N N 343 
THM C5M   HM53   sing N N 344 
THM C6    H6     sing N N 345 
THR N     CA     sing N N 346 
THR N     H      sing N N 347 
THR N     H2     sing N N 348 
THR CA    C      sing N N 349 
THR CA    CB     sing N N 350 
THR CA    HA     sing N N 351 
THR C     O      doub N N 352 
THR C     OXT    sing N N 353 
THR CB    OG1    sing N N 354 
THR CB    CG2    sing N N 355 
THR CB    HB     sing N N 356 
THR OG1   HG1    sing N N 357 
THR CG2   HG21   sing N N 358 
THR CG2   HG22   sing N N 359 
THR CG2   HG23   sing N N 360 
THR OXT   HXT    sing N N 361 
TRP N     CA     sing N N 362 
TRP N     H      sing N N 363 
TRP N     H2     sing N N 364 
TRP CA    C      sing N N 365 
TRP CA    CB     sing N N 366 
TRP CA    HA     sing N N 367 
TRP C     O      doub N N 368 
TRP C     OXT    sing N N 369 
TRP CB    CG     sing N N 370 
TRP CB    HB2    sing N N 371 
TRP CB    HB3    sing N N 372 
TRP CG    CD1    doub Y N 373 
TRP CG    CD2    sing Y N 374 
TRP CD1   NE1    sing Y N 375 
TRP CD1   HD1    sing N N 376 
TRP CD2   CE2    doub Y N 377 
TRP CD2   CE3    sing Y N 378 
TRP NE1   CE2    sing Y N 379 
TRP NE1   HE1    sing N N 380 
TRP CE2   CZ2    sing Y N 381 
TRP CE3   CZ3    doub Y N 382 
TRP CE3   HE3    sing N N 383 
TRP CZ2   CH2    doub Y N 384 
TRP CZ2   HZ2    sing N N 385 
TRP CZ3   CH2    sing Y N 386 
TRP CZ3   HZ3    sing N N 387 
TRP CH2   HH2    sing N N 388 
TRP OXT   HXT    sing N N 389 
TYR N     CA     sing N N 390 
TYR N     H      sing N N 391 
TYR N     H2     sing N N 392 
TYR CA    C      sing N N 393 
TYR CA    CB     sing N N 394 
TYR CA    HA     sing N N 395 
TYR C     O      doub N N 396 
TYR C     OXT    sing N N 397 
TYR CB    CG     sing N N 398 
TYR CB    HB2    sing N N 399 
TYR CB    HB3    sing N N 400 
TYR CG    CD1    doub Y N 401 
TYR CG    CD2    sing Y N 402 
TYR CD1   CE1    sing Y N 403 
TYR CD1   HD1    sing N N 404 
TYR CD2   CE2    doub Y N 405 
TYR CD2   HD2    sing N N 406 
TYR CE1   CZ     doub Y N 407 
TYR CE1   HE1    sing N N 408 
TYR CE2   CZ     sing Y N 409 
TYR CE2   HE2    sing N N 410 
TYR CZ    OH     sing N N 411 
TYR OH    HH     sing N N 412 
TYR OXT   HXT    sing N N 413 
VAL N     CA     sing N N 414 
VAL N     H      sing N N 415 
VAL N     H2     sing N N 416 
VAL CA    C      sing N N 417 
VAL CA    CB     sing N N 418 
VAL CA    HA     sing N N 419 
VAL C     O      doub N N 420 
VAL C     OXT    sing N N 421 
VAL CB    CG1    sing N N 422 
VAL CB    CG2    sing N N 423 
VAL CB    HB     sing N N 424 
VAL CG1   HG11   sing N N 425 
VAL CG1   HG12   sing N N 426 
VAL CG1   HG13   sing N N 427 
VAL CG2   HG21   sing N N 428 
VAL CG2   HG22   sing N N 429 
VAL CG2   HG23   sing N N 430 
VAL OXT   HXT    sing N N 431 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HDM 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.017246 
_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]   0.009234 
_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]   0.008641 
_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  
CL 
MN 
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     . GLY A 1 13  ? -2.093  51.298  -36.600 1.00 69.90  ? -7  GLY A N     1 
ATOM   2    C  CA    . GLY A 1 13  ? -2.655  50.173  -37.326 1.00 59.24  ? -7  GLY A CA    1 
ATOM   3    C  C     . GLY A 1 13  ? -1.665  49.040  -37.509 1.00 61.86  ? -7  GLY A C     1 
ATOM   4    O  O     . GLY A 1 13  ? -0.690  49.171  -38.247 1.00 56.27  ? -7  GLY A O     1 
ATOM   5    N  N     . LEU A 1 14  ? -1.914  47.926  -36.822 1.00 47.72  ? -6  LEU A N     1 
ATOM   6    C  CA    . LEU A 1 14  ? -1.079  46.736  -36.913 1.00 37.94  ? -6  LEU A CA    1 
ATOM   7    C  C     . LEU A 1 14  ? -1.622  45.713  -37.899 1.00 37.58  ? -6  LEU A C     1 
ATOM   8    O  O     . LEU A 1 14  ? -0.849  45.068  -38.611 1.00 41.72  ? -6  LEU A O     1 
ATOM   9    C  CB    . LEU A 1 14  ? -0.949  46.083  -35.535 1.00 38.23  ? -6  LEU A CB    1 
ATOM   10   C  CG    . LEU A 1 14  ? -0.735  47.062  -34.383 1.00 38.77  ? -6  LEU A CG    1 
ATOM   11   C  CD1   . LEU A 1 14  ? -0.770  46.331  -33.055 1.00 46.81  ? -6  LEU A CD1   1 
ATOM   12   C  CD2   . LEU A 1 14  ? 0.568   47.816  -34.548 1.00 48.54  ? -6  LEU A CD2   1 
ATOM   13   N  N     . VAL A 1 15  ? -2.939  45.556  -37.948 1.00 33.12  ? -5  VAL A N     1 
ATOM   14   C  CA    . VAL A 1 15  ? -3.615  44.581  -38.796 1.00 29.09  ? -5  VAL A CA    1 
ATOM   15   C  C     . VAL A 1 15  ? -4.387  45.402  -39.820 1.00 33.86  ? -5  VAL A C     1 
ATOM   16   O  O     . VAL A 1 15  ? -4.808  46.521  -39.497 1.00 33.56  ? -5  VAL A O     1 
ATOM   17   C  CB    . VAL A 1 15  ? -4.510  43.660  -37.945 1.00 35.16  ? -5  VAL A CB    1 
ATOM   18   C  CG1   . VAL A 1 15  ? -5.522  42.871  -38.771 1.00 37.75  ? -5  VAL A CG1   1 
ATOM   19   C  CG2   . VAL A 1 15  ? -3.635  42.716  -37.124 1.00 32.80  ? -5  VAL A CG2   1 
ATOM   20   N  N     . PRO A 1 16  ? -4.555  44.935  -41.059 1.00 30.14  ? -4  PRO A N     1 
ATOM   21   C  CA    . PRO A 1 16  ? -5.325  45.719  -42.031 1.00 32.15  ? -4  PRO A CA    1 
ATOM   22   C  C     . PRO A 1 16  ? -6.745  45.954  -41.536 1.00 31.72  ? -4  PRO A C     1 
ATOM   23   O  O     . PRO A 1 16  ? -7.376  45.064  -40.965 1.00 31.31  ? -4  PRO A O     1 
ATOM   24   C  CB    . PRO A 1 16  ? -5.304  44.843  -43.292 1.00 32.02  ? -4  PRO A CB    1 
ATOM   25   C  CG    . PRO A 1 16  ? -4.060  43.988  -43.133 1.00 28.88  ? -4  PRO A CG    1 
ATOM   26   C  CD    . PRO A 1 16  ? -4.026  43.689  -41.653 1.00 26.63  ? -4  PRO A CD    1 
ATOM   27   N  N     . ARG A 1 17  ? -7.227  47.178  -41.744 1.00 39.50  ? -3  ARG A N     1 
ATOM   28   C  CA    . ARG A 1 17  ? -8.606  47.538  -41.446 1.00 48.90  ? -3  ARG A CA    1 
ATOM   29   C  C     . ARG A 1 17  ? -9.552  46.973  -42.502 1.00 47.61  ? -3  ARG A C     1 
ATOM   30   O  O     . ARG A 1 17  ? -9.159  46.665  -43.631 1.00 40.75  ? -3  ARG A O     1 
ATOM   31   C  CB    . ARG A 1 17  ? -8.759  49.060  -41.382 1.00 48.46  ? -3  ARG A CB    1 
ATOM   32   C  CG    . ARG A 1 17  ? -8.454  49.672  -40.025 1.00 55.65  ? -3  ARG A CG    1 
ATOM   33   C  CD    . ARG A 1 17  ? -7.782  51.030  -40.170 1.00 61.54  ? -3  ARG A CD    1 
ATOM   34   N  NE    . ARG A 1 17  ? -8.455  51.892  -41.136 1.00 64.18  ? -3  ARG A NE    1 
ATOM   35   C  CZ    . ARG A 1 17  ? -7.934  53.007  -41.631 1.00 60.93  ? -3  ARG A CZ    1 
ATOM   36   N  NH1   . ARG A 1 17  ? -6.729  53.425  -41.277 1.00 61.29  ? -3  ARG A NH1   1 
ATOM   37   N  NH2   . ARG A 1 17  ? -8.637  53.719  -42.507 1.00 58.21  ? -3  ARG A NH2   1 
ATOM   38   N  N     . GLY A 1 18  ? -10.822 46.847  -42.122 1.00 35.29  ? -2  GLY A N     1 
ATOM   39   C  CA    . GLY A 1 18  ? -11.842 46.413  -43.056 1.00 34.94  ? -2  GLY A CA    1 
ATOM   40   C  C     . GLY A 1 18  ? -11.854 44.921  -43.300 1.00 38.32  ? -2  GLY A C     1 
ATOM   41   O  O     . GLY A 1 18  ? -11.621 44.129  -42.382 1.00 39.21  ? -2  GLY A O     1 
ATOM   42   N  N     . SER A 1 19  ? -12.129 44.528  -44.543 1.00 34.08  ? -1  SER A N     1 
ATOM   43   C  CA    . SER A 1 19  ? -12.221 43.123  -44.914 1.00 31.79  ? -1  SER A CA    1 
ATOM   44   C  C     . SER A 1 19  ? -10.869 42.496  -45.231 1.00 29.01  ? -1  SER A C     1 
ATOM   45   O  O     . SER A 1 19  ? -10.808 41.276  -45.423 1.00 30.70  ? -1  SER A O     1 
ATOM   46   C  CB    . SER A 1 19  ? -13.147 42.963  -46.122 1.00 41.87  ? -1  SER A CB    1 
ATOM   47   O  OG    . SER A 1 19  ? -12.763 43.844  -47.170 1.00 53.57  ? -1  SER A OG    1 
ATOM   48   N  N     . HIS A 1 20  ? -9.799  43.286  -45.279 1.00 31.40  ? 0   HIS A N     1 
ATOM   49   C  CA    . HIS A 1 20  ? -8.489  42.765  -45.653 1.00 28.45  ? 0   HIS A CA    1 
ATOM   50   C  C     . HIS A 1 20  ? -7.888  41.964  -44.503 1.00 32.44  ? 0   HIS A C     1 
ATOM   51   O  O     . HIS A 1 20  ? -8.102  42.277  -43.329 1.00 32.13  ? 0   HIS A O     1 
ATOM   52   C  CB    . HIS A 1 20  ? -7.564  43.910  -46.068 1.00 27.98  ? 0   HIS A CB    1 
ATOM   53   C  CG    . HIS A 1 20  ? -8.167  44.813  -47.100 1.00 24.82  ? 0   HIS A CG    1 
ATOM   54   N  ND1   . HIS A 1 20  ? -8.724  44.334  -48.264 1.00 24.43  ? 0   HIS A ND1   1 
ATOM   55   C  CD2   . HIS A 1 20  ? -8.344  46.154  -47.119 1.00 29.29  ? 0   HIS A CD2   1 
ATOM   56   C  CE1   . HIS A 1 20  ? -9.211  45.344  -48.963 1.00 27.69  ? 0   HIS A CE1   1 
ATOM   57   N  NE2   . HIS A 1 20  ? -8.983  46.461  -48.295 1.00 28.82  ? 0   HIS A NE2   1 
ATOM   58   N  N     . MET A 1 21  ? -7.139  40.922  -44.853 1.00 23.44  ? 1   MET A N     1 
ATOM   59   C  CA    . MET A 1 21  ? -6.656  39.923  -43.911 1.00 23.42  ? 1   MET A CA    1 
ATOM   60   C  C     . MET A 1 21  ? -5.156  40.060  -43.694 1.00 25.09  ? 1   MET A C     1 
ATOM   61   O  O     . MET A 1 21  ? -4.408  40.399  -44.615 1.00 25.63  ? 1   MET A O     1 
ATOM   62   C  CB    . MET A 1 21  ? -6.944  38.520  -44.435 1.00 26.75  ? 1   MET A CB    1 
ATOM   63   C  CG    . MET A 1 21  ? -8.368  38.325  -44.862 1.00 38.33  ? 1   MET A CG    1 
ATOM   64   S  SD    . MET A 1 21  ? -9.462  38.244  -43.449 1.00 36.70  ? 1   MET A SD    1 
ATOM   65   C  CE    . MET A 1 21  ? -9.013  36.653  -42.763 1.00 32.55  ? 1   MET A CE    1 
ATOM   66   N  N     . ALA A 1 22  ? -4.721  39.791  -42.463 1.00 21.93  ? 2   ALA A N     1 
ATOM   67   C  CA    . ALA A 1 22  ? -3.300  39.653  -42.188 1.00 23.70  ? 2   ALA A CA    1 
ATOM   68   C  C     . ALA A 1 22  ? -2.826  38.280  -42.658 1.00 19.15  ? 2   ALA A C     1 
ATOM   69   O  O     . ALA A 1 22  ? -3.613  37.333  -42.725 1.00 23.09  ? 2   ALA A O     1 
ATOM   70   C  CB    . ALA A 1 22  ? -3.027  39.804  -40.688 1.00 22.15  ? 2   ALA A CB    1 
ATOM   71   N  N     . PRO A 1 23  ? -1.539  38.143  -42.994 1.00 21.67  ? 3   PRO A N     1 
ATOM   72   C  CA    . PRO A 1 23  ? -1.009  36.813  -43.298 1.00 22.31  ? 3   PRO A CA    1 
ATOM   73   C  C     . PRO A 1 23  ? -1.078  35.923  -42.069 1.00 23.08  ? 3   PRO A C     1 
ATOM   74   O  O     . PRO A 1 23  ? -1.041  36.401  -40.932 1.00 22.01  ? 3   PRO A O     1 
ATOM   75   C  CB    . PRO A 1 23  ? 0.447   37.084  -43.703 1.00 24.44  ? 3   PRO A CB    1 
ATOM   76   C  CG    . PRO A 1 23  ? 0.529   38.564  -43.960 1.00 30.49  ? 3   PRO A CG    1 
ATOM   77   C  CD    . PRO A 1 23  ? -0.506  39.181  -43.055 1.00 24.07  ? 3   PRO A CD    1 
ATOM   78   N  N     . ILE A 1 24  ? -1.206  34.620  -42.305 1.00 21.36  ? 4   ILE A N     1 
ATOM   79   C  CA    . ILE A 1 24  ? -1.190  33.623  -41.239 1.00 18.83  ? 4   ILE A CA    1 
ATOM   80   C  C     . ILE A 1 24  ? 0.199   33.003  -41.174 1.00 27.83  ? 4   ILE A C     1 
ATOM   81   O  O     . ILE A 1 24  ? 0.772   32.641  -42.208 1.00 29.79  ? 4   ILE A O     1 
ATOM   82   C  CB    . ILE A 1 24  ? -2.261  32.541  -41.461 1.00 23.08  ? 4   ILE A CB    1 
ATOM   83   C  CG1   . ILE A 1 24  ? -3.668  33.151  -41.415 1.00 25.74  ? 4   ILE A CG1   1 
ATOM   84   C  CG2   . ILE A 1 24  ? -2.106  31.421  -40.419 1.00 23.48  ? 4   ILE A CG2   1 
ATOM   85   C  CD1   . ILE A 1 24  ? -4.732  32.307  -42.097 1.00 26.58  ? 4   ILE A CD1   1 
ATOM   86   N  N     . ALA A 1 25  ? 0.753   32.906  -39.969 1.00 23.53  ? 5   ALA A N     1 
ATOM   87   C  CA    . ALA A 1 25  ? 2.058   32.296  -39.747 1.00 20.86  ? 5   ALA A CA    1 
ATOM   88   C  C     . ALA A 1 25  ? 1.904   31.014  -38.933 1.00 24.70  ? 5   ALA A C     1 
ATOM   89   O  O     . ALA A 1 25  ? 1.029   30.906  -38.071 1.00 23.67  ? 5   ALA A O     1 
ATOM   90   C  CB    . ALA A 1 25  ? 2.994   33.263  -39.023 1.00 24.81  ? 5   ALA A CB    1 
ATOM   91   N  N     . GLN A 1 26  ? 2.779   30.050  -39.197 1.00 28.64  ? 6   GLN A N     1 
ATOM   92   C  CA    . GLN A 1 26  ? 2.759   28.766  -38.505 1.00 30.83  ? 6   GLN A CA    1 
ATOM   93   C  C     . GLN A 1 26  ? 3.637   28.822  -37.260 1.00 21.51  ? 6   GLN A C     1 
ATOM   94   O  O     . GLN A 1 26  ? 4.802   29.213  -37.342 1.00 26.40  ? 6   GLN A O     1 
ATOM   95   C  CB    . GLN A 1 26  ? 3.241   27.662  -39.451 1.00 38.53  ? 6   GLN A CB    1 
ATOM   96   C  CG    . GLN A 1 26  ? 3.471   26.312  -38.792 1.00 53.78  ? 6   GLN A CG    1 
ATOM   97   C  CD    . GLN A 1 26  ? 2.188   25.657  -38.326 1.00 59.72  ? 6   GLN A CD    1 
ATOM   98   O  OE1   . GLN A 1 26  ? 1.264   25.442  -39.114 1.00 63.72  ? 6   GLN A OE1   1 
ATOM   99   N  NE2   . GLN A 1 26  ? 2.124   25.331  -37.038 1.00 45.72  ? 6   GLN A NE2   1 
ATOM   100  N  N     . ALA A 1 27  ? 3.056   28.491  -36.105 1.00 23.76  ? 7   ALA A N     1 
ATOM   101  C  CA    . ALA A 1 27  ? 3.836   28.409  -34.876 1.00 25.88  ? 7   ALA A CA    1 
ATOM   102  C  C     . ALA A 1 27  ? 4.643   27.115  -34.840 1.00 21.10  ? 7   ALA A C     1 
ATOM   103  O  O     . ALA A 1 27  ? 4.224   26.081  -35.369 1.00 24.07  ? 7   ALA A O     1 
ATOM   104  C  CB    . ALA A 1 27  ? 2.930   28.487  -33.646 1.00 24.44  ? 7   ALA A CB    1 
ATOM   105  N  N     . VAL A 1 28  ? 5.810   27.185  -34.198 1.00 21.40  ? 8   VAL A N     1 
ATOM   106  C  CA    . VAL A 1 28  ? 6.611   25.991  -33.956 1.00 24.10  ? 8   VAL A CA    1 
ATOM   107  C  C     . VAL A 1 28  ? 5.801   24.991  -33.148 1.00 23.72  ? 8   VAL A C     1 
ATOM   108  O  O     . VAL A 1 28  ? 5.202   25.346  -32.126 1.00 21.40  ? 8   VAL A O     1 
ATOM   109  C  CB    . VAL A 1 28  ? 7.898   26.368  -33.212 1.00 22.99  ? 8   VAL A CB    1 
ATOM   110  C  CG1   . VAL A 1 28  ? 8.654   25.098  -32.756 1.00 23.58  ? 8   VAL A CG1   1 
ATOM   111  C  CG2   . VAL A 1 28  ? 8.789   27.281  -34.075 1.00 24.34  ? 8   VAL A CG2   1 
ATOM   112  N  N     . THR A 1 29  ? 5.802   23.733  -33.582 1.00 22.36  ? 9   THR A N     1 
ATOM   113  C  CA    . THR A 1 29  ? 4.987   22.684  -32.975 1.00 21.01  ? 9   THR A CA    1 
ATOM   114  C  C     . THR A 1 29  ? 5.880   21.527  -32.545 1.00 25.36  ? 9   THR A C     1 
ATOM   115  O  O     . THR A 1 29  ? 6.719   21.066  -33.323 1.00 27.53  ? 9   THR A O     1 
ATOM   116  C  CB    . THR A 1 29  ? 3.920   22.190  -33.953 1.00 22.71  ? 9   THR A CB    1 
ATOM   117  O  OG1   . THR A 1 29  ? 3.087   23.290  -34.345 1.00 25.62  ? 9   THR A OG1   1 
ATOM   118  C  CG2   . THR A 1 29  ? 3.048   21.095  -33.316 1.00 25.51  ? 9   THR A CG2   1 
ATOM   119  N  N     . VAL A 1 30  ? 5.687   21.046  -31.315 1.00 23.27  ? 10  VAL A N     1 
ATOM   120  C  CA    . VAL A 1 30  ? 6.394   19.872  -30.810 1.00 21.86  ? 10  VAL A CA    1 
ATOM   121  C  C     . VAL A 1 30  ? 5.379   18.892  -30.232 1.00 25.51  ? 10  VAL A C     1 
ATOM   122  O  O     . VAL A 1 30  ? 4.235   19.245  -29.936 1.00 23.40  ? 10  VAL A O     1 
ATOM   123  C  CB    . VAL A 1 30  ? 7.455   20.223  -29.747 1.00 23.23  ? 10  VAL A CB    1 
ATOM   124  C  CG1   . VAL A 1 30  ? 8.535   21.138  -30.336 1.00 24.42  ? 10  VAL A CG1   1 
ATOM   125  C  CG2   . VAL A 1 30  ? 6.790   20.852  -28.523 1.00 24.64  ? 10  VAL A CG2   1 
ATOM   126  N  N     . SER A 1 31  ? 5.819   17.644  -30.062 1.00 23.34  ? 11  SER A N     1 
ATOM   127  C  CA    . SER A 1 31  ? 4.982   16.594  -29.494 1.00 25.85  ? 11  SER A CA    1 
ATOM   128  C  C     . SER A 1 31  ? 5.162   16.511  -27.981 1.00 23.11  ? 11  SER A C     1 
ATOM   129  O  O     . SER A 1 31  ? 6.281   16.595  -27.474 1.00 24.09  ? 11  SER A O     1 
ATOM   130  C  CB    . SER A 1 31  ? 5.330   15.237  -30.112 1.00 30.13  ? 11  SER A CB    1 
ATOM   131  O  OG    . SER A 1 31  ? 4.646   14.197  -29.423 1.00 28.97  ? 11  SER A OG    1 
ATOM   132  N  N     . LEU A 1 32  ? 4.049   16.324  -27.262 1.00 23.37  ? 12  LEU A N     1 
ATOM   133  C  CA    . LEU A 1 32  ? 4.139   16.073  -25.826 1.00 22.15  ? 12  LEU A CA    1 
ATOM   134  C  C     . LEU A 1 32  ? 4.998   14.846  -25.527 1.00 28.59  ? 12  LEU A C     1 
ATOM   135  O  O     . LEU A 1 32  ? 5.639   14.779  -24.470 1.00 25.23  ? 12  LEU A O     1 
ATOM   136  C  CB    . LEU A 1 32  ? 2.738   15.905  -25.225 1.00 25.16  ? 12  LEU A CB    1 
ATOM   137  C  CG    . LEU A 1 32  ? 2.655   15.591  -23.725 1.00 23.29  ? 12  LEU A CG    1 
ATOM   138  C  CD1   . LEU A 1 32  ? 3.322   16.671  -22.870 1.00 23.80  ? 12  LEU A CD1   1 
ATOM   139  C  CD2   . LEU A 1 32  ? 1.206   15.408  -23.312 1.00 24.02  ? 12  LEU A CD2   1 
ATOM   140  N  N     . ASN A 1 33  ? 5.010   13.857  -26.429 1.00 26.14  ? 13  ASN A N     1 
ATOM   141  C  CA    . ASN A 1 33  ? 5.847   12.678  -26.206 1.00 26.11  ? 13  ASN A CA    1 
ATOM   142  C  C     . ASN A 1 33  ? 7.317   13.059  -26.073 1.00 29.47  ? 13  ASN A C     1 
ATOM   143  O  O     . ASN A 1 33  ? 8.045   12.509  -25.231 1.00 29.99  ? 13  ASN A O     1 
ATOM   144  C  CB    . ASN A 1 33  ? 5.661   11.672  -27.342 1.00 26.28  ? 13  ASN A CB    1 
ATOM   145  C  CG    . ASN A 1 33  ? 4.232   11.204  -27.467 1.00 35.24  ? 13  ASN A CG    1 
ATOM   146  O  OD1   . ASN A 1 33  ? 3.558   10.980  -26.464 1.00 38.98  ? 13  ASN A OD1   1 
ATOM   147  N  ND2   . ASN A 1 33  ? 3.760   11.047  -28.700 1.00 38.51  ? 13  ASN A ND2   1 
ATOM   148  N  N     . ASP A 1 34  ? 7.774   13.994  -26.903 1.00 28.86  ? 14  ASP A N     1 
ATOM   149  C  CA    . ASP A 1 34  ? 9.163   14.416  -26.824 1.00 27.99  ? 14  ASP A CA    1 
ATOM   150  C  C     . ASP A 1 34  ? 9.415   15.289  -25.603 1.00 28.08  ? 14  ASP A C     1 
ATOM   151  O  O     . ASP A 1 34  ? 10.515  15.265  -25.048 1.00 31.47  ? 14  ASP A O     1 
ATOM   152  C  CB    . ASP A 1 34  ? 9.562   15.108  -28.120 1.00 28.35  ? 14  ASP A CB    1 
ATOM   153  C  CG    . ASP A 1 34  ? 9.496   14.160  -29.298 1.00 35.22  ? 14  ASP A CG    1 
ATOM   154  O  OD1   . ASP A 1 34  ? 9.933   13.003  -29.137 1.00 40.55  ? 14  ASP A OD1   1 
ATOM   155  O  OD2   . ASP A 1 34  ? 9.034   14.562  -30.381 1.00 32.60  ? 14  ASP A OD2   1 
ATOM   156  N  N     . LEU A 1 35  ? 8.419   16.062  -25.167 1.00 26.51  ? 15  LEU A N     1 
ATOM   157  C  CA    . LEU A 1 35  ? 8.573   16.787  -23.911 1.00 24.59  ? 15  LEU A CA    1 
ATOM   158  C  C     . LEU A 1 35  ? 8.710   15.824  -22.739 1.00 28.09  ? 15  LEU A C     1 
ATOM   159  O  O     . LEU A 1 35  ? 9.526   16.042  -21.837 1.00 30.80  ? 15  LEU A O     1 
ATOM   160  C  CB    . LEU A 1 35  ? 7.381   17.717  -23.696 1.00 23.71  ? 15  LEU A CB    1 
ATOM   161  C  CG    . LEU A 1 35  ? 7.341   18.962  -24.576 1.00 21.70  ? 15  LEU A CG    1 
ATOM   162  C  CD1   . LEU A 1 35  ? 5.964   19.617  -24.461 1.00 24.96  ? 15  LEU A CD1   1 
ATOM   163  C  CD2   . LEU A 1 35  ? 8.421   19.936  -24.161 1.00 22.56  ? 15  LEU A CD2   1 
ATOM   164  N  N     . LYS A 1 36  ? 7.922   14.748  -22.741 1.00 27.94  ? 16  LYS A N     1 
ATOM   165  C  CA    . LYS A 1 36  ? 7.959   13.793  -21.637 1.00 27.82  ? 16  LYS A CA    1 
ATOM   166  C  C     . LYS A 1 36  ? 9.254   12.989  -21.621 1.00 29.31  ? 16  LYS A C     1 
ATOM   167  O  O     . LYS A 1 36  ? 9.778   12.682  -20.548 1.00 33.17  ? 16  LYS A O     1 
ATOM   168  C  CB    . LYS A 1 36  ? 6.764   12.850  -21.732 1.00 30.82  ? 16  LYS A CB    1 
ATOM   169  C  CG    . LYS A 1 36  ? 5.432   13.530  -21.477 1.00 33.65  ? 16  LYS A CG    1 
ATOM   170  C  CD    . LYS A 1 36  ? 4.259   12.701  -21.979 1.00 44.17  ? 16  LYS A CD    1 
ATOM   171  C  CE    . LYS A 1 36  ? 4.089   11.407  -21.216 1.00 51.62  ? 16  LYS A CE    1 
ATOM   172  N  NZ    . LYS A 1 36  ? 2.859   10.695  -21.675 1.00 53.48  ? 16  LYS A NZ    1 
ATOM   173  N  N     . ASN A 1 37  ? 9.790   12.639  -22.789 1.00 31.41  ? 17  ASN A N     1 
ATOM   174  C  CA    . ASN A 1 37  ? 10.992  11.816  -22.806 1.00 30.41  ? 17  ASN A CA    1 
ATOM   175  C  C     . ASN A 1 37  ? 12.277  12.641  -22.847 1.00 37.14  ? 17  ASN A C     1 
ATOM   176  O  O     . ASN A 1 37  ? 13.366  12.064  -22.894 1.00 39.65  ? 17  ASN A O     1 
ATOM   177  C  CB    . ASN A 1 37  ? 10.931  10.788  -23.954 1.00 34.48  ? 17  ASN A CB    1 
ATOM   178  C  CG    . ASN A 1 37  ? 10.985  11.414  -25.334 1.00 46.96  ? 17  ASN A CG    1 
ATOM   179  O  OD1   . ASN A 1 37  ? 11.436  12.544  -25.510 1.00 42.48  ? 17  ASN A OD1   1 
ATOM   180  N  ND2   . ASN A 1 37  ? 10.538  10.659  -26.335 1.00 46.85  ? 17  ASN A ND2   1 
ATOM   181  N  N     . GLY A 1 38  ? 12.174  13.968  -22.853 1.00 32.57  ? 18  GLY A N     1 
ATOM   182  C  CA    . GLY A 1 38  ? 13.337  14.831  -22.843 1.00 37.16  ? 18  GLY A CA    1 
ATOM   183  C  C     . GLY A 1 38  ? 14.101  14.924  -24.141 1.00 36.42  ? 18  GLY A C     1 
ATOM   184  O  O     . GLY A 1 38  ? 15.281  15.284  -24.124 1.00 41.36  ? 18  GLY A O     1 
ATOM   185  N  N     . THR A 1 39  ? 13.463  14.638  -25.274 1.00 35.25  ? 19  THR A N     1 
ATOM   186  C  CA    . THR A 1 39  ? 14.137  14.662  -26.568 1.00 34.27  ? 19  THR A CA    1 
ATOM   187  C  C     . THR A 1 39  ? 13.673  15.816  -27.442 1.00 34.45  ? 19  THR A C     1 
ATOM   188  O  O     . THR A 1 39  ? 13.997  15.844  -28.634 1.00 39.82  ? 19  THR A O     1 
ATOM   189  C  CB    . THR A 1 39  ? 13.930  13.344  -27.320 1.00 36.05  ? 19  THR A CB    1 
ATOM   190  O  OG1   . THR A 1 39  ? 12.529  13.123  -27.537 1.00 40.00  ? 19  THR A OG1   1 
ATOM   191  C  CG2   . THR A 1 39  ? 14.507  12.173  -26.531 1.00 40.08  ? 19  THR A CG2   1 
ATOM   192  N  N     . VAL A 1 40  ? 12.915  16.766  -26.888 1.00 33.78  ? 20  VAL A N     1 
ATOM   193  C  CA    . VAL A 1 40  ? 12.519  17.924  -27.674 1.00 31.09  ? 20  VAL A CA    1 
ATOM   194  C  C     . VAL A 1 40  ? 13.757  18.701  -28.104 1.00 29.63  ? 20  VAL A C     1 
ATOM   195  O  O     . VAL A 1 40  ? 14.721  18.862  -27.344 1.00 30.07  ? 20  VAL A O     1 
ATOM   196  C  CB    . VAL A 1 40  ? 11.535  18.807  -26.888 1.00 36.08  ? 20  VAL A CB    1 
ATOM   197  C  CG1   . VAL A 1 40  ? 12.189  19.361  -25.630 1.00 40.80  ? 20  VAL A CG1   1 
ATOM   198  C  CG2   . VAL A 1 40  ? 11.032  19.936  -27.773 1.00 37.63  ? 20  VAL A CG2   1 
ATOM   199  N  N     . SER A 1 41  ? 13.737  19.164  -29.350 1.00 33.46  ? 21  SER A N     1 
ATOM   200  C  CA    . SER A 1 41  ? 14.849  19.908  -29.921 1.00 32.16  ? 21  SER A CA    1 
ATOM   201  C  C     . SER A 1 41  ? 14.990  21.283  -29.276 1.00 35.98  ? 21  SER A C     1 
ATOM   202  O  O     . SER A 1 41  ? 14.037  22.069  -29.253 1.00 35.80  ? 21  SER A O     1 
ATOM   203  C  CB    . SER A 1 41  ? 14.635  20.059  -31.428 1.00 35.68  ? 21  SER A CB    1 
ATOM   204  O  OG    . SER A 1 41  ? 15.453  21.083  -31.950 1.00 37.46  ? 21  SER A OG    1 
ATOM   205  N  N     . LEU A 1 42  ? 16.185  21.587  -28.766 1.00 37.58  ? 22  LEU A N     1 
ATOM   206  C  CA    . LEU A 1 42  ? 16.413  22.935  -28.257 1.00 34.04  ? 22  LEU A CA    1 
ATOM   207  C  C     . LEU A 1 42  ? 16.524  23.945  -29.390 1.00 35.52  ? 22  LEU A C     1 
ATOM   208  O  O     . LEU A 1 42  ? 16.276  25.137  -29.170 1.00 31.28  ? 22  LEU A O     1 
ATOM   209  C  CB    . LEU A 1 42  ? 17.664  22.985  -27.377 1.00 32.04  ? 22  LEU A CB    1 
ATOM   210  C  CG    . LEU A 1 42  ? 17.617  22.098  -26.132 1.00 33.76  ? 22  LEU A CG    1 
ATOM   211  C  CD1   . LEU A 1 42  ? 18.861  22.314  -25.283 1.00 38.39  ? 22  LEU A CD1   1 
ATOM   212  C  CD2   . LEU A 1 42  ? 16.331  22.345  -25.326 1.00 33.52  ? 22  LEU A CD2   1 
ATOM   213  N  N     . GLU A 1 43  ? 16.878  23.490  -30.596 1.00 31.96  ? 23  GLU A N     1 
ATOM   214  C  CA    . GLU A 1 43  ? 16.809  24.359  -31.763 1.00 36.16  ? 23  GLU A CA    1 
ATOM   215  C  C     . GLU A 1 43  ? 15.370  24.799  -32.013 1.00 27.95  ? 23  GLU A C     1 
ATOM   216  O  O     . GLU A 1 43  ? 15.099  25.989  -32.202 1.00 31.66  ? 23  GLU A O     1 
ATOM   217  C  CB    . GLU A 1 43  ? 17.386  23.647  -32.990 1.00 39.63  ? 23  GLU A CB    1 
ATOM   218  C  CG    . GLU A 1 43  ? 17.338  24.465  -34.275 1.00 47.56  ? 23  GLU A CG    1 
ATOM   219  C  CD    . GLU A 1 43  ? 18.140  23.844  -35.415 1.00 62.58  ? 23  GLU A CD    1 
ATOM   220  O  OE1   . GLU A 1 43  ? 18.600  22.690  -35.274 1.00 65.12  ? 23  GLU A OE1   1 
ATOM   221  O  OE2   . GLU A 1 43  ? 18.316  24.516  -36.454 1.00 69.60  ? 23  GLU A OE2   1 
ATOM   222  N  N     . ALA A 1 44  ? 14.432  23.845  -31.995 1.00 30.32  ? 24  ALA A N     1 
ATOM   223  C  CA    . ALA A 1 44  ? 13.024  24.191  -32.162 1.00 25.78  ? 24  ALA A CA    1 
ATOM   224  C  C     . ALA A 1 44  ? 12.533  25.081  -31.028 1.00 31.96  ? 24  ALA A C     1 
ATOM   225  O  O     . ALA A 1 44  ? 11.763  26.024  -31.250 1.00 24.54  ? 24  ALA A O     1 
ATOM   226  C  CB    . ALA A 1 44  ? 12.175  22.921  -32.239 1.00 28.41  ? 24  ALA A CB    1 
ATOM   227  N  N     . LEU A 1 45  ? 12.967  24.801  -29.798 1.00 26.45  ? 25  LEU A N     1 
ATOM   228  C  CA    . LEU A 1 45  ? 12.523  25.622  -28.681 1.00 24.88  ? 25  LEU A CA    1 
ATOM   229  C  C     . LEU A 1 45  ? 12.998  27.062  -28.847 1.00 26.03  ? 25  LEU A C     1 
ATOM   230  O  O     . LEU A 1 45  ? 12.233  28.009  -28.620 1.00 25.39  ? 25  LEU A O     1 
ATOM   231  C  CB    . LEU A 1 45  ? 13.014  25.026  -27.360 1.00 28.71  ? 25  LEU A CB    1 
ATOM   232  C  CG    . LEU A 1 45  ? 12.393  25.610  -26.089 1.00 25.15  ? 25  LEU A CG    1 
ATOM   233  C  CD1   . LEU A 1 45  ? 10.929  25.184  -25.965 1.00 23.25  ? 25  LEU A CD1   1 
ATOM   234  C  CD2   . LEU A 1 45  ? 13.185  25.189  -24.857 1.00 25.44  ? 25  LEU A CD2   1 
ATOM   235  N  N     . GLU A 1 46  ? 14.252  27.251  -29.269 1.00 24.87  ? 26  GLU A N     1 
ATOM   236  C  CA    . GLU A 1 46  ? 14.726  28.610  -29.493 1.00 26.84  ? 26  GLU A CA    1 
ATOM   237  C  C     . GLU A 1 46  ? 14.018  29.254  -30.679 1.00 25.48  ? 26  GLU A C     1 
ATOM   238  O  O     . GLU A 1 46  ? 13.773  30.465  -30.662 1.00 25.59  ? 26  GLU A O     1 
ATOM   239  C  CB    . GLU A 1 46  ? 16.248  28.627  -29.692 1.00 29.05  ? 26  GLU A CB    1 
ATOM   240  C  CG    . GLU A 1 46  ? 16.875  30.015  -29.600 1.00 32.81  ? 26  GLU A CG    1 
ATOM   241  C  CD    . GLU A 1 46  ? 16.757  30.812  -30.890 1.00 39.64  ? 26  GLU A CD    1 
ATOM   242  O  OE1   . GLU A 1 46  ? 16.573  30.197  -31.967 1.00 34.87  ? 26  GLU A OE1   1 
ATOM   243  O  OE2   . GLU A 1 46  ? 16.847  32.057  -30.823 1.00 41.34  ? 26  GLU A OE2   1 
ATOM   244  N  N     . GLU A 1 47  ? 13.665  28.470  -31.703 1.00 25.90  ? 27  GLU A N     1 
ATOM   245  C  CA    . GLU A 1 47  ? 12.896  29.030  -32.811 1.00 24.81  ? 27  GLU A CA    1 
ATOM   246  C  C     . GLU A 1 47  ? 11.523  29.487  -32.346 1.00 25.75  ? 27  GLU A C     1 
ATOM   247  O  O     . GLU A 1 47  ? 10.938  30.404  -32.934 1.00 26.38  ? 27  GLU A O     1 
ATOM   248  C  CB    . GLU A 1 47  ? 12.745  28.011  -33.940 1.00 27.57  ? 27  GLU A CB    1 
ATOM   249  C  CG    . GLU A 1 47  ? 12.065  28.574  -35.177 1.00 33.78  ? 27  GLU A CG    1 
ATOM   250  C  CD    . GLU A 1 47  ? 11.995  27.585  -36.317 1.00 49.26  ? 27  GLU A CD    1 
ATOM   251  O  OE1   . GLU A 1 47  ? 12.691  26.553  -36.247 1.00 59.78  ? 27  GLU A OE1   1 
ATOM   252  O  OE2   . GLU A 1 47  ? 11.247  27.843  -37.286 1.00 50.96  ? 27  GLU A OE2   1 
ATOM   253  N  N     . ALA A 1 48  ? 10.999  28.854  -31.296 1.00 21.25  ? 28  ALA A N     1 
ATOM   254  C  CA    . ALA A 1 48  ? 9.671   29.192  -30.791 1.00 21.61  ? 28  ALA A CA    1 
ATOM   255  C  C     . ALA A 1 48  ? 9.687   30.368  -29.824 1.00 21.82  ? 28  ALA A C     1 
ATOM   256  O  O     . ALA A 1 48  ? 8.722   31.148  -29.789 1.00 22.74  ? 28  ALA A O     1 
ATOM   257  C  CB    . ALA A 1 48  ? 9.067   27.976  -30.085 1.00 21.43  ? 28  ALA A CB    1 
ATOM   258  N  N     . PHE A 1 49  ? 10.759  30.512  -29.038 1.00 21.31  ? 29  PHE A N     1 
ATOM   259  C  CA    . PHE A 1 49  ? 10.793  31.424  -27.900 1.00 21.94  ? 29  PHE A CA    1 
ATOM   260  C  C     . PHE A 1 49  ? 11.914  32.458  -27.955 1.00 21.86  ? 29  PHE A C     1 
ATOM   261  O  O     . PHE A 1 49  ? 11.985  33.310  -27.063 1.00 23.61  ? 29  PHE A O     1 
ATOM   262  C  CB    . PHE A 1 49  ? 10.945  30.624  -26.594 1.00 22.45  ? 29  PHE A CB    1 
ATOM   263  C  CG    . PHE A 1 49  ? 9.713   29.875  -26.161 1.00 19.95  ? 29  PHE A CG    1 
ATOM   264  C  CD1   . PHE A 1 49  ? 8.453   30.173  -26.673 1.00 19.77  ? 29  PHE A CD1   1 
ATOM   265  C  CD2   . PHE A 1 49  ? 9.826   28.877  -25.207 1.00 22.64  ? 29  PHE A CD2   1 
ATOM   266  C  CE1   . PHE A 1 49  ? 7.323   29.472  -26.226 1.00 22.17  ? 29  PHE A CE1   1 
ATOM   267  C  CE2   . PHE A 1 49  ? 8.723   28.175  -24.763 1.00 22.99  ? 29  PHE A CE2   1 
ATOM   268  C  CZ    . PHE A 1 49  ? 7.462   28.472  -25.269 1.00 20.41  ? 29  PHE A CZ    1 
ATOM   269  N  N     . GLY A 1 50  ? 12.793  32.412  -28.967 1.00 24.79  ? 30  GLY A N     1 
ATOM   270  C  CA    . GLY A 1 50  ? 13.972  33.263  -29.003 1.00 27.18  ? 30  GLY A CA    1 
ATOM   271  C  C     . GLY A 1 50  ? 13.663  34.693  -29.410 1.00 26.86  ? 30  GLY A C     1 
ATOM   272  O  O     . GLY A 1 50  ? 12.512  35.087  -29.616 1.00 26.70  ? 30  GLY A O     1 
ATOM   273  N  N     . PRO A 1 51  ? 14.720  35.506  -29.508 1.00 27.32  ? 31  PRO A N     1 
ATOM   274  C  CA    . PRO A 1 51  ? 14.521  36.945  -29.780 1.00 29.82  ? 31  PRO A CA    1 
ATOM   275  C  C     . PRO A 1 51  ? 13.829  37.267  -31.100 1.00 31.24  ? 31  PRO A C     1 
ATOM   276  O  O     . PRO A 1 51  ? 13.167  38.310  -31.193 1.00 35.07  ? 31  PRO A O     1 
ATOM   277  C  CB    . PRO A 1 51  ? 15.953  37.499  -29.750 1.00 34.25  ? 31  PRO A CB    1 
ATOM   278  C  CG    . PRO A 1 51  ? 16.695  36.535  -28.875 1.00 34.05  ? 31  PRO A CG    1 
ATOM   279  C  CD    . PRO A 1 51  ? 16.132  35.191  -29.224 1.00 29.94  ? 31  PRO A CD    1 
ATOM   280  N  N     . ASP A 1 52  ? 13.963  36.422  -32.124 1.00 30.02  ? 32  ASP A N     1 
ATOM   281  C  CA    . ASP A 1 52  ? 13.329  36.652  -33.419 1.00 30.98  ? 32  ASP A CA    1 
ATOM   282  C  C     . ASP A 1 52  ? 12.052  35.840  -33.594 1.00 29.30  ? 32  ASP A C     1 
ATOM   283  O  O     . ASP A 1 52  ? 11.516  35.767  -34.705 1.00 30.51  ? 32  ASP A O     1 
ATOM   284  C  CB    . ASP A 1 52  ? 14.319  36.335  -34.539 1.00 32.14  ? 32  ASP A CB    1 
ATOM   285  C  CG    . ASP A 1 52  ? 15.545  37.222  -34.482 1.00 43.05  ? 32  ASP A CG    1 
ATOM   286  O  OD1   . ASP A 1 52  ? 15.386  38.445  -34.274 1.00 47.19  ? 32  ASP A OD1   1 
ATOM   287  O  OD2   . ASP A 1 52  ? 16.667  36.693  -34.615 1.00 46.48  ? 32  ASP A OD2   1 
ATOM   288  N  N     . SER A 1 53  ? 11.550  35.243  -32.515 1.00 25.50  ? 33  SER A N     1 
ATOM   289  C  CA    . SER A 1 53  ? 10.462  34.288  -32.573 1.00 24.58  ? 33  SER A CA    1 
ATOM   290  C  C     . SER A 1 53  ? 9.107   34.970  -32.423 1.00 21.79  ? 33  SER A C     1 
ATOM   291  O  O     . SER A 1 53  ? 8.997   36.173  -32.173 1.00 23.80  ? 33  SER A O     1 
ATOM   292  C  CB    . SER A 1 53  ? 10.611  33.243  -31.466 1.00 24.47  ? 33  SER A CB    1 
ATOM   293  O  OG    . SER A 1 53  ? 10.276  33.821  -30.210 1.00 23.24  ? 33  SER A OG    1 
ATOM   294  N  N     . LEU A 1 54  ? 8.070   34.150  -32.512 1.00 19.70  ? 34  LEU A N     1 
ATOM   295  C  CA    . LEU A 1 54  ? 6.699   34.527  -32.209 1.00 18.47  ? 34  LEU A CA    1 
ATOM   296  C  C     . LEU A 1 54  ? 6.368   34.370  -30.730 1.00 20.30  ? 34  LEU A C     1 
ATOM   297  O  O     . LEU A 1 54  ? 5.252   34.706  -30.327 1.00 20.01  ? 34  LEU A O     1 
ATOM   298  C  CB    . LEU A 1 54  ? 5.721   33.668  -33.027 1.00 20.29  ? 34  LEU A CB    1 
ATOM   299  C  CG    . LEU A 1 54  ? 5.822   33.816  -34.547 1.00 22.74  ? 34  LEU A CG    1 
ATOM   300  C  CD1   . LEU A 1 54  ? 4.958   32.765  -35.231 1.00 21.85  ? 34  LEU A CD1   1 
ATOM   301  C  CD2   . LEU A 1 54  ? 5.425   35.213  -34.980 1.00 24.32  ? 34  LEU A CD2   1 
ATOM   302  N  N     . GLY A 1 55  ? 7.301   33.869  -29.919 1.00 19.46  ? 35  GLY A N     1 
ATOM   303  C  CA    . GLY A 1 55  ? 7.037   33.720  -28.494 1.00 20.41  ? 35  GLY A CA    1 
ATOM   304  C  C     . GLY A 1 55  ? 5.919   32.751  -28.166 1.00 18.31  ? 35  GLY A C     1 
ATOM   305  O  O     . GLY A 1 55  ? 5.175   32.973  -27.204 1.00 19.62  ? 35  GLY A O     1 
ATOM   306  N  N     . ILE A 1 56  ? 5.759   31.694  -28.954 1.00 18.44  ? 36  ILE A N     1 
ATOM   307  C  CA    . ILE A 1 56  ? 4.672   30.741  -28.751 1.00 17.68  ? 36  ILE A CA    1 
ATOM   308  C  C     . ILE A 1 56  ? 5.120   29.374  -29.244 1.00 20.12  ? 36  ILE A C     1 
ATOM   309  O  O     . ILE A 1 56  ? 5.865   29.268  -30.225 1.00 20.36  ? 36  ILE A O     1 
ATOM   310  C  CB    . ILE A 1 56  ? 3.370   31.211  -29.446 1.00 18.43  ? 36  ILE A CB    1 
ATOM   311  C  CG1   . ILE A 1 56  ? 2.190   30.323  -29.040 1.00 19.47  ? 36  ILE A CG1   1 
ATOM   312  C  CG2   . ILE A 1 56  ? 3.521   31.261  -30.971 1.00 19.86  ? 36  ILE A CG2   1 
ATOM   313  C  CD1   . ILE A 1 56  ? 0.807   30.939  -29.402 1.00 17.03  ? 36  ILE A CD1   1 
ATOM   314  N  N     . LEU A 1 57  ? 4.678   28.332  -28.535 1.00 17.78  ? 37  LEU A N     1 
ATOM   315  C  CA    . LEU A 1 57  ? 4.978   26.940  -28.845 1.00 16.93  ? 37  LEU A CA    1 
ATOM   316  C  C     . LEU A 1 57  ? 3.685   26.133  -28.810 1.00 22.09  ? 37  LEU A C     1 
ATOM   317  O  O     . LEU A 1 57  ? 2.965   26.150  -27.806 1.00 19.35  ? 37  LEU A O     1 
ATOM   318  C  CB    . LEU A 1 57  ? 5.988   26.363  -27.839 1.00 18.67  ? 37  LEU A CB    1 
ATOM   319  C  CG    . LEU A 1 57  ? 6.342   24.879  -27.977 1.00 18.20  ? 37  LEU A CG    1 
ATOM   320  C  CD1   . LEU A 1 57  ? 7.306   24.671  -29.155 1.00 20.68  ? 37  LEU A CD1   1 
ATOM   321  C  CD2   . LEU A 1 57  ? 6.950   24.334  -26.689 1.00 22.68  ? 37  LEU A CD2   1 
ATOM   322  N  N     . VAL A 1 58  ? 3.398   25.398  -29.878 1.00 17.65  ? 38  VAL A N     1 
ATOM   323  C  CA    . VAL A 1 58  ? 2.213   24.548  -29.938 1.00 17.72  ? 38  VAL A CA    1 
ATOM   324  C  C     . VAL A 1 58  ? 2.628   23.133  -29.554 1.00 19.96  ? 38  VAL A C     1 
ATOM   325  O  O     . VAL A 1 58  ? 3.623   22.616  -30.073 1.00 22.77  ? 38  VAL A O     1 
ATOM   326  C  CB    . VAL A 1 58  ? 1.577   24.584  -31.340 1.00 20.71  ? 38  VAL A CB    1 
ATOM   327  C  CG1   . VAL A 1 58  ? 0.481   23.512  -31.489 1.00 20.98  ? 38  VAL A CG1   1 
ATOM   328  C  CG2   . VAL A 1 58  ? 1.015   25.978  -31.636 1.00 21.95  ? 38  VAL A CG2   1 
ATOM   329  N  N     . VAL A 1 59  ? 1.879   22.513  -28.646 1.00 19.20  ? 39  VAL A N     1 
ATOM   330  C  CA    . VAL A 1 59  ? 2.136   21.150  -28.186 1.00 21.39  ? 39  VAL A CA    1 
ATOM   331  C  C     . VAL A 1 59  ? 0.996   20.267  -28.678 1.00 20.91  ? 39  VAL A C     1 
ATOM   332  O  O     . VAL A 1 59  ? -0.170  20.498  -28.328 1.00 19.52  ? 39  VAL A O     1 
ATOM   333  C  CB    . VAL A 1 59  ? 2.262   21.087  -26.654 1.00 18.10  ? 39  VAL A CB    1 
ATOM   334  C  CG1   . VAL A 1 59  ? 2.461   19.640  -26.177 1.00 19.00  ? 39  VAL A CG1   1 
ATOM   335  C  CG2   . VAL A 1 59  ? 3.386   22.004  -26.174 1.00 20.85  ? 39  VAL A CG2   1 
ATOM   336  N  N     . LYS A 1 60  ? 1.336   19.254  -29.487 1.00 20.76  ? 40  LYS A N     1 
ATOM   337  C  CA    . LYS A 1 60  ? 0.390   18.259  -29.973 1.00 21.94  ? 40  LYS A CA    1 
ATOM   338  C  C     . LYS A 1 60  ? 0.587   16.947  -29.208 1.00 22.70  ? 40  LYS A C     1 
ATOM   339  O  O     . LYS A 1 60  ? 1.468   16.826  -28.348 1.00 23.14  ? 40  LYS A O     1 
ATOM   340  C  CB    . LYS A 1 60  ? 0.545   18.036  -31.483 1.00 22.19  ? 40  LYS A CB    1 
ATOM   341  C  CG    . LYS A 1 60  ? 1.864   17.368  -31.877 1.00 28.25  ? 40  LYS A CG    1 
ATOM   342  C  CD    . LYS A 1 60  ? 1.902   17.110  -33.389 1.00 31.59  ? 40  LYS A CD    1 
ATOM   343  C  CE    . LYS A 1 60  ? 3.123   16.307  -33.783 1.00 35.99  ? 40  LYS A CE    1 
ATOM   344  N  NZ    . LYS A 1 60  ? 3.156   16.062  -35.259 1.00 52.57  ? 40  LYS A NZ    1 
ATOM   345  N  N     . ASP A 1 61  ? -0.243  15.949  -29.539 1.00 24.82  ? 41  ASP A N     1 
ATOM   346  C  CA    . ASP A 1 61  ? -0.226  14.646  -28.861 1.00 22.95  ? 41  ASP A CA    1 
ATOM   347  C  C     . ASP A 1 61  ? -0.532  14.803  -27.368 1.00 24.54  ? 41  ASP A C     1 
ATOM   348  O  O     . ASP A 1 61  ? 0.124   14.205  -26.514 1.00 25.20  ? 41  ASP A O     1 
ATOM   349  C  CB    . ASP A 1 61  ? 1.111   13.918  -29.063 1.00 26.58  ? 41  ASP A CB    1 
ATOM   350  C  CG    . ASP A 1 61  ? 1.416   13.631  -30.523 1.00 28.71  ? 41  ASP A CG    1 
ATOM   351  O  OD1   . ASP A 1 61  ? 0.500   13.212  -31.257 1.00 31.87  ? 41  ASP A OD1   1 
ATOM   352  O  OD2   . ASP A 1 61  ? 2.578   13.816  -30.930 1.00 29.43  ? 41  ASP A OD2   1 
ATOM   353  N  N     . VAL A 1 62  ? -1.524  15.633  -27.045 1.00 25.30  ? 42  VAL A N     1 
ATOM   354  C  CA    . VAL A 1 62  ? -1.826  15.948  -25.648 1.00 28.46  ? 42  VAL A CA    1 
ATOM   355  C  C     . VAL A 1 62  ? -2.611  14.789  -25.033 1.00 26.94  ? 42  VAL A C     1 
ATOM   356  O  O     . VAL A 1 62  ? -3.047  13.893  -25.771 1.00 25.14  ? 42  VAL A O     1 
ATOM   357  C  CB    . VAL A 1 62  ? -2.561  17.297  -25.540 1.00 28.71  ? 42  VAL A CB    1 
ATOM   358  C  CG1   . VAL A 1 62  ? -1.698  18.395  -26.191 1.00 28.10  ? 42  VAL A CG1   1 
ATOM   359  C  CG2   . VAL A 1 62  ? -3.942  17.220  -26.150 1.00 26.89  ? 42  VAL A CG2   1 
ATOM   360  N  N     . PRO A 1 63  ? -2.773  14.720  -23.703 1.00 23.02  ? 43  PRO A N     1 
ATOM   361  C  CA    . PRO A 1 63  ? -3.493  13.580  -23.116 1.00 27.05  ? 43  PRO A CA    1 
ATOM   362  C  C     . PRO A 1 63  ? -4.896  13.428  -23.689 1.00 29.17  ? 43  PRO A C     1 
ATOM   363  O  O     . PRO A 1 63  ? -5.535  14.393  -24.128 1.00 25.98  ? 43  PRO A O     1 
ATOM   364  C  CB    . PRO A 1 63  ? -3.524  13.906  -21.619 1.00 33.66  ? 43  PRO A CB    1 
ATOM   365  C  CG    . PRO A 1 63  ? -2.361  14.803  -21.408 1.00 29.40  ? 43  PRO A CG    1 
ATOM   366  C  CD    . PRO A 1 63  ? -2.285  15.639  -22.659 1.00 26.04  ? 43  PRO A CD    1 
ATOM   367  N  N     . ALA A 1 64  ? -5.364  12.177  -23.698 1.00 30.30  ? 44  ALA A N     1 
ATOM   368  C  CA    . ALA A 1 64  ? -6.626  11.849  -24.354 1.00 27.68  ? 44  ALA A CA    1 
ATOM   369  C  C     . ALA A 1 64  ? -7.810  12.586  -23.735 1.00 28.54  ? 44  ALA A C     1 
ATOM   370  O  O     . ALA A 1 64  ? -8.775  12.906  -24.441 1.00 29.96  ? 44  ALA A O     1 
ATOM   371  C  CB    . ALA A 1 64  ? -6.854  10.335  -24.303 1.00 33.38  ? 44  ALA A CB    1 
ATOM   372  N  N     . GLU A 1 65  ? -7.755  12.865  -22.433 1.00 28.93  ? 45  GLU A N     1 
ATOM   373  C  CA    . GLU A 1 65  ? -8.868  13.525  -21.764 1.00 26.45  ? 45  GLU A CA    1 
ATOM   374  C  C     . GLU A 1 65  ? -8.984  15.005  -22.131 1.00 24.80  ? 45  GLU A C     1 
ATOM   375  O  O     . GLU A 1 65  ? -10.060 15.597  -21.924 1.00 25.07  ? 45  GLU A O     1 
ATOM   376  C  CB    . GLU A 1 65  ? -8.730  13.334  -20.247 1.00 29.55  ? 45  GLU A CB    1 
ATOM   377  C  CG    . GLU A 1 65  ? -7.467  13.924  -19.619 1.00 35.53  ? 45  GLU A CG    1 
ATOM   378  C  CD    . GLU A 1 65  ? -6.344  12.908  -19.404 1.00 46.77  ? 45  GLU A CD    1 
ATOM   379  O  OE1   . GLU A 1 65  ? -6.285  11.884  -20.124 1.00 37.52  ? 45  GLU A OE1   1 
ATOM   380  O  OE2   . GLU A 1 65  ? -5.508  13.144  -18.502 1.00 53.01  ? 45  GLU A OE2   1 
ATOM   381  N  N     . PHE A 1 66  ? -7.953  15.582  -22.768 1.00 20.79  ? 46  PHE A N     1 
ATOM   382  C  CA    . PHE A 1 66  ? -7.956  17.024  -23.021 1.00 18.19  ? 46  PHE A CA    1 
ATOM   383  C  C     . PHE A 1 66  ? -9.188  17.445  -23.812 1.00 22.08  ? 46  PHE A C     1 
ATOM   384  O  O     . PHE A 1 66  ? -9.885  18.397  -23.436 1.00 19.01  ? 46  PHE A O     1 
ATOM   385  C  CB    . PHE A 1 66  ? -6.696  17.448  -23.779 1.00 21.87  ? 46  PHE A CB    1 
ATOM   386  C  CG    . PHE A 1 66  ? -6.740  18.886  -24.252 1.00 18.90  ? 46  PHE A CG    1 
ATOM   387  C  CD1   . PHE A 1 66  ? -6.567  19.922  -23.347 1.00 16.39  ? 46  PHE A CD1   1 
ATOM   388  C  CD2   . PHE A 1 66  ? -6.973  19.200  -25.580 1.00 19.71  ? 46  PHE A CD2   1 
ATOM   389  C  CE1   . PHE A 1 66  ? -6.641  21.251  -23.750 1.00 17.89  ? 46  PHE A CE1   1 
ATOM   390  C  CE2   . PHE A 1 66  ? -7.022  20.540  -26.006 1.00 17.49  ? 46  PHE A CE2   1 
ATOM   391  C  CZ    . PHE A 1 66  ? -6.862  21.567  -25.086 1.00 18.59  ? 46  PHE A CZ    1 
ATOM   392  N  N     . ALA A 1 67  ? -9.476  16.739  -24.911 1.00 21.88  ? 47  ALA A N     1 
ATOM   393  C  CA    . ALA A 1 67  ? -10.551 17.178  -25.792 1.00 21.05  ? 47  ALA A CA    1 
ATOM   394  C  C     . ALA A 1 67  ? -11.856 17.336  -25.026 1.00 20.13  ? 47  ALA A C     1 
ATOM   395  O  O     . ALA A 1 67  ? -12.544 18.351  -25.180 1.00 19.37  ? 47  ALA A O     1 
ATOM   396  C  CB    . ALA A 1 67  ? -10.719 16.204  -26.958 1.00 25.53  ? 47  ALA A CB    1 
ATOM   397  N  N     . GLU A 1 68  ? -12.208 16.355  -24.183 1.00 21.29  ? 48  GLU A N     1 
ATOM   398  C  CA    . GLU A 1 68  ? -13.492 16.469  -23.500 1.00 24.59  ? 48  GLU A CA    1 
ATOM   399  C  C     . GLU A 1 68  ? -13.454 17.573  -22.450 1.00 22.77  ? 48  GLU A C     1 
ATOM   400  O  O     . GLU A 1 68  ? -14.417 18.347  -22.321 1.00 22.34  ? 48  GLU A O     1 
ATOM   401  C  CB    . GLU A 1 68  ? -13.916 15.132  -22.887 1.00 27.44  ? 48  GLU A CB    1 
ATOM   402  C  CG    . GLU A 1 68  ? -15.306 15.191  -22.255 1.00 35.00  ? 48  GLU A CG    1 
ATOM   403  C  CD    . GLU A 1 68  ? -15.742 13.877  -21.623 1.00 72.25  ? 48  GLU A CD    1 
ATOM   404  O  OE1   . GLU A 1 68  ? -15.226 12.811  -22.026 1.00 70.44  ? 48  GLU A OE1   1 
ATOM   405  O  OE2   . GLU A 1 68  ? -16.609 13.912  -20.723 1.00 77.14  ? 48  GLU A OE2   1 
ATOM   406  N  N     . LEU A 1 69  ? -12.332 17.691  -21.725 1.00 19.41  ? 49  LEU A N     1 
ATOM   407  C  CA    . LEU A 1 69  ? -12.240 18.713  -20.684 1.00 18.29  ? 49  LEU A CA    1 
ATOM   408  C  C     . LEU A 1 69  ? -12.337 20.103  -21.292 1.00 17.95  ? 49  LEU A C     1 
ATOM   409  O  O     . LEU A 1 69  ? -13.082 20.962  -20.796 1.00 18.32  ? 49  LEU A O     1 
ATOM   410  C  CB    . LEU A 1 69  ? -10.933 18.563  -19.896 1.00 16.87  ? 49  LEU A CB    1 
ATOM   411  C  CG    . LEU A 1 69  ? -10.917 17.438  -18.864 1.00 18.51  ? 49  LEU A CG    1 
ATOM   412  C  CD1   . LEU A 1 69  ? -9.519  17.258  -18.265 1.00 18.78  ? 49  LEU A CD1   1 
ATOM   413  C  CD2   . LEU A 1 69  ? -11.927 17.687  -17.756 1.00 22.98  ? 49  LEU A CD2   1 
ATOM   414  N  N     . ARG A 1 70  ? -11.625 20.324  -22.399 1.00 15.71  ? 50  ARG A N     1 
ATOM   415  C  CA    . ARG A 1 70  ? -11.733 21.599  -23.091 1.00 16.12  ? 50  ARG A CA    1 
ATOM   416  C  C     . ARG A 1 70  ? -13.178 21.859  -23.477 1.00 17.47  ? 50  ARG A C     1 
ATOM   417  O  O     . ARG A 1 70  ? -13.728 22.935  -23.189 1.00 16.87  ? 50  ARG A O     1 
ATOM   418  C  CB    . ARG A 1 70  ? -10.833 21.616  -24.332 1.00 18.52  ? 50  ARG A CB    1 
ATOM   419  C  CG    . ARG A 1 70  ? -11.031 22.838  -25.216 1.00 15.37  ? 50  ARG A CG    1 
ATOM   420  C  CD    . ARG A 1 70  ? -10.342 22.714  -26.600 1.00 16.27  ? 50  ARG A CD    1 
ATOM   421  N  NE    . ARG A 1 70  ? -10.768 23.789  -27.489 1.00 17.55  ? 50  ARG A NE    1 
ATOM   422  C  CZ    . ARG A 1 70  ? -11.898 23.765  -28.182 1.00 18.20  ? 50  ARG A CZ    1 
ATOM   423  N  NH1   . ARG A 1 70  ? -12.681 22.700  -28.179 1.00 17.88  ? 50  ARG A NH1   1 
ATOM   424  N  NH2   . ARG A 1 70  ? -12.267 24.848  -28.864 1.00 17.18  ? 50  ARG A NH2   1 
ATOM   425  N  N     . HIS A 1 71  ? -13.822 20.859  -24.092 1.00 17.10  ? 51  HIS A N     1 
ATOM   426  C  CA    . HIS A 1 71  ? -15.189 21.067  -24.552 1.00 20.91  ? 51  HIS A CA    1 
ATOM   427  C  C     . HIS A 1 71  ? -16.093 21.397  -23.376 1.00 20.22  ? 51  HIS A C     1 
ATOM   428  O  O     . HIS A 1 71  ? -16.933 22.310  -23.455 1.00 18.92  ? 51  HIS A O     1 
ATOM   429  C  CB    . HIS A 1 71  ? -15.675 19.825  -25.298 1.00 17.93  ? 51  HIS A CB    1 
ATOM   430  C  CG    . HIS A 1 71  ? -17.022 19.986  -25.940 1.00 21.42  ? 51  HIS A CG    1 
ATOM   431  N  ND1   . HIS A 1 71  ? -17.740 18.913  -26.422 1.00 28.04  ? 51  HIS A ND1   1 
ATOM   432  C  CD2   . HIS A 1 71  ? -17.755 21.088  -26.216 1.00 24.19  ? 51  HIS A CD2   1 
ATOM   433  C  CE1   . HIS A 1 71  ? -18.873 19.347  -26.951 1.00 26.02  ? 51  HIS A CE1   1 
ATOM   434  N  NE2   . HIS A 1 71  ? -18.909 20.662  -26.833 1.00 25.31  ? 51  HIS A NE2   1 
ATOM   435  N  N     . ARG A 1 72  ? -15.907 20.697  -22.255 1.00 17.32  ? 52  ARG A N     1 
ATOM   436  C  CA    . ARG A 1 72  ? -16.795 20.954  -21.129 1.00 18.06  ? 52  ARG A CA    1 
ATOM   437  C  C     . ARG A 1 72  ? -16.511 22.320  -20.526 1.00 17.61  ? 52  ARG A C     1 
ATOM   438  O  O     . ARG A 1 72  ? -17.444 23.095  -20.251 1.00 17.97  ? 52  ARG A O     1 
ATOM   439  C  CB    . ARG A 1 72  ? -16.687 19.837  -20.092 1.00 23.01  ? 52  ARG A CB    1 
ATOM   440  C  CG    . ARG A 1 72  ? -17.248 18.515  -20.627 1.00 36.76  ? 52  ARG A CG    1 
ATOM   441  C  CD    . ARG A 1 72  ? -17.647 17.535  -19.532 1.00 38.81  ? 52  ARG A CD    1 
ATOM   442  N  NE    . ARG A 1 72  ? -16.574 17.277  -18.580 1.00 48.57  ? 52  ARG A NE    1 
ATOM   443  C  CZ    . ARG A 1 72  ? -16.614 17.619  -17.299 1.00 62.42  ? 52  ARG A CZ    1 
ATOM   444  N  NH1   . ARG A 1 72  ? -17.673 18.220  -16.776 1.00 55.31  ? 52  ARG A NH1   1 
ATOM   445  N  NH2   . ARG A 1 72  ? -15.570 17.343  -16.519 1.00 44.55  ? 52  ARG A NH2   1 
ATOM   446  N  N     . LEU A 1 73  ? -15.226 22.663  -20.341 1.00 17.39  ? 53  LEU A N     1 
ATOM   447  C  CA    . LEU A 1 73  ? -14.976 23.893  -19.598 1.00 16.20  ? 53  LEU A CA    1 
ATOM   448  C  C     . LEU A 1 73  ? -15.318 25.107  -20.442 1.00 15.04  ? 53  LEU A C     1 
ATOM   449  O  O     . LEU A 1 73  ? -15.836 26.105  -19.930 1.00 16.69  ? 53  LEU A O     1 
ATOM   450  C  CB    . LEU A 1 73  ? -13.523 23.978  -19.110 1.00 15.51  ? 53  LEU A CB    1 
ATOM   451  C  CG    . LEU A 1 73  ? -13.362 25.085  -18.052 1.00 15.30  ? 53  LEU A CG    1 
ATOM   452  C  CD1   . LEU A 1 73  ? -14.168 24.776  -16.780 1.00 18.60  ? 53  LEU A CD1   1 
ATOM   453  C  CD2   . LEU A 1 73  ? -11.884 25.354  -17.706 1.00 15.64  ? 53  LEU A CD2   1 
ATOM   454  N  N     . LEU A 1 74  ? -15.005 25.061  -21.742 1.00 14.80  ? 54  LEU A N     1 
ATOM   455  C  CA    . LEU A 1 74  ? -15.399 26.181  -22.578 1.00 15.13  ? 54  LEU A CA    1 
ATOM   456  C  C     . LEU A 1 74  ? -16.923 26.280  -22.643 1.00 17.54  ? 54  LEU A C     1 
ATOM   457  O  O     . LEU A 1 74  ? -17.462 27.394  -22.649 1.00 17.94  ? 54  LEU A O     1 
ATOM   458  C  CB    . LEU A 1 74  ? -14.739 26.077  -23.957 1.00 15.09  ? 54  LEU A CB    1 
ATOM   459  C  CG    . LEU A 1 74  ? -13.198 26.135  -23.874 1.00 16.67  ? 54  LEU A CG    1 
ATOM   460  C  CD1   . LEU A 1 74  ? -12.570 26.187  -25.271 1.00 16.11  ? 54  LEU A CD1   1 
ATOM   461  C  CD2   . LEU A 1 74  ? -12.675 27.286  -23.005 1.00 20.31  ? 54  LEU A CD2   1 
ATOM   462  N  N     . SER A 1 75  ? -17.639 25.142  -22.570 1.00 16.71  ? 55  SER A N     1 
ATOM   463  C  CA    A SER A 1 75  ? -19.096 25.228  -22.454 0.76 17.16  ? 55  SER A CA    1 
ATOM   464  C  CA    B SER A 1 75  ? -19.092 25.225  -22.454 0.24 17.24  ? 55  SER A CA    1 
ATOM   465  C  C     . SER A 1 75  ? -19.492 25.909  -21.149 1.00 20.12  ? 55  SER A C     1 
ATOM   466  O  O     . SER A 1 75  ? -20.395 26.760  -21.129 1.00 17.02  ? 55  SER A O     1 
ATOM   467  C  CB    A SER A 1 75  ? -19.740 23.845  -22.531 0.76 17.06  ? 55  SER A CB    1 
ATOM   468  C  CB    B SER A 1 75  ? -19.712 23.832  -22.553 0.24 17.14  ? 55  SER A CB    1 
ATOM   469  O  OG    A SER A 1 75  ? -19.549 23.264  -23.793 0.76 17.25  ? 55  SER A OG    1 
ATOM   470  O  OG    B SER A 1 75  ? -21.109 23.898  -22.353 0.24 15.94  ? 55  SER A OG    1 
ATOM   471  N  N     . TYR A 1 76  ? -18.821 25.557  -20.045 1.00 17.82  ? 56  TYR A N     1 
ATOM   472  C  CA    . TYR A 1 76  ? -19.109 26.210  -18.775 1.00 16.44  ? 56  TYR A CA    1 
ATOM   473  C  C     . TYR A 1 76  ? -18.940 27.719  -18.871 1.00 16.46  ? 56  TYR A C     1 
ATOM   474  O  O     . TYR A 1 76  ? -19.653 28.459  -18.191 1.00 17.28  ? 56  TYR A O     1 
ATOM   475  C  CB    . TYR A 1 76  ? -18.210 25.646  -17.667 1.00 16.00  ? 56  TYR A CB    1 
ATOM   476  C  CG    . TYR A 1 76  ? -18.714 24.380  -16.996 1.00 16.48  ? 56  TYR A CG    1 
ATOM   477  C  CD1   . TYR A 1 76  ? -19.853 24.394  -16.201 1.00 17.38  ? 56  TYR A CD1   1 
ATOM   478  C  CD2   . TYR A 1 76  ? -18.033 23.176  -17.145 1.00 18.25  ? 56  TYR A CD2   1 
ATOM   479  C  CE1   . TYR A 1 76  ? -20.308 23.227  -15.567 1.00 18.78  ? 56  TYR A CE1   1 
ATOM   480  C  CE2   . TYR A 1 76  ? -18.458 22.020  -16.524 1.00 17.56  ? 56  TYR A CE2   1 
ATOM   481  C  CZ    . TYR A 1 76  ? -19.610 22.041  -15.753 1.00 18.46  ? 56  TYR A CZ    1 
ATOM   482  O  OH    . TYR A 1 76  ? -20.029 20.883  -15.141 1.00 20.13  ? 56  TYR A OH    1 
ATOM   483  N  N     . SER A 1 77  ? -18.021 28.201  -19.720 1.00 15.65  ? 57  SER A N     1 
ATOM   484  C  CA    . SER A 1 77  ? -17.859 29.643  -19.855 1.00 15.72  ? 57  SER A CA    1 
ATOM   485  C  C     . SER A 1 77  ? -19.159 30.305  -20.311 1.00 16.07  ? 57  SER A C     1 
ATOM   486  O  O     . SER A 1 77  ? -19.536 31.364  -19.791 1.00 16.25  ? 57  SER A O     1 
ATOM   487  C  CB    . SER A 1 77  ? -16.720 29.948  -20.831 1.00 16.07  ? 57  SER A CB    1 
ATOM   488  O  OG    . SER A 1 77  ? -16.393 31.324  -20.801 1.00 17.65  ? 57  SER A OG    1 
ATOM   489  N  N     . SER A 1 78  ? -19.861 29.680  -21.266 1.00 17.23  ? 58  SER A N     1 
ATOM   490  C  CA    . SER A 1 78  ? -21.168 30.193  -21.687 1.00 16.14  ? 58  SER A CA    1 
ATOM   491  C  C     . SER A 1 78  ? -22.205 30.058  -20.575 1.00 17.03  ? 58  SER A C     1 
ATOM   492  O  O     . SER A 1 78  ? -22.943 31.014  -20.278 1.00 19.16  ? 58  SER A O     1 
ATOM   493  C  CB    . SER A 1 78  ? -21.629 29.481  -22.964 1.00 17.60  ? 58  SER A CB    1 
ATOM   494  O  OG    . SER A 1 78  ? -21.016 30.027  -24.133 1.00 17.45  ? 58  SER A OG    1 
ATOM   495  N  N     . TYR A 1 79  ? -22.250 28.896  -19.913 1.00 16.88  ? 59  TYR A N     1 
ATOM   496  C  CA    . TYR A 1 79  ? -23.242 28.720  -18.850 1.00 17.00  ? 59  TYR A CA    1 
ATOM   497  C  C     . TYR A 1 79  ? -23.031 29.766  -17.759 1.00 17.37  ? 59  TYR A C     1 
ATOM   498  O  O     . TYR A 1 79  ? -23.969 30.463  -17.335 1.00 19.54  ? 59  TYR A O     1 
ATOM   499  C  CB    . TYR A 1 79  ? -23.141 27.316  -18.261 1.00 18.07  ? 59  TYR A CB    1 
ATOM   500  C  CG    . TYR A 1 79  ? -23.697 26.161  -19.074 1.00 16.87  ? 59  TYR A CG    1 
ATOM   501  C  CD1   . TYR A 1 79  ? -25.035 26.148  -19.480 1.00 20.78  ? 59  TYR A CD1   1 
ATOM   502  C  CD2   . TYR A 1 79  ? -22.909 25.062  -19.372 1.00 18.63  ? 59  TYR A CD2   1 
ATOM   503  C  CE1   . TYR A 1 79  ? -25.554 25.068  -20.195 1.00 23.39  ? 59  TYR A CE1   1 
ATOM   504  C  CE2   . TYR A 1 79  ? -23.414 23.983  -20.073 1.00 21.50  ? 59  TYR A CE2   1 
ATOM   505  C  CZ    . TYR A 1 79  ? -24.741 23.991  -20.481 1.00 21.79  ? 59  TYR A CZ    1 
ATOM   506  O  OH    . TYR A 1 79  ? -25.241 22.913  -21.185 1.00 26.96  ? 59  TYR A OH    1 
ATOM   507  N  N     . LEU A 1 80  ? -21.780 29.904  -17.315 1.00 17.12  ? 60  LEU A N     1 
ATOM   508  C  CA    . LEU A 1 80  ? -21.445 30.880  -16.287 1.00 17.41  ? 60  LEU A CA    1 
ATOM   509  C  C     . LEU A 1 80  ? -21.862 32.278  -16.713 1.00 21.72  ? 60  LEU A C     1 
ATOM   510  O  O     . LEU A 1 80  ? -22.488 33.016  -15.937 1.00 18.33  ? 60  LEU A O     1 
ATOM   511  C  CB    . LEU A 1 80  ? -19.936 30.828  -16.016 1.00 17.09  ? 60  LEU A CB    1 
ATOM   512  C  CG    . LEU A 1 80  ? -19.410 31.851  -15.015 1.00 17.35  ? 60  LEU A CG    1 
ATOM   513  C  CD1   . LEU A 1 80  ? -19.991 31.601  -13.645 1.00 21.52  ? 60  LEU A CD1   1 
ATOM   514  C  CD2   . LEU A 1 80  ? -17.868 31.705  -14.981 1.00 17.51  ? 60  LEU A CD2   1 
ATOM   515  N  N     . GLY A 1 81  ? -21.544 32.649  -17.960 1.00 20.57  ? 61  GLY A N     1 
ATOM   516  C  CA    . GLY A 1 81  ? -21.814 34.011  -18.377 1.00 20.25  ? 61  GLY A CA    1 
ATOM   517  C  C     . GLY A 1 81  ? -23.284 34.343  -18.463 1.00 23.38  ? 61  GLY A C     1 
ATOM   518  O  O     . GLY A 1 81  ? -23.634 35.526  -18.559 1.00 21.30  ? 61  GLY A O     1 
ATOM   519  N  N     . ASN A 1 82  ? -24.143 33.329  -18.411 1.00 18.93  ? 62  ASN A N     1 
ATOM   520  C  CA    . ASN A 1 82  ? -25.580 33.541  -18.540 1.00 19.26  ? 62  ASN A CA    1 
ATOM   521  C  C     . ASN A 1 82  ? -26.341 33.267  -17.254 1.00 22.56  ? 62  ASN A C     1 
ATOM   522  O  O     . ASN A 1 82  ? -27.581 33.300  -17.255 1.00 24.56  ? 62  ASN A O     1 
ATOM   523  C  CB    . ASN A 1 82  ? -26.102 32.678  -19.680 1.00 20.08  ? 62  ASN A CB    1 
ATOM   524  C  CG    . ASN A 1 82  ? -25.787 33.276  -21.028 1.00 28.09  ? 62  ASN A CG    1 
ATOM   525  O  OD1   . ASN A 1 82  ? -26.544 34.107  -21.530 1.00 36.55  ? 62  ASN A OD1   1 
ATOM   526  N  ND2   . ASN A 1 82  ? -24.660 32.880  -21.614 1.00 21.20  ? 62  ASN A ND2   1 
ATOM   527  N  N     . LEU A 1 83  ? -25.639 33.019  -16.156 1.00 23.08  ? 63  LEU A N     1 
ATOM   528  C  CA    . LEU A 1 83  ? -26.287 32.886  -14.865 1.00 22.75  ? 63  LEU A CA    1 
ATOM   529  C  C     . LEU A 1 83  ? -26.986 34.194  -14.488 1.00 26.84  ? 63  LEU A C     1 
ATOM   530  O  O     . LEU A 1 83  ? -26.591 35.277  -14.939 1.00 23.96  ? 63  LEU A O     1 
ATOM   531  C  CB    . LEU A 1 83  ? -25.263 32.503  -13.795 1.00 22.93  ? 63  LEU A CB    1 
ATOM   532  C  CG    . LEU A 1 83  ? -24.697 31.078  -13.841 1.00 25.15  ? 63  LEU A CG    1 
ATOM   533  C  CD1   . LEU A 1 83  ? -23.718 30.850  -12.692 1.00 25.80  ? 63  LEU A CD1   1 
ATOM   534  C  CD2   . LEU A 1 83  ? -25.817 30.022  -13.808 1.00 22.21  ? 63  LEU A CD2   1 
ATOM   535  N  N     . PRO A 1 84  ? -28.026 34.128  -13.658 1.00 25.88  ? 64  PRO A N     1 
ATOM   536  C  CA    . PRO A 1 84  ? -28.695 35.362  -13.234 1.00 29.77  ? 64  PRO A CA    1 
ATOM   537  C  C     . PRO A 1 84  ? -27.721 36.326  -12.572 1.00 30.83  ? 64  PRO A C     1 
ATOM   538  O  O     . PRO A 1 84  ? -26.772 35.918  -11.898 1.00 28.12  ? 64  PRO A O     1 
ATOM   539  C  CB    . PRO A 1 84  ? -29.753 34.868  -12.239 1.00 28.68  ? 64  PRO A CB    1 
ATOM   540  C  CG    . PRO A 1 84  ? -30.025 33.446  -12.664 1.00 26.29  ? 64  PRO A CG    1 
ATOM   541  C  CD    . PRO A 1 84  ? -28.659 32.929  -13.083 1.00 27.43  ? 64  PRO A CD    1 
ATOM   542  N  N     . LYS A 1 85  ? -27.978 37.626  -12.772 1.00 34.30  ? 65  LYS A N     1 
ATOM   543  C  CA    . LYS A 1 85  ? -27.095 38.662  -12.241 1.00 34.83  ? 65  LYS A CA    1 
ATOM   544  C  C     . LYS A 1 85  ? -26.909 38.541  -10.737 1.00 33.66  ? 65  LYS A C     1 
ATOM   545  O  O     . LYS A 1 85  ? -25.834 38.860  -10.221 1.00 33.27  ? 65  LYS A O     1 
ATOM   546  C  CB    . LYS A 1 85  ? -27.649 40.054  -12.560 1.00 44.71  ? 65  LYS A CB    1 
ATOM   547  C  CG    . LYS A 1 85  ? -26.706 41.193  -12.157 1.00 57.91  ? 65  LYS A CG    1 
ATOM   548  C  CD    . LYS A 1 85  ? -27.273 42.577  -12.464 1.00 66.30  ? 65  LYS A CD    1 
ATOM   549  C  CE    . LYS A 1 85  ? -26.186 43.656  -12.401 1.00 68.71  ? 65  LYS A CE    1 
ATOM   550  N  NZ    . LYS A 1 85  ? -25.463 43.705  -11.093 1.00 60.11  ? 65  LYS A NZ    1 
ATOM   551  N  N     . SER A 1 86  ? -27.943 38.101  -10.017 1.00 33.81  ? 66  SER A N     1 
ATOM   552  C  CA    . SER A 1 86  ? -27.816 37.908  -8.577  1.00 36.27  ? 66  SER A CA    1 
ATOM   553  C  C     . SER A 1 86  ? -26.698 36.927  -8.247  1.00 39.03  ? 66  SER A C     1 
ATOM   554  O  O     . SER A 1 86  ? -25.966 37.115  -7.269  1.00 42.53  ? 66  SER A O     1 
ATOM   555  C  CB    . SER A 1 86  ? -29.152 37.441  -7.995  1.00 46.87  ? 66  SER A CB    1 
ATOM   556  O  OG    . SER A 1 86  ? -29.605 36.259  -8.634  1.00 49.68  ? 66  SER A OG    1 
ATOM   557  N  N     . GLU A 1 87  ? -26.548 35.873  -9.054  1.00 33.12  ? 67  GLU A N     1 
ATOM   558  C  CA    . GLU A 1 87  ? -25.471 34.917  -8.818  1.00 31.59  ? 67  GLU A CA    1 
ATOM   559  C  C     . GLU A 1 87  ? -24.120 35.486  -9.225  1.00 24.77  ? 67  GLU A C     1 
ATOM   560  O  O     . GLU A 1 87  ? -23.130 35.314  -8.507  1.00 31.18  ? 67  GLU A O     1 
ATOM   561  C  CB    . GLU A 1 87  ? -25.746 33.619  -9.573  1.00 33.90  ? 67  GLU A CB    1 
ATOM   562  C  CG    . GLU A 1 87  ? -26.853 32.771  -8.975  1.00 35.66  ? 67  GLU A CG    1 
ATOM   563  C  CD    . GLU A 1 87  ? -26.930 31.413  -9.635  1.00 50.64  ? 67  GLU A CD    1 
ATOM   564  O  OE1   . GLU A 1 87  ? -25.860 30.778  -9.812  1.00 39.33  ? 67  GLU A OE1   1 
ATOM   565  O  OE2   . GLU A 1 87  ? -28.052 30.993  -9.996  1.00 46.64  ? 67  GLU A OE2   1 
ATOM   566  N  N     . LEU A 1 88  ? -24.050 36.148  -10.378 1.00 28.00  ? 68  LEU A N     1 
ATOM   567  C  CA    . LEU A 1 88  ? -22.757 36.664  -10.820 1.00 24.61  ? 68  LEU A CA    1 
ATOM   568  C  C     . LEU A 1 88  ? -22.255 37.778  -9.905  1.00 27.83  ? 68  LEU A C     1 
ATOM   569  O  O     . LEU A 1 88  ? -21.046 37.899  -9.691  1.00 26.86  ? 68  LEU A O     1 
ATOM   570  C  CB    . LEU A 1 88  ? -22.845 37.146  -12.267 1.00 27.67  ? 68  LEU A CB    1 
ATOM   571  C  CG    . LEU A 1 88  ? -23.074 36.056  -13.332 1.00 25.62  ? 68  LEU A CG    1 
ATOM   572  C  CD1   . LEU A 1 88  ? -23.172 36.669  -14.705 1.00 27.73  ? 68  LEU A CD1   1 
ATOM   573  C  CD2   . LEU A 1 88  ? -21.955 35.008  -13.301 1.00 26.98  ? 68  LEU A CD2   1 
ATOM   574  N  N     . ASP A 1 89  ? -23.160 38.582  -9.332  1.00 27.82  ? 69  ASP A N     1 
ATOM   575  C  CA    . ASP A 1 89  ? -22.728 39.646  -8.426  1.00 26.46  ? 69  ASP A CA    1 
ATOM   576  C  C     . ASP A 1 89  ? -21.998 39.083  -7.219  1.00 30.53  ? 69  ASP A C     1 
ATOM   577  O  O     . ASP A 1 89  ? -21.053 39.708  -6.722  1.00 31.98  ? 69  ASP A O     1 
ATOM   578  C  CB    . ASP A 1 89  ? -23.925 40.487  -7.967  1.00 33.62  ? 69  ASP A CB    1 
ATOM   579  C  CG    . ASP A 1 89  ? -24.467 41.391  -9.059  1.00 34.21  ? 69  ASP A CG    1 
ATOM   580  O  OD1   . ASP A 1 89  ? -23.793 41.573  -10.094 1.00 44.06  ? 69  ASP A OD1   1 
ATOM   581  O  OD2   . ASP A 1 89  ? -25.573 41.940  -8.868  1.00 43.83  ? 69  ASP A OD2   1 
ATOM   582  N  N     . ARG A 1 90  ? -22.400 37.898  -6.749  1.00 31.44  ? 70  ARG A N     1 
ATOM   583  C  CA    . ARG A 1 90  ? -21.695 37.255  -5.646  1.00 29.60  ? 70  ARG A CA    1 
ATOM   584  C  C     . ARG A 1 90  ? -20.283 36.817  -5.999  1.00 33.71  ? 70  ARG A C     1 
ATOM   585  O  O     . ARG A 1 90  ? -19.509 36.517  -5.081  1.00 31.51  ? 70  ARG A O     1 
ATOM   586  C  CB    . ARG A 1 90  ? -22.488 36.061  -5.118  1.00 42.82  ? 70  ARG A CB    1 
ATOM   587  C  CG    . ARG A 1 90  ? -23.769 36.470  -4.429  1.00 54.08  ? 70  ARG A CG    1 
ATOM   588  C  CD    . ARG A 1 90  ? -24.459 35.284  -3.795  1.00 60.13  ? 70  ARG A CD    1 
ATOM   589  N  NE    . ARG A 1 90  ? -25.587 35.728  -2.987  1.00 84.87  ? 70  ARG A NE    1 
ATOM   590  C  CZ    . ARG A 1 90  ? -25.470 36.082  -1.713  1.00 86.60  ? 70  ARG A CZ    1 
ATOM   591  N  NH1   . ARG A 1 90  ? -24.305 36.025  -1.086  1.00 83.72  ? 70  ARG A NH1   1 
ATOM   592  N  NH2   . ARG A 1 90  ? -26.542 36.510  -1.054  1.00 80.12  ? 70  ARG A NH2   1 
ATOM   593  N  N     . LEU A 1 91  ? -19.922 36.783  -7.283  1.00 27.00  ? 71  LEU A N     1 
ATOM   594  C  CA    . LEU A 1 91  ? -18.600 36.343  -7.698  1.00 26.83  ? 71  LEU A CA    1 
ATOM   595  C  C     . LEU A 1 91  ? -17.670 37.507  -7.991  1.00 25.61  ? 71  LEU A C     1 
ATOM   596  O  O     . LEU A 1 91  ? -16.518 37.288  -8.380  1.00 25.10  ? 71  LEU A O     1 
ATOM   597  C  CB    . LEU A 1 91  ? -18.701 35.441  -8.940  1.00 25.58  ? 71  LEU A CB    1 
ATOM   598  C  CG    . LEU A 1 91  ? -19.585 34.196  -8.780  1.00 26.76  ? 71  LEU A CG    1 
ATOM   599  C  CD1   . LEU A 1 91  ? -19.641 33.396  -10.081 1.00 29.82  ? 71  LEU A CD1   1 
ATOM   600  C  CD2   . LEU A 1 91  ? -19.078 33.320  -7.642  1.00 29.59  ? 71  LEU A CD2   1 
ATOM   601  N  N     . GLU A 1 92  ? -18.119 38.735  -7.776  1.00 29.05  ? 72  GLU A N     1 
ATOM   602  C  CA    . GLU A 1 92  ? -17.287 39.897  -8.048  1.00 32.02  ? 72  GLU A CA    1 
ATOM   603  C  C     . GLU A 1 92  ? -16.414 40.185  -6.832  1.00 32.93  ? 72  GLU A C     1 
ATOM   604  O  O     . GLU A 1 92  ? -16.852 40.028  -5.690  1.00 36.43  ? 72  GLU A O     1 
ATOM   605  C  CB    . GLU A 1 92  ? -18.172 41.093  -8.403  1.00 33.92  ? 72  GLU A CB    1 
ATOM   606  C  CG    . GLU A 1 92  ? -18.864 40.926  -9.765  1.00 37.89  ? 72  GLU A CG    1 
ATOM   607  C  CD    . GLU A 1 92  ? -19.523 42.201  -10.263 1.00 52.75  ? 72  GLU A CD    1 
ATOM   608  O  OE1   . GLU A 1 92  ? -19.242 43.281  -9.700  1.00 51.89  ? 72  GLU A OE1   1 
ATOM   609  O  OE2   . GLU A 1 92  ? -20.332 42.115  -11.212 1.00 50.89  ? 72  GLU A OE2   1 
ATOM   610  N  N     . ASN A 1 93  ? -15.155 40.573  -7.081  1.00 25.72  ? 73  ASN A N     1 
ATOM   611  C  CA    . ASN A 1 93  ? -14.215 40.909  -6.006  1.00 26.27  ? 73  ASN A CA    1 
ATOM   612  C  C     . ASN A 1 93  ? -13.433 42.153  -6.427  1.00 23.54  ? 73  ASN A C     1 
ATOM   613  O  O     . ASN A 1 93  ? -12.392 42.054  -7.077  1.00 24.88  ? 73  ASN A O     1 
ATOM   614  C  CB    . ASN A 1 93  ? -13.282 39.745  -5.691  1.00 28.74  ? 73  ASN A CB    1 
ATOM   615  C  CG    . ASN A 1 93  ? -12.370 40.029  -4.497  1.00 40.01  ? 73  ASN A CG    1 
ATOM   616  O  OD1   . ASN A 1 93  ? -12.084 41.186  -4.172  1.00 32.98  ? 73  ASN A OD1   1 
ATOM   617  N  ND2   . ASN A 1 93  ? -11.900 38.970  -3.851  1.00 39.47  ? 73  ASN A ND2   1 
ATOM   618  N  N     . GLU A 1 94  ? -13.930 43.323  -6.012  1.00 28.81  ? 74  GLU A N     1 
ATOM   619  C  CA    . GLU A 1 94  ? -13.281 44.578  -6.375  1.00 26.92  ? 74  GLU A CA    1 
ATOM   620  C  C     . GLU A 1 94  ? -11.942 44.756  -5.668  1.00 28.62  ? 74  GLU A C     1 
ATOM   621  O  O     . GLU A 1 94  ? -11.023 45.362  -6.233  1.00 27.24  ? 74  GLU A O     1 
ATOM   622  C  CB    . GLU A 1 94  ? -14.220 45.749  -6.069  1.00 28.93  ? 74  GLU A CB    1 
ATOM   623  C  CG    . GLU A 1 94  ? -13.683 47.105  -6.495  1.00 36.62  ? 74  GLU A CG    1 
ATOM   624  C  CD    . GLU A 1 94  ? -14.622 48.245  -6.116  1.00 47.84  ? 74  GLU A CD    1 
ATOM   625  O  OE1   . GLU A 1 94  ? -15.661 47.974  -5.476  1.00 40.97  ? 74  GLU A OE1   1 
ATOM   626  O  OE2   . GLU A 1 94  ? -14.326 49.406  -6.470  1.00 55.02  ? 74  GLU A OE2   1 
ATOM   627  N  N     . LYS A 1 95  ? -11.815 44.257  -4.436  1.00 29.04  ? 75  LYS A N     1 
ATOM   628  C  CA    . LYS A 1 95  ? -10.543 44.359  -3.726  1.00 31.96  ? 75  LYS A CA    1 
ATOM   629  C  C     . LYS A 1 95  ? -9.431  43.618  -4.465  1.00 37.50  ? 75  LYS A C     1 
ATOM   630  O  O     . LYS A 1 95  ? -8.283  44.080  -4.498  1.00 30.23  ? 75  LYS A O     1 
ATOM   631  C  CB    . LYS A 1 95  ? -10.704 43.826  -2.301  1.00 35.17  ? 75  LYS A CB    1 
ATOM   632  C  CG    . LYS A 1 95  ? -9.489  44.033  -1.409  1.00 39.59  ? 75  LYS A CG    1 
ATOM   633  C  CD    . LYS A 1 95  ? -9.852  43.825  0.060   1.00 57.92  ? 75  LYS A CD    1 
ATOM   634  C  CE    . LYS A 1 95  ? -9.537  42.419  0.541   1.00 58.85  ? 75  LYS A CE    1 
ATOM   635  N  NZ    . LYS A 1 95  ? -8.075  42.130  0.471   1.00 46.58  ? 75  LYS A NZ    1 
ATOM   636  N  N     . ALA A 1 96  ? -9.763  42.509  -5.119  1.00 35.40  ? 76  ALA A N     1 
ATOM   637  C  CA    . ALA A 1 96  ? -8.793  41.779  -5.916  1.00 30.21  ? 76  ALA A CA    1 
ATOM   638  C  C     . ALA A 1 96  ? -8.568  42.406  -7.284  1.00 31.66  ? 76  ALA A C     1 
ATOM   639  O  O     . ALA A 1 96  ? -7.944  41.777  -8.147  1.00 25.67  ? 76  ALA A O     1 
ATOM   640  C  CB    . ALA A 1 96  ? -9.236  40.322  -6.071  1.00 32.13  ? 76  ALA A CB    1 
ATOM   641  N  N     . LYS A 1 97  ? -9.062  43.626  -7.506  1.00 25.49  ? 77  LYS A N     1 
ATOM   642  C  CA    . LYS A 1 97  ? -8.954  44.280  -8.806  1.00 26.95  ? 77  LYS A CA    1 
ATOM   643  C  C     . LYS A 1 97  ? -9.647  43.458  -9.889  1.00 19.15  ? 77  LYS A C     1 
ATOM   644  O  O     . LYS A 1 97  ? -9.264  43.494  -11.063 1.00 24.27  ? 77  LYS A O     1 
ATOM   645  C  CB    . LYS A 1 97  ? -7.488  44.566  -9.171  1.00 31.06  ? 77  LYS A CB    1 
ATOM   646  C  CG    . LYS A 1 97  ? -6.726  45.323  -8.070  1.00 39.10  ? 77  LYS A CG    1 
ATOM   647  C  CD    . LYS A 1 97  ? -5.472  46.013  -8.604  1.00 40.78  ? 77  LYS A CD    1 
ATOM   648  C  CE    . LYS A 1 97  ? -4.255  45.088  -8.604  1.00 54.14  ? 77  LYS A CE    1 
ATOM   649  N  NZ    . LYS A 1 97  ? -3.552  45.057  -7.283  1.00 57.19  ? 77  LYS A NZ    1 
ATOM   650  N  N     . TYR A 1 98  ? -10.676 42.708  -9.485  1.00 23.68  ? 78  TYR A N     1 
ATOM   651  C  CA    . TYR A 1 98  ? -11.460 41.848  -10.371 1.00 22.83  ? 78  TYR A CA    1 
ATOM   652  C  C     . TYR A 1 98  ? -10.611 40.755  -11.013 1.00 20.85  ? 78  TYR A C     1 
ATOM   653  O  O     . TYR A 1 98  ? -10.978 40.205  -12.056 1.00 23.35  ? 78  TYR A O     1 
ATOM   654  C  CB    . TYR A 1 98  ? -12.199 42.676  -11.439 1.00 22.18  ? 78  TYR A CB    1 
ATOM   655  C  CG    . TYR A 1 98  ? -13.073 43.768  -10.851 1.00 21.76  ? 78  TYR A CG    1 
ATOM   656  C  CD1   . TYR A 1 98  ? -14.271 43.459  -10.221 1.00 23.75  ? 78  TYR A CD1   1 
ATOM   657  C  CD2   . TYR A 1 98  ? -12.682 45.102  -10.903 1.00 27.24  ? 78  TYR A CD2   1 
ATOM   658  C  CE1   . TYR A 1 98  ? -15.070 44.453  -9.674  1.00 30.76  ? 78  TYR A CE1   1 
ATOM   659  C  CE2   . TYR A 1 98  ? -13.480 46.108  -10.358 1.00 28.53  ? 78  TYR A CE2   1 
ATOM   660  C  CZ    . TYR A 1 98  ? -14.668 45.773  -9.747  1.00 31.61  ? 78  TYR A CZ    1 
ATOM   661  O  OH    . TYR A 1 98  ? -15.458 46.760  -9.204  1.00 36.90  ? 78  TYR A OH    1 
ATOM   662  N  N     . LEU A 1 99  ? -9.465  40.440  -10.412 1.00 20.12  ? 79  LEU A N     1 
ATOM   663  C  CA    . LEU A 1 99  ? -8.593  39.368  -10.869 1.00 19.71  ? 79  LEU A CA    1 
ATOM   664  C  C     . LEU A 1 99  ? -8.821  38.081  -10.086 1.00 20.35  ? 79  LEU A C     1 
ATOM   665  O  O     . LEU A 1 99  ? -8.027  37.138  -10.182 1.00 21.27  ? 79  LEU A O     1 
ATOM   666  C  CB    . LEU A 1 99  ? -7.136  39.832  -10.793 1.00 22.53  ? 79  LEU A CB    1 
ATOM   667  C  CG    . LEU A 1 99  ? -6.914  40.970  -11.800 1.00 22.61  ? 79  LEU A CG    1 
ATOM   668  C  CD1   . LEU A 1 99  ? -5.503  41.536  -11.689 1.00 21.89  ? 79  LEU A CD1   1 
ATOM   669  C  CD2   . LEU A 1 99  ? -7.187  40.526  -13.244 1.00 22.50  ? 79  LEU A CD2   1 
ATOM   670  N  N     . THR A 1 100 ? -9.906  38.036  -9.322  1.00 19.50  ? 80  THR A N     1 
ATOM   671  C  CA    . THR A 1 100 ? -10.465 36.830  -8.735  1.00 18.84  ? 80  THR A CA    1 
ATOM   672  C  C     . THR A 1 100 ? -11.962 36.895  -8.978  1.00 19.71  ? 80  THR A C     1 
ATOM   673  O  O     . THR A 1 100 ? -12.572 37.942  -8.745  1.00 22.06  ? 80  THR A O     1 
ATOM   674  C  CB    . THR A 1 100 ? -10.188 36.751  -7.229  1.00 23.77  ? 80  THR A CB    1 
ATOM   675  O  OG1   . THR A 1 100 ? -8.792  36.510  -7.016  1.00 23.98  ? 80  THR A OG1   1 
ATOM   676  C  CG2   . THR A 1 100 ? -11.016 35.643  -6.587  1.00 28.61  ? 80  THR A CG2   1 
ATOM   677  N  N     . GLY A 1 101 ? -12.546 35.807  -9.470  1.00 17.95  ? 81  GLY A N     1 
ATOM   678  C  CA    . GLY A 1 101 ? -13.986 35.782  -9.675  1.00 18.16  ? 81  GLY A CA    1 
ATOM   679  C  C     . GLY A 1 101 ? -14.399 36.389  -11.007 1.00 19.43  ? 81  GLY A C     1 
ATOM   680  O  O     . GLY A 1 101 ? -13.640 36.410  -11.971 1.00 18.38  ? 81  GLY A O     1 
ATOM   681  N  N     . TRP A 1 102 ? -15.649 36.870  -11.057 1.00 18.46  ? 82  TRP A N     1 
ATOM   682  C  CA    . TRP A 1 102 ? -16.282 37.287  -12.301 1.00 18.90  ? 82  TRP A CA    1 
ATOM   683  C  C     . TRP A 1 102 ? -16.249 38.801  -12.480 1.00 22.05  ? 82  TRP A C     1 
ATOM   684  O  O     . TRP A 1 102 ? -16.350 39.562  -11.514 1.00 24.49  ? 82  TRP A O     1 
ATOM   685  C  CB    . TRP A 1 102 ? -17.740 36.804  -12.324 1.00 18.49  ? 82  TRP A CB    1 
ATOM   686  C  CG    . TRP A 1 102 ? -18.553 37.325  -13.483 1.00 21.52  ? 82  TRP A CG    1 
ATOM   687  C  CD1   . TRP A 1 102 ? -19.417 38.392  -13.469 1.00 25.37  ? 82  TRP A CD1   1 
ATOM   688  C  CD2   . TRP A 1 102 ? -18.593 36.796  -14.809 1.00 23.50  ? 82  TRP A CD2   1 
ATOM   689  N  NE1   . TRP A 1 102 ? -19.971 38.567  -14.714 1.00 25.29  ? 82  TRP A NE1   1 
ATOM   690  C  CE2   . TRP A 1 102 ? -19.494 37.592  -15.552 1.00 25.23  ? 82  TRP A CE2   1 
ATOM   691  C  CE3   . TRP A 1 102 ? -17.964 35.718  -15.441 1.00 23.25  ? 82  TRP A CE3   1 
ATOM   692  C  CZ2   . TRP A 1 102 ? -19.768 37.354  -16.898 1.00 23.47  ? 82  TRP A CZ2   1 
ATOM   693  C  CZ3   . TRP A 1 102 ? -18.243 35.478  -16.789 1.00 25.46  ? 82  TRP A CZ3   1 
ATOM   694  C  CH2   . TRP A 1 102 ? -19.133 36.293  -17.498 1.00 23.22  ? 82  TRP A CH2   1 
ATOM   695  N  N     . SER A 1 103 ? -16.143 39.233  -13.738 1.00 23.60  ? 83  SER A N     1 
ATOM   696  C  CA    . SER A 1 103 ? -16.340 40.653  -14.049 1.00 26.64  ? 83  SER A CA    1 
ATOM   697  C  C     . SER A 1 103 ? -16.589 40.835  -15.539 1.00 21.38  ? 83  SER A C     1 
ATOM   698  O  O     . SER A 1 103 ? -16.343 39.937  -16.341 1.00 24.11  ? 83  SER A O     1 
ATOM   699  C  CB    . SER A 1 103 ? -15.147 41.513  -13.615 1.00 24.99  ? 83  SER A CB    1 
ATOM   700  O  OG    . SER A 1 103 ? -14.002 41.155  -14.354 1.00 24.34  ? 83  SER A OG    1 
ATOM   701  N  N     . LEU A 1 104 ? -17.111 42.011  -15.889 1.00 26.97  ? 84  LEU A N     1 
ATOM   702  C  CA    . LEU A 1 104 ? -17.398 42.394  -17.270 1.00 25.62  ? 84  LEU A CA    1 
ATOM   703  C  C     . LEU A 1 104 ? -16.360 43.374  -17.801 1.00 24.69  ? 84  LEU A C     1 
ATOM   704  O  O     . LEU A 1 104 ? -16.013 44.341  -17.121 1.00 26.40  ? 84  LEU A O     1 
ATOM   705  C  CB    . LEU A 1 104 ? -18.780 43.042  -17.372 1.00 28.50  ? 84  LEU A CB    1 
ATOM   706  C  CG    . LEU A 1 104 ? -20.037 42.187  -17.393 1.00 35.61  ? 84  LEU A CG    1 
ATOM   707  C  CD1   . LEU A 1 104 ? -21.232 43.106  -17.582 1.00 32.26  ? 84  LEU A CD1   1 
ATOM   708  C  CD2   . LEU A 1 104 ? -19.972 41.173  -18.516 1.00 37.31  ? 84  LEU A CD2   1 
ATOM   709  N  N     . GLY A 1 105 ? -15.880 43.132  -19.027 1.00 25.10  ? 85  GLY A N     1 
ATOM   710  C  CA    . GLY A 1 105 ? -14.954 44.029  -19.678 1.00 28.14  ? 85  GLY A CA    1 
ATOM   711  C  C     . GLY A 1 105 ? -15.386 44.271  -21.115 1.00 30.80  ? 85  GLY A C     1 
ATOM   712  O  O     . GLY A 1 105 ? -16.328 43.646  -21.620 1.00 30.66  ? 85  GLY A O     1 
ATOM   713  N  N     . LYS A 1 106 ? -14.675 45.181  -21.777 1.00 30.76  ? 86  LYS A N     1 
ATOM   714  C  CA    . LYS A 1 106 ? -15.056 45.591  -23.120 1.00 36.41  ? 86  LYS A CA    1 
ATOM   715  C  C     . LYS A 1 106 ? -13.823 45.649  -24.008 1.00 42.13  ? 86  LYS A C     1 
ATOM   716  O  O     . LYS A 1 106 ? -12.725 45.990  -23.563 1.00 35.15  ? 86  LYS A O     1 
ATOM   717  C  CB    . LYS A 1 106 ? -15.767 46.948  -23.106 1.00 34.99  ? 86  LYS A CB    1 
ATOM   718  C  CG    . LYS A 1 106 ? -16.434 47.326  -24.410 1.00 46.15  ? 86  LYS A CG    1 
ATOM   719  C  CD    . LYS A 1 106 ? -16.913 48.755  -24.328 1.00 49.63  ? 86  LYS A CD    1 
ATOM   720  C  CE    . LYS A 1 106 ? -17.963 49.082  -25.365 1.00 49.55  ? 86  LYS A CE    1 
ATOM   721  N  NZ    . LYS A 1 106 ? -18.411 50.498  -25.216 1.00 46.82  ? 86  LYS A NZ    1 
ATOM   722  N  N     . GLU A 1 107 ? -14.026 45.316  -25.278 1.00 36.42  ? 87  GLU A N     1 
ATOM   723  C  CA    . GLU A 1 107 ? -12.994 45.365  -26.300 1.00 36.93  ? 87  GLU A CA    1 
ATOM   724  C  C     . GLU A 1 107 ? -13.470 46.263  -27.436 1.00 35.12  ? 87  GLU A C     1 
ATOM   725  O  O     . GLU A 1 107 ? -14.594 46.106  -27.918 1.00 36.27  ? 87  GLU A O     1 
ATOM   726  C  CB    . GLU A 1 107 ? -12.716 43.933  -26.764 1.00 42.90  ? 87  GLU A CB    1 
ATOM   727  C  CG    . GLU A 1 107 ? -11.972 43.744  -28.047 1.00 36.76  ? 87  GLU A CG    1 
ATOM   728  C  CD    . GLU A 1 107 ? -11.776 42.264  -28.336 1.00 28.35  ? 87  GLU A CD    1 
ATOM   729  O  OE1   . GLU A 1 107 ? -11.318 41.534  -27.422 1.00 28.24  ? 87  GLU A OE1   1 
ATOM   730  O  OE2   . GLU A 1 107 ? -12.109 41.829  -29.452 1.00 30.50  ? 87  GLU A OE2   1 
ATOM   731  N  N     . THR A 1 108 ? -12.637 47.215  -27.849 1.00 42.16  ? 88  THR A N     1 
ATOM   732  C  CA    . THR A 1 108 ? -13.012 48.142  -28.910 1.00 53.99  ? 88  THR A CA    1 
ATOM   733  C  C     . THR A 1 108 ? -12.003 48.108  -30.052 1.00 57.83  ? 88  THR A C     1 
ATOM   734  O  O     . THR A 1 108 ? -10.819 47.814  -29.856 1.00 48.80  ? 88  THR A O     1 
ATOM   735  C  CB    . THR A 1 108 ? -13.164 49.578  -28.382 1.00 55.14  ? 88  THR A CB    1 
ATOM   736  O  OG1   . THR A 1 108 ? -12.036 49.920  -27.569 1.00 56.39  ? 88  THR A OG1   1 
ATOM   737  C  CG2   . THR A 1 108 ? -14.442 49.708  -27.566 1.00 51.03  ? 88  THR A CG2   1 
ATOM   738  N  N     . LEU A 1 109 ? -12.492 48.423  -31.250 1.00 68.03  ? 89  LEU A N     1 
ATOM   739  C  CA    . LEU A 1 109 ? -11.686 48.414  -32.467 1.00 72.46  ? 89  LEU A CA    1 
ATOM   740  C  C     . LEU A 1 109 ? -11.232 49.823  -32.844 1.00 67.00  ? 89  LEU A C     1 
ATOM   741  O  O     . LEU A 1 109 ? -10.041 50.133  -32.831 1.00 64.57  ? 89  LEU A O     1 
ATOM   742  C  CB    . LEU A 1 109 ? -12.485 47.797  -33.618 1.00 69.41  ? 89  LEU A CB    1 
ATOM   743  C  CG    . LEU A 1 109 ? -11.743 47.485  -34.917 1.00 78.16  ? 89  LEU A CG    1 
ATOM   744  C  CD1   . LEU A 1 109 ? -10.734 46.368  -34.694 1.00 69.96  ? 89  LEU A CD1   1 
ATOM   745  C  CD2   . LEU A 1 109 ? -12.725 47.117  -36.025 1.00 67.62  ? 89  LEU A CD2   1 
ATOM   746  N  N     . ASP A 1 115 ? -15.915 46.212  -30.534 1.00 71.00  ? 95  ASP A N     1 
ATOM   747  C  CA    . ASP A 1 115 ? -17.020 46.724  -29.729 1.00 70.57  ? 95  ASP A CA    1 
ATOM   748  C  C     . ASP A 1 115 ? -17.759 45.571  -29.047 1.00 70.34  ? 95  ASP A C     1 
ATOM   749  O  O     . ASP A 1 115 ? -18.988 45.511  -29.049 1.00 74.39  ? 95  ASP A O     1 
ATOM   750  C  CB    . ASP A 1 115 ? -17.980 47.536  -30.598 1.00 70.43  ? 95  ASP A CB    1 
ATOM   751  C  CG    . ASP A 1 115 ? -18.737 48.574  -29.807 1.00 83.36  ? 95  ASP A CG    1 
ATOM   752  O  OD1   . ASP A 1 115 ? -18.351 48.826  -28.645 1.00 76.60  ? 95  ASP A OD1   1 
ATOM   753  O  OD2   . ASP A 1 115 ? -19.715 49.136  -30.344 1.00 91.66  ? 95  ASP A OD2   1 
ATOM   754  N  N     . ASN A 1 116 ? -16.985 44.670  -28.453 1.00 41.86  ? 96  ASN A N     1 
ATOM   755  C  CA    . ASN A 1 116 ? -17.461 43.415  -27.893 1.00 44.38  ? 96  ASN A CA    1 
ATOM   756  C  C     . ASN A 1 116 ? -17.430 43.428  -26.371 1.00 34.83  ? 96  ASN A C     1 
ATOM   757  O  O     . ASN A 1 116 ? -16.489 43.939  -25.759 1.00 37.88  ? 96  ASN A O     1 
ATOM   758  C  CB    . ASN A 1 116 ? -16.633 42.235  -28.402 1.00 45.41  ? 96  ASN A CB    1 
ATOM   759  C  CG    . ASN A 1 116 ? -17.119 41.717  -29.738 1.00 56.20  ? 96  ASN A CG    1 
ATOM   760  O  OD1   . ASN A 1 116 ? -18.238 42.013  -30.162 1.00 60.98  ? 96  ASN A OD1   1 
ATOM   761  N  ND2   . ASN A 1 116 ? -16.291 40.916  -30.399 1.00 50.09  ? 96  ASN A ND2   1 
ATOM   762  N  N     . LEU A 1 117 ? -18.462 42.851  -25.772 1.00 29.63  ? 97  LEU A N     1 
ATOM   763  C  CA    . LEU A 1 117 ? -18.514 42.642  -24.333 1.00 28.50  ? 97  LEU A CA    1 
ATOM   764  C  C     . LEU A 1 117 ? -17.938 41.267  -24.006 1.00 23.09  ? 97  LEU A C     1 
ATOM   765  O  O     . LEU A 1 117 ? -18.211 40.293  -24.712 1.00 26.76  ? 97  LEU A O     1 
ATOM   766  C  CB    . LEU A 1 117 ? -19.964 42.739  -23.859 1.00 27.31  ? 97  LEU A CB    1 
ATOM   767  C  CG    . LEU A 1 117 ? -20.255 42.716  -22.364 1.00 39.21  ? 97  LEU A CG    1 
ATOM   768  C  CD1   . LEU A 1 117 ? -19.724 43.980  -21.709 1.00 37.95  ? 97  LEU A CD1   1 
ATOM   769  C  CD2   . LEU A 1 117 ? -21.748 42.566  -22.143 1.00 40.70  ? 97  LEU A CD2   1 
ATOM   770  N  N     . LYS A 1 118 ? -17.085 41.196  -22.988 1.00 22.27  ? 98  LYS A N     1 
ATOM   771  C  CA    . LYS A 1 118 ? -16.455 39.927  -22.633 1.00 23.93  ? 98  LYS A CA    1 
ATOM   772  C  C     . LYS A 1 118 ? -16.425 39.792  -21.117 1.00 25.31  ? 98  LYS A C     1 
ATOM   773  O  O     . LYS A 1 118 ? -15.902 40.665  -20.423 1.00 31.53  ? 98  LYS A O     1 
ATOM   774  C  CB    . LYS A 1 118 ? -15.047 39.799  -23.236 1.00 29.88  ? 98  LYS A CB    1 
ATOM   775  C  CG    . LYS A 1 118 ? -14.163 41.019  -23.123 1.00 33.92  ? 98  LYS A CG    1 
ATOM   776  C  CD    . LYS A 1 118 ? -12.915 40.822  -23.989 1.00 27.90  ? 98  LYS A CD    1 
ATOM   777  C  CE    . LYS A 1 118 ? -11.905 41.935  -23.768 1.00 35.99  ? 98  LYS A CE    1 
ATOM   778  N  NZ    . LYS A 1 118 ? -10.655 41.670  -24.542 1.00 35.66  ? 98  LYS A NZ    1 
ATOM   779  N  N     . GLY A 1 119 ? -16.983 38.692  -20.614 1.00 21.08  ? 99  GLY A N     1 
ATOM   780  C  CA    . GLY A 1 119 ? -16.920 38.365  -19.202 1.00 20.02  ? 99  GLY A CA    1 
ATOM   781  C  C     . GLY A 1 119 ? -15.733 37.479  -18.885 1.00 17.74  ? 99  GLY A C     1 
ATOM   782  O  O     . GLY A 1 119 ? -15.459 36.518  -19.605 1.00 18.16  ? 99  GLY A O     1 
ATOM   783  N  N     . SER A 1 120 ? -15.018 37.818  -17.813 1.00 19.87  ? 100 SER A N     1 
ATOM   784  C  CA    . SER A 1 120 ? -13.864 37.051  -17.364 1.00 16.91  ? 100 SER A CA    1 
ATOM   785  C  C     . SER A 1 120 ? -14.136 36.395  -16.018 1.00 17.50  ? 100 SER A C     1 
ATOM   786  O  O     . SER A 1 120 ? -14.737 37.003  -15.125 1.00 18.16  ? 100 SER A O     1 
ATOM   787  C  CB    . SER A 1 120 ? -12.605 37.931  -17.235 1.00 20.65  ? 100 SER A CB    1 
ATOM   788  O  OG    . SER A 1 120 ? -12.203 38.502  -18.484 1.00 25.81  ? 100 SER A OG    1 
ATOM   789  N  N     . TYR A 1 121 ? -13.652 35.158  -15.874 1.00 16.57  ? 101 TYR A N     1 
ATOM   790  C  CA    . TYR A 1 121 ? -13.661 34.446  -14.606 1.00 16.70  ? 101 TYR A CA    1 
ATOM   791  C  C     . TYR A 1 121 ? -12.228 34.043  -14.287 1.00 16.51  ? 101 TYR A C     1 
ATOM   792  O  O     . TYR A 1 121 ? -11.596 33.308  -15.053 1.00 16.18  ? 101 TYR A O     1 
ATOM   793  C  CB    . TYR A 1 121 ? -14.590 33.215  -14.644 1.00 17.88  ? 101 TYR A CB    1 
ATOM   794  C  CG    . TYR A 1 121 ? -14.589 32.505  -13.314 1.00 16.87  ? 101 TYR A CG    1 
ATOM   795  C  CD1   . TYR A 1 121 ? -15.386 32.955  -12.267 1.00 17.32  ? 101 TYR A CD1   1 
ATOM   796  C  CD2   . TYR A 1 121 ? -13.727 31.439  -13.079 1.00 16.67  ? 101 TYR A CD2   1 
ATOM   797  C  CE1   . TYR A 1 121 ? -15.348 32.338  -11.023 1.00 19.07  ? 101 TYR A CE1   1 
ATOM   798  C  CE2   . TYR A 1 121 ? -13.673 30.816  -11.836 1.00 18.66  ? 101 TYR A CE2   1 
ATOM   799  C  CZ    . TYR A 1 121 ? -14.482 31.272  -10.818 1.00 19.21  ? 101 TYR A CZ    1 
ATOM   800  O  OH    . TYR A 1 121 ? -14.429 30.649  -9.594  1.00 21.03  ? 101 TYR A OH    1 
ATOM   801  N  N     . TYR A 1 122 ? -11.728 34.507  -13.145 1.00 16.75  ? 102 TYR A N     1 
ATOM   802  C  CA    . TYR A 1 122 ? -10.343 34.268  -12.761 1.00 18.35  ? 102 TYR A CA    1 
ATOM   803  C  C     . TYR A 1 122 ? -10.291 33.398  -11.515 1.00 17.54  ? 102 TYR A C     1 
ATOM   804  O  O     . TYR A 1 122 ? -11.070 33.589  -10.576 1.00 17.13  ? 102 TYR A O     1 
ATOM   805  C  CB    . TYR A 1 122 ? -9.608  35.574  -12.463 1.00 18.73  ? 102 TYR A CB    1 
ATOM   806  C  CG    . TYR A 1 122 ? -9.276  36.483  -13.628 1.00 18.19  ? 102 TYR A CG    1 
ATOM   807  C  CD1   . TYR A 1 122 ? -8.056  36.379  -14.291 1.00 21.77  ? 102 TYR A CD1   1 
ATOM   808  C  CD2   . TYR A 1 122 ? -10.161 37.476  -14.030 1.00 18.99  ? 102 TYR A CD2   1 
ATOM   809  C  CE1   . TYR A 1 122 ? -7.735  37.232  -15.342 1.00 20.84  ? 102 TYR A CE1   1 
ATOM   810  C  CE2   . TYR A 1 122 ? -9.850  38.328  -15.072 1.00 21.55  ? 102 TYR A CE2   1 
ATOM   811  C  CZ    . TYR A 1 122 ? -8.640  38.203  -15.725 1.00 23.52  ? 102 TYR A CZ    1 
ATOM   812  O  OH    . TYR A 1 122 ? -8.352  39.067  -16.766 1.00 27.42  ? 102 TYR A OH    1 
ATOM   813  N  N     . ALA A 1 123 ? -9.321  32.490  -11.480 1.00 16.61  ? 103 ALA A N     1 
ATOM   814  C  CA    . ALA A 1 123 ? -9.065  31.712  -10.274 1.00 16.81  ? 103 ALA A CA    1 
ATOM   815  C  C     . ALA A 1 123 ? -7.573  31.482  -10.131 1.00 18.49  ? 103 ALA A C     1 
ATOM   816  O  O     . ALA A 1 123 ? -6.887  31.223  -11.120 1.00 19.19  ? 103 ALA A O     1 
ATOM   817  C  CB    . ALA A 1 123 ? -9.773  30.354  -10.304 1.00 18.41  ? 103 ALA A CB    1 
ATOM   818  N  N     . ASN A 1 124 ? -7.074  31.556  -8.903  1.00 16.98  ? 104 ASN A N     1 
ATOM   819  C  CA    . ASN A 1 124 ? -5.702  31.108  -8.718  1.00 18.75  ? 104 ASN A CA    1 
ATOM   820  C  C     . ASN A 1 124 ? -5.660  29.582  -8.758  1.00 17.38  ? 104 ASN A C     1 
ATOM   821  O  O     . ASN A 1 124 ? -6.659  28.897  -8.524  1.00 17.93  ? 104 ASN A O     1 
ATOM   822  C  CB    . ASN A 1 124 ? -5.111  31.626  -7.403  1.00 18.54  ? 104 ASN A CB    1 
ATOM   823  C  CG    . ASN A 1 124 ? -5.699  30.931  -6.190  1.00 19.45  ? 104 ASN A CG    1 
ATOM   824  O  OD1   . ASN A 1 124 ? -5.399  29.767  -5.919  1.00 20.32  ? 104 ASN A OD1   1 
ATOM   825  N  ND2   . ASN A 1 124 ? -6.534  31.646  -5.446  1.00 18.23  ? 104 ASN A ND2   1 
ATOM   826  N  N     . CYS A 1 125 ? -4.480  29.045  -9.065  1.00 16.98  ? 105 CYS A N     1 
ATOM   827  C  CA    . CYS A 1 125 ? -4.302  27.607  -9.196  1.00 16.79  ? 105 CYS A CA    1 
ATOM   828  C  C     . CYS A 1 125 ? -3.465  27.022  -8.068  1.00 17.96  ? 105 CYS A C     1 
ATOM   829  O  O     . CYS A 1 125 ? -2.706  26.078  -8.293  1.00 18.17  ? 105 CYS A O     1 
ATOM   830  C  CB    . CYS A 1 125 ? -3.680  27.264  -10.550 1.00 16.69  ? 105 CYS A CB    1 
ATOM   831  S  SG    . CYS A 1 125 ? -4.783  27.701  -11.930 1.00 17.39  ? 105 CYS A SG    1 
ATOM   832  N  N     . ALA A 1 126 ? -3.600  27.574  -6.855  1.00 17.82  ? 106 ALA A N     1 
ATOM   833  C  CA    . ALA A 1 126 ? -2.926  26.999  -5.695  1.00 18.15  ? 106 ALA A CA    1 
ATOM   834  C  C     . ALA A 1 126 ? -3.318  25.539  -5.499  1.00 18.82  ? 106 ALA A C     1 
ATOM   835  O  O     . ALA A 1 126 ? -2.523  24.739  -4.988  1.00 20.05  ? 106 ALA A O     1 
ATOM   836  C  CB    . ALA A 1 126 ? -3.253  27.818  -4.436  1.00 18.05  ? 106 ALA A CB    1 
ATOM   837  N  N     . PHE A 1 127 ? -4.535  25.171  -5.915  1.00 17.82  ? 107 PHE A N     1 
ATOM   838  C  CA    . PHE A 1 127 ? -5.000  23.793  -5.807  1.00 19.58  ? 107 PHE A CA    1 
ATOM   839  C  C     . PHE A 1 127 ? -4.083  22.809  -6.517  1.00 20.05  ? 107 PHE A C     1 
ATOM   840  O  O     . PHE A 1 127 ? -4.099  21.620  -6.180  1.00 22.15  ? 107 PHE A O     1 
ATOM   841  C  CB    . PHE A 1 127 ? -6.435  23.659  -6.366  1.00 19.75  ? 107 PHE A CB    1 
ATOM   842  C  CG    . PHE A 1 127 ? -6.570  24.034  -7.827  1.00 19.63  ? 107 PHE A CG    1 
ATOM   843  C  CD1   . PHE A 1 127 ? -6.234  23.138  -8.839  1.00 19.81  ? 107 PHE A CD1   1 
ATOM   844  C  CD2   . PHE A 1 127 ? -7.060  25.285  -8.186  1.00 20.02  ? 107 PHE A CD2   1 
ATOM   845  C  CE1   . PHE A 1 127 ? -6.358  23.495  -10.177 1.00 16.84  ? 107 PHE A CE1   1 
ATOM   846  C  CE2   . PHE A 1 127 ? -7.199  25.647  -9.515  1.00 21.61  ? 107 PHE A CE2   1 
ATOM   847  C  CZ    . PHE A 1 127 ? -6.844  24.750  -10.519 1.00 22.36  ? 107 PHE A CZ    1 
ATOM   848  N  N     . TYR A 1 128 ? -3.300  23.274  -7.501  1.00 20.17  ? 108 TYR A N     1 
ATOM   849  C  CA    . TYR A 1 128 ? -2.363  22.399  -8.197  1.00 18.40  ? 108 TYR A CA    1 
ATOM   850  C  C     . TYR A 1 128 ? -1.350  21.815  -7.235  1.00 17.97  ? 108 TYR A C     1 
ATOM   851  O  O     . TYR A 1 128 ? -0.988  20.638  -7.339  1.00 22.42  ? 108 TYR A O     1 
ATOM   852  C  CB    . TYR A 1 128 ? -1.634  23.179  -9.299  1.00 19.84  ? 108 TYR A CB    1 
ATOM   853  C  CG    . TYR A 1 128 ? -0.681  22.333  -10.110 1.00 17.59  ? 108 TYR A CG    1 
ATOM   854  C  CD1   . TYR A 1 128 ? -1.149  21.508  -11.126 1.00 19.47  ? 108 TYR A CD1   1 
ATOM   855  C  CD2   . TYR A 1 128 ? 0.691   22.355  -9.863  1.00 20.67  ? 108 TYR A CD2   1 
ATOM   856  C  CE1   . TYR A 1 128 ? -0.288  20.714  -11.867 1.00 19.81  ? 108 TYR A CE1   1 
ATOM   857  C  CE2   . TYR A 1 128 ? 1.562   21.563  -10.602 1.00 23.63  ? 108 TYR A CE2   1 
ATOM   858  C  CZ    . TYR A 1 128 ? 1.067   20.749  -11.602 1.00 21.53  ? 108 TYR A CZ    1 
ATOM   859  O  OH    . TYR A 1 128 ? 1.907   19.955  -12.356 1.00 23.26  ? 108 TYR A OH    1 
ATOM   860  N  N     . VAL A 1 129 ? -0.873  22.639  -6.305  1.00 21.06  ? 109 VAL A N     1 
ATOM   861  C  CA    . VAL A 1 129 ? 0.123   22.222  -5.328  1.00 22.79  ? 109 VAL A CA    1 
ATOM   862  C  C     . VAL A 1 129 ? -0.522  21.421  -4.207  1.00 24.33  ? 109 VAL A C     1 
ATOM   863  O  O     . VAL A 1 129 ? 0.024   20.408  -3.753  1.00 26.99  ? 109 VAL A O     1 
ATOM   864  C  CB    . VAL A 1 129 ? 0.850   23.463  -4.787  1.00 22.69  ? 109 VAL A CB    1 
ATOM   865  C  CG1   . VAL A 1 129 ? 1.818   23.069  -3.681  1.00 28.12  ? 109 VAL A CG1   1 
ATOM   866  C  CG2   . VAL A 1 129 ? 1.577   24.190  -5.924  1.00 22.16  ? 109 VAL A CG2   1 
ATOM   867  N  N     . ASP A 1 130 ? -1.683  21.865  -3.744  1.00 23.57  ? 110 ASP A N     1 
ATOM   868  C  CA    . ASP A 1 130 ? -2.399  21.229  -2.646  1.00 26.55  ? 110 ASP A CA    1 
ATOM   869  C  C     . ASP A 1 130 ? -3.887  21.437  -2.902  1.00 24.77  ? 110 ASP A C     1 
ATOM   870  O  O     . ASP A 1 130 ? -4.378  22.573  -2.834  1.00 25.59  ? 110 ASP A O     1 
ATOM   871  C  CB    . ASP A 1 130 ? -1.937  21.819  -1.307  1.00 25.90  ? 110 ASP A CB    1 
ATOM   872  C  CG    . ASP A 1 130 ? -2.766  21.344  -0.101  1.00 31.23  ? 110 ASP A CG    1 
ATOM   873  O  OD1   . ASP A 1 130 ? -3.804  20.655  -0.260  1.00 31.60  ? 110 ASP A OD1   1 
ATOM   874  O  OD2   . ASP A 1 130 ? -2.351  21.678  1.031   1.00 34.41  ? 110 ASP A OD2   1 
ATOM   875  N  N     . PRO A 1 131 ? -4.623  20.368  -3.225  1.00 28.08  ? 111 PRO A N     1 
ATOM   876  C  CA    . PRO A 1 131 ? -6.020  20.535  -3.660  1.00 28.70  ? 111 PRO A CA    1 
ATOM   877  C  C     . PRO A 1 131 ? -6.914  21.184  -2.623  1.00 25.45  ? 111 PRO A C     1 
ATOM   878  O  O     . PRO A 1 131 ? -8.004  21.649  -2.977  1.00 29.72  ? 111 PRO A O     1 
ATOM   879  C  CB    . PRO A 1 131 ? -6.468  19.100  -3.972  1.00 34.26  ? 111 PRO A CB    1 
ATOM   880  C  CG    . PRO A 1 131 ? -5.194  18.338  -4.199  1.00 43.56  ? 111 PRO A CG    1 
ATOM   881  C  CD    . PRO A 1 131 ? -4.193  18.959  -3.266  1.00 36.48  ? 111 PRO A CD    1 
ATOM   882  N  N     . SER A 1 132 ? -6.492  21.246  -1.362  1.00 25.53  ? 112 SER A N     1 
ATOM   883  C  CA    . SER A 1 132 ? -7.321  21.858  -0.331  1.00 26.75  ? 112 SER A CA    1 
ATOM   884  C  C     . SER A 1 132 ? -7.204  23.378  -0.294  1.00 32.34  ? 112 SER A C     1 
ATOM   885  O  O     . SER A 1 132 ? -7.984  24.024  0.414   1.00 27.74  ? 112 SER A O     1 
ATOM   886  C  CB    . SER A 1 132 ? -6.956  21.285  1.046   1.00 31.92  ? 112 SER A CB    1 
ATOM   887  O  OG    . SER A 1 132 ? -5.676  21.722  1.465   1.00 35.04  ? 112 SER A OG    1 
ATOM   888  N  N     . LEU A 1 133 ? -6.264  23.967  -1.030  1.00 23.38  ? 113 LEU A N     1 
ATOM   889  C  CA    . LEU A 1 133 ? -6.000  25.398  -0.939  1.00 22.68  ? 113 LEU A CA    1 
ATOM   890  C  C     . LEU A 1 133 ? -6.948  26.183  -1.837  1.00 23.08  ? 113 LEU A C     1 
ATOM   891  O  O     . LEU A 1 133 ? -7.144  25.830  -3.005  1.00 25.98  ? 113 LEU A O     1 
ATOM   892  C  CB    . LEU A 1 133 ? -4.550  25.710  -1.328  1.00 24.11  ? 113 LEU A CB    1 
ATOM   893  C  CG    . LEU A 1 133 ? -3.459  25.163  -0.408  1.00 27.33  ? 113 LEU A CG    1 
ATOM   894  C  CD1   . LEU A 1 133 ? -2.080  25.504  -0.967  1.00 27.57  ? 113 LEU A CD1   1 
ATOM   895  C  CD2   . LEU A 1 133 ? -3.628  25.689  1.007   1.00 31.60  ? 113 LEU A CD2   1 
ATOM   896  N  N     . SER A 1 134 ? -7.522  27.256  -1.293  1.00 21.03  ? 114 SER A N     1 
ATOM   897  C  CA    . SER A 1 134 ? -8.285  28.205  -2.096  1.00 22.14  ? 114 SER A CA    1 
ATOM   898  C  C     . SER A 1 134 ? -7.432  29.365  -2.592  1.00 24.08  ? 114 SER A C     1 
ATOM   899  O  O     . SER A 1 134 ? -7.928  30.206  -3.347  1.00 21.58  ? 114 SER A O     1 
ATOM   900  C  CB    . SER A 1 134 ? -9.468  28.747  -1.287  1.00 26.97  ? 114 SER A CB    1 
ATOM   901  O  OG    . SER A 1 134 ? -9.013  29.490  -0.168  1.00 33.68  ? 114 SER A OG    1 
ATOM   902  N  N     . CYS A 1 135 ? -6.170  29.412  -2.178  1.00 20.92  ? 115 CYS A N     1 
ATOM   903  C  CA    . CYS A 1 135 ? -5.209  30.474  -2.443  1.00 22.34  ? 115 CYS A CA    1 
ATOM   904  C  C     . CYS A 1 135 ? -3.951  30.116  -1.663  1.00 19.71  ? 115 CYS A C     1 
ATOM   905  O  O     . CYS A 1 135 ? -3.954  29.204  -0.827  1.00 19.33  ? 115 CYS A O     1 
ATOM   906  C  CB    . CYS A 1 135 ? -5.718  31.859  -2.022  1.00 19.50  ? 115 CYS A CB    1 
ATOM   907  S  SG    . CYS A 1 135 ? -6.267  31.933  -0.290  1.00 23.89  ? 115 CYS A SG    1 
ATOM   908  N  N     . ALA A 1 136 ? -2.882  30.862  -1.928  1.00 18.72  ? 116 ALA A N     1 
ATOM   909  C  CA    . ALA A 1 136 ? -1.636  30.666  -1.199  1.00 20.73  ? 116 ALA A CA    1 
ATOM   910  C  C     . ALA A 1 136 ? -1.871  30.829  0.295   1.00 22.82  ? 116 ALA A C     1 
ATOM   911  O  O     . ALA A 1 136 ? -2.698  31.632  0.730   1.00 21.69  ? 116 ALA A O     1 
ATOM   912  C  CB    . ALA A 1 136 ? -0.580  31.670  -1.668  1.00 22.44  ? 116 ALA A CB    1 
ATOM   913  N  N     . LYS A 1 137 ? -1.125  30.065  1.085   1.00 23.74  ? 117 LYS A N     1 
ATOM   914  C  CA    . LYS A 1 137 ? -1.165  30.250  2.526   1.00 28.60  ? 117 LYS A CA    1 
ATOM   915  C  C     . LYS A 1 137 ? -0.629  31.641  2.854   1.00 25.47  ? 117 LYS A C     1 
ATOM   916  O  O     . LYS A 1 137 ? 0.494   31.974  2.439   1.00 26.19  ? 117 LYS A O     1 
ATOM   917  C  CB    . LYS A 1 137 ? -0.322  29.176  3.220   1.00 31.28  ? 117 LYS A CB    1 
ATOM   918  C  CG    . LYS A 1 137 ? -0.743  27.726  2.940   1.00 41.37  ? 117 LYS A CG    1 
ATOM   919  C  CD    . LYS A 1 137 ? 0.345   26.760  3.428   1.00 51.39  ? 117 LYS A CD    1 
ATOM   920  C  CE    . LYS A 1 137 ? -0.048  25.296  3.305   1.00 49.12  ? 117 LYS A CE    1 
ATOM   921  N  NZ    . LYS A 1 137 ? -1.169  24.918  4.208   1.00 56.73  ? 117 LYS A NZ    1 
ATOM   922  N  N     . PRO A 1 138 ? -1.378  32.477  3.567   1.00 23.65  ? 118 PRO A N     1 
ATOM   923  C  CA    . PRO A 1 138 ? -0.945  33.865  3.762   1.00 24.05  ? 118 PRO A CA    1 
ATOM   924  C  C     . PRO A 1 138 ? 0.186   33.994  4.771   1.00 25.65  ? 118 PRO A C     1 
ATOM   925  O  O     . PRO A 1 138 ? 0.276   33.247  5.748   1.00 26.86  ? 118 PRO A O     1 
ATOM   926  C  CB    . PRO A 1 138 ? -2.213  34.561  4.268   1.00 27.26  ? 118 PRO A CB    1 
ATOM   927  C  CG    . PRO A 1 138 ? -2.972  33.482  4.939   1.00 29.85  ? 118 PRO A CG    1 
ATOM   928  C  CD    . PRO A 1 138 ? -2.689  32.215  4.185   1.00 28.28  ? 118 PRO A CD    1 
ATOM   929  N  N     . THR A 1 139 ? 1.048   34.980  4.533   1.00 21.42  ? 119 THR A N     1 
ATOM   930  C  CA    . THR A 1 139 ? 2.117   35.328  5.468   1.00 24.15  ? 119 THR A CA    1 
ATOM   931  C  C     . THR A 1 139 ? 2.128   36.836  5.693   1.00 23.27  ? 119 THR A C     1 
ATOM   932  O  O     . THR A 1 139 ? 1.492   37.599  4.963   1.00 25.89  ? 119 THR A O     1 
ATOM   933  C  CB    . THR A 1 139 ? 3.501   34.877  4.964   1.00 24.51  ? 119 THR A CB    1 
ATOM   934  O  OG1   . THR A 1 139 ? 3.857   35.634  3.798   1.00 22.64  ? 119 THR A OG1   1 
ATOM   935  C  CG2   . THR A 1 139 ? 3.531   33.376  4.658   1.00 25.91  ? 119 THR A CG2   1 
ATOM   936  N  N     . GLU A 1 140 ? 2.876   37.277  6.716   1.00 22.41  ? 120 GLU A N     1 
ATOM   937  C  CA    . GLU A 1 140 ? 3.012   38.715  6.918   1.00 24.53  ? 120 GLU A CA    1 
ATOM   938  C  C     . GLU A 1 140 ? 3.567   39.391  5.671   1.00 29.58  ? 120 GLU A C     1 
ATOM   939  O  O     . GLU A 1 140 ? 3.119   40.479  5.293   1.00 27.83  ? 120 GLU A O     1 
ATOM   940  C  CB    . GLU A 1 140 ? 3.919   39.008  8.116   1.00 28.45  ? 120 GLU A CB    1 
ATOM   941  C  CG    . GLU A 1 140 ? 4.241   40.499  8.272   1.00 37.07  ? 120 GLU A CG    1 
ATOM   942  C  CD    . GLU A 1 140 ? 5.173   40.789  9.437   1.00 61.86  ? 120 GLU A CD    1 
ATOM   943  O  OE1   . GLU A 1 140 ? 5.758   39.834  9.993   1.00 63.78  ? 120 GLU A OE1   1 
ATOM   944  O  OE2   . GLU A 1 140 ? 5.324   41.977  9.795   1.00 78.36  ? 120 GLU A OE2   1 
ATOM   945  N  N     . GLU A 1 141 ? 4.507   38.733  4.987   1.00 24.77  ? 121 GLU A N     1 
ATOM   946  C  CA    . GLU A 1 141 ? 5.117   39.341  3.808   1.00 22.88  ? 121 GLU A CA    1 
ATOM   947  C  C     . GLU A 1 141 ? 4.175   39.325  2.607   1.00 24.18  ? 121 GLU A C     1 
ATOM   948  O  O     . GLU A 1 141 ? 4.149   40.287  1.832   1.00 27.48  ? 121 GLU A O     1 
ATOM   949  C  CB    . GLU A 1 141 ? 6.435   38.637  3.473   1.00 25.13  ? 121 GLU A CB    1 
ATOM   950  C  CG    . GLU A 1 141 ? 7.189   39.268  2.299   1.00 31.02  ? 121 GLU A CG    1 
ATOM   951  C  CD    . GLU A 1 141 ? 8.517   38.583  1.990   1.00 33.42  ? 121 GLU A CD    1 
ATOM   952  O  OE1   . GLU A 1 141 ? 8.697   37.410  2.382   1.00 37.06  ? 121 GLU A OE1   1 
ATOM   953  O  OE2   . GLU A 1 141 ? 9.375   39.217  1.335   1.00 35.79  ? 121 GLU A OE2   1 
ATOM   954  N  N     . PHE A 1 142 ? 3.411   38.245  2.424   1.00 22.66  ? 122 PHE A N     1 
ATOM   955  C  CA    . PHE A 1 142 ? 2.568   38.070  1.236   1.00 21.13  ? 122 PHE A CA    1 
ATOM   956  C  C     . PHE A 1 142 ? 1.188   37.578  1.652   1.00 20.04  ? 122 PHE A C     1 
ATOM   957  O  O     . PHE A 1 142 ? 1.032   36.408  2.011   1.00 20.68  ? 122 PHE A O     1 
ATOM   958  C  CB    . PHE A 1 142 ? 3.198   37.086  0.250   1.00 21.91  ? 122 PHE A CB    1 
ATOM   959  C  CG    . PHE A 1 142 ? 4.540   37.517  -0.266  1.00 22.69  ? 122 PHE A CG    1 
ATOM   960  C  CD1   . PHE A 1 142 ? 4.668   38.702  -0.967  1.00 25.91  ? 122 PHE A CD1   1 
ATOM   961  C  CD2   . PHE A 1 142 ? 5.667   36.722  -0.076  1.00 24.02  ? 122 PHE A CD2   1 
ATOM   962  C  CE1   . PHE A 1 142 ? 5.901   39.104  -1.452  1.00 24.20  ? 122 PHE A CE1   1 
ATOM   963  C  CE2   . PHE A 1 142 ? 6.891   37.117  -0.569  1.00 28.26  ? 122 PHE A CE2   1 
ATOM   964  C  CZ    . PHE A 1 142 ? 7.000   38.316  -1.262  1.00 21.01  ? 122 PHE A CZ    1 
ATOM   965  N  N     . ASN A 1 143 ? 0.178   38.432  1.536   1.00 21.11  ? 123 ASN A N     1 
ATOM   966  C  CA    . ASN A 1 143 ? -1.158  38.095  2.005   1.00 22.71  ? 123 ASN A CA    1 
ATOM   967  C  C     . ASN A 1 143 ? -2.174  38.802  1.119   1.00 24.80  ? 123 ASN A C     1 
ATOM   968  O  O     . ASN A 1 143 ? -1.803  39.615  0.263   1.00 25.27  ? 123 ASN A O     1 
ATOM   969  C  CB    . ASN A 1 143 ? -1.328  38.492  3.474   1.00 25.50  ? 123 ASN A CB    1 
ATOM   970  C  CG    . ASN A 1 143 ? -0.986  39.934  3.713   1.00 29.53  ? 123 ASN A CG    1 
ATOM   971  O  OD1   . ASN A 1 143 ? -1.689  40.832  3.243   1.00 30.77  ? 123 ASN A OD1   1 
ATOM   972  N  ND2   . ASN A 1 143 ? 0.107   40.173  4.428   1.00 29.00  ? 123 ASN A ND2   1 
ATOM   973  N  N     . PRO A 1 144 ? -3.469  38.501  1.285   1.00 22.07  ? 124 PRO A N     1 
ATOM   974  C  CA    . PRO A 1 144 ? -4.485  39.176  0.458   1.00 27.20  ? 124 PRO A CA    1 
ATOM   975  C  C     . PRO A 1 144 ? -4.550  40.688  0.628   1.00 28.37  ? 124 PRO A C     1 
ATOM   976  O  O     . PRO A 1 144 ? -5.082  41.367  -0.259  1.00 30.97  ? 124 PRO A O     1 
ATOM   977  C  CB    . PRO A 1 144 ? -5.793  38.513  0.909   1.00 27.06  ? 124 PRO A CB    1 
ATOM   978  C  CG    . PRO A 1 144 ? -5.397  37.179  1.349   1.00 25.96  ? 124 PRO A CG    1 
ATOM   979  C  CD    . PRO A 1 144 ? -4.058  37.367  2.024   1.00 23.41  ? 124 PRO A CD    1 
ATOM   980  N  N     . ASP A 1 145 ? -4.014  41.252  1.710   1.00 30.59  ? 125 ASP A N     1 
ATOM   981  C  CA    . ASP A 1 145 ? -4.117  42.699  1.865   1.00 28.01  ? 125 ASP A CA    1 
ATOM   982  C  C     . ASP A 1 145 ? -3.081  43.445  1.034   1.00 32.49  ? 125 ASP A C     1 
ATOM   983  O  O     . ASP A 1 145 ? -3.375  44.519  0.502   1.00 37.90  ? 125 ASP A O     1 
ATOM   984  C  CB    . ASP A 1 145 ? -4.013  43.086  3.342   1.00 30.80  ? 125 ASP A CB    1 
ATOM   985  C  CG    . ASP A 1 145 ? -5.198  42.595  4.148   1.00 42.00  ? 125 ASP A CG    1 
ATOM   986  O  OD1   . ASP A 1 145 ? -6.320  42.565  3.595   1.00 48.98  ? 125 ASP A OD1   1 
ATOM   987  O  OD2   . ASP A 1 145 ? -5.015  42.237  5.330   1.00 57.25  ? 125 ASP A OD2   1 
ATOM   988  N  N     . ASN A 1 146 ? -1.868  42.910  0.895   1.00 25.51  ? 126 ASN A N     1 
ATOM   989  C  CA    . ASN A 1 146 ? -0.886  43.610  0.079   1.00 25.83  ? 126 ASN A CA    1 
ATOM   990  C  C     . ASN A 1 146 ? -0.747  43.058  -1.333  1.00 26.34  ? 126 ASN A C     1 
ATOM   991  O  O     . ASN A 1 146 ? -0.235  43.772  -2.201  1.00 28.37  ? 126 ASN A O     1 
ATOM   992  C  CB    . ASN A 1 146 ? 0.487   43.656  0.776   1.00 24.31  ? 126 ASN A CB    1 
ATOM   993  C  CG    . ASN A 1 146 ? 1.045   42.284  1.120   1.00 28.32  ? 126 ASN A CG    1 
ATOM   994  O  OD1   . ASN A 1 146 ? 0.395   41.258  0.952   1.00 29.48  ? 126 ASN A OD1   1 
ATOM   995  N  ND2   . ASN A 1 146 ? 2.265   42.276  1.646   1.00 37.38  ? 126 ASN A ND2   1 
ATOM   996  N  N     . PHE A 1 147 ? -1.203  41.835  -1.608  1.00 24.15  ? 127 PHE A N     1 
ATOM   997  C  CA    . PHE A 1 147 ? -1.220  41.309  -2.976  1.00 25.78  ? 127 PHE A CA    1 
ATOM   998  C  C     . PHE A 1 147 ? -2.564  40.655  -3.280  1.00 23.24  ? 127 PHE A C     1 
ATOM   999  O  O     . PHE A 1 147 ? -2.630  39.474  -3.639  1.00 22.04  ? 127 PHE A O     1 
ATOM   1000 C  CB    . PHE A 1 147 ? -0.063  40.335  -3.205  1.00 22.90  ? 127 PHE A CB    1 
ATOM   1001 C  CG    . PHE A 1 147 ? 1.274   41.012  -3.377  1.00 23.89  ? 127 PHE A CG    1 
ATOM   1002 C  CD1   . PHE A 1 147 ? 1.697   41.444  -4.620  1.00 26.10  ? 127 PHE A CD1   1 
ATOM   1003 C  CD2   . PHE A 1 147 ? 2.101   41.210  -2.288  1.00 25.63  ? 127 PHE A CD2   1 
ATOM   1004 C  CE1   . PHE A 1 147 ? 2.926   42.063  -4.777  1.00 28.94  ? 127 PHE A CE1   1 
ATOM   1005 C  CE2   . PHE A 1 147 ? 3.330   41.834  -2.441  1.00 27.36  ? 127 PHE A CE2   1 
ATOM   1006 C  CZ    . PHE A 1 147 ? 3.736   42.259  -3.689  1.00 28.96  ? 127 PHE A CZ    1 
ATOM   1007 N  N     . PRO A 1 148 ? -3.662  41.417  -3.196  1.00 23.49  ? 128 PRO A N     1 
ATOM   1008 C  CA    . PRO A 1 148 ? -4.981  40.821  -3.469  1.00 26.59  ? 128 PRO A CA    1 
ATOM   1009 C  C     . PRO A 1 148 ? -5.128  40.311  -4.886  1.00 23.32  ? 128 PRO A C     1 
ATOM   1010 O  O     . PRO A 1 148 ? -5.954  39.422  -5.119  1.00 25.52  ? 128 PRO A O     1 
ATOM   1011 C  CB    . PRO A 1 148 ? -5.959  41.974  -3.193  1.00 26.41  ? 128 PRO A CB    1 
ATOM   1012 C  CG    . PRO A 1 148 ? -5.155  43.209  -3.430  1.00 28.33  ? 128 PRO A CG    1 
ATOM   1013 C  CD    . PRO A 1 148 ? -3.756  42.866  -2.944  1.00 26.69  ? 128 PRO A CD    1 
ATOM   1014 N  N     . GLU A 1 149 ? -4.357  40.828  -5.842  1.00 24.85  ? 129 GLU A N     1 
ATOM   1015 C  CA    . GLU A 1 149 ? -4.507  40.385  -7.222  1.00 24.65  ? 129 GLU A CA    1 
ATOM   1016 C  C     . GLU A 1 149 ? -3.913  39.004  -7.471  1.00 23.68  ? 129 GLU A C     1 
ATOM   1017 O  O     . GLU A 1 149 ? -4.127  38.439  -8.558  1.00 22.58  ? 129 GLU A O     1 
ATOM   1018 C  CB    . GLU A 1 149 ? -3.881  41.416  -8.170  1.00 27.93  ? 129 GLU A CB    1 
ATOM   1019 C  CG    . GLU A 1 149 ? -2.374  41.548  -8.086  1.00 36.67  ? 129 GLU A CG    1 
ATOM   1020 C  CD    . GLU A 1 149 ? -1.885  42.459  -6.960  1.00 42.76  ? 129 GLU A CD    1 
ATOM   1021 O  OE1   . GLU A 1 149 ? -2.636  42.737  -6.005  1.00 31.26  ? 129 GLU A OE1   1 
ATOM   1022 O  OE2   . GLU A 1 149 ? -0.725  42.906  -7.045  1.00 53.49  ? 129 GLU A OE2   1 
ATOM   1023 N  N     . TYR A 1 150 ? -3.210  38.430  -6.489  1.00 22.44  ? 130 TYR A N     1 
ATOM   1024 C  CA    . TYR A 1 150 ? -2.647  37.093  -6.616  1.00 20.59  ? 130 TYR A CA    1 
ATOM   1025 C  C     . TYR A 1 150 ? -3.108  36.138  -5.535  1.00 20.33  ? 130 TYR A C     1 
ATOM   1026 O  O     . TYR A 1 150 ? -3.161  34.930  -5.785  1.00 21.42  ? 130 TYR A O     1 
ATOM   1027 C  CB    . TYR A 1 150 ? -1.106  37.128  -6.561  1.00 20.39  ? 130 TYR A CB    1 
ATOM   1028 C  CG    . TYR A 1 150 ? -0.471  37.858  -7.715  1.00 20.85  ? 130 TYR A CG    1 
ATOM   1029 C  CD1   . TYR A 1 150 ? -0.433  37.301  -8.990  1.00 21.57  ? 130 TYR A CD1   1 
ATOM   1030 C  CD2   . TYR A 1 150 ? 0.107   39.110  -7.523  1.00 21.30  ? 130 TYR A CD2   1 
ATOM   1031 C  CE1   . TYR A 1 150 ? 0.149   37.986  -10.047 1.00 22.34  ? 130 TYR A CE1   1 
ATOM   1032 C  CE2   . TYR A 1 150 ? 0.688   39.798  -8.569  1.00 26.49  ? 130 TYR A CE2   1 
ATOM   1033 C  CZ    . TYR A 1 150 ? 0.711   39.234  -9.830  1.00 29.13  ? 130 TYR A CZ    1 
ATOM   1034 O  OH    . TYR A 1 150 ? 1.303   39.929  -10.873 1.00 24.79  ? 130 TYR A OH    1 
ATOM   1035 N  N     . LEU A 1 151 ? -3.438  36.642  -4.345  1.00 18.88  ? 131 LEU A N     1 
ATOM   1036 C  CA    . LEU A 1 151 ? -3.560  35.800  -3.160  1.00 18.62  ? 131 LEU A CA    1 
ATOM   1037 C  C     . LEU A 1 151 ? -4.961  35.769  -2.563  1.00 19.38  ? 131 LEU A C     1 
ATOM   1038 O  O     . LEU A 1 151 ? -5.142  35.190  -1.487  1.00 19.93  ? 131 LEU A O     1 
ATOM   1039 C  CB    . LEU A 1 151 ? -2.553  36.266  -2.098  1.00 21.11  ? 131 LEU A CB    1 
ATOM   1040 C  CG    . LEU A 1 151 ? -1.106  36.422  -2.575  1.00 20.28  ? 131 LEU A CG    1 
ATOM   1041 C  CD1   . LEU A 1 151 ? -0.216  36.914  -1.415  1.00 21.42  ? 131 LEU A CD1   1 
ATOM   1042 C  CD2   . LEU A 1 151 ? -0.561  35.116  -3.165  1.00 23.13  ? 131 LEU A CD2   1 
ATOM   1043 N  N     . SER A 1 152 ? -5.958  36.361  -3.225  1.00 21.24  ? 132 SER A N     1 
ATOM   1044 C  CA    . SER A 1 152 ? -7.320  36.308  -2.712  1.00 21.65  ? 132 SER A CA    1 
ATOM   1045 C  C     . SER A 1 152 ? -7.916  34.916  -2.905  1.00 19.74  ? 132 SER A C     1 
ATOM   1046 O  O     . SER A 1 152 ? -7.601  34.225  -3.881  1.00 21.10  ? 132 SER A O     1 
ATOM   1047 C  CB    . SER A 1 152 ? -8.213  37.330  -3.410  1.00 21.60  ? 132 SER A CB    1 
ATOM   1048 O  OG    . SER A 1 152 ? -7.768  38.655  -3.170  1.00 25.09  ? 132 SER A OG    1 
ATOM   1049 N  N     . PRO A 1 153 ? -8.781  34.482  -1.985  1.00 21.30  ? 133 PRO A N     1 
ATOM   1050 C  CA    A PRO A 1 153 ? -9.398  33.158  -2.125  0.61 21.07  ? 133 PRO A CA    1 
ATOM   1051 C  CA    B PRO A 1 153 ? -9.404  33.161  -2.119  0.39 21.11  ? 133 PRO A CA    1 
ATOM   1052 C  C     . PRO A 1 153 ? -10.298 33.089  -3.347  1.00 19.88  ? 133 PRO A C     1 
ATOM   1053 O  O     . PRO A 1 153 ? -10.975 34.057  -3.708  1.00 22.62  ? 133 PRO A O     1 
ATOM   1054 C  CB    A PRO A 1 153 ? -10.203 32.995  -0.829  0.61 22.56  ? 133 PRO A CB    1 
ATOM   1055 C  CB    B PRO A 1 153 ? -10.219 33.018  -0.828  0.39 22.58  ? 133 PRO A CB    1 
ATOM   1056 C  CG    A PRO A 1 153 ? -10.380 34.378  -0.299  0.61 22.26  ? 133 PRO A CG    1 
ATOM   1057 C  CG    B PRO A 1 153 ? -9.582  33.969  0.132   0.39 23.72  ? 133 PRO A CG    1 
ATOM   1058 C  CD    A PRO A 1 153 ? -9.134  35.120  -0.705  0.61 24.12  ? 133 PRO A CD    1 
ATOM   1059 C  CD    B PRO A 1 153 ? -9.098  35.119  -0.696  0.39 24.07  ? 133 PRO A CD    1 
ATOM   1060 N  N     . ASN A 1 154 ? -10.300 31.922  -3.983  1.00 19.50  ? 134 ASN A N     1 
ATOM   1061 C  CA    . ASN A 1 154 ? -11.168 31.703  -5.129  1.00 20.66  ? 134 ASN A CA    1 
ATOM   1062 C  C     . ASN A 1 154 ? -12.636 31.815  -4.721  1.00 19.00  ? 134 ASN A C     1 
ATOM   1063 O  O     . ASN A 1 154 ? -13.031 31.461  -3.601  1.00 22.33  ? 134 ASN A O     1 
ATOM   1064 C  CB    . ASN A 1 154 ? -10.887 30.332  -5.738  1.00 18.24  ? 134 ASN A CB    1 
ATOM   1065 C  CG    . ASN A 1 154 ? -9.604  30.315  -6.545  1.00 17.82  ? 134 ASN A CG    1 
ATOM   1066 O  OD1   . ASN A 1 154 ? -9.171  31.351  -7.050  1.00 17.66  ? 134 ASN A OD1   1 
ATOM   1067 N  ND2   . ASN A 1 154 ? -8.994  29.137  -6.671  1.00 19.39  ? 134 ASN A ND2   1 
ATOM   1068 N  N     . LEU A 1 155 ? -13.445 32.346  -5.639  1.00 18.99  ? 135 LEU A N     1 
ATOM   1069 C  CA    . LEU A 1 155 ? -14.883 32.505  -5.438  1.00 19.24  ? 135 LEU A CA    1 
ATOM   1070 C  C     . LEU A 1 155 ? -15.583 31.637  -6.473  1.00 18.97  ? 135 LEU A C     1 
ATOM   1071 O  O     . LEU A 1 155 ? -15.576 31.963  -7.663  1.00 22.20  ? 135 LEU A O     1 
ATOM   1072 C  CB    . LEU A 1 155 ? -15.312 33.961  -5.586  1.00 24.80  ? 135 LEU A CB    1 
ATOM   1073 C  CG    . LEU A 1 155 ? -14.657 34.982  -4.666  1.00 29.52  ? 135 LEU A CG    1 
ATOM   1074 C  CD1   . LEU A 1 155 ? -15.141 36.387  -5.028  1.00 30.33  ? 135 LEU A CD1   1 
ATOM   1075 C  CD2   . LEU A 1 155 ? -14.989 34.637  -3.225  1.00 33.08  ? 135 LEU A CD2   1 
ATOM   1076 N  N     . TRP A 1 156 ? -16.236 30.551  -6.013  1.00 21.93  ? 136 TRP A N     1 
ATOM   1077 C  CA    . TRP A 1 156 ? -16.794 29.598  -6.963  1.00 23.11  ? 136 TRP A CA    1 
ATOM   1078 C  C     . TRP A 1 156 ? -18.303 29.763  -7.071  1.00 23.32  ? 136 TRP A C     1 
ATOM   1079 O  O     . TRP A 1 156 ? -18.972 30.060  -6.072  1.00 25.77  ? 136 TRP A O     1 
ATOM   1080 C  CB    . TRP A 1 156 ? -16.481 28.154  -6.543  1.00 22.89  ? 136 TRP A CB    1 
ATOM   1081 C  CG    . TRP A 1 156 ? -15.005 27.811  -6.585  1.00 20.70  ? 136 TRP A CG    1 
ATOM   1082 C  CD1   . TRP A 1 156 ? -14.128 27.778  -5.533  1.00 24.04  ? 136 TRP A CD1   1 
ATOM   1083 C  CD2   . TRP A 1 156 ? -14.240 27.483  -7.753  1.00 20.75  ? 136 TRP A CD2   1 
ATOM   1084 N  NE1   . TRP A 1 156 ? -12.869 27.431  -5.979  1.00 22.71  ? 136 TRP A NE1   1 
ATOM   1085 C  CE2   . TRP A 1 156 ? -12.915 27.246  -7.336  1.00 22.47  ? 136 TRP A CE2   1 
ATOM   1086 C  CE3   . TRP A 1 156 ? -14.553 27.353  -9.110  1.00 20.86  ? 136 TRP A CE3   1 
ATOM   1087 C  CZ2   . TRP A 1 156 ? -11.903 26.891  -8.228  1.00 24.26  ? 136 TRP A CZ2   1 
ATOM   1088 C  CZ3   . TRP A 1 156 ? -13.547 27.006  -9.993  1.00 21.12  ? 136 TRP A CZ3   1 
ATOM   1089 C  CH2   . TRP A 1 156 ? -12.238 26.784  -9.554  1.00 20.65  ? 136 TRP A CH2   1 
ATOM   1090 N  N     . PRO A 1 157 ? -18.842 29.562  -8.276  1.00 22.97  ? 137 PRO A N     1 
ATOM   1091 C  CA    . PRO A 1 157 ? -20.295 29.489  -8.425  1.00 26.38  ? 137 PRO A CA    1 
ATOM   1092 C  C     . PRO A 1 157 ? -20.847 28.349  -7.593  1.00 30.92  ? 137 PRO A C     1 
ATOM   1093 O  O     . PRO A 1 157 ? -20.165 27.368  -7.292  1.00 25.24  ? 137 PRO A O     1 
ATOM   1094 C  CB    . PRO A 1 157 ? -20.494 29.227  -9.925  1.00 27.29  ? 137 PRO A CB    1 
ATOM   1095 C  CG    . PRO A 1 157 ? -19.194 29.615  -10.562 1.00 32.98  ? 137 PRO A CG    1 
ATOM   1096 C  CD    . PRO A 1 157 ? -18.147 29.317  -9.546  1.00 24.06  ? 137 PRO A CD    1 
ATOM   1097 N  N     . GLN A 1 158 ? -22.115 28.488  -7.227  1.00 32.59  ? 138 GLN A N     1 
ATOM   1098 C  CA    . GLN A 1 158 ? -22.764 27.467  -6.424  1.00 33.54  ? 138 GLN A CA    1 
ATOM   1099 C  C     . GLN A 1 158 ? -22.815 26.156  -7.196  1.00 23.01  ? 138 GLN A C     1 
ATOM   1100 O  O     . GLN A 1 158 ? -23.102 26.138  -8.396  1.00 27.09  ? 138 GLN A O     1 
ATOM   1101 C  CB    . GLN A 1 158 ? -24.176 27.927  -6.072  1.00 38.46  ? 138 GLN A CB    1 
ATOM   1102 C  CG    . GLN A 1 158 ? -24.203 29.196  -5.252  1.00 37.12  ? 138 GLN A CG    1 
ATOM   1103 C  CD    . GLN A 1 158 ? -25.600 29.757  -5.089  1.00 48.74  ? 138 GLN A CD    1 
ATOM   1104 O  OE1   . GLN A 1 158 ? -26.356 29.873  -6.057  1.00 56.90  ? 138 GLN A OE1   1 
ATOM   1105 N  NE2   . GLN A 1 158 ? -25.954 30.098  -3.858  1.00 56.83  ? 138 GLN A NE2   1 
ATOM   1106 N  N     . GLU A 1 159 ? -22.519 25.047  -6.502  1.00 26.37  ? 139 GLU A N     1 
ATOM   1107 C  CA    . GLU A 1 159 ? -22.608 23.740  -7.154  1.00 24.79  ? 139 GLU A CA    1 
ATOM   1108 C  C     . GLU A 1 159 ? -24.027 23.476  -7.652  1.00 22.37  ? 139 GLU A C     1 
ATOM   1109 O  O     . GLU A 1 159 ? -24.214 22.867  -8.705  1.00 26.03  ? 139 GLU A O     1 
ATOM   1110 C  CB    . GLU A 1 159 ? -22.120 22.621  -6.219  1.00 27.69  ? 139 GLU A CB    1 
ATOM   1111 C  CG    . GLU A 1 159 ? -22.528 21.165  -6.607  1.00 30.02  ? 139 GLU A CG    1 
ATOM   1112 C  CD    . GLU A 1 159 ? -21.837 20.572  -7.864  1.00 33.20  ? 139 GLU A CD    1 
ATOM   1113 O  OE1   . GLU A 1 159 ? -20.868 21.149  -8.368  1.00 30.66  ? 139 GLU A OE1   1 
ATOM   1114 O  OE2   . GLU A 1 159 ? -22.283 19.504  -8.351  1.00 39.03  ? 139 GLU A OE2   1 
ATOM   1115 N  N     . SER A 1 160 ? -25.047 23.917  -6.908  1.00 25.36  ? 140 SER A N     1 
ATOM   1116 C  CA    . SER A 1 160 ? -26.406 23.588  -7.331  1.00 26.42  ? 140 SER A CA    1 
ATOM   1117 C  C     . SER A 1 160 ? -26.820 24.320  -8.604  1.00 28.08  ? 140 SER A C     1 
ATOM   1118 O  O     . SER A 1 160 ? -27.600 23.778  -9.396  1.00 34.68  ? 140 SER A O     1 
ATOM   1119 C  CB    . SER A 1 160 ? -27.397 23.922  -6.215  1.00 31.33  ? 140 SER A CB    1 
ATOM   1120 O  OG    . SER A 1 160 ? -27.326 25.301  -5.880  1.00 37.32  ? 140 SER A OG    1 
ATOM   1121 N  N     . THR A 1 161 ? -26.310 25.530  -8.826  1.00 26.69  ? 141 THR A N     1 
ATOM   1122 C  CA    . THR A 1 161 ? -26.665 26.318  -10.005 1.00 27.27  ? 141 THR A CA    1 
ATOM   1123 C  C     . THR A 1 161 ? -25.730 26.103  -11.187 1.00 22.54  ? 141 THR A C     1 
ATOM   1124 O  O     . THR A 1 161 ? -26.125 26.378  -12.327 1.00 27.89  ? 141 THR A O     1 
ATOM   1125 C  CB    . THR A 1 161 ? -26.726 27.805  -9.661  1.00 32.26  ? 141 THR A CB    1 
ATOM   1126 O  OG1   . THR A 1 161 ? -25.518 28.205  -9.013  1.00 44.22  ? 141 THR A OG1   1 
ATOM   1127 C  CG2   . THR A 1 161 ? -27.912 28.081  -8.745  1.00 49.70  ? 141 THR A CG2   1 
ATOM   1128 N  N     . LEU A 1 162 ? -24.491 25.673  -10.945 1.00 22.58  ? 142 LEU A N     1 
ATOM   1129 C  CA    . LEU A 1 162 ? -23.547 25.357  -12.019 1.00 23.23  ? 142 LEU A CA    1 
ATOM   1130 C  C     . LEU A 1 162 ? -22.824 24.061  -11.668 1.00 24.45  ? 142 LEU A C     1 
ATOM   1131 O  O     . LEU A 1 162 ? -21.626 24.054  -11.354 1.00 20.10  ? 142 LEU A O     1 
ATOM   1132 C  CB    . LEU A 1 162 ? -22.559 26.505  -12.220 1.00 21.25  ? 142 LEU A CB    1 
ATOM   1133 C  CG    . LEU A 1 162 ? -21.811 26.511  -13.541 1.00 18.30  ? 142 LEU A CG    1 
ATOM   1134 C  CD1   . LEU A 1 162 ? -22.797 26.621  -14.711 1.00 23.24  ? 142 LEU A CD1   1 
ATOM   1135 C  CD2   . LEU A 1 162 ? -20.801 27.659  -13.566 1.00 21.16  ? 142 LEU A CD2   1 
ATOM   1136 N  N     . PRO A 1 163 ? -23.524 22.929  -11.755 1.00 21.07  ? 143 PRO A N     1 
ATOM   1137 C  CA    . PRO A 1 163 ? -22.971 21.657  -11.257 1.00 21.77  ? 143 PRO A CA    1 
ATOM   1138 C  C     . PRO A 1 163 ? -21.763 21.187  -12.054 1.00 18.54  ? 143 PRO A C     1 
ATOM   1139 O  O     . PRO A 1 163 ? -21.795 21.155  -13.285 1.00 19.67  ? 143 PRO A O     1 
ATOM   1140 C  CB    . PRO A 1 163 ? -24.149 20.682  -11.396 1.00 23.43  ? 143 PRO A CB    1 
ATOM   1141 C  CG    . PRO A 1 163 ? -25.075 21.322  -12.392 1.00 28.46  ? 143 PRO A CG    1 
ATOM   1142 C  CD    . PRO A 1 163 ? -24.938 22.794  -12.157 1.00 23.84  ? 143 PRO A CD    1 
ATOM   1143 N  N     . GLY A 1 164 ? -20.708 20.799  -11.330 1.00 20.11  ? 144 GLY A N     1 
ATOM   1144 C  CA    . GLY A 1 164 ? -19.513 20.235  -11.928 1.00 20.61  ? 144 GLY A CA    1 
ATOM   1145 C  C     . GLY A 1 164 ? -18.481 21.238  -12.388 1.00 22.31  ? 144 GLY A C     1 
ATOM   1146 O  O     . GLY A 1 164 ? -17.433 20.829  -12.908 1.00 19.33  ? 144 GLY A O     1 
ATOM   1147 N  N     . PHE A 1 165 ? -18.736 22.536  -12.223 1.00 20.03  ? 145 PHE A N     1 
ATOM   1148 C  CA    . PHE A 1 165 ? -17.829 23.552  -12.753 1.00 17.27  ? 145 PHE A CA    1 
ATOM   1149 C  C     . PHE A 1 165 ? -16.461 23.472  -12.084 1.00 18.15  ? 145 PHE A C     1 
ATOM   1150 O  O     . PHE A 1 165 ? -15.423 23.475  -12.767 1.00 16.86  ? 145 PHE A O     1 
ATOM   1151 C  CB    . PHE A 1 165 ? -18.443 24.942  -12.564 1.00 17.41  ? 145 PHE A CB    1 
ATOM   1152 C  CG    . PHE A 1 165 ? -17.541 26.079  -12.970 1.00 17.10  ? 145 PHE A CG    1 
ATOM   1153 C  CD1   . PHE A 1 165 ? -17.209 26.279  -14.301 1.00 19.73  ? 145 PHE A CD1   1 
ATOM   1154 C  CD2   . PHE A 1 165 ? -17.015 26.931  -12.016 1.00 20.62  ? 145 PHE A CD2   1 
ATOM   1155 C  CE1   . PHE A 1 165 ? -16.388 27.336  -14.680 1.00 21.20  ? 145 PHE A CE1   1 
ATOM   1156 C  CE2   . PHE A 1 165 ? -16.189 27.991  -12.387 1.00 22.66  ? 145 PHE A CE2   1 
ATOM   1157 C  CZ    . PHE A 1 165 ? -15.877 28.192  -13.721 1.00 19.30  ? 145 PHE A CZ    1 
ATOM   1158 N  N     . LYS A 1 166 ? -16.435 23.422  -10.749 1.00 17.66  ? 146 LYS A N     1 
ATOM   1159 C  CA    . LYS A 1 166 ? -15.151 23.474  -10.046 1.00 17.64  ? 146 LYS A CA    1 
ATOM   1160 C  C     . LYS A 1 166 ? -14.257 22.286  -10.363 1.00 17.50  ? 146 LYS A C     1 
ATOM   1161 O  O     . LYS A 1 166 ? -13.088 22.512  -10.720 1.00 18.39  ? 146 LYS A O     1 
ATOM   1162 C  CB    . LYS A 1 166 ? -15.379 23.617  -8.533  1.00 18.76  ? 146 LYS A CB    1 
ATOM   1163 C  CG    . LYS A 1 166 ? -14.094 23.645  -7.701  1.00 20.20  ? 146 LYS A CG    1 
ATOM   1164 C  CD    . LYS A 1 166 ? -14.419 24.008  -6.241  1.00 20.79  ? 146 LYS A CD    1 
ATOM   1165 C  CE    . LYS A 1 166 ? -13.166 24.056  -5.363  1.00 27.73  ? 146 LYS A CE    1 
ATOM   1166 N  NZ    . LYS A 1 166 ? -12.591 22.688  -5.172  1.00 27.36  ? 146 LYS A NZ    1 
ATOM   1167 N  N     . PRO A 1 167 ? -14.702 21.026  -10.264 1.00 19.22  ? 147 PRO A N     1 
ATOM   1168 C  CA    . PRO A 1 167 ? -13.786 19.928  -10.628 1.00 20.63  ? 147 PRO A CA    1 
ATOM   1169 C  C     . PRO A 1 167 ? -13.358 19.961  -12.082 1.00 21.35  ? 147 PRO A C     1 
ATOM   1170 O  O     . PRO A 1 167 ? -12.208 19.623  -12.376 1.00 19.11  ? 147 PRO A O     1 
ATOM   1171 C  CB    . PRO A 1 167 ? -14.587 18.662  -10.289 1.00 23.12  ? 147 PRO A CB    1 
ATOM   1172 C  CG    . PRO A 1 167 ? -16.014 19.106  -10.233 1.00 25.77  ? 147 PRO A CG    1 
ATOM   1173 C  CD    . PRO A 1 167 ? -15.969 20.506  -9.716  1.00 20.63  ? 147 PRO A CD    1 
ATOM   1174 N  N     . THR A 1 168 ? -14.237 20.369  -13.003 1.00 16.92  ? 148 THR A N     1 
ATOM   1175 C  CA    . THR A 1 168 ? -13.852 20.473  -14.412 1.00 16.48  ? 148 THR A CA    1 
ATOM   1176 C  C     . THR A 1 168 ? -12.775 21.528  -14.611 1.00 20.01  ? 148 THR A C     1 
ATOM   1177 O  O     . THR A 1 168 ? -11.785 21.296  -15.323 1.00 18.44  ? 148 THR A O     1 
ATOM   1178 C  CB    . THR A 1 168 ? -15.067 20.816  -15.274 1.00 16.39  ? 148 THR A CB    1 
ATOM   1179 O  OG1   . THR A 1 168 ? -16.093 19.838  -15.051 1.00 19.02  ? 148 THR A OG1   1 
ATOM   1180 C  CG2   . THR A 1 168 ? -14.670 20.825  -16.732 1.00 19.60  ? 148 THR A CG2   1 
ATOM   1181 N  N     . PHE A 1 169 ? -12.963 22.695  -13.982 1.00 17.95  ? 149 PHE A N     1 
ATOM   1182 C  CA    . PHE A 1 169 ? -11.967 23.773  -14.012 1.00 16.24  ? 149 PHE A CA    1 
ATOM   1183 C  C     . PHE A 1 169 ? -10.627 23.288  -13.476 1.00 19.93  ? 149 PHE A C     1 
ATOM   1184 O  O     . PHE A 1 169 ? -9.577  23.482  -14.109 1.00 17.19  ? 149 PHE A O     1 
ATOM   1185 C  CB    . PHE A 1 169 ? -12.501 24.958  -13.189 1.00 16.36  ? 149 PHE A CB    1 
ATOM   1186 C  CG    . PHE A 1 169 ? -11.770 26.259  -13.397 1.00 16.60  ? 149 PHE A CG    1 
ATOM   1187 C  CD1   . PHE A 1 169 ? -10.510 26.465  -12.820 1.00 17.21  ? 149 PHE A CD1   1 
ATOM   1188 C  CD2   . PHE A 1 169 ? -12.334 27.293  -14.148 1.00 16.51  ? 149 PHE A CD2   1 
ATOM   1189 C  CE1   . PHE A 1 169 ? -9.835  27.669  -13.004 1.00 17.05  ? 149 PHE A CE1   1 
ATOM   1190 C  CE2   . PHE A 1 169 ? -11.660 28.501  -14.321 1.00 18.91  ? 149 PHE A CE2   1 
ATOM   1191 C  CZ    . PHE A 1 169 ? -10.397 28.689  -13.753 1.00 17.20  ? 149 PHE A CZ    1 
ATOM   1192 N  N     . GLU A 1 170 ? -10.643 22.668  -12.295 1.00 16.74  ? 150 GLU A N     1 
ATOM   1193 C  CA    . GLU A 1 170 ? -9.395  22.205  -11.692 1.00 16.67  ? 150 GLU A CA    1 
ATOM   1194 C  C     . GLU A 1 170 ? -8.723  21.143  -12.557 1.00 16.88  ? 150 GLU A C     1 
ATOM   1195 O  O     . GLU A 1 170 ? -7.499  21.182  -12.749 1.00 18.98  ? 150 GLU A O     1 
ATOM   1196 C  CB    . GLU A 1 170 ? -9.644  21.679  -10.275 1.00 17.97  ? 150 GLU A CB    1 
ATOM   1197 C  CG    . GLU A 1 170 ? -9.958  22.785  -9.291  1.00 19.64  ? 150 GLU A CG    1 
ATOM   1198 C  CD    . GLU A 1 170 ? -10.328 22.274  -7.914  1.00 38.37  ? 150 GLU A CD    1 
ATOM   1199 O  OE1   . GLU A 1 170 ? -10.842 21.138  -7.796  1.00 48.29  ? 150 GLU A OE1   1 
ATOM   1200 O  OE2   . GLU A 1 170 ? -10.119 23.038  -6.954  1.00 36.59  ? 150 GLU A OE2   1 
ATOM   1201 N  N     . ASP A 1 171 ? -9.496  20.185  -13.089 1.00 17.95  ? 151 ASP A N     1 
ATOM   1202 C  CA    . ASP A 1 171 ? -8.886  19.104  -13.864 1.00 20.06  ? 151 ASP A CA    1 
ATOM   1203 C  C     . ASP A 1 171 ? -8.241  19.626  -15.143 1.00 17.01  ? 151 ASP A C     1 
ATOM   1204 O  O     . ASP A 1 171 ? -7.133  19.192  -15.510 1.00 17.59  ? 151 ASP A O     1 
ATOM   1205 C  CB    . ASP A 1 171 ? -9.919  18.031  -14.206 1.00 18.22  ? 151 ASP A CB    1 
ATOM   1206 C  CG    . ASP A 1 171 ? -10.321 17.205  -13.002 1.00 25.82  ? 151 ASP A CG    1 
ATOM   1207 O  OD1   . ASP A 1 171 ? -9.674  17.315  -11.945 1.00 25.53  ? 151 ASP A OD1   1 
ATOM   1208 O  OD2   . ASP A 1 171 ? -11.286 16.426  -13.133 1.00 28.14  ? 151 ASP A OD2   1 
ATOM   1209 N  N     . LEU A 1 172 ? -8.914  20.544  -15.852 1.00 16.17  ? 152 LEU A N     1 
ATOM   1210 C  CA    . LEU A 1 172 ? -8.312  21.063  -17.080 1.00 15.59  ? 152 LEU A CA    1 
ATOM   1211 C  C     . LEU A 1 172 ? -7.090  21.924  -16.760 1.00 18.42  ? 152 LEU A C     1 
ATOM   1212 O  O     . LEU A 1 172 ? -6.059  21.843  -17.454 1.00 16.33  ? 152 LEU A O     1 
ATOM   1213 C  CB    . LEU A 1 172 ? -9.345  21.848  -17.897 1.00 16.02  ? 152 LEU A CB    1 
ATOM   1214 C  CG    . LEU A 1 172 ? -8.816  22.383  -19.241 1.00 16.23  ? 152 LEU A CG    1 
ATOM   1215 C  CD1   . LEU A 1 172 ? -8.106  21.336  -20.122 1.00 17.93  ? 152 LEU A CD1   1 
ATOM   1216 C  CD2   . LEU A 1 172 ? -9.959  23.016  -20.017 1.00 15.46  ? 152 LEU A CD2   1 
ATOM   1217 N  N     . CYS A 1 173 ? -7.174  22.749  -15.709 1.00 16.43  ? 153 CYS A N     1 
ATOM   1218 C  CA    . CYS A 1 173 ? -6.000  23.541  -15.345 1.00 16.75  ? 153 CYS A CA    1 
ATOM   1219 C  C     . CYS A 1 173 ? -4.840  22.644  -14.951 1.00 19.24  ? 153 CYS A C     1 
ATOM   1220 O  O     . CYS A 1 173 ? -3.687  22.925  -15.312 1.00 17.49  ? 153 CYS A O     1 
ATOM   1221 C  CB    . CYS A 1 173 ? -6.325  24.513  -14.213 1.00 17.50  ? 153 CYS A CB    1 
ATOM   1222 S  SG    . CYS A 1 173 ? -7.352  25.904  -14.764 1.00 18.78  ? 153 CYS A SG    1 
ATOM   1223 N  N     . ARG A 1 174 ? -5.117  21.557  -14.224 1.00 16.46  ? 154 ARG A N     1 
ATOM   1224 C  CA    . ARG A 1 174 ? -4.043  20.648  -13.814 1.00 16.69  ? 154 ARG A CA    1 
ATOM   1225 C  C     . ARG A 1 174 ? -3.383  20.008  -15.024 1.00 19.28  ? 154 ARG A C     1 
ATOM   1226 O  O     . ARG A 1 174 ? -2.150  19.890  -15.079 1.00 18.11  ? 154 ARG A O     1 
ATOM   1227 C  CB    . ARG A 1 174 ? -4.594  19.555  -12.890 1.00 20.32  ? 154 ARG A CB    1 
ATOM   1228 C  CG    . ARG A 1 174 ? -3.526  18.544  -12.439 1.00 22.79  ? 154 ARG A CG    1 
ATOM   1229 C  CD    . ARG A 1 174 ? -4.064  17.560  -11.393 1.00 23.46  ? 154 ARG A CD    1 
ATOM   1230 N  NE    . ARG A 1 174 ? -4.631  18.251  -10.241 1.00 23.61  ? 154 ARG A NE    1 
ATOM   1231 C  CZ    . ARG A 1 174 ? -3.918  18.774  -9.247  1.00 26.21  ? 154 ARG A CZ    1 
ATOM   1232 N  NH1   . ARG A 1 174 ? -2.590  18.698  -9.221  1.00 27.93  ? 154 ARG A NH1   1 
ATOM   1233 N  NH2   . ARG A 1 174 ? -4.551  19.403  -8.257  1.00 25.79  ? 154 ARG A NH2   1 
ATOM   1234 N  N     . LEU A 1 175 ? -4.183  19.591  -16.006 1.00 17.37  ? 155 LEU A N     1 
ATOM   1235 C  CA    . LEU A 1 175 ? -3.607  19.028  -17.224 1.00 17.16  ? 155 LEU A CA    1 
ATOM   1236 C  C     . LEU A 1 175 ? -2.698  20.046  -17.918 1.00 17.67  ? 155 LEU A C     1 
ATOM   1237 O  O     . LEU A 1 175 ? -1.552  19.735  -18.291 1.00 18.13  ? 155 LEU A O     1 
ATOM   1238 C  CB    . LEU A 1 175 ? -4.745  18.555  -18.140 1.00 16.32  ? 155 LEU A CB    1 
ATOM   1239 C  CG    . LEU A 1 175 ? -4.433  17.790  -19.433 1.00 20.42  ? 155 LEU A CG    1 
ATOM   1240 C  CD1   . LEU A 1 175 ? -5.703  17.056  -19.891 1.00 21.34  ? 155 LEU A CD1   1 
ATOM   1241 C  CD2   . LEU A 1 175 ? -3.931  18.691  -20.559 1.00 21.84  ? 155 LEU A CD2   1 
ATOM   1242 N  N     . ILE A 1 176 ? -3.188  21.278  -18.081 1.00 16.90  ? 156 ILE A N     1 
ATOM   1243 C  CA    . ILE A 1 176 ? -2.397  22.293  -18.777 1.00 16.53  ? 156 ILE A CA    1 
ATOM   1244 C  C     . ILE A 1 176 ? -1.133  22.636  -18.000 1.00 18.13  ? 156 ILE A C     1 
ATOM   1245 O  O     . ILE A 1 176 ? -0.062  22.811  -18.597 1.00 17.41  ? 156 ILE A O     1 
ATOM   1246 C  CB    . ILE A 1 176 ? -3.250  23.540  -19.059 1.00 16.98  ? 156 ILE A CB    1 
ATOM   1247 C  CG1   . ILE A 1 176 ? -4.302  23.192  -20.112 1.00 15.18  ? 156 ILE A CG1   1 
ATOM   1248 C  CG2   . ILE A 1 176 ? -2.371  24.690  -19.520 1.00 18.18  ? 156 ILE A CG2   1 
ATOM   1249 C  CD1   . ILE A 1 176 ? -5.340  24.276  -20.311 1.00 19.75  ? 156 ILE A CD1   1 
ATOM   1250 N  N     . ILE A 1 177 ? -1.225  22.739  -16.669 1.00 15.99  ? 157 ILE A N     1 
ATOM   1251 C  CA    . ILE A 1 177 ? -0.038  23.059  -15.875 1.00 16.24  ? 157 ILE A CA    1 
ATOM   1252 C  C     . ILE A 1 177 ? 0.963   21.905  -15.917 1.00 17.20  ? 157 ILE A C     1 
ATOM   1253 O  O     . ILE A 1 177 ? 2.178   22.138  -15.936 1.00 17.68  ? 157 ILE A O     1 
ATOM   1254 C  CB    . ILE A 1 177 ? -0.420  23.419  -14.421 1.00 16.33  ? 157 ILE A CB    1 
ATOM   1255 C  CG1   . ILE A 1 177 ? -1.228  24.714  -14.378 1.00 17.97  ? 157 ILE A CG1   1 
ATOM   1256 C  CG2   . ILE A 1 177 ? 0.845   23.566  -13.550 1.00 16.62  ? 157 ILE A CG2   1 
ATOM   1257 C  CD1   . ILE A 1 177 ? -1.916  25.003  -13.026 1.00 17.18  ? 157 ILE A CD1   1 
ATOM   1258 N  N     . ASP A 1 178 ? 0.488   20.645  -15.907 1.00 16.69  ? 158 ASP A N     1 
ATOM   1259 C  CA    . ASP A 1 178 ? 1.406   19.505  -16.064 1.00 16.99  ? 158 ASP A CA    1 
ATOM   1260 C  C     . ASP A 1 178 ? 2.235   19.663  -17.341 1.00 20.38  ? 158 ASP A C     1 
ATOM   1261 O  O     . ASP A 1 178 ? 3.476   19.493  -17.345 1.00 19.55  ? 158 ASP A O     1 
ATOM   1262 C  CB    . ASP A 1 178 ? 0.622   18.181  -16.122 1.00 19.01  ? 158 ASP A CB    1 
ATOM   1263 C  CG    . ASP A 1 178 ? 0.124   17.686  -14.750 1.00 20.51  ? 158 ASP A CG    1 
ATOM   1264 O  OD1   . ASP A 1 178 ? 0.599   18.143  -13.688 1.00 21.61  ? 158 ASP A OD1   1 
ATOM   1265 O  OD2   . ASP A 1 178 ? -0.775  16.799  -14.749 1.00 24.37  ? 158 ASP A OD2   1 
ATOM   1266 N  N     . VAL A 1 179 ? 1.563   20.021  -18.440 1.00 17.92  ? 159 VAL A N     1 
ATOM   1267 C  CA    . VAL A 1 179 ? 2.301   20.239  -19.689 1.00 17.63  ? 159 VAL A CA    1 
ATOM   1268 C  C     . VAL A 1 179 ? 3.233   21.448  -19.569 1.00 21.03  ? 159 VAL A C     1 
ATOM   1269 O  O     . VAL A 1 179 ? 4.373   21.426  -20.066 1.00 18.50  ? 159 VAL A O     1 
ATOM   1270 C  CB    . VAL A 1 179 ? 1.337   20.380  -20.881 1.00 17.38  ? 159 VAL A CB    1 
ATOM   1271 C  CG1   . VAL A 1 179 ? 2.164   20.604  -22.181 1.00 20.32  ? 159 VAL A CG1   1 
ATOM   1272 C  CG2   . VAL A 1 179 ? 0.489   19.127  -20.991 1.00 17.60  ? 159 VAL A CG2   1 
ATOM   1273 N  N     . ALA A 1 180 ? 2.770   22.515  -18.908 1.00 18.46  ? 160 ALA A N     1 
ATOM   1274 C  CA    . ALA A 1 180 ? 3.616   23.693  -18.699 1.00 16.56  ? 160 ALA A CA    1 
ATOM   1275 C  C     . ALA A 1 180 ? 4.893   23.335  -17.949 1.00 19.37  ? 160 ALA A C     1 
ATOM   1276 O  O     . ALA A 1 180 ? 5.953   23.900  -18.231 1.00 18.76  ? 160 ALA A O     1 
ATOM   1277 C  CB    . ALA A 1 180 ? 2.856   24.788  -17.934 1.00 17.34  ? 160 ALA A CB    1 
ATOM   1278 N  N     . VAL A 1 181 ? 4.800   22.434  -16.963 1.00 17.95  ? 161 VAL A N     1 
ATOM   1279 C  CA    . VAL A 1 181 ? 5.981   22.009  -16.209 1.00 18.20  ? 161 VAL A CA    1 
ATOM   1280 C  C     . VAL A 1 181 ? 6.984   21.346  -17.142 1.00 20.24  ? 161 VAL A C     1 
ATOM   1281 O  O     . VAL A 1 181 ? 8.203   21.566  -17.025 1.00 19.42  ? 161 VAL A O     1 
ATOM   1282 C  CB    . VAL A 1 181 ? 5.574   21.073  -15.051 1.00 17.72  ? 161 VAL A CB    1 
ATOM   1283 C  CG1   . VAL A 1 181 ? 6.801   20.426  -14.401 1.00 20.53  ? 161 VAL A CG1   1 
ATOM   1284 C  CG2   . VAL A 1 181 ? 4.776   21.858  -14.009 1.00 21.11  ? 161 VAL A CG2   1 
ATOM   1285 N  N     . LEU A 1 182 ? 6.491   20.531  -18.091 1.00 19.66  ? 162 LEU A N     1 
ATOM   1286 C  CA    . LEU A 1 182 ? 7.420   19.918  -19.059 1.00 21.66  ? 162 LEU A CA    1 
ATOM   1287 C  C     . LEU A 1 182 ? 8.016   20.952  -20.030 1.00 20.23  ? 162 LEU A C     1 
ATOM   1288 O  O     . LEU A 1 182 ? 9.193   20.835  -20.433 1.00 19.99  ? 162 LEU A O     1 
ATOM   1289 C  CB    . LEU A 1 182 ? 6.730   18.790  -19.828 1.00 19.59  ? 162 LEU A CB    1 
ATOM   1290 C  CG    . LEU A 1 182 ? 6.317   17.605  -18.946 1.00 21.02  ? 162 LEU A CG    1 
ATOM   1291 C  CD1   . LEU A 1 182 ? 5.456   16.614  -19.730 1.00 22.95  ? 162 LEU A CD1   1 
ATOM   1292 C  CD2   . LEU A 1 182 ? 7.539   16.924  -18.338 1.00 25.38  ? 162 LEU A CD2   1 
ATOM   1293 N  N     . VAL A 1 183 ? 7.230   21.956  -20.434 1.00 18.49  ? 163 VAL A N     1 
ATOM   1294 C  CA    . VAL A 1 183 ? 7.783   23.022  -21.280 1.00 17.71  ? 163 VAL A CA    1 
ATOM   1295 C  C     . VAL A 1 183 ? 8.853   23.800  -20.518 1.00 20.25  ? 163 VAL A C     1 
ATOM   1296 O  O     . VAL A 1 183 ? 9.929   24.126  -21.056 1.00 19.12  ? 163 VAL A O     1 
ATOM   1297 C  CB    . VAL A 1 183 ? 6.665   23.960  -21.773 1.00 17.25  ? 163 VAL A CB    1 
ATOM   1298 C  CG1   . VAL A 1 183 ? 7.271   25.164  -22.484 1.00 19.16  ? 163 VAL A CG1   1 
ATOM   1299 C  CG2   . VAL A 1 183 ? 5.704   23.209  -22.697 1.00 18.01  ? 163 VAL A CG2   1 
ATOM   1300 N  N     . ALA A 1 184 ? 8.574   24.103  -19.248 1.00 20.09  ? 164 ALA A N     1 
ATOM   1301 C  CA    . ALA A 1 184 ? 9.555   24.755  -18.383 1.00 18.10  ? 164 ALA A CA    1 
ATOM   1302 C  C     . ALA A 1 184 ? 10.826  23.927  -18.260 1.00 20.50  ? 164 ALA A C     1 
ATOM   1303 O  O     . ALA A 1 184 ? 11.928  24.485  -18.217 1.00 20.92  ? 164 ALA A O     1 
ATOM   1304 C  CB    . ALA A 1 184 ? 8.948   24.991  -16.995 1.00 19.52  ? 164 ALA A CB    1 
ATOM   1305 N  N     . ARG A 1 185 ? 10.689  22.599  -18.155 1.00 18.79  ? 165 ARG A N     1 
ATOM   1306 C  CA    . ARG A 1 185 ? 11.862  21.723  -18.097 1.00 20.10  ? 165 ARG A CA    1 
ATOM   1307 C  C     . ARG A 1 185 ? 12.708  21.848  -19.360 1.00 20.65  ? 165 ARG A C     1 
ATOM   1308 O  O     . ARG A 1 185 ? 13.950  21.883  -19.292 1.00 20.19  ? 165 ARG A O     1 
ATOM   1309 C  CB    . ARG A 1 185 ? 11.414  20.276  -17.883 1.00 22.43  ? 165 ARG A CB    1 
ATOM   1310 C  CG    . ARG A 1 185 ? 12.553  19.257  -17.872 1.00 25.01  ? 165 ARG A CG    1 
ATOM   1311 C  CD    . ARG A 1 185 ? 12.004  17.844  -17.715 1.00 26.82  ? 165 ARG A CD    1 
ATOM   1312 N  NE    . ARG A 1 185 ? 11.284  17.685  -16.453 1.00 29.44  ? 165 ARG A NE    1 
ATOM   1313 C  CZ    . ARG A 1 185 ? 10.586  16.606  -16.127 1.00 41.99  ? 165 ARG A CZ    1 
ATOM   1314 N  NH1   . ARG A 1 185 ? 10.522  15.557  -16.931 1.00 35.97  ? 165 ARG A NH1   1 
ATOM   1315 N  NH2   . ARG A 1 185 ? 9.928   16.581  -14.969 1.00 33.78  ? 165 ARG A NH2   1 
ATOM   1316 N  N     . ALA A 1 186 ? 12.058  21.917  -20.523 1.00 23.56  ? 166 ALA A N     1 
ATOM   1317 C  CA    . ALA A 1 186 ? 12.824  22.119  -21.758 1.00 22.18  ? 166 ALA A CA    1 
ATOM   1318 C  C     . ALA A 1 186 ? 13.530  23.479  -21.755 1.00 19.83  ? 166 ALA A C     1 
ATOM   1319 O  O     . ALA A 1 186 ? 14.701  23.595  -22.172 1.00 20.92  ? 166 ALA A O     1 
ATOM   1320 C  CB    . ALA A 1 186 ? 11.900  21.971  -22.967 1.00 22.55  ? 166 ALA A CB    1 
ATOM   1321 N  N     . CYS A 1 187 ? 12.830  24.522  -21.284 1.00 20.01  ? 167 CYS A N     1 
ATOM   1322 C  CA    . CYS A 1 187 ? 13.459  25.835  -21.138 1.00 22.16  ? 167 CYS A CA    1 
ATOM   1323 C  C     . CYS A 1 187 ? 14.672  25.762  -20.219 1.00 24.73  ? 167 CYS A C     1 
ATOM   1324 O  O     . CYS A 1 187 ? 15.706  26.386  -20.496 1.00 22.43  ? 167 CYS A O     1 
ATOM   1325 C  CB    . CYS A 1 187 ? 12.456  26.862  -20.612 1.00 20.42  ? 167 CYS A CB    1 
ATOM   1326 S  SG    . CYS A 1 187 ? 11.107  27.226  -21.756 1.00 21.48  ? 167 CYS A SG    1 
ATOM   1327 N  N     . ASP A 1 188 ? 14.570  25.000  -19.122 1.00 19.95  ? 168 ASP A N     1 
ATOM   1328 C  CA    . ASP A 1 188 ? 15.717  24.821  -18.230 1.00 20.44  ? 168 ASP A CA    1 
ATOM   1329 C  C     . ASP A 1 188 ? 16.876  24.140  -18.947 1.00 23.06  ? 168 ASP A C     1 
ATOM   1330 O  O     . ASP A 1 188 ? 18.036  24.475  -18.708 1.00 22.62  ? 168 ASP A O     1 
ATOM   1331 C  CB    . ASP A 1 188 ? 15.342  23.995  -16.992 1.00 22.25  ? 168 ASP A CB    1 
ATOM   1332 C  CG    . ASP A 1 188 ? 14.561  24.788  -15.952 1.00 24.48  ? 168 ASP A CG    1 
ATOM   1333 O  OD1   . ASP A 1 188 ? 14.703  26.033  -15.878 1.00 21.43  ? 168 ASP A OD1   1 
ATOM   1334 O  OD2   . ASP A 1 188 ? 13.813  24.142  -15.188 1.00 22.45  ? 168 ASP A OD2   1 
ATOM   1335 N  N     . ARG A 1 189 ? 16.597  23.140  -19.784 1.00 22.16  ? 169 ARG A N     1 
ATOM   1336 C  CA    . ARG A 1 189 ? 17.706  22.520  -20.516 1.00 23.45  ? 169 ARG A CA    1 
ATOM   1337 C  C     . ARG A 1 189 ? 18.435  23.554  -21.373 1.00 24.12  ? 169 ARG A C     1 
ATOM   1338 O  O     . ARG A 1 189 ? 19.685  23.612  -21.396 1.00 22.74  ? 169 ARG A O     1 
ATOM   1339 C  CB    . ARG A 1 189 ? 17.196  21.374  -21.382 1.00 27.20  ? 169 ARG A CB    1 
ATOM   1340 C  CG    . ARG A 1 189 ? 16.751  20.143  -20.620 1.00 33.74  ? 169 ARG A CG    1 
ATOM   1341 C  CD    . ARG A 1 189 ? 16.104  19.178  -21.586 1.00 37.70  ? 169 ARG A CD    1 
ATOM   1342 N  NE    . ARG A 1 189 ? 16.902  19.051  -22.799 1.00 47.75  ? 169 ARG A NE    1 
ATOM   1343 C  CZ    . ARG A 1 189 ? 16.414  18.776  -24.002 1.00 39.05  ? 169 ARG A CZ    1 
ATOM   1344 N  NH1   . ARG A 1 189 ? 15.118  18.600  -24.201 1.00 33.92  ? 169 ARG A NH1   1 
ATOM   1345 N  NH2   . ARG A 1 189 ? 17.248  18.691  -25.034 1.00 40.17  ? 169 ARG A NH2   1 
ATOM   1346 N  N     . PHE A 1 190 ? 17.668  24.405  -22.057 1.00 25.20  ? 170 PHE A N     1 
ATOM   1347 C  CA    . PHE A 1 190 ? 18.278  25.475  -22.846 1.00 22.54  ? 170 PHE A CA    1 
ATOM   1348 C  C     . PHE A 1 190 ? 19.123  26.406  -21.974 1.00 22.12  ? 170 PHE A C     1 
ATOM   1349 O  O     . PHE A 1 190 ? 20.290  26.694  -22.292 1.00 23.10  ? 170 PHE A O     1 
ATOM   1350 C  CB    . PHE A 1 190 ? 17.181  26.268  -23.570 1.00 21.67  ? 170 PHE A CB    1 
ATOM   1351 C  CG    . PHE A 1 190 ? 17.679  27.533  -24.220 1.00 24.11  ? 170 PHE A CG    1 
ATOM   1352 C  CD1   . PHE A 1 190 ? 18.153  27.512  -25.515 1.00 28.19  ? 170 PHE A CD1   1 
ATOM   1353 C  CD2   . PHE A 1 190 ? 17.661  28.746  -23.535 1.00 27.87  ? 170 PHE A CD2   1 
ATOM   1354 C  CE1   . PHE A 1 190 ? 18.617  28.669  -26.127 1.00 25.31  ? 170 PHE A CE1   1 
ATOM   1355 C  CE2   . PHE A 1 190 ? 18.131  29.907  -24.137 1.00 28.86  ? 170 PHE A CE2   1 
ATOM   1356 C  CZ    . PHE A 1 190 ? 18.612  29.862  -25.436 1.00 26.27  ? 170 PHE A CZ    1 
ATOM   1357 N  N     . ALA A 1 191 ? 18.555  26.876  -20.859 1.00 21.85  ? 171 ALA A N     1 
ATOM   1358 C  CA    . ALA A 1 191 ? 19.244  27.852  -20.012 1.00 21.97  ? 171 ALA A CA    1 
ATOM   1359 C  C     . ALA A 1 191 ? 20.478  27.248  -19.343 1.00 24.48  ? 171 ALA A C     1 
ATOM   1360 O  O     . ALA A 1 191 ? 21.508  27.922  -19.193 1.00 25.54  ? 171 ALA A O     1 
ATOM   1361 C  CB    . ALA A 1 191 ? 18.273  28.409  -18.965 1.00 25.08  ? 171 ALA A CB    1 
ATOM   1362 N  N     . GLU A 1 192 ? 20.388  25.986  -18.916 1.00 22.54  ? 172 GLU A N     1 
ATOM   1363 C  CA    . GLU A 1 192 ? 21.534  25.313  -18.316 1.00 23.20  ? 172 GLU A CA    1 
ATOM   1364 C  C     . GLU A 1 192 ? 22.657  25.165  -19.319 1.00 23.92  ? 172 GLU A C     1 
ATOM   1365 O  O     . GLU A 1 192 ? 23.834  25.163  -18.933 1.00 25.46  ? 172 GLU A O     1 
ATOM   1366 C  CB    . GLU A 1 192 ? 21.115  23.942  -17.779 1.00 26.83  ? 172 GLU A CB    1 
ATOM   1367 C  CG    . GLU A 1 192 ? 20.226  24.017  -16.527 1.00 23.95  ? 172 GLU A CG    1 
ATOM   1368 C  CD    . GLU A 1 192 ? 19.421  22.752  -16.302 1.00 33.83  ? 172 GLU A CD    1 
ATOM   1369 O  OE1   . GLU A 1 192 ? 19.760  21.708  -16.897 1.00 33.40  ? 172 GLU A OE1   1 
ATOM   1370 O  OE2   . GLU A 1 192 ? 18.434  22.807  -15.536 1.00 26.68  ? 172 GLU A OE2   1 
ATOM   1371 N  N     . LYS A 1 193 ? 22.319  25.059  -20.608 1.00 24.79  ? 173 LYS A N     1 
ATOM   1372 C  CA    . LYS A 1 193 ? 23.388  24.997  -21.599 1.00 26.89  ? 173 LYS A CA    1 
ATOM   1373 C  C     . LYS A 1 193 ? 23.936  26.374  -21.974 1.00 26.18  ? 173 LYS A C     1 
ATOM   1374 O  O     . LYS A 1 193 ? 25.133  26.489  -22.271 1.00 26.79  ? 173 LYS A O     1 
ATOM   1375 C  CB    . LYS A 1 193 ? 22.870  24.292  -22.859 1.00 27.00  ? 173 LYS A CB    1 
ATOM   1376 C  CG    . LYS A 1 193 ? 23.855  24.219  -24.024 1.00 33.18  ? 173 LYS A CG    1 
ATOM   1377 C  CD    . LYS A 1 193 ? 23.221  23.412  -25.160 1.00 39.69  ? 173 LYS A CD    1 
ATOM   1378 C  CE    . LYS A 1 193 ? 24.195  23.156  -26.299 1.00 51.61  ? 173 LYS A CE    1 
ATOM   1379 N  NZ    . LYS A 1 193 ? 24.445  24.380  -27.106 1.00 65.01  ? 173 LYS A NZ    1 
ATOM   1380 N  N     . GLN A 1 194 ? 23.122  27.433  -21.889 1.00 27.38  ? 174 GLN A N     1 
ATOM   1381 C  CA    . GLN A 1 194 ? 23.480  28.712  -22.499 1.00 27.30  ? 174 GLN A CA    1 
ATOM   1382 C  C     . GLN A 1 194 ? 23.802  29.838  -21.523 1.00 29.68  ? 174 GLN A C     1 
ATOM   1383 O  O     . GLN A 1 194 ? 24.371  30.853  -21.951 1.00 28.26  ? 174 GLN A O     1 
ATOM   1384 C  CB    . GLN A 1 194 ? 22.348  29.209  -23.424 1.00 23.83  ? 174 GLN A CB    1 
ATOM   1385 C  CG    . GLN A 1 194 ? 21.963  28.265  -24.569 1.00 23.86  ? 174 GLN A CG    1 
ATOM   1386 C  CD    . GLN A 1 194 ? 22.995  28.278  -25.697 1.00 32.83  ? 174 GLN A CD    1 
ATOM   1387 O  OE1   . GLN A 1 194 ? 23.823  29.191  -25.790 1.00 34.99  ? 174 GLN A OE1   1 
ATOM   1388 N  NE2   . GLN A 1 194 ? 22.949  27.268  -26.555 1.00 31.89  ? 174 GLN A NE2   1 
ATOM   1389 N  N     . ILE A 1 195 ? 23.456  29.706  -20.245 1.00 25.39  ? 175 ILE A N     1 
ATOM   1390 C  CA    . ILE A 1 195 ? 23.571  30.795  -19.275 1.00 23.85  ? 175 ILE A CA    1 
ATOM   1391 C  C     . ILE A 1 195 ? 24.506  30.362  -18.155 1.00 24.50  ? 175 ILE A C     1 
ATOM   1392 O  O     . ILE A 1 195 ? 24.167  29.476  -17.363 1.00 24.75  ? 175 ILE A O     1 
ATOM   1393 C  CB    . ILE A 1 195 ? 22.205  31.194  -18.704 1.00 25.42  ? 175 ILE A CB    1 
ATOM   1394 C  CG1   . ILE A 1 195 ? 21.276  31.643  -19.831 1.00 24.01  ? 175 ILE A CG1   1 
ATOM   1395 C  CG2   . ILE A 1 195 ? 22.379  32.274  -17.657 1.00 24.46  ? 175 ILE A CG2   1 
ATOM   1396 C  CD1   . ILE A 1 195 ? 19.851  31.968  -19.363 1.00 23.45  ? 175 ILE A CD1   1 
ATOM   1397 N  N     . ALA A 1 196 ? 25.671  31.010  -18.051 1.00 24.89  ? 176 ALA A N     1 
ATOM   1398 C  CA    . ALA A 1 196 ? 26.594  30.686  -16.971 1.00 25.33  ? 176 ALA A CA    1 
ATOM   1399 C  C     . ALA A 1 196 ? 26.005  31.090  -15.623 1.00 25.04  ? 176 ALA A C     1 
ATOM   1400 O  O     . ALA A 1 196 ? 25.516  32.214  -15.458 1.00 29.67  ? 176 ALA A O     1 
ATOM   1401 C  CB    . ALA A 1 196 ? 27.936  31.383  -17.192 1.00 29.43  ? 176 ALA A CB    1 
ATOM   1402 N  N     . GLY A 1 197 ? 26.047  30.171  -14.658 1.00 26.67  ? 177 GLY A N     1 
ATOM   1403 C  CA    . GLY A 1 197 ? 25.543  30.436  -13.322 1.00 25.54  ? 177 GLY A CA    1 
ATOM   1404 C  C     . GLY A 1 197 ? 24.058  30.210  -13.126 1.00 27.86  ? 177 GLY A C     1 
ATOM   1405 O  O     . GLY A 1 197 ? 23.561  30.428  -12.013 1.00 29.19  ? 177 GLY A O     1 
ATOM   1406 N  N     . TYR A 1 198 ? 23.341  29.799  -14.165 1.00 26.54  ? 178 TYR A N     1 
ATOM   1407 C  CA    . TYR A 1 198 ? 21.908  29.551  -14.053 1.00 22.75  ? 178 TYR A CA    1 
ATOM   1408 C  C     . TYR A 1 198 ? 21.636  28.440  -13.038 1.00 25.44  ? 178 TYR A C     1 
ATOM   1409 O  O     . TYR A 1 198 ? 22.338  27.423  -13.029 1.00 25.70  ? 178 TYR A O     1 
ATOM   1410 C  CB    . TYR A 1 198 ? 21.354  29.160  -15.422 1.00 22.48  ? 178 TYR A CB    1 
ATOM   1411 C  CG    . TYR A 1 198 ? 19.852  28.989  -15.487 1.00 21.77  ? 178 TYR A CG    1 
ATOM   1412 C  CD1   . TYR A 1 198 ? 19.022  30.088  -15.636 1.00 22.90  ? 178 TYR A CD1   1 
ATOM   1413 C  CD2   . TYR A 1 198 ? 19.280  27.722  -15.451 1.00 21.63  ? 178 TYR A CD2   1 
ATOM   1414 C  CE1   . TYR A 1 198 ? 17.641  29.929  -15.718 1.00 20.72  ? 178 TYR A CE1   1 
ATOM   1415 C  CE2   . TYR A 1 198 ? 17.897  27.552  -15.527 1.00 22.92  ? 178 TYR A CE2   1 
ATOM   1416 C  CZ    . TYR A 1 198 ? 17.094  28.659  -15.669 1.00 24.51  ? 178 TYR A CZ    1 
ATOM   1417 O  OH    . TYR A 1 198 ? 15.724  28.483  -15.749 1.00 24.27  ? 178 TYR A OH    1 
ATOM   1418 N  N     . PRO A 1 199 ? 20.607  28.578  -12.197 1.00 23.77  ? 179 PRO A N     1 
ATOM   1419 C  CA    . PRO A 1 199 ? 20.280  27.510  -11.238 1.00 25.79  ? 179 PRO A CA    1 
ATOM   1420 C  C     . PRO A 1 199 ? 19.585  26.364  -11.955 1.00 23.81  ? 179 PRO A C     1 
ATOM   1421 O  O     . PRO A 1 199 ? 18.524  26.553  -12.548 1.00 24.54  ? 179 PRO A O     1 
ATOM   1422 C  CB    . PRO A 1 199 ? 19.335  28.197  -10.240 1.00 28.12  ? 179 PRO A CB    1 
ATOM   1423 C  CG    . PRO A 1 199 ? 19.274  29.645  -10.637 1.00 36.23  ? 179 PRO A CG    1 
ATOM   1424 C  CD    . PRO A 1 199 ? 19.704  29.730  -12.063 1.00 28.21  ? 179 PRO A CD    1 
ATOM   1425 N  N     . ALA A 1 200 ? 20.184  25.179  -11.896 1.00 29.76  ? 180 ALA A N     1 
ATOM   1426 C  CA    . ALA A 1 200 ? 19.632  24.029  -12.594 1.00 27.86  ? 180 ALA A CA    1 
ATOM   1427 C  C     . ALA A 1 200 ? 18.189  23.800  -12.180 1.00 26.79  ? 180 ALA A C     1 
ATOM   1428 O  O     . ALA A 1 200 ? 17.857  23.847  -10.993 1.00 27.11  ? 180 ALA A O     1 
ATOM   1429 C  CB    . ALA A 1 200 ? 20.463  22.783  -12.302 1.00 33.69  ? 180 ALA A CB    1 
ATOM   1430 N  N     . GLY A 1 201 ? 17.331  23.585  -13.172 1.00 21.38  ? 181 GLY A N     1 
ATOM   1431 C  CA    . GLY A 1 201 ? 15.958  23.213  -12.892 1.00 24.73  ? 181 GLY A CA    1 
ATOM   1432 C  C     . GLY A 1 201 ? 15.075  24.327  -12.384 1.00 28.10  ? 181 GLY A C     1 
ATOM   1433 O  O     . GLY A 1 201 ? 13.983  24.047  -11.885 1.00 22.29  ? 181 GLY A O     1 
ATOM   1434 N  N     . TYR A 1 202 ? 15.488  25.585  -12.546 1.00 22.07  ? 182 TYR A N     1 
ATOM   1435 C  CA    . TYR A 1 202 ? 14.803  26.697  -11.878 1.00 20.28  ? 182 TYR A CA    1 
ATOM   1436 C  C     . TYR A 1 202 ? 13.366  26.879  -12.358 1.00 23.23  ? 182 TYR A C     1 
ATOM   1437 O  O     . TYR A 1 202 ? 12.453  27.024  -11.536 1.00 22.29  ? 182 TYR A O     1 
ATOM   1438 C  CB    . TYR A 1 202 ? 15.579  28.000  -12.068 1.00 22.02  ? 182 TYR A CB    1 
ATOM   1439 C  CG    . TYR A 1 202 ? 15.059  29.124  -11.206 1.00 20.39  ? 182 TYR A CG    1 
ATOM   1440 C  CD1   . TYR A 1 202 ? 15.209  29.084  -9.828  1.00 24.55  ? 182 TYR A CD1   1 
ATOM   1441 C  CD2   . TYR A 1 202 ? 14.404  30.215  -11.758 1.00 21.43  ? 182 TYR A CD2   1 
ATOM   1442 C  CE1   . TYR A 1 202 ? 14.732  30.102  -9.021  1.00 26.66  ? 182 TYR A CE1   1 
ATOM   1443 C  CE2   . TYR A 1 202 ? 13.928  31.250  -10.955 1.00 21.81  ? 182 TYR A CE2   1 
ATOM   1444 C  CZ    . TYR A 1 202 ? 14.097  31.183  -9.585  1.00 22.21  ? 182 TYR A CZ    1 
ATOM   1445 O  OH    . TYR A 1 202 ? 13.618  32.195  -8.775  1.00 25.68  ? 182 TYR A OH    1 
ATOM   1446 N  N     . LEU A 1 203 ? 13.154  26.980  -13.680 1.00 19.24  ? 183 LEU A N     1 
ATOM   1447 C  CA    . LEU A 1 203 ? 11.806  27.286  -14.171 1.00 18.73  ? 183 LEU A CA    1 
ATOM   1448 C  C     . LEU A 1 203 ? 10.843  26.140  -13.885 1.00 19.39  ? 183 LEU A C     1 
ATOM   1449 O  O     . LEU A 1 203 ? 9.671   26.376  -13.545 1.00 20.30  ? 183 LEU A O     1 
ATOM   1450 C  CB    . LEU A 1 203 ? 11.841  27.595  -15.669 1.00 20.34  ? 183 LEU A CB    1 
ATOM   1451 C  CG    . LEU A 1 203 ? 12.371  28.973  -16.087 1.00 20.10  ? 183 LEU A CG    1 
ATOM   1452 C  CD1   . LEU A 1 203 ? 12.760  28.970  -17.555 1.00 21.94  ? 183 LEU A CD1   1 
ATOM   1453 C  CD2   . LEU A 1 203 ? 11.327  30.067  -15.797 1.00 21.75  ? 183 LEU A CD2   1 
ATOM   1454 N  N     . GLU A 1 204 ? 11.307  24.893  -14.010 1.00 19.42  ? 184 GLU A N     1 
ATOM   1455 C  CA    . GLU A 1 204 ? 10.446  23.752  -13.672 1.00 18.82  ? 184 GLU A CA    1 
ATOM   1456 C  C     . GLU A 1 204 ? 9.986   23.829  -12.218 1.00 21.07  ? 184 GLU A C     1 
ATOM   1457 O  O     . GLU A 1 204 ? 8.796   23.639  -11.916 1.00 20.74  ? 184 GLU A O     1 
ATOM   1458 C  CB    . GLU A 1 204 ? 11.174  22.431  -13.943 1.00 24.42  ? 184 GLU A CB    1 
ATOM   1459 C  CG    . GLU A 1 204 ? 10.313  21.200  -13.659 1.00 21.18  ? 184 GLU A CG    1 
ATOM   1460 C  CD    . GLU A 1 204 ? 11.055  19.886  -13.839 1.00 32.75  ? 184 GLU A CD    1 
ATOM   1461 O  OE1   . GLU A 1 204 ? 12.171  19.884  -14.405 1.00 31.76  ? 184 GLU A OE1   1 
ATOM   1462 O  OE2   . GLU A 1 204 ? 10.526  18.847  -13.385 1.00 26.91  ? 184 GLU A OE2   1 
ATOM   1463 N  N     . GLY A 1 205 ? 10.907  24.134  -11.304 1.00 20.95  ? 185 GLY A N     1 
ATOM   1464 C  CA    . GLY A 1 205 ? 10.533  24.226  -9.901  1.00 19.60  ? 185 GLY A CA    1 
ATOM   1465 C  C     . GLY A 1 205 ? 9.607   25.395  -9.634  1.00 26.69  ? 185 GLY A C     1 
ATOM   1466 O  O     . GLY A 1 205 ? 8.661   25.281  -8.848  1.00 24.77  ? 185 GLY A O     1 
ATOM   1467 N  N     . VAL A 1 206 ? 9.849   26.527  -10.301 1.00 21.50  ? 186 VAL A N     1 
ATOM   1468 C  CA    . VAL A 1 206 ? 9.007   27.704  -10.105 1.00 22.82  ? 186 VAL A CA    1 
ATOM   1469 C  C     . VAL A 1 206 ? 7.567   27.426  -10.540 1.00 22.74  ? 186 VAL A C     1 
ATOM   1470 O  O     . VAL A 1 206 ? 6.613   27.763  -9.821  1.00 24.36  ? 186 VAL A O     1 
ATOM   1471 C  CB    . VAL A 1 206 ? 9.624   28.910  -10.838 1.00 24.40  ? 186 VAL A CB    1 
ATOM   1472 C  CG1   . VAL A 1 206 ? 8.584   29.951  -11.144 1.00 33.48  ? 186 VAL A CG1   1 
ATOM   1473 C  CG2   . VAL A 1 206 ? 10.794  29.476  -10.003 1.00 26.73  ? 186 VAL A CG2   1 
ATOM   1474 N  N     . VAL A 1 207 ? 7.381   26.793  -11.705 1.00 18.24  ? 187 VAL A N     1 
ATOM   1475 C  CA    . VAL A 1 207 ? 6.028   26.537  -12.199 1.00 19.95  ? 187 VAL A CA    1 
ATOM   1476 C  C     . VAL A 1 207 ? 5.352   25.456  -11.360 1.00 23.00  ? 187 VAL A C     1 
ATOM   1477 O  O     . VAL A 1 207 ? 4.170   25.568  -11.005 1.00 22.38  ? 187 VAL A O     1 
ATOM   1478 C  CB    . VAL A 1 207 ? 6.058   26.158  -13.694 1.00 19.26  ? 187 VAL A CB    1 
ATOM   1479 C  CG1   . VAL A 1 207 ? 4.652   25.721  -14.170 1.00 21.24  ? 187 VAL A CG1   1 
ATOM   1480 C  CG2   . VAL A 1 207 ? 6.582   27.316  -14.526 1.00 21.83  ? 187 VAL A CG2   1 
ATOM   1481 N  N     . LYS A 1 208 ? 6.093   24.401  -11.016 1.00 19.54  ? 188 LYS A N     1 
ATOM   1482 C  CA    . LYS A 1 208 ? 5.498   23.250  -10.339 1.00 22.47  ? 188 LYS A CA    1 
ATOM   1483 C  C     . LYS A 1 208 ? 5.034   23.579  -8.920  1.00 21.97  ? 188 LYS A C     1 
ATOM   1484 O  O     . LYS A 1 208 ? 4.093   22.951  -8.415  1.00 22.15  ? 188 LYS A O     1 
ATOM   1485 C  CB    . LYS A 1 208 ? 6.525   22.113  -10.313 1.00 27.07  ? 188 LYS A CB    1 
ATOM   1486 C  CG    . LYS A 1 208 ? 6.045   20.806  -9.723  1.00 36.02  ? 188 LYS A CG    1 
ATOM   1487 C  CD    . LYS A 1 208 ? 7.221   19.841  -9.538  1.00 38.76  ? 188 LYS A CD    1 
ATOM   1488 C  CE    . LYS A 1 208 ? 7.986   19.647  -10.838 1.00 48.42  ? 188 LYS A CE    1 
ATOM   1489 N  NZ    . LYS A 1 208 ? 9.040   18.595  -10.720 1.00 53.67  ? 188 LYS A NZ    1 
ATOM   1490 N  N     . THR A 1 209 ? 5.660   24.553  -8.263  1.00 19.44  ? 189 THR A N     1 
ATOM   1491 C  CA    . THR A 1 209 ? 5.362   24.880  -6.872  1.00 19.23  ? 189 THR A CA    1 
ATOM   1492 C  C     . THR A 1 209 ? 4.595   26.189  -6.727  1.00 19.94  ? 189 THR A C     1 
ATOM   1493 O  O     . THR A 1 209 ? 4.340   26.627  -5.601  1.00 22.06  ? 189 THR A O     1 
ATOM   1494 C  CB    . THR A 1 209 ? 6.659   24.937  -6.052  1.00 23.99  ? 189 THR A CB    1 
ATOM   1495 O  OG1   . THR A 1 209 ? 7.498   25.982  -6.569  1.00 22.73  ? 189 THR A OG1   1 
ATOM   1496 C  CG2   . THR A 1 209 ? 7.388   23.604  -6.133  1.00 26.82  ? 189 THR A CG2   1 
ATOM   1497 N  N     . SER A 1 210 ? 4.189   26.809  -7.828  1.00 19.60  ? 190 SER A N     1 
ATOM   1498 C  CA    . SER A 1 210 ? 3.562   28.122  -7.732  1.00 20.88  ? 190 SER A CA    1 
ATOM   1499 C  C     . SER A 1 210 ? 2.154   28.029  -7.162  1.00 19.85  ? 190 SER A C     1 
ATOM   1500 O  O     . SER A 1 210 ? 1.353   27.188  -7.578  1.00 20.92  ? 190 SER A O     1 
ATOM   1501 C  CB    . SER A 1 210 ? 3.497   28.783  -9.107  1.00 17.95  ? 190 SER A CB    1 
ATOM   1502 O  OG    . SER A 1 210 ? 2.724   29.977  -9.048  1.00 18.98  ? 190 SER A OG    1 
ATOM   1503 N  N     . THR A 1 211 ? 1.844   28.929  -6.224  1.00 17.78  ? 191 THR A N     1 
ATOM   1504 C  CA    . THR A 1 211 ? 0.468   29.146  -5.790  1.00 19.61  ? 191 THR A CA    1 
ATOM   1505 C  C     . THR A 1 211 ? -0.117  30.448  -6.326  1.00 19.58  ? 191 THR A C     1 
ATOM   1506 O  O     . THR A 1 211 ? -1.238  30.814  -5.941  1.00 21.68  ? 191 THR A O     1 
ATOM   1507 C  CB    . THR A 1 211 ? 0.379   29.128  -4.260  1.00 26.79  ? 191 THR A CB    1 
ATOM   1508 O  OG1   . THR A 1 211 ? 1.256   30.122  -3.723  1.00 28.09  ? 191 THR A OG1   1 
ATOM   1509 C  CG2   . THR A 1 211 ? 0.759   27.768  -3.736  1.00 26.20  ? 191 THR A CG2   1 
ATOM   1510 N  N     . THR A 1 212 ? 0.606   31.159  -7.202  1.00 18.69  ? 192 THR A N     1 
ATOM   1511 C  CA    . THR A 1 212 ? 0.138   32.402  -7.815  1.00 18.61  ? 192 THR A CA    1 
ATOM   1512 C  C     . THR A 1 212 ? -0.329  32.236  -9.253  1.00 18.07  ? 192 THR A C     1 
ATOM   1513 O  O     . THR A 1 212 ? -0.977  33.152  -9.785  1.00 18.48  ? 192 THR A O     1 
ATOM   1514 C  CB    . THR A 1 212 ? 1.239   33.468  -7.828  1.00 22.01  ? 192 THR A CB    1 
ATOM   1515 O  OG1   . THR A 1 212 ? 2.257   33.070  -8.765  1.00 23.34  ? 192 THR A OG1   1 
ATOM   1516 C  CG2   . THR A 1 212 ? 1.830   33.629  -6.443  1.00 24.88  ? 192 THR A CG2   1 
ATOM   1517 N  N     . THR A 1 213 ? 0.004   31.118  -9.902  1.00 16.83  ? 193 THR A N     1 
ATOM   1518 C  CA    . THR A 1 213 ? -0.512  30.833  -11.240 1.00 16.49  ? 193 THR A CA    1 
ATOM   1519 C  C     . THR A 1 213 ? -2.006  31.105  -11.319 1.00 16.39  ? 193 THR A C     1 
ATOM   1520 O  O     . THR A 1 213 ? -2.756  30.734  -10.419 1.00 18.34  ? 193 THR A O     1 
ATOM   1521 C  CB    . THR A 1 213 ? -0.218  29.378  -11.599 1.00 17.97  ? 193 THR A CB    1 
ATOM   1522 O  OG1   . THR A 1 213 ? 1.196   29.248  -11.824 1.00 16.55  ? 193 THR A OG1   1 
ATOM   1523 C  CG2   . THR A 1 213 ? -0.993  28.923  -12.858 1.00 18.07  ? 193 THR A CG2   1 
ATOM   1524 N  N     . LYS A 1 214 ? -2.416  31.813  -12.371 1.00 16.23  ? 194 LYS A N     1 
ATOM   1525 C  CA    . LYS A 1 214 ? -3.779  32.330  -12.450 1.00 16.89  ? 194 LYS A CA    1 
ATOM   1526 C  C     . LYS A 1 214 ? -4.437  31.872  -13.743 1.00 18.12  ? 194 LYS A C     1 
ATOM   1527 O  O     . LYS A 1 214 ? -3.878  32.063  -14.818 1.00 17.26  ? 194 LYS A O     1 
ATOM   1528 C  CB    . LYS A 1 214 ? -3.760  33.858  -12.362 1.00 19.59  ? 194 LYS A CB    1 
ATOM   1529 C  CG    . LYS A 1 214 ? -5.108  34.523  -12.591 1.00 26.74  ? 194 LYS A CG    1 
ATOM   1530 C  CD    . LYS A 1 214 ? -5.748  34.898  -11.306 1.00 26.61  ? 194 LYS A CD    1 
ATOM   1531 C  CE    . LYS A 1 214 ? -5.002  36.007  -10.581 1.00 31.58  ? 194 LYS A CE    1 
ATOM   1532 N  NZ    . LYS A 1 214 ? -5.586  36.126  -9.206  1.00 26.74  ? 194 LYS A NZ    1 
ATOM   1533 N  N     . ALA A 1 215 ? -5.626  31.280  -13.650 1.00 16.26  ? 195 ALA A N     1 
ATOM   1534 C  CA    . ALA A 1 215 ? -6.372  30.865  -14.836 1.00 15.70  ? 195 ALA A CA    1 
ATOM   1535 C  C     . ALA A 1 215 ? -7.510  31.838  -15.124 1.00 18.11  ? 195 ALA A C     1 
ATOM   1536 O  O     . ALA A 1 215 ? -8.135  32.368  -14.202 1.00 18.64  ? 195 ALA A O     1 
ATOM   1537 C  CB    . ALA A 1 215 ? -6.932  29.451  -14.668 1.00 17.62  ? 195 ALA A CB    1 
ATOM   1538 N  N     . ARG A 1 216 ? -7.747  32.083  -16.414 1.00 15.57  ? 196 ARG A N     1 
ATOM   1539 C  CA    . ARG A 1 216 ? -8.780  33.006  -16.881 1.00 15.63  ? 196 ARG A CA    1 
ATOM   1540 C  C     . ARG A 1 216 ? -9.650  32.311  -17.917 1.00 15.44  ? 196 ARG A C     1 
ATOM   1541 O  O     . ARG A 1 216 ? -9.174  31.915  -18.994 1.00 15.24  ? 196 ARG A O     1 
ATOM   1542 C  CB    . ARG A 1 216 ? -8.171  34.275  -17.486 1.00 17.15  ? 196 ARG A CB    1 
ATOM   1543 C  CG    . ARG A 1 216 ? -9.240  35.267  -17.995 1.00 16.88  ? 196 ARG A CG    1 
ATOM   1544 C  CD    . ARG A 1 216 ? -8.585  36.343  -18.850 1.00 24.99  ? 196 ARG A CD    1 
ATOM   1545 N  NE    . ARG A 1 216 ? -8.141  35.775  -20.116 1.00 30.55  ? 196 ARG A NE    1 
ATOM   1546 C  CZ    . ARG A 1 216 ? -7.381  36.402  -21.006 1.00 38.24  ? 196 ARG A CZ    1 
ATOM   1547 N  NH1   . ARG A 1 216 ? -6.919  37.623  -20.782 1.00 40.79  ? 196 ARG A NH1   1 
ATOM   1548 N  NH2   . ARG A 1 216 ? -7.064  35.780  -22.143 1.00 25.35  ? 196 ARG A NH2   1 
ATOM   1549 N  N     . LEU A 1 217 ? -10.935 32.202  -17.603 1.00 15.99  ? 197 LEU A N     1 
ATOM   1550 C  CA    . LEU A 1 217 ? -11.934 31.680  -18.515 1.00 16.66  ? 197 LEU A CA    1 
ATOM   1551 C  C     . LEU A 1 217 ? -12.691 32.882  -19.064 1.00 15.88  ? 197 LEU A C     1 
ATOM   1552 O  O     . LEU A 1 217 ? -13.265 33.655  -18.290 1.00 19.18  ? 197 LEU A O     1 
ATOM   1553 C  CB    . LEU A 1 217 ? -12.859 30.724  -17.763 1.00 17.92  ? 197 LEU A CB    1 
ATOM   1554 C  CG    . LEU A 1 217 ? -13.866 29.907  -18.556 1.00 20.34  ? 197 LEU A CG    1 
ATOM   1555 C  CD1   . LEU A 1 217 ? -13.121 28.900  -19.440 1.00 17.76  ? 197 LEU A CD1   1 
ATOM   1556 C  CD2   . LEU A 1 217 ? -14.810 29.198  -17.577 1.00 20.52  ? 197 LEU A CD2   1 
ATOM   1557 N  N     . LEU A 1 218 ? -12.652 33.070  -20.381 1.00 15.42  ? 198 LEU A N     1 
ATOM   1558 C  CA    . LEU A 1 218 ? -13.199 34.255  -21.030 1.00 16.34  ? 198 LEU A CA    1 
ATOM   1559 C  C     . LEU A 1 218 ? -14.399 33.896  -21.904 1.00 16.71  ? 198 LEU A C     1 
ATOM   1560 O  O     . LEU A 1 218 ? -14.338 32.942  -22.687 1.00 18.91  ? 198 LEU A O     1 
ATOM   1561 C  CB    . LEU A 1 218 ? -12.111 34.933  -21.877 1.00 17.28  ? 198 LEU A CB    1 
ATOM   1562 C  CG    . LEU A 1 218 ? -12.387 36.236  -22.631 1.00 27.86  ? 198 LEU A CG    1 
ATOM   1563 C  CD1   . LEU A 1 218 ? -12.698 37.354  -21.654 1.00 24.24  ? 198 LEU A CD1   1 
ATOM   1564 C  CD2   . LEU A 1 218 ? -11.182 36.599  -23.491 1.00 31.39  ? 198 LEU A CD2   1 
ATOM   1565 N  N     . HIS A 1 219 ? -15.444 34.723  -21.819 1.00 19.60  ? 199 HIS A N     1 
ATOM   1566 C  CA    . HIS A 1 219 ? -16.682 34.561  -22.584 1.00 18.20  ? 199 HIS A CA    1 
ATOM   1567 C  C     . HIS A 1 219 ? -16.974 35.854  -23.335 1.00 19.41  ? 199 HIS A C     1 
ATOM   1568 O  O     . HIS A 1 219 ? -17.304 36.867  -22.717 1.00 21.43  ? 199 HIS A O     1 
ATOM   1569 C  CB    . HIS A 1 219 ? -17.842 34.221  -21.646 1.00 17.29  ? 199 HIS A CB    1 
ATOM   1570 C  CG    . HIS A 1 219 ? -19.182 34.159  -22.321 1.00 17.77  ? 199 HIS A CG    1 
ATOM   1571 N  ND1   . HIS A 1 219 ? -19.568 33.104  -23.122 1.00 16.00  ? 199 HIS A ND1   1 
ATOM   1572 C  CD2   . HIS A 1 219 ? -20.224 35.025  -22.306 1.00 18.44  ? 199 HIS A CD2   1 
ATOM   1573 C  CE1   . HIS A 1 219 ? -20.805 33.316  -23.553 1.00 16.23  ? 199 HIS A CE1   1 
ATOM   1574 N  NE2   . HIS A 1 219 ? -21.219 34.474  -23.078 1.00 17.76  ? 199 HIS A NE2   1 
ATOM   1575 N  N     . TYR A 1 220 ? -16.877 35.820  -24.660 1.00 16.43  ? 200 TYR A N     1 
ATOM   1576 C  CA    . TYR A 1 220 ? -17.376 36.906  -25.498 1.00 19.24  ? 200 TYR A CA    1 
ATOM   1577 C  C     . TYR A 1 220 ? -18.877 36.738  -25.706 1.00 19.13  ? 200 TYR A C     1 
ATOM   1578 O  O     . TYR A 1 220 ? -19.327 35.689  -26.196 1.00 19.22  ? 200 TYR A O     1 
ATOM   1579 C  CB    . TYR A 1 220 ? -16.710 36.921  -26.873 1.00 20.79  ? 200 TYR A CB    1 
ATOM   1580 C  CG    . TYR A 1 220 ? -15.297 37.431  -26.952 1.00 22.86  ? 200 TYR A CG    1 
ATOM   1581 C  CD1   . TYR A 1 220 ? -14.227 36.619  -26.644 1.00 23.69  ? 200 TYR A CD1   1 
ATOM   1582 C  CD2   . TYR A 1 220 ? -15.047 38.722  -27.406 1.00 27.52  ? 200 TYR A CD2   1 
ATOM   1583 C  CE1   . TYR A 1 220 ? -12.923 37.091  -26.749 1.00 26.00  ? 200 TYR A CE1   1 
ATOM   1584 C  CE2   . TYR A 1 220 ? -13.762 39.201  -27.516 1.00 24.11  ? 200 TYR A CE2   1 
ATOM   1585 C  CZ    . TYR A 1 220 ? -12.707 38.383  -27.188 1.00 24.69  ? 200 TYR A CZ    1 
ATOM   1586 O  OH    . TYR A 1 220 ? -11.430 38.875  -27.293 1.00 30.89  ? 200 TYR A OH    1 
ATOM   1587 N  N     . PHE A 1 221 ? -19.637 37.753  -25.285 1.00 19.51  ? 201 PHE A N     1 
ATOM   1588 C  CA    . PHE A 1 221 ? -21.082 37.758  -25.446 1.00 19.35  ? 201 PHE A CA    1 
ATOM   1589 C  C     . PHE A 1 221 ? -21.446 38.006  -26.910 1.00 24.06  ? 201 PHE A C     1 
ATOM   1590 O  O     . PHE A 1 221 ? -20.767 38.775  -27.599 1.00 26.26  ? 201 PHE A O     1 
ATOM   1591 C  CB    . PHE A 1 221 ? -21.711 38.834  -24.562 1.00 21.31  ? 201 PHE A CB    1 
ATOM   1592 C  CG    . PHE A 1 221 ? -21.697 38.494  -23.096 1.00 20.58  ? 201 PHE A CG    1 
ATOM   1593 C  CD1   . PHE A 1 221 ? -22.741 37.778  -22.540 1.00 20.51  ? 201 PHE A CD1   1 
ATOM   1594 C  CD2   . PHE A 1 221 ? -20.620 38.844  -22.279 1.00 20.84  ? 201 PHE A CD2   1 
ATOM   1595 C  CE1   . PHE A 1 221 ? -22.752 37.453  -21.199 1.00 22.82  ? 201 PHE A CE1   1 
ATOM   1596 C  CE2   . PHE A 1 221 ? -20.627 38.524  -20.920 1.00 18.91  ? 201 PHE A CE2   1 
ATOM   1597 C  CZ    . PHE A 1 221 ? -21.689 37.814  -20.384 1.00 23.29  ? 201 PHE A CZ    1 
ATOM   1598 N  N     . PRO A 1 222 ? -22.500 37.371  -27.413 1.00 20.69  ? 202 PRO A N     1 
ATOM   1599 C  CA    . PRO A 1 222 ? -22.930 37.637  -28.791 1.00 22.63  ? 202 PRO A CA    1 
ATOM   1600 C  C     . PRO A 1 222 ? -23.326 39.094  -28.961 1.00 30.28  ? 202 PRO A C     1 
ATOM   1601 O  O     . PRO A 1 222 ? -23.807 39.739  -28.030 1.00 30.15  ? 202 PRO A O     1 
ATOM   1602 C  CB    . PRO A 1 222 ? -24.133 36.707  -28.975 1.00 26.64  ? 202 PRO A CB    1 
ATOM   1603 C  CG    . PRO A 1 222 ? -23.946 35.632  -27.981 1.00 24.03  ? 202 PRO A CG    1 
ATOM   1604 C  CD    . PRO A 1 222 ? -23.276 36.285  -26.791 1.00 21.64  ? 202 PRO A CD    1 
ATOM   1605 N  N     . GLU A 1 223 ? -23.127 39.620  -30.164 1.00 28.98  ? 203 GLU A N     1 
ATOM   1606 C  CA    . GLU A 1 223 ? -23.522 40.998  -30.408 1.00 38.47  ? 203 GLU A CA    1 
ATOM   1607 C  C     . GLU A 1 223 ? -24.135 41.102  -31.798 1.00 31.74  ? 203 GLU A C     1 
ATOM   1608 O  O     . GLU A 1 223 ? -23.805 40.324  -32.696 1.00 28.68  ? 203 GLU A O     1 
ATOM   1609 C  CB    . GLU A 1 223 ? -22.325 41.947  -30.220 1.00 42.65  ? 203 GLU A CB    1 
ATOM   1610 C  CG    . GLU A 1 223 ? -22.689 43.421  -30.287 1.00 58.62  ? 203 GLU A CG    1 
ATOM   1611 C  CD    . GLU A 1 223 ? -21.482 44.317  -30.421 1.00 69.04  ? 203 GLU A CD    1 
ATOM   1612 O  OE1   . GLU A 1 223 ? -20.399 43.806  -30.777 1.00 73.30  ? 203 GLU A OE1   1 
ATOM   1613 O  OE2   . GLU A 1 223 ? -21.616 45.533  -30.157 1.00 82.87  ? 203 GLU A OE2   1 
ATOM   1614 N  N     . GLU A 1 224 ? -25.072 42.039  -31.950 1.00 46.33  ? 204 GLU A N     1 
ATOM   1615 C  CA    . GLU A 1 224 ? -25.806 42.221  -33.197 1.00 45.95  ? 204 GLU A CA    1 
ATOM   1616 C  C     . GLU A 1 224 ? -25.114 43.246  -34.087 1.00 41.11  ? 204 GLU A C     1 
ATOM   1617 O  O     . GLU A 1 224 ? -24.543 44.229  -33.606 1.00 42.20  ? 204 GLU A O     1 
ATOM   1618 C  CB    . GLU A 1 224 ? -27.242 42.675  -32.926 1.00 51.91  ? 204 GLU A CB    1 
ATOM   1619 C  CG    . GLU A 1 224 ? -28.048 41.732  -32.056 1.00 51.82  ? 204 GLU A CG    1 
ATOM   1620 C  CD    . GLU A 1 224 ? -29.361 42.343  -31.608 1.00 77.33  ? 204 GLU A CD    1 
ATOM   1621 O  OE1   . GLU A 1 224 ? -30.059 42.939  -32.455 1.00 77.24  ? 204 GLU A OE1   1 
ATOM   1622 O  OE2   . GLU A 1 224 ? -29.686 42.240  -30.405 1.00 85.68  ? 204 GLU A OE2   1 
ATOM   1623 N  N     . ALA A 1 225 ? -25.188 43.012  -35.396 1.00 46.84  ? 205 ALA A N     1 
ATOM   1624 C  CA    . ALA A 1 225 ? -24.520 43.856  -36.389 1.00 54.26  ? 205 ALA A CA    1 
ATOM   1625 C  C     . ALA A 1 225 ? -24.939 45.321  -36.286 1.00 55.76  ? 205 ALA A C     1 
ATOM   1626 O  O     . ALA A 1 225 ? -26.121 45.629  -36.152 1.00 56.45  ? 205 ALA A O     1 
ATOM   1627 C  CB    . ALA A 1 225 ? -24.797 43.331  -37.795 1.00 56.05  ? 205 ALA A CB    1 
ATOM   1628 N  N     . CYS A 1 246 ? -2.065  51.528  -27.280 1.00 58.42  ? 226 CYS A N     1 
ATOM   1629 C  CA    . CYS A 1 246 ? -1.330  50.336  -27.692 1.00 55.88  ? 226 CYS A CA    1 
ATOM   1630 C  C     . CYS A 1 246 ? -2.229  49.111  -27.791 1.00 54.78  ? 226 CYS A C     1 
ATOM   1631 O  O     . CYS A 1 246 ? -2.897  48.734  -26.824 1.00 46.99  ? 226 CYS A O     1 
ATOM   1632 C  CB    . CYS A 1 246 ? -0.184  50.047  -26.718 1.00 61.99  ? 226 CYS A CB    1 
ATOM   1633 S  SG    . CYS A 1 246 ? 0.998   48.817  -27.320 1.00 53.02  ? 226 CYS A SG    1 
ATOM   1634 N  N     . ALA A 1 247 ? -2.244  48.487  -28.969 1.00 35.67  ? 227 ALA A N     1 
ATOM   1635 C  CA    . ALA A 1 247 ? -3.120  47.345  -29.181 1.00 38.43  ? 227 ALA A CA    1 
ATOM   1636 C  C     . ALA A 1 247 ? -2.527  46.054  -28.629 1.00 33.12  ? 227 ALA A C     1 
ATOM   1637 O  O     . ALA A 1 247 ? -3.278  45.128  -28.311 1.00 31.72  ? 227 ALA A O     1 
ATOM   1638 C  CB    . ALA A 1 247 ? -3.433  47.187  -30.669 1.00 45.74  ? 227 ALA A CB    1 
ATOM   1639 N  N     . THR A 1 248 ? -1.202  45.954  -28.537 1.00 26.85  ? 228 THR A N     1 
ATOM   1640 C  CA    . THR A 1 248 ? -0.579  44.737  -28.042 1.00 24.50  ? 228 THR A CA    1 
ATOM   1641 C  C     . THR A 1 248 ? -0.309  44.799  -26.543 1.00 24.53  ? 228 THR A C     1 
ATOM   1642 O  O     . THR A 1 248 ? -0.283  45.861  -25.920 1.00 26.55  ? 228 THR A O     1 
ATOM   1643 C  CB    . THR A 1 248 ? 0.743   44.457  -28.761 1.00 21.25  ? 228 THR A CB    1 
ATOM   1644 O  OG1   . THR A 1 248 ? 1.621   45.568  -28.575 1.00 27.60  ? 228 THR A OG1   1 
ATOM   1645 C  CG2   . THR A 1 248 ? 0.518   44.230  -30.236 1.00 24.81  ? 228 THR A CG2   1 
ATOM   1646 N  N     . HIS A 1 249 ? -0.070  43.627  -25.979 1.00 21.83  ? 229 HIS A N     1 
ATOM   1647 C  CA    . HIS A 1 249 ? 0.430   43.504  -24.624 1.00 23.26  ? 229 HIS A CA    1 
ATOM   1648 C  C     . HIS A 1 249 ? 1.462   42.393  -24.603 1.00 21.01  ? 229 HIS A C     1 
ATOM   1649 O  O     . HIS A 1 249 ? 1.597   41.609  -25.549 1.00 20.20  ? 229 HIS A O     1 
ATOM   1650 C  CB    . HIS A 1 249 ? -0.695  43.213  -23.622 1.00 22.36  ? 229 HIS A CB    1 
ATOM   1651 C  CG    . HIS A 1 249 ? -1.333  41.874  -23.816 1.00 21.15  ? 229 HIS A CG    1 
ATOM   1652 N  ND1   . HIS A 1 249 ? -2.380  41.680  -24.687 1.00 19.86  ? 229 HIS A ND1   1 
ATOM   1653 C  CD2   . HIS A 1 249 ? -1.058  40.660  -23.276 1.00 18.50  ? 229 HIS A CD2   1 
ATOM   1654 C  CE1   . HIS A 1 249 ? -2.729  40.405  -24.674 1.00 18.90  ? 229 HIS A CE1   1 
ATOM   1655 N  NE2   . HIS A 1 249 ? -1.961  39.769  -23.806 1.00 20.27  ? 229 HIS A NE2   1 
ATOM   1656 N  N     . LEU A 1 250 ? 2.180   42.340  -23.493 1.00 20.46  ? 230 LEU A N     1 
ATOM   1657 C  CA    . LEU A 1 250 ? 3.053   41.237  -23.146 1.00 19.55  ? 230 LEU A CA    1 
ATOM   1658 C  C     . LEU A 1 250 ? 2.428   40.535  -21.955 1.00 18.42  ? 230 LEU A C     1 
ATOM   1659 O  O     . LEU A 1 250 ? 1.928   41.197  -21.039 1.00 21.49  ? 230 LEU A O     1 
ATOM   1660 C  CB    . LEU A 1 250 ? 4.448   41.724  -22.745 1.00 22.35  ? 230 LEU A CB    1 
ATOM   1661 C  CG    . LEU A 1 250 ? 5.276   42.480  -23.780 1.00 27.03  ? 230 LEU A CG    1 
ATOM   1662 C  CD1   . LEU A 1 250 ? 6.553   43.024  -23.134 1.00 27.76  ? 230 LEU A CD1   1 
ATOM   1663 C  CD2   . LEU A 1 250 ? 5.589   41.544  -24.929 1.00 24.12  ? 230 LEU A CD2   1 
ATOM   1664 N  N     . ASP A 1 251 ? 2.454   39.206  -21.959 1.00 18.16  ? 231 ASP A N     1 
ATOM   1665 C  CA    . ASP A 1 251 ? 2.081   38.492  -20.743 1.00 17.98  ? 231 ASP A CA    1 
ATOM   1666 C  C     . ASP A 1 251 ? 3.183   38.694  -19.714 1.00 20.71  ? 231 ASP A C     1 
ATOM   1667 O  O     . ASP A 1 251 ? 4.368   38.750  -20.054 1.00 18.75  ? 231 ASP A O     1 
ATOM   1668 C  CB    . ASP A 1 251 ? 1.869   37.001  -21.001 1.00 17.56  ? 231 ASP A CB    1 
ATOM   1669 C  CG    . ASP A 1 251 ? 0.592   36.696  -21.776 1.00 17.43  ? 231 ASP A CG    1 
ATOM   1670 O  OD1   . ASP A 1 251 ? -0.078  37.625  -22.294 1.00 17.89  ? 231 ASP A OD1   1 
ATOM   1671 O  OD2   . ASP A 1 251 ? 0.263   35.498  -21.860 1.00 19.05  ? 231 ASP A OD2   1 
ATOM   1672 N  N     . HIS A 1 252 ? 2.802   38.811  -18.448 1.00 18.98  ? 232 HIS A N     1 
ATOM   1673 C  CA    A HIS A 1 252 ? 3.828   39.171  -17.484 0.48 17.28  ? 232 HIS A CA    1 
ATOM   1674 C  CA    B HIS A 1 252 ? 3.699   39.183  -17.363 0.52 17.27  ? 232 HIS A CA    1 
ATOM   1675 C  C     . HIS A 1 252 ? 4.382   37.986  -16.701 1.00 20.47  ? 232 HIS A C     1 
ATOM   1676 O  O     . HIS A 1 252 ? 5.430   38.146  -16.074 1.00 20.07  ? 232 HIS A O     1 
ATOM   1677 C  CB    A HIS A 1 252 ? 3.331   40.284  -16.535 0.48 22.98  ? 232 HIS A CB    1 
ATOM   1678 C  CB    B HIS A 1 252 ? 2.885   39.975  -16.331 0.52 23.33  ? 232 HIS A CB    1 
ATOM   1679 C  CG    A HIS A 1 252 ? 2.468   39.819  -15.404 0.48 23.04  ? 232 HIS A CG    1 
ATOM   1680 C  CG    B HIS A 1 252 ? 3.687   40.513  -15.193 0.52 18.95  ? 232 HIS A CG    1 
ATOM   1681 N  ND1   A HIS A 1 252 ? 1.106   40.031  -15.373 0.48 22.48  ? 232 HIS A ND1   1 
ATOM   1682 N  ND1   B HIS A 1 252 ? 4.488   41.629  -15.310 0.52 26.54  ? 232 HIS A ND1   1 
ATOM   1683 C  CD2   A HIS A 1 252 ? 2.783   39.228  -14.226 0.48 20.27  ? 232 HIS A CD2   1 
ATOM   1684 C  CD2   B HIS A 1 252 ? 3.789   40.107  -13.906 0.52 19.94  ? 232 HIS A CD2   1 
ATOM   1685 C  CE1   A HIS A 1 252 ? 0.614   39.554  -14.242 0.48 21.89  ? 232 HIS A CE1   1 
ATOM   1686 C  CE1   B HIS A 1 252 ? 5.061   41.879  -14.145 0.52 20.51  ? 232 HIS A CE1   1 
ATOM   1687 N  NE2   A HIS A 1 252 ? 1.610   39.056  -13.531 0.48 22.58  ? 232 HIS A NE2   1 
ATOM   1688 N  NE2   B HIS A 1 252 ? 4.661   40.964  -13.279 0.52 28.49  ? 232 HIS A NE2   1 
ATOM   1689 N  N     . GLY A 1 253 ? 3.796   36.798  -16.808 1.00 19.32  ? 233 GLY A N     1 
ATOM   1690 C  CA    . GLY A 1 253 ? 4.248   35.619  -16.085 1.00 18.42  ? 233 GLY A CA    1 
ATOM   1691 C  C     . GLY A 1 253 ? 5.344   34.844  -16.785 1.00 17.73  ? 233 GLY A C     1 
ATOM   1692 O  O     . GLY A 1 253 ? 6.174   35.408  -17.511 1.00 19.00  ? 233 GLY A O     1 
ATOM   1693 N  N     . CYS A 1 254 ? 5.340   33.521  -16.578 1.00 18.61  ? 234 CYS A N     1 
ATOM   1694 C  CA    . CYS A 1 254 ? 6.362   32.661  -17.176 1.00 17.71  ? 234 CYS A CA    1 
ATOM   1695 C  C     . CYS A 1 254 ? 5.867   32.030  -18.464 1.00 16.82  ? 234 CYS A C     1 
ATOM   1696 O  O     . CYS A 1 254 ? 6.398   32.323  -19.547 1.00 18.88  ? 234 CYS A O     1 
ATOM   1697 C  CB    . CYS A 1 254 ? 6.782   31.559  -16.213 1.00 17.36  ? 234 CYS A CB    1 
ATOM   1698 S  SG    . CYS A 1 254 ? 7.748   32.156  -14.800 1.00 21.71  ? 234 CYS A SG    1 
ATOM   1699 N  N     . LEU A 1 255 ? 4.854   31.163  -18.357 1.00 17.53  ? 235 LEU A N     1 
ATOM   1700 C  CA    . LEU A 1 255 ? 4.350   30.447  -19.528 1.00 16.40  ? 235 LEU A CA    1 
ATOM   1701 C  C     . LEU A 1 255 ? 2.837   30.441  -19.469 1.00 16.09  ? 235 LEU A C     1 
ATOM   1702 O  O     . LEU A 1 255 ? 2.268   29.998  -18.469 1.00 17.38  ? 235 LEU A O     1 
ATOM   1703 C  CB    . LEU A 1 255 ? 4.851   29.001  -19.592 1.00 16.50  ? 235 LEU A CB    1 
ATOM   1704 C  CG    . LEU A 1 255 ? 6.343   28.804  -19.859 1.00 17.80  ? 235 LEU A CG    1 
ATOM   1705 C  CD1   . LEU A 1 255 ? 6.767   27.404  -19.461 1.00 17.57  ? 235 LEU A CD1   1 
ATOM   1706 C  CD2   . LEU A 1 255 ? 6.624   29.038  -21.352 1.00 17.12  ? 235 LEU A CD2   1 
ATOM   1707 N  N     . THR A 1 256 ? 2.196   30.921  -20.525 1.00 15.96  ? 236 THR A N     1 
ATOM   1708 C  CA    . THR A 1 256 ? 0.736   30.976  -20.576 1.00 15.70  ? 236 THR A CA    1 
ATOM   1709 C  C     . THR A 1 256 ? 0.227   29.829  -21.440 1.00 16.64  ? 236 THR A C     1 
ATOM   1710 O  O     . THR A 1 256 ? 0.459   29.818  -22.653 1.00 17.52  ? 236 THR A O     1 
ATOM   1711 C  CB    . THR A 1 256 ? 0.273   32.314  -21.137 1.00 15.71  ? 236 THR A CB    1 
ATOM   1712 O  OG1   . THR A 1 256 ? 0.822   33.384  -20.349 1.00 16.15  ? 236 THR A OG1   1 
ATOM   1713 C  CG2   . THR A 1 256 ? -1.266  32.379  -21.153 1.00 15.50  ? 236 THR A CG2   1 
ATOM   1714 N  N     . GLY A 1 257 ? -0.476  28.881  -20.810 1.00 15.43  ? 237 GLY A N     1 
ATOM   1715 C  CA    . GLY A 1 257 ? -1.132  27.803  -21.552 1.00 15.62  ? 237 GLY A CA    1 
ATOM   1716 C  C     . GLY A 1 257 ? -2.454  28.269  -22.144 1.00 16.39  ? 237 GLY A C     1 
ATOM   1717 O  O     . GLY A 1 257 ? -3.220  29.003  -21.516 1.00 17.11  ? 237 GLY A O     1 
ATOM   1718 N  N     . LEU A 1 258 ? -2.719  27.836  -23.373 1.00 15.32  ? 238 LEU A N     1 
ATOM   1719 C  CA    . LEU A 1 258 ? -3.869  28.330  -24.124 1.00 15.29  ? 238 LEU A CA    1 
ATOM   1720 C  C     . LEU A 1 258 ? -4.604  27.175  -24.765 1.00 19.59  ? 238 LEU A C     1 
ATOM   1721 O  O     . LEU A 1 258 ? -3.974  26.292  -25.365 1.00 18.22  ? 238 LEU A O     1 
ATOM   1722 C  CB    . LEU A 1 258 ? -3.449  29.285  -25.245 1.00 17.08  ? 238 LEU A CB    1 
ATOM   1723 C  CG    . LEU A 1 258 ? -2.592  30.498  -24.876 1.00 19.97  ? 238 LEU A CG    1 
ATOM   1724 C  CD1   . LEU A 1 258 ? -2.034  31.143  -26.146 1.00 25.56  ? 238 LEU A CD1   1 
ATOM   1725 C  CD2   . LEU A 1 258 ? -3.407  31.499  -24.066 1.00 18.81  ? 238 LEU A CD2   1 
ATOM   1726 N  N     . THR A 1 259 ? -5.937  27.250  -24.725 1.00 19.50  ? 239 THR A N     1 
ATOM   1727 C  CA    . THR A 1 259 ? -6.743  26.406  -25.605 1.00 20.96  ? 239 THR A CA    1 
ATOM   1728 C  C     . THR A 1 259 ? -7.106  27.177  -26.870 1.00 18.45  ? 239 THR A C     1 
ATOM   1729 O  O     . THR A 1 259 ? -7.080  28.410  -26.902 1.00 17.86  ? 239 THR A O     1 
ATOM   1730 C  CB    . THR A 1 259 ? -8.055  25.949  -24.930 1.00 18.80  ? 239 THR A CB    1 
ATOM   1731 O  OG1   . THR A 1 259 ? -8.936  27.074  -24.749 1.00 20.42  ? 239 THR A OG1   1 
ATOM   1732 C  CG2   . THR A 1 259 ? -7.810  25.288  -23.599 1.00 20.24  ? 239 THR A CG2   1 
ATOM   1733 N  N     . SER A 1 260 ? -7.467  26.434  -27.921 1.00 18.01  ? 240 SER A N     1 
ATOM   1734 C  CA    . SER A 1 260 ? -8.138  27.069  -29.048 1.00 19.05  ? 240 SER A CA    1 
ATOM   1735 C  C     . SER A 1 260 ? -9.530  27.527  -28.618 1.00 16.70  ? 240 SER A C     1 
ATOM   1736 O  O     . SER A 1 260 ? -10.121 26.989  -27.678 1.00 20.89  ? 240 SER A O     1 
ATOM   1737 C  CB    . SER A 1 260 ? -8.279  26.119  -30.240 1.00 22.00  ? 240 SER A CB    1 
ATOM   1738 O  OG    . SER A 1 260 ? -9.247  25.120  -29.946 1.00 24.88  ? 240 SER A OG    1 
ATOM   1739 N  N     . ALA A 1 261 ? -10.043 28.536  -29.308 1.00 17.01  ? 241 ALA A N     1 
ATOM   1740 C  CA    . ALA A 1 261 ? -11.345 29.091  -28.934 1.00 17.24  ? 241 ALA A CA    1 
ATOM   1741 C  C     . ALA A 1 261 ? -12.500 28.187  -29.357 1.00 20.29  ? 241 ALA A C     1 
ATOM   1742 O  O     . ALA A 1 261 ? -12.450 27.521  -30.393 1.00 17.72  ? 241 ALA A O     1 
ATOM   1743 C  CB    . ALA A 1 261 ? -11.527 30.471  -29.562 1.00 20.84  ? 241 ALA A CB    1 
ATOM   1744 N  N     . MET A 1 262 ? -13.579 28.221  -28.564 1.00 17.17  ? 242 MET A N     1 
ATOM   1745 C  CA    . MET A 1 262 ? -14.832 27.530  -28.873 1.00 15.76  ? 242 MET A CA    1 
ATOM   1746 C  C     . MET A 1 262 ? -15.877 28.582  -29.227 1.00 19.79  ? 242 MET A C     1 
ATOM   1747 O  O     . MET A 1 262 ? -16.207 29.431  -28.398 1.00 20.19  ? 242 MET A O     1 
ATOM   1748 C  CB    . MET A 1 262 ? -15.321 26.694  -27.687 1.00 17.68  ? 242 MET A CB    1 
ATOM   1749 C  CG    . MET A 1 262 ? -16.719 26.082  -27.900 1.00 18.40  ? 242 MET A CG    1 
ATOM   1750 S  SD    . MET A 1 262 ? -17.431 25.525  -26.336 1.00 22.77  ? 242 MET A SD    1 
ATOM   1751 C  CE    . MET A 1 262 ? -18.857 24.567  -26.900 1.00 21.94  ? 242 MET A CE    1 
ATOM   1752 N  N     . PHE A 1 263 ? -16.435 28.500  -30.428 1.00 16.43  ? 243 PHE A N     1 
ATOM   1753 C  CA    . PHE A 1 263 ? -17.581 29.335  -30.779 1.00 16.18  ? 243 PHE A CA    1 
ATOM   1754 C  C     . PHE A 1 263 ? -18.851 28.536  -30.562 1.00 18.12  ? 243 PHE A C     1 
ATOM   1755 O  O     . PHE A 1 263 ? -18.895 27.335  -30.837 1.00 17.42  ? 243 PHE A O     1 
ATOM   1756 C  CB    . PHE A 1 263 ? -17.520 29.827  -32.228 1.00 17.19  ? 243 PHE A CB    1 
ATOM   1757 C  CG    . PHE A 1 263 ? -16.453 30.855  -32.474 1.00 16.72  ? 243 PHE A CG    1 
ATOM   1758 C  CD1   . PHE A 1 263 ? -16.708 32.212  -32.298 1.00 17.33  ? 243 PHE A CD1   1 
ATOM   1759 C  CD2   . PHE A 1 263 ? -15.188 30.457  -32.859 1.00 19.49  ? 243 PHE A CD2   1 
ATOM   1760 C  CE1   . PHE A 1 263 ? -15.729 33.156  -32.527 1.00 19.15  ? 243 PHE A CE1   1 
ATOM   1761 C  CE2   . PHE A 1 263 ? -14.196 31.405  -33.089 1.00 19.81  ? 243 PHE A CE2   1 
ATOM   1762 C  CZ    . PHE A 1 263 ? -14.464 32.749  -32.924 1.00 23.01  ? 243 PHE A CZ    1 
ATOM   1763 N  N     . VAL A 1 264 ? -19.859 29.203  -30.007 1.00 18.85  ? 244 VAL A N     1 
ATOM   1764 C  CA    . VAL A 1 264 ? -21.128 28.575  -29.643 1.00 19.38  ? 244 VAL A CA    1 
ATOM   1765 C  C     . VAL A 1 264 ? -22.271 29.398  -30.215 1.00 15.83  ? 244 VAL A C     1 
ATOM   1766 O  O     . VAL A 1 264 ? -22.325 30.614  -30.012 1.00 19.04  ? 244 VAL A O     1 
ATOM   1767 C  CB    . VAL A 1 264 ? -21.297 28.461  -28.113 1.00 18.82  ? 244 VAL A CB    1 
ATOM   1768 C  CG1   . VAL A 1 264 ? -22.603 27.702  -27.787 1.00 18.04  ? 244 VAL A CG1   1 
ATOM   1769 C  CG2   . VAL A 1 264 ? -20.116 27.768  -27.486 1.00 23.13  ? 244 VAL A CG2   1 
ATOM   1770 N  N     . ASP A 1 265 ? -23.206 28.734  -30.904 1.00 17.71  ? 245 ASP A N     1 
ATOM   1771 C  CA    . ASP A 1 265 ? -24.457 29.376  -31.309 1.00 19.82  ? 245 ASP A CA    1 
ATOM   1772 C  C     . ASP A 1 265 ? -25.421 29.209  -30.145 1.00 20.31  ? 245 ASP A C     1 
ATOM   1773 O  O     . ASP A 1 265 ? -25.992 28.136  -29.949 1.00 19.48  ? 245 ASP A O     1 
ATOM   1774 C  CB    . ASP A 1 265 ? -24.984 28.759  -32.600 1.00 18.91  ? 245 ASP A CB    1 
ATOM   1775 C  CG    . ASP A 1 265 ? -26.303 29.370  -33.063 1.00 21.49  ? 245 ASP A CG    1 
ATOM   1776 O  OD1   . ASP A 1 265 ? -26.961 30.096  -32.291 1.00 21.92  ? 245 ASP A OD1   1 
ATOM   1777 O  OD2   . ASP A 1 265 ? -26.658 29.133  -34.237 1.00 27.86  ? 245 ASP A OD2   1 
ATOM   1778 N  N     . GLU A 1 266 ? -25.560 30.266  -29.342 1.00 20.70  ? 246 GLU A N     1 
ATOM   1779 C  CA    . GLU A 1 266 ? -26.332 30.188  -28.108 1.00 18.48  ? 246 GLU A CA    1 
ATOM   1780 C  C     . GLU A 1 266 ? -27.826 30.282  -28.348 1.00 20.68  ? 246 GLU A C     1 
ATOM   1781 O  O     . GLU A 1 266 ? -28.593 30.088  -27.402 1.00 23.62  ? 246 GLU A O     1 
ATOM   1782 C  CB    . GLU A 1 266 ? -25.887 31.278  -27.128 1.00 18.58  ? 246 GLU A CB    1 
ATOM   1783 C  CG    . GLU A 1 266 ? -24.471 30.996  -26.602 1.00 17.25  ? 246 GLU A CG    1 
ATOM   1784 C  CD    . GLU A 1 266 ? -23.959 32.004  -25.588 1.00 18.00  ? 246 GLU A CD    1 
ATOM   1785 O  OE1   . GLU A 1 266 ? -24.495 33.120  -25.504 1.00 20.35  ? 246 GLU A OE1   1 
ATOM   1786 O  OE2   . GLU A 1 266 ? -22.970 31.665  -24.879 1.00 19.05  ? 246 GLU A OE2   1 
ATOM   1787 N  N     . ALA A 1 267 ? -28.249 30.597  -29.575 1.00 22.11  ? 247 ALA A N     1 
ATOM   1788 C  CA    . ALA A 1 267 ? -29.655 30.396  -29.922 1.00 23.08  ? 247 ALA A CA    1 
ATOM   1789 C  C     . ALA A 1 267 ? -29.950 28.923  -30.195 1.00 25.17  ? 247 ALA A C     1 
ATOM   1790 O  O     . ALA A 1 267 ? -30.978 28.399  -29.741 1.00 27.90  ? 247 ALA A O     1 
ATOM   1791 C  CB    . ALA A 1 267 ? -30.024 31.263  -31.129 1.00 25.02  ? 247 ALA A CB    1 
ATOM   1792 N  N     . ALA A 1 268 ? -29.059 28.243  -30.923 1.00 22.10  ? 248 ALA A N     1 
ATOM   1793 C  CA    . ALA A 1 268 ? -29.237 26.827  -31.245 1.00 24.36  ? 248 ALA A CA    1 
ATOM   1794 C  C     . ALA A 1 268 ? -29.057 25.936  -30.018 1.00 28.40  ? 248 ALA A C     1 
ATOM   1795 O  O     . ALA A 1 268 ? -29.812 24.975  -29.832 1.00 26.65  ? 248 ALA A O     1 
ATOM   1796 C  CB    . ALA A 1 268 ? -28.275 26.422  -32.364 1.00 28.50  ? 248 ALA A CB    1 
ATOM   1797 N  N     . THR A 1 269 ? -28.060 26.222  -29.173 1.00 22.08  ? 249 THR A N     1 
ATOM   1798 C  CA    . THR A 1 269 ? -27.822 25.465  -27.940 1.00 24.04  ? 249 THR A CA    1 
ATOM   1799 C  C     . THR A 1 269 ? -27.801 26.469  -26.791 1.00 24.25  ? 249 THR A C     1 
ATOM   1800 O  O     . THR A 1 269 ? -26.743 27.022  -26.454 1.00 19.90  ? 249 THR A O     1 
ATOM   1801 C  CB    . THR A 1 269 ? -26.526 24.647  -28.002 1.00 21.82  ? 249 THR A CB    1 
ATOM   1802 O  OG1   . THR A 1 269 ? -25.390 25.515  -28.153 1.00 21.93  ? 249 THR A OG1   1 
ATOM   1803 C  CG2   . THR A 1 269 ? -26.549 23.664  -29.182 1.00 20.14  ? 249 THR A CG2   1 
ATOM   1804 N  N     . PRO A 1 270 ? -28.954 26.751  -26.185 1.00 19.94  ? 250 PRO A N     1 
ATOM   1805 C  CA    . PRO A 1 270 ? -29.042 27.828  -25.181 1.00 17.21  ? 250 PRO A CA    1 
ATOM   1806 C  C     . PRO A 1 270 ? -28.146 27.561  -23.987 1.00 20.89  ? 250 PRO A C     1 
ATOM   1807 O  O     . PRO A 1 270 ? -28.081 26.428  -23.490 1.00 20.87  ? 250 PRO A O     1 
ATOM   1808 C  CB    . PRO A 1 270 ? -30.527 27.817  -24.776 1.00 23.47  ? 250 PRO A CB    1 
ATOM   1809 C  CG    . PRO A 1 270 ? -31.218 27.210  -25.934 1.00 26.01  ? 250 PRO A CG    1 
ATOM   1810 C  CD    . PRO A 1 270 ? -30.280 26.197  -26.515 1.00 25.50  ? 250 PRO A CD    1 
ATOM   1811 N  N     . PRO A 1 271 ? -27.444 28.585  -23.503 1.00 19.85  ? 251 PRO A N     1 
ATOM   1812 C  CA    . PRO A 1 271 ? -26.509 28.430  -22.373 1.00 23.13  ? 251 PRO A CA    1 
ATOM   1813 C  C     . PRO A 1 271 ? -27.224 28.467  -21.027 1.00 22.76  ? 251 PRO A C     1 
ATOM   1814 O  O     . PRO A 1 271 ? -27.003 29.350  -20.191 1.00 21.27  ? 251 PRO A O     1 
ATOM   1815 C  CB    . PRO A 1 271 ? -25.558 29.618  -22.578 1.00 24.85  ? 251 PRO A CB    1 
ATOM   1816 C  CG    . PRO A 1 271 ? -26.418 30.679  -23.190 1.00 23.37  ? 251 PRO A CG    1 
ATOM   1817 C  CD    . PRO A 1 271 ? -27.410 29.945  -24.072 1.00 21.54  ? 251 PRO A CD    1 
ATOM   1818 N  N     . VAL A 1 272 ? -28.121 27.503  -20.837 1.00 19.59  ? 252 VAL A N     1 
ATOM   1819 C  CA    . VAL A 1 272 ? -29.047 27.450  -19.713 1.00 21.96  ? 252 VAL A CA    1 
ATOM   1820 C  C     . VAL A 1 272 ? -28.867 26.103  -19.027 1.00 20.81  ? 252 VAL A C     1 
ATOM   1821 O  O     . VAL A 1 272 ? -28.933 25.057  -19.683 1.00 26.20  ? 252 VAL A O     1 
ATOM   1822 C  CB    . VAL A 1 272 ? -30.496 27.656  -20.197 1.00 25.10  ? 252 VAL A CB    1 
ATOM   1823 C  CG1   . VAL A 1 272 ? -31.505 27.314  -19.105 1.00 24.58  ? 252 VAL A CG1   1 
ATOM   1824 C  CG2   . VAL A 1 272 ? -30.677 29.086  -20.642 1.00 21.03  ? 252 VAL A CG2   1 
ATOM   1825 N  N     . VAL A 1 273 ? -28.655 26.136  -17.714 1.00 21.41  ? 253 VAL A N     1 
ATOM   1826 C  CA    . VAL A 1 273 ? -28.454 24.942  -16.899 1.00 25.80  ? 253 VAL A CA    1 
ATOM   1827 C  C     . VAL A 1 273 ? -29.798 24.255  -16.679 1.00 29.35  ? 253 VAL A C     1 
ATOM   1828 O  O     . VAL A 1 273 ? -30.657 24.765  -15.959 1.00 28.67  ? 253 VAL A O     1 
ATOM   1829 C  CB    . VAL A 1 273 ? -27.784 25.281  -15.568 1.00 27.69  ? 253 VAL A CB    1 
ATOM   1830 C  CG1   . VAL A 1 273 ? -27.669 24.030  -14.703 1.00 32.59  ? 253 VAL A CG1   1 
ATOM   1831 C  CG2   . VAL A 1 273 ? -26.415 25.896  -15.824 1.00 30.16  ? 253 VAL A CG2   1 
ATOM   1832 N  N     . ASN A 1 274 ? -29.990 23.114  -17.330 1.00 32.15  ? 254 ASN A N     1 
ATOM   1833 C  CA    . ASN A 1 274 ? -31.239 22.383  -17.235 1.00 44.45  ? 254 ASN A CA    1 
ATOM   1834 C  C     . ASN A 1 274 ? -31.005 20.889  -17.039 1.00 48.06  ? 254 ASN A C     1 
ATOM   1835 O  O     . ASN A 1 274 ? -29.951 20.363  -17.389 1.00 58.33  ? 254 ASN A O     1 
ATOM   1836 C  CB    . ASN A 1 274 ? -32.066 22.630  -18.491 1.00 39.13  ? 254 ASN A CB    1 
ATOM   1837 C  CG    . ASN A 1 274 ? -33.423 21.978  -18.433 1.00 36.78  ? 254 ASN A CG    1 
ATOM   1838 O  OD1   . ASN A 1 274 ? -34.016 21.818  -17.361 1.00 38.58  ? 254 ASN A OD1   1 
ATOM   1839 N  ND2   . ASN A 1 274 ? -33.927 21.588  -19.598 1.00 36.31  ? 254 ASN A ND2   1 
ATOM   1840 N  N     . GLY A 1 279 ? -28.667 13.755  -13.195 1.00 55.16  ? 259 GLY A N     1 
ATOM   1841 C  CA    . GLY A 1 279 ? -28.100 13.888  -14.525 1.00 62.83  ? 259 GLY A CA    1 
ATOM   1842 C  C     . GLY A 1 279 ? -26.913 14.835  -14.598 1.00 64.38  ? 259 GLY A C     1 
ATOM   1843 O  O     . GLY A 1 279 ? -26.821 15.796  -13.835 1.00 59.76  ? 259 GLY A O     1 
ATOM   1844 N  N     . SER A 1 280 ? -26.007 14.564  -15.532 1.00 68.61  ? 260 SER A N     1 
ATOM   1845 C  CA    . SER A 1 280 ? -24.835 15.401  -15.735 1.00 83.66  ? 260 SER A CA    1 
ATOM   1846 C  C     . SER A 1 280 ? -25.178 16.583  -16.642 1.00 72.08  ? 260 SER A C     1 
ATOM   1847 O  O     . SER A 1 280 ? -26.209 16.607  -17.320 1.00 70.16  ? 260 SER A O     1 
ATOM   1848 C  CB    . SER A 1 280 ? -23.679 14.586  -16.314 1.00 82.34  ? 260 SER A CB    1 
ATOM   1849 O  OG    . SER A 1 280 ? -24.058 13.932  -17.511 1.00 87.05  ? 260 SER A OG    1 
ATOM   1850 N  N     . LEU A 1 281 ? -24.279 17.569  -16.662 1.00 56.05  ? 261 LEU A N     1 
ATOM   1851 C  CA    . LEU A 1 281 ? -24.498 18.794  -17.420 1.00 53.07  ? 261 LEU A CA    1 
ATOM   1852 C  C     . LEU A 1 281 ? -23.884 18.655  -18.802 1.00 41.91  ? 261 LEU A C     1 
ATOM   1853 O  O     . LEU A 1 281 ? -22.651 18.601  -18.917 1.00 48.18  ? 261 LEU A O     1 
ATOM   1854 C  CB    . LEU A 1 281 ? -23.884 19.986  -16.703 1.00 39.01  ? 261 LEU A CB    1 
ATOM   1855 C  CG    . LEU A 1 281 ? -24.147 21.345  -17.353 1.00 29.84  ? 261 LEU A CG    1 
ATOM   1856 C  CD1   . LEU A 1 281 ? -25.634 21.572  -17.572 1.00 37.19  ? 261 LEU A CD1   1 
ATOM   1857 C  CD2   . LEU A 1 281 ? -23.561 22.454  -16.505 1.00 32.98  ? 261 LEU A CD2   1 
ATOM   1858 N  N     . PRO A 1 282 ? -24.679 18.620  -19.870 1.00 37.75  ? 262 PRO A N     1 
ATOM   1859 C  CA    . PRO A 1 282 ? -24.104 18.357  -21.182 1.00 36.00  ? 262 PRO A CA    1 
ATOM   1860 C  C     . PRO A 1 282 ? -23.341 19.557  -21.686 1.00 39.67  ? 262 PRO A C     1 
ATOM   1861 O  O     . PRO A 1 282 ? -23.642 20.712  -21.325 1.00 30.56  ? 262 PRO A O     1 
ATOM   1862 C  CB    . PRO A 1 282 ? -25.340 18.071  -22.053 1.00 30.82  ? 262 PRO A CB    1 
ATOM   1863 C  CG    . PRO A 1 282 ? -26.432 18.845  -21.402 1.00 49.09  ? 262 PRO A CG    1 
ATOM   1864 C  CD    . PRO A 1 282 ? -26.142 18.786  -19.922 1.00 40.35  ? 262 PRO A CD    1 
ATOM   1865 N  N     . PRO A 1 283 ? -22.310 19.351  -22.499 1.00 33.14  ? 263 PRO A N     1 
ATOM   1866 C  CA    . PRO A 1 283 ? -21.654 20.470  -23.171 1.00 29.01  ? 263 PRO A CA    1 
ATOM   1867 C  C     . PRO A 1 283 ? -22.565 21.084  -24.222 1.00 29.18  ? 263 PRO A C     1 
ATOM   1868 O  O     . PRO A 1 283 ? -23.532 20.482  -24.690 1.00 31.17  ? 263 PRO A O     1 
ATOM   1869 C  CB    . PRO A 1 283 ? -20.419 19.834  -23.816 1.00 33.98  ? 263 PRO A CB    1 
ATOM   1870 C  CG    . PRO A 1 283 ? -20.774 18.392  -23.973 1.00 38.55  ? 263 PRO A CG    1 
ATOM   1871 C  CD    . PRO A 1 283 ? -21.658 18.062  -22.797 1.00 41.17  ? 263 PRO A CD    1 
ATOM   1872 N  N     . LEU A 1 284 ? -22.252 22.324  -24.561 1.00 25.36  ? 264 LEU A N     1 
ATOM   1873 C  CA    . LEU A 1 284 ? -22.948 23.076  -25.588 1.00 18.87  ? 264 LEU A CA    1 
ATOM   1874 C  C     . LEU A 1 284 ? -22.336 22.785  -26.959 1.00 21.43  ? 264 LEU A C     1 
ATOM   1875 O  O     . LEU A 1 284 ? -21.275 22.171  -27.081 1.00 22.11  ? 264 LEU A O     1 
ATOM   1876 C  CB    . LEU A 1 284 ? -22.916 24.567  -25.257 1.00 18.98  ? 264 LEU A CB    1 
ATOM   1877 C  CG    . LEU A 1 284 ? -23.605 24.868  -23.928 1.00 18.73  ? 264 LEU A CG    1 
ATOM   1878 C  CD1   . LEU A 1 284 ? -23.279 26.281  -23.512 1.00 21.90  ? 264 LEU A CD1   1 
ATOM   1879 C  CD2   . LEU A 1 284 ? -25.126 24.644  -24.071 1.00 19.52  ? 264 LEU A CD2   1 
ATOM   1880 N  N     . GLY A 1 285 ? -23.061 23.165  -28.010 1.00 21.82  ? 265 GLY A N     1 
ATOM   1881 C  CA    . GLY A 1 285 ? -22.613 22.882  -29.356 1.00 24.88  ? 265 GLY A CA    1 
ATOM   1882 C  C     . GLY A 1 285 ? -21.477 23.764  -29.828 1.00 17.20  ? 265 GLY A C     1 
ATOM   1883 O  O     . GLY A 1 285 ? -21.647 24.984  -29.939 1.00 24.80  ? 265 GLY A O     1 
ATOM   1884 N  N     . GLU A 1 286 ? -20.335 23.169  -30.165 1.00 19.38  ? 266 GLU A N     1 
ATOM   1885 C  CA    . GLU A 1 286 ? -19.228 23.943  -30.705 1.00 19.87  ? 266 GLU A CA    1 
ATOM   1886 C  C     . GLU A 1 286 ? -19.398 24.068  -32.212 1.00 19.51  ? 266 GLU A C     1 
ATOM   1887 O  O     . GLU A 1 286 ? -19.593 23.061  -32.898 1.00 22.51  ? 266 GLU A O     1 
ATOM   1888 C  CB    . GLU A 1 286 ? -17.880 23.288  -30.398 1.00 22.45  ? 266 GLU A CB    1 
ATOM   1889 C  CG    . GLU A 1 286 ? -16.749 24.088  -31.034 1.00 17.72  ? 266 GLU A CG    1 
ATOM   1890 C  CD    . GLU A 1 286 ? -15.373 23.817  -30.442 1.00 20.74  ? 266 GLU A CD    1 
ATOM   1891 O  OE1   . GLU A 1 286 ? -15.217 22.833  -29.688 1.00 23.82  ? 266 GLU A OE1   1 
ATOM   1892 O  OE2   . GLU A 1 286 ? -14.475 24.648  -30.709 1.00 19.73  ? 266 GLU A OE2   1 
ATOM   1893 N  N     . LEU A 1 287 ? -19.284 25.285  -32.729 1.00 18.55  ? 267 LEU A N     1 
ATOM   1894 C  CA    . LEU A 1 287 ? -19.305 25.455  -34.184 1.00 18.15  ? 267 LEU A CA    1 
ATOM   1895 C  C     . LEU A 1 287 ? -18.025 24.868  -34.763 1.00 20.08  ? 267 LEU A C     1 
ATOM   1896 O  O     . LEU A 1 287 ? -16.928 25.204  -34.294 1.00 19.12  ? 267 LEU A O     1 
ATOM   1897 C  CB    . LEU A 1 287 ? -19.404 26.918  -34.586 1.00 19.47  ? 267 LEU A CB    1 
ATOM   1898 C  CG    . LEU A 1 287 ? -20.606 27.709  -34.095 1.00 26.22  ? 267 LEU A CG    1 
ATOM   1899 C  CD1   . LEU A 1 287 ? -20.584 29.062  -34.773 1.00 29.97  ? 267 LEU A CD1   1 
ATOM   1900 C  CD2   . LEU A 1 287 ? -21.902 26.962  -34.372 1.00 31.69  ? 267 LEU A CD2   1 
ATOM   1901 N  N     . PRO A 1 288 ? -18.116 24.048  -35.809 1.00 20.69  ? 268 PRO A N     1 
ATOM   1902 C  CA    . PRO A 1 288 ? -16.901 23.433  -36.374 1.00 23.57  ? 268 PRO A CA    1 
ATOM   1903 C  C     . PRO A 1 288 ? -15.866 24.439  -36.834 1.00 18.49  ? 268 PRO A C     1 
ATOM   1904 O  O     . PRO A 1 288 ? -14.662 24.211  -36.654 1.00 20.52  ? 268 PRO A O     1 
ATOM   1905 C  CB    . PRO A 1 288 ? -17.453 22.616  -37.556 1.00 22.26  ? 268 PRO A CB    1 
ATOM   1906 C  CG    . PRO A 1 288 ? -18.865 22.272  -37.130 1.00 22.19  ? 268 PRO A CG    1 
ATOM   1907 C  CD    . PRO A 1 288 ? -19.359 23.488  -36.377 1.00 24.96  ? 268 PRO A CD    1 
ATOM   1908 N  N     . THR A 1 289 ? -16.306 25.562  -37.393 1.00 19.54  ? 269 THR A N     1 
ATOM   1909 C  CA    . THR A 1 289 ? -15.446 26.560  -38.005 1.00 21.40  ? 269 THR A CA    1 
ATOM   1910 C  C     . THR A 1 289 ? -15.799 27.927  -37.442 1.00 19.25  ? 269 THR A C     1 
ATOM   1911 O  O     . THR A 1 289 ? -16.972 28.230  -37.213 1.00 21.55  ? 269 THR A O     1 
ATOM   1912 C  CB    . THR A 1 289 ? -15.647 26.543  -39.540 1.00 32.75  ? 269 THR A CB    1 
ATOM   1913 O  OG1   . THR A 1 289 ? -15.322 25.240  -40.051 1.00 31.95  ? 269 THR A OG1   1 
ATOM   1914 C  CG2   . THR A 1 289 ? -14.800 27.584  -40.227 1.00 31.72  ? 269 THR A CG2   1 
ATOM   1915 N  N     . SER A 1 290 ? -14.785 28.766  -37.245 1.00 21.56  ? 270 SER A N     1 
ATOM   1916 C  CA    . SER A 1 290 ? -15.031 30.114  -36.764 1.00 20.17  ? 270 SER A CA    1 
ATOM   1917 C  C     . SER A 1 290 ? -15.945 30.872  -37.723 1.00 21.67  ? 270 SER A C     1 
ATOM   1918 O  O     . SER A 1 290 ? -15.772 30.780  -38.945 1.00 22.72  ? 270 SER A O     1 
ATOM   1919 C  CB    . SER A 1 290 ? -13.714 30.871  -36.602 1.00 20.09  ? 270 SER A CB    1 
ATOM   1920 O  OG    . SER A 1 290 ? -13.982 32.247  -36.470 1.00 21.20  ? 270 SER A OG    1 
ATOM   1921 N  N     . PRO A 1 291 ? -16.903 31.653  -37.210 1.00 20.44  ? 271 PRO A N     1 
ATOM   1922 C  CA    . PRO A 1 291 ? -17.733 32.490  -38.094 1.00 21.46  ? 271 PRO A CA    1 
ATOM   1923 C  C     . PRO A 1 291 ? -17.016 33.711  -38.645 1.00 23.02  ? 271 PRO A C     1 
ATOM   1924 O  O     . PRO A 1 291 ? -17.556 34.359  -39.550 1.00 24.91  ? 271 PRO A O     1 
ATOM   1925 C  CB    . PRO A 1 291 ? -18.887 32.926  -37.179 1.00 25.53  ? 271 PRO A CB    1 
ATOM   1926 C  CG    . PRO A 1 291 ? -18.208 33.011  -35.816 1.00 21.39  ? 271 PRO A CG    1 
ATOM   1927 C  CD    . PRO A 1 291 ? -17.246 31.846  -35.783 1.00 24.85  ? 271 PRO A CD    1 
ATOM   1928 N  N     . ASP A 1 292 ? -15.838 34.062  -38.128 1.00 22.37  ? 272 ASP A N     1 
ATOM   1929 C  CA    . ASP A 1 292 ? -15.127 35.267  -38.556 1.00 21.25  ? 272 ASP A CA    1 
ATOM   1930 C  C     . ASP A 1 292 ? -13.654 34.912  -38.680 1.00 25.40  ? 272 ASP A C     1 
ATOM   1931 O  O     . ASP A 1 292 ? -12.947 34.811  -37.665 1.00 21.68  ? 272 ASP A O     1 
ATOM   1932 C  CB    . ASP A 1 292 ? -15.320 36.428  -37.581 1.00 20.68  ? 272 ASP A CB    1 
ATOM   1933 C  CG    . ASP A 1 292 ? -14.621 37.713  -38.034 1.00 26.61  ? 272 ASP A CG    1 
ATOM   1934 O  OD1   . ASP A 1 292 ? -13.896 37.699  -39.055 1.00 23.94  ? 272 ASP A OD1   1 
ATOM   1935 O  OD2   . ASP A 1 292 ? -14.819 38.760  -37.378 1.00 23.40  ? 272 ASP A OD2   1 
ATOM   1936 N  N     . PRO A 1 293 ? -13.146 34.756  -39.899 1.00 21.74  ? 273 PRO A N     1 
ATOM   1937 C  CA    . PRO A 1 293 ? -11.736 34.362  -40.048 1.00 25.91  ? 273 PRO A CA    1 
ATOM   1938 C  C     . PRO A 1 293 ? -10.747 35.383  -39.511 1.00 26.85  ? 273 PRO A C     1 
ATOM   1939 O  O     . PRO A 1 293 ? -9.578  35.031  -39.324 1.00 25.17  ? 273 PRO A O     1 
ATOM   1940 C  CB    . PRO A 1 293 ? -11.584 34.157  -41.564 1.00 24.42  ? 273 PRO A CB    1 
ATOM   1941 C  CG    . PRO A 1 293 ? -12.691 34.958  -42.175 1.00 31.53  ? 273 PRO A CG    1 
ATOM   1942 C  CD    . PRO A 1 293 ? -13.836 34.848  -41.195 1.00 27.01  ? 273 PRO A CD    1 
ATOM   1943 N  N     . LYS A 1 294 ? -11.160 36.629  -39.270 1.00 21.43  ? 274 LYS A N     1 
ATOM   1944 C  CA    . LYS A 1 294 ? -10.277 37.626  -38.676 1.00 20.39  ? 274 LYS A CA    1 
ATOM   1945 C  C     . LYS A 1 294 ? -10.216 37.546  -37.158 1.00 23.24  ? 274 LYS A C     1 
ATOM   1946 O  O     . LYS A 1 294 ? -9.362  38.207  -36.561 1.00 21.93  ? 274 LYS A O     1 
ATOM   1947 C  CB    . LYS A 1 294 ? -10.702 39.047  -39.057 1.00 21.70  ? 274 LYS A CB    1 
ATOM   1948 C  CG    . LYS A 1 294 ? -10.319 39.464  -40.459 1.00 35.05  ? 274 LYS A CG    1 
ATOM   1949 C  CD    . LYS A 1 294 ? -10.535 40.960  -40.721 1.00 25.29  ? 274 LYS A CD    1 
ATOM   1950 C  CE    . LYS A 1 294 ? -9.283  41.795  -40.459 1.00 29.70  ? 274 LYS A CE    1 
ATOM   1951 N  NZ    . LYS A 1 294 ? -9.433  43.167  -41.040 1.00 30.02  ? 274 LYS A NZ    1 
ATOM   1952 N  N     . ALA A 1 295 ? -11.104 36.787  -36.516 1.00 19.21  ? 275 ALA A N     1 
ATOM   1953 C  CA    . ALA A 1 295 ? -10.984 36.607  -35.077 1.00 20.17  ? 275 ALA A CA    1 
ATOM   1954 C  C     . ALA A 1 295 ? -9.759  35.759  -34.760 1.00 22.06  ? 275 ALA A C     1 
ATOM   1955 O  O     . ALA A 1 295 ? -9.353  34.907  -35.555 1.00 20.73  ? 275 ALA A O     1 
ATOM   1956 C  CB    . ALA A 1 295 ? -12.237 35.936  -34.505 1.00 20.61  ? 275 ALA A CB    1 
ATOM   1957 N  N     . GLY A 1 296 ? -9.149  36.012  -33.592 1.00 19.37  ? 276 GLY A N     1 
ATOM   1958 C  CA    . GLY A 1 296 ? -8.091  35.140  -33.129 1.00 19.29  ? 276 GLY A CA    1 
ATOM   1959 C  C     . GLY A 1 296 ? -6.887  35.905  -32.624 1.00 19.63  ? 276 GLY A C     1 
ATOM   1960 O  O     . GLY A 1 296 ? -6.957  37.100  -32.316 1.00 18.71  ? 276 GLY A O     1 
ATOM   1961 N  N     . LEU A 1 297 ? -5.771  35.179  -32.540 1.00 18.79  ? 277 LEU A N     1 
ATOM   1962 C  CA    . LEU A 1 297 ? -4.526  35.667  -31.966 1.00 19.25  ? 277 LEU A CA    1 
ATOM   1963 C  C     . LEU A 1 297 ? -3.628  36.276  -33.035 1.00 19.60  ? 277 LEU A C     1 
ATOM   1964 O  O     . LEU A 1 297 ? -3.438  35.690  -34.109 1.00 19.97  ? 277 LEU A O     1 
ATOM   1965 C  CB    . LEU A 1 297 ? -3.802  34.516  -31.270 1.00 18.91  ? 277 LEU A CB    1 
ATOM   1966 C  CG    . LEU A 1 297 ? -2.366  34.734  -30.798 1.00 19.88  ? 277 LEU A CG    1 
ATOM   1967 C  CD1   . LEU A 1 297 ? -2.269  35.799  -29.702 1.00 20.50  ? 277 LEU A CD1   1 
ATOM   1968 C  CD2   . LEU A 1 297 ? -1.859  33.392  -30.296 1.00 22.65  ? 277 LEU A CD2   1 
ATOM   1969 N  N     . TYR A 1 298 ? -3.063  37.441  -32.730 1.00 17.46  ? 278 TYR A N     1 
ATOM   1970 C  CA    . TYR A 1 298 ? -2.172  38.160  -33.632 1.00 19.73  ? 278 TYR A CA    1 
ATOM   1971 C  C     . TYR A 1 298 ? -0.889  38.462  -32.886 1.00 23.26  ? 278 TYR A C     1 
ATOM   1972 O  O     . TYR A 1 298 ? -0.935  38.902  -31.733 1.00 20.24  ? 278 TYR A O     1 
ATOM   1973 C  CB    . TYR A 1 298 ? -2.813  39.455  -34.126 1.00 19.61  ? 278 TYR A CB    1 
ATOM   1974 C  CG    . TYR A 1 298 ? -3.966  39.244  -35.083 1.00 18.83  ? 278 TYR A CG    1 
ATOM   1975 C  CD1   . TYR A 1 298 ? -5.236  38.939  -34.615 1.00 20.00  ? 278 TYR A CD1   1 
ATOM   1976 C  CD2   . TYR A 1 298 ? -3.777  39.354  -36.462 1.00 19.88  ? 278 TYR A CD2   1 
ATOM   1977 C  CE1   . TYR A 1 298 ? -6.291  38.751  -35.495 1.00 19.95  ? 278 TYR A CE1   1 
ATOM   1978 C  CE2   . TYR A 1 298 ? -4.817  39.171  -37.336 1.00 19.98  ? 278 TYR A CE2   1 
ATOM   1979 C  CZ    . TYR A 1 298 ? -6.069  38.876  -36.853 1.00 23.64  ? 278 TYR A CZ    1 
ATOM   1980 O  OH    . TYR A 1 298 ? -7.104  38.695  -37.745 1.00 24.84  ? 278 TYR A OH    1 
ATOM   1981 N  N     . ILE A 1 299 ? 0.254   38.227  -33.534 1.00 18.18  ? 279 ILE A N     1 
ATOM   1982 C  CA    . ILE A 1 299 ? 1.556   38.369  -32.892 1.00 19.72  ? 279 ILE A CA    1 
ATOM   1983 C  C     . ILE A 1 299 ? 2.417   39.292  -33.737 1.00 20.10  ? 279 ILE A C     1 
ATOM   1984 O  O     . ILE A 1 299 ? 2.442   39.185  -34.970 1.00 22.89  ? 279 ILE A O     1 
ATOM   1985 C  CB    . ILE A 1 299 ? 2.225   36.993  -32.688 1.00 17.77  ? 279 ILE A CB    1 
ATOM   1986 C  CG1   . ILE A 1 299 ? 1.305   36.104  -31.833 1.00 19.79  ? 279 ILE A CG1   1 
ATOM   1987 C  CG2   . ILE A 1 299 ? 3.577   37.145  -32.005 1.00 18.55  ? 279 ILE A CG2   1 
ATOM   1988 C  CD1   . ILE A 1 299 ? 1.798   34.675  -31.618 1.00 20.93  ? 279 ILE A CD1   1 
ATOM   1989 N  N     . LYS A 1 300 ? 3.104   40.214  -33.074 1.00 21.55  ? 280 LYS A N     1 
ATOM   1990 C  CA    . LYS A 1 300 ? 4.015   41.155  -33.722 1.00 20.96  ? 280 LYS A CA    1 
ATOM   1991 C  C     . LYS A 1 300 ? 5.434   40.793  -33.305 1.00 31.47  ? 280 LYS A C     1 
ATOM   1992 O  O     . LYS A 1 300 ? 5.892   41.193  -32.232 1.00 34.45  ? 280 LYS A O     1 
ATOM   1993 C  CB    . LYS A 1 300 ? 3.700   42.594  -33.327 1.00 29.05  ? 280 LYS A CB    1 
ATOM   1994 C  CG    . LYS A 1 300 ? 4.600   43.605  -34.018 1.00 32.41  ? 280 LYS A CG    1 
ATOM   1995 C  CD    . LYS A 1 300 ? 4.555   44.956  -33.335 1.00 46.60  ? 280 LYS A CD    1 
ATOM   1996 C  CE    . LYS A 1 300 ? 3.400   45.797  -33.805 1.00 51.89  ? 280 LYS A CE    1 
ATOM   1997 N  NZ    . LYS A 1 300 ? 3.566   47.203  -33.336 1.00 70.19  ? 280 LYS A NZ    1 
ATOM   1998 N  N     . SER A 1 301 ? 6.133   40.049  -34.156 1.00 30.55  ? 281 SER A N     1 
ATOM   1999 C  CA    . SER A 1 301 ? 7.521   39.718  -33.877 1.00 34.96  ? 281 SER A CA    1 
ATOM   2000 C  C     . SER A 1 301 ? 8.391   40.968  -34.038 1.00 48.25  ? 281 SER A C     1 
ATOM   2001 O  O     . SER A 1 301 ? 7.919   42.049  -34.408 1.00 37.48  ? 281 SER A O     1 
ATOM   2002 C  CB    . SER A 1 301 ? 8.009   38.621  -34.818 1.00 45.17  ? 281 SER A CB    1 
ATOM   2003 O  OG    . SER A 1 301 ? 8.289   39.167  -36.100 1.00 41.94  ? 281 SER A OG    1 
ATOM   2004 N  N     . ARG A 1 302 ? 9.696   40.818  -33.794 1.00 39.84  ? 282 ARG A N     1 
ATOM   2005 C  CA    . ARG A 1 302 ? 10.577  41.975  -33.928 1.00 39.25  ? 282 ARG A CA    1 
ATOM   2006 C  C     . ARG A 1 302 ? 10.713  42.462  -35.369 1.00 49.63  ? 282 ARG A C     1 
ATOM   2007 O  O     . ARG A 1 302 ? 11.305  43.524  -35.585 1.00 43.59  ? 282 ARG A O     1 
ATOM   2008 C  CB    . ARG A 1 302 ? 11.957  41.681  -33.330 1.00 50.63  ? 282 ARG A CB    1 
ATOM   2009 C  CG    . ARG A 1 302 ? 11.988  41.974  -31.830 1.00 60.52  ? 282 ARG A CG    1 
ATOM   2010 C  CD    . ARG A 1 302 ? 13.373  41.920  -31.202 1.00 75.12  ? 282 ARG A CD    1 
ATOM   2011 N  NE    . ARG A 1 302 ? 14.322  42.810  -31.860 1.00 91.92  ? 282 ARG A NE    1 
ATOM   2012 C  CZ    . ARG A 1 302 ? 15.604  42.909  -31.533 1.00 91.70  ? 282 ARG A CZ    1 
ATOM   2013 N  NH1   . ARG A 1 302 ? 16.126  42.185  -30.554 1.00 67.81  ? 282 ARG A NH1   1 
ATOM   2014 N  NH2   . ARG A 1 302 ? 16.376  43.771  -32.189 1.00 73.04  ? 282 ARG A NH2   1 
ATOM   2015 N  N     . THR A 1 303 ? 10.172  41.735  -36.352 1.00 46.23  ? 283 THR A N     1 
ATOM   2016 C  CA    . THR A 1 303 ? 10.092  42.265  -37.710 1.00 39.78  ? 283 THR A CA    1 
ATOM   2017 C  C     . THR A 1 303 ? 9.210   43.507  -37.796 1.00 44.29  ? 283 THR A C     1 
ATOM   2018 O  O     . THR A 1 303 ? 9.290   44.244  -38.785 1.00 41.46  ? 283 THR A O     1 
ATOM   2019 C  CB    . THR A 1 303 ? 9.555   41.198  -38.658 1.00 43.02  ? 283 THR A CB    1 
ATOM   2020 O  OG1   . THR A 1 303 ? 8.184   40.929  -38.334 1.00 48.80  ? 283 THR A OG1   1 
ATOM   2021 C  CG2   . THR A 1 303 ? 10.364  39.919  -38.524 1.00 52.83  ? 283 THR A CG2   1 
ATOM   2022 N  N     . GLY A 1 304 ? 8.362   43.748  -36.794 1.00 38.48  ? 284 GLY A N     1 
ATOM   2023 C  CA    . GLY A 1 304 ? 7.504   44.914  -36.760 1.00 31.06  ? 284 GLY A CA    1 
ATOM   2024 C  C     . GLY A 1 304 ? 6.167   44.760  -37.444 1.00 32.42  ? 284 GLY A C     1 
ATOM   2025 O  O     . GLY A 1 304 ? 5.354   45.692  -37.391 1.00 38.93  ? 284 GLY A O     1 
ATOM   2026 N  N     . GLN A 1 305 ? 5.932   43.642  -38.119 1.00 25.90  ? 285 GLN A N     1 
ATOM   2027 C  CA    . GLN A 1 305 ? 4.673   43.371  -38.791 1.00 26.04  ? 285 GLN A CA    1 
ATOM   2028 C  C     . GLN A 1 305 ? 3.935   42.255  -38.061 1.00 31.61  ? 285 GLN A C     1 
ATOM   2029 O  O     . GLN A 1 305 ? 4.544   41.390  -37.425 1.00 32.33  ? 285 GLN A O     1 
ATOM   2030 C  CB    . GLN A 1 305 ? 4.907   43.076  -40.271 1.00 35.66  ? 285 GLN A CB    1 
ATOM   2031 C  CG    . GLN A 1 305 ? 5.373   44.369  -40.961 1.00 38.66  ? 285 GLN A CG    1 
ATOM   2032 C  CD    . GLN A 1 305 ? 5.596   44.243  -42.447 1.00 44.75  ? 285 GLN A CD    1 
ATOM   2033 O  OE1   . GLN A 1 305 ? 6.284   43.333  -42.910 1.00 48.02  ? 285 GLN A OE1   1 
ATOM   2034 N  NE2   . GLN A 1 305 ? 5.026   45.176  -43.210 1.00 35.13  ? 285 GLN A NE2   1 
ATOM   2035 N  N     . THR A 1 306 ? 2.614   42.351  -38.081 1.00 24.72  ? 286 THR A N     1 
ATOM   2036 C  CA    . THR A 1 306 ? 1.729   41.477  -37.321 1.00 25.99  ? 286 THR A CA    1 
ATOM   2037 C  C     . THR A 1 306 ? 1.165   40.349  -38.179 1.00 26.61  ? 286 THR A C     1 
ATOM   2038 O  O     . THR A 1 306 ? 0.708   40.590  -39.302 1.00 26.35  ? 286 THR A O     1 
ATOM   2039 C  CB    . THR A 1 306 ? 0.597   42.313  -36.729 1.00 26.42  ? 286 THR A CB    1 
ATOM   2040 O  OG1   . THR A 1 306 ? 1.166   43.350  -35.930 1.00 32.37  ? 286 THR A OG1   1 
ATOM   2041 C  CG2   . THR A 1 306 ? -0.320  41.453  -35.876 1.00 24.93  ? 286 THR A CG2   1 
ATOM   2042 N  N     . VAL A 1 307 ? 1.186   39.125  -37.641 1.00 20.51  ? 287 VAL A N     1 
ATOM   2043 C  CA    . VAL A 1 307 ? 0.655   37.943  -38.315 1.00 21.95  ? 287 VAL A CA    1 
ATOM   2044 C  C     . VAL A 1 307 ? -0.391  37.266  -37.431 1.00 20.37  ? 287 VAL A C     1 
ATOM   2045 O  O     . VAL A 1 307 ? -0.341  37.349  -36.199 1.00 20.61  ? 287 VAL A O     1 
ATOM   2046 C  CB    . VAL A 1 307 ? 1.777   36.945  -38.695 1.00 23.37  ? 287 VAL A CB    1 
ATOM   2047 C  CG1   . VAL A 1 307 ? 2.729   37.586  -39.692 1.00 26.29  ? 287 VAL A CG1   1 
ATOM   2048 C  CG2   . VAL A 1 307 ? 2.548   36.493  -37.455 1.00 22.29  ? 287 VAL A CG2   1 
ATOM   2049 N  N     . GLN A 1 308 ? -1.339  36.576  -38.065 1.00 18.02  ? 288 GLN A N     1 
ATOM   2050 C  CA    . GLN A 1 308 ? -2.318  35.780  -37.332 1.00 17.68  ? 288 GLN A CA    1 
ATOM   2051 C  C     . GLN A 1 308 ? -1.749  34.391  -37.080 1.00 23.97  ? 288 GLN A C     1 
ATOM   2052 O  O     . GLN A 1 308 ? -1.084  33.823  -37.947 1.00 23.70  ? 288 GLN A O     1 
ATOM   2053 C  CB    . GLN A 1 308 ? -3.619  35.648  -38.126 1.00 17.85  ? 288 GLN A CB    1 
ATOM   2054 C  CG    . GLN A 1 308 ? -4.809  35.129  -37.311 1.00 20.38  ? 288 GLN A CG    1 
ATOM   2055 C  CD    . GLN A 1 308 ? -6.057  34.940  -38.170 1.00 25.13  ? 288 GLN A CD    1 
ATOM   2056 O  OE1   . GLN A 1 308 ? -5.962  34.634  -39.358 1.00 25.13  ? 288 GLN A OE1   1 
ATOM   2057 N  NE2   . GLN A 1 308 ? -7.227  35.174  -37.585 1.00 25.51  ? 288 GLN A NE2   1 
ATOM   2058 N  N     . VAL A 1 309 ? -2.000  33.841  -35.890 1.00 19.83  ? 289 VAL A N     1 
ATOM   2059 C  CA    . VAL A 1 309 ? -1.467  32.530  -35.531 1.00 18.38  ? 289 VAL A CA    1 
ATOM   2060 C  C     . VAL A 1 309 ? -2.587  31.691  -34.939 1.00 21.67  ? 289 VAL A C     1 
ATOM   2061 O  O     . VAL A 1 309 ? -3.289  32.143  -34.027 1.00 22.59  ? 289 VAL A O     1 
ATOM   2062 C  CB    . VAL A 1 309 ? -0.291  32.633  -34.541 1.00 19.74  ? 289 VAL A CB    1 
ATOM   2063 C  CG1   . VAL A 1 309 ? 0.154   31.227  -34.096 1.00 24.40  ? 289 VAL A CG1   1 
ATOM   2064 C  CG2   . VAL A 1 309 ? 0.850   33.400  -35.179 1.00 22.70  ? 289 VAL A CG2   1 
ATOM   2065 N  N     . LYS A 1 310 ? -2.730  30.462  -35.426 1.00 20.44  ? 290 LYS A N     1 
ATOM   2066 C  CA    . LYS A 1 310 ? -3.831  29.598  -35.039 1.00 21.33  ? 290 LYS A CA    1 
ATOM   2067 C  C     . LYS A 1 310 ? -3.353  28.468  -34.135 1.00 24.08  ? 290 LYS A C     1 
ATOM   2068 O  O     . LYS A 1 310 ? -2.207  28.022  -34.219 1.00 26.79  ? 290 LYS A O     1 
ATOM   2069 C  CB    . LYS A 1 310 ? -4.522  29.031  -36.280 1.00 26.11  ? 290 LYS A CB    1 
ATOM   2070 C  CG    . LYS A 1 310 ? -5.215  30.112  -37.100 1.00 26.93  ? 290 LYS A CG    1 
ATOM   2071 C  CD    . LYS A 1 310 ? -5.875  29.536  -38.341 1.00 41.39  ? 290 LYS A CD    1 
ATOM   2072 C  CE    . LYS A 1 310 ? -6.526  30.628  -39.179 1.00 40.48  ? 290 LYS A CE    1 
ATOM   2073 N  NZ    . LYS A 1 310 ? -7.702  31.254  -38.522 1.00 39.91  ? 290 LYS A NZ    1 
ATOM   2074 N  N     . ILE A 1 311 ? -4.226  28.058  -33.222 1.00 20.85  ? 291 ILE A N     1 
ATOM   2075 C  CA    . ILE A 1 311 ? -4.003  26.914  -32.345 1.00 19.97  ? 291 ILE A CA    1 
ATOM   2076 C  C     . ILE A 1 311 ? -4.911  25.783  -32.815 1.00 18.91  ? 291 ILE A C     1 
ATOM   2077 O  O     . ILE A 1 311 ? -6.142  25.929  -32.765 1.00 19.14  ? 291 ILE A O     1 
ATOM   2078 C  CB    . ILE A 1 311 ? -4.294  27.267  -30.877 1.00 20.68  ? 291 ILE A CB    1 
ATOM   2079 C  CG1   . ILE A 1 311 ? -3.451  28.466  -30.442 1.00 27.46  ? 291 ILE A CG1   1 
ATOM   2080 C  CG2   . ILE A 1 311 ? -4.020  26.058  -29.986 1.00 20.85  ? 291 ILE A CG2   1 
ATOM   2081 C  CD1   . ILE A 1 311 ? -3.775  28.965  -29.040 1.00 29.97  ? 291 ILE A CD1   1 
ATOM   2082 N  N     . PRO A 1 312 ? -4.374  24.639  -33.236 1.00 19.04  ? 292 PRO A N     1 
ATOM   2083 C  CA    . PRO A 1 312 ? -5.246  23.505  -33.578 1.00 20.15  ? 292 PRO A CA    1 
ATOM   2084 C  C     . PRO A 1 312 ? -6.101  23.081  -32.389 1.00 20.62  ? 292 PRO A C     1 
ATOM   2085 O  O     . PRO A 1 312 ? -5.667  23.117  -31.235 1.00 20.09  ? 292 PRO A O     1 
ATOM   2086 C  CB    . PRO A 1 312 ? -4.262  22.404  -33.996 1.00 21.63  ? 292 PRO A CB    1 
ATOM   2087 C  CG    . PRO A 1 312 ? -3.005  23.146  -34.386 1.00 27.97  ? 292 PRO A CG    1 
ATOM   2088 C  CD    . PRO A 1 312 ? -2.948  24.337  -33.465 1.00 24.81  ? 292 PRO A CD    1 
ATOM   2089 N  N     . ARG A 1 313 ? -7.338  22.676  -32.686 1.00 19.13  ? 293 ARG A N     1 
ATOM   2090 C  CA    . ARG A 1 313 ? -8.307  22.382  -31.635 1.00 19.88  ? 293 ARG A CA    1 
ATOM   2091 C  C     . ARG A 1 313 ? -7.822  21.297  -30.683 1.00 19.47  ? 293 ARG A C     1 
ATOM   2092 O  O     . ARG A 1 313 ? -8.197  21.306  -29.501 1.00 20.22  ? 293 ARG A O     1 
ATOM   2093 C  CB    . ARG A 1 313 ? -9.650  21.993  -32.259 1.00 22.68  ? 293 ARG A CB    1 
ATOM   2094 C  CG    . ARG A 1 313 ? -10.775 21.802  -31.252 1.00 22.52  ? 293 ARG A CG    1 
ATOM   2095 C  CD    . ARG A 1 313 ? -12.110 21.700  -32.002 1.00 22.22  ? 293 ARG A CD    1 
ATOM   2096 N  NE    . ARG A 1 313 ? -12.372 22.970  -32.665 1.00 25.19  ? 293 ARG A NE    1 
ATOM   2097 C  CZ    . ARG A 1 313 ? -13.308 23.174  -33.582 1.00 31.32  ? 293 ARG A CZ    1 
ATOM   2098 N  NH1   . ARG A 1 313 ? -14.085 22.193  -34.007 1.00 41.68  ? 293 ARG A NH1   1 
ATOM   2099 N  NH2   . ARG A 1 313 ? -13.468 24.396  -34.083 1.00 30.37  ? 293 ARG A NH2   1 
ATOM   2100 N  N     . ASP A 1 314 ? -6.988  20.365  -31.162 1.00 19.39  ? 294 ASP A N     1 
ATOM   2101 C  CA    . ASP A 1 314 ? -6.505  19.256  -30.345 1.00 19.26  ? 294 ASP A CA    1 
ATOM   2102 C  C     . ASP A 1 314 ? -5.175  19.554  -29.656 1.00 18.80  ? 294 ASP A C     1 
ATOM   2103 O  O     . ASP A 1 314 ? -4.575  18.642  -29.081 1.00 26.06  ? 294 ASP A O     1 
ATOM   2104 C  CB    . ASP A 1 314 ? -6.373  17.963  -31.179 1.00 22.61  ? 294 ASP A CB    1 
ATOM   2105 C  CG    . ASP A 1 314 ? -5.384  18.073  -32.342 1.00 21.38  ? 294 ASP A CG    1 
ATOM   2106 O  OD1   . ASP A 1 314 ? -5.032  19.191  -32.778 1.00 23.38  ? 294 ASP A OD1   1 
ATOM   2107 O  OD2   . ASP A 1 314 ? -4.947  16.997  -32.835 1.00 26.74  ? 294 ASP A OD2   1 
ATOM   2108 N  N     . CYS A 1 315 ? -4.720  20.797  -29.675 1.00 19.14  ? 295 CYS A N     1 
ATOM   2109 C  CA    . CYS A 1 315 ? -3.412  21.150  -29.138 1.00 20.16  ? 295 CYS A CA    1 
ATOM   2110 C  C     . CYS A 1 315 ? -3.539  22.138  -27.991 1.00 20.10  ? 295 CYS A C     1 
ATOM   2111 O  O     . CYS A 1 315 ? -4.583  22.756  -27.786 1.00 19.75  ? 295 CYS A O     1 
ATOM   2112 C  CB    . CYS A 1 315 ? -2.531  21.763  -30.223 1.00 22.61  ? 295 CYS A CB    1 
ATOM   2113 S  SG    . CYS A 1 315 ? -2.027  20.586  -31.474 1.00 23.36  ? 295 CYS A SG    1 
ATOM   2114 N  N     . ILE A 1 316 ? -2.438  22.296  -27.252 1.00 17.01  ? 296 ILE A N     1 
ATOM   2115 C  CA    . ILE A 1 316 ? -2.309  23.348  -26.246 1.00 16.08  ? 296 ILE A CA    1 
ATOM   2116 C  C     . ILE A 1 316 ? -1.140  24.224  -26.663 1.00 19.53  ? 296 ILE A C     1 
ATOM   2117 O  O     . ILE A 1 316 ? -0.075  23.701  -26.999 1.00 21.80  ? 296 ILE A O     1 
ATOM   2118 C  CB    . ILE A 1 316 ? -2.058  22.766  -24.839 1.00 18.18  ? 296 ILE A CB    1 
ATOM   2119 C  CG1   . ILE A 1 316 ? -3.160  21.777  -24.446 1.00 19.15  ? 296 ILE A CG1   1 
ATOM   2120 C  CG2   . ILE A 1 316 ? -1.909  23.890  -23.791 1.00 20.54  ? 296 ILE A CG2   1 
ATOM   2121 C  CD1   . ILE A 1 316 ? -2.796  20.897  -23.257 1.00 24.10  ? 296 ILE A CD1   1 
ATOM   2122 N  N     . ALA A 1 317 ? -1.298  25.542  -26.589 1.00 17.34  ? 297 ALA A N     1 
ATOM   2123 C  CA    . ALA A 1 317 ? -0.169  26.402  -26.922 1.00 17.65  ? 297 ALA A CA    1 
ATOM   2124 C  C     . ALA A 1 317 ? 0.366   27.070  -25.665 1.00 17.71  ? 297 ALA A C     1 
ATOM   2125 O  O     . ALA A 1 317 ? -0.335  27.187  -24.666 1.00 18.40  ? 297 ALA A O     1 
ATOM   2126 C  CB    . ALA A 1 317 ? -0.550  27.464  -27.959 1.00 22.69  ? 297 ALA A CB    1 
ATOM   2127 N  N     . PHE A 1 318 ? 1.631   27.501  -25.722 1.00 17.25  ? 298 PHE A N     1 
ATOM   2128 C  CA    . PHE A 1 318 ? 2.273   28.168  -24.592 1.00 18.68  ? 298 PHE A CA    1 
ATOM   2129 C  C     . PHE A 1 318 ? 2.964   29.423  -25.083 1.00 19.61  ? 298 PHE A C     1 
ATOM   2130 O  O     . PHE A 1 318 ? 3.814   29.352  -25.975 1.00 18.45  ? 298 PHE A O     1 
ATOM   2131 C  CB    . PHE A 1 318 ? 3.274   27.225  -23.899 1.00 16.14  ? 298 PHE A CB    1 
ATOM   2132 C  CG    . PHE A 1 318 ? 2.602   26.080  -23.227 1.00 16.98  ? 298 PHE A CG    1 
ATOM   2133 C  CD1   . PHE A 1 318 ? 2.137   26.212  -21.929 1.00 17.25  ? 298 PHE A CD1   1 
ATOM   2134 C  CD2   . PHE A 1 318 ? 2.335   24.914  -23.921 1.00 16.63  ? 298 PHE A CD2   1 
ATOM   2135 C  CE1   . PHE A 1 318 ? 1.442   25.162  -21.301 1.00 18.52  ? 298 PHE A CE1   1 
ATOM   2136 C  CE2   . PHE A 1 318 ? 1.648   23.868  -23.309 1.00 18.93  ? 298 PHE A CE2   1 
ATOM   2137 C  CZ    . PHE A 1 318 ? 1.204   23.997  -21.991 1.00 19.76  ? 298 PHE A CZ    1 
ATOM   2138 N  N     . GLN A 1 319 ? 2.598   30.567  -24.507 1.00 16.66  ? 299 GLN A N     1 
ATOM   2139 C  CA    . GLN A 1 319 ? 3.277   31.827  -24.795 1.00 16.31  ? 299 GLN A CA    1 
ATOM   2140 C  C     . GLN A 1 319 ? 4.239   32.186  -23.668 1.00 16.51  ? 299 GLN A C     1 
ATOM   2141 O  O     . GLN A 1 319 ? 3.928   32.007  -22.487 1.00 18.81  ? 299 GLN A O     1 
ATOM   2142 C  CB    . GLN A 1 319 ? 2.281   32.971  -24.968 1.00 18.28  ? 299 GLN A CB    1 
ATOM   2143 C  CG    . GLN A 1 319 ? 1.592   32.946  -26.323 1.00 17.34  ? 299 GLN A CG    1 
ATOM   2144 C  CD    . GLN A 1 319 ? 0.568   34.045  -26.480 1.00 19.77  ? 299 GLN A CD    1 
ATOM   2145 O  OE1   . GLN A 1 319 ? -0.470  34.027  -25.821 1.00 21.55  ? 299 GLN A OE1   1 
ATOM   2146 N  NE2   . GLN A 1 319 ? 0.865   35.021  -27.333 1.00 18.85  ? 299 GLN A NE2   1 
ATOM   2147 N  N     . THR A 1 320 ? 5.402   32.708  -24.033 1.00 18.33  ? 300 THR A N     1 
ATOM   2148 C  CA    . THR A 1 320 ? 6.335   33.205  -23.033 1.00 18.74  ? 300 THR A CA    1 
ATOM   2149 C  C     . THR A 1 320 ? 5.875   34.540  -22.466 1.00 19.46  ? 300 THR A C     1 
ATOM   2150 O  O     . THR A 1 320 ? 5.314   35.372  -23.175 1.00 21.06  ? 300 THR A O     1 
ATOM   2151 C  CB    . THR A 1 320 ? 7.715   33.380  -23.651 1.00 22.39  ? 300 THR A CB    1 
ATOM   2152 O  OG1   . THR A 1 320 ? 7.554   34.045  -24.909 1.00 25.47  ? 300 THR A OG1   1 
ATOM   2153 C  CG2   . THR A 1 320 ? 8.360   32.041  -23.849 1.00 21.62  ? 300 THR A CG2   1 
ATOM   2154 N  N     . GLY A 1 321 ? 6.183   34.771  -21.188 1.00 18.24  ? 301 GLY A N     1 
ATOM   2155 C  CA    . GLY A 1 321 ? 5.886   36.024  -20.534 1.00 18.35  ? 301 GLY A CA    1 
ATOM   2156 C  C     . GLY A 1 321 ? 7.135   36.711  -20.002 1.00 20.19  ? 301 GLY A C     1 
ATOM   2157 O  O     . GLY A 1 321 ? 8.237   36.166  -20.047 1.00 20.54  ? 301 GLY A O     1 
ATOM   2158 N  N     . GLU A 1 322 ? 6.930   37.922  -19.470 1.00 17.68  ? 302 GLU A N     1 
ATOM   2159 C  CA    . GLU A 1 322 ? 8.068   38.766  -19.092 1.00 18.08  ? 302 GLU A CA    1 
ATOM   2160 C  C     . GLU A 1 322 ? 8.883   38.174  -17.950 1.00 20.61  ? 302 GLU A C     1 
ATOM   2161 O  O     . GLU A 1 322 ? 10.094  38.424  -17.859 1.00 19.77  ? 302 GLU A O     1 
ATOM   2162 C  CB    . GLU A 1 322 ? 7.582   40.154  -18.700 1.00 20.54  ? 302 GLU A CB    1 
ATOM   2163 C  CG    . GLU A 1 322 ? 6.926   40.934  -19.821 1.00 24.78  ? 302 GLU A CG    1 
ATOM   2164 C  CD    . GLU A 1 322 ? 6.781   42.396  -19.460 1.00 28.78  ? 302 GLU A CD    1 
ATOM   2165 O  OE1   . GLU A 1 322 ? 7.797   43.121  -19.538 1.00 36.65  ? 302 GLU A OE1   1 
ATOM   2166 O  OE2   . GLU A 1 322 ? 5.668   42.811  -19.082 1.00 33.04  ? 302 GLU A OE2   1 
ATOM   2167 N  N     . ALA A 1 323 ? 8.253   37.437  -17.038 1.00 18.26  ? 303 ALA A N     1 
ATOM   2168 C  CA    . ALA A 1 323 ? 9.043   36.856  -15.956 1.00 21.64  ? 303 ALA A CA    1 
ATOM   2169 C  C     . ALA A 1 323 ? 10.015  35.806  -16.487 1.00 20.84  ? 303 ALA A C     1 
ATOM   2170 O  O     . ALA A 1 323 ? 11.156  35.710  -16.012 1.00 19.34  ? 303 ALA A O     1 
ATOM   2171 C  CB    . ALA A 1 323 ? 8.124   36.266  -14.884 1.00 19.35  ? 303 ALA A CB    1 
ATOM   2172 N  N     . LEU A 1 324 ? 9.584   35.008  -17.474 1.00 19.35  ? 304 LEU A N     1 
ATOM   2173 C  CA    . LEU A 1 324 ? 10.498  34.030  -18.063 1.00 21.64  ? 304 LEU A CA    1 
ATOM   2174 C  C     . LEU A 1 324 ? 11.601  34.727  -18.851 1.00 21.03  ? 304 LEU A C     1 
ATOM   2175 O  O     . LEU A 1 324 ? 12.771  34.310  -18.807 1.00 21.21  ? 304 LEU A O     1 
ATOM   2176 C  CB    . LEU A 1 324 ? 9.722   33.050  -18.948 1.00 22.22  ? 304 LEU A CB    1 
ATOM   2177 C  CG    . LEU A 1 324 ? 10.545  31.918  -19.579 1.00 22.97  ? 304 LEU A CG    1 
ATOM   2178 C  CD1   . LEU A 1 324 ? 9.705   30.642  -19.650 1.00 27.56  ? 304 LEU A CD1   1 
ATOM   2179 C  CD2   . LEU A 1 324 ? 11.036  32.302  -20.963 1.00 27.53  ? 304 LEU A CD2   1 
ATOM   2180 N  N     . GLU A 1 325 ? 11.252  35.798  -19.568 1.00 20.49  ? 305 GLU A N     1 
ATOM   2181 C  CA    . GLU A 1 325 ? 12.271  36.599  -20.240 1.00 22.73  ? 305 GLU A CA    1 
ATOM   2182 C  C     . GLU A 1 325 ? 13.324  37.086  -19.248 1.00 25.28  ? 305 GLU A C     1 
ATOM   2183 O  O     . GLU A 1 325 ? 14.531  36.977  -19.501 1.00 22.45  ? 305 GLU A O     1 
ATOM   2184 C  CB    . GLU A 1 325 ? 11.613  37.780  -20.962 1.00 22.48  ? 305 GLU A CB    1 
ATOM   2185 C  CG    . GLU A 1 325 ? 12.609  38.721  -21.627 1.00 22.78  ? 305 GLU A CG    1 
ATOM   2186 C  CD    . GLU A 1 325 ? 11.949  39.899  -22.316 1.00 30.88  ? 305 GLU A CD    1 
ATOM   2187 O  OE1   . GLU A 1 325 ? 10.858  39.724  -22.900 1.00 25.75  ? 305 GLU A OE1   1 
ATOM   2188 O  OE2   . GLU A 1 325 ? 12.524  41.006  -22.272 1.00 34.12  ? 305 GLU A OE2   1 
ATOM   2189 N  N     . ARG A 1 326 ? 12.890  37.598  -18.094 1.00 21.64  ? 306 ARG A N     1 
ATOM   2190 C  CA    . ARG A 1 326 ? 13.863  38.091  -17.119 1.00 21.86  ? 306 ARG A CA    1 
ATOM   2191 C  C     . ARG A 1 326 ? 14.710  36.943  -16.563 1.00 24.06  ? 306 ARG A C     1 
ATOM   2192 O  O     . ARG A 1 326 ? 15.936  37.078  -16.418 1.00 22.55  ? 306 ARG A O     1 
ATOM   2193 C  CB    . ARG A 1 326 ? 13.141  38.845  -16.001 1.00 22.32  ? 306 ARG A CB    1 
ATOM   2194 C  CG    . ARG A 1 326 ? 14.018  39.769  -15.169 1.00 37.39  ? 306 ARG A CG    1 
ATOM   2195 C  CD    . ARG A 1 326 ? 14.626  40.883  -16.034 1.00 49.95  ? 306 ARG A CD    1 
ATOM   2196 N  NE    . ARG A 1 326 ? 15.251  41.928  -15.227 1.00 64.11  ? 306 ARG A NE    1 
ATOM   2197 C  CZ    . ARG A 1 326 ? 14.725  43.128  -15.011 1.00 59.67  ? 306 ARG A CZ    1 
ATOM   2198 N  NH1   . ARG A 1 326 ? 13.579  43.492  -15.565 1.00 60.73  ? 306 ARG A NH1   1 
ATOM   2199 N  NH2   . ARG A 1 326 ? 15.366  43.987  -14.223 1.00 53.13  ? 306 ARG A NH2   1 
ATOM   2200 N  N     . ILE A 1 327 ? 14.078  35.798  -16.267 1.00 20.77  ? 307 ILE A N     1 
ATOM   2201 C  CA    . ILE A 1 327 ? 14.801  34.646  -15.715 1.00 21.88  ? 307 ILE A CA    1 
ATOM   2202 C  C     . ILE A 1 327 ? 15.863  34.132  -16.684 1.00 21.01  ? 307 ILE A C     1 
ATOM   2203 O  O     . ILE A 1 327 ? 16.922  33.642  -16.254 1.00 23.36  ? 307 ILE A O     1 
ATOM   2204 C  CB    . ILE A 1 327 ? 13.790  33.548  -15.324 1.00 22.54  ? 307 ILE A CB    1 
ATOM   2205 C  CG1   . ILE A 1 327 ? 13.067  33.959  -14.045 1.00 20.56  ? 307 ILE A CG1   1 
ATOM   2206 C  CG2   . ILE A 1 327 ? 14.462  32.183  -15.160 1.00 21.31  ? 307 ILE A CG2   1 
ATOM   2207 C  CD1   . ILE A 1 327 ? 11.818  33.127  -13.748 1.00 20.25  ? 307 ILE A CD1   1 
ATOM   2208 N  N     . THR A 1 328 ? 15.610  34.225  -17.994 1.00 21.18  ? 308 THR A N     1 
ATOM   2209 C  CA    . THR A 1 328 ? 16.574  33.780  -18.991 1.00 22.91  ? 308 THR A CA    1 
ATOM   2210 C  C     . THR A 1 328 ? 17.463  34.911  -19.495 1.00 26.86  ? 308 THR A C     1 
ATOM   2211 O  O     . THR A 1 328 ? 18.157  34.731  -20.501 1.00 26.70  ? 308 THR A O     1 
ATOM   2212 C  CB    . THR A 1 328 ? 15.878  33.097  -20.173 1.00 22.83  ? 308 THR A CB    1 
ATOM   2213 O  OG1   . THR A 1 328 ? 15.018  34.028  -20.850 1.00 23.47  ? 308 THR A OG1   1 
ATOM   2214 C  CG2   . THR A 1 328 ? 15.051  31.901  -19.701 1.00 21.50  ? 308 THR A CG2   1 
ATOM   2215 N  N     . GLY A 1 329 ? 17.446  36.063  -18.826 1.00 23.59  ? 309 GLY A N     1 
ATOM   2216 C  CA    . GLY A 1 329 ? 18.283  37.182  -19.226 1.00 23.32  ? 309 GLY A CA    1 
ATOM   2217 C  C     . GLY A 1 329 ? 18.042  37.654  -20.639 1.00 24.44  ? 309 GLY A C     1 
ATOM   2218 O  O     . GLY A 1 329 ? 18.982  38.121  -21.303 1.00 27.62  ? 309 GLY A O     1 
ATOM   2219 N  N     . GLY A 1 330 ? 16.804  37.538  -21.127 1.00 23.12  ? 310 GLY A N     1 
ATOM   2220 C  CA    . GLY A 1 330 ? 16.453  37.967  -22.460 1.00 23.44  ? 310 GLY A CA    1 
ATOM   2221 C  C     . GLY A 1 330 ? 16.780  36.985  -23.557 1.00 24.87  ? 310 GLY A C     1 
ATOM   2222 O  O     . GLY A 1 330 ? 16.544  37.296  -24.730 1.00 29.58  ? 310 GLY A O     1 
ATOM   2223 N  N     . LYS A 1 331 ? 17.324  35.814  -23.222 1.00 26.42  ? 311 LYS A N     1 
ATOM   2224 C  CA    . LYS A 1 331 ? 17.625  34.829  -24.252 1.00 28.25  ? 311 LYS A CA    1 
ATOM   2225 C  C     . LYS A 1 331 ? 16.357  34.233  -24.835 1.00 30.60  ? 311 LYS A C     1 
ATOM   2226 O  O     . LYS A 1 331 ? 16.342  33.857  -26.012 1.00 27.42  ? 311 LYS A O     1 
ATOM   2227 C  CB    . LYS A 1 331 ? 18.537  33.742  -23.694 1.00 26.71  ? 311 LYS A CB    1 
ATOM   2228 C  CG    . LYS A 1 331 ? 19.953  34.248  -23.399 1.00 30.50  ? 311 LYS A CG    1 
ATOM   2229 C  CD    . LYS A 1 331 ? 20.937  33.087  -23.300 1.00 32.76  ? 311 LYS A CD    1 
ATOM   2230 C  CE    . LYS A 1 331 ? 22.324  33.552  -22.865 1.00 36.51  ? 311 LYS A CE    1 
ATOM   2231 N  NZ    . LYS A 1 331 ? 22.879  34.578  -23.783 1.00 44.06  ? 311 LYS A NZ    1 
ATOM   2232 N  N     . PHE A 1 332 ? 15.305  34.114  -24.027 1.00 21.15  ? 312 PHE A N     1 
ATOM   2233 C  CA    . PHE A 1 332 ? 13.946  33.950  -24.515 1.00 23.71  ? 312 PHE A CA    1 
ATOM   2234 C  C     . PHE A 1 332 ? 13.189  35.251  -24.259 1.00 23.37  ? 312 PHE A C     1 
ATOM   2235 O  O     . PHE A 1 332 ? 13.510  35.999  -23.330 1.00 24.55  ? 312 PHE A O     1 
ATOM   2236 C  CB    . PHE A 1 332 ? 13.239  32.764  -23.842 1.00 21.94  ? 312 PHE A CB    1 
ATOM   2237 C  CG    . PHE A 1 332 ? 13.717  31.403  -24.309 1.00 24.16  ? 312 PHE A CG    1 
ATOM   2238 C  CD1   . PHE A 1 332 ? 14.598  31.281  -25.370 1.00 23.60  ? 312 PHE A CD1   1 
ATOM   2239 C  CD2   . PHE A 1 332 ? 13.249  30.242  -23.701 1.00 26.57  ? 312 PHE A CD2   1 
ATOM   2240 C  CE1   . PHE A 1 332 ? 15.016  30.028  -25.814 1.00 25.67  ? 312 PHE A CE1   1 
ATOM   2241 C  CE2   . PHE A 1 332 ? 13.659  28.979  -24.142 1.00 22.99  ? 312 PHE A CE2   1 
ATOM   2242 C  CZ    . PHE A 1 332 ? 14.553  28.875  -25.194 1.00 23.32  ? 312 PHE A CZ    1 
ATOM   2243 N  N     . LYS A 1 333 ? 12.197  35.535  -25.102 1.00 23.95  ? 313 LYS A N     1 
ATOM   2244 C  CA    . LYS A 1 333 ? 11.543  36.836  -25.102 1.00 23.23  ? 313 LYS A CA    1 
ATOM   2245 C  C     . LYS A 1 333 ? 10.037  36.689  -24.986 1.00 20.40  ? 313 LYS A C     1 
ATOM   2246 O  O     . LYS A 1 333 ? 9.441   35.787  -25.587 1.00 25.17  ? 313 LYS A O     1 
ATOM   2247 C  CB    . LYS A 1 333 ? 11.845  37.629  -26.393 1.00 31.19  ? 313 LYS A CB    1 
ATOM   2248 C  CG    . LYS A 1 333 ? 13.231  38.261  -26.457 1.00 39.02  ? 313 LYS A CG    1 
ATOM   2249 C  CD    . LYS A 1 333 ? 13.419  39.221  -25.290 1.00 46.60  ? 313 LYS A CD    1 
ATOM   2250 C  CE    . LYS A 1 333 ? 14.420  40.322  -25.596 1.00 55.45  ? 313 LYS A CE    1 
ATOM   2251 N  NZ    . LYS A 1 333 ? 13.757  41.657  -25.505 1.00 61.83  ? 313 LYS A NZ    1 
ATOM   2252 N  N     . ALA A 1 334 ? 9.426   37.605  -24.240 1.00 19.56  ? 314 ALA A N     1 
ATOM   2253 C  CA    . ALA A 1 334 ? 7.982   37.806  -24.338 1.00 20.17  ? 314 ALA A CA    1 
ATOM   2254 C  C     . ALA A 1 334 ? 7.718   38.648  -25.578 1.00 22.48  ? 314 ALA A C     1 
ATOM   2255 O  O     . ALA A 1 334 ? 8.386   39.666  -25.788 1.00 25.86  ? 314 ALA A O     1 
ATOM   2256 C  CB    . ALA A 1 334 ? 7.444   38.509  -23.093 1.00 22.35  ? 314 ALA A CB    1 
ATOM   2257 N  N     . VAL A 1 335 ? 6.780   38.218  -26.410 1.00 19.70  ? 315 VAL A N     1 
ATOM   2258 C  CA    . VAL A 1 335 ? 6.552   38.815  -27.727 1.00 21.04  ? 315 VAL A CA    1 
ATOM   2259 C  C     . VAL A 1 335 ? 5.186   39.491  -27.729 1.00 19.52  ? 315 VAL A C     1 
ATOM   2260 O  O     . VAL A 1 335 ? 4.205   38.873  -27.304 1.00 22.65  ? 315 VAL A O     1 
ATOM   2261 C  CB    . VAL A 1 335 ? 6.641   37.769  -28.853 1.00 19.46  ? 315 VAL A CB    1 
ATOM   2262 C  CG1   . VAL A 1 335 ? 6.387   38.417  -30.215 1.00 21.64  ? 315 VAL A CG1   1 
ATOM   2263 C  CG2   . VAL A 1 335 ? 8.016   37.123  -28.839 1.00 24.06  ? 315 VAL A CG2   1 
ATOM   2264 N  N     . PRO A 1 336 ? 5.088   40.744  -28.181 1.00 21.57  ? 316 PRO A N     1 
ATOM   2265 C  CA    . PRO A 1 336 ? 3.806   41.470  -28.159 1.00 20.59  ? 316 PRO A CA    1 
ATOM   2266 C  C     . PRO A 1 336 ? 2.740   40.799  -29.013 1.00 20.92  ? 316 PRO A C     1 
ATOM   2267 O  O     . PRO A 1 336 ? 3.017   40.289  -30.103 1.00 20.81  ? 316 PRO A O     1 
ATOM   2268 C  CB    . PRO A 1 336 ? 4.176   42.849  -28.724 1.00 22.74  ? 316 PRO A CB    1 
ATOM   2269 C  CG    . PRO A 1 336 ? 5.629   42.981  -28.493 1.00 29.56  ? 316 PRO A CG    1 
ATOM   2270 C  CD    . PRO A 1 336 ? 6.184   41.598  -28.665 1.00 21.20  ? 316 PRO A CD    1 
ATOM   2271 N  N     . HIS A 1 337 ? 1.500   40.825  -28.525 1.00 19.50  ? 317 HIS A N     1 
ATOM   2272 C  CA    . HIS A 1 337 ? 0.410   40.142  -29.209 1.00 19.30  ? 317 HIS A CA    1 
ATOM   2273 C  C     . HIS A 1 337 ? -0.921  40.707  -28.728 1.00 22.10  ? 317 HIS A C     1 
ATOM   2274 O  O     . HIS A 1 337 ? -0.980  41.473  -27.763 1.00 21.08  ? 317 HIS A O     1 
ATOM   2275 C  CB    . HIS A 1 337 ? 0.474   38.634  -28.947 1.00 19.22  ? 317 HIS A CB    1 
ATOM   2276 C  CG    . HIS A 1 337 ? 0.334   38.277  -27.500 1.00 18.19  ? 317 HIS A CG    1 
ATOM   2277 N  ND1   . HIS A 1 337 ? 1.385   38.333  -26.603 1.00 18.91  ? 317 HIS A ND1   1 
ATOM   2278 C  CD2   . HIS A 1 337 ? -0.750  37.886  -26.789 1.00 18.34  ? 317 HIS A CD2   1 
ATOM   2279 C  CE1   . HIS A 1 337 ? 0.952   37.972  -25.407 1.00 19.26  ? 317 HIS A CE1   1 
ATOM   2280 N  NE2   . HIS A 1 337 ? -0.342  37.704  -25.491 1.00 17.04  ? 317 HIS A NE2   1 
ATOM   2281 N  N     . PHE A 1 338 ? -1.996  40.306  -29.410 1.00 20.18  ? 318 PHE A N     1 
ATOM   2282 C  CA    . PHE A 1 338 ? -3.345  40.651  -28.961 1.00 22.24  ? 318 PHE A CA    1 
ATOM   2283 C  C     . PHE A 1 338 ? -4.334  39.654  -29.545 1.00 21.77  ? 318 PHE A C     1 
ATOM   2284 O  O     . PHE A 1 338 ? -4.016  38.896  -30.458 1.00 19.08  ? 318 PHE A O     1 
ATOM   2285 C  CB    . PHE A 1 338 ? -3.749  42.087  -29.342 1.00 20.98  ? 318 PHE A CB    1 
ATOM   2286 C  CG    . PHE A 1 338 ? -3.917  42.311  -30.823 1.00 24.70  ? 318 PHE A CG    1 
ATOM   2287 C  CD1   . PHE A 1 338 ? -5.156  42.136  -31.430 1.00 30.78  ? 318 PHE A CD1   1 
ATOM   2288 C  CD2   . PHE A 1 338 ? -2.844  42.718  -31.597 1.00 27.97  ? 318 PHE A CD2   1 
ATOM   2289 C  CE1   . PHE A 1 338 ? -5.312  42.351  -32.796 1.00 31.95  ? 318 PHE A CE1   1 
ATOM   2290 C  CE2   . PHE A 1 338 ? -2.996  42.933  -32.961 1.00 28.89  ? 318 PHE A CE2   1 
ATOM   2291 C  CZ    . PHE A 1 338 ? -4.226  42.750  -33.552 1.00 25.49  ? 318 PHE A CZ    1 
ATOM   2292 N  N     . VAL A 1 339 ? -5.534  39.626  -28.969 1.00 19.93  ? 319 VAL A N     1 
ATOM   2293 C  CA    . VAL A 1 339 ? -6.612  38.756  -29.430 1.00 19.27  ? 319 VAL A CA    1 
ATOM   2294 C  C     . VAL A 1 339 ? -7.793  39.616  -29.856 1.00 22.64  ? 319 VAL A C     1 
ATOM   2295 O  O     . VAL A 1 339 ? -8.151  40.572  -29.162 1.00 23.42  ? 319 VAL A O     1 
ATOM   2296 C  CB    . VAL A 1 339 ? -7.041  37.748  -28.339 1.00 19.95  ? 319 VAL A CB    1 
ATOM   2297 C  CG1   . VAL A 1 339 ? -8.300  36.992  -28.762 1.00 21.18  ? 319 VAL A CG1   1 
ATOM   2298 C  CG2   . VAL A 1 339 ? -5.904  36.772  -28.043 1.00 21.55  ? 319 VAL A CG2   1 
ATOM   2299 N  N     . ARG A 1 340 ? -8.371  39.282  -31.012 1.00 18.90  ? 320 ARG A N     1 
ATOM   2300 C  CA    . ARG A 1 340 ? -9.574  39.903  -31.564 1.00 22.73  ? 320 ARG A CA    1 
ATOM   2301 C  C     . ARG A 1 340 ? -10.741 38.937  -31.456 1.00 21.67  ? 320 ARG A C     1 
ATOM   2302 O  O     . ARG A 1 340 ? -10.615 37.788  -31.874 1.00 22.03  ? 320 ARG A O     1 
ATOM   2303 C  CB    . ARG A 1 340 ? -9.378  40.195  -33.058 1.00 29.81  ? 320 ARG A CB    1 
ATOM   2304 C  CG    . ARG A 1 340 ? -8.752  41.478  -33.452 1.00 41.71  ? 320 ARG A CG    1 
ATOM   2305 C  CD    . ARG A 1 340 ? -8.604  41.437  -34.963 1.00 27.73  ? 320 ARG A CD    1 
ATOM   2306 N  NE    . ARG A 1 340 ? -9.870  41.404  -35.682 1.00 27.73  ? 320 ARG A NE    1 
ATOM   2307 C  CZ    . ARG A 1 340 ? -10.324 42.419  -36.406 1.00 30.49  ? 320 ARG A CZ    1 
ATOM   2308 N  NH1   . ARG A 1 340 ? -9.645  43.549  -36.511 1.00 33.12  ? 320 ARG A NH1   1 
ATOM   2309 N  NH2   . ARG A 1 340 ? -11.470 42.287  -37.066 1.00 26.20  ? 320 ARG A NH2   1 
ATOM   2310 N  N     . GLY A 1 341 ? -11.907 39.419  -31.000 1.00 20.84  ? 321 GLY A N     1 
ATOM   2311 C  CA    . GLY A 1 341 ? -13.115 38.622  -31.094 1.00 21.37  ? 321 GLY A CA    1 
ATOM   2312 C  C     . GLY A 1 341 ? -13.738 38.717  -32.488 1.00 23.63  ? 321 GLY A C     1 
ATOM   2313 O  O     . GLY A 1 341 ? -13.258 39.419  -33.375 1.00 25.65  ? 321 GLY A O     1 
ATOM   2314 N  N     . ALA A 1 342 ? -14.858 38.021  -32.661 1.00 20.46  ? 322 ALA A N     1 
ATOM   2315 C  CA    . ALA A 1 342 ? -15.566 38.042  -33.936 1.00 20.23  ? 322 ALA A CA    1 
ATOM   2316 C  C     . ALA A 1 342 ? -16.339 39.345  -34.100 1.00 26.68  ? 322 ALA A C     1 
ATOM   2317 O  O     . ALA A 1 342 ? -16.866 39.906  -33.131 1.00 25.27  ? 322 ALA A O     1 
ATOM   2318 C  CB    . ALA A 1 342 ? -16.528 36.856  -34.040 1.00 22.24  ? 322 ALA A CB    1 
ATOM   2319 N  N     . ARG A 1 343 ? -16.366 39.849  -35.332 1.00 22.29  ? 323 ARG A N     1 
ATOM   2320 C  CA    . ARG A 1 343 ? -17.130 41.049  -35.634 1.00 24.53  ? 323 ARG A CA    1 
ATOM   2321 C  C     . ARG A 1 343 ? -18.627 40.787  -35.496 1.00 25.16  ? 323 ARG A C     1 
ATOM   2322 O  O     . ARG A 1 343 ? -19.116 39.685  -35.756 1.00 25.43  ? 323 ARG A O     1 
ATOM   2323 C  CB    . ARG A 1 343 ? -16.797 41.547  -37.044 1.00 26.95  ? 323 ARG A CB    1 
ATOM   2324 C  CG    . ARG A 1 343 ? -15.428 42.214  -37.130 1.00 28.57  ? 323 ARG A CG    1 
ATOM   2325 C  CD    . ARG A 1 343 ? -14.983 42.388  -38.568 1.00 32.56  ? 323 ARG A CD    1 
ATOM   2326 N  NE    . ARG A 1 343 ? -14.664 41.117  -39.206 1.00 29.51  ? 323 ARG A NE    1 
ATOM   2327 C  CZ    . ARG A 1 343 ? -14.356 40.986  -40.489 1.00 33.73  ? 323 ARG A CZ    1 
ATOM   2328 N  NH1   . ARG A 1 343 ? -14.325 42.032  -41.302 1.00 32.44  ? 323 ARG A NH1   1 
ATOM   2329 N  NH2   . ARG A 1 343 ? -14.073 39.778  -40.967 1.00 25.08  ? 323 ARG A NH2   1 
ATOM   2330 N  N     . ALA A 1 344 ? -19.356 41.828  -35.072 1.00 31.32  ? 324 ALA A N     1 
ATOM   2331 C  CA    . ALA A 1 344 ? -20.783 41.675  -34.782 1.00 32.51  ? 324 ALA A CA    1 
ATOM   2332 C  C     . ALA A 1 344 ? -21.558 41.168  -35.993 1.00 30.21  ? 324 ALA A C     1 
ATOM   2333 O  O     . ALA A 1 344 ? -22.496 40.375  -35.847 1.00 29.96  ? 324 ALA A O     1 
ATOM   2334 C  CB    . ALA A 1 344 ? -21.362 43.004  -34.296 1.00 33.39  ? 324 ALA A CB    1 
ATOM   2335 N  N     . GLU A 1 345 ? -21.188 41.615  -37.198 1.00 29.49  ? 325 GLU A N     1 
ATOM   2336 C  CA    . GLU A 1 345 ? -21.835 41.102  -38.406 1.00 32.37  ? 325 GLU A CA    1 
ATOM   2337 C  C     . GLU A 1 345 ? -21.808 39.581  -38.458 1.00 32.78  ? 325 GLU A C     1 
ATOM   2338 O  O     . GLU A 1 345 ? -22.769 38.947  -38.906 1.00 32.51  ? 325 GLU A O     1 
ATOM   2339 C  CB    . GLU A 1 345 ? -21.154 41.669  -39.655 1.00 42.82  ? 325 GLU A CB    1 
ATOM   2340 C  CG    . GLU A 1 345 ? -21.595 40.990  -40.953 1.00 52.00  ? 325 GLU A CG    1 
ATOM   2341 C  CD    . GLU A 1 345 ? -20.795 41.441  -42.164 1.00 62.58  ? 325 GLU A CD    1 
ATOM   2342 O  OE1   . GLU A 1 345 ? -20.092 42.469  -42.072 1.00 71.51  ? 325 GLU A OE1   1 
ATOM   2343 O  OE2   . GLU A 1 345 ? -20.864 40.756  -43.207 1.00 54.66  ? 325 GLU A OE2   1 
ATOM   2344 N  N     . MET A 1 346 ? -20.730 38.973  -37.969 1.00 29.30  ? 326 MET A N     1 
ATOM   2345 C  CA    . MET A 1 346 ? -20.615 37.522  -37.984 1.00 28.53  ? 326 MET A CA    1 
ATOM   2346 C  C     . MET A 1 346 ? -21.138 36.855  -36.720 1.00 25.18  ? 326 MET A C     1 
ATOM   2347 O  O     . MET A 1 346 ? -21.595 35.708  -36.788 1.00 28.40  ? 326 MET A O     1 
ATOM   2348 C  CB    . MET A 1 346 ? -19.165 37.121  -38.258 1.00 24.99  ? 326 MET A CB    1 
ATOM   2349 C  CG    . MET A 1 346 ? -18.896 36.989  -39.754 1.00 46.00  ? 326 MET A CG    1 
ATOM   2350 S  SD    . MET A 1 346 ? -18.675 38.514  -40.658 1.00 71.32  ? 326 MET A SD    1 
ATOM   2351 C  CE    . MET A 1 346 ? -17.351 39.230  -39.730 1.00 34.55  ? 326 MET A CE    1 
ATOM   2352 N  N     . SER A 1 347 ? -21.095 37.536  -35.575 1.00 26.86  ? 327 SER A N     1 
ATOM   2353 C  CA    . SER A 1 347 ? -21.747 36.977  -34.393 1.00 25.71  ? 327 SER A CA    1 
ATOM   2354 C  C     . SER A 1 347 ? -23.259 36.923  -34.584 1.00 27.57  ? 327 SER A C     1 
ATOM   2355 O  O     . SER A 1 347 ? -23.910 35.964  -34.151 1.00 26.31  ? 327 SER A O     1 
ATOM   2356 C  CB    . SER A 1 347 ? -21.400 37.790  -33.148 1.00 27.36  ? 327 SER A CB    1 
ATOM   2357 O  OG    . SER A 1 347 ? -22.196 37.363  -32.043 1.00 29.57  ? 327 SER A OG    1 
ATOM   2358 N  N     . ALA A 1 348 ? -23.826 37.939  -35.246 1.00 26.02  ? 328 ALA A N     1 
ATOM   2359 C  CA    . ALA A 1 348 ? -25.243 37.968  -35.632 1.00 31.16  ? 328 ALA A CA    1 
ATOM   2360 C  C     . ALA A 1 348 ? -26.167 37.818  -34.428 1.00 34.81  ? 328 ALA A C     1 
ATOM   2361 O  O     . ALA A 1 348 ? -27.255 37.240  -34.536 1.00 32.78  ? 328 ALA A O     1 
ATOM   2362 C  CB    . ALA A 1 348 ? -25.556 36.895  -36.680 1.00 33.05  ? 328 ALA A CB    1 
ATOM   2363 N  N     . GLY A 1 349 ? -25.740 38.348  -33.283 1.00 30.31  ? 329 GLY A N     1 
ATOM   2364 C  CA    . GLY A 1 349 ? -26.501 38.264  -32.054 1.00 31.17  ? 329 GLY A CA    1 
ATOM   2365 C  C     . GLY A 1 349 ? -26.664 36.876  -31.483 1.00 27.90  ? 329 GLY A C     1 
ATOM   2366 O  O     . GLY A 1 349 ? -27.399 36.712  -30.506 1.00 30.23  ? 329 GLY A O     1 
ATOM   2367 N  N     . ARG A 1 350 ? -25.991 35.866  -32.041 1.00 23.67  ? 330 ARG A N     1 
ATOM   2368 C  CA    . ARG A 1 350 ? -26.157 34.499  -31.569 1.00 22.10  ? 330 ARG A CA    1 
ATOM   2369 C  C     . ARG A 1 350 ? -24.871 33.810  -31.151 1.00 20.54  ? 330 ARG A C     1 
ATOM   2370 O  O     . ARG A 1 350 ? -24.931 32.892  -30.333 1.00 21.91  ? 330 ARG A O     1 
ATOM   2371 C  CB    . ARG A 1 350 ? -26.795 33.607  -32.649 1.00 28.40  ? 330 ARG A CB    1 
ATOM   2372 C  CG    . ARG A 1 350 ? -27.758 34.285  -33.597 1.00 48.24  ? 330 ARG A CG    1 
ATOM   2373 C  CD    . ARG A 1 350 ? -28.454 33.265  -34.504 1.00 39.21  ? 330 ARG A CD    1 
ATOM   2374 N  NE    . ARG A 1 350 ? -27.589 32.164  -34.922 1.00 48.35  ? 330 ARG A NE    1 
ATOM   2375 C  CZ    . ARG A 1 350 ? -26.786 32.183  -35.980 1.00 56.51  ? 330 ARG A CZ    1 
ATOM   2376 N  NH1   . ARG A 1 350 ? -26.700 33.245  -36.768 1.00 51.80  ? 330 ARG A NH1   1 
ATOM   2377 N  NH2   . ARG A 1 350 ? -26.054 31.106  -36.261 1.00 45.70  ? 330 ARG A NH2   1 
ATOM   2378 N  N     . ILE A 1 351 ? -23.727 34.169  -31.724 1.00 20.71  ? 331 ILE A N     1 
ATOM   2379 C  CA    . ILE A 1 351 ? -22.515 33.366  -31.564 1.00 16.89  ? 331 ILE A CA    1 
ATOM   2380 C  C     . ILE A 1 351 ? -21.606 34.000  -30.517 1.00 17.99  ? 331 ILE A C     1 
ATOM   2381 O  O     . ILE A 1 351 ? -21.190 35.158  -30.637 1.00 22.53  ? 331 ILE A O     1 
ATOM   2382 C  CB    . ILE A 1 351 ? -21.794 33.153  -32.906 1.00 18.72  ? 331 ILE A CB    1 
ATOM   2383 C  CG1   . ILE A 1 351 ? -22.771 32.503  -33.903 1.00 21.85  ? 331 ILE A CG1   1 
ATOM   2384 C  CG2   . ILE A 1 351 ? -20.549 32.286  -32.710 1.00 21.86  ? 331 ILE A CG2   1 
ATOM   2385 C  CD1   . ILE A 1 351 ? -22.206 32.343  -35.294 1.00 24.68  ? 331 ILE A CD1   1 
ATOM   2386 N  N     . ALA A 1 352 ? -21.311 33.217  -29.490 1.00 16.86  ? 332 ALA A N     1 
ATOM   2387 C  CA    . ALA A 1 352 ? -20.397 33.560  -28.409 1.00 17.60  ? 332 ALA A CA    1 
ATOM   2388 C  C     . ALA A 1 352 ? -19.057 32.889  -28.643 1.00 19.12  ? 332 ALA A C     1 
ATOM   2389 O  O     . ALA A 1 352 ? -18.949 31.942  -29.431 1.00 17.39  ? 332 ALA A O     1 
ATOM   2390 C  CB    . ALA A 1 352 ? -20.958 33.103  -27.060 1.00 18.46  ? 332 ALA A CB    1 
ATOM   2391 N  N     . ARG A 1 353 ? -18.025 33.382  -27.938 1.00 17.25  ? 333 ARG A N     1 
ATOM   2392 C  CA    . ARG A 1 353 ? -16.673 32.825  -28.076 1.00 17.26  ? 333 ARG A CA    1 
ATOM   2393 C  C     . ARG A 1 353 ? -16.051 32.588  -26.700 1.00 15.69  ? 333 ARG A C     1 
ATOM   2394 O  O     . ARG A 1 353 ? -15.996 33.506  -25.889 1.00 19.93  ? 333 ARG A O     1 
ATOM   2395 C  CB    . ARG A 1 353 ? -15.772 33.762  -28.904 1.00 16.69  ? 333 ARG A CB    1 
ATOM   2396 C  CG    . ARG A 1 353 ? -14.322 33.261  -29.079 1.00 17.31  ? 333 ARG A CG    1 
ATOM   2397 C  CD    . ARG A 1 353 ? -13.488 34.310  -29.837 1.00 19.00  ? 333 ARG A CD    1 
ATOM   2398 N  NE    . ARG A 1 353 ? -12.155 33.858  -30.234 1.00 22.80  ? 333 ARG A NE    1 
ATOM   2399 C  CZ    . ARG A 1 353 ? -11.060 33.978  -29.488 1.00 26.48  ? 333 ARG A CZ    1 
ATOM   2400 N  NH1   . ARG A 1 353 ? -11.103 34.488  -28.268 1.00 23.54  ? 333 ARG A NH1   1 
ATOM   2401 N  NH2   . ARG A 1 353 ? -9.890  33.587  -29.985 1.00 25.53  ? 333 ARG A NH2   1 
ATOM   2402 N  N     . ASN A 1 354 ? -15.581 31.373  -26.432 1.00 14.83  ? 334 ASN A N     1 
ATOM   2403 C  CA    . ASN A 1 354 ? -15.043 30.993  -25.125 1.00 17.33  ? 334 ASN A CA    1 
ATOM   2404 C  C     . ASN A 1 354 ? -13.598 30.514  -25.222 1.00 17.23  ? 334 ASN A C     1 
ATOM   2405 O  O     . ASN A 1 354 ? -13.254 29.750  -26.119 1.00 15.29  ? 334 ASN A O     1 
ATOM   2406 C  CB    . ASN A 1 354 ? -15.904 29.881  -24.519 1.00 15.99  ? 334 ASN A CB    1 
ATOM   2407 C  CG    . ASN A 1 354 ? -17.337 30.322  -24.301 1.00 16.09  ? 334 ASN A CG    1 
ATOM   2408 O  OD1   . ASN A 1 354 ? -17.602 31.374  -23.710 1.00 18.86  ? 334 ASN A OD1   1 
ATOM   2409 N  ND2   . ASN A 1 354 ? -18.276 29.542  -24.836 1.00 18.16  ? 334 ASN A ND2   1 
ATOM   2410 N  N     . THR A 1 355 ? -12.756 30.956  -24.285 1.00 17.09  ? 335 THR A N     1 
ATOM   2411 C  CA    . THR A 1 355 ? -11.364 30.499  -24.223 1.00 18.51  ? 335 THR A CA    1 
ATOM   2412 C  C     . THR A 1 355 ? -10.888 30.334  -22.790 1.00 19.19  ? 335 THR A C     1 
ATOM   2413 O  O     . THR A 1 355 ? -11.425 30.931  -21.860 1.00 16.27  ? 335 THR A O     1 
ATOM   2414 C  CB    . THR A 1 355 ? -10.368 31.447  -24.917 1.00 21.13  ? 335 THR A CB    1 
ATOM   2415 O  OG1   . THR A 1 355 ? -10.516 32.771  -24.387 1.00 20.47  ? 335 THR A OG1   1 
ATOM   2416 C  CG2   . THR A 1 355 ? -10.486 31.423  -26.421 1.00 27.08  ? 335 THR A CG2   1 
ATOM   2417 N  N     . LEU A 1 356 ? -9.801  29.573  -22.646 1.00 17.58  ? 336 LEU A N     1 
ATOM   2418 C  CA    . LEU A 1 356 ? -9.101  29.416  -21.376 1.00 16.69  ? 336 LEU A CA    1 
ATOM   2419 C  C     . LEU A 1 356 ? -7.629  29.762  -21.569 1.00 16.58  ? 336 LEU A C     1 
ATOM   2420 O  O     . LEU A 1 356 ? -6.985  29.287  -22.521 1.00 18.02  ? 336 LEU A O     1 
ATOM   2421 C  CB    . LEU A 1 356 ? -9.207  27.988  -20.822 1.00 16.28  ? 336 LEU A CB    1 
ATOM   2422 C  CG    . LEU A 1 356 ? -8.416  27.706  -19.544 1.00 15.36  ? 336 LEU A CG    1 
ATOM   2423 C  CD1   . LEU A 1 356 ? -9.030  28.443  -18.362 1.00 17.96  ? 336 LEU A CD1   1 
ATOM   2424 C  CD2   . LEU A 1 356 ? -8.295  26.199  -19.239 1.00 20.21  ? 336 LEU A CD2   1 
ATOM   2425 N  N     . ALA A 1 357 ? -7.101  30.551  -20.623 1.00 14.94  ? 337 ALA A N     1 
ATOM   2426 C  CA    . ALA A 1 357 ? -5.670  30.836  -20.545 1.00 15.02  ? 337 ALA A CA    1 
ATOM   2427 C  C     . ALA A 1 357 ? -5.211  30.532  -19.125 1.00 16.70  ? 337 ALA A C     1 
ATOM   2428 O  O     . ALA A 1 357 ? -5.918  30.823  -18.164 1.00 16.21  ? 337 ALA A O     1 
ATOM   2429 C  CB    . ALA A 1 357 ? -5.378  32.301  -20.908 1.00 18.10  ? 337 ALA A CB    1 
ATOM   2430 N  N     . VAL A 1 358 ? -4.039  29.936  -18.984 1.00 15.20  ? 338 VAL A N     1 
ATOM   2431 C  CA    . VAL A 1 358 ? -3.477  29.604  -17.675 1.00 15.35  ? 338 VAL A CA    1 
ATOM   2432 C  C     . VAL A 1 358 ? -2.125  30.303  -17.586 1.00 15.50  ? 338 VAL A C     1 
ATOM   2433 O  O     . VAL A 1 358 ? -1.166  29.887  -18.248 1.00 16.02  ? 338 VAL A O     1 
ATOM   2434 C  CB    . VAL A 1 358 ? -3.322  28.093  -17.472 1.00 15.36  ? 338 VAL A CB    1 
ATOM   2435 C  CG1   . VAL A 1 358 ? -2.768  27.801  -16.081 1.00 17.88  ? 338 VAL A CG1   1 
ATOM   2436 C  CG2   . VAL A 1 358 ? -4.666  27.375  -17.656 1.00 15.82  ? 338 VAL A CG2   1 
ATOM   2437 N  N     . PHE A 1 359 ? -2.050  31.368  -16.799 1.00 15.63  ? 339 PHE A N     1 
ATOM   2438 C  CA    . PHE A 1 359 ? -0.824  32.168  -16.650 1.00 15.81  ? 339 PHE A CA    1 
ATOM   2439 C  C     . PHE A 1 359 ? 0.035   31.555  -15.548 1.00 15.97  ? 339 PHE A C     1 
ATOM   2440 O  O     . PHE A 1 359 ? -0.105  31.896  -14.362 1.00 16.65  ? 339 PHE A O     1 
ATOM   2441 C  CB    . PHE A 1 359 ? -1.165  33.620  -16.310 1.00 17.16  ? 339 PHE A CB    1 
ATOM   2442 C  CG    . PHE A 1 359 ? -2.111  34.284  -17.285 1.00 16.62  ? 339 PHE A CG    1 
ATOM   2443 C  CD1   . PHE A 1 359 ? -1.673  34.673  -18.547 1.00 17.34  ? 339 PHE A CD1   1 
ATOM   2444 C  CD2   . PHE A 1 359 ? -3.435  34.546  -16.932 1.00 19.17  ? 339 PHE A CD2   1 
ATOM   2445 C  CE1   . PHE A 1 359 ? -2.548  35.285  -19.445 1.00 16.50  ? 339 PHE A CE1   1 
ATOM   2446 C  CE2   . PHE A 1 359 ? -4.297  35.159  -17.825 1.00 19.47  ? 339 PHE A CE2   1 
ATOM   2447 C  CZ    . PHE A 1 359 ? -3.856  35.528  -19.078 1.00 17.93  ? 339 PHE A CZ    1 
ATOM   2448 N  N     . THR A 1 360 ? 0.921   30.617  -15.914 1.00 16.03  ? 340 THR A N     1 
ATOM   2449 C  CA    . THR A 1 360 ? 1.843   30.108  -14.910 1.00 16.36  ? 340 THR A CA    1 
ATOM   2450 C  C     . THR A 1 360 ? 2.917   31.159  -14.659 1.00 17.50  ? 340 THR A C     1 
ATOM   2451 O  O     . THR A 1 360 ? 3.405   31.815  -15.598 1.00 19.17  ? 340 THR A O     1 
ATOM   2452 C  CB    . THR A 1 360 ? 2.477   28.769  -15.316 1.00 16.46  ? 340 THR A CB    1 
ATOM   2453 O  OG1   . THR A 1 360 ? 3.453   28.961  -16.356 1.00 16.36  ? 340 THR A OG1   1 
ATOM   2454 C  CG2   . THR A 1 360 ? 1.418   27.753  -15.777 1.00 18.09  ? 340 THR A CG2   1 
ATOM   2455 N  N     . GLN A 1 361 ? 3.246   31.347  -13.380 1.00 16.70  ? 341 GLN A N     1 
ATOM   2456 C  CA    . GLN A 1 361 ? 4.120   32.436  -12.962 1.00 20.66  ? 341 GLN A CA    1 
ATOM   2457 C  C     . GLN A 1 361 ? 4.684   32.104  -11.582 1.00 18.10  ? 341 GLN A C     1 
ATOM   2458 O  O     . GLN A 1 361 ? 4.183   31.203  -10.903 1.00 17.68  ? 341 GLN A O     1 
ATOM   2459 C  CB    . GLN A 1 361 ? 3.359   33.774  -12.948 1.00 18.20  ? 341 GLN A CB    1 
ATOM   2460 C  CG    . GLN A 1 361 ? 2.045   33.740  -12.176 1.00 17.99  ? 341 GLN A CG    1 
ATOM   2461 C  CD    . GLN A 1 361 ? 1.095   34.828  -12.611 1.00 19.19  ? 341 GLN A CD    1 
ATOM   2462 O  OE1   . GLN A 1 361 ? 1.403   35.626  -13.505 1.00 21.34  ? 341 GLN A OE1   1 
ATOM   2463 N  NE2   . GLN A 1 361 ? -0.077  34.870  -11.988 1.00 18.01  ? 341 GLN A NE2   1 
ATOM   2464 N  N     . PRO A 1 362 ? 5.736   32.794  -11.148 1.00 17.32  ? 342 PRO A N     1 
ATOM   2465 C  CA    . PRO A 1 362 ? 6.398   32.420  -9.894  1.00 19.76  ? 342 PRO A CA    1 
ATOM   2466 C  C     . PRO A 1 362 ? 5.619   32.821  -8.654  1.00 19.78  ? 342 PRO A C     1 
ATOM   2467 O  O     . PRO A 1 362 ? 4.729   33.669  -8.679  1.00 19.70  ? 342 PRO A O     1 
ATOM   2468 C  CB    . PRO A 1 362 ? 7.727   33.192  -9.944  1.00 20.04  ? 342 PRO A CB    1 
ATOM   2469 C  CG    . PRO A 1 362 ? 7.866   33.663  -11.363 1.00 17.74  ? 342 PRO A CG    1 
ATOM   2470 C  CD    . PRO A 1 362 ? 6.466   33.863  -11.849 1.00 18.92  ? 342 PRO A CD    1 
ATOM   2471 N  N     . ASN A 1 363 ? 5.999   32.205  -7.542  1.00 19.81  ? 343 ASN A N     1 
ATOM   2472 C  CA    . ASN A 1 363 ? 5.574   32.735  -6.256  1.00 21.20  ? 343 ASN A CA    1 
ATOM   2473 C  C     . ASN A 1 363 ? 6.195   34.111  -6.038  1.00 19.69  ? 343 ASN A C     1 
ATOM   2474 O  O     . ASN A 1 363 ? 7.230   34.444  -6.612  1.00 19.81  ? 343 ASN A O     1 
ATOM   2475 C  CB    . ASN A 1 363 ? 5.958   31.781  -5.130  1.00 20.07  ? 343 ASN A CB    1 
ATOM   2476 C  CG    . ASN A 1 363 ? 5.049   30.568  -5.086  1.00 23.24  ? 343 ASN A CG    1 
ATOM   2477 O  OD1   . ASN A 1 363 ? 3.847   30.693  -5.260  1.00 22.28  ? 343 ASN A OD1   1 
ATOM   2478 N  ND2   . ASN A 1 363 ? 5.618   29.395  -4.855  1.00 24.34  ? 343 ASN A ND2   1 
ATOM   2479 N  N     . LEU A 1 364 ? 5.526   34.926  -5.221  1.00 23.00  ? 344 LEU A N     1 
ATOM   2480 C  CA    . LEU A 1 364 ? 5.910   36.332  -5.113  1.00 20.69  ? 344 LEU A CA    1 
ATOM   2481 C  C     . LEU A 1 364 ? 7.332   36.504  -4.593  1.00 28.09  ? 344 LEU A C     1 
ATOM   2482 O  O     . LEU A 1 364 ? 8.001   37.481  -4.951  1.00 22.30  ? 344 LEU A O     1 
ATOM   2483 C  CB    . LEU A 1 364 ? 4.897   37.066  -4.232  1.00 19.26  ? 344 LEU A CB    1 
ATOM   2484 C  CG    . LEU A 1 364 ? 3.478   37.103  -4.832  1.00 22.56  ? 344 LEU A CG    1 
ATOM   2485 C  CD1   . LEU A 1 364 ? 2.470   37.661  -3.830  1.00 23.70  ? 344 LEU A CD1   1 
ATOM   2486 C  CD2   . LEU A 1 364 ? 3.461   37.932  -6.107  1.00 24.12  ? 344 LEU A CD2   1 
ATOM   2487 N  N     . GLY A 1 365 ? 7.822   35.565  -3.780  1.00 22.28  ? 345 GLY A N     1 
ATOM   2488 C  CA    . GLY A 1 365 ? 9.167   35.667  -3.240  1.00 21.68  ? 345 GLY A CA    1 
ATOM   2489 C  C     . GLY A 1 365 ? 10.274  35.095  -4.106  1.00 27.01  ? 345 GLY A C     1 
ATOM   2490 O  O     . GLY A 1 365 ? 11.453  35.265  -3.775  1.00 25.91  ? 345 GLY A O     1 
ATOM   2491 N  N     . ASP A 1 366 ? 9.932   34.437  -5.216  1.00 22.17  ? 346 ASP A N     1 
ATOM   2492 C  CA    . ASP A 1 366 ? 10.927  33.857  -6.116  1.00 21.98  ? 346 ASP A CA    1 
ATOM   2493 C  C     . ASP A 1 366 ? 11.602  34.953  -6.929  1.00 22.23  ? 346 ASP A C     1 
ATOM   2494 O  O     . ASP A 1 366 ? 10.942  35.889  -7.391  1.00 23.37  ? 346 ASP A O     1 
ATOM   2495 C  CB    . ASP A 1 366 ? 10.270  32.886  -7.106  1.00 20.83  ? 346 ASP A CB    1 
ATOM   2496 C  CG    . ASP A 1 366 ? 9.665   31.670  -6.448  1.00 28.98  ? 346 ASP A CG    1 
ATOM   2497 O  OD1   . ASP A 1 366 ? 10.041  31.334  -5.308  1.00 30.85  ? 346 ASP A OD1   1 
ATOM   2498 O  OD2   . ASP A 1 366 ? 8.790   31.053  -7.101  1.00 28.33  ? 346 ASP A OD2   1 
ATOM   2499 N  N     . GLU A 1 367 ? 12.906  34.810  -7.153  1.00 22.32  ? 347 GLU A N     1 
ATOM   2500 C  CA    . GLU A 1 367 ? 13.626  35.791  -7.955  1.00 24.80  ? 347 GLU A CA    1 
ATOM   2501 C  C     . GLU A 1 367 ? 13.307  35.632  -9.436  1.00 23.58  ? 347 GLU A C     1 
ATOM   2502 O  O     . GLU A 1 367 ? 13.184  34.514  -9.945  1.00 25.05  ? 347 GLU A O     1 
ATOM   2503 C  CB    . GLU A 1 367 ? 15.132  35.656  -7.737  1.00 23.13  ? 347 GLU A CB    1 
ATOM   2504 C  CG    . GLU A 1 367 ? 15.555  36.034  -6.327  1.00 25.73  ? 347 GLU A CG    1 
ATOM   2505 C  CD    . GLU A 1 367 ? 17.067  36.092  -6.150  1.00 33.91  ? 347 GLU A CD    1 
ATOM   2506 O  OE1   . GLU A 1 367 ? 17.807  35.737  -7.092  1.00 38.61  ? 347 GLU A OE1   1 
ATOM   2507 O  OE2   . GLU A 1 367 ? 17.507  36.499  -5.062  1.00 44.43  ? 347 GLU A OE2   1 
ATOM   2508 N  N     . VAL A 1 368 ? 13.148  36.768  -10.120 1.00 20.99  ? 348 VAL A N     1 
ATOM   2509 C  CA    . VAL A 1 368 ? 13.034  36.792  -11.570 1.00 19.38  ? 348 VAL A CA    1 
ATOM   2510 C  C     . VAL A 1 368 ? 14.250  37.445  -12.224 1.00 26.16  ? 348 VAL A C     1 
ATOM   2511 O  O     . VAL A 1 368 ? 14.629  37.050  -13.331 1.00 23.97  ? 348 VAL A O     1 
ATOM   2512 C  CB    . VAL A 1 368 ? 11.727  37.476  -12.035 1.00 25.81  ? 348 VAL A CB    1 
ATOM   2513 C  CG1   . VAL A 1 368 ? 10.492  36.698  -11.527 1.00 26.19  ? 348 VAL A CG1   1 
ATOM   2514 C  CG2   . VAL A 1 368 ? 11.676  38.930  -11.586 1.00 29.23  ? 348 VAL A CG2   1 
ATOM   2515 N  N     . ASP A 1 369 ? 14.882  38.413  -11.569 1.00 27.65  ? 349 ASP A N     1 
ATOM   2516 C  CA    . ASP A 1 369 ? 16.168  38.952  -12.004 1.00 34.65  ? 349 ASP A CA    1 
ATOM   2517 C  C     . ASP A 1 369 ? 17.182  38.446  -10.995 1.00 31.88  ? 349 ASP A C     1 
ATOM   2518 O  O     . ASP A 1 369 ? 17.185  38.876  -9.837  1.00 28.85  ? 349 ASP A O     1 
ATOM   2519 C  CB    . ASP A 1 369 ? 16.150  40.478  -12.080 1.00 34.19  ? 349 ASP A CB    1 
ATOM   2520 C  CG    . ASP A 1 369 ? 17.443  41.057  -12.661 1.00 33.50  ? 349 ASP A CG    1 
ATOM   2521 O  OD1   . ASP A 1 369 ? 18.538  40.555  -12.340 1.00 33.52  ? 349 ASP A OD1   1 
ATOM   2522 O  OD2   . ASP A 1 369 ? 17.353  42.012  -13.456 1.00 41.34  ? 349 ASP A OD2   1 
ATOM   2523 N  N     . MET A 1 370 ? 18.009  37.501  -11.419 1.00 31.32  ? 350 MET A N     1 
ATOM   2524 C  CA    . MET A 1 370 ? 18.888  36.830  -10.479 1.00 37.07  ? 350 MET A CA    1 
ATOM   2525 C  C     . MET A 1 370 ? 20.195  37.573  -10.261 1.00 36.09  ? 350 MET A C     1 
ATOM   2526 O  O     . MET A 1 370 ? 20.958  37.193  -9.369  1.00 39.04  ? 350 MET A O     1 
ATOM   2527 C  CB    . MET A 1 370 ? 19.149  35.400  -10.948 1.00 34.17  ? 350 MET A CB    1 
ATOM   2528 C  CG    . MET A 1 370 ? 17.919  34.534  -10.792 1.00 51.69  ? 350 MET A CG    1 
ATOM   2529 S  SD    . MET A 1 370 ? 18.203  32.846  -11.310 1.00 54.94  ? 350 MET A SD    1 
ATOM   2530 C  CE    . MET A 1 370 ? 17.289  32.817  -12.852 1.00 36.48  ? 350 MET A CE    1 
ATOM   2531 N  N     . GLU A 1 371 ? 20.460  38.620  -11.047 1.00 34.40  ? 351 GLU A N     1 
ATOM   2532 C  CA    . GLU A 1 371 ? 21.603  39.488  -10.777 1.00 37.68  ? 351 GLU A CA    1 
ATOM   2533 C  C     . GLU A 1 371 ? 21.268  40.542  -9.731  1.00 41.79  ? 351 GLU A C     1 
ATOM   2534 O  O     . GLU A 1 371 ? 22.009  40.724  -8.759  1.00 42.00  ? 351 GLU A O     1 
ATOM   2535 C  CB    . GLU A 1 371 ? 22.063  40.181  -12.058 1.00 39.84  ? 351 GLU A CB    1 
ATOM   2536 C  CG    . GLU A 1 371 ? 23.099  41.272  -11.785 1.00 56.27  ? 351 GLU A CG    1 
ATOM   2537 C  CD    . GLU A 1 371 ? 23.056  42.399  -12.803 1.00 72.31  ? 351 GLU A CD    1 
ATOM   2538 O  OE1   . GLU A 1 371 ? 22.239  42.324  -13.746 1.00 74.99  ? 351 GLU A OE1   1 
ATOM   2539 O  OE2   . GLU A 1 371 ? 23.816  43.380  -12.636 1.00 75.49  ? 351 GLU A OE2   1 
ATOM   2540 N  N     . GLN A 1 372 ? 20.151  41.241  -9.912  1.00 33.44  ? 352 GLN A N     1 
ATOM   2541 C  CA    . GLN A 1 372 ? 19.744  42.273  -8.972  1.00 33.54  ? 352 GLN A CA    1 
ATOM   2542 C  C     . GLN A 1 372 ? 18.869  41.738  -7.855  1.00 37.59  ? 352 GLN A C     1 
ATOM   2543 O  O     . GLN A 1 372 ? 18.514  42.505  -6.953  1.00 32.88  ? 352 GLN A O     1 
ATOM   2544 C  CB    . GLN A 1 372 ? 19.003  43.401  -9.689  1.00 37.76  ? 352 GLN A CB    1 
ATOM   2545 C  CG    . GLN A 1 372 ? 19.716  43.940  -10.910 1.00 47.58  ? 352 GLN A CG    1 
ATOM   2546 C  CD    . GLN A 1 372 ? 19.199  45.301  -11.320 1.00 48.96  ? 352 GLN A CD    1 
ATOM   2547 O  OE1   . GLN A 1 372 ? 18.969  46.171  -10.475 1.00 46.59  ? 352 GLN A OE1   1 
ATOM   2548 N  NE2   . GLN A 1 372 ? 18.983  45.488  -12.617 1.00 59.89  ? 352 GLN A NE2   1 
ATOM   2549 N  N     . HIS A 1 373 ? 18.495  40.456  -7.918  1.00 28.76  ? 353 HIS A N     1 
ATOM   2550 C  CA    . HIS A 1 373 ? 17.710  39.798  -6.875  1.00 27.72  ? 353 HIS A CA    1 
ATOM   2551 C  C     . HIS A 1 373 ? 16.331  40.438  -6.748  1.00 30.29  ? 353 HIS A C     1 
ATOM   2552 O  O     . HIS A 1 373 ? 15.804  40.623  -5.650  1.00 30.78  ? 353 HIS A O     1 
ATOM   2553 C  CB    . HIS A 1 373 ? 18.456  39.778  -5.539  1.00 34.77  ? 353 HIS A CB    1 
ATOM   2554 C  CG    . HIS A 1 373 ? 19.805  39.138  -5.632  1.00 32.33  ? 353 HIS A CG    1 
ATOM   2555 N  ND1   . HIS A 1 373 ? 19.975  37.774  -5.720  1.00 41.53  ? 353 HIS A ND1   1 
ATOM   2556 C  CD2   . HIS A 1 373 ? 21.049  39.674  -5.643  1.00 49.01  ? 353 HIS A CD2   1 
ATOM   2557 C  CE1   . HIS A 1 373 ? 21.264  37.496  -5.793  1.00 37.65  ? 353 HIS A CE1   1 
ATOM   2558 N  NE2   . HIS A 1 373 ? 21.938  38.631  -5.746  1.00 37.52  ? 353 HIS A NE2   1 
ATOM   2559 N  N     . ILE A 1 374 ? 15.742  40.781  -7.888  1.00 26.64  ? 354 ILE A N     1 
ATOM   2560 C  CA    . ILE A 1 374 ? 14.382  41.303  -7.913  1.00 23.34  ? 354 ILE A CA    1 
ATOM   2561 C  C     . ILE A 1 374 ? 13.416  40.128  -7.904  1.00 28.85  ? 354 ILE A C     1 
ATOM   2562 O  O     . ILE A 1 374 ? 13.537  39.210  -8.723  1.00 24.73  ? 354 ILE A O     1 
ATOM   2563 C  CB    . ILE A 1 374 ? 14.160  42.188  -9.150  1.00 23.02  ? 354 ILE A CB    1 
ATOM   2564 C  CG1   . ILE A 1 374 ? 15.092  43.409  -9.129  1.00 28.33  ? 354 ILE A CG1   1 
ATOM   2565 C  CG2   . ILE A 1 374 ? 12.712  42.597  -9.251  1.00 23.91  ? 354 ILE A CG2   1 
ATOM   2566 C  CD1   . ILE A 1 374 ? 15.076  44.191  -10.425 1.00 31.50  ? 354 ILE A CD1   1 
ATOM   2567 N  N     . THR A 1 375 ? 12.462  40.150  -6.979  1.00 22.68  ? 355 THR A N     1 
ATOM   2568 C  CA    . THR A 1 375 ? 11.486  39.078  -6.855  1.00 24.11  ? 355 THR A CA    1 
ATOM   2569 C  C     . THR A 1 375 ? 10.318  39.299  -7.804  1.00 22.69  ? 355 THR A C     1 
ATOM   2570 O  O     . THR A 1 375 ? 10.114  40.384  -8.349  1.00 22.88  ? 355 THR A O     1 
ATOM   2571 C  CB    . THR A 1 375 ? 10.941  38.999  -5.433  1.00 26.25  ? 355 THR A CB    1 
ATOM   2572 O  OG1   . THR A 1 375 ? 10.217  40.209  -5.149  1.00 27.93  ? 355 THR A OG1   1 
ATOM   2573 C  CG2   . THR A 1 375 ? 12.064  38.789  -4.436  1.00 27.20  ? 355 THR A CG2   1 
ATOM   2574 N  N     . PHE A 1 376 ? 9.494   38.261  -7.949  1.00 25.26  ? 356 PHE A N     1 
ATOM   2575 C  CA    . PHE A 1 376 ? 8.335   38.401  -8.818  1.00 20.16  ? 356 PHE A CA    1 
ATOM   2576 C  C     . PHE A 1 376 ? 7.360   39.439  -8.271  1.00 21.66  ? 356 PHE A C     1 
ATOM   2577 O  O     . PHE A 1 376 ? 6.786   40.207  -9.042  1.00 21.87  ? 356 PHE A O     1 
ATOM   2578 C  CB    . PHE A 1 376 ? 7.656   37.049  -9.023  1.00 18.34  ? 356 PHE A CB    1 
ATOM   2579 C  CG    . PHE A 1 376 ? 6.437   37.105  -9.906  1.00 19.43  ? 356 PHE A CG    1 
ATOM   2580 C  CD1   . PHE A 1 376 ? 6.524   37.552  -11.224 1.00 19.25  ? 356 PHE A CD1   1 
ATOM   2581 C  CD2   . PHE A 1 376 ? 5.204   36.690  -9.424  1.00 22.83  ? 356 PHE A CD2   1 
ATOM   2582 C  CE1   . PHE A 1 376 ? 5.405   37.599  -12.045 1.00 20.72  ? 356 PHE A CE1   1 
ATOM   2583 C  CE2   . PHE A 1 376 ? 4.069   36.726  -10.238 1.00 23.04  ? 356 PHE A CE2   1 
ATOM   2584 C  CZ    . PHE A 1 376 ? 4.170   37.177  -11.547 1.00 24.90  ? 356 PHE A CZ    1 
ATOM   2585 N  N     . GLY A 1 377 ? 7.185   39.503  -6.948  1.00 25.07  ? 357 GLY A N     1 
ATOM   2586 C  CA    . GLY A 1 377 ? 6.309   40.526  -6.381  1.00 26.92  ? 357 GLY A CA    1 
ATOM   2587 C  C     . GLY A 1 377 ? 6.799   41.936  -6.667  1.00 24.66  ? 357 GLY A C     1 
ATOM   2588 O  O     . GLY A 1 377 ? 6.017   42.818  -7.051  1.00 28.93  ? 357 GLY A O     1 
ATOM   2589 N  N     . GLU A 1 378 ? 8.106   42.162  -6.503  1.00 25.19  ? 358 GLU A N     1 
ATOM   2590 C  CA    . GLU A 1 378 ? 8.693   43.456  -6.846  1.00 28.46  ? 358 GLU A CA    1 
ATOM   2591 C  C     . GLU A 1 378 ? 8.517   43.753  -8.328  1.00 29.74  ? 358 GLU A C     1 
ATOM   2592 O  O     . GLU A 1 378 ? 8.089   44.848  -8.713  1.00 25.56  ? 358 GLU A O     1 
ATOM   2593 C  CB    . GLU A 1 378 ? 10.176  43.479  -6.457  1.00 26.01  ? 358 GLU A CB    1 
ATOM   2594 C  CG    . GLU A 1 378 ? 10.425  43.496  -4.947  1.00 26.98  ? 358 GLU A CG    1 
ATOM   2595 C  CD    . GLU A 1 378 ? 11.827  43.070  -4.535  1.00 32.51  ? 358 GLU A CD    1 
ATOM   2596 O  OE1   . GLU A 1 378 ? 12.625  42.619  -5.389  1.00 30.30  ? 358 GLU A OE1   1 
ATOM   2597 O  OE2   . GLU A 1 378 ? 12.147  43.225  -3.339  1.00 36.45  ? 358 GLU A OE2   1 
ATOM   2598 N  N     . PHE A 1 379 ? 8.824   42.767  -9.171  1.00 28.26  ? 359 PHE A N     1 
ATOM   2599 C  CA    . PHE A 1 379 ? 8.678   42.899  -10.616 1.00 23.53  ? 359 PHE A CA    1 
ATOM   2600 C  C     . PHE A 1 379 ? 7.248   43.273  -10.992 1.00 25.14  ? 359 PHE A C     1 
ATOM   2601 O  O     . PHE A 1 379 ? 7.019   44.137  -11.850 1.00 27.81  ? 359 PHE A O     1 
ATOM   2602 C  CB    . PHE A 1 379 ? 9.110   41.570  -11.244 1.00 24.13  ? 359 PHE A CB    1 
ATOM   2603 C  CG    . PHE A 1 379 ? 9.040   41.521  -12.735 1.00 27.40  ? 359 PHE A CG    1 
ATOM   2604 C  CD1   . PHE A 1 379 ? 9.977   42.194  -13.504 1.00 36.68  ? 359 PHE A CD1   1 
ATOM   2605 C  CD2   . PHE A 1 379 ? 8.103   40.718  -13.368 1.00 30.19  ? 359 PHE A CD2   1 
ATOM   2606 C  CE1   . PHE A 1 379 ? 9.939   42.121  -14.886 1.00 42.42  ? 359 PHE A CE1   1 
ATOM   2607 C  CE2   . PHE A 1 379 ? 8.064   40.635  -14.750 1.00 36.60  ? 359 PHE A CE2   1 
ATOM   2608 C  CZ    . PHE A 1 379 ? 8.980   41.340  -15.507 1.00 36.92  ? 359 PHE A CZ    1 
ATOM   2609 N  N     . ALA A 1 380 ? 6.274   42.635  -10.342 1.00 24.41  ? 360 ALA A N     1 
ATOM   2610 C  CA    . ALA A 1 380 ? 4.865   42.914  -10.581 1.00 24.66  ? 360 ALA A CA    1 
ATOM   2611 C  C     . ALA A 1 380 ? 4.487   44.318  -10.131 1.00 30.42  ? 360 ALA A C     1 
ATOM   2612 O  O     . ALA A 1 380 ? 3.554   44.911  -10.688 1.00 38.78  ? 360 ALA A O     1 
ATOM   2613 C  CB    . ALA A 1 380 ? 3.995   41.881  -9.863  1.00 30.96  ? 360 ALA A CB    1 
ATOM   2614 N  N     . ARG A 1 381 ? 5.177   44.861  -9.130  1.00 31.12  ? 361 ARG A N     1 
ATOM   2615 C  CA    . ARG A 1 381 ? 4.911   46.228  -8.696  1.00 30.28  ? 361 ARG A CA    1 
ATOM   2616 C  C     . ARG A 1 381 ? 5.676   47.263  -9.517  1.00 34.72  ? 361 ARG A C     1 
ATOM   2617 O  O     . ARG A 1 381 ? 5.686   48.443  -9.153  1.00 40.20  ? 361 ARG A O     1 
ATOM   2618 C  CB    . ARG A 1 381 ? 5.219   46.382  -7.202  1.00 36.38  ? 361 ARG A CB    1 
ATOM   2619 C  CG    . ARG A 1 381 ? 4.248   45.589  -6.328  1.00 36.48  ? 361 ARG A CG    1 
ATOM   2620 C  CD    . ARG A 1 381 ? 2.950   46.370  -6.140  1.00 49.09  ? 361 ARG A CD    1 
ATOM   2621 N  NE    . ARG A 1 381 ? 1.974   45.678  -5.304  1.00 42.33  ? 361 ARG A NE    1 
ATOM   2622 C  CZ    . ARG A 1 381 ? 0.929   45.019  -5.786  1.00 38.91  ? 361 ARG A CZ    1 
ATOM   2623 N  NH1   . ARG A 1 381 ? 0.708   44.933  -7.088  1.00 43.04  ? 361 ARG A NH1   1 
ATOM   2624 N  NH2   . ARG A 1 381 ? 0.081   44.433  -4.942  1.00 28.95  ? 361 ARG A NH2   1 
ATOM   2625 N  N     . GLY A 1 382 ? 6.310   46.844  -10.609 1.00 32.74  ? 362 GLY A N     1 
ATOM   2626 C  CA    . GLY A 1 382 ? 6.983   47.736  -11.533 1.00 33.14  ? 362 GLY A CA    1 
ATOM   2627 C  C     . GLY A 1 382 ? 8.433   48.033  -11.224 1.00 28.65  ? 362 GLY A C     1 
ATOM   2628 O  O     . GLY A 1 382 ? 9.029   48.882  -11.899 1.00 30.77  ? 362 GLY A O     1 
ATOM   2629 N  N     . ILE A 1 383 ? 9.030   47.344  -10.254 1.00 27.09  ? 363 ILE A N     1 
ATOM   2630 C  CA    . ILE A 1 383 ? 10.429  47.579  -9.924  1.00 25.39  ? 363 ILE A CA    1 
ATOM   2631 C  C     . ILE A 1 383 ? 11.305  46.972  -11.011 1.00 37.56  ? 363 ILE A C     1 
ATOM   2632 O  O     . ILE A 1 383 ? 11.187  45.784  -11.335 1.00 31.80  ? 363 ILE A O     1 
ATOM   2633 C  CB    . ILE A 1 383 ? 10.748  46.992  -8.540  1.00 30.49  ? 363 ILE A CB    1 
ATOM   2634 C  CG1   . ILE A 1 383 ? 10.013  47.793  -7.459  1.00 32.35  ? 363 ILE A CG1   1 
ATOM   2635 C  CG2   . ILE A 1 383 ? 12.252  46.917  -8.296  1.00 29.06  ? 363 ILE A CG2   1 
ATOM   2636 C  CD1   . ILE A 1 383 ? 10.125  47.210  -6.086  1.00 41.59  ? 363 ILE A CD1   1 
ATOM   2637 N  N     . VAL A 1 384 ? 12.215  47.775  -11.559 1.00 32.14  ? 364 VAL A N     1 
ATOM   2638 C  CA    . VAL A 1 384 ? 13.102  47.319  -12.621 1.00 33.91  ? 364 VAL A CA    1 
ATOM   2639 C  C     . VAL A 1 384 ? 14.563  47.413  -12.229 1.00 35.09  ? 364 VAL A C     1 
ATOM   2640 O  O     . VAL A 1 384 ? 15.427  46.968  -12.991 1.00 41.85  ? 364 VAL A O     1 
ATOM   2641 C  CB    . VAL A 1 384 ? 12.856  48.096  -13.930 1.00 34.20  ? 364 VAL A CB    1 
ATOM   2642 C  CG1   . VAL A 1 384 ? 11.427  47.896  -14.406 1.00 35.48  ? 364 VAL A CG1   1 
ATOM   2643 C  CG2   . VAL A 1 384 ? 13.162  49.579  -13.724 1.00 34.61  ? 364 VAL A CG2   1 
ATOM   2644 N  N     . ALA A 1 385 ? 14.862  47.944  -11.046 1.00 33.65  ? 365 ALA A N     1 
ATOM   2645 C  CA    . ALA A 1 385 ? 16.225  48.055  -10.556 1.00 34.91  ? 365 ALA A CA    1 
ATOM   2646 C  C     . ALA A 1 385 ? 16.198  47.991  -9.038  1.00 35.02  ? 365 ALA A C     1 
ATOM   2647 O  O     . ALA A 1 385 ? 15.246  48.450  -8.399  1.00 35.57  ? 365 ALA A O     1 
ATOM   2648 C  CB    . ALA A 1 385 ? 16.893  49.352  -11.031 1.00 45.05  ? 365 ALA A CB    1 
ATOM   2649 N  N     . LYS A 1 386 ? 17.256  47.430  -8.463  1.00 34.79  ? 366 LYS A N     1 
ATOM   2650 C  CA    . LYS A 1 386 ? 17.288  47.174  -7.032  1.00 33.67  ? 366 LYS A CA    1 
ATOM   2651 C  C     . LYS A 1 386 ? 18.725  47.164  -6.539  1.00 47.23  ? 366 LYS A C     1 
ATOM   2652 O  O     . LYS A 1 386 ? 19.592  46.543  -7.161  1.00 46.84  ? 366 LYS A O     1 
ATOM   2653 C  CB    . LYS A 1 386 ? 16.621  45.828  -6.733  1.00 38.60  ? 366 LYS A CB    1 
ATOM   2654 C  CG    . LYS A 1 386 ? 16.491  45.457  -5.273  1.00 41.57  ? 366 LYS A CG    1 
ATOM   2655 C  CD    . LYS A 1 386 ? 15.706  44.155  -5.167  1.00 36.09  ? 366 LYS A CD    1 
ATOM   2656 C  CE    . LYS A 1 386 ? 15.713  43.603  -3.761  1.00 32.98  ? 366 LYS A CE    1 
ATOM   2657 N  NZ    . LYS A 1 386 ? 14.885  42.370  -3.653  1.00 36.61  ? 366 LYS A NZ    1 
ATOM   2658 N  N     . ASN A 1 387 ? 18.965  47.860  -5.435  1.00 51.66  ? 367 ASN A N     1 
ATOM   2659 C  CA    . ASN A 1 387 ? 20.234  47.801  -4.717  1.00 62.24  ? 367 ASN A CA    1 
ATOM   2660 C  C     . ASN A 1 387 ? 20.100  48.417  -3.324  1.00 70.31  ? 367 ASN A C     1 
ATOM   2661 O  O     . ASN A 1 387 ? 19.143  48.133  -2.597  1.00 67.82  ? 367 ASN A O     1 
ATOM   2662 C  CB    . ASN A 1 387 ? 21.358  48.451  -5.544  1.00 72.71  ? 367 ASN A CB    1 
ATOM   2663 C  CG    . ASN A 1 387 ? 21.077  49.899  -5.907  1.00 84.05  ? 367 ASN A CG    1 
ATOM   2664 O  OD1   . ASN A 1 387 ? 20.648  50.703  -5.079  1.00 84.49  ? 367 ASN A OD1   1 
ATOM   2665 N  ND2   . ASN A 1 387 ? 21.315  50.235  -7.173  1.00 74.33  ? 367 ASN A ND2   1 
ATOM   2666 N  N     . MET B 1 21  ? -22.588 3.846   -76.188 1.00 44.00  ? 1   MET B N     1 
ATOM   2667 C  CA    . MET B 1 21  ? -22.996 4.687   -75.064 1.00 37.25  ? 1   MET B CA    1 
ATOM   2668 C  C     . MET B 1 21  ? -24.470 4.535   -74.727 1.00 41.05  ? 1   MET B C     1 
ATOM   2669 O  O     . MET B 1 21  ? -25.312 4.390   -75.614 1.00 37.66  ? 1   MET B O     1 
ATOM   2670 C  CB    . MET B 1 21  ? -22.704 6.159   -75.360 1.00 38.27  ? 1   MET B CB    1 
ATOM   2671 C  CG    . MET B 1 21  ? -21.281 6.440   -75.791 1.00 44.13  ? 1   MET B CG    1 
ATOM   2672 S  SD    . MET B 1 21  ? -20.116 6.247   -74.436 1.00 43.53  ? 1   MET B SD    1 
ATOM   2673 C  CE    . MET B 1 21  ? -20.541 7.638   -73.391 1.00 42.48  ? 1   MET B CE    1 
ATOM   2674 N  N     . ALA B 1 22  ? -24.782 4.609   -73.437 1.00 30.72  ? 2   ALA B N     1 
ATOM   2675 C  CA    . ALA B 1 22  ? -26.177 4.656   -73.048 1.00 32.79  ? 2   ALA B CA    1 
ATOM   2676 C  C     . ALA B 1 22  ? -26.727 6.046   -73.355 1.00 30.21  ? 2   ALA B C     1 
ATOM   2677 O  O     . ALA B 1 22  ? -25.970 7.020   -73.386 1.00 28.11  ? 2   ALA B O     1 
ATOM   2678 C  CB    . ALA B 1 22  ? -26.320 4.354   -71.558 1.00 34.86  ? 2   ALA B CB    1 
ATOM   2679 N  N     . PRO B 1 23  ? -28.033 6.173   -73.590 1.00 25.71  ? 3   PRO B N     1 
ATOM   2680 C  CA    . PRO B 1 23  ? -28.601 7.512   -73.757 1.00 27.27  ? 3   PRO B CA    1 
ATOM   2681 C  C     . PRO B 1 23  ? -28.415 8.313   -72.478 1.00 25.81  ? 3   PRO B C     1 
ATOM   2682 O  O     . PRO B 1 23  ? -28.513 7.783   -71.366 1.00 24.09  ? 3   PRO B O     1 
ATOM   2683 C  CB    . PRO B 1 23  ? -30.090 7.244   -74.023 1.00 28.85  ? 3   PRO B CB    1 
ATOM   2684 C  CG    . PRO B 1 23  ? -30.186 5.790   -74.353 1.00 34.90  ? 3   PRO B CG    1 
ATOM   2685 C  CD    . PRO B 1 23  ? -29.070 5.128   -73.620 1.00 31.92  ? 3   PRO B CD    1 
ATOM   2686 N  N     . ILE B 1 24  ? -28.207 9.613   -72.638 1.00 22.05  ? 4   ILE B N     1 
ATOM   2687 C  CA    . ILE B 1 24  ? -28.084 10.516  -71.498 1.00 23.20  ? 4   ILE B CA    1 
ATOM   2688 C  C     . ILE B 1 24  ? -29.429 11.192  -71.272 1.00 26.82  ? 4   ILE B C     1 
ATOM   2689 O  O     . ILE B 1 24  ? -30.062 11.686  -72.216 1.00 24.93  ? 4   ILE B O     1 
ATOM   2690 C  CB    . ILE B 1 24  ? -26.956 11.543  -71.708 1.00 26.18  ? 4   ILE B CB    1 
ATOM   2691 C  CG1   . ILE B 1 24  ? -26.919 12.520  -70.530 1.00 30.19  ? 4   ILE B CG1   1 
ATOM   2692 C  CG2   . ILE B 1 24  ? -27.106 12.274  -73.046 1.00 33.18  ? 4   ILE B CG2   1 
ATOM   2693 C  CD1   . ILE B 1 24  ? -25.546 13.061  -70.244 1.00 40.46  ? 4   ILE B CD1   1 
ATOM   2694 N  N     . ALA B 1 25  ? -29.888 11.180  -70.029 1.00 22.87  ? 5   ALA B N     1 
ATOM   2695 C  CA    . ALA B 1 25  ? -31.146 11.815  -69.680 1.00 20.66  ? 5   ALA B CA    1 
ATOM   2696 C  C     . ALA B 1 25  ? -30.885 13.014  -68.783 1.00 24.43  ? 5   ALA B C     1 
ATOM   2697 O  O     . ALA B 1 25  ? -29.955 13.023  -67.965 1.00 25.30  ? 5   ALA B O     1 
ATOM   2698 C  CB    . ALA B 1 25  ? -32.097 10.842  -68.980 1.00 23.50  ? 5   ALA B CB    1 
ATOM   2699 N  N     . GLN B 1 26  ? -31.725 14.025  -68.947 1.00 20.92  ? 6   GLN B N     1 
ATOM   2700 C  CA    . GLN B 1 26  ? -31.664 15.232  -68.144 1.00 20.29  ? 6   GLN B CA    1 
ATOM   2701 C  C     . GLN B 1 26  ? -32.541 15.037  -66.915 1.00 20.23  ? 6   GLN B C     1 
ATOM   2702 O  O     . GLN B 1 26  ? -33.753 14.829  -67.042 1.00 23.77  ? 6   GLN B O     1 
ATOM   2703 C  CB    . GLN B 1 26  ? -32.145 16.426  -68.970 1.00 25.57  ? 6   GLN B CB    1 
ATOM   2704 C  CG    . GLN B 1 26  ? -32.292 17.680  -68.186 1.00 28.09  ? 6   GLN B CG    1 
ATOM   2705 C  CD    . GLN B 1 26  ? -30.955 18.193  -67.732 1.00 28.44  ? 6   GLN B CD    1 
ATOM   2706 O  OE1   . GLN B 1 26  ? -30.064 18.453  -68.548 1.00 29.84  ? 6   GLN B OE1   1 
ATOM   2707 N  NE2   . GLN B 1 26  ? -30.776 18.286  -66.421 1.00 30.24  ? 6   GLN B NE2   1 
ATOM   2708 N  N     . ALA B 1 27  ? -31.948 15.159  -65.732 1.00 19.14  ? 7   ALA B N     1 
ATOM   2709 C  CA    . ALA B 1 27  ? -32.721 15.043  -64.506 1.00 18.42  ? 7   ALA B CA    1 
ATOM   2710 C  C     . ALA B 1 27  ? -33.565 16.292  -64.298 1.00 18.39  ? 7   ALA B C     1 
ATOM   2711 O  O     . ALA B 1 27  ? -33.178 17.402  -64.681 1.00 20.77  ? 7   ALA B O     1 
ATOM   2712 C  CB    . ALA B 1 27  ? -31.790 14.846  -63.306 1.00 21.39  ? 7   ALA B CB    1 
ATOM   2713 N  N     . VAL B 1 28  ? -34.737 16.100  -63.681 1.00 18.37  ? 8   VAL B N     1 
ATOM   2714 C  CA    . VAL B 1 28  ? -35.555 17.236  -63.276 1.00 19.66  ? 8   VAL B CA    1 
ATOM   2715 C  C     . VAL B 1 28  ? -34.746 18.118  -62.341 1.00 22.25  ? 8   VAL B C     1 
ATOM   2716 O  O     . VAL B 1 28  ? -34.142 17.633  -61.376 1.00 21.00  ? 8   VAL B O     1 
ATOM   2717 C  CB    . VAL B 1 28  ? -36.836 16.744  -62.597 1.00 19.81  ? 8   VAL B CB    1 
ATOM   2718 C  CG1   . VAL B 1 28  ? -37.605 17.913  -61.981 1.00 23.09  ? 8   VAL B CG1   1 
ATOM   2719 C  CG2   . VAL B 1 28  ? -37.700 15.964  -63.592 1.00 24.07  ? 8   VAL B CG2   1 
ATOM   2720 N  N     . THR B 1 29  ? -34.760 19.426  -62.604 1.00 21.60  ? 9   THR B N     1 
ATOM   2721 C  CA    . THR B 1 29  ? -33.937 20.391  -61.883 1.00 21.00  ? 9   THR B CA    1 
ATOM   2722 C  C     . THR B 1 29  ? -34.825 21.479  -61.292 1.00 23.74  ? 9   THR B C     1 
ATOM   2723 O  O     . THR B 1 29  ? -35.707 22.006  -61.982 1.00 27.00  ? 9   THR B O     1 
ATOM   2724 C  CB    . THR B 1 29  ? -32.889 21.001  -62.825 1.00 23.78  ? 9   THR B CB    1 
ATOM   2725 O  OG1   . THR B 1 29  ? -32.093 19.947  -63.384 1.00 24.80  ? 9   THR B OG1   1 
ATOM   2726 C  CG2   . THR B 1 29  ? -31.965 21.986  -62.079 1.00 25.28  ? 9   THR B CG2   1 
ATOM   2727 N  N     . VAL B 1 30  ? -34.603 21.811  -60.019 1.00 21.43  ? 10  VAL B N     1 
ATOM   2728 C  CA    . VAL B 1 30  ? -35.306 22.922  -59.383 1.00 23.62  ? 10  VAL B CA    1 
ATOM   2729 C  C     . VAL B 1 30  ? -34.288 23.844  -58.729 1.00 25.36  ? 10  VAL B C     1 
ATOM   2730 O  O     . VAL B 1 30  ? -33.144 23.466  -58.477 1.00 22.18  ? 10  VAL B O     1 
ATOM   2731 C  CB    . VAL B 1 30  ? -36.348 22.454  -58.347 1.00 24.69  ? 10  VAL B CB    1 
ATOM   2732 C  CG1   . VAL B 1 30  ? -37.422 21.620  -59.032 1.00 25.23  ? 10  VAL B CG1   1 
ATOM   2733 C  CG2   . VAL B 1 30  ? -35.661 21.674  -57.220 1.00 23.11  ? 10  VAL B CG2   1 
ATOM   2734 N  N     . SER B 1 31  ? -34.723 25.068  -58.446 1.00 23.70  ? 11  SER B N     1 
ATOM   2735 C  CA    . SER B 1 31  ? -33.876 26.065  -57.808 1.00 21.59  ? 11  SER B CA    1 
ATOM   2736 C  C     . SER B 1 31  ? -34.031 26.013  -56.295 1.00 22.15  ? 11  SER B C     1 
ATOM   2737 O  O     . SER B 1 31  ? -35.142 25.872  -55.771 1.00 21.89  ? 11  SER B O     1 
ATOM   2738 C  CB    . SER B 1 31  ? -34.226 27.472  -58.307 1.00 27.67  ? 11  SER B CB    1 
ATOM   2739 O  OG    . SER B 1 31  ? -33.543 28.462  -57.553 1.00 27.49  ? 11  SER B OG    1 
ATOM   2740 N  N     . LEU B 1 32  ? -32.905 26.130  -55.597 1.00 21.48  ? 12  LEU B N     1 
ATOM   2741 C  CA    . LEU B 1 32  ? -32.949 26.226  -54.144 1.00 19.30  ? 12  LEU B CA    1 
ATOM   2742 C  C     . LEU B 1 32  ? -33.818 27.395  -53.688 1.00 22.12  ? 12  LEU B C     1 
ATOM   2743 O  O     . LEU B 1 32  ? -34.437 27.320  -52.626 1.00 23.94  ? 12  LEU B O     1 
ATOM   2744 C  CB    . LEU B 1 32  ? -31.525 26.370  -53.586 1.00 21.22  ? 12  LEU B CB    1 
ATOM   2745 C  CG    . LEU B 1 32  ? -31.376 26.539  -52.071 1.00 22.32  ? 12  LEU B CG    1 
ATOM   2746 C  CD1   . LEU B 1 32  ? -31.995 25.367  -51.325 1.00 22.52  ? 12  LEU B CD1   1 
ATOM   2747 C  CD2   . LEU B 1 32  ? -29.905 26.674  -51.687 1.00 26.97  ? 12  LEU B CD2   1 
ATOM   2748 N  N     . ASN B 1 33  ? -33.869 28.483  -54.463 1.00 25.19  ? 13  ASN B N     1 
ATOM   2749 C  CA    . ASN B 1 33  ? -34.722 29.610  -54.086 1.00 28.16  ? 13  ASN B CA    1 
ATOM   2750 C  C     . ASN B 1 33  ? -36.179 29.173  -53.967 1.00 27.53  ? 13  ASN B C     1 
ATOM   2751 O  O     . ASN B 1 33  ? -36.888 29.571  -53.029 1.00 27.32  ? 13  ASN B O     1 
ATOM   2752 C  CB    . ASN B 1 33  ? -34.591 30.741  -55.111 1.00 27.93  ? 13  ASN B CB    1 
ATOM   2753 C  CG    . ASN B 1 33  ? -33.166 31.253  -55.241 1.00 38.05  ? 13  ASN B CG    1 
ATOM   2754 O  OD1   . ASN B 1 33  ? -32.452 31.395  -54.246 1.00 44.42  ? 13  ASN B OD1   1 
ATOM   2755 N  ND2   . ASN B 1 33  ? -32.740 31.522  -56.469 1.00 50.38  ? 13  ASN B ND2   1 
ATOM   2756 N  N     . ASP B 1 34  ? -36.636 28.333  -54.899 1.00 23.13  ? 14  ASP B N     1 
ATOM   2757 C  CA    . ASP B 1 34  ? -38.010 27.841  -54.844 1.00 24.98  ? 14  ASP B CA    1 
ATOM   2758 C  C     . ASP B 1 34  ? -38.212 26.858  -53.701 1.00 23.33  ? 14  ASP B C     1 
ATOM   2759 O  O     . ASP B 1 34  ? -39.298 26.825  -53.106 1.00 24.96  ? 14  ASP B O     1 
ATOM   2760 C  CB    . ASP B 1 34  ? -38.384 27.194  -56.174 1.00 29.51  ? 14  ASP B CB    1 
ATOM   2761 C  CG    . ASP B 1 34  ? -38.492 28.203  -57.294 1.00 36.56  ? 14  ASP B CG    1 
ATOM   2762 O  OD1   . ASP B 1 34  ? -39.158 29.239  -57.081 1.00 50.64  ? 14  ASP B OD1   1 
ATOM   2763 O  OD2   . ASP B 1 34  ? -37.881 27.986  -58.361 1.00 30.18  ? 14  ASP B OD2   1 
ATOM   2764 N  N     . LEU B 1 35  ? -37.192 26.058  -53.372 1.00 21.98  ? 15  LEU B N     1 
ATOM   2765 C  CA    . LEU B 1 35  ? -37.302 25.193  -52.201 1.00 23.80  ? 15  LEU B CA    1 
ATOM   2766 C  C     . LEU B 1 35  ? -37.403 26.018  -50.920 1.00 25.32  ? 15  LEU B C     1 
ATOM   2767 O  O     . LEU B 1 35  ? -38.234 25.730  -50.049 1.00 25.74  ? 15  LEU B O     1 
ATOM   2768 C  CB    . LEU B 1 35  ? -36.113 24.231  -52.142 1.00 20.77  ? 15  LEU B CB    1 
ATOM   2769 C  CG    . LEU B 1 35  ? -36.145 23.082  -53.153 1.00 20.46  ? 15  LEU B CG    1 
ATOM   2770 C  CD1   . LEU B 1 35  ? -34.788 22.366  -53.226 1.00 20.59  ? 15  LEU B CD1   1 
ATOM   2771 C  CD2   . LEU B 1 35  ? -37.242 22.100  -52.791 1.00 23.49  ? 15  LEU B CD2   1 
ATOM   2772 N  N     . LYS B 1 36  ? -36.607 27.082  -50.813 1.00 25.65  ? 16  LYS B N     1 
ATOM   2773 C  CA    . LYS B 1 36  ? -36.647 27.909  -49.612 1.00 23.33  ? 16  LYS B CA    1 
ATOM   2774 C  C     . LYS B 1 36  ? -37.959 28.668  -49.496 1.00 29.06  ? 16  LYS B C     1 
ATOM   2775 O  O     . LYS B 1 36  ? -38.437 28.891  -48.376 1.00 31.42  ? 16  LYS B O     1 
ATOM   2776 C  CB    . LYS B 1 36  ? -35.481 28.901  -49.591 1.00 29.76  ? 16  LYS B CB    1 
ATOM   2777 C  CG    . LYS B 1 36  ? -34.130 28.250  -49.422 1.00 27.31  ? 16  LYS B CG    1 
ATOM   2778 C  CD    . LYS B 1 36  ? -32.984 29.203  -49.741 1.00 36.40  ? 16  LYS B CD    1 
ATOM   2779 C  CE    . LYS B 1 36  ? -32.914 30.331  -48.729 1.00 49.31  ? 16  LYS B CE    1 
ATOM   2780 N  NZ    . LYS B 1 36  ? -31.714 31.190  -48.949 1.00 64.39  ? 16  LYS B NZ    1 
ATOM   2781 N  N     . ASN B 1 37  ? -38.561 29.057  -50.625 1.00 26.06  ? 17  ASN B N     1 
ATOM   2782 C  CA    . ASN B 1 37  ? -39.787 29.844  -50.599 1.00 29.17  ? 17  ASN B CA    1 
ATOM   2783 C  C     . ASN B 1 37  ? -41.045 28.999  -50.562 1.00 26.91  ? 17  ASN B C     1 
ATOM   2784 O  O     . ASN B 1 37  ? -42.134 29.560  -50.408 1.00 32.40  ? 17  ASN B O     1 
ATOM   2785 C  CB    . ASN B 1 37  ? -39.900 30.723  -51.846 1.00 39.09  ? 17  ASN B CB    1 
ATOM   2786 C  CG    . ASN B 1 37  ? -38.958 31.885  -51.833 1.00 37.79  ? 17  ASN B CG    1 
ATOM   2787 O  OD1   . ASN B 1 37  ? -38.193 32.081  -50.887 1.00 38.12  ? 17  ASN B OD1   1 
ATOM   2788 N  ND2   . ASN B 1 37  ? -38.988 32.664  -52.914 1.00 39.72  ? 17  ASN B ND2   1 
ATOM   2789 N  N     . GLY B 1 38  ? -40.927 27.678  -50.670 1.00 24.86  ? 18  GLY B N     1 
ATOM   2790 C  CA    . GLY B 1 38  ? -42.105 26.835  -50.683 1.00 23.79  ? 18  GLY B CA    1 
ATOM   2791 C  C     . GLY B 1 38  ? -42.883 26.902  -51.975 1.00 28.50  ? 18  GLY B C     1 
ATOM   2792 O  O     . GLY B 1 38  ? -44.088 26.631  -51.983 1.00 32.37  ? 18  GLY B O     1 
ATOM   2793 N  N     . THR B 1 39  ? -42.232 27.289  -53.069 1.00 30.49  ? 19  THR B N     1 
ATOM   2794 C  CA    . THR B 1 39  ? -42.891 27.457  -54.359 1.00 31.35  ? 19  THR B CA    1 
ATOM   2795 C  C     . THR B 1 39  ? -42.438 26.452  -55.411 1.00 34.84  ? 19  THR B C     1 
ATOM   2796 O  O     . THR B 1 39  ? -42.727 26.649  -56.596 1.00 29.60  ? 19  THR B O     1 
ATOM   2797 C  CB    . THR B 1 39  ? -42.664 28.871  -54.882 1.00 28.83  ? 19  THR B CB    1 
ATOM   2798 O  OG1   . THR B 1 39  ? -41.258 29.097  -54.998 1.00 29.39  ? 19  THR B OG1   1 
ATOM   2799 C  CG2   . THR B 1 39  ? -43.266 29.898  -53.930 1.00 31.03  ? 19  THR B CG2   1 
ATOM   2800 N  N     . VAL B 1 40  ? -41.713 25.396  -55.031 1.00 29.23  ? 20  VAL B N     1 
ATOM   2801 C  CA    . VAL B 1 40  ? -41.329 24.404  -56.030 1.00 26.19  ? 20  VAL B CA    1 
ATOM   2802 C  C     . VAL B 1 40  ? -42.581 23.775  -56.627 1.00 30.34  ? 20  VAL B C     1 
ATOM   2803 O  O     . VAL B 1 40  ? -43.586 23.542  -55.936 1.00 30.26  ? 20  VAL B O     1 
ATOM   2804 C  CB    . VAL B 1 40  ? -40.408 23.328  -55.427 1.00 37.66  ? 20  VAL B CB    1 
ATOM   2805 C  CG1   . VAL B 1 40  ? -41.154 22.490  -54.426 1.00 39.91  ? 20  VAL B CG1   1 
ATOM   2806 C  CG2   . VAL B 1 40  ? -39.834 22.446  -56.514 1.00 40.48  ? 20  VAL B CG2   1 
ATOM   2807 N  N     . SER B 1 41  ? -42.541 23.523  -57.932 1.00 27.54  ? 21  SER B N     1 
ATOM   2808 C  CA    . SER B 1 41  ? -43.672 22.903  -58.602 1.00 28.57  ? 21  SER B CA    1 
ATOM   2809 C  C     . SER B 1 41  ? -43.832 21.462  -58.131 1.00 30.99  ? 21  SER B C     1 
ATOM   2810 O  O     . SER B 1 41  ? -42.893 20.671  -58.217 1.00 27.65  ? 21  SER B O     1 
ATOM   2811 C  CB    . SER B 1 41  ? -43.473 22.938  -60.117 1.00 31.46  ? 21  SER B CB    1 
ATOM   2812 O  OG    . SER B 1 41  ? -44.339 22.015  -60.756 1.00 34.39  ? 21  SER B OG    1 
ATOM   2813 N  N     . LEU B 1 42  ? -45.027 21.118  -57.645 1.00 26.69  ? 22  LEU B N     1 
ATOM   2814 C  CA    . LEU B 1 42  ? -45.295 19.734  -57.260 1.00 29.70  ? 22  LEU B CA    1 
ATOM   2815 C  C     . LEU B 1 42  ? -45.454 18.828  -58.474 1.00 28.37  ? 22  LEU B C     1 
ATOM   2816 O  O     . LEU B 1 42  ? -45.232 17.614  -58.371 1.00 26.84  ? 22  LEU B O     1 
ATOM   2817 C  CB    . LEU B 1 42  ? -46.535 19.662  -56.375 1.00 29.12  ? 22  LEU B CB    1 
ATOM   2818 C  CG    . LEU B 1 42  ? -46.462 20.445  -55.059 1.00 29.51  ? 22  LEU B CG    1 
ATOM   2819 C  CD1   . LEU B 1 42  ? -47.709 20.190  -54.238 1.00 31.10  ? 22  LEU B CD1   1 
ATOM   2820 C  CD2   . LEU B 1 42  ? -45.209 20.128  -54.237 1.00 29.78  ? 22  LEU B CD2   1 
ATOM   2821 N  N     . GLU B 1 43  ? -45.837 19.391  -59.620 1.00 26.37  ? 23  GLU B N     1 
ATOM   2822 C  CA    A GLU B 1 43  ? -45.801 18.625  -60.856 0.48 26.92  ? 23  GLU B CA    1 
ATOM   2823 C  CA    B GLU B 1 43  ? -45.798 18.626  -60.861 0.52 26.91  ? 23  GLU B CA    1 
ATOM   2824 C  C     . GLU B 1 43  ? -44.369 18.219  -61.196 1.00 24.94  ? 23  GLU B C     1 
ATOM   2825 O  O     . GLU B 1 43  ? -44.108 17.064  -61.556 1.00 26.54  ? 23  GLU B O     1 
ATOM   2826 C  CB    A GLU B 1 43  ? -46.445 19.442  -61.979 0.48 25.94  ? 23  GLU B CB    1 
ATOM   2827 C  CB    B GLU B 1 43  ? -46.414 19.436  -62.006 0.52 25.93  ? 23  GLU B CB    1 
ATOM   2828 C  CG    A GLU B 1 43  ? -47.961 19.662  -61.807 0.48 29.84  ? 23  GLU B CG    1 
ATOM   2829 C  CG    B GLU B 1 43  ? -46.540 18.655  -63.304 0.52 32.09  ? 23  GLU B CG    1 
ATOM   2830 C  CD    A GLU B 1 43  ? -48.340 20.600  -60.652 0.48 36.55  ? 23  GLU B CD    1 
ATOM   2831 C  CD    B GLU B 1 43  ? -47.128 19.471  -64.442 0.52 40.95  ? 23  GLU B CD    1 
ATOM   2832 O  OE1   A GLU B 1 43  ? -47.505 21.426  -60.224 0.48 32.64  ? 23  GLU B OE1   1 
ATOM   2833 O  OE1   B GLU B 1 43  ? -47.308 20.699  -64.280 0.52 38.67  ? 23  GLU B OE1   1 
ATOM   2834 O  OE2   A GLU B 1 43  ? -49.491 20.506  -60.170 0.48 36.14  ? 23  GLU B OE2   1 
ATOM   2835 O  OE2   B GLU B 1 43  ? -47.409 18.876  -65.503 0.52 40.52  ? 23  GLU B OE2   1 
ATOM   2836 N  N     . ALA B 1 44  ? -43.423 19.152  -61.061 1.00 26.49  ? 24  ALA B N     1 
ATOM   2837 C  CA    . ALA B 1 44  ? -42.020 18.818  -61.293 1.00 25.59  ? 24  ALA B CA    1 
ATOM   2838 C  C     . ALA B 1 44  ? -41.512 17.824  -60.257 1.00 24.00  ? 24  ALA B C     1 
ATOM   2839 O  O     . ALA B 1 44  ? -40.739 16.916  -60.589 1.00 22.51  ? 24  ALA B O     1 
ATOM   2840 C  CB    . ALA B 1 44  ? -41.164 20.083  -61.275 1.00 29.18  ? 24  ALA B CB    1 
ATOM   2841 N  N     . LEU B 1 45  ? -41.930 17.978  -58.997 1.00 21.41  ? 25  LEU B N     1 
ATOM   2842 C  CA    . LEU B 1 45  ? -41.472 17.050  -57.965 1.00 22.09  ? 25  LEU B CA    1 
ATOM   2843 C  C     . LEU B 1 45  ? -41.946 15.637  -58.272 1.00 22.84  ? 25  LEU B C     1 
ATOM   2844 O  O     . LEU B 1 45  ? -41.178 14.673  -58.158 1.00 20.79  ? 25  LEU B O     1 
ATOM   2845 C  CB    . LEU B 1 45  ? -41.959 17.503  -56.581 1.00 22.92  ? 25  LEU B CB    1 
ATOM   2846 C  CG    . LEU B 1 45  ? -41.361 16.773  -55.371 1.00 23.87  ? 25  LEU B CG    1 
ATOM   2847 C  CD1   . LEU B 1 45  ? -39.882 17.134  -55.182 1.00 21.35  ? 25  LEU B CD1   1 
ATOM   2848 C  CD2   . LEU B 1 45  ? -42.154 17.088  -54.095 1.00 22.82  ? 25  LEU B CD2   1 
ATOM   2849 N  N     . GLU B 1 46  ? -43.205 15.492  -58.689 1.00 19.81  ? 26  GLU B N     1 
ATOM   2850 C  CA    . GLU B 1 46  ? -43.678 14.167  -59.064 1.00 21.08  ? 26  GLU B CA    1 
ATOM   2851 C  C     . GLU B 1 46  ? -42.992 13.670  -60.332 1.00 20.61  ? 26  GLU B C     1 
ATOM   2852 O  O     . GLU B 1 46  ? -42.755 12.461  -60.477 1.00 22.08  ? 26  GLU B O     1 
ATOM   2853 C  CB    . GLU B 1 46  ? -45.197 14.182  -59.226 1.00 23.84  ? 26  GLU B CB    1 
ATOM   2854 C  CG    . GLU B 1 46  ? -45.810 12.791  -59.283 1.00 23.58  ? 26  GLU B CG    1 
ATOM   2855 C  CD    . GLU B 1 46  ? -45.739 12.145  -60.649 1.00 31.51  ? 26  GLU B CD    1 
ATOM   2856 O  OE1   . GLU B 1 46  ? -45.619 12.871  -61.665 1.00 31.68  ? 26  GLU B OE1   1 
ATOM   2857 O  OE2   . GLU B 1 46  ? -45.791 10.897  -60.702 1.00 34.39  ? 26  GLU B OE2   1 
ATOM   2858 N  N     . GLU B 1 47  ? -42.646 14.578  -61.253 1.00 20.91  ? 27  GLU B N     1 
ATOM   2859 C  CA    . GLU B 1 47  ? -41.898 14.159  -62.433 1.00 20.20  ? 27  GLU B CA    1 
ATOM   2860 C  C     . GLU B 1 47  ? -40.520 13.630  -62.053 1.00 19.76  ? 27  GLU B C     1 
ATOM   2861 O  O     . GLU B 1 47  ? -40.005 12.723  -62.715 1.00 20.25  ? 27  GLU B O     1 
ATOM   2862 C  CB    . GLU B 1 47  ? -41.777 15.329  -63.405 1.00 21.17  ? 27  GLU B CB    1 
ATOM   2863 C  CG    . GLU B 1 47  ? -41.124 14.996  -64.724 1.00 30.19  ? 27  GLU B CG    1 
ATOM   2864 C  CD    . GLU B 1 47  ? -41.128 16.179  -65.674 1.00 52.92  ? 27  GLU B CD    1 
ATOM   2865 O  OE1   . GLU B 1 47  ? -41.867 17.149  -65.397 1.00 50.32  ? 27  GLU B OE1   1 
ATOM   2866 O  OE2   . GLU B 1 47  ? -40.397 16.143  -66.689 1.00 53.24  ? 27  GLU B OE2   1 
ATOM   2867 N  N     . ALA B 1 48  ? -39.947 14.147  -60.964 1.00 18.83  ? 28  ALA B N     1 
ATOM   2868 C  CA    . ALA B 1 48  ? -38.623 13.718  -60.508 1.00 19.40  ? 28  ALA B CA    1 
ATOM   2869 C  C     . ALA B 1 48  ? -38.668 12.450  -59.667 1.00 19.57  ? 28  ALA B C     1 
ATOM   2870 O  O     . ALA B 1 48  ? -37.721 11.653  -59.704 1.00 18.93  ? 28  ALA B O     1 
ATOM   2871 C  CB    . ALA B 1 48  ? -37.973 14.827  -59.680 1.00 18.98  ? 28  ALA B CB    1 
ATOM   2872 N  N     . PHE B 1 49  ? -39.749 12.241  -58.904 1.00 17.95  ? 29  PHE B N     1 
ATOM   2873 C  CA    . PHE B 1 49  ? -39.770 11.226  -57.858 1.00 17.84  ? 29  PHE B CA    1 
ATOM   2874 C  C     . PHE B 1 49  ? -40.885 10.186  -58.002 1.00 20.38  ? 29  PHE B C     1 
ATOM   2875 O  O     . PHE B 1 49  ? -40.906 9.225   -57.224 1.00 19.86  ? 29  PHE B O     1 
ATOM   2876 C  CB    . PHE B 1 49  ? -39.928 11.890  -56.473 1.00 17.71  ? 29  PHE B CB    1 
ATOM   2877 C  CG    . PHE B 1 49  ? -38.692 12.595  -55.935 1.00 18.38  ? 29  PHE B CG    1 
ATOM   2878 C  CD1   . PHE B 1 49  ? -37.422 12.400  -56.477 1.00 17.22  ? 29  PHE B CD1   1 
ATOM   2879 C  CD2   . PHE B 1 49  ? -38.821 13.407  -54.816 1.00 19.49  ? 29  PHE B CD2   1 
ATOM   2880 C  CE1   . PHE B 1 49  ? -36.318 13.031  -55.908 1.00 20.51  ? 29  PHE B CE1   1 
ATOM   2881 C  CE2   . PHE B 1 49  ? -37.718 14.034  -54.242 1.00 19.37  ? 29  PHE B CE2   1 
ATOM   2882 C  CZ    . PHE B 1 49  ? -36.473 13.852  -54.801 1.00 17.41  ? 29  PHE B CZ    1 
ATOM   2883 N  N     . GLY B 1 50  ? -41.795 10.337  -58.972 1.00 20.53  ? 30  GLY B N     1 
ATOM   2884 C  CA    . GLY B 1 50  ? -42.957 9.471   -59.082 1.00 20.97  ? 30  GLY B CA    1 
ATOM   2885 C  C     . GLY B 1 50  ? -42.646 8.117   -59.689 1.00 22.45  ? 30  GLY B C     1 
ATOM   2886 O  O     . GLY B 1 50  ? -41.500 7.775   -60.009 1.00 21.02  ? 30  GLY B O     1 
ATOM   2887 N  N     . PRO B 1 51  ? -43.699 7.313   -59.853 1.00 22.52  ? 31  PRO B N     1 
ATOM   2888 C  CA    . PRO B 1 51  ? -43.511 5.924   -60.306 1.00 22.30  ? 31  PRO B CA    1 
ATOM   2889 C  C     . PRO B 1 51  ? -42.865 5.788   -61.674 1.00 19.62  ? 31  PRO B C     1 
ATOM   2890 O  O     . PRO B 1 51  ? -42.196 4.780   -61.926 1.00 24.41  ? 31  PRO B O     1 
ATOM   2891 C  CB    . PRO B 1 51  ? -44.946 5.374   -60.320 1.00 26.30  ? 31  PRO B CB    1 
ATOM   2892 C  CG    . PRO B 1 51  ? -45.692 6.249   -59.352 1.00 30.73  ? 31  PRO B CG    1 
ATOM   2893 C  CD    . PRO B 1 51  ? -45.116 7.614   -59.566 1.00 26.09  ? 31  PRO B CD    1 
ATOM   2894 N  N     . ASP B 1 52  ? -43.035 6.764   -62.562 1.00 22.51  ? 32  ASP B N     1 
ATOM   2895 C  CA    . ASP B 1 52  ? -42.427 6.734   -63.886 1.00 24.79  ? 32  ASP B CA    1 
ATOM   2896 C  C     . ASP B 1 52  ? -41.147 7.553   -63.956 1.00 19.49  ? 32  ASP B C     1 
ATOM   2897 O  O     . ASP B 1 52  ? -40.601 7.746   -65.046 1.00 23.22  ? 32  ASP B O     1 
ATOM   2898 C  CB    . ASP B 1 52  ? -43.416 7.252   -64.924 1.00 24.43  ? 32  ASP B CB    1 
ATOM   2899 C  CG    . ASP B 1 52  ? -44.645 6.386   -65.020 1.00 32.74  ? 32  ASP B CG    1 
ATOM   2900 O  OD1   . ASP B 1 52  ? -44.490 5.150   -65.050 1.00 39.26  ? 32  ASP B OD1   1 
ATOM   2901 O  OD2   . ASP B 1 52  ? -45.759 6.942   -65.028 1.00 40.34  ? 32  ASP B OD2   1 
ATOM   2902 N  N     . SER B 1 53  ? -40.631 7.992   -62.814 1.00 21.52  ? 33  SER B N     1 
ATOM   2903 C  CA    . SER B 1 53  ? -39.545 8.951   -62.783 1.00 20.42  ? 33  SER B CA    1 
ATOM   2904 C  C     . SER B 1 53  ? -38.184 8.266   -62.789 1.00 21.40  ? 33  SER B C     1 
ATOM   2905 O  O     . SER B 1 53  ? -38.061 7.040   -62.731 1.00 19.12  ? 33  SER B O     1 
ATOM   2906 C  CB    . SER B 1 53  ? -39.655 9.822   -61.537 1.00 19.39  ? 33  SER B CB    1 
ATOM   2907 O  OG    . SER B 1 53  ? -39.274 9.064   -60.394 1.00 18.20  ? 33  SER B OG    1 
ATOM   2908 N  N     . LEU B 1 54  ? -37.145 9.096   -62.806 1.00 18.56  ? 34  LEU B N     1 
ATOM   2909 C  CA    . LEU B 1 54  ? -35.775 8.655   -62.615 1.00 18.42  ? 34  LEU B CA    1 
ATOM   2910 C  C     . LEU B 1 54  ? -35.388 8.581   -61.142 1.00 18.88  ? 34  LEU B C     1 
ATOM   2911 O  O     . LEU B 1 54  ? -34.271 8.149   -60.833 1.00 19.00  ? 34  LEU B O     1 
ATOM   2912 C  CB    . LEU B 1 54  ? -34.824 9.610   -63.336 1.00 18.74  ? 34  LEU B CB    1 
ATOM   2913 C  CG    . LEU B 1 54  ? -34.992 9.714   -64.849 1.00 20.13  ? 34  LEU B CG    1 
ATOM   2914 C  CD1   . LEU B 1 54  ? -34.106 10.849  -65.395 1.00 19.22  ? 34  LEU B CD1   1 
ATOM   2915 C  CD2   . LEU B 1 54  ? -34.668 8.386   -65.520 1.00 21.06  ? 34  LEU B CD2   1 
ATOM   2916 N  N     . GLY B 1 55  ? -36.290 8.964   -60.239 1.00 17.78  ? 35  GLY B N     1 
ATOM   2917 C  CA    . GLY B 1 55  ? -36.008 8.919   -58.816 1.00 18.10  ? 35  GLY B CA    1 
ATOM   2918 C  C     . GLY B 1 55  ? -34.892 9.841   -58.378 1.00 17.26  ? 35  GLY B C     1 
ATOM   2919 O  O     . GLY B 1 55  ? -34.195 9.532   -57.403 1.00 17.90  ? 35  GLY B O     1 
ATOM   2920 N  N     . ILE B 1 56  ? -34.713 10.976  -59.054 1.00 17.40  ? 36  ILE B N     1 
ATOM   2921 C  CA    . ILE B 1 56  ? -33.614 11.889  -58.734 1.00 17.08  ? 36  ILE B CA    1 
ATOM   2922 C  C     . ILE B 1 56  ? -34.055 13.308  -59.060 1.00 17.75  ? 36  ILE B C     1 
ATOM   2923 O  O     . ILE B 1 56  ? -34.778 13.545  -60.034 1.00 17.92  ? 36  ILE B O     1 
ATOM   2924 C  CB    . ILE B 1 56  ? -32.310 11.506  -59.481 1.00 17.14  ? 36  ILE B CB    1 
ATOM   2925 C  CG1   . ILE B 1 56  ? -31.135 12.341  -58.954 1.00 17.07  ? 36  ILE B CG1   1 
ATOM   2926 C  CG2   . ILE B 1 56  ? -32.466 11.627  -61.008 1.00 17.46  ? 36  ILE B CG2   1 
ATOM   2927 C  CD1   . ILE B 1 56  ? -29.761 11.810  -59.406 1.00 17.38  ? 36  ILE B CD1   1 
ATOM   2928 N  N     . LEU B 1 57  ? -33.597 14.250  -58.233 1.00 17.98  ? 37  LEU B N     1 
ATOM   2929 C  CA    . LEU B 1 57  ? -33.880 15.672  -58.367 1.00 17.03  ? 37  LEU B CA    1 
ATOM   2930 C  C     . LEU B 1 57  ? -32.568 16.442  -58.261 1.00 18.32  ? 37  LEU B C     1 
ATOM   2931 O  O     . LEU B 1 57  ? -31.812 16.228  -57.315 1.00 19.05  ? 37  LEU B O     1 
ATOM   2932 C  CB    . LEU B 1 57  ? -34.853 16.118  -57.254 1.00 17.93  ? 37  LEU B CB    1 
ATOM   2933 C  CG    . LEU B 1 57  ? -35.197 17.604  -57.181 1.00 20.35  ? 37  LEU B CG    1 
ATOM   2934 C  CD1   . LEU B 1 57  ? -36.175 17.981  -58.310 1.00 22.14  ? 37  LEU B CD1   1 
ATOM   2935 C  CD2   . LEU B 1 57  ? -35.792 17.981  -55.817 1.00 24.77  ? 37  LEU B CD2   1 
ATOM   2936 N  N     . VAL B 1 58  ? -32.284 17.318  -59.221 1.00 17.13  ? 38  VAL B N     1 
ATOM   2937 C  CA    . VAL B 1 58  ? -31.093 18.172  -59.158 1.00 17.09  ? 38  VAL B CA    1 
ATOM   2938 C  C     . VAL B 1 58  ? -31.506 19.541  -58.629 1.00 19.73  ? 38  VAL B C     1 
ATOM   2939 O  O     . VAL B 1 58  ? -32.487 20.128  -59.103 1.00 20.95  ? 38  VAL B O     1 
ATOM   2940 C  CB    . VAL B 1 58  ? -30.407 18.295  -60.532 1.00 19.36  ? 38  VAL B CB    1 
ATOM   2941 C  CG1   . VAL B 1 58  ? -29.296 19.345  -60.499 1.00 20.21  ? 38  VAL B CG1   1 
ATOM   2942 C  CG2   . VAL B 1 58  ? -29.822 16.962  -60.969 1.00 18.78  ? 38  VAL B CG2   1 
ATOM   2943 N  N     . VAL B 1 59  ? -30.757 20.057  -57.664 1.00 17.64  ? 39  VAL B N     1 
ATOM   2944 C  CA    . VAL B 1 59  ? -30.995 21.362  -57.058 1.00 19.39  ? 39  VAL B CA    1 
ATOM   2945 C  C     . VAL B 1 59  ? -29.857 22.284  -57.478 1.00 18.36  ? 39  VAL B C     1 
ATOM   2946 O  O     . VAL B 1 59  ? -28.677 22.000  -57.195 1.00 18.01  ? 39  VAL B O     1 
ATOM   2947 C  CB    . VAL B 1 59  ? -31.092 21.267  -55.528 1.00 18.72  ? 39  VAL B CB    1 
ATOM   2948 C  CG1   . VAL B 1 59  ? -31.262 22.659  -54.910 1.00 20.46  ? 39  VAL B CG1   1 
ATOM   2949 C  CG2   . VAL B 1 59  ? -32.213 20.313  -55.110 1.00 18.61  ? 39  VAL B CG2   1 
ATOM   2950 N  N     . LYS B 1 60  ? -30.220 23.378  -58.155 1.00 19.37  ? 40  LYS B N     1 
ATOM   2951 C  CA    . LYS B 1 60  ? -29.297 24.413  -58.617 1.00 19.60  ? 40  LYS B CA    1 
ATOM   2952 C  C     . LYS B 1 60  ? -29.418 25.656  -57.733 1.00 23.18  ? 40  LYS B C     1 
ATOM   2953 O  O     . LYS B 1 60  ? -30.227 25.708  -56.804 1.00 20.84  ? 40  LYS B O     1 
ATOM   2954 C  CB    . LYS B 1 60  ? -29.557 24.746  -60.095 1.00 19.70  ? 40  LYS B CB    1 
ATOM   2955 C  CG    . LYS B 1 60  ? -30.895 25.415  -60.368 1.00 23.60  ? 40  LYS B CG    1 
ATOM   2956 C  CD    . LYS B 1 60  ? -31.036 25.797  -61.848 1.00 26.94  ? 40  LYS B CD    1 
ATOM   2957 C  CE    . LYS B 1 60  ? -32.322 26.575  -62.070 1.00 36.27  ? 40  LYS B CE    1 
ATOM   2958 N  NZ    . LYS B 1 60  ? -32.514 26.978  -63.493 1.00 42.91  ? 40  LYS B NZ    1 
ATOM   2959 N  N     . ASP B 1 61  ? -28.582 26.663  -58.020 1.00 19.63  ? 41  ASP B N     1 
ATOM   2960 C  CA    . ASP B 1 61  ? -28.547 27.906  -57.231 1.00 25.77  ? 41  ASP B CA    1 
ATOM   2961 C  C     . ASP B 1 61  ? -28.202 27.631  -55.768 1.00 23.79  ? 41  ASP B C     1 
ATOM   2962 O  O     . ASP B 1 61  ? -28.773 28.231  -54.853 1.00 25.32  ? 41  ASP B O     1 
ATOM   2963 C  CB    . ASP B 1 61  ? -29.877 28.666  -57.333 1.00 28.03  ? 41  ASP B CB    1 
ATOM   2964 C  CG    . ASP B 1 61  ? -30.201 29.088  -58.752 1.00 30.47  ? 41  ASP B CG    1 
ATOM   2965 O  OD1   . ASP B 1 61  ? -29.300 29.593  -59.445 1.00 31.47  ? 41  ASP B OD1   1 
ATOM   2966 O  OD2   . ASP B 1 61  ? -31.355 28.882  -59.184 1.00 32.21  ? 41  ASP B OD2   1 
ATOM   2967 N  N     . VAL B 1 62  ? -27.246 26.733  -55.536 1.00 22.71  ? 42  VAL B N     1 
ATOM   2968 C  CA    . VAL B 1 62  ? -26.918 26.288  -54.183 1.00 20.73  ? 42  VAL B CA    1 
ATOM   2969 C  C     . VAL B 1 62  ? -26.068 27.356  -53.498 1.00 25.16  ? 42  VAL B C     1 
ATOM   2970 O  O     . VAL B 1 62  ? -25.544 28.243  -54.186 1.00 24.90  ? 42  VAL B O     1 
ATOM   2971 C  CB    . VAL B 1 62  ? -26.213 24.919  -54.212 1.00 26.28  ? 42  VAL B CB    1 
ATOM   2972 C  CG1   . VAL B 1 62  ? -27.113 23.870  -54.897 1.00 25.42  ? 42  VAL B CG1   1 
ATOM   2973 C  CG2   . VAL B 1 62  ? -24.871 25.027  -54.897 1.00 31.23  ? 42  VAL B CG2   1 
ATOM   2974 N  N     . PRO B 1 63  ? -25.906 27.324  -52.166 1.00 24.03  ? 43  PRO B N     1 
ATOM   2975 C  CA    . PRO B 1 63  ? -25.129 28.376  -51.495 1.00 28.90  ? 43  PRO B CA    1 
ATOM   2976 C  C     . PRO B 1 63  ? -23.708 28.481  -52.033 1.00 33.90  ? 43  PRO B C     1 
ATOM   2977 O  O     . PRO B 1 63  ? -23.112 27.503  -52.492 1.00 25.27  ? 43  PRO B O     1 
ATOM   2978 C  CB    . PRO B 1 63  ? -25.132 27.940  -50.025 1.00 31.99  ? 43  PRO B CB    1 
ATOM   2979 C  CG    . PRO B 1 63  ? -26.346 27.073  -49.883 1.00 31.73  ? 43  PRO B CG    1 
ATOM   2980 C  CD    . PRO B 1 63  ? -26.438 26.345  -51.193 1.00 26.43  ? 43  PRO B CD    1 
ATOM   2981 N  N     . ALA B 1 64  ? -23.162 29.696  -51.958 1.00 32.11  ? 44  ALA B N     1 
ATOM   2982 C  CA    . ALA B 1 64  ? -21.848 29.951  -52.542 1.00 27.63  ? 44  ALA B CA    1 
ATOM   2983 C  C     . ALA B 1 64  ? -20.763 29.084  -51.908 1.00 27.87  ? 44  ALA B C     1 
ATOM   2984 O  O     . ALA B 1 64  ? -19.765 28.758  -52.561 1.00 32.87  ? 44  ALA B O     1 
ATOM   2985 C  CB    . ALA B 1 64  ? -21.495 31.431  -52.398 1.00 40.62  ? 44  ALA B CB    1 
ATOM   2986 N  N     . GLU B 1 65  ? -20.925 28.717  -50.639 1.00 26.29  ? 45  GLU B N     1 
ATOM   2987 C  CA    . GLU B 1 65  ? -19.908 27.924  -49.956 1.00 26.07  ? 45  GLU B CA    1 
ATOM   2988 C  C     . GLU B 1 65  ? -19.865 26.465  -50.415 1.00 22.74  ? 45  GLU B C     1 
ATOM   2989 O  O     . GLU B 1 65  ? -18.905 25.762  -50.066 1.00 23.77  ? 45  GLU B O     1 
ATOM   2990 C  CB    . GLU B 1 65  ? -20.133 27.998  -48.438 1.00 30.38  ? 45  GLU B CB    1 
ATOM   2991 C  CG    . GLU B 1 65  ? -21.462 27.442  -47.963 1.00 42.92  ? 45  GLU B CG    1 
ATOM   2992 C  CD    . GLU B 1 65  ? -22.525 28.511  -47.745 1.00 61.24  ? 45  GLU B CD    1 
ATOM   2993 O  OE1   . GLU B 1 65  ? -22.440 29.586  -48.382 1.00 42.14  ? 45  GLU B OE1   1 
ATOM   2994 O  OE2   . GLU B 1 65  ? -23.449 28.269  -46.934 1.00 61.40  ? 45  GLU B OE2   1 
ATOM   2995 N  N     . PHE B 1 66  ? -20.869 25.983  -51.161 1.00 21.91  ? 46  PHE B N     1 
ATOM   2996 C  CA    . PHE B 1 66  ? -20.907 24.562  -51.515 1.00 21.24  ? 46  PHE B CA    1 
ATOM   2997 C  C     . PHE B 1 66  ? -19.680 24.137  -52.322 1.00 19.50  ? 46  PHE B C     1 
ATOM   2998 O  O     . PHE B 1 66  ? -19.042 23.122  -52.007 1.00 21.47  ? 46  PHE B O     1 
ATOM   2999 C  CB    . PHE B 1 66  ? -22.182 24.223  -52.293 1.00 18.91  ? 46  PHE B CB    1 
ATOM   3000 C  CG    . PHE B 1 66  ? -22.154 22.839  -52.913 1.00 19.48  ? 46  PHE B CG    1 
ATOM   3001 C  CD1   . PHE B 1 66  ? -22.299 21.706  -52.121 1.00 17.45  ? 46  PHE B CD1   1 
ATOM   3002 C  CD2   . PHE B 1 66  ? -21.950 22.677  -54.287 1.00 22.42  ? 46  PHE B CD2   1 
ATOM   3003 C  CE1   . PHE B 1 66  ? -22.254 20.424  -52.683 1.00 16.51  ? 46  PHE B CE1   1 
ATOM   3004 C  CE2   . PHE B 1 66  ? -21.908 21.412  -54.855 1.00 21.90  ? 46  PHE B CE2   1 
ATOM   3005 C  CZ    . PHE B 1 66  ? -22.060 20.281  -54.052 1.00 17.58  ? 46  PHE B CZ    1 
ATOM   3006 N  N     . ALA B 1 67  ? -19.345 24.884  -53.384 1.00 20.41  ? 47  ALA B N     1 
ATOM   3007 C  CA    . ALA B 1 67  ? -18.293 24.424  -54.294 1.00 17.67  ? 47  ALA B CA    1 
ATOM   3008 C  C     . ALA B 1 67  ? -16.982 24.181  -53.551 1.00 21.53  ? 47  ALA B C     1 
ATOM   3009 O  O     . ALA B 1 67  ? -16.383 23.097  -53.655 1.00 21.09  ? 47  ALA B O     1 
ATOM   3010 C  CB    . ALA B 1 67  ? -18.102 25.427  -55.437 1.00 24.20  ? 47  ALA B CB    1 
ATOM   3011 N  N     . GLU B 1 68  ? -16.580 25.133  -52.709 1.00 20.90  ? 48  GLU B N     1 
ATOM   3012 C  CA    . GLU B 1 68  ? -15.326 24.949  -51.990 1.00 22.05  ? 48  GLU B CA    1 
ATOM   3013 C  C     . GLU B 1 68  ? -15.423 23.776  -51.021 1.00 20.12  ? 48  GLU B C     1 
ATOM   3014 O  O     . GLU B 1 68  ? -14.510 22.936  -50.962 1.00 21.76  ? 48  GLU B O     1 
ATOM   3015 C  CB    . GLU B 1 68  ? -14.933 26.231  -51.249 1.00 26.38  ? 48  GLU B CB    1 
ATOM   3016 C  CG    . GLU B 1 68  ? -13.579 26.117  -50.536 1.00 33.73  ? 48  GLU B CG    1 
ATOM   3017 C  CD    . GLU B 1 68  ? -13.205 27.373  -49.762 1.00 60.67  ? 48  GLU B CD    1 
ATOM   3018 O  OE1   . GLU B 1 68  ? -13.706 28.465  -50.110 1.00 55.42  ? 48  GLU B OE1   1 
ATOM   3019 O  OE2   . GLU B 1 68  ? -12.418 27.260  -48.794 1.00 60.35  ? 48  GLU B OE2   1 
ATOM   3020 N  N     . LEU B 1 69  ? -16.558 23.644  -50.320 1.00 18.25  ? 49  LEU B N     1 
ATOM   3021 C  CA    . LEU B 1 69  ? -16.687 22.536  -49.383 1.00 17.21  ? 49  LEU B CA    1 
ATOM   3022 C  C     . LEU B 1 69  ? -16.627 21.205  -50.124 1.00 16.01  ? 49  LEU B C     1 
ATOM   3023 O  O     . LEU B 1 69  ? -15.951 20.265  -49.675 1.00 17.25  ? 49  LEU B O     1 
ATOM   3024 C  CB    . LEU B 1 69  ? -17.996 22.651  -48.594 1.00 17.45  ? 49  LEU B CB    1 
ATOM   3025 C  CG    . LEU B 1 69  ? -18.002 23.694  -47.463 1.00 19.71  ? 49  LEU B CG    1 
ATOM   3026 C  CD1   . LEU B 1 69  ? -19.402 23.867  -46.871 1.00 19.71  ? 49  LEU B CD1   1 
ATOM   3027 C  CD2   . LEU B 1 69  ? -17.026 23.271  -46.360 1.00 22.56  ? 49  LEU B CD2   1 
ATOM   3028 N  N     . ARG B 1 70  ? -17.314 21.115  -51.276 1.00 17.35  ? 50  ARG B N     1 
ATOM   3029 C  CA    . ARG B 1 70  ? -17.267 19.871  -52.040 1.00 16.10  ? 50  ARG B CA    1 
ATOM   3030 C  C     . ARG B 1 70  ? -15.835 19.560  -52.429 1.00 18.88  ? 50  ARG B C     1 
ATOM   3031 O  O     . ARG B 1 70  ? -15.317 18.458  -52.165 1.00 17.15  ? 50  ARG B O     1 
ATOM   3032 C  CB    . ARG B 1 70  ? -18.165 19.978  -53.281 1.00 16.26  ? 50  ARG B CB    1 
ATOM   3033 C  CG    . ARG B 1 70  ? -17.980 18.802  -54.246 1.00 18.13  ? 50  ARG B CG    1 
ATOM   3034 C  CD    . ARG B 1 70  ? -18.599 19.068  -55.642 1.00 17.89  ? 50  ARG B CD    1 
ATOM   3035 N  NE    . ARG B 1 70  ? -18.147 18.053  -56.581 1.00 18.28  ? 50  ARG B NE    1 
ATOM   3036 C  CZ    . ARG B 1 70  ? -16.958 18.080  -57.169 1.00 19.03  ? 50  ARG B CZ    1 
ATOM   3037 N  NH1   . ARG B 1 70  ? -16.117 19.087  -56.971 1.00 19.67  ? 50  ARG B NH1   1 
ATOM   3038 N  NH2   . ARG B 1 70  ? -16.599 17.070  -57.964 1.00 18.08  ? 50  ARG B NH2   1 
ATOM   3039 N  N     . HIS B 1 71  ? -15.151 20.569  -52.972 1.00 16.49  ? 51  HIS B N     1 
ATOM   3040 C  CA    . HIS B 1 71  ? -13.798 20.347  -53.447 1.00 18.16  ? 51  HIS B CA    1 
ATOM   3041 C  C     . HIS B 1 71  ? -12.903 19.920  -52.295 1.00 19.18  ? 51  HIS B C     1 
ATOM   3042 O  O     . HIS B 1 71  ? -12.084 18.999  -52.443 1.00 19.74  ? 51  HIS B O     1 
ATOM   3043 C  CB    . HIS B 1 71  ? -13.286 21.601  -54.129 1.00 18.98  ? 51  HIS B CB    1 
ATOM   3044 C  CG    . HIS B 1 71  ? -11.969 21.414  -54.804 1.00 20.38  ? 51  HIS B CG    1 
ATOM   3045 N  ND1   . HIS B 1 71  ? -11.210 22.473  -55.250 1.00 27.02  ? 51  HIS B ND1   1 
ATOM   3046 C  CD2   . HIS B 1 71  ? -11.294 20.290  -55.142 1.00 20.49  ? 51  HIS B CD2   1 
ATOM   3047 C  CE1   . HIS B 1 71  ? -10.111 22.012  -55.818 1.00 26.78  ? 51  HIS B CE1   1 
ATOM   3048 N  NE2   . HIS B 1 71  ? -10.133 20.693  -55.765 1.00 23.20  ? 51  HIS B NE2   1 
ATOM   3049 N  N     . ARG B 1 72  ? -13.073 20.544  -51.123 1.00 16.86  ? 52  ARG B N     1 
ATOM   3050 C  CA    . ARG B 1 72  ? -12.203 20.181  -50.011 1.00 18.50  ? 52  ARG B CA    1 
ATOM   3051 C  C     . ARG B 1 72  ? -12.510 18.772  -49.521 1.00 18.06  ? 52  ARG B C     1 
ATOM   3052 O  O     . ARG B 1 72  ? -11.590 17.966  -49.307 1.00 18.86  ? 52  ARG B O     1 
ATOM   3053 C  CB    . ARG B 1 72  ? -12.314 21.217  -48.886 1.00 20.38  ? 52  ARG B CB    1 
ATOM   3054 C  CG    . ARG B 1 72  ? -11.722 22.565  -49.326 1.00 25.42  ? 52  ARG B CG    1 
ATOM   3055 C  CD    . ARG B 1 72  ? -11.338 23.512  -48.202 1.00 37.66  ? 52  ARG B CD    1 
ATOM   3056 N  NE    . ARG B 1 72  ? -12.401 23.783  -47.246 1.00 47.78  ? 52  ARG B NE    1 
ATOM   3057 C  CZ    . ARG B 1 72  ? -12.356 23.434  -45.968 1.00 59.10  ? 52  ARG B CZ    1 
ATOM   3058 N  NH1   . ARG B 1 72  ? -11.301 22.814  -45.460 1.00 61.24  ? 52  ARG B NH1   1 
ATOM   3059 N  NH2   . ARG B 1 72  ? -13.385 23.730  -45.176 1.00 44.45  ? 52  ARG B NH2   1 
ATOM   3060 N  N     . LEU B 1 73  ? -13.798 18.431  -49.369 1.00 16.83  ? 53  LEU B N     1 
ATOM   3061 C  CA    . LEU B 1 73  ? -14.082 17.155  -48.715 1.00 15.70  ? 53  LEU B CA    1 
ATOM   3062 C  C     . LEU B 1 73  ? -13.745 15.989  -49.630 1.00 16.56  ? 53  LEU B C     1 
ATOM   3063 O  O     . LEU B 1 73  ? -13.198 14.976  -49.184 1.00 16.58  ? 53  LEU B O     1 
ATOM   3064 C  CB    . LEU B 1 73  ? -15.550 17.072  -48.266 1.00 15.50  ? 53  LEU B CB    1 
ATOM   3065 C  CG    . LEU B 1 73  ? -15.788 15.902  -47.293 1.00 15.27  ? 53  LEU B CG    1 
ATOM   3066 C  CD1   . LEU B 1 73  ? -15.003 16.051  -45.965 1.00 18.95  ? 53  LEU B CD1   1 
ATOM   3067 C  CD2   . LEU B 1 73  ? -17.278 15.698  -47.022 1.00 15.96  ? 53  LEU B CD2   1 
ATOM   3068 N  N     . LEU B 1 74  ? -14.050 16.119  -50.922 1.00 16.89  ? 54  LEU B N     1 
ATOM   3069 C  CA    . LEU B 1 74  ? -13.648 15.070  -51.849 1.00 16.62  ? 54  LEU B CA    1 
ATOM   3070 C  C     . LEU B 1 74  ? -12.121 14.958  -51.904 1.00 18.75  ? 54  LEU B C     1 
ATOM   3071 O  O     . LEU B 1 74  ? -11.585 13.839  -51.974 1.00 19.34  ? 54  LEU B O     1 
ATOM   3072 C  CB    . LEU B 1 74  ? -14.292 15.324  -53.227 1.00 16.81  ? 54  LEU B CB    1 
ATOM   3073 C  CG    . LEU B 1 74  ? -15.832 15.266  -53.214 1.00 16.52  ? 54  LEU B CG    1 
ATOM   3074 C  CD1   . LEU B 1 74  ? -16.410 15.465  -54.612 1.00 17.87  ? 54  LEU B CD1   1 
ATOM   3075 C  CD2   . LEU B 1 74  ? -16.325 13.938  -52.636 1.00 21.22  ? 54  LEU B CD2   1 
ATOM   3076 N  N     . SER B 1 75  ? -11.399 16.080  -51.748 1.00 17.01  ? 55  SER B N     1 
ATOM   3077 C  CA    . SER B 1 75  ? -9.943  15.980  -51.638 1.00 20.11  ? 55  SER B CA    1 
ATOM   3078 C  C     . SER B 1 75  ? -9.541  15.211  -50.387 1.00 18.63  ? 55  SER B C     1 
ATOM   3079 O  O     . SER B 1 75  ? -8.601  14.398  -50.427 1.00 17.57  ? 55  SER B O     1 
ATOM   3080 C  CB    . SER B 1 75  ? -9.306  17.370  -51.624 1.00 20.37  ? 55  SER B CB    1 
ATOM   3081 O  OG    . SER B 1 75  ? -9.455  18.010  -52.878 1.00 21.09  ? 55  SER B OG    1 
ATOM   3082 N  N     . TYR B 1 76  ? -10.246 15.454  -49.268 1.00 17.51  ? 56  TYR B N     1 
ATOM   3083 C  CA    . TYR B 1 76  ? -9.944  14.733  -48.035 1.00 17.82  ? 56  TYR B CA    1 
ATOM   3084 C  C     . TYR B 1 76  ? -10.102 13.234  -48.221 1.00 18.24  ? 56  TYR B C     1 
ATOM   3085 O  O     . TYR B 1 76  ? -9.400  12.460  -47.574 1.00 18.77  ? 56  TYR B O     1 
ATOM   3086 C  CB    . TYR B 1 76  ? -10.832 15.205  -46.879 1.00 18.06  ? 56  TYR B CB    1 
ATOM   3087 C  CG    . TYR B 1 76  ? -10.334 16.461  -46.188 1.00 17.87  ? 56  TYR B CG    1 
ATOM   3088 C  CD1   . TYR B 1 76  ? -9.131  16.468  -45.490 1.00 19.10  ? 56  TYR B CD1   1 
ATOM   3089 C  CD2   . TYR B 1 76  ? -11.086 17.632  -46.210 1.00 19.58  ? 56  TYR B CD2   1 
ATOM   3090 C  CE1   . TYR B 1 76  ? -8.680  17.634  -44.850 1.00 19.84  ? 56  TYR B CE1   1 
ATOM   3091 C  CE2   . TYR B 1 76  ? -10.654 18.786  -45.574 1.00 19.82  ? 56  TYR B CE2   1 
ATOM   3092 C  CZ    . TYR B 1 76  ? -9.448  18.781  -44.904 1.00 21.59  ? 56  TYR B CZ    1 
ATOM   3093 O  OH    . TYR B 1 76  ? -9.029  19.945  -44.293 1.00 21.79  ? 56  TYR B OH    1 
ATOM   3094 N  N     . SER B 1 77  ? -11.006 12.798  -49.114 1.00 16.91  ? 57  SER B N     1 
ATOM   3095 C  CA    . SER B 1 77  ? -11.129 11.361  -49.338 1.00 18.83  ? 57  SER B CA    1 
ATOM   3096 C  C     . SER B 1 77  ? -9.803  10.770  -49.810 1.00 20.74  ? 57  SER B C     1 
ATOM   3097 O  O     . SER B 1 77  ? -9.392  9.693   -49.353 1.00 18.64  ? 57  SER B O     1 
ATOM   3098 C  CB    . SER B 1 77  ? -12.244 11.082  -50.351 1.00 18.27  ? 57  SER B CB    1 
ATOM   3099 O  OG    . SER B 1 77  ? -12.547 9.699   -50.380 1.00 18.52  ? 57  SER B OG    1 
ATOM   3100 N  N     . SER B 1 78  ? -9.108  11.474  -50.703 1.00 17.95  ? 58  SER B N     1 
ATOM   3101 C  CA    . SER B 1 78  ? -7.785  11.024  -51.121 1.00 18.53  ? 58  SER B CA    1 
ATOM   3102 C  C     . SER B 1 78  ? -6.778  11.119  -49.977 1.00 20.76  ? 58  SER B C     1 
ATOM   3103 O  O     . SER B 1 78  ? -6.011  10.172  -49.731 1.00 21.51  ? 58  SER B O     1 
ATOM   3104 C  CB    . SER B 1 78  ? -7.316  11.840  -52.331 1.00 19.43  ? 58  SER B CB    1 
ATOM   3105 O  OG    . SER B 1 78  ? -7.903  11.368  -53.536 1.00 20.48  ? 58  SER B OG    1 
ATOM   3106 N  N     . TYR B 1 79  ? -6.767  12.244  -49.255 1.00 21.14  ? 59  TYR B N     1 
ATOM   3107 C  CA    . TYR B 1 79  ? -5.785  12.394  -48.182 1.00 19.60  ? 59  TYR B CA    1 
ATOM   3108 C  C     . TYR B 1 79  ? -5.976  11.293  -47.145 1.00 21.82  ? 59  TYR B C     1 
ATOM   3109 O  O     . TYR B 1 79  ? -5.023  10.584  -46.766 1.00 22.30  ? 59  TYR B O     1 
ATOM   3110 C  CB    . TYR B 1 79  ? -5.921  13.766  -47.527 1.00 18.21  ? 59  TYR B CB    1 
ATOM   3111 C  CG    . TYR B 1 79  ? -5.424  14.967  -48.307 1.00 20.40  ? 59  TYR B CG    1 
ATOM   3112 C  CD1   . TYR B 1 79  ? -4.126  15.021  -48.816 1.00 23.05  ? 59  TYR B CD1   1 
ATOM   3113 C  CD2   . TYR B 1 79  ? -6.236  16.093  -48.460 1.00 23.55  ? 59  TYR B CD2   1 
ATOM   3114 C  CE1   . TYR B 1 79  ? -3.679  16.142  -49.506 1.00 24.13  ? 59  TYR B CE1   1 
ATOM   3115 C  CE2   . TYR B 1 79  ? -5.784  17.223  -49.144 1.00 23.30  ? 59  TYR B CE2   1 
ATOM   3116 C  CZ    . TYR B 1 79  ? -4.513  17.242  -49.653 1.00 22.82  ? 59  TYR B CZ    1 
ATOM   3117 O  OH    . TYR B 1 79  ? -4.064  18.365  -50.317 1.00 24.92  ? 59  TYR B OH    1 
ATOM   3118 N  N     . LEU B 1 80  ? -7.225  11.107  -46.719 1.00 19.98  ? 60  LEU B N     1 
ATOM   3119 C  CA    . LEU B 1 80  ? -7.562  10.082  -45.747 1.00 19.76  ? 60  LEU B CA    1 
ATOM   3120 C  C     . LEU B 1 80  ? -7.106  8.718   -46.234 1.00 23.59  ? 60  LEU B C     1 
ATOM   3121 O  O     . LEU B 1 80  ? -6.483  7.955   -45.480 1.00 23.43  ? 60  LEU B O     1 
ATOM   3122 C  CB    . LEU B 1 80  ? -9.076  10.089  -45.510 1.00 17.46  ? 60  LEU B CB    1 
ATOM   3123 C  CG    . LEU B 1 80  ? -9.644  9.025   -44.570 1.00 20.86  ? 60  LEU B CG    1 
ATOM   3124 C  CD1   . LEU B 1 80  ? -9.148  9.250   -43.153 1.00 24.40  ? 60  LEU B CD1   1 
ATOM   3125 C  CD2   . LEU B 1 80  ? -11.188 9.029   -44.605 1.00 19.01  ? 60  LEU B CD2   1 
ATOM   3126 N  N     . GLY B 1 81  ? -7.379  8.408   -47.510 1.00 21.70  ? 61  GLY B N     1 
ATOM   3127 C  CA    . GLY B 1 81  ? -7.083  7.081   -48.013 1.00 20.90  ? 61  GLY B CA    1 
ATOM   3128 C  C     . GLY B 1 81  ? -5.611  6.767   -48.074 1.00 23.51  ? 61  GLY B C     1 
ATOM   3129 O  O     . GLY B 1 81  ? -5.247  5.597   -48.239 1.00 24.92  ? 61  GLY B O     1 
ATOM   3130 N  N     . ASN B 1 82  ? -4.762  7.782   -47.930 1.00 22.44  ? 62  ASN B N     1 
ATOM   3131 C  CA    . ASN B 1 82  ? -3.321  7.590   -48.011 1.00 24.10  ? 62  ASN B CA    1 
ATOM   3132 C  C     . ASN B 1 82  ? -2.616  7.811   -46.678 1.00 26.16  ? 62  ASN B C     1 
ATOM   3133 O  O     . ASN B 1 82  ? -1.381  7.828   -46.642 1.00 28.95  ? 62  ASN B O     1 
ATOM   3134 C  CB    . ASN B 1 82  ? -2.755  8.482   -49.113 1.00 24.34  ? 62  ASN B CB    1 
ATOM   3135 C  CG    . ASN B 1 82  ? -3.024  7.913   -50.495 1.00 25.68  ? 62  ASN B CG    1 
ATOM   3136 O  OD1   . ASN B 1 82  ? -2.243  7.106   -51.000 1.00 31.96  ? 62  ASN B OD1   1 
ATOM   3137 N  ND2   . ASN B 1 82  ? -4.164  8.287   -51.093 1.00 25.44  ? 62  ASN B ND2   1 
ATOM   3138 N  N     . LEU B 1 83  ? -3.358  7.973   -45.585 1.00 25.83  ? 63  LEU B N     1 
ATOM   3139 C  CA    . LEU B 1 83  ? -2.734  7.993   -44.270 1.00 27.75  ? 63  LEU B CA    1 
ATOM   3140 C  C     . LEU B 1 83  ? -2.049  6.649   -44.021 1.00 27.30  ? 63  LEU B C     1 
ATOM   3141 O  O     . LEU B 1 83  ? -2.425  5.634   -44.608 1.00 24.97  ? 63  LEU B O     1 
ATOM   3142 C  CB    . LEU B 1 83  ? -3.769  8.254   -43.176 1.00 28.68  ? 63  LEU B CB    1 
ATOM   3143 C  CG    . LEU B 1 83  ? -4.374  9.659   -43.102 1.00 24.91  ? 63  LEU B CG    1 
ATOM   3144 C  CD1   . LEU B 1 83  ? -5.329  9.787   -41.947 1.00 29.33  ? 63  LEU B CD1   1 
ATOM   3145 C  CD2   . LEU B 1 83  ? -3.263  10.711  -43.025 1.00 29.70  ? 63  LEU B CD2   1 
ATOM   3146 N  N     . PRO B 1 84  ? -1.005  6.618   -43.193 1.00 32.23  ? 64  PRO B N     1 
ATOM   3147 C  CA    . PRO B 1 84  ? -0.376  5.333   -42.871 1.00 34.81  ? 64  PRO B CA    1 
ATOM   3148 C  C     . PRO B 1 84  ? -1.385  4.375   -42.253 1.00 31.16  ? 64  PRO B C     1 
ATOM   3149 O  O     . PRO B 1 84  ? -2.319  4.785   -41.561 1.00 33.35  ? 64  PRO B O     1 
ATOM   3150 C  CB    . PRO B 1 84  ? 0.731   5.717   -41.884 1.00 41.84  ? 64  PRO B CB    1 
ATOM   3151 C  CG    . PRO B 1 84  ? 1.056   7.145   -42.251 1.00 39.48  ? 64  PRO B CG    1 
ATOM   3152 C  CD    . PRO B 1 84  ? -0.279  7.752   -42.596 1.00 40.19  ? 64  PRO B CD    1 
ATOM   3153 N  N     . LYS B 1 85  ? -1.196  3.079   -42.525 1.00 32.02  ? 65  LYS B N     1 
ATOM   3154 C  CA    . LYS B 1 85  ? -2.173  2.088   -42.076 1.00 39.40  ? 65  LYS B CA    1 
ATOM   3155 C  C     . LYS B 1 85  ? -2.376  2.126   -40.565 1.00 41.67  ? 65  LYS B C     1 
ATOM   3156 O  O     . LYS B 1 85  ? -3.464  1.796   -40.086 1.00 36.66  ? 65  LYS B O     1 
ATOM   3157 C  CB    . LYS B 1 85  ? -1.776  0.685   -42.541 1.00 50.62  ? 65  LYS B CB    1 
ATOM   3158 C  CG    . LYS B 1 85  ? -2.877  -0.350  -42.314 1.00 58.50  ? 65  LYS B CG    1 
ATOM   3159 C  CD    . LYS B 1 85  ? -2.489  -1.726  -42.837 1.00 68.66  ? 65  LYS B CD    1 
ATOM   3160 C  CE    . LYS B 1 85  ? -3.707  -2.645  -42.961 1.00 64.87  ? 65  LYS B CE    1 
ATOM   3161 N  NZ    . LYS B 1 85  ? -4.450  -2.806  -41.677 1.00 58.98  ? 65  LYS B NZ    1 
ATOM   3162 N  N     . SER B 1 86  ? -1.347  2.508   -39.799 1.00 37.33  ? 66  SER B N     1 
ATOM   3163 C  CA    . SER B 1 86  ? -1.505  2.639   -38.352 1.00 35.09  ? 66  SER B CA    1 
ATOM   3164 C  C     . SER B 1 86  ? -2.610  3.626   -38.002 1.00 42.69  ? 66  SER B C     1 
ATOM   3165 O  O     . SER B 1 86  ? -3.362  3.415   -37.043 1.00 42.63  ? 66  SER B O     1 
ATOM   3166 C  CB    . SER B 1 86  ? -0.182  3.059   -37.703 1.00 49.18  ? 66  SER B CB    1 
ATOM   3167 O  OG    . SER B 1 86  ? 0.308   4.271   -38.251 1.00 47.39  ? 66  SER B OG    1 
ATOM   3168 N  N     . GLU B 1 87  ? -2.727  4.712   -38.766 1.00 37.04  ? 67  GLU B N     1 
ATOM   3169 C  CA    . GLU B 1 87  ? -3.788  5.674   -38.503 1.00 34.27  ? 67  GLU B CA    1 
ATOM   3170 C  C     . GLU B 1 87  ? -5.145  5.116   -38.917 1.00 31.27  ? 67  GLU B C     1 
ATOM   3171 O  O     . GLU B 1 87  ? -6.126  5.239   -38.175 1.00 33.10  ? 67  GLU B O     1 
ATOM   3172 C  CB    . GLU B 1 87  ? -3.495  6.986   -39.233 1.00 43.65  ? 67  GLU B CB    1 
ATOM   3173 C  CG    . GLU B 1 87  ? -2.348  7.794   -38.633 1.00 38.56  ? 67  GLU B CG    1 
ATOM   3174 C  CD    . GLU B 1 87  ? -2.631  8.220   -37.211 1.00 51.12  ? 67  GLU B CD    1 
ATOM   3175 O  OE1   . GLU B 1 87  ? -3.789  8.593   -36.926 1.00 57.00  ? 67  GLU B OE1   1 
ATOM   3176 O  OE2   . GLU B 1 87  ? -1.701  8.171   -36.376 1.00 64.08  ? 67  GLU B OE2   1 
ATOM   3177 N  N     . LEU B 1 88  ? -5.213  4.471   -40.084 1.00 27.94  ? 68  LEU B N     1 
ATOM   3178 C  CA    . LEU B 1 88  ? -6.492  3.968   -40.581 1.00 26.93  ? 68  LEU B CA    1 
ATOM   3179 C  C     . LEU B 1 88  ? -7.029  2.822   -39.729 1.00 29.82  ? 68  LEU B C     1 
ATOM   3180 O  O     . LEU B 1 88  ? -8.249  2.676   -39.587 1.00 28.00  ? 68  LEU B O     1 
ATOM   3181 C  CB    . LEU B 1 88  ? -6.339  3.539   -42.039 1.00 25.37  ? 68  LEU B CB    1 
ATOM   3182 C  CG    . LEU B 1 88  ? -6.052  4.699   -43.010 1.00 28.65  ? 68  LEU B CG    1 
ATOM   3183 C  CD1   . LEU B 1 88  ? -5.858  4.174   -44.430 1.00 28.07  ? 68  LEU B CD1   1 
ATOM   3184 C  CD2   . LEU B 1 88  ? -7.161  5.751   -42.985 1.00 25.24  ? 68  LEU B CD2   1 
ATOM   3185 N  N     . ASP B 1 89  ? -6.142  2.004   -39.154 1.00 32.20  ? 69  ASP B N     1 
ATOM   3186 C  CA    . ASP B 1 89  ? -6.581  0.890   -38.319 1.00 31.75  ? 69  ASP B CA    1 
ATOM   3187 C  C     . ASP B 1 89  ? -7.377  1.376   -37.118 1.00 32.06  ? 69  ASP B C     1 
ATOM   3188 O  O     . ASP B 1 89  ? -8.305  0.691   -36.670 1.00 37.87  ? 69  ASP B O     1 
ATOM   3189 C  CB    . ASP B 1 89  ? -5.374  0.075   -37.842 1.00 36.33  ? 69  ASP B CB    1 
ATOM   3190 C  CG    . ASP B 1 89  ? -4.717  -0.719  -38.958 1.00 40.05  ? 69  ASP B CG    1 
ATOM   3191 O  OD1   . ASP B 1 89  ? -5.310  -0.844  -40.046 1.00 46.44  ? 69  ASP B OD1   1 
ATOM   3192 O  OD2   . ASP B 1 89  ? -3.596  -1.230  -38.739 1.00 48.66  ? 69  ASP B OD2   1 
ATOM   3193 N  N     . ARG B 1 90  ? -7.046  2.564   -36.601 1.00 30.33  ? 70  ARG B N     1 
ATOM   3194 C  CA    . ARG B 1 90  ? -7.758  3.135   -35.463 1.00 34.60  ? 70  ARG B CA    1 
ATOM   3195 C  C     . ARG B 1 90  ? -9.199  3.479   -35.805 1.00 30.44  ? 70  ARG B C     1 
ATOM   3196 O  O     . ARG B 1 90  ? -10.007 3.695   -34.897 1.00 33.15  ? 70  ARG B O     1 
ATOM   3197 C  CB    . ARG B 1 90  ? -7.089  4.437   -35.023 1.00 41.60  ? 70  ARG B CB    1 
ATOM   3198 C  CG    . ARG B 1 90  ? -5.605  4.371   -34.778 1.00 51.99  ? 70  ARG B CG    1 
ATOM   3199 C  CD    . ARG B 1 90  ? -5.118  5.707   -34.248 1.00 52.62  ? 70  ARG B CD    1 
ATOM   3200 N  NE    . ARG B 1 90  ? -3.666  5.744   -34.133 1.00 72.27  ? 70  ARG B NE    1 
ATOM   3201 C  CZ    . ARG B 1 90  ? -2.970  5.312   -33.093 1.00 74.89  ? 70  ARG B CZ    1 
ATOM   3202 N  NH1   . ARG B 1 90  ? -3.563  4.798   -32.029 1.00 68.94  ? 70  ARG B NH1   1 
ATOM   3203 N  NH2   . ARG B 1 90  ? -1.643  5.402   -33.122 1.00 85.61  ? 70  ARG B NH2   1 
ATOM   3204 N  N     . LEU B 1 91  ? -9.528  3.550   -37.092 1.00 26.69  ? 71  LEU B N     1 
ATOM   3205 C  CA    . LEU B 1 91  ? -10.843 3.981   -37.548 1.00 26.97  ? 71  LEU B CA    1 
ATOM   3206 C  C     . LEU B 1 91  ? -11.739 2.819   -37.943 1.00 31.91  ? 71  LEU B C     1 
ATOM   3207 O  O     . LEU B 1 91  ? -12.839 3.052   -38.457 1.00 28.20  ? 71  LEU B O     1 
ATOM   3208 C  CB    . LEU B 1 91  ? -10.689 4.938   -38.731 1.00 25.84  ? 71  LEU B CB    1 
ATOM   3209 C  CG    . LEU B 1 91  ? -9.818  6.174   -38.484 1.00 25.78  ? 71  LEU B CG    1 
ATOM   3210 C  CD1   . LEU B 1 91  ? -9.720  7.009   -39.757 1.00 26.12  ? 71  LEU B CD1   1 
ATOM   3211 C  CD2   . LEU B 1 91  ? -10.345 7.014   -37.308 1.00 28.12  ? 71  LEU B CD2   1 
ATOM   3212 N  N     . GLU B 1 92  ? -11.300 1.576   -37.738 1.00 27.19  ? 72  GLU B N     1 
ATOM   3213 C  CA    . GLU B 1 92  ? -12.109 0.427   -38.129 1.00 26.26  ? 72  GLU B CA    1 
ATOM   3214 C  C     . GLU B 1 92  ? -13.079 0.046   -37.023 1.00 34.30  ? 72  GLU B C     1 
ATOM   3215 O  O     . GLU B 1 92  ? -12.744 0.108   -35.837 1.00 36.46  ? 72  GLU B O     1 
ATOM   3216 C  CB    . GLU B 1 92  ? -11.243 -0.778  -38.497 1.00 33.72  ? 72  GLU B CB    1 
ATOM   3217 C  CG    . GLU B 1 92  ? -10.502 -0.626  -39.817 1.00 49.84  ? 72  GLU B CG    1 
ATOM   3218 C  CD    . GLU B 1 92  ? -9.947  -1.948  -40.329 1.00 64.19  ? 72  GLU B CD    1 
ATOM   3219 O  OE1   . GLU B 1 92  ? -10.350 -3.015  -39.807 1.00 56.60  ? 72  GLU B OE1   1 
ATOM   3220 O  OE2   . GLU B 1 92  ? -9.111  -1.916  -41.259 1.00 62.76  ? 72  GLU B OE2   1 
ATOM   3221 N  N     . ASN B 1 93  ? -14.295 -0.336  -37.419 1.00 28.57  ? 73  ASN B N     1 
ATOM   3222 C  CA    . ASN B 1 93  ? -15.310 -0.789  -36.467 1.00 29.36  ? 73  ASN B CA    1 
ATOM   3223 C  C     . ASN B 1 93  ? -16.016 -1.987  -37.101 1.00 25.76  ? 73  ASN B C     1 
ATOM   3224 O  O     . ASN B 1 93  ? -16.972 -1.836  -37.869 1.00 24.50  ? 73  ASN B O     1 
ATOM   3225 C  CB    . ASN B 1 93  ? -16.282 0.328   -36.090 1.00 29.07  ? 73  ASN B CB    1 
ATOM   3226 C  CG    . ASN B 1 93  ? -17.259 -0.086  -34.991 1.00 36.53  ? 73  ASN B CG    1 
ATOM   3227 O  OD1   . ASN B 1 93  ? -17.556 -1.272  -34.810 1.00 33.49  ? 73  ASN B OD1   1 
ATOM   3228 N  ND2   . ASN B 1 93  ? -17.751 0.895   -34.242 1.00 35.06  ? 73  ASN B ND2   1 
ATOM   3229 N  N     . GLU B 1 94  ? -15.522 -3.187  -36.773 1.00 29.03  ? 74  GLU B N     1 
ATOM   3230 C  CA    . GLU B 1 94  ? -16.116 -4.415  -37.291 1.00 26.81  ? 74  GLU B CA    1 
ATOM   3231 C  C     . GLU B 1 94  ? -17.497 -4.662  -36.694 1.00 27.04  ? 74  GLU B C     1 
ATOM   3232 O  O     . GLU B 1 94  ? -18.386 -5.177  -37.382 1.00 27.63  ? 74  GLU B O     1 
ATOM   3233 C  CB    . GLU B 1 94  ? -15.182 -5.596  -37.001 1.00 32.02  ? 74  GLU B CB    1 
ATOM   3234 C  CG    . GLU B 1 94  ? -15.667 -6.943  -37.530 1.00 41.09  ? 74  GLU B CG    1 
ATOM   3235 C  CD    . GLU B 1 94  ? -14.752 -8.089  -37.116 1.00 48.50  ? 74  GLU B CD    1 
ATOM   3236 O  OE1   . GLU B 1 94  ? -13.770 -7.827  -36.392 1.00 45.86  ? 74  GLU B OE1   1 
ATOM   3237 O  OE2   . GLU B 1 94  ? -15.025 -9.248  -37.497 1.00 55.29  ? 74  GLU B OE2   1 
ATOM   3238 N  N     . LYS B 1 95  ? -17.695 -4.296  -35.424 1.00 29.55  ? 75  LYS B N     1 
ATOM   3239 C  CA    . LYS B 1 95  ? -18.998 -4.477  -34.788 1.00 36.48  ? 75  LYS B CA    1 
ATOM   3240 C  C     . LYS B 1 95  ? -20.080 -3.676  -35.496 1.00 31.39  ? 75  LYS B C     1 
ATOM   3241 O  O     . LYS B 1 95  ? -21.236 -4.113  -35.566 1.00 31.57  ? 75  LYS B O     1 
ATOM   3242 C  CB    . LYS B 1 95  ? -18.925 -4.091  -33.309 1.00 43.61  ? 75  LYS B CB    1 
ATOM   3243 C  CG    . LYS B 1 95  ? -20.207 -4.380  -32.538 1.00 52.41  ? 75  LYS B CG    1 
ATOM   3244 C  CD    . LYS B 1 95  ? -19.996 -4.321  -31.032 1.00 67.20  ? 75  LYS B CD    1 
ATOM   3245 C  CE    . LYS B 1 95  ? -20.346 -2.951  -30.471 1.00 65.76  ? 75  LYS B CE    1 
ATOM   3246 N  NZ    . LYS B 1 95  ? -21.779 -2.595  -30.682 1.00 56.53  ? 75  LYS B NZ    1 
ATOM   3247 N  N     . ALA B 1 96  ? -19.723 -2.517  -36.043 1.00 31.00  ? 76  ALA B N     1 
ATOM   3248 C  CA    . ALA B 1 96  ? -20.649 -1.709  -36.824 1.00 30.30  ? 76  ALA B CA    1 
ATOM   3249 C  C     . ALA B 1 96  ? -20.796 -2.194  -38.263 1.00 29.54  ? 76  ALA B C     1 
ATOM   3250 O  O     . ALA B 1 96  ? -21.408 -1.489  -39.078 1.00 28.89  ? 76  ALA B O     1 
ATOM   3251 C  CB    . ALA B 1 96  ? -20.190 -0.248  -36.813 1.00 25.23  ? 76  ALA B CB    1 
ATOM   3252 N  N     . LYS B 1 97  ? -20.266 -3.378  -38.584 1.00 28.71  ? 77  LYS B N     1 
ATOM   3253 C  CA    . LYS B 1 97  ? -20.269 -3.918  -39.945 1.00 27.48  ? 77  LYS B CA    1 
ATOM   3254 C  C     . LYS B 1 97  ? -19.510 -2.996  -40.901 1.00 23.26  ? 77  LYS B C     1 
ATOM   3255 O  O     . LYS B 1 97  ? -19.824 -2.927  -42.094 1.00 25.37  ? 77  LYS B O     1 
ATOM   3256 C  CB    . LYS B 1 97  ? -21.695 -4.157  -40.460 1.00 30.45  ? 77  LYS B CB    1 
ATOM   3257 C  CG    . LYS B 1 97  ? -22.606 -4.928  -39.513 1.00 41.49  ? 77  LYS B CG    1 
ATOM   3258 C  CD    . LYS B 1 97  ? -21.975 -6.211  -39.001 1.00 47.69  ? 77  LYS B CD    1 
ATOM   3259 C  CE    . LYS B 1 97  ? -22.922 -6.932  -38.041 1.00 64.34  ? 77  LYS B CE    1 
ATOM   3260 N  NZ    . LYS B 1 97  ? -22.275 -8.072  -37.326 1.00 58.32  ? 77  LYS B NZ    1 
ATOM   3261 N  N     . TYR B 1 98  ? -18.525 -2.265  -40.375 1.00 24.84  ? 78  TYR B N     1 
ATOM   3262 C  CA    . TYR B 1 98  ? -17.734 -1.290  -41.136 1.00 23.22  ? 78  TYR B CA    1 
ATOM   3263 C  C     . TYR B 1 98  ? -18.591 -0.145  -41.686 1.00 24.59  ? 78  TYR B C     1 
ATOM   3264 O  O     . TYR B 1 98  ? -18.182 0.553   -42.619 1.00 24.96  ? 78  TYR B O     1 
ATOM   3265 C  CB    . TYR B 1 98  ? -16.948 -1.972  -42.267 1.00 25.00  ? 78  TYR B CB    1 
ATOM   3266 C  CG    . TYR B 1 98  ? -16.121 -3.133  -41.769 1.00 24.67  ? 78  TYR B CG    1 
ATOM   3267 C  CD1   . TYR B 1 98  ? -14.975 -2.925  -41.005 1.00 26.21  ? 78  TYR B CD1   1 
ATOM   3268 C  CD2   . TYR B 1 98  ? -16.504 -4.443  -42.036 1.00 34.20  ? 78  TYR B CD2   1 
ATOM   3269 C  CE1   . TYR B 1 98  ? -14.221 -3.997  -40.534 1.00 25.77  ? 78  TYR B CE1   1 
ATOM   3270 C  CE2   . TYR B 1 98  ? -15.755 -5.517  -41.574 1.00 33.45  ? 78  TYR B CE2   1 
ATOM   3271 C  CZ    . TYR B 1 98  ? -14.621 -5.287  -40.822 1.00 32.41  ? 78  TYR B CZ    1 
ATOM   3272 O  OH    . TYR B 1 98  ? -13.871 -6.351  -40.357 1.00 36.05  ? 78  TYR B OH    1 
ATOM   3273 N  N     . LEU B 1 99  ? -19.775 0.075   -41.111 1.00 22.04  ? 79  LEU B N     1 
ATOM   3274 C  CA    . LEU B 1 99  ? -20.628 1.196   -41.476 1.00 21.96  ? 79  LEU B CA    1 
ATOM   3275 C  C     . LEU B 1 99  ? -20.414 2.386   -40.544 1.00 21.43  ? 79  LEU B C     1 
ATOM   3276 O  O     . LEU B 1 99  ? -21.220 3.326   -40.528 1.00 21.54  ? 79  LEU B O     1 
ATOM   3277 C  CB    . LEU B 1 99  ? -22.091 0.752   -41.494 1.00 20.88  ? 79  LEU B CB    1 
ATOM   3278 C  CG    . LEU B 1 99  ? -22.356 -0.271  -42.598 1.00 22.05  ? 79  LEU B CG    1 
ATOM   3279 C  CD1   . LEU B 1 99  ? -23.801 -0.755  -42.530 1.00 24.88  ? 79  LEU B CD1   1 
ATOM   3280 C  CD2   . LEU B 1 99  ? -22.078 0.315   -43.977 1.00 23.49  ? 79  LEU B CD2   1 
ATOM   3281 N  N     . THR B 1 100 ? -19.342 2.345   -39.761 1.00 22.86  ? 80  THR B N     1 
ATOM   3282 C  CA    . THR B 1 100 ? -18.795 3.485   -39.045 1.00 21.44  ? 80  THR B CA    1 
ATOM   3283 C  C     . THR B 1 100 ? -17.291 3.449   -39.256 1.00 18.71  ? 80  THR B C     1 
ATOM   3284 O  O     . THR B 1 100 ? -16.690 2.375   -39.157 1.00 22.57  ? 80  THR B O     1 
ATOM   3285 C  CB    . THR B 1 100 ? -19.114 3.421   -37.548 1.00 26.11  ? 80  THR B CB    1 
ATOM   3286 O  OG1   . THR B 1 100 ? -20.507 3.677   -37.344 1.00 25.51  ? 80  THR B OG1   1 
ATOM   3287 C  CG2   . THR B 1 100 ? -18.285 4.442   -36.786 1.00 27.06  ? 80  THR B CG2   1 
ATOM   3288 N  N     . GLY B 1 101 ? -16.698 4.587   -39.605 1.00 20.16  ? 81  GLY B N     1 
ATOM   3289 C  CA    . GLY B 1 101 ? -15.249 4.640   -39.742 1.00 20.74  ? 81  GLY B CA    1 
ATOM   3290 C  C     . GLY B 1 101 ? -14.766 4.173   -41.106 1.00 19.03  ? 81  GLY B C     1 
ATOM   3291 O  O     . GLY B 1 101 ? -15.503 4.178   -42.092 1.00 19.90  ? 81  GLY B O     1 
ATOM   3292 N  N     . TRP B 1 102 ? -13.507 3.730   -41.141 1.00 20.04  ? 82  TRP B N     1 
ATOM   3293 C  CA    A TRP B 1 102 ? -12.820 3.412   -42.385 0.57 20.52  ? 82  TRP B CA    1 
ATOM   3294 C  CA    B TRP B 1 102 ? -12.798 3.409   -42.372 0.43 20.57  ? 82  TRP B CA    1 
ATOM   3295 C  C     . TRP B 1 102 ? -12.734 1.906   -42.605 1.00 20.86  ? 82  TRP B C     1 
ATOM   3296 O  O     . TRP B 1 102 ? -12.623 1.119   -41.662 1.00 25.35  ? 82  TRP B O     1 
ATOM   3297 C  CB    A TRP B 1 102 ? -11.404 4.009   -42.388 0.57 23.77  ? 82  TRP B CB    1 
ATOM   3298 C  CB    B TRP B 1 102 ? -11.370 3.966   -42.321 0.43 23.65  ? 82  TRP B CB    1 
ATOM   3299 C  CG    A TRP B 1 102 ? -10.837 4.216   -43.766 0.57 18.84  ? 82  TRP B CG    1 
ATOM   3300 C  CG    B TRP B 1 102 ? -10.484 3.455   -43.411 0.43 21.30  ? 82  TRP B CG    1 
ATOM   3301 C  CD1   A TRP B 1 102 ? -11.021 5.303   -44.572 0.57 21.39  ? 82  TRP B CD1   1 
ATOM   3302 C  CD1   B TRP B 1 102 ? -9.660  2.361   -43.365 0.43 22.29  ? 82  TRP B CD1   1 
ATOM   3303 C  CD2   A TRP B 1 102 ? -10.002 3.311   -44.499 0.57 21.08  ? 82  TRP B CD2   1 
ATOM   3304 C  CD2   B TRP B 1 102 ? -10.320 4.025   -44.710 0.43 18.45  ? 82  TRP B CD2   1 
ATOM   3305 N  NE1   A TRP B 1 102 ? -10.348 5.134   -45.759 0.57 22.70  ? 82  TRP B NE1   1 
ATOM   3306 N  NE1   B TRP B 1 102 ? -9.004  2.213   -44.563 0.43 21.64  ? 82  TRP B NE1   1 
ATOM   3307 C  CE2   A TRP B 1 102 ? -9.715  3.918   -45.740 0.57 18.85  ? 82  TRP B CE2   1 
ATOM   3308 C  CE2   B TRP B 1 102 ? -9.390  3.225   -45.404 0.43 20.80  ? 82  TRP B CE2   1 
ATOM   3309 C  CE3   A TRP B 1 102 ? -9.463  2.047   -44.225 0.57 22.03  ? 82  TRP B CE3   1 
ATOM   3310 C  CE3   B TRP B 1 102 ? -10.870 5.136   -45.356 0.43 21.78  ? 82  TRP B CE3   1 
ATOM   3311 C  CZ2   A TRP B 1 102 ? -8.926  3.299   -46.712 0.57 21.29  ? 82  TRP B CZ2   1 
ATOM   3312 C  CZ2   B TRP B 1 102 ? -9.002  3.499   -46.714 0.43 21.30  ? 82  TRP B CZ2   1 
ATOM   3313 C  CZ3   A TRP B 1 102 ? -8.675  1.438   -45.188 0.57 21.99  ? 82  TRP B CZ3   1 
ATOM   3314 C  CZ3   B TRP B 1 102 ? -10.478 5.408   -46.653 0.43 24.21  ? 82  TRP B CZ3   1 
ATOM   3315 C  CH2   A TRP B 1 102 ? -8.411  2.066   -46.415 0.57 24.39  ? 82  TRP B CH2   1 
ATOM   3316 C  CH2   B TRP B 1 102 ? -9.550  4.597   -47.316 0.43 21.72  ? 82  TRP B CH2   1 
ATOM   3317 N  N     . SER B 1 103 ? -12.782 1.511   -43.879 1.00 21.06  ? 83  SER B N     1 
ATOM   3318 C  CA    . SER B 1 103 ? -12.522 0.118   -44.237 1.00 21.33  ? 83  SER B CA    1 
ATOM   3319 C  C     . SER B 1 103 ? -12.082 0.022   -45.690 1.00 24.88  ? 83  SER B C     1 
ATOM   3320 O  O     . SER B 1 103 ? -12.334 0.917   -46.500 1.00 22.78  ? 83  SER B O     1 
ATOM   3321 C  CB    . SER B 1 103 ? -13.754 -0.773  -44.016 1.00 25.91  ? 83  SER B CB    1 
ATOM   3322 O  OG    . SER B 1 103 ? -14.803 -0.377  -44.884 1.00 26.71  ? 83  SER B OG    1 
ATOM   3323 N  N     . LEU B 1 104 ? -11.430 -1.093  -46.009 1.00 24.90  ? 84  LEU B N     1 
ATOM   3324 C  CA    . LEU B 1 104 ? -11.027 -1.399  -47.373 1.00 24.33  ? 84  LEU B CA    1 
ATOM   3325 C  C     . LEU B 1 104 ? -11.981 -2.455  -47.919 1.00 30.46  ? 84  LEU B C     1 
ATOM   3326 O  O     . LEU B 1 104 ? -12.211 -3.483  -47.272 1.00 33.57  ? 84  LEU B O     1 
ATOM   3327 C  CB    . LEU B 1 104 ? -9.578  -1.895  -47.404 1.00 25.31  ? 84  LEU B CB    1 
ATOM   3328 C  CG    . LEU B 1 104 ? -8.836  -1.972  -48.737 1.00 39.49  ? 84  LEU B CG    1 
ATOM   3329 C  CD1   . LEU B 1 104 ? -8.732  -0.589  -49.361 1.00 30.62  ? 84  LEU B CD1   1 
ATOM   3330 C  CD2   . LEU B 1 104 ? -7.453  -2.569  -48.509 1.00 35.35  ? 84  LEU B CD2   1 
ATOM   3331 N  N     . GLY B 1 105 ? -12.533 -2.200  -49.108 1.00 25.63  ? 85  GLY B N     1 
ATOM   3332 C  CA    . GLY B 1 105 ? -13.476 -3.093  -49.747 1.00 29.31  ? 85  GLY B CA    1 
ATOM   3333 C  C     . GLY B 1 105 ? -13.193 -3.225  -51.232 1.00 28.70  ? 85  GLY B C     1 
ATOM   3334 O  O     . GLY B 1 105 ? -12.299 -2.571  -51.775 1.00 34.02  ? 85  GLY B O     1 
ATOM   3335 N  N     . LYS B 1 106 ? -13.978 -4.088  -51.880 1.00 34.07  ? 86  LYS B N     1 
ATOM   3336 C  CA    . LYS B 1 106 ? -13.782 -4.430  -53.281 1.00 36.91  ? 86  LYS B CA    1 
ATOM   3337 C  C     . LYS B 1 106 ? -15.119 -4.459  -54.008 1.00 49.31  ? 86  LYS B C     1 
ATOM   3338 O  O     . LYS B 1 106 ? -16.162 -4.752  -53.416 1.00 45.66  ? 86  LYS B O     1 
ATOM   3339 C  CB    . LYS B 1 106 ? -13.088 -5.794  -53.432 1.00 37.56  ? 86  LYS B CB    1 
ATOM   3340 C  CG    . LYS B 1 106 ? -12.626 -6.122  -54.837 1.00 45.40  ? 86  LYS B CG    1 
ATOM   3341 C  CD    . LYS B 1 106 ? -12.141 -7.550  -54.917 1.00 41.37  ? 86  LYS B CD    1 
ATOM   3342 C  CE    . LYS B 1 106 ? -11.267 -7.767  -56.134 1.00 40.63  ? 86  LYS B CE    1 
ATOM   3343 N  NZ    . LYS B 1 106 ? -10.770 -9.163  -56.197 1.00 43.32  ? 86  LYS B NZ    1 
ATOM   3344 N  N     . GLU B 1 107 ? -15.072 -4.121  -55.297 1.00 51.75  ? 87  GLU B N     1 
ATOM   3345 C  CA    . GLU B 1 107 ? -16.202 -4.218  -56.212 1.00 54.45  ? 87  GLU B CA    1 
ATOM   3346 C  C     . GLU B 1 107 ? -15.797 -5.134  -57.359 1.00 61.20  ? 87  GLU B C     1 
ATOM   3347 O  O     . GLU B 1 107 ? -14.702 -4.987  -57.917 1.00 54.34  ? 87  GLU B O     1 
ATOM   3348 C  CB    . GLU B 1 107 ? -16.624 -2.844  -56.746 1.00 49.28  ? 87  GLU B CB    1 
ATOM   3349 C  CG    . GLU B 1 107 ? -17.441 -2.020  -55.761 1.00 50.03  ? 87  GLU B CG    1 
ATOM   3350 C  CD    . GLU B 1 107 ? -17.668 -0.590  -56.231 1.00 48.76  ? 87  GLU B CD    1 
ATOM   3351 O  OE1   . GLU B 1 107 ? -17.451 -0.305  -57.430 1.00 50.07  ? 87  GLU B OE1   1 
ATOM   3352 O  OE2   . GLU B 1 107 ? -18.062 0.251   -55.397 1.00 42.51  ? 87  GLU B OE2   1 
ATOM   3353 N  N     . THR B 1 108 ? -16.668 -6.075  -57.708 1.00 63.12  ? 88  THR B N     1 
ATOM   3354 C  CA    . THR B 1 108 ? -16.339 -7.049  -58.744 1.00 72.09  ? 88  THR B CA    1 
ATOM   3355 C  C     . THR B 1 108 ? -17.308 -6.987  -59.921 1.00 66.04  ? 88  THR B C     1 
ATOM   3356 O  O     . THR B 1 108 ? -18.384 -6.399  -59.823 1.00 69.19  ? 88  THR B O     1 
ATOM   3357 C  CB    . THR B 1 108 ? -16.340 -8.481  -58.176 1.00 79.45  ? 88  THR B CB    1 
ATOM   3358 O  OG1   . THR B 1 108 ? -17.546 -8.696  -57.429 1.00 80.12  ? 88  THR B OG1   1 
ATOM   3359 C  CG2   . THR B 1 108 ? -15.136 -8.695  -57.264 1.00 58.79  ? 88  THR B CG2   1 
ATOM   3360 N  N     . ASN B 1 116 ? -12.257 -3.217  -58.635 1.00 47.40  ? 96  ASN B N     1 
ATOM   3361 C  CA    . ASN B 1 116 ? -12.050 -1.915  -58.009 1.00 47.57  ? 96  ASN B CA    1 
ATOM   3362 C  C     . ASN B 1 116 ? -11.710 -2.066  -56.528 1.00 42.24  ? 96  ASN B C     1 
ATOM   3363 O  O     . ASN B 1 116 ? -12.392 -2.793  -55.808 1.00 46.08  ? 96  ASN B O     1 
ATOM   3364 C  CB    . ASN B 1 116 ? -13.314 -1.060  -58.144 1.00 50.07  ? 96  ASN B CB    1 
ATOM   3365 C  CG    . ASN B 1 116 ? -13.447 -0.414  -59.506 1.00 67.72  ? 96  ASN B CG    1 
ATOM   3366 O  OD1   . ASN B 1 116 ? -12.482 -0.327  -60.265 1.00 70.47  ? 96  ASN B OD1   1 
ATOM   3367 N  ND2   . ASN B 1 116 ? -14.660 0.025   -59.833 1.00 64.77  ? 96  ASN B ND2   1 
ATOM   3368 N  N     . LEU B 1 117 ? -10.669 -1.377  -56.067 1.00 36.40  ? 97  LEU B N     1 
ATOM   3369 C  CA    . LEU B 1 117 ? -10.357 -1.296  -54.645 1.00 32.94  ? 97  LEU B CA    1 
ATOM   3370 C  C     . LEU B 1 117 ? -10.923 0.016   -54.113 1.00 30.35  ? 97  LEU B C     1 
ATOM   3371 O  O     . LEU B 1 117 ? -10.706 1.072   -54.718 1.00 30.83  ? 97  LEU B O     1 
ATOM   3372 C  CB    . LEU B 1 117 ? -8.850  -1.377  -54.409 1.00 36.29  ? 97  LEU B CB    1 
ATOM   3373 C  CG    . LEU B 1 117 ? -8.457  -1.519  -52.945 1.00 43.31  ? 97  LEU B CG    1 
ATOM   3374 C  CD1   . LEU B 1 117 ? -8.917  -2.877  -52.438 1.00 47.63  ? 97  LEU B CD1   1 
ATOM   3375 C  CD2   . LEU B 1 117 ? -6.955  -1.359  -52.780 1.00 48.07  ? 97  LEU B CD2   1 
ATOM   3376 N  N     . LYS B 1 118 ? -11.605 -0.038  -52.967 1.00 28.04  ? 98  LYS B N     1 
ATOM   3377 C  CA    . LYS B 1 118 ? -12.364 1.105   -52.474 1.00 28.40  ? 98  LYS B CA    1 
ATOM   3378 C  C     . LYS B 1 118 ? -12.138 1.284   -50.984 1.00 30.99  ? 98  LYS B C     1 
ATOM   3379 O  O     . LYS B 1 118 ? -12.386 0.367   -50.206 1.00 31.58  ? 98  LYS B O     1 
ATOM   3380 C  CB    . LYS B 1 118 ? -13.858 0.880   -52.753 1.00 34.86  ? 98  LYS B CB    1 
ATOM   3381 C  CG    . LYS B 1 118 ? -14.801 1.912   -52.167 1.00 40.17  ? 98  LYS B CG    1 
ATOM   3382 C  CD    . LYS B 1 118 ? -16.066 1.279   -51.583 1.00 39.93  ? 98  LYS B CD    1 
ATOM   3383 C  CE    . LYS B 1 118 ? -16.590 0.112   -52.399 1.00 43.84  ? 98  LYS B CE    1 
ATOM   3384 N  NZ    . LYS B 1 118 ? -17.967 -0.289  -51.966 1.00 46.47  ? 98  LYS B NZ    1 
ATOM   3385 N  N     . GLY B 1 119 ? -11.689 2.473   -50.570 1.00 24.48  ? 99  GLY B N     1 
ATOM   3386 C  CA    . GLY B 1 119 ? -11.708 2.829   -49.167 1.00 24.29  ? 99  GLY B CA    1 
ATOM   3387 C  C     . GLY B 1 119 ? -13.016 3.541   -48.876 1.00 26.50  ? 99  GLY B C     1 
ATOM   3388 O  O     . GLY B 1 119 ? -13.427 4.432   -49.624 1.00 22.60  ? 99  GLY B O     1 
ATOM   3389 N  N     . SER B 1 120 ? -13.692 3.116   -47.815 1.00 19.90  ? 100 SER B N     1 
ATOM   3390 C  CA    . SER B 1 120 ? -14.950 3.729   -47.410 1.00 18.43  ? 100 SER B CA    1 
ATOM   3391 C  C     . SER B 1 120 ? -14.784 4.395   -46.058 1.00 20.26  ? 100 SER B C     1 
ATOM   3392 O  O     . SER B 1 120 ? -14.160 3.828   -45.153 1.00 19.44  ? 100 SER B O     1 
ATOM   3393 C  CB    . SER B 1 120 ? -16.071 2.692   -47.302 1.00 20.84  ? 100 SER B CB    1 
ATOM   3394 O  OG    . SER B 1 120 ? -16.258 2.016   -48.526 1.00 24.86  ? 100 SER B OG    1 
ATOM   3395 N  N     . TYR B 1 121 ? -15.372 5.584   -45.903 1.00 17.02  ? 101 TYR B N     1 
ATOM   3396 C  CA    . TYR B 1 121 ? -15.423 6.245   -44.607 1.00 17.33  ? 101 TYR B CA    1 
ATOM   3397 C  C     . TYR B 1 121 ? -16.860 6.633   -44.318 1.00 19.41  ? 101 TYR B C     1 
ATOM   3398 O  O     . TYR B 1 121 ? -17.462 7.382   -45.090 1.00 17.82  ? 101 TYR B O     1 
ATOM   3399 C  CB    . TYR B 1 121 ? -14.501 7.475   -44.552 1.00 19.17  ? 101 TYR B CB    1 
ATOM   3400 C  CG    . TYR B 1 121 ? -14.572 8.125   -43.190 1.00 17.46  ? 101 TYR B CG    1 
ATOM   3401 C  CD1   . TYR B 1 121 ? -13.844 7.613   -42.122 1.00 18.87  ? 101 TYR B CD1   1 
ATOM   3402 C  CD2   . TYR B 1 121 ? -15.409 9.207   -42.961 1.00 16.81  ? 101 TYR B CD2   1 
ATOM   3403 C  CE1   . TYR B 1 121 ? -13.943 8.174   -40.862 1.00 18.14  ? 101 TYR B CE1   1 
ATOM   3404 C  CE2   . TYR B 1 121 ? -15.515 9.772   -41.709 1.00 20.09  ? 101 TYR B CE2   1 
ATOM   3405 C  CZ    . TYR B 1 121 ? -14.762 9.257   -40.661 1.00 20.11  ? 101 TYR B CZ    1 
ATOM   3406 O  OH    . TYR B 1 121 ? -14.890 9.819   -39.409 1.00 22.19  ? 101 TYR B OH    1 
ATOM   3407 N  N     . TYR B 1 122 ? -17.400 6.136   -43.211 1.00 16.88  ? 102 TYR B N     1 
ATOM   3408 C  CA    . TYR B 1 122 ? -18.792 6.381   -42.850 1.00 18.07  ? 102 TYR B CA    1 
ATOM   3409 C  C     . TYR B 1 122 ? -18.878 7.158   -41.547 1.00 17.96  ? 102 TYR B C     1 
ATOM   3410 O  O     . TYR B 1 122 ? -18.120 6.891   -40.608 1.00 18.91  ? 102 TYR B O     1 
ATOM   3411 C  CB    . TYR B 1 122 ? -19.565 5.078   -42.659 1.00 18.22  ? 102 TYR B CB    1 
ATOM   3412 C  CG    . TYR B 1 122 ? -19.851 4.269   -43.893 1.00 18.64  ? 102 TYR B CG    1 
ATOM   3413 C  CD1   . TYR B 1 122 ? -18.944 3.324   -44.338 1.00 20.13  ? 102 TYR B CD1   1 
ATOM   3414 C  CD2   . TYR B 1 122 ? -21.064 4.391   -44.571 1.00 19.32  ? 102 TYR B CD2   1 
ATOM   3415 C  CE1   . TYR B 1 122 ? -19.206 2.543   -45.450 1.00 18.08  ? 102 TYR B CE1   1 
ATOM   3416 C  CE2   . TYR B 1 122 ? -21.341 3.606   -45.680 1.00 16.95  ? 102 TYR B CE2   1 
ATOM   3417 C  CZ    . TYR B 1 122 ? -20.403 2.696   -46.123 1.00 20.86  ? 102 TYR B CZ    1 
ATOM   3418 O  OH    . TYR B 1 122 ? -20.648 1.897   -47.217 1.00 21.83  ? 102 TYR B OH    1 
ATOM   3419 N  N     . ALA B 1 123 ? -19.854 8.063   -41.465 1.00 17.32  ? 103 ALA B N     1 
ATOM   3420 C  CA    . ALA B 1 123 ? -20.155 8.750   -40.213 1.00 16.57  ? 103 ALA B CA    1 
ATOM   3421 C  C     . ALA B 1 123 ? -21.648 8.970   -40.086 1.00 21.69  ? 103 ALA B C     1 
ATOM   3422 O  O     . ALA B 1 123 ? -22.299 9.325   -41.065 1.00 20.24  ? 103 ALA B O     1 
ATOM   3423 C  CB    . ALA B 1 123 ? -19.462 10.115  -40.120 1.00 18.60  ? 103 ALA B CB    1 
ATOM   3424 N  N     . ASN B 1 124 ? -22.187 8.802   -38.881 1.00 18.29  ? 104 ASN B N     1 
ATOM   3425 C  CA    . ASN B 1 124 ? -23.556 9.266   -38.701 1.00 19.05  ? 104 ASN B CA    1 
ATOM   3426 C  C     . ASN B 1 124 ? -23.567 10.791  -38.609 1.00 17.51  ? 104 ASN B C     1 
ATOM   3427 O  O     . ASN B 1 124 ? -22.565 11.428  -38.273 1.00 18.80  ? 104 ASN B O     1 
ATOM   3428 C  CB    . ASN B 1 124 ? -24.191 8.646   -37.451 1.00 21.73  ? 104 ASN B CB    1 
ATOM   3429 C  CG    . ASN B 1 124 ? -23.627 9.222   -36.167 1.00 19.87  ? 104 ASN B CG    1 
ATOM   3430 O  OD1   . ASN B 1 124 ? -23.917 10.365  -35.808 1.00 20.55  ? 104 ASN B OD1   1 
ATOM   3431 N  ND2   . ASN B 1 124 ? -22.798 8.439   -35.479 1.00 21.62  ? 104 ASN B ND2   1 
ATOM   3432 N  N     . CYS B 1 125 ? -24.727 11.383  -38.910 1.00 18.10  ? 105 CYS B N     1 
ATOM   3433 C  CA    . CYS B 1 125 ? -24.884 12.831  -38.897 1.00 16.41  ? 105 CYS B CA    1 
ATOM   3434 C  C     . CYS B 1 125 ? -25.754 13.295  -37.734 1.00 16.53  ? 105 CYS B C     1 
ATOM   3435 O  O     . CYS B 1 125 ? -26.492 14.277  -37.855 1.00 18.25  ? 105 CYS B O     1 
ATOM   3436 C  CB    . CYS B 1 125 ? -25.456 13.325  -40.222 1.00 16.05  ? 105 CYS B CB    1 
ATOM   3437 S  SG    . CYS B 1 125 ? -24.319 12.984  -41.574 1.00 18.46  ? 105 CYS B SG    1 
ATOM   3438 N  N     . ALA B 1 126 ? -25.655 12.608  -36.583 1.00 17.41  ? 106 ALA B N     1 
ATOM   3439 C  CA    . ALA B 1 126 ? -26.363 13.073  -35.388 1.00 17.07  ? 106 ALA B CA    1 
ATOM   3440 C  C     . ALA B 1 126 ? -25.955 14.497  -35.020 1.00 18.03  ? 106 ALA B C     1 
ATOM   3441 O  O     . ALA B 1 126 ? -26.754 15.251  -34.450 1.00 20.28  ? 106 ALA B O     1 
ATOM   3442 C  CB    . ALA B 1 126 ? -26.113 12.116  -34.219 1.00 20.08  ? 106 ALA B CB    1 
ATOM   3443 N  N     . PHE B 1 127 ? -24.720 14.884  -35.352 1.00 20.00  ? 107 PHE B N     1 
ATOM   3444 C  CA    . PHE B 1 127 ? -24.249 16.242  -35.104 1.00 20.53  ? 107 PHE B CA    1 
ATOM   3445 C  C     . PHE B 1 127 ? -25.135 17.291  -35.757 1.00 22.20  ? 107 PHE B C     1 
ATOM   3446 O  O     . PHE B 1 127 ? -25.123 18.446  -35.327 1.00 20.75  ? 107 PHE B O     1 
ATOM   3447 C  CB    . PHE B 1 127 ? -22.805 16.407  -35.593 1.00 18.86  ? 107 PHE B CB    1 
ATOM   3448 C  CG    . PHE B 1 127 ? -22.621 16.204  -37.085 1.00 18.68  ? 107 PHE B CG    1 
ATOM   3449 C  CD1   . PHE B 1 127 ? -22.894 17.223  -37.977 1.00 21.94  ? 107 PHE B CD1   1 
ATOM   3450 C  CD2   . PHE B 1 127 ? -22.120 15.000  -37.580 1.00 20.89  ? 107 PHE B CD2   1 
ATOM   3451 C  CE1   . PHE B 1 127 ? -22.730 17.034  -39.352 1.00 17.78  ? 107 PHE B CE1   1 
ATOM   3452 C  CE2   . PHE B 1 127 ? -21.929 14.807  -38.930 1.00 21.87  ? 107 PHE B CE2   1 
ATOM   3453 C  CZ    . PHE B 1 127 ? -22.227 15.822  -39.822 1.00 19.36  ? 107 PHE B CZ    1 
ATOM   3454 N  N     . TYR B 1 128 ? -25.900 16.923  -36.793 1.00 18.64  ? 108 TYR B N     1 
ATOM   3455 C  CA    . TYR B 1 128 ? -26.821 17.877  -37.394 1.00 19.73  ? 108 TYR B CA    1 
ATOM   3456 C  C     . TYR B 1 128 ? -27.843 18.364  -36.380 1.00 20.35  ? 108 TYR B C     1 
ATOM   3457 O  O     . TYR B 1 128 ? -28.176 19.556  -36.342 1.00 20.88  ? 108 TYR B O     1 
ATOM   3458 C  CB    . TYR B 1 128 ? -27.548 17.236  -38.584 1.00 16.94  ? 108 TYR B CB    1 
ATOM   3459 C  CG    . TYR B 1 128 ? -28.472 18.191  -39.290 1.00 17.32  ? 108 TYR B CG    1 
ATOM   3460 C  CD1   . TYR B 1 128 ? -27.972 19.102  -40.218 1.00 19.80  ? 108 TYR B CD1   1 
ATOM   3461 C  CD2   . TYR B 1 128 ? -29.842 18.207  -39.018 1.00 18.48  ? 108 TYR B CD2   1 
ATOM   3462 C  CE1   . TYR B 1 128 ? -28.806 19.987  -40.879 1.00 17.73  ? 108 TYR B CE1   1 
ATOM   3463 C  CE2   . TYR B 1 128 ? -30.683 19.094  -39.677 1.00 20.87  ? 108 TYR B CE2   1 
ATOM   3464 C  CZ    . TYR B 1 128 ? -30.154 19.985  -40.598 1.00 19.17  ? 108 TYR B CZ    1 
ATOM   3465 O  OH    . TYR B 1 128 ? -30.979 20.875  -41.251 1.00 20.69  ? 108 TYR B OH    1 
ATOM   3466 N  N     . VAL B 1 129 ? -28.353 17.446  -35.555 1.00 19.22  ? 109 VAL B N     1 
ATOM   3467 C  CA    . VAL B 1 129 ? -29.378 17.763  -34.570 1.00 21.13  ? 109 VAL B CA    1 
ATOM   3468 C  C     . VAL B 1 129 ? -28.765 18.462  -33.360 1.00 22.95  ? 109 VAL B C     1 
ATOM   3469 O  O     . VAL B 1 129 ? -29.353 19.392  -32.797 1.00 26.62  ? 109 VAL B O     1 
ATOM   3470 C  CB    . VAL B 1 129 ? -30.107 16.470  -34.158 1.00 22.79  ? 109 VAL B CB    1 
ATOM   3471 C  CG1   . VAL B 1 129 ? -31.154 16.770  -33.095 1.00 30.77  ? 109 VAL B CG1   1 
ATOM   3472 C  CG2   . VAL B 1 129 ? -30.727 15.779  -35.373 1.00 19.69  ? 109 VAL B CG2   1 
ATOM   3473 N  N     . ASP B 1 130 ? -27.607 17.999  -32.926 1.00 23.24  ? 110 ASP B N     1 
ATOM   3474 C  CA    . ASP B 1 130 ? -26.924 18.529  -31.751 1.00 25.80  ? 110 ASP B CA    1 
ATOM   3475 C  C     . ASP B 1 130 ? -25.432 18.366  -31.989 1.00 22.79  ? 110 ASP B C     1 
ATOM   3476 O  O     . ASP B 1 130 ? -24.927 17.235  -31.984 1.00 22.99  ? 110 ASP B O     1 
ATOM   3477 C  CB    . ASP B 1 130 ? -27.398 17.799  -30.489 1.00 28.02  ? 110 ASP B CB    1 
ATOM   3478 C  CG    . ASP B 1 130 ? -26.599 18.167  -29.243 1.00 35.47  ? 110 ASP B CG    1 
ATOM   3479 O  OD1   . ASP B 1 130 ? -25.577 18.886  -29.337 1.00 29.25  ? 110 ASP B OD1   1 
ATOM   3480 O  OD2   . ASP B 1 130 ? -27.012 17.720  -28.151 1.00 33.27  ? 110 ASP B OD2   1 
ATOM   3481 N  N     . PRO B 1 131 ? -24.698 19.469  -32.171 1.00 24.81  ? 111 PRO B N     1 
ATOM   3482 C  CA    . PRO B 1 131 ? -23.301 19.370  -32.620 1.00 25.53  ? 111 PRO B CA    1 
ATOM   3483 C  C     . PRO B 1 131 ? -22.407 18.567  -31.697 1.00 24.56  ? 111 PRO B C     1 
ATOM   3484 O  O     . PRO B 1 131 ? -21.326 18.133  -32.127 1.00 28.92  ? 111 PRO B O     1 
ATOM   3485 C  CB    . PRO B 1 131 ? -22.844 20.836  -32.674 1.00 25.09  ? 111 PRO B CB    1 
ATOM   3486 C  CG    . PRO B 1 131 ? -24.119 21.632  -32.757 1.00 27.36  ? 111 PRO B CG    1 
ATOM   3487 C  CD    . PRO B 1 131 ? -25.124 20.864  -31.964 1.00 30.37  ? 111 PRO B CD    1 
ATOM   3488 N  N     . SER B 1 132 ? -22.822 18.340  -30.451 1.00 24.37  ? 112 SER B N     1 
ATOM   3489 C  CA    . SER B 1 132 ? -22.003 17.577  -29.517 1.00 25.85  ? 112 SER B CA    1 
ATOM   3490 C  C     . SER B 1 132 ? -22.171 16.074  -29.651 1.00 30.47  ? 112 SER B C     1 
ATOM   3491 O  O     . SER B 1 132 ? -21.406 15.331  -29.031 1.00 28.93  ? 112 SER B O     1 
ATOM   3492 C  CB    . SER B 1 132 ? -22.321 17.984  -28.075 1.00 28.45  ? 112 SER B CB    1 
ATOM   3493 O  OG    . SER B 1 132 ? -21.921 19.321  -27.850 1.00 31.05  ? 112 SER B OG    1 
ATOM   3494 N  N     . LEU B 1 133 ? -23.138 15.603  -30.434 1.00 22.65  ? 113 LEU B N     1 
ATOM   3495 C  CA    . LEU B 1 133 ? -23.408 14.175  -30.488 1.00 23.29  ? 113 LEU B CA    1 
ATOM   3496 C  C     . LEU B 1 133 ? -22.450 13.483  -31.453 1.00 26.68  ? 113 LEU B C     1 
ATOM   3497 O  O     . LEU B 1 133 ? -22.265 13.929  -32.592 1.00 24.83  ? 113 LEU B O     1 
ATOM   3498 C  CB    . LEU B 1 133 ? -24.849 13.918  -30.926 1.00 22.41  ? 113 LEU B CB    1 
ATOM   3499 C  CG    . LEU B 1 133 ? -25.963 14.346  -29.981 1.00 29.40  ? 113 LEU B CG    1 
ATOM   3500 C  CD1   . LEU B 1 133 ? -27.312 14.079  -30.639 1.00 28.32  ? 113 LEU B CD1   1 
ATOM   3501 C  CD2   . LEU B 1 133 ? -25.847 13.603  -28.653 1.00 28.78  ? 113 LEU B CD2   1 
ATOM   3502 N  N     . SER B 1 134 ? -21.867 12.375  -31.004 1.00 24.73  ? 114 SER B N     1 
ATOM   3503 C  CA    . SER B 1 134 ? -21.082 11.508  -31.872 1.00 24.84  ? 114 SER B CA    1 
ATOM   3504 C  C     . SER B 1 134 ? -21.922 10.383  -32.459 1.00 21.45  ? 114 SER B C     1 
ATOM   3505 O  O     . SER B 1 134 ? -21.419 9.591   -33.266 1.00 22.40  ? 114 SER B O     1 
ATOM   3506 C  CB    . SER B 1 134 ? -19.894 10.925  -31.096 1.00 27.64  ? 114 SER B CB    1 
ATOM   3507 O  OG    . SER B 1 134 ? -20.348 10.074  -30.059 1.00 35.28  ? 114 SER B OG    1 
ATOM   3508 N  N     . CYS B 1 135 ? -23.186 10.305  -32.052 1.00 20.47  ? 115 CYS B N     1 
ATOM   3509 C  CA    . CYS B 1 135 ? -24.149 9.266   -32.401 1.00 20.87  ? 115 CYS B CA    1 
ATOM   3510 C  C     . CYS B 1 135 ? -25.398 9.578   -31.596 1.00 21.41  ? 115 CYS B C     1 
ATOM   3511 O  O     . CYS B 1 135 ? -25.381 10.439  -30.709 1.00 24.31  ? 115 CYS B O     1 
ATOM   3512 C  CB    . CYS B 1 135 ? -23.638 7.853   -32.093 1.00 19.90  ? 115 CYS B CB    1 
ATOM   3513 S  SG    . CYS B 1 135 ? -23.090 7.638   -30.361 1.00 25.82  ? 115 CYS B SG    1 
ATOM   3514 N  N     . ALA B 1 136 ? -26.477 8.858   -31.902 1.00 20.42  ? 116 ALA B N     1 
ATOM   3515 C  CA    . ALA B 1 136 ? -27.701 8.997   -31.128 1.00 23.77  ? 116 ALA B CA    1 
ATOM   3516 C  C     . ALA B 1 136 ? -27.440 8.722   -29.651 1.00 26.04  ? 116 ALA B C     1 
ATOM   3517 O  O     . ALA B 1 136 ? -26.609 7.884   -29.288 1.00 25.62  ? 116 ALA B O     1 
ATOM   3518 C  CB    . ALA B 1 136 ? -28.759 8.026   -31.642 1.00 22.83  ? 116 ALA B CB    1 
ATOM   3519 N  N     . LYS B 1 137 ? -28.161 9.438   -28.793 1.00 28.20  ? 117 LYS B N     1 
ATOM   3520 C  CA    . LYS B 1 137 ? -28.126 9.109   -27.376 1.00 30.48  ? 117 LYS B CA    1 
ATOM   3521 C  C     . LYS B 1 137 ? -28.731 7.723   -27.192 1.00 30.82  ? 117 LYS B C     1 
ATOM   3522 O  O     . LYS B 1 137 ? -29.851 7.473   -27.656 1.00 31.14  ? 117 LYS B O     1 
ATOM   3523 C  CB    . LYS B 1 137 ? -28.877 10.140  -26.535 1.00 38.67  ? 117 LYS B CB    1 
ATOM   3524 C  CG    . LYS B 1 137 ? -28.328 11.547  -26.667 1.00 48.94  ? 117 LYS B CG    1 
ATOM   3525 C  CD    . LYS B 1 137 ? -29.230 12.577  -26.003 1.00 60.64  ? 117 LYS B CD    1 
ATOM   3526 C  CE    . LYS B 1 137 ? -28.580 13.950  -26.042 1.00 53.42  ? 117 LYS B CE    1 
ATOM   3527 N  NZ    . LYS B 1 137 ? -27.323 13.990  -25.244 1.00 48.60  ? 117 LYS B NZ    1 
ATOM   3528 N  N     . PRO B 1 138 ? -28.021 6.795   -26.558 1.00 33.86  ? 118 PRO B N     1 
ATOM   3529 C  CA    . PRO B 1 138 ? -28.513 5.416   -26.485 1.00 27.60  ? 118 PRO B CA    1 
ATOM   3530 C  C     . PRO B 1 138 ? -29.673 5.265   -25.516 1.00 31.85  ? 118 PRO B C     1 
ATOM   3531 O  O     . PRO B 1 138 ? -29.787 5.986   -24.522 1.00 36.93  ? 118 PRO B O     1 
ATOM   3532 C  CB    . PRO B 1 138 ? -27.290 4.629   -26.003 1.00 34.08  ? 118 PRO B CB    1 
ATOM   3533 C  CG    . PRO B 1 138 ? -26.479 5.633   -25.240 1.00 37.71  ? 118 PRO B CG    1 
ATOM   3534 C  CD    . PRO B 1 138 ? -26.695 6.952   -25.936 1.00 32.40  ? 118 PRO B CD    1 
ATOM   3535 N  N     . THR B 1 139 ? -30.550 4.322   -25.841 1.00 31.62  ? 119 THR B N     1 
ATOM   3536 C  CA    . THR B 1 139 ? -31.653 3.902   -24.989 1.00 34.92  ? 119 THR B CA    1 
ATOM   3537 C  C     . THR B 1 139 ? -31.620 2.383   -24.891 1.00 39.35  ? 119 THR B C     1 
ATOM   3538 O  O     . THR B 1 139 ? -30.925 1.706   -25.652 1.00 37.37  ? 119 THR B O     1 
ATOM   3539 C  CB    . THR B 1 139 ? -33.015 4.352   -25.542 1.00 36.66  ? 119 THR B CB    1 
ATOM   3540 O  OG1   . THR B 1 139 ? -33.306 3.627   -26.743 1.00 37.51  ? 119 THR B OG1   1 
ATOM   3541 C  CG2   . THR B 1 139 ? -33.007 5.845   -25.855 1.00 37.72  ? 119 THR B CG2   1 
ATOM   3542 N  N     . GLU B 1 140 ? -32.377 1.840   -23.936 1.00 39.94  ? 120 GLU B N     1 
ATOM   3543 C  CA    . GLU B 1 140 ? -32.495 0.390   -23.858 1.00 39.65  ? 120 GLU B CA    1 
ATOM   3544 C  C     . GLU B 1 140 ? -33.066 -0.178  -25.151 1.00 36.91  ? 120 GLU B C     1 
ATOM   3545 O  O     . GLU B 1 140 ? -32.680 -1.272  -25.580 1.00 41.84  ? 120 GLU B O     1 
ATOM   3546 C  CB    . GLU B 1 140 ? -33.340 -0.007  -22.643 1.00 46.72  ? 120 GLU B CB    1 
ATOM   3547 C  CG    . GLU B 1 140 ? -33.620 -1.497  -22.535 1.00 63.74  ? 120 GLU B CG    1 
ATOM   3548 C  CD    . GLU B 1 140 ? -34.445 -1.853  -21.310 1.00 87.36  ? 120 GLU B CD    1 
ATOM   3549 O  OE1   . GLU B 1 140 ? -34.984 -0.931  -20.658 1.00 82.01  ? 120 GLU B OE1   1 
ATOM   3550 O  OE2   . GLU B 1 140 ? -34.553 -3.059  -21.000 1.00 93.06  ? 120 GLU B OE2   1 
ATOM   3551 N  N     . GLU B 1 141 ? -33.970 0.559   -25.794 1.00 35.29  ? 121 GLU B N     1 
ATOM   3552 C  CA    . GLU B 1 141 ? -34.587 0.081   -27.025 1.00 34.06  ? 121 GLU B CA    1 
ATOM   3553 C  C     . GLU B 1 141 ? -33.629 0.170   -28.213 1.00 32.60  ? 121 GLU B C     1 
ATOM   3554 O  O     . GLU B 1 141 ? -33.610 -0.725  -29.068 1.00 32.63  ? 121 GLU B O     1 
ATOM   3555 C  CB    . GLU B 1 141 ? -35.853 0.887   -27.306 1.00 35.89  ? 121 GLU B CB    1 
ATOM   3556 C  CG    . GLU B 1 141 ? -36.648 0.406   -28.505 1.00 35.49  ? 121 GLU B CG    1 
ATOM   3557 C  CD    . GLU B 1 141 ? -37.891 1.238   -28.735 1.00 48.55  ? 121 GLU B CD    1 
ATOM   3558 O  OE1   . GLU B 1 141 ? -37.917 2.402   -28.272 1.00 43.93  ? 121 GLU B OE1   1 
ATOM   3559 O  OE2   . GLU B 1 141 ? -38.843 0.720   -29.364 1.00 43.82  ? 121 GLU B OE2   1 
ATOM   3560 N  N     . PHE B 1 142 ? -32.846 1.247   -28.295 1.00 28.92  ? 122 PHE B N     1 
ATOM   3561 C  CA    . PHE B 1 142 ? -31.986 1.513   -29.449 1.00 29.17  ? 122 PHE B CA    1 
ATOM   3562 C  C     . PHE B 1 142 ? -30.608 1.944   -28.968 1.00 27.01  ? 122 PHE B C     1 
ATOM   3563 O  O     . PHE B 1 142 ? -30.446 3.060   -28.466 1.00 26.88  ? 122 PHE B O     1 
ATOM   3564 C  CB    . PHE B 1 142 ? -32.593 2.591   -30.353 1.00 24.45  ? 122 PHE B CB    1 
ATOM   3565 C  CG    . PHE B 1 142 ? -33.936 2.228   -30.935 1.00 27.77  ? 122 PHE B CG    1 
ATOM   3566 C  CD1   . PHE B 1 142 ? -34.080 1.114   -31.749 1.00 30.04  ? 122 PHE B CD1   1 
ATOM   3567 C  CD2   . PHE B 1 142 ? -35.046 3.030   -30.708 1.00 31.67  ? 122 PHE B CD2   1 
ATOM   3568 C  CE1   . PHE B 1 142 ? -35.310 0.786   -32.299 1.00 32.37  ? 122 PHE B CE1   1 
ATOM   3569 C  CE2   . PHE B 1 142 ? -36.284 2.708   -31.262 1.00 30.07  ? 122 PHE B CE2   1 
ATOM   3570 C  CZ    . PHE B 1 142 ? -36.415 1.586   -32.055 1.00 30.37  ? 122 PHE B CZ    1 
ATOM   3571 N  N     . ASN B 1 143 ? -29.607 1.090   -29.156 1.00 25.14  ? 123 ASN B N     1 
ATOM   3572 C  CA    . ASN B 1 143 ? -28.271 1.372   -28.651 1.00 28.80  ? 123 ASN B CA    1 
ATOM   3573 C  C     . ASN B 1 143 ? -27.251 0.741   -29.585 1.00 27.62  ? 123 ASN B C     1 
ATOM   3574 O  O     . ASN B 1 143 ? -27.613 -0.003  -30.505 1.00 27.38  ? 123 ASN B O     1 
ATOM   3575 C  CB    . ASN B 1 143 ? -28.115 0.852   -27.217 1.00 30.60  ? 123 ASN B CB    1 
ATOM   3576 C  CG    . ASN B 1 143 ? -28.539 -0.590  -27.079 1.00 37.43  ? 123 ASN B CG    1 
ATOM   3577 O  OD1   . ASN B 1 143 ? -27.907 -1.488  -27.629 1.00 37.32  ? 123 ASN B OD1   1 
ATOM   3578 N  ND2   . ASN B 1 143 ? -29.625 -0.820  -26.345 1.00 36.15  ? 123 ASN B ND2   1 
ATOM   3579 N  N     . PRO B 1 144 ? -25.958 1.030   -29.391 1.00 25.76  ? 124 PRO B N     1 
ATOM   3580 C  CA    . PRO B 1 144 ? -24.946 0.408   -30.262 1.00 30.10  ? 124 PRO B CA    1 
ATOM   3581 C  C     . PRO B 1 144 ? -24.920 -1.108  -30.201 1.00 35.14  ? 124 PRO B C     1 
ATOM   3582 O  O     . PRO B 1 144 ? -24.393 -1.732  -31.126 1.00 37.06  ? 124 PRO B O     1 
ATOM   3583 C  CB    . PRO B 1 144 ? -23.628 1.009   -29.757 1.00 30.25  ? 124 PRO B CB    1 
ATOM   3584 C  CG    . PRO B 1 144 ? -24.015 2.329   -29.213 1.00 30.65  ? 124 PRO B CG    1 
ATOM   3585 C  CD    . PRO B 1 144 ? -25.369 2.106   -28.573 1.00 24.09  ? 124 PRO B CD    1 
ATOM   3586 N  N     . ASP B 1 145 ? -25.499 -1.730  -29.172 1.00 34.72  ? 125 ASP B N     1 
ATOM   3587 C  CA    . ASP B 1 145 ? -25.444 -3.186  -29.109 1.00 36.65  ? 125 ASP B CA    1 
ATOM   3588 C  C     . ASP B 1 145 ? -26.460 -3.843  -30.037 1.00 35.04  ? 125 ASP B C     1 
ATOM   3589 O  O     . ASP B 1 145 ? -26.161 -4.880  -30.638 1.00 44.26  ? 125 ASP B O     1 
ATOM   3590 C  CB    . ASP B 1 145 ? -25.646 -3.667  -27.670 1.00 36.95  ? 125 ASP B CB    1 
ATOM   3591 C  CG    . ASP B 1 145 ? -24.508 -3.262  -26.758 1.00 55.09  ? 125 ASP B CG    1 
ATOM   3592 O  OD1   . ASP B 1 145 ? -23.351 -3.222  -27.231 1.00 54.72  ? 125 ASP B OD1   1 
ATOM   3593 O  OD2   . ASP B 1 145 ? -24.770 -2.984  -25.569 1.00 66.43  ? 125 ASP B OD2   1 
ATOM   3594 N  N     . ASN B 1 146 ? -27.660 -3.276  -30.185 1.00 29.47  ? 126 ASN B N     1 
ATOM   3595 C  CA    . ASN B 1 146 ? -28.639 -3.906  -31.065 1.00 32.30  ? 126 ASN B CA    1 
ATOM   3596 C  C     . ASN B 1 146 ? -28.735 -3.257  -32.442 1.00 27.21  ? 126 ASN B C     1 
ATOM   3597 O  O     . ASN B 1 146 ? -29.271 -3.881  -33.363 1.00 29.97  ? 126 ASN B O     1 
ATOM   3598 C  CB    . ASN B 1 146 ? -30.029 -3.958  -30.405 1.00 35.64  ? 126 ASN B CB    1 
ATOM   3599 C  CG    . ASN B 1 146 ? -30.572 -2.590  -30.027 1.00 37.42  ? 126 ASN B CG    1 
ATOM   3600 O  OD1   . ASN B 1 146 ? -29.891 -1.578  -30.131 1.00 34.13  ? 126 ASN B OD1   1 
ATOM   3601 N  ND2   . ASN B 1 146 ? -31.822 -2.565  -29.578 1.00 45.04  ? 126 ASN B ND2   1 
ATOM   3602 N  N     . PHE B 1 147 ? -28.243 -2.034  -32.614 1.00 30.76  ? 127 PHE B N     1 
ATOM   3603 C  CA    . PHE B 1 147 ? -28.191 -1.397  -33.932 1.00 26.60  ? 127 PHE B CA    1 
ATOM   3604 C  C     . PHE B 1 147 ? -26.820 -0.764  -34.146 1.00 23.31  ? 127 PHE B C     1 
ATOM   3605 O  O     . PHE B 1 147 ? -26.699 0.452   -34.333 1.00 22.09  ? 127 PHE B O     1 
ATOM   3606 C  CB    . PHE B 1 147 ? -29.316 -0.372  -34.090 1.00 24.38  ? 127 PHE B CB    1 
ATOM   3607 C  CG    . PHE B 1 147 ? -30.677 -0.999  -34.337 1.00 25.97  ? 127 PHE B CG    1 
ATOM   3608 C  CD1   . PHE B 1 147 ? -31.093 -1.312  -35.627 1.00 26.14  ? 127 PHE B CD1   1 
ATOM   3609 C  CD2   . PHE B 1 147 ? -31.533 -1.278  -33.276 1.00 28.59  ? 127 PHE B CD2   1 
ATOM   3610 C  CE1   . PHE B 1 147 ? -32.344 -1.892  -35.858 1.00 29.80  ? 127 PHE B CE1   1 
ATOM   3611 C  CE2   . PHE B 1 147 ? -32.789 -1.861  -33.497 1.00 28.88  ? 127 PHE B CE2   1 
ATOM   3612 C  CZ    . PHE B 1 147 ? -33.193 -2.162  -34.791 1.00 29.83  ? 127 PHE B CZ    1 
ATOM   3613 N  N     . PRO B 1 148 ? -25.753 -1.570  -34.125 1.00 28.45  ? 128 PRO B N     1 
ATOM   3614 C  CA    . PRO B 1 148 ? -24.409 -0.996  -34.289 1.00 26.97  ? 128 PRO B CA    1 
ATOM   3615 C  C     . PRO B 1 148 ? -24.198 -0.342  -35.641 1.00 26.45  ? 128 PRO B C     1 
ATOM   3616 O  O     . PRO B 1 148 ? -23.373 0.571   -35.741 1.00 27.34  ? 128 PRO B O     1 
ATOM   3617 C  CB    . PRO B 1 148 ? -23.483 -2.207  -34.097 1.00 27.87  ? 128 PRO B CB    1 
ATOM   3618 C  CG    . PRO B 1 148 ? -24.308 -3.370  -34.484 1.00 30.67  ? 128 PRO B CG    1 
ATOM   3619 C  CD    . PRO B 1 148 ? -25.706 -3.043  -34.030 1.00 37.34  ? 128 PRO B CD    1 
ATOM   3620 N  N     . GLU B 1 149 ? -24.945 -0.741  -36.669 1.00 27.98  ? 129 GLU B N     1 
ATOM   3621 C  CA    . GLU B 1 149 ? -24.770 -0.179  -38.005 1.00 27.45  ? 129 GLU B CA    1 
ATOM   3622 C  C     . GLU B 1 149 ? -25.361 1.221   -38.154 1.00 25.48  ? 129 GLU B C     1 
ATOM   3623 O  O     . GLU B 1 149 ? -25.166 1.853   -39.201 1.00 25.30  ? 129 GLU B O     1 
ATOM   3624 C  CB    . GLU B 1 149 ? -25.385 -1.117  -39.048 1.00 29.80  ? 129 GLU B CB    1 
ATOM   3625 C  CG    . GLU B 1 149 ? -26.901 -1.221  -38.998 1.00 29.69  ? 129 GLU B CG    1 
ATOM   3626 C  CD    . GLU B 1 149 ? -27.432 -2.186  -37.939 1.00 32.34  ? 129 GLU B CD    1 
ATOM   3627 O  OE1   . GLU B 1 149 ? -26.709 -2.534  -36.985 1.00 33.05  ? 129 GLU B OE1   1 
ATOM   3628 O  OE2   . GLU B 1 149 ? -28.602 -2.601  -38.072 1.00 46.18  ? 129 GLU B OE2   1 
ATOM   3629 N  N     . TYR B 1 150 ? -26.078 1.721   -37.144 1.00 21.61  ? 130 TYR B N     1 
ATOM   3630 C  CA    . TYR B 1 150 ? -26.630 3.069   -37.164 1.00 18.88  ? 130 TYR B CA    1 
ATOM   3631 C  C     . TYR B 1 150 ? -26.195 3.926   -35.991 1.00 21.03  ? 130 TYR B C     1 
ATOM   3632 O  O     . TYR B 1 150 ? -26.151 5.147   -36.129 1.00 19.35  ? 130 TYR B O     1 
ATOM   3633 C  CB    . TYR B 1 150 ? -28.170 3.037   -37.176 1.00 21.55  ? 130 TYR B CB    1 
ATOM   3634 C  CG    . TYR B 1 150 ? -28.803 2.465   -38.426 1.00 21.01  ? 130 TYR B CG    1 
ATOM   3635 C  CD1   . TYR B 1 150 ? -28.832 3.190   -39.616 1.00 19.83  ? 130 TYR B CD1   1 
ATOM   3636 C  CD2   . TYR B 1 150 ? -29.395 1.211   -38.408 1.00 20.16  ? 130 TYR B CD2   1 
ATOM   3637 C  CE1   . TYR B 1 150 ? -29.430 2.661   -40.766 1.00 20.78  ? 130 TYR B CE1   1 
ATOM   3638 C  CE2   . TYR B 1 150 ? -29.984 0.677   -39.546 1.00 24.45  ? 130 TYR B CE2   1 
ATOM   3639 C  CZ    . TYR B 1 150 ? -29.998 1.408   -40.721 1.00 23.87  ? 130 TYR B CZ    1 
ATOM   3640 O  OH    . TYR B 1 150 ? -30.597 0.878   -41.843 1.00 21.84  ? 130 TYR B OH    1 
ATOM   3641 N  N     . LEU B 1 151 ? -25.898 3.328   -34.839 1.00 23.32  ? 131 LEU B N     1 
ATOM   3642 C  CA    . LEU B 1 151 ? -25.777 4.096   -33.606 1.00 22.87  ? 131 LEU B CA    1 
ATOM   3643 C  C     . LEU B 1 151 ? -24.377 4.079   -33.005 1.00 25.50  ? 131 LEU B C     1 
ATOM   3644 O  O     . LEU B 1 151 ? -24.195 4.579   -31.888 1.00 22.55  ? 131 LEU B O     1 
ATOM   3645 C  CB    . LEU B 1 151 ? -26.784 3.579   -32.565 1.00 21.55  ? 131 LEU B CB    1 
ATOM   3646 C  CG    . LEU B 1 151 ? -28.233 3.464   -33.044 1.00 23.03  ? 131 LEU B CG    1 
ATOM   3647 C  CD1   . LEU B 1 151 ? -29.082 2.876   -31.917 1.00 26.53  ? 131 LEU B CD1   1 
ATOM   3648 C  CD2   . LEU B 1 151 ? -28.795 4.804   -33.490 1.00 22.33  ? 131 LEU B CD2   1 
ATOM   3649 N  N     . SER B 1 152 ? -23.382 3.535   -33.702 1.00 22.49  ? 132 SER B N     1 
ATOM   3650 C  CA    . SER B 1 152 ? -22.035 3.534   -33.158 1.00 23.89  ? 132 SER B CA    1 
ATOM   3651 C  C     . SER B 1 152 ? -21.421 4.933   -33.238 1.00 24.19  ? 132 SER B C     1 
ATOM   3652 O  O     . SER B 1 152 ? -21.693 5.691   -34.177 1.00 25.22  ? 132 SER B O     1 
ATOM   3653 C  CB    . SER B 1 152 ? -21.162 2.531   -33.903 1.00 22.02  ? 132 SER B CB    1 
ATOM   3654 O  OG    . SER B 1 152 ? -21.663 1.216   -33.760 1.00 26.51  ? 132 SER B OG    1 
ATOM   3655 N  N     . PRO B 1 153 ? -20.583 5.303   -32.262 1.00 22.65  ? 133 PRO B N     1 
ATOM   3656 C  CA    A PRO B 1 153 ? -19.964 6.633   -32.279 0.44 21.42  ? 133 PRO B CA    1 
ATOM   3657 C  CA    B PRO B 1 153 ? -19.974 6.636   -32.286 0.56 21.37  ? 133 PRO B CA    1 
ATOM   3658 C  C     . PRO B 1 153 ? -19.010 6.800   -33.452 1.00 20.80  ? 133 PRO B C     1 
ATOM   3659 O  O     . PRO B 1 153 ? -18.322 5.863   -33.861 1.00 24.37  ? 133 PRO B O     1 
ATOM   3660 C  CB    A PRO B 1 153 ? -19.211 6.695   -30.943 0.44 23.97  ? 133 PRO B CB    1 
ATOM   3661 C  CB    B PRO B 1 153 ? -19.236 6.713   -30.943 0.56 24.00  ? 133 PRO B CB    1 
ATOM   3662 C  CG    A PRO B 1 153 ? -19.871 5.682   -30.082 0.44 20.54  ? 133 PRO B CG    1 
ATOM   3663 C  CG    B PRO B 1 153 ? -18.972 5.303   -30.591 0.56 21.15  ? 133 PRO B CG    1 
ATOM   3664 C  CD    A PRO B 1 153 ? -20.327 4.586   -31.000 0.44 24.71  ? 133 PRO B CD    1 
ATOM   3665 C  CD    B PRO B 1 153 ? -20.184 4.543   -31.064 0.56 25.03  ? 133 PRO B CD    1 
ATOM   3666 N  N     . ASN B 1 154 ? -18.982 8.015   -33.989 1.00 21.76  ? 134 ASN B N     1 
ATOM   3667 C  CA    . ASN B 1 154 ? -18.097 8.338   -35.100 1.00 18.96  ? 134 ASN B CA    1 
ATOM   3668 C  C     . ASN B 1 154 ? -16.642 8.225   -34.668 1.00 24.78  ? 134 ASN B C     1 
ATOM   3669 O  O     . ASN B 1 154 ? -16.294 8.518   -33.520 1.00 24.45  ? 134 ASN B O     1 
ATOM   3670 C  CB    . ASN B 1 154 ? -18.379 9.744   -35.619 1.00 19.00  ? 134 ASN B CB    1 
ATOM   3671 C  CG    . ASN B 1 154 ? -19.640 9.805   -36.451 1.00 17.22  ? 134 ASN B CG    1 
ATOM   3672 O  OD1   . ASN B 1 154 ? -20.084 8.794   -37.013 1.00 20.70  ? 134 ASN B OD1   1 
ATOM   3673 N  ND2   . ASN B 1 154 ? -20.227 10.982  -36.528 1.00 18.07  ? 134 ASN B ND2   1 
ATOM   3674 N  N     . LEU B 1 155 ? -15.793 7.774   -35.597 1.00 20.18  ? 135 LEU B N     1 
ATOM   3675 C  CA    . LEU B 1 155 ? -14.354 7.611   -35.366 1.00 19.84  ? 135 LEU B CA    1 
ATOM   3676 C  C     . LEU B 1 155 ? -13.591 8.545   -36.294 1.00 24.17  ? 135 LEU B C     1 
ATOM   3677 O  O     . LEU B 1 155 ? -13.602 8.356   -37.514 1.00 25.90  ? 135 LEU B O     1 
ATOM   3678 C  CB    . LEU B 1 155 ? -13.925 6.159   -35.593 1.00 19.83  ? 135 LEU B CB    1 
ATOM   3679 C  CG    . LEU B 1 155 ? -14.590 5.070   -34.747 1.00 26.58  ? 135 LEU B CG    1 
ATOM   3680 C  CD1   . LEU B 1 155 ? -14.118 3.703   -35.190 1.00 33.91  ? 135 LEU B CD1   1 
ATOM   3681 C  CD2   . LEU B 1 155 ? -14.289 5.290   -33.265 1.00 29.53  ? 135 LEU B CD2   1 
ATOM   3682 N  N     . TRP B 1 156 ? -12.928 9.557   -35.720 1.00 23.01  ? 136 TRP B N     1 
ATOM   3683 C  CA    . TRP B 1 156 ? -12.237 10.569  -36.511 1.00 22.90  ? 136 TRP B CA    1 
ATOM   3684 C  C     . TRP B 1 156 ? -10.731 10.446  -36.362 1.00 25.50  ? 136 TRP B C     1 
ATOM   3685 O  O     . TRP B 1 156 ? -10.244 10.150  -35.265 1.00 24.21  ? 136 TRP B O     1 
ATOM   3686 C  CB    . TRP B 1 156 ? -12.646 11.977  -36.063 1.00 25.01  ? 136 TRP B CB    1 
ATOM   3687 C  CG    . TRP B 1 156 ? -14.090 12.254  -36.234 1.00 23.92  ? 136 TRP B CG    1 
ATOM   3688 C  CD1   . TRP B 1 156 ? -15.058 12.178  -35.272 1.00 24.42  ? 136 TRP B CD1   1 
ATOM   3689 C  CD2   . TRP B 1 156 ? -14.750 12.653  -37.440 1.00 22.45  ? 136 TRP B CD2   1 
ATOM   3690 N  NE1   . TRP B 1 156 ? -16.279 12.508  -35.804 1.00 23.02  ? 136 TRP B NE1   1 
ATOM   3691 C  CE2   . TRP B 1 156 ? -16.120 12.801  -37.133 1.00 23.08  ? 136 TRP B CE2   1 
ATOM   3692 C  CE3   . TRP B 1 156 ? -14.317 12.902  -38.745 1.00 23.07  ? 136 TRP B CE3   1 
ATOM   3693 C  CZ2   . TRP B 1 156 ? -17.060 13.188  -38.087 1.00 24.64  ? 136 TRP B CZ2   1 
ATOM   3694 C  CZ3   . TRP B 1 156 ? -15.246 13.279  -39.689 1.00 20.36  ? 136 TRP B CZ3   1 
ATOM   3695 C  CH2   . TRP B 1 156 ? -16.605 13.425  -39.355 1.00 24.69  ? 136 TRP B CH2   1 
ATOM   3696 N  N     . PRO B 1 157 ? -9.961  10.695  -37.414 1.00 26.24  ? 137 PRO B N     1 
ATOM   3697 C  CA    . PRO B 1 157 ? -8.526  10.895  -37.211 1.00 25.16  ? 137 PRO B CA    1 
ATOM   3698 C  C     . PRO B 1 157 ? -8.305  12.141  -36.361 1.00 25.30  ? 137 PRO B C     1 
ATOM   3699 O  O     . PRO B 1 157 ? -9.149  13.034  -36.295 1.00 27.35  ? 137 PRO B O     1 
ATOM   3700 C  CB    . PRO B 1 157 ? -7.978  11.065  -38.635 1.00 28.11  ? 137 PRO B CB    1 
ATOM   3701 C  CG    . PRO B 1 157 ? -9.138  11.523  -39.439 1.00 31.32  ? 137 PRO B CG    1 
ATOM   3702 C  CD    . PRO B 1 157 ? -10.371 10.925  -38.810 1.00 27.17  ? 137 PRO B CD    1 
ATOM   3703 N  N     . GLN B 1 158 ? -7.155  12.190  -35.682 1.00 32.54  ? 138 GLN B N     1 
ATOM   3704 C  CA    . GLN B 1 158 ? -6.832  13.376  -34.893 1.00 31.85  ? 138 GLN B CA    1 
ATOM   3705 C  C     . GLN B 1 158 ? -6.733  14.599  -35.789 1.00 27.68  ? 138 GLN B C     1 
ATOM   3706 O  O     . GLN B 1 158 ? -6.218  14.523  -36.910 1.00 30.20  ? 138 GLN B O     1 
ATOM   3707 C  CB    . GLN B 1 158 ? -5.517  13.194  -34.124 1.00 41.46  ? 138 GLN B CB    1 
ATOM   3708 C  CG    . GLN B 1 158 ? -5.570  12.163  -33.021 1.00 42.95  ? 138 GLN B CG    1 
ATOM   3709 C  CD    . GLN B 1 158 ? -5.970  12.787  -31.696 1.00 43.94  ? 138 GLN B CD    1 
ATOM   3710 O  OE1   . GLN B 1 158 ? -5.732  13.975  -31.461 1.00 51.60  ? 138 GLN B OE1   1 
ATOM   3711 N  NE2   . GLN B 1 158 ? -6.592  11.998  -30.830 1.00 57.16  ? 138 GLN B NE2   1 
ATOM   3712 N  N     . GLU B 1 159 ? -7.222  15.739  -35.279 1.00 28.97  ? 139 GLU B N     1 
ATOM   3713 C  CA    . GLU B 1 159 ? -7.187  16.971  -36.057 1.00 30.53  ? 139 GLU B CA    1 
ATOM   3714 C  C     . GLU B 1 159 ? -5.794  17.256  -36.580 1.00 30.70  ? 139 GLU B C     1 
ATOM   3715 O  O     . GLU B 1 159 ? -5.627  17.647  -37.738 1.00 33.80  ? 139 GLU B O     1 
ATOM   3716 C  CB    . GLU B 1 159 ? -7.693  18.148  -35.212 1.00 29.96  ? 139 GLU B CB    1 
ATOM   3717 C  CG    . GLU B 1 159 ? -7.206  19.536  -35.669 1.00 31.72  ? 139 GLU B CG    1 
ATOM   3718 C  CD    . GLU B 1 159 ? -7.778  20.015  -37.006 1.00 32.44  ? 139 GLU B CD    1 
ATOM   3719 O  OE1   . GLU B 1 159 ? -8.724  19.395  -37.509 1.00 32.12  ? 139 GLU B OE1   1 
ATOM   3720 O  OE2   . GLU B 1 159 ? -7.262  21.022  -37.551 1.00 41.58  ? 139 GLU B OE2   1 
ATOM   3721 N  N     . SER B 1 160 ? -4.768  17.024  -35.759 1.00 26.53  ? 140 SER B N     1 
ATOM   3722 C  CA    . SER B 1 160 ? -3.417  17.331  -36.207 1.00 27.65  ? 140 SER B CA    1 
ATOM   3723 C  C     . SER B 1 160 ? -2.916  16.348  -37.263 1.00 28.26  ? 140 SER B C     1 
ATOM   3724 O  O     . SER B 1 160 ? -1.976  16.673  -37.991 1.00 31.03  ? 140 SER B O     1 
ATOM   3725 C  CB    . SER B 1 160 ? -2.486  17.436  -35.003 1.00 40.16  ? 140 SER B CB    1 
ATOM   3726 O  OG    . SER B 1 160 ? -2.745  18.667  -34.334 1.00 31.93  ? 140 SER B OG    1 
ATOM   3727 N  N     . THR B 1 161 ? -3.515  15.159  -37.373 1.00 27.14  ? 141 THR B N     1 
ATOM   3728 C  CA    . THR B 1 161 ? -3.072  14.211  -38.398 1.00 24.89  ? 141 THR B CA    1 
ATOM   3729 C  C     . THR B 1 161 ? -3.717  14.491  -39.756 1.00 30.16  ? 141 THR B C     1 
ATOM   3730 O  O     . THR B 1 161 ? -3.090  14.282  -40.805 1.00 27.16  ? 141 THR B O     1 
ATOM   3731 C  CB    . THR B 1 161 ? -3.420  12.787  -37.955 1.00 37.14  ? 141 THR B CB    1 
ATOM   3732 O  OG1   . THR B 1 161 ? -2.759  12.494  -36.718 1.00 35.22  ? 141 THR B OG1   1 
ATOM   3733 C  CG2   . THR B 1 161 ? -3.030  11.755  -39.015 1.00 38.76  ? 141 THR B CG2   1 
ATOM   3734 N  N     . LEU B 1 162 ? -4.937  15.007  -39.756 1.00 27.37  ? 142 LEU B N     1 
ATOM   3735 C  CA    . LEU B 1 162 ? -5.649  15.361  -40.985 1.00 25.82  ? 142 LEU B CA    1 
ATOM   3736 C  C     . LEU B 1 162 ? -6.367  16.673  -40.729 1.00 20.77  ? 142 LEU B C     1 
ATOM   3737 O  O     . LEU B 1 162 ? -7.576  16.698  -40.463 1.00 22.16  ? 142 LEU B O     1 
ATOM   3738 C  CB    . LEU B 1 162 ? -6.618  14.252  -41.415 1.00 25.10  ? 142 LEU B CB    1 
ATOM   3739 C  CG    . LEU B 1 162 ? -7.112  14.363  -42.864 1.00 23.09  ? 142 LEU B CG    1 
ATOM   3740 C  CD1   . LEU B 1 162 ? -5.957  14.350  -43.847 1.00 24.93  ? 142 LEU B CD1   1 
ATOM   3741 C  CD2   . LEU B 1 162 ? -8.067  13.221  -43.191 1.00 20.95  ? 142 LEU B CD2   1 
ATOM   3742 N  N     . PRO B 1 163 ? -5.639  17.792  -40.771 1.00 19.19  ? 143 PRO B N     1 
ATOM   3743 C  CA    . PRO B 1 163 ? -6.205  19.076  -40.326 1.00 22.91  ? 143 PRO B CA    1 
ATOM   3744 C  C     . PRO B 1 163 ? -7.367  19.520  -41.193 1.00 19.66  ? 143 PRO B C     1 
ATOM   3745 O  O     . PRO B 1 163 ? -7.265  19.568  -42.422 1.00 21.65  ? 143 PRO B O     1 
ATOM   3746 C  CB    . PRO B 1 163 ? -5.025  20.050  -40.451 1.00 26.43  ? 143 PRO B CB    1 
ATOM   3747 C  CG    . PRO B 1 163 ? -3.815  19.198  -40.556 1.00 29.46  ? 143 PRO B CG    1 
ATOM   3748 C  CD    . PRO B 1 163 ? -4.227  17.908  -41.173 1.00 24.94  ? 143 PRO B CD    1 
ATOM   3749 N  N     . GLY B 1 164 ? -8.461  19.890  -40.526 1.00 19.43  ? 144 GLY B N     1 
ATOM   3750 C  CA    . GLY B 1 164 ? -9.645  20.415  -41.168 1.00 19.52  ? 144 GLY B CA    1 
ATOM   3751 C  C     . GLY B 1 164 ? -10.639 19.384  -41.653 1.00 18.45  ? 144 GLY B C     1 
ATOM   3752 O  O     . GLY B 1 164 ? -11.699 19.774  -42.151 1.00 18.81  ? 144 GLY B O     1 
ATOM   3753 N  N     . PHE B 1 165 ? -10.343 18.093  -41.508 1.00 20.47  ? 145 PHE B N     1 
ATOM   3754 C  CA    . PHE B 1 165 ? -11.220 17.066  -42.073 1.00 18.05  ? 145 PHE B CA    1 
ATOM   3755 C  C     . PHE B 1 165 ? -12.576 17.055  -41.395 1.00 19.09  ? 145 PHE B C     1 
ATOM   3756 O  O     . PHE B 1 165 ? -13.619 17.131  -42.069 1.00 18.57  ? 145 PHE B O     1 
ATOM   3757 C  CB    . PHE B 1 165 ? -10.556 15.697  -41.976 1.00 19.40  ? 145 PHE B CB    1 
ATOM   3758 C  CG    . PHE B 1 165 ? -11.461 14.550  -42.347 1.00 18.70  ? 145 PHE B CG    1 
ATOM   3759 C  CD1   . PHE B 1 165 ? -12.014 14.464  -43.615 1.00 20.69  ? 145 PHE B CD1   1 
ATOM   3760 C  CD2   . PHE B 1 165 ? -11.680 13.514  -41.458 1.00 24.11  ? 145 PHE B CD2   1 
ATOM   3761 C  CE1   . PHE B 1 165 ? -12.823 13.383  -43.961 1.00 21.28  ? 145 PHE B CE1   1 
ATOM   3762 C  CE2   . PHE B 1 165 ? -12.491 12.429  -41.797 1.00 21.99  ? 145 PHE B CE2   1 
ATOM   3763 C  CZ    . PHE B 1 165 ? -13.050 12.364  -43.057 1.00 19.23  ? 145 PHE B CZ    1 
ATOM   3764 N  N     . LYS B 1 166 ? -12.591 16.968  -40.065 1.00 19.41  ? 146 LYS B N     1 
ATOM   3765 C  CA    . LYS B 1 166 ? -13.872 16.882  -39.368 1.00 18.21  ? 146 LYS B CA    1 
ATOM   3766 C  C     . LYS B 1 166 ? -14.728 18.127  -39.578 1.00 18.56  ? 146 LYS B C     1 
ATOM   3767 O  O     . LYS B 1 166 ? -15.912 17.975  -39.928 1.00 17.29  ? 146 LYS B O     1 
ATOM   3768 C  CB    . LYS B 1 166 ? -13.644 16.580  -37.881 1.00 17.10  ? 146 LYS B CB    1 
ATOM   3769 C  CG    . LYS B 1 166 ? -14.936 16.471  -37.073 1.00 20.78  ? 146 LYS B CG    1 
ATOM   3770 C  CD    . LYS B 1 166 ? -14.620 15.904  -35.681 1.00 22.30  ? 146 LYS B CD    1 
ATOM   3771 C  CE    . LYS B 1 166 ? -15.857 15.729  -34.813 1.00 22.45  ? 146 LYS B CE    1 
ATOM   3772 N  NZ    . LYS B 1 166 ? -16.481 17.014  -34.391 1.00 27.30  ? 146 LYS B NZ    1 
ATOM   3773 N  N     . PRO B 1 167 ? -14.230 19.360  -39.396 1.00 15.85  ? 147 PRO B N     1 
ATOM   3774 C  CA    . PRO B 1 167 ? -15.099 20.524  -39.639 1.00 19.95  ? 147 PRO B CA    1 
ATOM   3775 C  C     . PRO B 1 167 ? -15.583 20.633  -41.074 1.00 18.99  ? 147 PRO B C     1 
ATOM   3776 O  O     . PRO B 1 167 ? -16.719 21.066  -41.293 1.00 17.40  ? 147 PRO B O     1 
ATOM   3777 C  CB    . PRO B 1 167 ? -14.218 21.718  -39.240 1.00 19.73  ? 147 PRO B CB    1 
ATOM   3778 C  CG    . PRO B 1 167 ? -13.208 21.124  -38.302 1.00 21.68  ? 147 PRO B CG    1 
ATOM   3779 C  CD    . PRO B 1 167 ? -12.920 19.768  -38.850 1.00 17.46  ? 147 PRO B CD    1 
ATOM   3780 N  N     . THR B 1 168 ? -14.758 20.271  -42.059 1.00 17.25  ? 148 THR B N     1 
ATOM   3781 C  CA    . THR B 1 168 ? -15.217 20.300  -43.448 1.00 17.04  ? 148 THR B CA    1 
ATOM   3782 C  C     . THR B 1 168 ? -16.331 19.289  -43.671 1.00 18.24  ? 148 THR B C     1 
ATOM   3783 O  O     . THR B 1 168 ? -17.339 19.598  -44.322 1.00 17.68  ? 148 THR B O     1 
ATOM   3784 C  CB    . THR B 1 168 ? -14.057 20.025  -44.402 1.00 19.82  ? 148 THR B CB    1 
ATOM   3785 O  OG1   . THR B 1 168 ? -13.015 20.994  -44.179 1.00 21.51  ? 148 THR B OG1   1 
ATOM   3786 C  CG2   . THR B 1 168 ? -14.528 20.115  -45.856 1.00 20.49  ? 148 THR B CG2   1 
ATOM   3787 N  N     . PHE B 1 169 ? -16.149 18.073  -43.146 1.00 17.98  ? 149 PHE B N     1 
ATOM   3788 C  CA    . PHE B 1 169 ? -17.175 17.026  -43.221 1.00 14.95  ? 149 PHE B CA    1 
ATOM   3789 C  C     . PHE B 1 169 ? -18.478 17.512  -42.604 1.00 17.96  ? 149 PHE B C     1 
ATOM   3790 O  O     . PHE B 1 169 ? -19.555 17.411  -43.211 1.00 18.33  ? 149 PHE B O     1 
ATOM   3791 C  CB    . PHE B 1 169 ? -16.645 15.775  -42.491 1.00 16.10  ? 149 PHE B CB    1 
ATOM   3792 C  CG    . PHE B 1 169 ? -17.367 14.493  -42.831 1.00 18.52  ? 149 PHE B CG    1 
ATOM   3793 C  CD1   . PHE B 1 169 ? -18.649 14.248  -42.339 1.00 17.06  ? 149 PHE B CD1   1 
ATOM   3794 C  CD2   . PHE B 1 169 ? -16.745 13.517  -43.596 1.00 19.26  ? 149 PHE B CD2   1 
ATOM   3795 C  CE1   . PHE B 1 169 ? -19.306 13.050  -42.637 1.00 18.08  ? 149 PHE B CE1   1 
ATOM   3796 C  CE2   . PHE B 1 169 ? -17.390 12.321  -43.892 1.00 18.46  ? 149 PHE B CE2   1 
ATOM   3797 C  CZ    . PHE B 1 169 ? -18.680 12.092  -43.418 1.00 17.94  ? 149 PHE B CZ    1 
ATOM   3798 N  N     . GLU B 1 170 ? -18.396 18.061  -41.388 1.00 17.37  ? 150 GLU B N     1 
ATOM   3799 C  CA    . GLU B 1 170 ? -19.597 18.531  -40.695 1.00 16.92  ? 150 GLU B CA    1 
ATOM   3800 C  C     . GLU B 1 170 ? -20.270 19.686  -41.439 1.00 18.40  ? 150 GLU B C     1 
ATOM   3801 O  O     . GLU B 1 170 ? -21.497 19.700  -41.585 1.00 19.18  ? 150 GLU B O     1 
ATOM   3802 C  CB    . GLU B 1 170 ? -19.223 18.943  -39.270 1.00 19.58  ? 150 GLU B CB    1 
ATOM   3803 C  CG    . GLU B 1 170 ? -18.920 17.752  -38.375 1.00 17.79  ? 150 GLU B CG    1 
ATOM   3804 C  CD    . GLU B 1 170 ? -18.221 18.164  -37.084 1.00 34.42  ? 150 GLU B CD    1 
ATOM   3805 O  OE1   . GLU B 1 170 ? -17.475 19.177  -37.104 1.00 30.68  ? 150 GLU B OE1   1 
ATOM   3806 O  OE2   . GLU B 1 170 ? -18.406 17.478  -36.063 1.00 37.50  ? 150 GLU B OE2   1 
ATOM   3807 N  N     . ASP B 1 171 ? -19.489 20.666  -41.917 1.00 18.12  ? 151 ASP B N     1 
ATOM   3808 C  CA    . ASP B 1 171 ? -20.075 21.816  -42.592 1.00 17.30  ? 151 ASP B CA    1 
ATOM   3809 C  C     . ASP B 1 171 ? -20.743 21.408  -43.901 1.00 18.62  ? 151 ASP B C     1 
ATOM   3810 O  O     . ASP B 1 171 ? -21.850 21.877  -44.211 1.00 18.97  ? 151 ASP B O     1 
ATOM   3811 C  CB    . ASP B 1 171 ? -19.013 22.894  -42.847 1.00 17.54  ? 151 ASP B CB    1 
ATOM   3812 C  CG    . ASP B 1 171 ? -18.647 23.678  -41.587 1.00 24.22  ? 151 ASP B CG    1 
ATOM   3813 O  OD1   . ASP B 1 171 ? -19.377 23.575  -40.580 1.00 24.65  ? 151 ASP B OD1   1 
ATOM   3814 O  OD2   . ASP B 1 171 ? -17.615 24.397  -41.622 1.00 25.68  ? 151 ASP B OD2   1 
ATOM   3815 N  N     . LEU B 1 172 ? -20.104 20.523  -44.671 1.00 16.45  ? 152 LEU B N     1 
ATOM   3816 C  CA    . LEU B 1 172 ? -20.714 20.128  -45.939 1.00 15.19  ? 152 LEU B CA    1 
ATOM   3817 C  C     . LEU B 1 172 ? -21.951 19.275  -45.703 1.00 16.86  ? 152 LEU B C     1 
ATOM   3818 O  O     . LEU B 1 172 ? -22.979 19.474  -46.371 1.00 17.59  ? 152 LEU B O     1 
ATOM   3819 C  CB    . LEU B 1 172 ? -19.700 19.380  -46.822 1.00 16.37  ? 152 LEU B CB    1 
ATOM   3820 C  CG    . LEU B 1 172 ? -20.266 18.921  -48.178 1.00 16.49  ? 152 LEU B CG    1 
ATOM   3821 C  CD1   . LEU B 1 172 ? -20.971 20.057  -48.912 1.00 16.23  ? 152 LEU B CD1   1 
ATOM   3822 C  CD2   . LEU B 1 172 ? -19.155 18.332  -49.039 1.00 18.19  ? 152 LEU B CD2   1 
ATOM   3823 N  N     . CYS B 1 173 ? -21.880 18.324  -44.764 1.00 15.89  ? 153 CYS B N     1 
ATOM   3824 C  CA    . CYS B 1 173 ? -23.072 17.529  -44.476 1.00 15.14  ? 153 CYS B CA    1 
ATOM   3825 C  C     . CYS B 1 173 ? -24.200 18.408  -43.966 1.00 18.61  ? 153 CYS B C     1 
ATOM   3826 O  O     . CYS B 1 173 ? -25.359 18.196  -44.332 1.00 17.30  ? 153 CYS B O     1 
ATOM   3827 C  CB    . CYS B 1 173 ? -22.759 16.412  -43.480 1.00 18.99  ? 153 CYS B CB    1 
ATOM   3828 S  SG    . CYS B 1 173 ? -21.775 15.087  -44.213 1.00 20.21  ? 153 CYS B SG    1 
ATOM   3829 N  N     . ARG B 1 174 ? -23.901 19.405  -43.130 1.00 15.24  ? 154 ARG B N     1 
ATOM   3830 C  CA    . ARG B 1 174 ? -24.982 20.269  -42.650 1.00 16.44  ? 154 ARG B CA    1 
ATOM   3831 C  C     . ARG B 1 174 ? -25.624 21.035  -43.795 1.00 19.66  ? 154 ARG B C     1 
ATOM   3832 O  O     . ARG B 1 174 ? -26.855 21.197  -43.833 1.00 18.86  ? 154 ARG B O     1 
ATOM   3833 C  CB    . ARG B 1 174 ? -24.472 21.236  -41.572 1.00 17.86  ? 154 ARG B CB    1 
ATOM   3834 C  CG    . ARG B 1 174 ? -25.581 22.190  -41.079 1.00 18.72  ? 154 ARG B CG    1 
ATOM   3835 C  CD    . ARG B 1 174 ? -25.147 23.044  -39.881 1.00 19.53  ? 154 ARG B CD    1 
ATOM   3836 N  NE    . ARG B 1 174 ? -24.668 22.224  -38.772 1.00 21.31  ? 154 ARG B NE    1 
ATOM   3837 C  CZ    . ARG B 1 174 ? -25.453 21.593  -37.909 1.00 21.36  ? 154 ARG B CZ    1 
ATOM   3838 N  NH1   . ARG B 1 174 ? -26.774 21.665  -37.989 1.00 22.75  ? 154 ARG B NH1   1 
ATOM   3839 N  NH2   . ARG B 1 174 ? -24.900 20.870  -36.942 1.00 26.36  ? 154 ARG B NH2   1 
ATOM   3840 N  N     . LEU B 1 175 ? -24.814 21.522  -44.734 1.00 16.61  ? 155 LEU B N     1 
ATOM   3841 C  CA    . LEU B 1 175 ? -25.361 22.209  -45.903 1.00 17.48  ? 155 LEU B CA    1 
ATOM   3842 C  C     . LEU B 1 175 ? -26.268 21.279  -46.715 1.00 20.60  ? 155 LEU B C     1 
ATOM   3843 O  O     . LEU B 1 175 ? -27.400 21.638  -47.080 1.00 17.89  ? 155 LEU B O     1 
ATOM   3844 C  CB    . LEU B 1 175 ? -24.196 22.743  -46.745 1.00 18.59  ? 155 LEU B CB    1 
ATOM   3845 C  CG    . LEU B 1 175 ? -24.478 23.631  -47.956 1.00 18.15  ? 155 LEU B CG    1 
ATOM   3846 C  CD1   . LEU B 1 175 ? -23.177 24.347  -48.310 1.00 23.02  ? 155 LEU B CD1   1 
ATOM   3847 C  CD2   . LEU B 1 175 ? -24.988 22.851  -49.176 1.00 21.60  ? 155 LEU B CD2   1 
ATOM   3848 N  N     . ILE B 1 176 ? -25.789 20.064  -46.990 1.00 17.22  ? 156 ILE B N     1 
ATOM   3849 C  CA    . ILE B 1 176 ? -26.577 19.124  -47.796 1.00 15.04  ? 156 ILE B CA    1 
ATOM   3850 C  C     . ILE B 1 176 ? -27.860 18.721  -47.074 1.00 19.48  ? 156 ILE B C     1 
ATOM   3851 O  O     . ILE B 1 176 ? -28.934 18.641  -47.690 1.00 16.60  ? 156 ILE B O     1 
ATOM   3852 C  CB    . ILE B 1 176 ? -25.731 17.892  -48.172 1.00 14.93  ? 156 ILE B CB    1 
ATOM   3853 C  CG1   . ILE B 1 176 ? -24.628 18.314  -49.157 1.00 15.34  ? 156 ILE B CG1   1 
ATOM   3854 C  CG2   . ILE B 1 176 ? -26.651 16.798  -48.768 1.00 18.23  ? 156 ILE B CG2   1 
ATOM   3855 C  CD1   . ILE B 1 176 ? -23.569 17.264  -49.406 1.00 18.40  ? 156 ILE B CD1   1 
ATOM   3856 N  N     . ILE B 1 177 ? -27.783 18.472  -45.761 1.00 16.10  ? 157 ILE B N     1 
ATOM   3857 C  CA    . ILE B 1 177 ? -28.978 18.081  -45.018 1.00 14.97  ? 157 ILE B CA    1 
ATOM   3858 C  C     . ILE B 1 177 ? -29.961 19.241  -44.935 1.00 15.65  ? 157 ILE B C     1 
ATOM   3859 O  O     . ILE B 1 177 ? -31.174 19.028  -45.015 1.00 17.19  ? 157 ILE B O     1 
ATOM   3860 C  CB    . ILE B 1 177 ? -28.605 17.543  -43.620 1.00 14.87  ? 157 ILE B CB    1 
ATOM   3861 C  CG1   . ILE B 1 177 ? -27.808 16.246  -43.760 1.00 15.91  ? 157 ILE B CG1   1 
ATOM   3862 C  CG2   . ILE B 1 177 ? -29.870 17.281  -42.809 1.00 16.02  ? 157 ILE B CG2   1 
ATOM   3863 C  CD1   . ILE B 1 177 ? -27.084 15.773  -42.453 1.00 19.16  ? 157 ILE B CD1   1 
ATOM   3864 N  N     . ASP B 1 178 ? -29.472 20.482  -44.779 1.00 16.47  ? 158 ASP B N     1 
ATOM   3865 C  CA    . ASP B 1 178 ? -30.379 21.637  -44.825 1.00 17.27  ? 158 ASP B CA    1 
ATOM   3866 C  C     . ASP B 1 178 ? -31.209 21.610  -46.107 1.00 16.24  ? 158 ASP B C     1 
ATOM   3867 O  O     . ASP B 1 178 ? -32.443 21.809  -46.092 1.00 17.28  ? 158 ASP B O     1 
ATOM   3868 C  CB    . ASP B 1 178 ? -29.587 22.958  -44.759 1.00 16.77  ? 158 ASP B CB    1 
ATOM   3869 C  CG    . ASP B 1 178 ? -29.110 23.319  -43.365 1.00 22.58  ? 158 ASP B CG    1 
ATOM   3870 O  OD1   . ASP B 1 178 ? -29.588 22.753  -42.363 1.00 21.48  ? 158 ASP B OD1   1 
ATOM   3871 O  OD2   . ASP B 1 178 ? -28.250 24.234  -43.275 1.00 23.29  ? 158 ASP B OD2   1 
ATOM   3872 N  N     . VAL B 1 179 ? -30.548 21.347  -47.237 1.00 15.71  ? 159 VAL B N     1 
ATOM   3873 C  CA    . VAL B 1 179 ? -31.313 21.285  -48.486 1.00 16.69  ? 159 VAL B CA    1 
ATOM   3874 C  C     . VAL B 1 179 ? -32.257 20.085  -48.484 1.00 17.55  ? 159 VAL B C     1 
ATOM   3875 O  O     . VAL B 1 179 ? -33.394 20.176  -48.962 1.00 18.08  ? 159 VAL B O     1 
ATOM   3876 C  CB    . VAL B 1 179 ? -30.380 21.265  -49.707 1.00 16.56  ? 159 VAL B CB    1 
ATOM   3877 C  CG1   . VAL B 1 179 ? -31.203 21.221  -51.013 1.00 17.49  ? 159 VAL B CG1   1 
ATOM   3878 C  CG2   . VAL B 1 179 ? -29.450 22.505  -49.701 1.00 19.44  ? 159 VAL B CG2   1 
ATOM   3879 N  N     . ALA B 1 180 ? -31.798 18.941  -47.966 1.00 17.01  ? 160 ALA B N     1 
ATOM   3880 C  CA    . ALA B 1 180 ? -32.661 17.760  -47.883 1.00 17.25  ? 160 ALA B CA    1 
ATOM   3881 C  C     . ALA B 1 180 ? -33.929 18.049  -47.088 1.00 17.79  ? 160 ALA B C     1 
ATOM   3882 O  O     . ALA B 1 180 ? -35.002 17.548  -47.428 1.00 17.12  ? 160 ALA B O     1 
ATOM   3883 C  CB    . ALA B 1 180 ? -31.893 16.584  -47.254 1.00 16.19  ? 160 ALA B CB    1 
ATOM   3884 N  N     . VAL B 1 181 ? -33.818 18.830  -46.010 1.00 17.97  ? 161 VAL B N     1 
ATOM   3885 C  CA    . VAL B 1 181 ? -34.991 19.179  -45.212 1.00 17.87  ? 161 VAL B CA    1 
ATOM   3886 C  C     . VAL B 1 181 ? -35.985 19.959  -46.063 1.00 16.44  ? 161 VAL B C     1 
ATOM   3887 O  O     . VAL B 1 181 ? -37.209 19.748  -45.976 1.00 18.47  ? 161 VAL B O     1 
ATOM   3888 C  CB    . VAL B 1 181 ? -34.579 19.967  -43.952 1.00 18.20  ? 161 VAL B CB    1 
ATOM   3889 C  CG1   . VAL B 1 181 ? -35.829 20.540  -43.249 1.00 19.81  ? 161 VAL B CG1   1 
ATOM   3890 C  CG2   . VAL B 1 181 ? -33.797 19.071  -42.992 1.00 18.99  ? 161 VAL B CG2   1 
ATOM   3891 N  N     . LEU B 1 182 ? -35.480 20.864  -46.913 1.00 18.39  ? 162 LEU B N     1 
ATOM   3892 C  CA    . LEU B 1 182 ? -36.390 21.599  -47.799 1.00 19.83  ? 162 LEU B CA    1 
ATOM   3893 C  C     . LEU B 1 182 ? -37.028 20.686  -48.852 1.00 17.38  ? 162 LEU B C     1 
ATOM   3894 O  O     . LEU B 1 182 ? -38.199 20.869  -49.227 1.00 19.16  ? 162 LEU B O     1 
ATOM   3895 C  CB    . LEU B 1 182 ? -35.656 22.755  -48.481 1.00 18.93  ? 162 LEU B CB    1 
ATOM   3896 C  CG    . LEU B 1 182 ? -35.158 23.814  -47.493 1.00 19.50  ? 162 LEU B CG    1 
ATOM   3897 C  CD1   . LEU B 1 182 ? -34.280 24.829  -48.199 1.00 25.45  ? 162 LEU B CD1   1 
ATOM   3898 C  CD2   . LEU B 1 182 ? -36.336 24.512  -46.800 1.00 23.25  ? 162 LEU B CD2   1 
ATOM   3899 N  N     . VAL B 1 183 ? -36.264 19.724  -49.373 1.00 17.92  ? 163 VAL B N     1 
ATOM   3900 C  CA    . VAL B 1 183 ? -36.830 18.770  -50.325 1.00 16.76  ? 163 VAL B CA    1 
ATOM   3901 C  C     . VAL B 1 183 ? -37.913 17.936  -49.644 1.00 19.19  ? 163 VAL B C     1 
ATOM   3902 O  O     . VAL B 1 183 ? -38.995 17.704  -50.208 1.00 18.38  ? 163 VAL B O     1 
ATOM   3903 C  CB    . VAL B 1 183 ? -35.715 17.893  -50.935 1.00 17.44  ? 163 VAL B CB    1 
ATOM   3904 C  CG1   . VAL B 1 183 ? -36.312 16.777  -51.784 1.00 18.88  ? 163 VAL B CG1   1 
ATOM   3905 C  CG2   . VAL B 1 183 ? -34.775 18.738  -51.788 1.00 17.96  ? 163 VAL B CG2   1 
ATOM   3906 N  N     . ALA B 1 184 ? -37.642 17.497  -48.411 1.00 18.96  ? 164 ALA B N     1 
ATOM   3907 C  CA    . ALA B 1 184 ? -38.628 16.770  -47.612 1.00 18.43  ? 164 ALA B CA    1 
ATOM   3908 C  C     . ALA B 1 184 ? -39.881 17.601  -47.398 1.00 21.09  ? 164 ALA B C     1 
ATOM   3909 O  O     . ALA B 1 184 ? -41.005 17.073  -47.432 1.00 20.16  ? 164 ALA B O     1 
ATOM   3910 C  CB    . ALA B 1 184 ? -38.013 16.389  -46.262 1.00 16.79  ? 164 ALA B CB    1 
ATOM   3911 N  N     . ARG B 1 185 ? -39.711 18.901  -47.151 1.00 17.40  ? 165 ARG B N     1 
ATOM   3912 C  CA    . ARG B 1 185 ? -40.878 19.775  -46.991 1.00 17.93  ? 165 ARG B CA    1 
ATOM   3913 C  C     . ARG B 1 185 ? -41.731 19.789  -48.257 1.00 21.20  ? 165 ARG B C     1 
ATOM   3914 O  O     . ARG B 1 185 ? -42.970 19.713  -48.189 1.00 20.24  ? 165 ARG B O     1 
ATOM   3915 C  CB    . ARG B 1 185 ? -40.413 21.186  -46.627 1.00 19.70  ? 165 ARG B CB    1 
ATOM   3916 C  CG    . ARG B 1 185 ? -41.535 22.215  -46.510 1.00 26.20  ? 165 ARG B CG    1 
ATOM   3917 C  CD    . ARG B 1 185 ? -40.954 23.591  -46.226 1.00 30.87  ? 165 ARG B CD    1 
ATOM   3918 N  NE    . ARG B 1 185 ? -40.229 23.627  -44.964 1.00 36.00  ? 165 ARG B NE    1 
ATOM   3919 C  CZ    . ARG B 1 185 ? -39.481 24.647  -44.560 1.00 45.98  ? 165 ARG B CZ    1 
ATOM   3920 N  NH1   . ARG B 1 185 ? -39.356 25.744  -45.290 1.00 39.58  ? 165 ARG B NH1   1 
ATOM   3921 N  NH2   . ARG B 1 185 ? -38.843 24.564  -43.396 1.00 43.93  ? 165 ARG B NH2   1 
ATOM   3922 N  N     . ALA B 1 186 ? -41.089 19.851  -49.427 1.00 18.21  ? 166 ALA B N     1 
ATOM   3923 C  CA    . ALA B 1 186 ? -41.855 19.782  -50.673 1.00 18.22  ? 166 ALA B CA    1 
ATOM   3924 C  C     . ALA B 1 186 ? -42.560 18.432  -50.828 1.00 20.05  ? 166 ALA B C     1 
ATOM   3925 O  O     . ALA B 1 186 ? -43.726 18.365  -51.262 1.00 20.47  ? 166 ALA B O     1 
ATOM   3926 C  CB    . ALA B 1 186 ? -40.932 20.055  -51.859 1.00 21.78  ? 166 ALA B CB    1 
ATOM   3927 N  N     . CYS B 1 187 ? -41.869 17.342  -50.480 1.00 20.19  ? 167 CYS B N     1 
ATOM   3928 C  CA    . CYS B 1 187 ? -42.512 16.030  -50.496 1.00 18.11  ? 167 CYS B CA    1 
ATOM   3929 C  C     . CYS B 1 187 ? -43.735 16.007  -49.587 1.00 21.45  ? 167 CYS B C     1 
ATOM   3930 O  O     . CYS B 1 187 ? -44.748 15.383  -49.922 1.00 22.54  ? 167 CYS B O     1 
ATOM   3931 C  CB    . CYS B 1 187 ? -41.532 14.934  -50.076 1.00 19.91  ? 167 CYS B CB    1 
ATOM   3932 S  SG    . CYS B 1 187 ? -40.133 14.673  -51.212 1.00 19.74  ? 167 CYS B SG    1 
ATOM   3933 N  N     . ASP B 1 188 ? -43.644 16.651  -48.419 1.00 18.54  ? 168 ASP B N     1 
ATOM   3934 C  CA    . ASP B 1 188 ? -44.798 16.737  -47.518 1.00 19.13  ? 168 ASP B CA    1 
ATOM   3935 C  C     . ASP B 1 188 ? -45.949 17.487  -48.164 1.00 21.42  ? 168 ASP B C     1 
ATOM   3936 O  O     . ASP B 1 188 ? -47.112 17.121  -47.970 1.00 21.33  ? 168 ASP B O     1 
ATOM   3937 C  CB    . ASP B 1 188 ? -44.434 17.440  -46.211 1.00 20.71  ? 168 ASP B CB    1 
ATOM   3938 C  CG    . ASP B 1 188 ? -43.662 16.557  -45.253 1.00 21.65  ? 168 ASP B CG    1 
ATOM   3939 O  OD1   . ASP B 1 188 ? -43.829 15.313  -45.310 1.00 22.16  ? 168 ASP B OD1   1 
ATOM   3940 O  OD2   . ASP B 1 188 ? -42.903 17.129  -44.435 1.00 21.16  ? 168 ASP B OD2   1 
ATOM   3941 N  N     . ARG B 1 189 ? -45.657 18.574  -48.887 1.00 20.20  ? 169 ARG B N     1 
ATOM   3942 C  CA    . ARG B 1 189 ? -46.753 19.297  -49.548 1.00 20.50  ? 169 ARG B CA    1 
ATOM   3943 C  C     . ARG B 1 189 ? -47.495 18.382  -50.522 1.00 23.35  ? 169 ARG B C     1 
ATOM   3944 O  O     . ARG B 1 189 ? -48.745 18.335  -50.550 1.00 23.41  ? 169 ARG B O     1 
ATOM   3945 C  CB    . ARG B 1 189 ? -46.215 20.520  -50.290 1.00 25.46  ? 169 ARG B CB    1 
ATOM   3946 C  CG    . ARG B 1 189 ? -45.732 21.664  -49.420 1.00 27.89  ? 169 ARG B CG    1 
ATOM   3947 C  CD    . ARG B 1 189 ? -45.059 22.739  -50.275 1.00 41.19  ? 169 ARG B CD    1 
ATOM   3948 N  NE    . ARG B 1 189 ? -45.823 23.082  -51.470 1.00 48.53  ? 169 ARG B NE    1 
ATOM   3949 C  CZ    . ARG B 1 189 ? -45.285 23.493  -52.612 1.00 48.36  ? 169 ARG B CZ    1 
ATOM   3950 N  NH1   . ARG B 1 189 ? -43.972 23.601  -52.762 1.00 36.49  ? 169 ARG B NH1   1 
ATOM   3951 N  NH2   . ARG B 1 189 ? -46.084 23.798  -53.632 1.00 46.88  ? 169 ARG B NH2   1 
ATOM   3952 N  N     . PHE B 1 190 ? -46.732 17.620  -51.307 1.00 21.11  ? 170 PHE B N     1 
ATOM   3953 C  CA    . PHE B 1 190 ? -47.335 16.655  -52.227 1.00 21.32  ? 170 PHE B CA    1 
ATOM   3954 C  C     . PHE B 1 190 ? -48.152 15.602  -51.478 1.00 22.96  ? 170 PHE B C     1 
ATOM   3955 O  O     . PHE B 1 190 ? -49.301 15.304  -51.839 1.00 22.45  ? 170 PHE B O     1 
ATOM   3956 C  CB    . PHE B 1 190 ? -46.239 15.990  -53.062 1.00 22.82  ? 170 PHE B CB    1 
ATOM   3957 C  CG    . PHE B 1 190 ? -46.724 14.836  -53.892 1.00 21.73  ? 170 PHE B CG    1 
ATOM   3958 C  CD1   . PHE B 1 190 ? -46.734 13.545  -53.382 1.00 23.13  ? 170 PHE B CD1   1 
ATOM   3959 C  CD2   . PHE B 1 190 ? -47.143 15.042  -55.189 1.00 24.36  ? 170 PHE B CD2   1 
ATOM   3960 C  CE1   . PHE B 1 190 ? -47.182 12.487  -54.149 1.00 27.84  ? 170 PHE B CE1   1 
ATOM   3961 C  CE2   . PHE B 1 190 ? -47.597 13.978  -55.968 1.00 29.36  ? 170 PHE B CE2   1 
ATOM   3962 C  CZ    . PHE B 1 190 ? -47.606 12.703  -55.444 1.00 26.46  ? 170 PHE B CZ    1 
ATOM   3963 N  N     . ALA B 1 191 ? -47.569 15.018  -50.434 1.00 20.53  ? 171 ALA B N     1 
ATOM   3964 C  CA    . ALA B 1 191 ? -48.236 13.934  -49.719 1.00 24.33  ? 171 ALA B CA    1 
ATOM   3965 C  C     . ALA B 1 191 ? -49.494 14.423  -49.009 1.00 22.90  ? 171 ALA B C     1 
ATOM   3966 O  O     . ALA B 1 191 ? -50.501 13.703  -48.950 1.00 24.31  ? 171 ALA B O     1 
ATOM   3967 C  CB    . ALA B 1 191 ? -47.268 13.300  -48.718 1.00 22.09  ? 171 ALA B CB    1 
ATOM   3968 N  N     . GLU B 1 192 ? -49.450 15.630  -48.446 1.00 21.51  ? 172 GLU B N     1 
ATOM   3969 C  CA    . GLU B 1 192 ? -50.626 16.195  -47.790 1.00 24.71  ? 172 GLU B CA    1 
ATOM   3970 C  C     . GLU B 1 192 ? -51.749 16.420  -48.786 1.00 24.59  ? 172 GLU B C     1 
ATOM   3971 O  O     . GLU B 1 192 ? -52.936 16.315  -48.426 1.00 25.23  ? 172 GLU B O     1 
ATOM   3972 C  CB    . GLU B 1 192 ? -50.251 17.509  -47.093 1.00 23.13  ? 172 GLU B CB    1 
ATOM   3973 C  CG    . GLU B 1 192 ? -49.360 17.334  -45.858 1.00 24.99  ? 172 GLU B CG    1 
ATOM   3974 C  CD    . GLU B 1 192 ? -48.596 18.598  -45.480 1.00 30.41  ? 172 GLU B CD    1 
ATOM   3975 O  OE1   . GLU B 1 192 ? -48.970 19.697  -45.936 1.00 31.85  ? 172 GLU B OE1   1 
ATOM   3976 O  OE2   . GLU B 1 192 ? -47.598 18.488  -44.738 1.00 25.26  ? 172 GLU B OE2   1 
ATOM   3977 N  N     . LYS B 1 193 ? -51.413 16.701  -50.048 1.00 23.83  ? 173 LYS B N     1 
ATOM   3978 C  CA    . LYS B 1 193 ? -52.483 16.837  -51.029 1.00 24.89  ? 173 LYS B CA    1 
ATOM   3979 C  C     . LYS B 1 193 ? -52.965 15.503  -51.597 1.00 25.03  ? 173 LYS B C     1 
ATOM   3980 O  O     . LYS B 1 193 ? -54.116 15.425  -52.053 1.00 30.14  ? 173 LYS B O     1 
ATOM   3981 C  CB    . LYS B 1 193 ? -52.034 17.742  -52.179 1.00 29.59  ? 173 LYS B CB    1 
ATOM   3982 C  CG    . LYS B 1 193 ? -51.939 19.210  -51.812 1.00 33.55  ? 173 LYS B CG    1 
ATOM   3983 C  CD    . LYS B 1 193 ? -51.501 20.039  -53.013 1.00 56.07  ? 173 LYS B CD    1 
ATOM   3984 C  CE    . LYS B 1 193 ? -51.549 21.530  -52.705 1.00 60.40  ? 173 LYS B CE    1 
ATOM   3985 N  NZ    . LYS B 1 193 ? -51.268 22.360  -53.912 1.00 69.03  ? 173 LYS B NZ    1 
ATOM   3986 N  N     . GLN B 1 194 ? -52.128 14.457  -51.583 1.00 26.27  ? 174 GLN B N     1 
ATOM   3987 C  CA    . GLN B 1 194 ? -52.420 13.237  -52.325 1.00 24.97  ? 174 GLN B CA    1 
ATOM   3988 C  C     . GLN B 1 194 ? -52.742 12.011  -51.477 1.00 26.23  ? 174 GLN B C     1 
ATOM   3989 O  O     . GLN B 1 194 ? -53.321 11.057  -52.013 1.00 26.62  ? 174 GLN B O     1 
ATOM   3990 C  CB    . GLN B 1 194 ? -51.239 12.888  -53.249 1.00 25.62  ? 174 GLN B CB    1 
ATOM   3991 C  CG    . GLN B 1 194 ? -50.942 13.971  -54.280 1.00 25.53  ? 174 GLN B CG    1 
ATOM   3992 C  CD    . GLN B 1 194 ? -51.940 13.939  -55.423 1.00 29.46  ? 174 GLN B CD    1 
ATOM   3993 O  OE1   . GLN B 1 194 ? -52.611 12.926  -55.648 1.00 36.61  ? 174 GLN B OE1   1 
ATOM   3994 N  NE2   . GLN B 1 194 ? -52.095 15.066  -56.103 1.00 31.27  ? 174 GLN B NE2   1 
ATOM   3995 N  N     . ILE B 1 195 ? -52.422 12.006  -50.184 1.00 25.32  ? 175 ILE B N     1 
ATOM   3996 C  CA    . ILE B 1 195 ? -52.519 10.800  -49.359 1.00 27.42  ? 175 ILE B CA    1 
ATOM   3997 C  C     . ILE B 1 195 ? -53.478 11.052  -48.202 1.00 22.71  ? 175 ILE B C     1 
ATOM   3998 O  O     . ILE B 1 195 ? -53.183 11.846  -47.299 1.00 27.10  ? 175 ILE B O     1 
ATOM   3999 C  CB    . ILE B 1 195 ? -51.143 10.364  -48.838 1.00 27.80  ? 175 ILE B CB    1 
ATOM   4000 C  CG1   . ILE B 1 195 ? -50.198 10.104  -50.012 1.00 22.95  ? 175 ILE B CG1   1 
ATOM   4001 C  CG2   . ILE B 1 195 ? -51.282 9.146   -47.927 1.00 26.38  ? 175 ILE B CG2   1 
ATOM   4002 C  CD1   . ILE B 1 195 ? -48.773 9.766   -49.569 1.00 27.41  ? 175 ILE B CD1   1 
ATOM   4003 N  N     . ALA B 1 196 ? -54.610 10.348  -48.195 1.00 29.27  ? 176 ALA B N     1 
ATOM   4004 C  CA    . ALA B 1 196 ? -55.557 10.507  -47.098 1.00 27.91  ? 176 ALA B CA    1 
ATOM   4005 C  C     . ALA B 1 196 ? -54.961 10.000  -45.786 1.00 26.85  ? 176 ALA B C     1 
ATOM   4006 O  O     . ALA B 1 196 ? -54.406 8.898   -45.723 1.00 36.48  ? 176 ALA B O     1 
ATOM   4007 C  CB    . ALA B 1 196 ? -56.859 9.770   -47.411 1.00 34.23  ? 176 ALA B CB    1 
ATOM   4008 N  N     . GLY B 1 197 ? -55.074 10.810  -44.738 1.00 28.15  ? 177 GLY B N     1 
ATOM   4009 C  CA    . GLY B 1 197 ? -54.577 10.442  -43.427 1.00 33.11  ? 177 GLY B CA    1 
ATOM   4010 C  C     . GLY B 1 197 ? -53.111 10.722  -43.188 1.00 29.81  ? 177 GLY B C     1 
ATOM   4011 O  O     . GLY B 1 197 ? -52.614 10.433  -42.095 1.00 30.71  ? 177 GLY B O     1 
ATOM   4012 N  N     . TYR B 1 198 ? -52.409 11.282  -44.166 1.00 28.59  ? 178 TYR B N     1 
ATOM   4013 C  CA    . TYR B 1 198 ? -50.988 11.555  -44.013 1.00 27.10  ? 178 TYR B CA    1 
ATOM   4014 C  C     . TYR B 1 198 ? -50.756 12.535  -42.862 1.00 28.35  ? 178 TYR B C     1 
ATOM   4015 O  O     . TYR B 1 198 ? -51.535 13.481  -42.681 1.00 29.48  ? 178 TYR B O     1 
ATOM   4016 C  CB    . TYR B 1 198 ? -50.444 12.118  -45.325 1.00 24.43  ? 178 TYR B CB    1 
ATOM   4017 C  CG    . TYR B 1 198 ? -48.945 12.291  -45.367 1.00 25.08  ? 178 TYR B CG    1 
ATOM   4018 C  CD1   . TYR B 1 198 ? -48.123 11.211  -45.635 1.00 26.33  ? 178 TYR B CD1   1 
ATOM   4019 C  CD2   . TYR B 1 198 ? -48.362 13.541  -45.185 1.00 20.58  ? 178 TYR B CD2   1 
ATOM   4020 C  CE1   . TYR B 1 198 ? -46.743 11.360  -45.693 1.00 23.04  ? 178 TYR B CE1   1 
ATOM   4021 C  CE2   . TYR B 1 198 ? -46.993 13.702  -45.239 1.00 22.91  ? 178 TYR B CE2   1 
ATOM   4022 C  CZ    . TYR B 1 198 ? -46.197 12.615  -45.500 1.00 25.36  ? 178 TYR B CZ    1 
ATOM   4023 O  OH    . TYR B 1 198 ? -44.839 12.792  -45.551 1.00 22.71  ? 178 TYR B OH    1 
ATOM   4024 N  N     . PRO B 1 199 ? -49.727 12.323  -42.036 1.00 26.95  ? 179 PRO B N     1 
ATOM   4025 C  CA    . PRO B 1 199 ? -49.431 13.272  -40.953 1.00 28.96  ? 179 PRO B CA    1 
ATOM   4026 C  C     . PRO B 1 199 ? -48.748 14.500  -41.533 1.00 28.45  ? 179 PRO B C     1 
ATOM   4027 O  O     . PRO B 1 199 ? -47.658 14.398  -42.097 1.00 25.82  ? 179 PRO B O     1 
ATOM   4028 C  CB    . PRO B 1 199 ? -48.478 12.489  -40.040 1.00 30.91  ? 179 PRO B CB    1 
ATOM   4029 C  CG    . PRO B 1 199 ? -48.351 11.126  -40.639 1.00 34.15  ? 179 PRO B CG    1 
ATOM   4030 C  CD    . PRO B 1 199 ? -48.752 11.224  -42.066 1.00 34.66  ? 179 PRO B CD    1 
ATOM   4031 N  N     . ALA B 1 200 ? -49.373 15.664  -41.374 1.00 29.94  ? 180 ALA B N     1 
ATOM   4032 C  CA    . ALA B 1 200 ? -48.818 16.886  -41.943 1.00 33.32  ? 180 ALA B CA    1 
ATOM   4033 C  C     . ALA B 1 200 ? -47.389 17.094  -41.463 1.00 27.72  ? 180 ALA B C     1 
ATOM   4034 O  O     . ALA B 1 200 ? -47.091 16.928  -40.278 1.00 26.32  ? 180 ALA B O     1 
ATOM   4035 C  CB    . ALA B 1 200 ? -49.687 18.088  -41.564 1.00 38.61  ? 180 ALA B CB    1 
ATOM   4036 N  N     . GLY B 1 201 ? -46.497 17.429  -42.398 1.00 23.91  ? 181 GLY B N     1 
ATOM   4037 C  CA    . GLY B 1 201 ? -45.133 17.770  -42.053 1.00 26.83  ? 181 GLY B CA    1 
ATOM   4038 C  C     . GLY B 1 201 ? -44.250 16.606  -41.673 1.00 22.41  ? 181 GLY B C     1 
ATOM   4039 O  O     . GLY B 1 201 ? -43.182 16.824  -41.100 1.00 21.65  ? 181 GLY B O     1 
ATOM   4040 N  N     . TYR B 1 202 ? -44.647 15.373  -42.006 1.00 23.46  ? 182 TYR B N     1 
ATOM   4041 C  CA    . TYR B 1 202 ? -43.969 14.194  -41.465 1.00 20.72  ? 182 TYR B CA    1 
ATOM   4042 C  C     . TYR B 1 202 ? -42.522 14.074  -41.940 1.00 20.87  ? 182 TYR B C     1 
ATOM   4043 O  O     . TYR B 1 202 ? -41.607 13.930  -41.121 1.00 21.38  ? 182 TYR B O     1 
ATOM   4044 C  CB    . TYR B 1 202 ? -44.756 12.932  -41.819 1.00 23.28  ? 182 TYR B CB    1 
ATOM   4045 C  CG    . TYR B 1 202 ? -44.227 11.720  -41.105 1.00 23.20  ? 182 TYR B CG    1 
ATOM   4046 C  CD1   . TYR B 1 202 ? -44.347 11.600  -39.726 1.00 27.69  ? 182 TYR B CD1   1 
ATOM   4047 C  CD2   . TYR B 1 202 ? -43.592 10.704  -41.797 1.00 23.15  ? 182 TYR B CD2   1 
ATOM   4048 C  CE1   . TYR B 1 202 ? -43.847 10.492  -39.056 1.00 29.38  ? 182 TYR B CE1   1 
ATOM   4049 C  CE2   . TYR B 1 202 ? -43.103 9.581   -41.135 1.00 22.31  ? 182 TYR B CE2   1 
ATOM   4050 C  CZ    . TYR B 1 202 ? -43.226 9.489   -39.763 1.00 26.56  ? 182 TYR B CZ    1 
ATOM   4051 O  OH    . TYR B 1 202 ? -42.734 8.390   -39.088 1.00 27.06  ? 182 TYR B OH    1 
ATOM   4052 N  N     . LEU B 1 203 ? -42.294 14.111  -43.258 1.00 19.17  ? 183 LEU B N     1 
ATOM   4053 C  CA    . LEU B 1 203 ? -40.946 13.868  -43.773 1.00 20.83  ? 183 LEU B CA    1 
ATOM   4054 C  C     . LEU B 1 203 ? -39.984 14.970  -43.357 1.00 19.82  ? 183 LEU B C     1 
ATOM   4055 O  O     . LEU B 1 203 ? -38.808 14.699  -43.064 1.00 18.94  ? 183 LEU B O     1 
ATOM   4056 C  CB    . LEU B 1 203 ? -40.976 13.745  -45.297 1.00 22.70  ? 183 LEU B CB    1 
ATOM   4057 C  CG    . LEU B 1 203 ? -41.513 12.420  -45.845 1.00 21.98  ? 183 LEU B CG    1 
ATOM   4058 C  CD1   . LEU B 1 203 ? -41.901 12.612  -47.284 1.00 23.12  ? 183 LEU B CD1   1 
ATOM   4059 C  CD2   . LEU B 1 203 ? -40.479 11.297  -45.708 1.00 22.97  ? 183 LEU B CD2   1 
ATOM   4060 N  N     . GLU B 1 204 ? -40.455 16.221  -43.329 1.00 20.93  ? 184 GLU B N     1 
ATOM   4061 C  CA    . GLU B 1 204 ? -39.587 17.312  -42.883 1.00 20.03  ? 184 GLU B CA    1 
ATOM   4062 C  C     . GLU B 1 204 ? -39.091 17.056  -41.461 1.00 20.91  ? 184 GLU B C     1 
ATOM   4063 O  O     . GLU B 1 204 ? -37.893 17.175  -41.172 1.00 20.25  ? 184 GLU B O     1 
ATOM   4064 C  CB    . GLU B 1 204 ? -40.336 18.650  -42.959 1.00 19.61  ? 184 GLU B CB    1 
ATOM   4065 C  CG    . GLU B 1 204 ? -39.477 19.842  -42.557 1.00 23.41  ? 184 GLU B CG    1 
ATOM   4066 C  CD    . GLU B 1 204 ? -40.244 21.154  -42.509 1.00 26.82  ? 184 GLU B CD    1 
ATOM   4067 O  OE1   . GLU B 1 204 ? -41.391 21.215  -42.993 1.00 30.29  ? 184 GLU B OE1   1 
ATOM   4068 O  OE2   . GLU B 1 204 ? -39.687 22.136  -41.976 1.00 32.53  ? 184 GLU B OE2   1 
ATOM   4069 N  N     . GLY B 1 205 ? -39.998 16.661  -40.566 1.00 22.42  ? 185 GLY B N     1 
ATOM   4070 C  CA    . GLY B 1 205 ? -39.592 16.413  -39.191 1.00 22.45  ? 185 GLY B CA    1 
ATOM   4071 C  C     . GLY B 1 205 ? -38.683 15.207  -39.070 1.00 23.66  ? 185 GLY B C     1 
ATOM   4072 O  O     . GLY B 1 205 ? -37.732 15.208  -38.279 1.00 23.80  ? 185 GLY B O     1 
ATOM   4073 N  N     . VAL B 1 206 ? -38.953 14.170  -39.862 1.00 23.76  ? 186 VAL B N     1 
ATOM   4074 C  CA    . VAL B 1 206 ? -38.138 12.958  -39.811 1.00 21.82  ? 186 VAL B CA    1 
ATOM   4075 C  C     . VAL B 1 206 ? -36.700 13.265  -40.214 1.00 23.27  ? 186 VAL B C     1 
ATOM   4076 O  O     . VAL B 1 206 ? -35.743 12.858  -39.536 1.00 21.82  ? 186 VAL B O     1 
ATOM   4077 C  CB    . VAL B 1 206 ? -38.759 11.872  -40.708 1.00 23.02  ? 186 VAL B CB    1 
ATOM   4078 C  CG1   . VAL B 1 206 ? -37.718 10.854  -41.110 1.00 25.71  ? 186 VAL B CG1   1 
ATOM   4079 C  CG2   . VAL B 1 206 ? -39.953 11.220  -40.000 1.00 24.57  ? 186 VAL B CG2   1 
ATOM   4080 N  N     . VAL B 1 207 ? -36.523 14.011  -41.306 1.00 19.61  ? 187 VAL B N     1 
ATOM   4081 C  CA    . VAL B 1 207 ? -35.172 14.295  -41.781 1.00 16.57  ? 187 VAL B CA    1 
ATOM   4082 C  C     . VAL B 1 207 ? -34.465 15.267  -40.844 1.00 19.64  ? 187 VAL B C     1 
ATOM   4083 O  O     . VAL B 1 207 ? -33.292 15.068  -40.489 1.00 20.48  ? 187 VAL B O     1 
ATOM   4084 C  CB    . VAL B 1 207 ? -35.205 14.827  -43.225 1.00 19.76  ? 187 VAL B CB    1 
ATOM   4085 C  CG1   . VAL B 1 207 ? -33.831 15.328  -43.628 1.00 20.20  ? 187 VAL B CG1   1 
ATOM   4086 C  CG2   . VAL B 1 207 ? -35.684 13.726  -44.183 1.00 24.03  ? 187 VAL B CG2   1 
ATOM   4087 N  N     . LYS B 1 208 ? -35.160 16.318  -40.406 1.00 17.06  ? 188 LYS B N     1 
ATOM   4088 C  CA    . LYS B 1 208 ? -34.477 17.337  -39.621 1.00 19.16  ? 188 LYS B CA    1 
ATOM   4089 C  C     . LYS B 1 208 ? -34.058 16.835  -38.241 1.00 20.06  ? 188 LYS B C     1 
ATOM   4090 O  O     . LYS B 1 208 ? -33.136 17.411  -37.656 1.00 19.65  ? 188 LYS B O     1 
ATOM   4091 C  CB    . LYS B 1 208 ? -35.346 18.591  -39.503 1.00 22.59  ? 188 LYS B CB    1 
ATOM   4092 C  CG    . LYS B 1 208 ? -36.349 18.551  -38.402 1.00 27.83  ? 188 LYS B CG    1 
ATOM   4093 C  CD    . LYS B 1 208 ? -37.463 19.535  -38.667 1.00 41.09  ? 188 LYS B CD    1 
ATOM   4094 C  CE    . LYS B 1 208 ? -36.936 20.921  -38.964 1.00 37.57  ? 188 LYS B CE    1 
ATOM   4095 N  NZ    . LYS B 1 208 ? -38.080 21.878  -39.080 1.00 54.87  ? 188 LYS B NZ    1 
ATOM   4096 N  N     . THR B 1 209 ? -34.712 15.800  -37.702 1.00 19.95  ? 189 THR B N     1 
ATOM   4097 C  CA    . THR B 1 209 ? -34.405 15.316  -36.357 1.00 19.34  ? 189 THR B CA    1 
ATOM   4098 C  C     . THR B 1 209 ? -33.656 13.988  -36.346 1.00 21.24  ? 189 THR B C     1 
ATOM   4099 O  O     . THR B 1 209 ? -33.435 13.427  -35.269 1.00 19.88  ? 189 THR B O     1 
ATOM   4100 C  CB    . THR B 1 209 ? -35.677 15.172  -35.516 1.00 21.63  ? 189 THR B CB    1 
ATOM   4101 O  OG1   . THR B 1 209 ? -36.531 14.168  -36.083 1.00 23.77  ? 189 THR B OG1   1 
ATOM   4102 C  CG2   . THR B 1 209 ? -36.430 16.484  -35.441 1.00 25.42  ? 189 THR B CG2   1 
ATOM   4103 N  N     . SER B 1 210 ? -33.248 13.475  -37.503 1.00 19.72  ? 190 SER B N     1 
ATOM   4104 C  CA    . SER B 1 210 ? -32.647 12.147  -37.541 1.00 17.34  ? 190 SER B CA    1 
ATOM   4105 C  C     . SER B 1 210 ? -31.244 12.144  -36.954 1.00 17.10  ? 190 SER B C     1 
ATOM   4106 O  O     . SER B 1 210 ? -30.420 13.013  -37.254 1.00 20.42  ? 190 SER B O     1 
ATOM   4107 C  CB    . SER B 1 210 ? -32.577 11.628  -38.978 1.00 21.06  ? 190 SER B CB    1 
ATOM   4108 O  OG    . SER B 1 210 ? -31.810 10.426  -39.017 1.00 18.59  ? 190 SER B OG    1 
ATOM   4109 N  N     . THR B 1 211 ? -30.971 11.134  -36.135 1.00 19.15  ? 191 THR B N     1 
ATOM   4110 C  CA    . THR B 1 211 ? -29.613 10.834  -35.710 1.00 19.33  ? 191 THR B CA    1 
ATOM   4111 C  C     . THR B 1 211 ? -29.056 9.611   -36.413 1.00 21.87  ? 191 THR B C     1 
ATOM   4112 O  O     . THR B 1 211 ? -27.933 9.193   -36.107 1.00 20.86  ? 191 THR B O     1 
ATOM   4113 C  CB    . THR B 1 211 ? -29.570 10.606  -34.193 1.00 22.48  ? 191 THR B CB    1 
ATOM   4114 O  OG1   . THR B 1 211 ? -30.458 9.534   -33.857 1.00 24.92  ? 191 THR B OG1   1 
ATOM   4115 C  CG2   . THR B 1 211 ? -30.001 11.867  -33.450 1.00 23.54  ? 191 THR B CG2   1 
ATOM   4116 N  N     . THR B 1 212 ? -29.798 9.034   -37.360 1.00 19.01  ? 192 THR B N     1 
ATOM   4117 C  CA    . THR B 1 212 ? -29.339 7.860   -38.092 1.00 19.24  ? 192 THR B CA    1 
ATOM   4118 C  C     . THR B 1 212 ? -28.845 8.182   -39.486 1.00 17.52  ? 192 THR B C     1 
ATOM   4119 O  O     . THR B 1 212 ? -28.177 7.331   -40.096 1.00 18.25  ? 192 THR B O     1 
ATOM   4120 C  CB    . THR B 1 212 ? -30.468 6.830   -38.238 1.00 17.79  ? 192 THR B CB    1 
ATOM   4121 O  OG1   . THR B 1 212 ? -31.477 7.363   -39.118 1.00 19.70  ? 192 THR B OG1   1 
ATOM   4122 C  CG2   . THR B 1 212 ? -31.083 6.483   -36.878 1.00 21.47  ? 192 THR B CG2   1 
ATOM   4123 N  N     . THR B 1 213 ? -29.162 9.373   -40.004 1.00 17.69  ? 193 THR B N     1 
ATOM   4124 C  CA    . THR B 1 213 ? -28.644 9.810   -41.298 1.00 17.46  ? 193 THR B CA    1 
ATOM   4125 C  C     . THR B 1 213 ? -27.152 9.532   -41.398 1.00 18.05  ? 193 THR B C     1 
ATOM   4126 O  O     . THR B 1 213 ? -26.388 9.837   -40.479 1.00 18.58  ? 193 THR B O     1 
ATOM   4127 C  CB    . THR B 1 213 ? -28.937 11.300  -41.493 1.00 15.47  ? 193 THR B CB    1 
ATOM   4128 O  OG1   . THR B 1 213 ? -30.351 11.455  -41.703 1.00 15.96  ? 193 THR B OG1   1 
ATOM   4129 C  CG2   . THR B 1 213 ? -28.140 11.880  -42.698 1.00 16.13  ? 193 THR B CG2   1 
ATOM   4130 N  N     . LYS B 1 214 ? -26.747 8.920   -42.506 1.00 15.83  ? 194 LYS B N     1 
ATOM   4131 C  CA    . LYS B 1 214 ? -25.402 8.369   -42.614 1.00 17.00  ? 194 LYS B CA    1 
ATOM   4132 C  C     . LYS B 1 214 ? -24.696 8.958   -43.824 1.00 19.05  ? 194 LYS B C     1 
ATOM   4133 O  O     . LYS B 1 214 ? -25.199 8.874   -44.944 1.00 17.62  ? 194 LYS B O     1 
ATOM   4134 C  CB    . LYS B 1 214 ? -25.466 6.841   -42.721 1.00 16.74  ? 194 LYS B CB    1 
ATOM   4135 C  CG    . LYS B 1 214 ? -24.105 6.203   -42.968 1.00 26.23  ? 194 LYS B CG    1 
ATOM   4136 C  CD    . LYS B 1 214 ? -23.522 5.669   -41.687 1.00 27.72  ? 194 LYS B CD    1 
ATOM   4137 C  CE    . LYS B 1 214 ? -24.299 4.486   -41.103 1.00 26.21  ? 194 LYS B CE    1 
ATOM   4138 N  NZ    . LYS B 1 214 ? -23.768 4.229   -39.715 1.00 24.45  ? 194 LYS B NZ    1 
ATOM   4139 N  N     . ALA B 1 215 ? -23.514 9.525   -43.614 1.00 16.02  ? 195 ALA B N     1 
ATOM   4140 C  CA    . ALA B 1 215 ? -22.725 10.055  -44.715 1.00 16.92  ? 195 ALA B CA    1 
ATOM   4141 C  C     . ALA B 1 215 ? -21.630 9.060   -45.072 1.00 16.90  ? 195 ALA B C     1 
ATOM   4142 O  O     . ALA B 1 215 ? -21.009 8.450   -44.190 1.00 18.49  ? 195 ALA B O     1 
ATOM   4143 C  CB    . ALA B 1 215 ? -22.114 11.412  -44.351 1.00 15.00  ? 195 ALA B CB    1 
ATOM   4144 N  N     . ARG B 1 216 ? -21.388 8.916   -46.373 1.00 15.60  ? 196 ARG B N     1 
ATOM   4145 C  CA    . ARG B 1 216 ? -20.416 7.971   -46.897 1.00 15.91  ? 196 ARG B CA    1 
ATOM   4146 C  C     . ARG B 1 216 ? -19.475 8.682   -47.855 1.00 17.83  ? 196 ARG B C     1 
ATOM   4147 O  O     . ARG B 1 216 ? -19.908 9.191   -48.899 1.00 17.54  ? 196 ARG B O     1 
ATOM   4148 C  CB    . ARG B 1 216 ? -21.130 6.820   -47.617 1.00 18.54  ? 196 ARG B CB    1 
ATOM   4149 C  CG    . ARG B 1 216 ? -20.174 5.777   -48.186 1.00 19.81  ? 196 ARG B CG    1 
ATOM   4150 C  CD    . ARG B 1 216 ? -20.921 4.823   -49.122 1.00 19.39  ? 196 ARG B CD    1 
ATOM   4151 N  NE    . ARG B 1 216 ? -21.252 5.449   -50.395 1.00 18.83  ? 196 ARG B NE    1 
ATOM   4152 C  CZ    . ARG B 1 216 ? -22.030 4.898   -51.323 1.00 19.64  ? 196 ARG B CZ    1 
ATOM   4153 N  NH1   . ARG B 1 216 ? -22.635 3.735   -51.122 1.00 21.10  ? 196 ARG B NH1   1 
ATOM   4154 N  NH2   . ARG B 1 216 ? -22.173 5.511   -52.496 1.00 20.65  ? 196 ARG B NH2   1 
ATOM   4155 N  N     . LEU B 1 217 ? -18.187 8.709   -47.509 1.00 16.03  ? 197 LEU B N     1 
ATOM   4156 C  CA    . LEU B 1 217 ? -17.146 9.277   -48.351 1.00 16.19  ? 197 LEU B CA    1 
ATOM   4157 C  C     . LEU B 1 217 ? -16.316 8.134   -48.924 1.00 16.69  ? 197 LEU B C     1 
ATOM   4158 O  O     . LEU B 1 217 ? -15.735 7.357   -48.161 1.00 19.04  ? 197 LEU B O     1 
ATOM   4159 C  CB    . LEU B 1 217 ? -16.284 10.232  -47.521 1.00 17.33  ? 197 LEU B CB    1 
ATOM   4160 C  CG    . LEU B 1 217 ? -15.244 11.097  -48.219 1.00 19.64  ? 197 LEU B CG    1 
ATOM   4161 C  CD1   . LEU B 1 217 ? -15.901 12.153  -49.135 1.00 19.77  ? 197 LEU B CD1   1 
ATOM   4162 C  CD2   . LEU B 1 217 ? -14.363 11.759  -47.134 1.00 19.37  ? 197 LEU B CD2   1 
ATOM   4163 N  N     . LEU B 1 218 ? -16.276 8.012   -50.252 1.00 16.87  ? 198 LEU B N     1 
ATOM   4164 C  CA    . LEU B 1 218 ? -15.602 6.888   -50.895 1.00 17.37  ? 198 LEU B CA    1 
ATOM   4165 C  C     . LEU B 1 218 ? -14.359 7.368   -51.620 1.00 18.60  ? 198 LEU B C     1 
ATOM   4166 O  O     . LEU B 1 218 ? -14.358 8.458   -52.201 1.00 19.88  ? 198 LEU B O     1 
ATOM   4167 C  CB    . LEU B 1 218 ? -16.505 6.172   -51.903 1.00 19.08  ? 198 LEU B CB    1 
ATOM   4168 C  CG    . LEU B 1 218 ? -17.717 5.460   -51.305 1.00 19.93  ? 198 LEU B CG    1 
ATOM   4169 C  CD1   . LEU B 1 218 ? -18.444 4.723   -52.412 1.00 19.61  ? 198 LEU B CD1   1 
ATOM   4170 C  CD2   . LEU B 1 218 ? -17.301 4.508   -50.196 1.00 21.38  ? 198 LEU B CD2   1 
ATOM   4171 N  N     . HIS B 1 219 ? -13.305 6.554   -51.555 1.00 18.66  ? 199 HIS B N     1 
ATOM   4172 C  CA    . HIS B 1 219 ? -12.061 6.777   -52.289 1.00 18.98  ? 199 HIS B CA    1 
ATOM   4173 C  C     . HIS B 1 219 ? -11.781 5.520   -53.102 1.00 22.68  ? 199 HIS B C     1 
ATOM   4174 O  O     . HIS B 1 219 ? -11.464 4.471   -52.533 1.00 22.71  ? 199 HIS B O     1 
ATOM   4175 C  CB    . HIS B 1 219 ? -10.901 7.079   -51.333 1.00 19.16  ? 199 HIS B CB    1 
ATOM   4176 C  CG    . HIS B 1 219 ? -9.578  7.180   -52.028 1.00 19.06  ? 199 HIS B CG    1 
ATOM   4177 N  ND1   . HIS B 1 219 ? -9.242  8.253   -52.825 1.00 20.47  ? 199 HIS B ND1   1 
ATOM   4178 C  CD2   . HIS B 1 219 ? -8.513  6.340   -52.057 1.00 20.93  ? 199 HIS B CD2   1 
ATOM   4179 C  CE1   . HIS B 1 219 ? -8.024  8.076   -53.311 1.00 19.67  ? 199 HIS B CE1   1 
ATOM   4180 N  NE2   . HIS B 1 219 ? -7.562  6.920   -52.866 1.00 21.86  ? 199 HIS B NE2   1 
ATOM   4181 N  N     . TYR B 1 220 ? -11.908 5.611   -54.424 1.00 21.28  ? 200 TYR B N     1 
ATOM   4182 C  CA    . TYR B 1 220 ? -11.503 4.543   -55.328 1.00 24.21  ? 200 TYR B CA    1 
ATOM   4183 C  C     . TYR B 1 220 ? -10.036 4.725   -55.681 1.00 26.09  ? 200 TYR B C     1 
ATOM   4184 O  O     . TYR B 1 220 ? -9.661  5.724   -56.326 1.00 24.37  ? 200 TYR B O     1 
ATOM   4185 C  CB    . TYR B 1 220 ? -12.376 4.533   -56.577 1.00 24.36  ? 200 TYR B CB    1 
ATOM   4186 C  CG    . TYR B 1 220 ? -13.777 4.081   -56.262 1.00 24.92  ? 200 TYR B CG    1 
ATOM   4187 C  CD1   . TYR B 1 220 ? -14.124 2.737   -56.301 1.00 29.02  ? 200 TYR B CD1   1 
ATOM   4188 C  CD2   . TYR B 1 220 ? -14.751 5.005   -55.893 1.00 23.01  ? 200 TYR B CD2   1 
ATOM   4189 C  CE1   . TYR B 1 220 ? -15.404 2.324   -55.997 1.00 29.18  ? 200 TYR B CE1   1 
ATOM   4190 C  CE2   . TYR B 1 220 ? -16.036 4.599   -55.589 1.00 27.82  ? 200 TYR B CE2   1 
ATOM   4191 C  CZ    . TYR B 1 220 ? -16.354 3.258   -55.645 1.00 27.97  ? 200 TYR B CZ    1 
ATOM   4192 O  OH    . TYR B 1 220 ? -17.635 2.851   -55.347 1.00 31.27  ? 200 TYR B OH    1 
ATOM   4193 N  N     . PHE B 1 221 ? -9.231  3.732   -55.288 1.00 23.32  ? 201 PHE B N     1 
ATOM   4194 C  CA    . PHE B 1 221 ? -7.794  3.774   -55.475 1.00 24.64  ? 201 PHE B CA    1 
ATOM   4195 C  C     . PHE B 1 221 ? -7.451  3.608   -56.953 1.00 30.32  ? 201 PHE B C     1 
ATOM   4196 O  O     . PHE B 1 221 ? -8.164  2.911   -57.683 1.00 32.63  ? 201 PHE B O     1 
ATOM   4197 C  CB    . PHE B 1 221 ? -7.124  2.669   -54.651 1.00 25.04  ? 201 PHE B CB    1 
ATOM   4198 C  CG    . PHE B 1 221 ? -7.112  2.923   -53.158 1.00 22.60  ? 201 PHE B CG    1 
ATOM   4199 C  CD1   . PHE B 1 221 ? -6.073  3.637   -52.573 1.00 21.86  ? 201 PHE B CD1   1 
ATOM   4200 C  CD2   . PHE B 1 221 ? -8.118  2.424   -52.335 1.00 22.27  ? 201 PHE B CD2   1 
ATOM   4201 C  CE1   . PHE B 1 221 ? -6.043  3.873   -51.204 1.00 22.08  ? 201 PHE B CE1   1 
ATOM   4202 C  CE2   . PHE B 1 221 ? -8.103  2.661   -50.963 1.00 23.22  ? 201 PHE B CE2   1 
ATOM   4203 C  CZ    . PHE B 1 221 ? -7.066  3.384   -50.391 1.00 26.83  ? 201 PHE B CZ    1 
ATOM   4204 N  N     . PRO B 1 222 ? -6.401  4.271   -57.432 1.00 27.96  ? 202 PRO B N     1 
ATOM   4205 C  CA    . PRO B 1 222 ? -5.978  4.070   -58.821 1.00 32.40  ? 202 PRO B CA    1 
ATOM   4206 C  C     . PRO B 1 222 ? -5.605  2.616   -59.065 1.00 38.77  ? 202 PRO B C     1 
ATOM   4207 O  O     . PRO B 1 222 ? -5.142  1.916   -58.160 1.00 39.51  ? 202 PRO B O     1 
ATOM   4208 C  CB    . PRO B 1 222 ? -4.756  4.986   -58.957 1.00 35.62  ? 202 PRO B CB    1 
ATOM   4209 C  CG    . PRO B 1 222 ? -4.927  6.013   -57.896 1.00 27.83  ? 202 PRO B CG    1 
ATOM   4210 C  CD    . PRO B 1 222 ? -5.617  5.316   -56.751 1.00 29.01  ? 202 PRO B CD    1 
ATOM   4211 N  N     . GLU B 1 223 ? -5.829  2.165   -60.299 1.00 46.14  ? 203 GLU B N     1 
ATOM   4212 C  CA    . GLU B 1 223 ? -5.460  0.811   -60.717 1.00 57.87  ? 203 GLU B CA    1 
ATOM   4213 C  C     . GLU B 1 223 ? -4.111  0.351   -60.167 1.00 67.84  ? 203 GLU B C     1 
ATOM   4214 O  O     . GLU B 1 223 ? -3.060  0.705   -60.703 1.00 64.23  ? 203 GLU B O     1 
ATOM   4215 C  CB    . GLU B 1 223 ? -5.411  0.711   -62.237 1.00 56.96  ? 203 GLU B CB    1 
ATOM   4216 C  CG    . GLU B 1 223 ? -5.085  -0.695  -62.713 1.00 72.33  ? 203 GLU B CG    1 
ATOM   4217 C  CD    . GLU B 1 223 ? -4.607  -0.727  -64.148 1.00 81.53  ? 203 GLU B CD    1 
ATOM   4218 O  OE1   . GLU B 1 223 ? -4.230  0.343   -64.669 1.00 78.37  ? 203 GLU B OE1   1 
ATOM   4219 O  OE2   . GLU B 1 223 ? -4.592  -1.822  -64.748 1.00 96.50  ? 203 GLU B OE2   1 
ATOM   4220 N  N     . CYS B 1 246 ? -24.773 -4.963  -65.544 1.00 64.75  ? 226 CYS B N     1 
ATOM   4221 C  CA    . CYS B 1 246 ? -24.430 -4.314  -64.280 1.00 72.65  ? 226 CYS B CA    1 
ATOM   4222 C  C     . CYS B 1 246 ? -25.650 -4.283  -63.347 1.00 57.70  ? 226 CYS B C     1 
ATOM   4223 O  O     . CYS B 1 246 ? -26.720 -3.814  -63.733 1.00 56.92  ? 226 CYS B O     1 
ATOM   4224 C  CB    . CYS B 1 246 ? -23.897 -2.902  -64.527 1.00 69.51  ? 226 CYS B CB    1 
ATOM   4225 S  SG    . CYS B 1 246 ? -23.057 -2.198  -63.088 1.00 100.38 ? 226 CYS B SG    1 
ATOM   4226 N  N     . ALA B 1 247 ? -25.492 -4.787  -62.123 1.00 45.81  ? 227 ALA B N     1 
ATOM   4227 C  CA    . ALA B 1 247 ? -26.628 -4.941  -61.225 1.00 42.26  ? 227 ALA B CA    1 
ATOM   4228 C  C     . ALA B 1 247 ? -27.014 -3.617  -60.572 1.00 29.93  ? 227 ALA B C     1 
ATOM   4229 O  O     . ALA B 1 247 ? -26.160 -2.834  -60.142 1.00 29.49  ? 227 ALA B O     1 
ATOM   4230 C  CB    . ALA B 1 247 ? -26.331 -5.982  -60.144 1.00 37.75  ? 227 ALA B CB    1 
ATOM   4231 N  N     . THR B 1 248 ? -28.314 -3.379  -60.503 1.00 27.60  ? 228 THR B N     1 
ATOM   4232 C  CA    . THR B 1 248 ? -28.850 -2.174  -59.898 1.00 24.32  ? 228 THR B CA    1 
ATOM   4233 C  C     . THR B 1 248 ? -29.079 -2.398  -58.408 1.00 25.61  ? 228 THR B C     1 
ATOM   4234 O  O     . THR B 1 248 ? -29.109 -3.535  -57.924 1.00 25.93  ? 228 THR B O     1 
ATOM   4235 C  CB    . THR B 1 248 ? -30.173 -1.790  -60.549 1.00 24.05  ? 228 THR B CB    1 
ATOM   4236 O  OG1   . THR B 1 248 ? -31.096 -2.883  -60.399 1.00 25.54  ? 228 THR B OG1   1 
ATOM   4237 C  CG2   . THR B 1 248 ? -29.977 -1.480  -62.026 1.00 27.04  ? 228 THR B CG2   1 
ATOM   4238 N  N     . HIS B 1 249 ? -29.241 -1.291  -57.684 1.00 21.75  ? 229 HIS B N     1 
ATOM   4239 C  CA    . HIS B 1 249 ? -29.674 -1.320  -56.292 1.00 22.47  ? 229 HIS B CA    1 
ATOM   4240 C  C     . HIS B 1 249 ? -30.677 -0.200  -56.069 1.00 21.53  ? 229 HIS B C     1 
ATOM   4241 O  O     . HIS B 1 249 ? -30.841 0.702   -56.900 1.00 19.03  ? 229 HIS B O     1 
ATOM   4242 C  CB    . HIS B 1 249 ? -28.504 -1.167  -55.309 1.00 21.58  ? 229 HIS B CB    1 
ATOM   4243 C  CG    . HIS B 1 249 ? -27.885 0.198   -55.311 1.00 21.65  ? 229 HIS B CG    1 
ATOM   4244 N  ND1   . HIS B 1 249 ? -26.890 0.556   -56.196 1.00 20.01  ? 229 HIS B ND1   1 
ATOM   4245 C  CD2   . HIS B 1 249 ? -28.100 1.284   -54.527 1.00 20.25  ? 229 HIS B CD2   1 
ATOM   4246 C  CE1   . HIS B 1 249 ? -26.526 1.804   -55.964 1.00 18.93  ? 229 HIS B CE1   1 
ATOM   4247 N  NE2   . HIS B 1 249 ? -27.247 2.271   -54.958 1.00 22.40  ? 229 HIS B NE2   1 
ATOM   4248 N  N     . LEU B 1 250 ? -31.352 -0.276  -54.922 1.00 20.30  ? 230 LEU B N     1 
ATOM   4249 C  CA    . LEU B 1 250 ? -32.206 0.786   -54.410 1.00 19.56  ? 230 LEU B CA    1 
ATOM   4250 C  C     . LEU B 1 250 ? -31.595 1.340   -53.130 1.00 23.65  ? 230 LEU B C     1 
ATOM   4251 O  O     . LEU B 1 250 ? -31.099 0.571   -52.293 1.00 22.10  ? 230 LEU B O     1 
ATOM   4252 C  CB    . LEU B 1 250 ? -33.604 0.242   -54.098 1.00 19.08  ? 230 LEU B CB    1 
ATOM   4253 C  CG    . LEU B 1 250 ? -34.374 -0.378  -55.266 1.00 21.70  ? 230 LEU B CG    1 
ATOM   4254 C  CD1   . LEU B 1 250 ? -35.649 -1.031  -54.733 1.00 26.19  ? 230 LEU B CD1   1 
ATOM   4255 C  CD2   . LEU B 1 250 ? -34.712 0.660   -56.322 1.00 23.08  ? 230 LEU B CD2   1 
ATOM   4256 N  N     . ASP B 1 251 ? -31.621 2.665   -52.970 1.00 18.46  ? 231 ASP B N     1 
ATOM   4257 C  CA    . ASP B 1 251 ? -31.225 3.235   -51.682 1.00 17.29  ? 231 ASP B CA    1 
ATOM   4258 C  C     . ASP B 1 251 ? -32.313 2.933   -50.661 1.00 19.01  ? 231 ASP B C     1 
ATOM   4259 O  O     . ASP B 1 251 ? -33.499 2.926   -50.984 1.00 18.10  ? 231 ASP B O     1 
ATOM   4260 C  CB    . ASP B 1 251 ? -31.019 4.749   -51.764 1.00 16.93  ? 231 ASP B CB    1 
ATOM   4261 C  CG    . ASP B 1 251 ? -29.775 5.142   -52.526 1.00 18.43  ? 231 ASP B CG    1 
ATOM   4262 O  OD1   . ASP B 1 251 ? -29.143 4.270   -53.164 1.00 17.74  ? 231 ASP B OD1   1 
ATOM   4263 O  OD2   . ASP B 1 251 ? -29.450 6.346   -52.488 1.00 20.08  ? 231 ASP B OD2   1 
ATOM   4264 N  N     . HIS B 1 252 ? -31.918 2.701   -49.413 1.00 18.01  ? 232 HIS B N     1 
ATOM   4265 C  CA    A HIS B 1 252 ? -32.825 2.215   -48.381 0.60 19.87  ? 232 HIS B CA    1 
ATOM   4266 C  CA    B HIS B 1 252 ? -32.937 2.232   -48.485 0.40 19.63  ? 232 HIS B CA    1 
ATOM   4267 C  C     . HIS B 1 252 ? -33.514 3.327   -47.594 1.00 24.12  ? 232 HIS B C     1 
ATOM   4268 O  O     . HIS B 1 252 ? -34.583 3.104   -47.012 1.00 18.84  ? 232 HIS B O     1 
ATOM   4269 C  CB    A HIS B 1 252 ? -32.030 1.320   -47.425 0.60 21.49  ? 232 HIS B CB    1 
ATOM   4270 C  CB    B HIS B 1 252 ? -32.416 1.037   -47.649 0.40 23.75  ? 232 HIS B CB    1 
ATOM   4271 C  CG    A HIS B 1 252 ? -32.867 0.637   -46.398 0.60 21.86  ? 232 HIS B CG    1 
ATOM   4272 C  CG    B HIS B 1 252 ? -31.625 1.395   -46.427 0.40 23.96  ? 232 HIS B CG    1 
ATOM   4273 N  ND1   A HIS B 1 252 ? -32.849 0.996   -45.068 0.60 23.50  ? 232 HIS B ND1   1 
ATOM   4274 N  ND1   B HIS B 1 252 ? -30.274 1.138   -46.319 0.40 23.86  ? 232 HIS B ND1   1 
ATOM   4275 C  CD2   A HIS B 1 252 ? -33.742 -0.390  -46.502 0.60 28.19  ? 232 HIS B CD2   1 
ATOM   4276 C  CD2   B HIS B 1 252 ? -32.007 1.898   -45.228 0.40 22.65  ? 232 HIS B CD2   1 
ATOM   4277 C  CE1   A HIS B 1 252 ? -33.682 0.222   -44.397 0.60 21.58  ? 232 HIS B CE1   1 
ATOM   4278 C  CE1   B HIS B 1 252 ? -29.851 1.510   -45.124 0.40 24.02  ? 232 HIS B CE1   1 
ATOM   4279 N  NE2   A HIS B 1 252 ? -34.236 -0.628  -45.243 0.60 23.77  ? 232 HIS B NE2   1 
ATOM   4280 N  NE2   B HIS B 1 252 ? -30.881 1.980   -44.444 0.40 24.13  ? 232 HIS B NE2   1 
ATOM   4281 N  N     . GLY B 1 253 ? -32.920 4.511   -47.542 1.00 18.11  ? 233 GLY B N     1 
ATOM   4282 C  CA    . GLY B 1 253 ? -33.387 5.593   -46.683 1.00 16.84  ? 233 GLY B CA    1 
ATOM   4283 C  C     . GLY B 1 253 ? -34.472 6.453   -47.311 1.00 16.83  ? 233 GLY B C     1 
ATOM   4284 O  O     . GLY B 1 253 ? -35.285 5.982   -48.115 1.00 17.05  ? 233 GLY B O     1 
ATOM   4285 N  N     . CYS B 1 254 ? -34.469 7.743   -46.946 1.00 16.61  ? 234 CYS B N     1 
ATOM   4286 C  CA    . CYS B 1 254 ? -35.477 8.683   -47.440 1.00 17.85  ? 234 CYS B CA    1 
ATOM   4287 C  C     . CYS B 1 254 ? -34.970 9.458   -48.640 1.00 16.46  ? 234 CYS B C     1 
ATOM   4288 O  O     . CYS B 1 254 ? -35.492 9.304   -49.756 1.00 17.18  ? 234 CYS B O     1 
ATOM   4289 C  CB    . CYS B 1 254 ? -35.893 9.679   -46.357 1.00 16.61  ? 234 CYS B CB    1 
ATOM   4290 S  SG    . CYS B 1 254 ? -36.878 8.925   -45.054 1.00 21.28  ? 234 CYS B SG    1 
ATOM   4291 N  N     . LEU B 1 255 ? -33.946 10.287  -48.419 1.00 16.19  ? 235 LEU B N     1 
ATOM   4292 C  CA    . LEU B 1 255 ? -33.420 11.138  -49.484 1.00 16.06  ? 235 LEU B CA    1 
ATOM   4293 C  C     . LEU B 1 255 ? -31.904 11.085  -49.413 1.00 15.86  ? 235 LEU B C     1 
ATOM   4294 O  O     . LEU B 1 255 ? -31.318 11.384  -48.370 1.00 18.17  ? 235 LEU B O     1 
ATOM   4295 C  CB    . LEU B 1 255 ? -33.907 12.588  -49.355 1.00 16.02  ? 235 LEU B CB    1 
ATOM   4296 C  CG    . LEU B 1 255 ? -35.397 12.839  -49.610 1.00 16.55  ? 235 LEU B CG    1 
ATOM   4297 C  CD1   . LEU B 1 255 ? -35.772 14.189  -49.005 1.00 19.64  ? 235 LEU B CD1   1 
ATOM   4298 C  CD2   . LEU B 1 255 ? -35.690 12.826  -51.106 1.00 19.16  ? 235 LEU B CD2   1 
ATOM   4299 N  N     . THR B 1 256 ? -31.276 10.712  -50.512 1.00 15.90  ? 236 THR B N     1 
ATOM   4300 C  CA    . THR B 1 256 ? -29.823 10.616  -50.574 1.00 16.38  ? 236 THR B CA    1 
ATOM   4301 C  C     . THR B 1 256 ? -29.271 11.845  -51.277 1.00 18.56  ? 236 THR B C     1 
ATOM   4302 O  O     . THR B 1 256 ? -29.495 12.026  -52.480 1.00 16.94  ? 236 THR B O     1 
ATOM   4303 C  CB    . THR B 1 256 ? -29.395 9.360   -51.313 1.00 15.99  ? 236 THR B CB    1 
ATOM   4304 O  OG1   . THR B 1 256 ? -29.978 8.214   -50.673 1.00 16.13  ? 236 THR B OG1   1 
ATOM   4305 C  CG2   . THR B 1 256 ? -27.852 9.267   -51.297 1.00 16.13  ? 236 THR B CG2   1 
ATOM   4306 N  N     . GLY B 1 257 ? -28.533 12.670  -50.529 1.00 15.51  ? 237 GLY B N     1 
ATOM   4307 C  CA    . GLY B 1 257 ? -27.844 13.811  -51.123 1.00 15.47  ? 237 GLY B CA    1 
ATOM   4308 C  C     . GLY B 1 257 ? -26.550 13.375  -51.794 1.00 18.16  ? 237 GLY B C     1 
ATOM   4309 O  O     . GLY B 1 257 ? -25.821 12.521  -51.295 1.00 17.86  ? 237 GLY B O     1 
ATOM   4310 N  N     . LEU B 1 258 ? -26.284 13.961  -52.960 1.00 16.09  ? 238 LEU B N     1 
ATOM   4311 C  CA    . LEU B 1 258 ? -25.183 13.546  -53.825 1.00 16.98  ? 238 LEU B CA    1 
ATOM   4312 C  C     . LEU B 1 258 ? -24.466 14.767  -54.370 1.00 17.00  ? 238 LEU B C     1 
ATOM   4313 O  O     . LEU B 1 258 ? -25.103 15.760  -54.724 1.00 17.64  ? 238 LEU B O     1 
ATOM   4314 C  CB    . LEU B 1 258 ? -25.685 12.743  -55.031 1.00 17.97  ? 238 LEU B CB    1 
ATOM   4315 C  CG    . LEU B 1 258 ? -26.570 11.535  -54.714 1.00 18.14  ? 238 LEU B CG    1 
ATOM   4316 C  CD1   . LEU B 1 258 ? -27.285 11.098  -55.997 1.00 25.15  ? 238 LEU B CD1   1 
ATOM   4317 C  CD2   . LEU B 1 258 ? -25.726 10.400  -54.167 1.00 19.48  ? 238 LEU B CD2   1 
ATOM   4318 N  N     . THR B 1 259 ? -23.140 14.680  -54.450 1.00 18.04  ? 239 THR B N     1 
ATOM   4319 C  CA    . THR B 1 259 ? -22.345 15.565  -55.294 1.00 17.52  ? 239 THR B CA    1 
ATOM   4320 C  C     . THR B 1 259 ? -21.882 14.820  -56.542 1.00 17.84  ? 239 THR B C     1 
ATOM   4321 O  O     . THR B 1 259 ? -21.843 13.582  -56.576 1.00 19.12  ? 239 THR B O     1 
ATOM   4322 C  CB    . THR B 1 259 ? -21.115 16.112  -54.548 1.00 20.00  ? 239 THR B CB    1 
ATOM   4323 O  OG1   . THR B 1 259 ? -20.160 15.061  -54.343 1.00 22.83  ? 239 THR B OG1   1 
ATOM   4324 C  CG2   . THR B 1 259 ? -21.517 16.684  -53.186 1.00 21.72  ? 239 THR B CG2   1 
ATOM   4325 N  N     . SER B 1 260 ? -21.456 15.580  -57.551 1.00 16.85  ? 240 SER B N     1 
ATOM   4326 C  CA    . SER B 1 260 ? -20.727 14.948  -58.641 1.00 19.01  ? 240 SER B CA    1 
ATOM   4327 C  C     . SER B 1 260 ? -19.392 14.426  -58.117 1.00 18.09  ? 240 SER B C     1 
ATOM   4328 O  O     . SER B 1 260 ? -18.827 14.951  -57.150 1.00 18.85  ? 240 SER B O     1 
ATOM   4329 C  CB    . SER B 1 260 ? -20.481 15.928  -59.793 1.00 21.98  ? 240 SER B CB    1 
ATOM   4330 O  OG    . SER B 1 260 ? -19.535 16.925  -59.417 1.00 20.23  ? 240 SER B OG    1 
ATOM   4331 N  N     . ALA B 1 261 ? -18.890 13.384  -58.769 1.00 17.62  ? 241 ALA B N     1 
ATOM   4332 C  CA    . ALA B 1 261 ? -17.647 12.759  -58.332 1.00 19.14  ? 241 ALA B CA    1 
ATOM   4333 C  C     . ALA B 1 261 ? -16.451 13.643  -58.661 1.00 19.74  ? 241 ALA B C     1 
ATOM   4334 O  O     . ALA B 1 261 ? -16.493 14.489  -59.564 1.00 20.64  ? 241 ALA B O     1 
ATOM   4335 C  CB    . ALA B 1 261 ? -17.468 11.392  -58.993 1.00 21.19  ? 241 ALA B CB    1 
ATOM   4336 N  N     . MET B 1 262 ? -15.370 13.455  -57.893 1.00 18.05  ? 242 MET B N     1 
ATOM   4337 C  CA    . MET B 1 262 ? -14.096 14.129  -58.147 1.00 18.37  ? 242 MET B CA    1 
ATOM   4338 C  C     . MET B 1 262 ? -13.074 13.135  -58.683 1.00 19.19  ? 242 MET B C     1 
ATOM   4339 O  O     . MET B 1 262 ? -12.811 12.110  -58.055 1.00 19.86  ? 242 MET B O     1 
ATOM   4340 C  CB    . MET B 1 262 ? -13.561 14.793  -56.876 1.00 18.50  ? 242 MET B CB    1 
ATOM   4341 C  CG    . MET B 1 262 ? -12.179 15.413  -57.065 1.00 21.03  ? 242 MET B CG    1 
ATOM   4342 S  SD    . MET B 1 262 ? -11.446 15.826  -55.464 1.00 22.30  ? 242 MET B SD    1 
ATOM   4343 C  CE    . MET B 1 262 ? -10.070 16.866  -55.973 1.00 21.54  ? 242 MET B CE    1 
ATOM   4344 N  N     . PHE B 1 263 ? -12.509 13.427  -59.847 1.00 19.43  ? 243 PHE B N     1 
ATOM   4345 C  CA    . PHE B 1 263 ? -11.374 12.665  -60.351 1.00 20.03  ? 243 PHE B CA    1 
ATOM   4346 C  C     . PHE B 1 263 ? -10.093 13.427  -60.052 1.00 23.76  ? 243 PHE B C     1 
ATOM   4347 O  O     . PHE B 1 263 ? -10.035 14.649  -60.217 1.00 22.24  ? 243 PHE B O     1 
ATOM   4348 C  CB    . PHE B 1 263 ? -11.530 12.399  -61.852 1.00 20.58  ? 243 PHE B CB    1 
ATOM   4349 C  CG    . PHE B 1 263 ? -12.657 11.459  -62.164 1.00 25.13  ? 243 PHE B CG    1 
ATOM   4350 C  CD1   . PHE B 1 263 ? -12.449 10.087  -62.170 1.00 23.96  ? 243 PHE B CD1   1 
ATOM   4351 C  CD2   . PHE B 1 263 ? -13.928 11.946  -62.430 1.00 26.00  ? 243 PHE B CD2   1 
ATOM   4352 C  CE1   . PHE B 1 263 ? -13.494 9.215   -62.443 1.00 27.55  ? 243 PHE B CE1   1 
ATOM   4353 C  CE2   . PHE B 1 263 ? -14.984 11.081  -62.700 1.00 27.38  ? 243 PHE B CE2   1 
ATOM   4354 C  CZ    . PHE B 1 263 ? -14.760 9.710   -62.718 1.00 25.98  ? 243 PHE B CZ    1 
ATOM   4355 N  N     . VAL B 1 264 ? -9.076  12.704  -59.581 1.00 20.51  ? 244 VAL B N     1 
ATOM   4356 C  CA    . VAL B 1 264 ? -7.813  13.309  -59.156 1.00 21.97  ? 244 VAL B CA    1 
ATOM   4357 C  C     . VAL B 1 264 ? -6.667  12.525  -59.779 1.00 22.71  ? 244 VAL B C     1 
ATOM   4358 O  O     . VAL B 1 264 ? -6.645  11.297  -59.690 1.00 23.56  ? 244 VAL B O     1 
ATOM   4359 C  CB    . VAL B 1 264 ? -7.661  13.319  -57.617 1.00 23.23  ? 244 VAL B CB    1 
ATOM   4360 C  CG1   . VAL B 1 264 ? -6.397  14.120  -57.197 1.00 20.64  ? 244 VAL B CG1   1 
ATOM   4361 C  CG2   . VAL B 1 264 ? -8.872  13.851  -56.952 1.00 30.32  ? 244 VAL B CG2   1 
ATOM   4362 N  N     . ASP B 1 265 ? -5.711  13.226  -60.397 1.00 22.05  ? 245 ASP B N     1 
ATOM   4363 C  CA    . ASP B 1 265 ? -4.460  12.611  -60.851 1.00 22.86  ? 245 ASP B CA    1 
ATOM   4364 C  C     . ASP B 1 265 ? -3.488  12.681  -59.680 1.00 26.89  ? 245 ASP B C     1 
ATOM   4365 O  O     . ASP B 1 265 ? -2.887  13.724  -59.419 1.00 23.07  ? 245 ASP B O     1 
ATOM   4366 C  CB    . ASP B 1 265 ? -3.919  13.324  -62.085 1.00 24.72  ? 245 ASP B CB    1 
ATOM   4367 C  CG    . ASP B 1 265 ? -2.622  12.707  -62.607 1.00 31.02  ? 245 ASP B CG    1 
ATOM   4368 O  OD1   . ASP B 1 265 ? -2.042  11.853  -61.908 1.00 26.24  ? 245 ASP B OD1   1 
ATOM   4369 O  OD2   . ASP B 1 265 ? -2.176  13.086  -63.712 1.00 34.73  ? 245 ASP B OD2   1 
ATOM   4370 N  N     . GLU B 1 266 ? -3.343  11.566  -58.962 1.00 24.23  ? 246 GLU B N     1 
ATOM   4371 C  CA    . GLU B 1 266 ? -2.569  11.566  -57.731 1.00 22.60  ? 246 GLU B CA    1 
ATOM   4372 C  C     . GLU B 1 266 ? -1.069  11.503  -57.974 1.00 25.85  ? 246 GLU B C     1 
ATOM   4373 O  O     . GLU B 1 266 ? -0.305  11.701  -57.023 1.00 27.83  ? 246 GLU B O     1 
ATOM   4374 C  CB    . GLU B 1 266 ? -3.026  10.416  -56.820 1.00 22.38  ? 246 GLU B CB    1 
ATOM   4375 C  CG    . GLU B 1 266 ? -4.422  10.667  -56.248 1.00 23.02  ? 246 GLU B CG    1 
ATOM   4376 C  CD    . GLU B 1 266 ? -4.912  9.595   -55.280 1.00 21.30  ? 246 GLU B CD    1 
ATOM   4377 O  OE1   . GLU B 1 266 ? -4.370  8.463   -55.294 1.00 24.93  ? 246 GLU B OE1   1 
ATOM   4378 O  OE2   . GLU B 1 266 ? -5.854  9.901   -54.520 1.00 20.66  ? 246 GLU B OE2   1 
ATOM   4379 N  N     . ALA B 1 267 ? -0.631  11.262  -59.211 1.00 28.33  ? 247 ALA B N     1 
ATOM   4380 C  CA    . ALA B 1 267 ? 0.777   11.484  -59.533 1.00 30.09  ? 247 ALA B CA    1 
ATOM   4381 C  C     . ALA B 1 267 ? 1.065   12.972  -59.689 1.00 32.46  ? 247 ALA B C     1 
ATOM   4382 O  O     . ALA B 1 267 ? 2.077   13.474  -59.179 1.00 33.58  ? 247 ALA B O     1 
ATOM   4383 C  CB    . ALA B 1 267 ? 1.155   10.726  -60.808 1.00 31.99  ? 247 ALA B CB    1 
ATOM   4384 N  N     . ALA B 1 268 ? 0.172   13.693  -60.372 1.00 26.34  ? 248 ALA B N     1 
ATOM   4385 C  CA    . ALA B 1 268 ? 0.345   15.130  -60.564 1.00 29.14  ? 248 ALA B CA    1 
ATOM   4386 C  C     . ALA B 1 268 ? 0.151   15.900  -59.264 1.00 27.84  ? 248 ALA B C     1 
ATOM   4387 O  O     . ALA B 1 268 ? 0.864   16.873  -59.007 1.00 29.77  ? 248 ALA B O     1 
ATOM   4388 C  CB    . ALA B 1 268 ? -0.634  15.641  -61.623 1.00 32.80  ? 248 ALA B CB    1 
ATOM   4389 N  N     . THR B 1 269 ? -0.842  15.514  -58.455 1.00 25.27  ? 249 THR B N     1 
ATOM   4390 C  CA    . THR B 1 269 ? -1.131  16.178  -57.184 1.00 26.36  ? 249 THR B CA    1 
ATOM   4391 C  C     . THR B 1 269 ? -1.147  15.123  -56.085 1.00 28.32  ? 249 THR B C     1 
ATOM   4392 O  O     . THR B 1 269 ? -2.194  14.541  -55.787 1.00 23.97  ? 249 THR B O     1 
ATOM   4393 C  CB    . THR B 1 269 ? -2.454  16.945  -57.236 1.00 27.86  ? 249 THR B CB    1 
ATOM   4394 O  OG1   . THR B 1 269 ? -3.530  16.034  -57.483 1.00 26.77  ? 249 THR B OG1   1 
ATOM   4395 C  CG2   . THR B 1 269 ? -2.435  17.985  -58.351 1.00 32.36  ? 249 THR B CG2   1 
ATOM   4396 N  N     . PRO B 1 270 ? -0.001  14.845  -55.468 1.00 24.67  ? 250 PRO B N     1 
ATOM   4397 C  CA    . PRO B 1 270 ? 0.088   13.724  -54.512 1.00 23.83  ? 250 PRO B CA    1 
ATOM   4398 C  C     . PRO B 1 270 ? -0.832  13.917  -53.320 1.00 23.67  ? 250 PRO B C     1 
ATOM   4399 O  O     . PRO B 1 270 ? -0.947  15.022  -52.764 1.00 22.87  ? 250 PRO B O     1 
ATOM   4400 C  CB    . PRO B 1 270 ? 1.567   13.738  -54.090 1.00 25.58  ? 250 PRO B CB    1 
ATOM   4401 C  CG    . PRO B 1 270 ? 2.273   14.431  -55.226 1.00 31.98  ? 250 PRO B CG    1 
ATOM   4402 C  CD    . PRO B 1 270 ? 1.310   15.462  -55.734 1.00 29.03  ? 250 PRO B CD    1 
ATOM   4403 N  N     . PRO B 1 271 ? -1.527  12.849  -52.892 1.00 24.66  ? 251 PRO B N     1 
ATOM   4404 C  CA    . PRO B 1 271 ? -2.466  12.945  -51.760 1.00 25.29  ? 251 PRO B CA    1 
ATOM   4405 C  C     . PRO B 1 271 ? -1.751  12.882  -50.413 1.00 26.72  ? 251 PRO B C     1 
ATOM   4406 O  O     . PRO B 1 271 ? -1.948  11.968  -49.609 1.00 26.43  ? 251 PRO B O     1 
ATOM   4407 C  CB    . PRO B 1 271 ? -3.385  11.740  -51.999 1.00 25.24  ? 251 PRO B CB    1 
ATOM   4408 C  CG    . PRO B 1 271 ? -2.505  10.728  -52.631 1.00 24.66  ? 251 PRO B CG    1 
ATOM   4409 C  CD    . PRO B 1 271 ? -1.529  11.504  -53.498 1.00 23.69  ? 251 PRO B CD    1 
ATOM   4410 N  N     . VAL B 1 272 ? -0.917  13.884  -50.154 1.00 23.67  ? 252 VAL B N     1 
ATOM   4411 C  CA    . VAL B 1 272 ? 0.019   13.886  -49.037 1.00 23.05  ? 252 VAL B CA    1 
ATOM   4412 C  C     . VAL B 1 272 ? -0.295  15.061  -48.127 1.00 24.43  ? 252 VAL B C     1 
ATOM   4413 O  O     . VAL B 1 272 ? -0.446  16.194  -48.600 1.00 34.48  ? 252 VAL B O     1 
ATOM   4414 C  CB    . VAL B 1 272 ? 1.467   13.969  -49.550 1.00 26.44  ? 252 VAL B CB    1 
ATOM   4415 C  CG1   . VAL B 1 272 ? 2.397   14.256  -48.417 1.00 29.57  ? 252 VAL B CG1   1 
ATOM   4416 C  CG2   . VAL B 1 272 ? 1.849   12.680  -50.259 1.00 28.90  ? 252 VAL B CG2   1 
ATOM   4417 N  N     . VAL B 1 273 ? -0.375  14.800  -46.821 1.00 22.55  ? 253 VAL B N     1 
ATOM   4418 C  CA    . VAL B 1 273 ? -0.673  15.847  -45.847 1.00 25.35  ? 253 VAL B CA    1 
ATOM   4419 C  C     . VAL B 1 273 ? 0.598   16.673  -45.673 1.00 35.16  ? 253 VAL B C     1 
ATOM   4420 O  O     . VAL B 1 273 ? 1.501   16.310  -44.917 1.00 32.70  ? 253 VAL B O     1 
ATOM   4421 C  CB    . VAL B 1 273 ? -1.158  15.266  -44.518 1.00 29.44  ? 253 VAL B CB    1 
ATOM   4422 C  CG1   . VAL B 1 273 ? -1.378  16.379  -43.501 1.00 35.52  ? 253 VAL B CG1   1 
ATOM   4423 C  CG2   . VAL B 1 273 ? -2.450  14.466  -44.735 1.00 30.40  ? 253 VAL B CG2   1 
ATOM   4424 N  N     . ASN B 1 274 ? 0.654   17.803  -46.372 1.00 29.43  ? 254 ASN B N     1 
ATOM   4425 C  CA    . ASN B 1 274 ? 1.804   18.703  -46.330 1.00 36.27  ? 254 ASN B CA    1 
ATOM   4426 C  C     . ASN B 1 274 ? 1.232   20.109  -46.276 1.00 48.05  ? 254 ASN B C     1 
ATOM   4427 O  O     . ASN B 1 274 ? 0.932   20.713  -47.316 1.00 47.36  ? 254 ASN B O     1 
ATOM   4428 C  CB    . ASN B 1 274 ? 2.713   18.508  -47.541 1.00 32.50  ? 254 ASN B CB    1 
ATOM   4429 C  CG    . ASN B 1 274 ? 3.982   19.332  -47.453 1.00 39.61  ? 254 ASN B CG    1 
ATOM   4430 O  OD1   . ASN B 1 274 ? 4.497   19.593  -46.361 1.00 43.43  ? 254 ASN B OD1   1 
ATOM   4431 N  ND2   . ASN B 1 274 ? 4.480   19.766  -48.602 1.00 35.82  ? 254 ASN B ND2   1 
ATOM   4432 N  N     . PRO B 1 275 ? 1.023   20.649  -45.076 1.00 43.85  ? 255 PRO B N     1 
ATOM   4433 C  CA    . PRO B 1 275 ? 0.376   21.962  -44.962 1.00 55.27  ? 255 PRO B CA    1 
ATOM   4434 C  C     . PRO B 1 275 ? 1.201   23.057  -45.623 1.00 60.78  ? 255 PRO B C     1 
ATOM   4435 O  O     . PRO B 1 275 ? 2.431   22.991  -45.687 1.00 63.31  ? 255 PRO B O     1 
ATOM   4436 C  CB    . PRO B 1 275 ? 0.269   22.175  -43.447 1.00 58.08  ? 255 PRO B CB    1 
ATOM   4437 C  CG    . PRO B 1 275 ? 0.291   20.784  -42.873 1.00 56.31  ? 255 PRO B CG    1 
ATOM   4438 C  CD    . PRO B 1 275 ? 1.228   20.014  -43.763 1.00 44.06  ? 255 PRO B CD    1 
ATOM   4439 N  N     . SER B 1 276 ? 0.498   24.074  -46.126 1.00 68.48  ? 256 SER B N     1 
ATOM   4440 C  CA    . SER B 1 276 ? 1.131   25.200  -46.804 1.00 72.15  ? 256 SER B CA    1 
ATOM   4441 C  C     . SER B 1 276 ? 2.005   26.000  -45.845 1.00 73.60  ? 256 SER B C     1 
ATOM   4442 O  O     . SER B 1 276 ? 2.118   25.659  -44.662 1.00 69.88  ? 256 SER B O     1 
ATOM   4443 C  CB    . SER B 1 276 ? 0.072   26.108  -47.437 1.00 67.29  ? 256 SER B CB    1 
ATOM   4444 O  OG    . SER B 1 276 ? -0.694  25.413  -48.407 1.00 64.70  ? 256 SER B OG    1 
ATOM   4445 N  N     . VAL B 1 277 ? 2.625   27.071  -46.348 1.00 77.29  ? 257 VAL B N     1 
ATOM   4446 C  CA    . VAL B 1 277 ? 3.510   27.885  -45.516 1.00 79.60  ? 257 VAL B CA    1 
ATOM   4447 C  C     . VAL B 1 277 ? 2.764   28.463  -44.319 1.00 74.75  ? 257 VAL B C     1 
ATOM   4448 O  O     . VAL B 1 277 ? 3.341   28.620  -43.235 1.00 69.94  ? 257 VAL B O     1 
ATOM   4449 C  CB    . VAL B 1 277 ? 4.166   28.992  -46.363 1.00 80.43  ? 257 VAL B CB    1 
ATOM   4450 C  CG1   . VAL B 1 277 ? 5.219   28.400  -47.284 1.00 71.62  ? 257 VAL B CG1   1 
ATOM   4451 C  CG2   . VAL B 1 277 ? 3.110   29.740  -47.169 1.00 74.79  ? 257 VAL B CG2   1 
ATOM   4452 N  N     . ASN B 1 278 ? 1.479   28.781  -44.486 1.00 66.96  ? 258 ASN B N     1 
ATOM   4453 C  CA    . ASN B 1 278 ? 0.680   29.295  -43.381 1.00 59.20  ? 258 ASN B CA    1 
ATOM   4454 C  C     . ASN B 1 278 ? 0.139   28.188  -42.484 1.00 65.98  ? 258 ASN B C     1 
ATOM   4455 O  O     . ASN B 1 278 ? -0.296  28.473  -41.363 1.00 52.16  ? 258 ASN B O     1 
ATOM   4456 C  CB    . ASN B 1 278 ? -0.479  30.142  -43.919 1.00 59.83  ? 258 ASN B CB    1 
ATOM   4457 C  CG    . ASN B 1 278 ? -1.445  29.342  -44.778 1.00 71.95  ? 258 ASN B CG    1 
ATOM   4458 O  OD1   . ASN B 1 278 ? -1.178  28.192  -45.133 1.00 77.34  ? 258 ASN B OD1   1 
ATOM   4459 N  ND2   . ASN B 1 278 ? -2.571  29.957  -45.127 1.00 60.75  ? 258 ASN B ND2   1 
ATOM   4460 N  N     . GLY B 1 279 ? 0.147   26.940  -42.950 1.00 71.61  ? 259 GLY B N     1 
ATOM   4461 C  CA    . GLY B 1 279 ? -0.311  25.815  -42.159 1.00 66.63  ? 259 GLY B CA    1 
ATOM   4462 C  C     . GLY B 1 279 ? -1.651  25.243  -42.565 1.00 59.69  ? 259 GLY B C     1 
ATOM   4463 O  O     . GLY B 1 279 ? -2.151  24.345  -41.874 1.00 63.94  ? 259 GLY B O     1 
ATOM   4464 N  N     . SER B 1 280 ? -2.262  25.737  -43.639 1.00 61.92  ? 260 SER B N     1 
ATOM   4465 C  CA    . SER B 1 280 ? -3.534  25.212  -44.115 1.00 71.58  ? 260 SER B CA    1 
ATOM   4466 C  C     . SER B 1 280 ? -3.322  24.026  -45.056 1.00 66.44  ? 260 SER B C     1 
ATOM   4467 O  O     . SER B 1 280 ? -2.245  23.844  -45.632 1.00 61.87  ? 260 SER B O     1 
ATOM   4468 C  CB    . SER B 1 280 ? -4.321  26.308  -44.835 1.00 69.10  ? 260 SER B CB    1 
ATOM   4469 O  OG    . SER B 1 280 ? -3.551  26.869  -45.887 1.00 75.44  ? 260 SER B OG    1 
ATOM   4470 N  N     . LEU B 1 281 ? -4.368  23.205  -45.194 1.00 40.88  ? 261 LEU B N     1 
ATOM   4471 C  CA    . LEU B 1 281 ? -4.320  22.043  -46.080 1.00 49.48  ? 261 LEU B CA    1 
ATOM   4472 C  C     . LEU B 1 281 ? -5.130  22.304  -47.348 1.00 42.95  ? 261 LEU B C     1 
ATOM   4473 O  O     . LEU B 1 281 ? -6.371  22.327  -47.290 1.00 38.62  ? 261 LEU B O     1 
ATOM   4474 C  CB    . LEU B 1 281 ? -4.832  20.795  -45.360 1.00 44.52  ? 261 LEU B CB    1 
ATOM   4475 C  CG    . LEU B 1 281 ? -4.638  19.487  -46.123 1.00 39.26  ? 261 LEU B CG    1 
ATOM   4476 C  CD1   . LEU B 1 281 ? -3.174  19.364  -46.546 1.00 35.40  ? 261 LEU B CD1   1 
ATOM   4477 C  CD2   . LEU B 1 281 ? -5.012  18.309  -45.246 1.00 31.75  ? 261 LEU B CD2   1 
ATOM   4478 N  N     . PRO B 1 282 ? -4.493  22.473  -48.502 1.00 37.12  ? 262 PRO B N     1 
ATOM   4479 C  CA    . PRO B 1 282 ? -5.224  22.863  -49.729 1.00 30.96  ? 262 PRO B CA    1 
ATOM   4480 C  C     . PRO B 1 282 ? -5.948  21.688  -50.363 1.00 27.69  ? 262 PRO B C     1 
ATOM   4481 O  O     . PRO B 1 282 ? -5.532  20.531  -50.200 1.00 30.26  ? 262 PRO B O     1 
ATOM   4482 C  CB    . PRO B 1 282 ? -4.107  23.381  -50.644 1.00 35.93  ? 262 PRO B CB    1 
ATOM   4483 C  CG    . PRO B 1 282 ? -2.894  22.603  -50.202 1.00 37.75  ? 262 PRO B CG    1 
ATOM   4484 C  CD    . PRO B 1 282 ? -3.035  22.417  -48.715 1.00 33.03  ? 262 PRO B CD    1 
ATOM   4485 N  N     . PRO B 1 283 ? -7.028  21.940  -51.107 1.00 26.56  ? 263 PRO B N     1 
ATOM   4486 C  CA    . PRO B 1 283 ? -7.633  20.866  -51.900 1.00 23.09  ? 263 PRO B CA    1 
ATOM   4487 C  C     . PRO B 1 283 ? -6.696  20.440  -53.018 1.00 27.96  ? 263 PRO B C     1 
ATOM   4488 O  O     . PRO B 1 283 ? -5.824  21.190  -53.454 1.00 25.87  ? 263 PRO B O     1 
ATOM   4489 C  CB    . PRO B 1 283 ? -8.907  21.505  -52.463 1.00 29.85  ? 263 PRO B CB    1 
ATOM   4490 C  CG    . PRO B 1 283 ? -8.633  22.965  -52.455 1.00 31.47  ? 263 PRO B CG    1 
ATOM   4491 C  CD    . PRO B 1 283 ? -7.758  23.211  -51.257 1.00 27.01  ? 263 PRO B CD    1 
ATOM   4492 N  N     . LEU B 1 284 ? -6.894  19.217  -53.488 1.00 22.80  ? 264 LEU B N     1 
ATOM   4493 C  CA    . LEU B 1 284 ? -6.099  18.679  -54.579 1.00 21.55  ? 264 LEU B CA    1 
ATOM   4494 C  C     . LEU B 1 284 ? -6.695  19.095  -55.919 1.00 26.48  ? 264 LEU B C     1 
ATOM   4495 O  O     . LEU B 1 284 ? -7.887  19.379  -56.034 1.00 29.34  ? 264 LEU B O     1 
ATOM   4496 C  CB    . LEU B 1 284 ? -6.039  17.155  -54.475 1.00 22.74  ? 264 LEU B CB    1 
ATOM   4497 C  CG    . LEU B 1 284 ? -5.367  16.607  -53.217 1.00 23.36  ? 264 LEU B CG    1 
ATOM   4498 C  CD1   . LEU B 1 284 ? -5.686  15.129  -53.074 1.00 26.93  ? 264 LEU B CD1   1 
ATOM   4499 C  CD2   . LEU B 1 284 ? -3.843  16.798  -53.366 1.00 20.74  ? 264 LEU B CD2   1 
ATOM   4500 N  N     . GLY B 1 285 ? -5.864  19.059  -56.957 1.00 24.37  ? 265 GLY B N     1 
ATOM   4501 C  CA    . GLY B 1 285 ? -6.298  19.500  -58.268 1.00 24.04  ? 265 GLY B CA    1 
ATOM   4502 C  C     . GLY B 1 285 ? -7.323  18.537  -58.837 1.00 23.74  ? 265 GLY B C     1 
ATOM   4503 O  O     . GLY B 1 285 ? -7.048  17.334  -58.972 1.00 28.25  ? 265 GLY B O     1 
ATOM   4504 N  N     . GLU B 1 286 ? -8.508  19.039  -59.153 1.00 26.52  ? 266 GLU B N     1 
ATOM   4505 C  CA    . GLU B 1 286 ? -9.553  18.228  -59.763 1.00 23.39  ? 266 GLU B CA    1 
ATOM   4506 C  C     . GLU B 1 286 ? -9.419  18.230  -61.282 1.00 24.18  ? 266 GLU B C     1 
ATOM   4507 O  O     . GLU B 1 286 ? -9.120  19.263  -61.891 1.00 24.15  ? 266 GLU B O     1 
ATOM   4508 C  CB    . GLU B 1 286 ? -10.935 18.735  -59.346 1.00 25.51  ? 266 GLU B CB    1 
ATOM   4509 C  CG    . GLU B 1 286 ? -12.056 17.955  -59.975 1.00 25.45  ? 266 GLU B CG    1 
ATOM   4510 C  CD    . GLU B 1 286 ? -13.379 18.123  -59.252 1.00 24.05  ? 266 GLU B CD    1 
ATOM   4511 O  OE1   . GLU B 1 286 ? -13.485 19.003  -58.357 1.00 21.78  ? 266 GLU B OE1   1 
ATOM   4512 O  OE2   . GLU B 1 286 ? -14.320 17.369  -59.604 1.00 21.97  ? 266 GLU B OE2   1 
ATOM   4513 N  N     . LEU B 1 287 ? -9.571  17.050  -61.886 1.00 21.48  ? 267 LEU B N     1 
ATOM   4514 C  CA    . LEU B 1 287 ? -9.574  16.956  -63.342 1.00 23.09  ? 267 LEU B CA    1 
ATOM   4515 C  C     . LEU B 1 287 ? -10.813 17.640  -63.912 1.00 26.52  ? 267 LEU B C     1 
ATOM   4516 O  O     . LEU B 1 287 ? -11.904 17.529  -63.342 1.00 28.67  ? 267 LEU B O     1 
ATOM   4517 C  CB    . LEU B 1 287 ? -9.531  15.501  -63.817 1.00 26.27  ? 267 LEU B CB    1 
ATOM   4518 C  CG    . LEU B 1 287 ? -8.322  14.654  -63.402 1.00 34.40  ? 267 LEU B CG    1 
ATOM   4519 C  CD1   . LEU B 1 287 ? -8.356  13.320  -64.129 1.00 31.92  ? 267 LEU B CD1   1 
ATOM   4520 C  CD2   . LEU B 1 287 ? -7.022  15.384  -63.676 1.00 36.32  ? 267 LEU B CD2   1 
ATOM   4521 N  N     . PRO B 1 288 ? -10.666 18.392  -65.002 1.00 28.89  ? 268 PRO B N     1 
ATOM   4522 C  CA    . PRO B 1 288 ? -11.836 19.082  -65.570 1.00 33.61  ? 268 PRO B CA    1 
ATOM   4523 C  C     . PRO B 1 288 ? -12.948 18.138  -65.981 1.00 36.68  ? 268 PRO B C     1 
ATOM   4524 O  O     . PRO B 1 288 ? -14.131 18.469  -65.839 1.00 39.99  ? 268 PRO B O     1 
ATOM   4525 C  CB    . PRO B 1 288 ? -11.242 19.822  -66.776 1.00 32.51  ? 268 PRO B CB    1 
ATOM   4526 C  CG    . PRO B 1 288 ? -10.038 19.013  -67.154 1.00 33.49  ? 268 PRO B CG    1 
ATOM   4527 C  CD    . PRO B 1 288 ? -9.472  18.512  -65.858 1.00 28.41  ? 268 PRO B CD    1 
ATOM   4528 N  N     . THR B 1 289 ? -12.600 16.979  -66.522 1.00 32.97  ? 269 THR B N     1 
ATOM   4529 C  CA    . THR B 1 289 ? -13.585 16.031  -67.012 1.00 44.11  ? 269 THR B CA    1 
ATOM   4530 C  C     . THR B 1 289 ? -13.196 14.627  -66.579 1.00 44.16  ? 269 THR B C     1 
ATOM   4531 O  O     . THR B 1 289 ? -12.023 14.339  -66.334 1.00 35.00  ? 269 THR B O     1 
ATOM   4532 C  CB    . THR B 1 289 ? -13.739 16.090  -68.537 1.00 39.03  ? 269 THR B CB    1 
ATOM   4533 O  OG1   . THR B 1 289 ? -14.650 15.066  -68.953 1.00 62.07  ? 269 THR B OG1   1 
ATOM   4534 C  CG2   . THR B 1 289 ? -12.401 15.886  -69.225 1.00 45.30  ? 269 THR B CG2   1 
ATOM   4535 N  N     . SER B 1 290 ? -14.197 13.769  -66.446 1.00 41.99  ? 270 SER B N     1 
ATOM   4536 C  CA    . SER B 1 290 ? -13.915 12.369  -66.187 1.00 31.92  ? 270 SER B CA    1 
ATOM   4537 C  C     . SER B 1 290 ? -12.996 11.827  -67.278 1.00 30.61  ? 270 SER B C     1 
ATOM   4538 O  O     . SER B 1 290 ? -13.183 12.138  -68.458 1.00 33.35  ? 270 SER B O     1 
ATOM   4539 C  CB    . SER B 1 290 ? -15.207 11.554  -66.167 1.00 39.60  ? 270 SER B CB    1 
ATOM   4540 O  OG    . SER B 1 290 ? -14.912 10.172  -66.267 1.00 38.03  ? 270 SER B OG    1 
ATOM   4541 N  N     . PRO B 1 291 ? -12.005 11.006  -66.927 1.00 34.35  ? 271 PRO B N     1 
ATOM   4542 C  CA    . PRO B 1 291 ? -11.170 10.389  -67.959 1.00 30.85  ? 271 PRO B CA    1 
ATOM   4543 C  C     . PRO B 1 291 ? -11.896 9.321   -68.759 1.00 37.96  ? 271 PRO B C     1 
ATOM   4544 O  O     . PRO B 1 291 ? -11.373 8.882   -69.787 1.00 37.04  ? 271 PRO B O     1 
ATOM   4545 C  CB    . PRO B 1 291 ? -10.006 9.799   -67.153 1.00 38.78  ? 271 PRO B CB    1 
ATOM   4546 C  CG    . PRO B 1 291 ? -10.626 9.464   -65.846 1.00 35.11  ? 271 PRO B CG    1 
ATOM   4547 C  CD    . PRO B 1 291 ? -11.611 10.577  -65.574 1.00 34.26  ? 271 PRO B CD    1 
ATOM   4548 N  N     . ASP B 1 292 ? -13.093 8.929   -68.346 1.00 32.81  ? 272 ASP B N     1 
ATOM   4549 C  CA    . ASP B 1 292 ? -13.853 7.867   -68.990 1.00 31.64  ? 272 ASP B CA    1 
ATOM   4550 C  C     . ASP B 1 292 ? -15.295 8.335   -69.121 1.00 31.37  ? 272 ASP B C     1 
ATOM   4551 O  O     . ASP B 1 292 ? -16.000 8.459   -68.112 1.00 28.27  ? 272 ASP B O     1 
ATOM   4552 C  CB    . ASP B 1 292 ? -13.760 6.568   -68.182 1.00 32.06  ? 272 ASP B CB    1 
ATOM   4553 C  CG    . ASP B 1 292 ? -14.522 5.409   -68.822 1.00 30.87  ? 272 ASP B CG    1 
ATOM   4554 O  OD1   . ASP B 1 292 ? -15.212 5.610   -69.846 1.00 29.71  ? 272 ASP B OD1   1 
ATOM   4555 O  OD2   . ASP B 1 292 ? -14.421 4.281   -68.292 1.00 33.97  ? 272 ASP B OD2   1 
ATOM   4556 N  N     . PRO B 1 293 ? -15.757 8.636   -70.336 1.00 29.06  ? 273 PRO B N     1 
ATOM   4557 C  CA    . PRO B 1 293 ? -17.127 9.150   -70.488 1.00 27.71  ? 273 PRO B CA    1 
ATOM   4558 C  C     . PRO B 1 293 ? -18.190 8.159   -70.059 1.00 29.90  ? 273 PRO B C     1 
ATOM   4559 O  O     . PRO B 1 293 ? -19.334 8.566   -69.834 1.00 32.34  ? 273 PRO B O     1 
ATOM   4560 C  CB    . PRO B 1 293 ? -17.225 9.455   -71.987 1.00 38.31  ? 273 PRO B CB    1 
ATOM   4561 C  CG    . PRO B 1 293 ? -16.202 8.564   -72.613 1.00 37.04  ? 273 PRO B CG    1 
ATOM   4562 C  CD    . PRO B 1 293 ? -15.071 8.500   -71.632 1.00 33.97  ? 273 PRO B CD    1 
ATOM   4563 N  N     . LYS B 1 294 ? -17.853 6.878   -69.927 1.00 27.95  ? 274 LYS B N     1 
ATOM   4564 C  CA    . LYS B 1 294 ? -18.830 5.903   -69.459 1.00 27.29  ? 274 LYS B CA    1 
ATOM   4565 C  C     . LYS B 1 294 ? -18.952 5.878   -67.940 1.00 29.01  ? 274 LYS B C     1 
ATOM   4566 O  O     . LYS B 1 294 ? -19.865 5.232   -67.418 1.00 28.15  ? 274 LYS B O     1 
ATOM   4567 C  CB    . LYS B 1 294 ? -18.468 4.511   -69.976 1.00 31.46  ? 274 LYS B CB    1 
ATOM   4568 C  CG    . LYS B 1 294 ? -18.743 4.351   -71.467 1.00 34.72  ? 274 LYS B CG    1 
ATOM   4569 C  CD    . LYS B 1 294 ? -18.589 2.918   -71.932 1.00 41.87  ? 274 LYS B CD    1 
ATOM   4570 C  CE    . LYS B 1 294 ? -19.923 2.190   -71.911 1.00 70.00  ? 274 LYS B CE    1 
ATOM   4571 N  NZ    . LYS B 1 294 ? -19.867 0.885   -72.628 1.00 78.70  ? 274 LYS B NZ    1 
ATOM   4572 N  N     . ALA B 1 295 ? -18.071 6.556   -67.214 1.00 23.56  ? 275 ALA B N     1 
ATOM   4573 C  CA    . ALA B 1 295 ? -18.234 6.624   -65.768 1.00 24.37  ? 275 ALA B CA    1 
ATOM   4574 C  C     . ALA B 1 295 ? -19.452 7.468   -65.406 1.00 20.39  ? 275 ALA B C     1 
ATOM   4575 O  O     . ALA B 1 295 ? -19.803 8.422   -66.106 1.00 27.70  ? 275 ALA B O     1 
ATOM   4576 C  CB    . ALA B 1 295 ? -16.985 7.212   -65.109 1.00 26.99  ? 275 ALA B CB    1 
ATOM   4577 N  N     . GLY B 1 296 ? -20.093 7.117   -64.293 1.00 22.22  ? 276 GLY B N     1 
ATOM   4578 C  CA    . GLY B 1 296 ? -21.151 7.946   -63.749 1.00 25.44  ? 276 GLY B CA    1 
ATOM   4579 C  C     . GLY B 1 296 ? -22.362 7.139   -63.316 1.00 22.73  ? 276 GLY B C     1 
ATOM   4580 O  O     . GLY B 1 296 ? -22.306 5.918   -63.156 1.00 20.68  ? 276 GLY B O     1 
ATOM   4581 N  N     . LEU B 1 297 ? -23.467 7.862   -63.141 1.00 20.99  ? 277 LEU B N     1 
ATOM   4582 C  CA    . LEU B 1 297 ? -24.716 7.322   -62.611 1.00 18.56  ? 277 LEU B CA    1 
ATOM   4583 C  C     . LEU B 1 297 ? -25.609 6.834   -63.747 1.00 20.29  ? 277 LEU B C     1 
ATOM   4584 O  O     . LEU B 1 297 ? -25.802 7.549   -64.740 1.00 19.92  ? 277 LEU B O     1 
ATOM   4585 C  CB    . LEU B 1 297 ? -25.437 8.400   -61.798 1.00 18.53  ? 277 LEU B CB    1 
ATOM   4586 C  CG    . LEU B 1 297 ? -26.859 8.085   -61.321 1.00 17.90  ? 277 LEU B CG    1 
ATOM   4587 C  CD1   . LEU B 1 297 ? -26.881 6.923   -60.338 1.00 17.84  ? 277 LEU B CD1   1 
ATOM   4588 C  CD2   . LEU B 1 297 ? -27.457 9.333   -60.682 1.00 19.54  ? 277 LEU B CD2   1 
ATOM   4589 N  N     . TYR B 1 298 ? -26.169 5.632   -63.585 1.00 18.94  ? 278 TYR B N     1 
ATOM   4590 C  CA    . TYR B 1 298 ? -27.060 5.006   -64.553 1.00 19.23  ? 278 TYR B CA    1 
ATOM   4591 C  C     . TYR B 1 298 ? -28.347 4.626   -63.833 1.00 22.42  ? 278 TYR B C     1 
ATOM   4592 O  O     . TYR B 1 298 ? -28.305 4.059   -62.736 1.00 18.83  ? 278 TYR B O     1 
ATOM   4593 C  CB    . TYR B 1 298 ? -26.418 3.756   -65.175 1.00 19.72  ? 278 TYR B CB    1 
ATOM   4594 C  CG    . TYR B 1 298 ? -25.254 4.044   -66.092 1.00 22.01  ? 278 TYR B CG    1 
ATOM   4595 C  CD1   . TYR B 1 298 ? -23.987 4.306   -65.588 1.00 21.62  ? 278 TYR B CD1   1 
ATOM   4596 C  CD2   . TYR B 1 298 ? -25.426 4.038   -67.469 1.00 22.99  ? 278 TYR B CD2   1 
ATOM   4597 C  CE1   . TYR B 1 298 ? -22.923 4.577   -66.437 1.00 22.03  ? 278 TYR B CE1   1 
ATOM   4598 C  CE2   . TYR B 1 298 ? -24.370 4.289   -68.323 1.00 25.91  ? 278 TYR B CE2   1 
ATOM   4599 C  CZ    . TYR B 1 298 ? -23.130 4.561   -67.805 1.00 25.61  ? 278 TYR B CZ    1 
ATOM   4600 O  OH    . TYR B 1 298 ? -22.091 4.807   -68.668 1.00 26.20  ? 278 TYR B OH    1 
ATOM   4601 N  N     . ILE B 1 299 ? -29.483 4.951   -64.437 1.00 19.01  ? 279 ILE B N     1 
ATOM   4602 C  CA    . ILE B 1 299 ? -30.791 4.746   -63.825 1.00 18.84  ? 279 ILE B CA    1 
ATOM   4603 C  C     . ILE B 1 299 ? -31.657 3.953   -64.791 1.00 23.56  ? 279 ILE B C     1 
ATOM   4604 O  O     . ILE B 1 299 ? -31.669 4.234   -65.995 1.00 22.49  ? 279 ILE B O     1 
ATOM   4605 C  CB    . ILE B 1 299 ? -31.457 6.094   -63.479 1.00 18.52  ? 279 ILE B CB    1 
ATOM   4606 C  CG1   . ILE B 1 299 ? -30.541 6.887   -62.533 1.00 21.33  ? 279 ILE B CG1   1 
ATOM   4607 C  CG2   . ILE B 1 299 ? -32.854 5.886   -62.889 1.00 18.42  ? 279 ILE B CG2   1 
ATOM   4608 C  CD1   . ILE B 1 299 ? -31.030 8.286   -62.186 1.00 21.02  ? 279 ILE B CD1   1 
ATOM   4609 N  N     . LYS B 1 300 ? -32.363 2.951   -64.273 1.00 21.71  ? 280 LYS B N     1 
ATOM   4610 C  CA    . LYS B 1 300 ? -33.276 2.145   -65.080 1.00 20.20  ? 280 LYS B CA    1 
ATOM   4611 C  C     . LYS B 1 300 ? -34.696 2.402   -64.582 1.00 23.16  ? 280 LYS B C     1 
ATOM   4612 O  O     . LYS B 1 300 ? -35.137 1.802   -63.597 1.00 24.49  ? 280 LYS B O     1 
ATOM   4613 C  CB    . LYS B 1 300 ? -32.903 0.669   -65.016 1.00 22.69  ? 280 LYS B CB    1 
ATOM   4614 C  CG    . LYS B 1 300 ? -33.768 -0.211  -65.921 1.00 34.40  ? 280 LYS B CG    1 
ATOM   4615 C  CD    . LYS B 1 300 ? -33.582 -1.685  -65.605 1.00 47.96  ? 280 LYS B CD    1 
ATOM   4616 C  CE    . LYS B 1 300 ? -32.372 -2.247  -66.336 1.00 48.67  ? 280 LYS B CE    1 
ATOM   4617 N  NZ    . LYS B 1 300 ? -32.503 -2.082  -67.815 1.00 52.78  ? 280 LYS B NZ    1 
ATOM   4618 N  N     . SER B 1 301 ? -35.393 3.318   -65.249 1.00 21.17  ? 281 SER B N     1 
ATOM   4619 C  CA    . SER B 1 301 ? -36.771 3.651   -64.906 1.00 20.36  ? 281 SER B CA    1 
ATOM   4620 C  C     . SER B 1 301 ? -37.723 2.553   -65.374 1.00 25.42  ? 281 SER B C     1 
ATOM   4621 O  O     . SER B 1 301 ? -37.325 1.523   -65.933 1.00 23.05  ? 281 SER B O     1 
ATOM   4622 C  CB    . SER B 1 301 ? -37.181 4.982   -65.527 1.00 24.71  ? 281 SER B CB    1 
ATOM   4623 O  OG    . SER B 1 301 ? -37.450 4.819   -66.911 1.00 26.67  ? 281 SER B OG    1 
ATOM   4624 N  N     . ARG B 1 302 ? -39.010 2.804   -65.144 1.00 23.72  ? 282 ARG B N     1 
ATOM   4625 C  CA    . ARG B 1 302 ? -40.058 1.882   -65.565 1.00 29.83  ? 282 ARG B CA    1 
ATOM   4626 C  C     . ARG B 1 302 ? -40.175 1.743   -67.078 1.00 30.74  ? 282 ARG B C     1 
ATOM   4627 O  O     . ARG B 1 302 ? -40.915 0.866   -67.533 1.00 29.38  ? 282 ARG B O     1 
ATOM   4628 C  CB    . ARG B 1 302 ? -41.400 2.326   -64.987 1.00 33.33  ? 282 ARG B CB    1 
ATOM   4629 C  CG    . ARG B 1 302 ? -41.722 1.709   -63.643 1.00 46.99  ? 282 ARG B CG    1 
ATOM   4630 C  CD    . ARG B 1 302 ? -43.119 2.097   -63.195 1.00 53.75  ? 282 ARG B CD    1 
ATOM   4631 N  NE    . ARG B 1 302 ? -44.135 1.850   -64.209 1.00 53.87  ? 282 ARG B NE    1 
ATOM   4632 C  CZ    . ARG B 1 302 ? -45.411 2.182   -64.073 1.00 72.45  ? 282 ARG B CZ    1 
ATOM   4633 N  NH1   . ARG B 1 302 ? -45.861 2.761   -62.970 1.00 57.22  ? 282 ARG B NH1   1 
ATOM   4634 N  NH2   . ARG B 1 302 ? -46.255 1.941   -65.073 1.00 74.42  ? 282 ARG B NH2   1 
ATOM   4635 N  N     . THR B 1 303 ? -39.496 2.578   -67.872 1.00 26.42  ? 283 THR B N     1 
ATOM   4636 C  CA    . THR B 1 303 ? -39.411 2.289   -69.301 1.00 29.21  ? 283 THR B CA    1 
ATOM   4637 C  C     . THR B 1 303 ? -38.613 1.025   -69.591 1.00 33.50  ? 283 THR B C     1 
ATOM   4638 O  O     . THR B 1 303 ? -38.717 0.484   -70.698 1.00 36.76  ? 283 THR B O     1 
ATOM   4639 C  CB    . THR B 1 303 ? -38.766 3.440   -70.073 1.00 26.89  ? 283 THR B CB    1 
ATOM   4640 O  OG1   . THR B 1 303 ? -37.381 3.542   -69.698 1.00 31.26  ? 283 THR B OG1   1 
ATOM   4641 C  CG2   . THR B 1 303 ? -39.476 4.751   -69.794 1.00 32.08  ? 283 THR B CG2   1 
ATOM   4642 N  N     . GLY B 1 304 ? -37.811 0.557   -68.638 1.00 27.17  ? 284 GLY B N     1 
ATOM   4643 C  CA    . GLY B 1 304 ? -36.968 -0.597  -68.848 1.00 29.49  ? 284 GLY B CA    1 
ATOM   4644 C  C     . GLY B 1 304 ? -35.626 -0.267  -69.456 1.00 29.48  ? 284 GLY B C     1 
ATOM   4645 O  O     . GLY B 1 304 ? -34.765 -1.151  -69.548 1.00 30.98  ? 284 GLY B O     1 
ATOM   4646 N  N     . GLN B 1 305 ? -35.399 0.985   -69.819 1.00 27.99  ? 285 GLN B N     1 
ATOM   4647 C  CA    . GLN B 1 305 ? -34.173 1.392   -70.480 1.00 24.00  ? 285 GLN B CA    1 
ATOM   4648 C  C     . GLN B 1 305 ? -33.247 2.057   -69.475 1.00 27.97  ? 285 GLN B C     1 
ATOM   4649 O  O     . GLN B 1 305 ? -33.688 2.843   -68.630 1.00 28.00  ? 285 GLN B O     1 
ATOM   4650 C  CB    . GLN B 1 305 ? -34.490 2.373   -71.610 1.00 32.45  ? 285 GLN B CB    1 
ATOM   4651 C  CG    . GLN B 1 305 ? -33.274 2.985   -72.276 1.00 27.12  ? 285 GLN B CG    1 
ATOM   4652 C  CD    . GLN B 1 305 ? -33.637 4.050   -73.288 1.00 31.27  ? 285 GLN B CD    1 
ATOM   4653 O  OE1   . GLN B 1 305 ? -33.279 3.949   -74.467 1.00 42.98  ? 285 GLN B OE1   1 
ATOM   4654 N  NE2   . GLN B 1 305 ? -34.331 5.090   -72.835 1.00 25.90  ? 285 GLN B NE2   1 
ATOM   4655 N  N     . THR B 1 306 ? -31.958 1.770   -69.597 1.00 25.99  ? 286 THR B N     1 
ATOM   4656 C  CA    . THR B 1 306 ? -30.968 2.338   -68.696 1.00 23.64  ? 286 THR B CA    1 
ATOM   4657 C  C     . THR B 1 306 ? -30.435 3.606   -69.342 1.00 24.97  ? 286 THR B C     1 
ATOM   4658 O  O     . THR B 1 306 ? -30.043 3.591   -70.514 1.00 27.21  ? 286 THR B O     1 
ATOM   4659 C  CB    . THR B 1 306 ? -29.833 1.351   -68.436 1.00 25.90  ? 286 THR B CB    1 
ATOM   4660 O  OG1   . THR B 1 306 ? -30.368 0.163   -67.837 1.00 29.23  ? 286 THR B OG1   1 
ATOM   4661 C  CG2   . THR B 1 306 ? -28.770 1.972   -67.521 1.00 26.01  ? 286 THR B CG2   1 
ATOM   4662 N  N     . VAL B 1 307 ? -30.432 4.700   -68.582 1.00 22.08  ? 287 VAL B N     1 
ATOM   4663 C  CA    . VAL B 1 307 ? -29.929 5.975   -69.074 1.00 23.63  ? 287 VAL B CA    1 
ATOM   4664 C  C     . VAL B 1 307 ? -28.844 6.474   -68.131 1.00 24.87  ? 287 VAL B C     1 
ATOM   4665 O  O     . VAL B 1 307 ? -28.844 6.176   -66.935 1.00 22.23  ? 287 VAL B O     1 
ATOM   4666 C  CB    . VAL B 1 307 ? -31.050 7.028   -69.208 1.00 24.31  ? 287 VAL B CB    1 
ATOM   4667 C  CG1   . VAL B 1 307 ? -32.111 6.548   -70.197 1.00 26.10  ? 287 VAL B CG1   1 
ATOM   4668 C  CG2   . VAL B 1 307 ? -31.672 7.323   -67.848 1.00 22.65  ? 287 VAL B CG2   1 
ATOM   4669 N  N     . GLN B 1 308 ? -27.906 7.230   -68.682 1.00 20.53  ? 288 GLN B N     1 
ATOM   4670 C  CA    . GLN B 1 308 ? -26.888 7.896   -67.885 1.00 21.15  ? 288 GLN B CA    1 
ATOM   4671 C  C     . GLN B 1 308 ? -27.398 9.270   -67.466 1.00 23.20  ? 288 GLN B C     1 
ATOM   4672 O  O     . GLN B 1 308 ? -28.053 9.959   -68.246 1.00 24.30  ? 288 GLN B O     1 
ATOM   4673 C  CB    . GLN B 1 308 ? -25.591 7.998   -68.693 1.00 20.30  ? 288 GLN B CB    1 
ATOM   4674 C  CG    . GLN B 1 308 ? -24.350 8.447   -67.935 1.00 22.36  ? 288 GLN B CG    1 
ATOM   4675 C  CD    . GLN B 1 308 ? -23.116 8.428   -68.840 1.00 30.96  ? 288 GLN B CD    1 
ATOM   4676 O  OE1   . GLN B 1 308 ? -23.232 8.532   -70.057 1.00 39.51  ? 288 GLN B OE1   1 
ATOM   4677 N  NE2   . GLN B 1 308 ? -21.934 8.306   -68.245 1.00 30.16  ? 288 GLN B NE2   1 
ATOM   4678 N  N     . VAL B 1 309 ? -27.116 9.658   -66.224 1.00 19.11  ? 289 VAL B N     1 
ATOM   4679 C  CA    . VAL B 1 309 ? -27.587 10.923  -65.668 1.00 18.81  ? 289 VAL B CA    1 
ATOM   4680 C  C     . VAL B 1 309 ? -26.413 11.607  -64.988 1.00 24.14  ? 289 VAL B C     1 
ATOM   4681 O  O     . VAL B 1 309 ? -25.699 10.980  -64.198 1.00 24.84  ? 289 VAL B O     1 
ATOM   4682 C  CB    . VAL B 1 309 ? -28.740 10.725  -64.668 1.00 20.59  ? 289 VAL B CB    1 
ATOM   4683 C  CG1   . VAL B 1 309 ? -29.128 12.050  -64.038 1.00 23.96  ? 289 VAL B CG1   1 
ATOM   4684 C  CG2   . VAL B 1 309 ? -29.948 10.076  -65.362 1.00 21.29  ? 289 VAL B CG2   1 
ATOM   4685 N  N     . LYS B 1 310 ? -26.206 12.883  -65.303 1.00 21.99  ? 290 LYS B N     1 
ATOM   4686 C  CA    . LYS B 1 310 ? -25.077 13.635  -64.779 1.00 22.46  ? 290 LYS B CA    1 
ATOM   4687 C  C     . LYS B 1 310 ? -25.553 14.687  -63.787 1.00 24.01  ? 290 LYS B C     1 
ATOM   4688 O  O     . LYS B 1 310 ? -26.640 15.253  -63.933 1.00 27.92  ? 290 LYS B O     1 
ATOM   4689 C  CB    . LYS B 1 310 ? -24.289 14.285  -65.921 1.00 27.72  ? 290 LYS B CB    1 
ATOM   4690 C  CG    . LYS B 1 310 ? -23.599 13.263  -66.810 1.00 28.80  ? 290 LYS B CG    1 
ATOM   4691 C  CD    . LYS B 1 310 ? -22.847 13.936  -67.951 1.00 38.75  ? 290 LYS B CD    1 
ATOM   4692 C  CE    . LYS B 1 310 ? -22.152 12.916  -68.847 1.00 44.07  ? 290 LYS B CE    1 
ATOM   4693 N  NZ    . LYS B 1 310 ? -21.014 12.249  -68.157 1.00 50.79  ? 290 LYS B NZ    1 
ATOM   4694 N  N     . ILE B 1 311 ? -24.737 14.932  -62.768 1.00 20.16  ? 291 ILE B N     1 
ATOM   4695 C  CA    . ILE B 1 311 ? -24.967 15.994  -61.795 1.00 18.46  ? 291 ILE B CA    1 
ATOM   4696 C  C     . ILE B 1 311 ? -23.988 17.119  -62.116 1.00 20.14  ? 291 ILE B C     1 
ATOM   4697 O  O     . ILE B 1 311 ? -22.771 16.885  -62.114 1.00 21.51  ? 291 ILE B O     1 
ATOM   4698 C  CB    . ILE B 1 311 ? -24.767 15.511  -60.346 1.00 18.17  ? 291 ILE B CB    1 
ATOM   4699 C  CG1   . ILE B 1 311 ? -25.684 14.329  -60.013 1.00 23.84  ? 291 ILE B CG1   1 
ATOM   4700 C  CG2   . ILE B 1 311 ? -24.976 16.672  -59.363 1.00 22.37  ? 291 ILE B CG2   1 
ATOM   4701 C  CD1   . ILE B 1 311 ? -25.396 13.734  -58.647 1.00 27.90  ? 291 ILE B CD1   1 
ATOM   4702 N  N     . PRO B 1 312 ? -24.452 18.328  -62.412 1.00 21.26  ? 292 PRO B N     1 
ATOM   4703 C  CA    . PRO B 1 312 ? -23.510 19.439  -62.609 1.00 21.02  ? 292 PRO B CA    1 
ATOM   4704 C  C     . PRO B 1 312 ? -22.645 19.633  -61.373 1.00 18.90  ? 292 PRO B C     1 
ATOM   4705 O  O     . PRO B 1 312 ? -23.102 19.460  -60.242 1.00 21.59  ? 292 PRO B O     1 
ATOM   4706 C  CB    . PRO B 1 312 ? -24.421 20.647  -62.859 1.00 22.86  ? 292 PRO B CB    1 
ATOM   4707 C  CG    . PRO B 1 312 ? -25.742 20.034  -63.349 1.00 22.91  ? 292 PRO B CG    1 
ATOM   4708 C  CD    . PRO B 1 312 ? -25.858 18.740  -62.581 1.00 22.32  ? 292 PRO B CD    1 
ATOM   4709 N  N     . ARG B 1 313 ? -21.370 19.978  -61.602 1.00 19.61  ? 293 ARG B N     1 
ATOM   4710 C  CA    . ARG B 1 313 ? -20.422 20.054  -60.495 1.00 19.73  ? 293 ARG B CA    1 
ATOM   4711 C  C     . ARG B 1 313 ? -20.870 21.052  -59.439 1.00 20.22  ? 293 ARG B C     1 
ATOM   4712 O  O     . ARG B 1 313 ? -20.590 20.863  -58.249 1.00 21.24  ? 293 ARG B O     1 
ATOM   4713 C  CB    . ARG B 1 313 ? -19.025 20.428  -61.007 1.00 21.69  ? 293 ARG B CB    1 
ATOM   4714 C  CG    . ARG B 1 313 ? -17.946 20.362  -59.933 1.00 26.26  ? 293 ARG B CG    1 
ATOM   4715 C  CD    . ARG B 1 313 ? -16.519 20.519  -60.492 1.00 25.28  ? 293 ARG B CD    1 
ATOM   4716 N  NE    . ARG B 1 313 ? -16.139 19.443  -61.399 1.00 28.55  ? 293 ARG B NE    1 
ATOM   4717 C  CZ    . ARG B 1 313 ? -15.006 19.414  -62.092 1.00 35.15  ? 293 ARG B CZ    1 
ATOM   4718 N  NH1   . ARG B 1 313 ? -14.105 20.376  -61.987 1.00 42.29  ? 293 ARG B NH1   1 
ATOM   4719 N  NH2   . ARG B 1 313 ? -14.774 18.395  -62.916 1.00 33.11  ? 293 ARG B NH2   1 
ATOM   4720 N  N     . ASP B 1 314 ? -21.581 22.105  -59.842 1.00 20.63  ? 294 ASP B N     1 
ATOM   4721 C  CA    . ASP B 1 314 ? -21.989 23.146  -58.911 1.00 23.81  ? 294 ASP B CA    1 
ATOM   4722 C  C     . ASP B 1 314 ? -23.368 22.901  -58.300 1.00 22.71  ? 294 ASP B C     1 
ATOM   4723 O  O     . ASP B 1 314 ? -23.880 23.786  -57.607 1.00 23.91  ? 294 ASP B O     1 
ATOM   4724 C  CB    . ASP B 1 314 ? -21.936 24.525  -59.595 1.00 25.12  ? 294 ASP B CB    1 
ATOM   4725 C  CG    . ASP B 1 314 ? -22.855 24.637  -60.811 1.00 32.05  ? 294 ASP B CG    1 
ATOM   4726 O  OD1   . ASP B 1 314 ? -23.310 23.609  -61.363 1.00 31.46  ? 294 ASP B OD1   1 
ATOM   4727 O  OD2   . ASP B 1 314 ? -23.101 25.782  -61.242 1.00 45.56  ? 294 ASP B OD2   1 
ATOM   4728 N  N     . CYS B 1 315 ? -23.953 21.717  -58.493 1.00 20.21  ? 295 CYS B N     1 
ATOM   4729 C  CA    . CYS B 1 315 ? -25.294 21.404  -58.011 1.00 18.09  ? 295 CYS B CA    1 
ATOM   4730 C  C     . CYS B 1 315 ? -25.258 20.258  -57.005 1.00 18.85  ? 295 CYS B C     1 
ATOM   4731 O  O     . CYS B 1 315 ? -24.260 19.549  -56.864 1.00 18.17  ? 295 CYS B O     1 
ATOM   4732 C  CB    . CYS B 1 315 ? -26.225 21.034  -59.169 1.00 18.35  ? 295 CYS B CB    1 
ATOM   4733 S  SG    . CYS B 1 315 ? -26.606 22.432  -60.245 1.00 24.37  ? 295 CYS B SG    1 
ATOM   4734 N  N     . ILE B 1 316 ? -26.377 20.080  -56.293 1.00 17.00  ? 296 ILE B N     1 
ATOM   4735 C  CA    . ILE B 1 316 ? -26.565 18.944  -55.392 1.00 16.14  ? 296 ILE B CA    1 
ATOM   4736 C  C     . ILE B 1 316 ? -27.749 18.138  -55.896 1.00 21.56  ? 296 ILE B C     1 
ATOM   4737 O  O     . ILE B 1 316 ? -28.748 18.726  -56.308 1.00 24.73  ? 296 ILE B O     1 
ATOM   4738 C  CB    . ILE B 1 316 ? -26.835 19.401  -53.946 1.00 18.75  ? 296 ILE B CB    1 
ATOM   4739 C  CG1   . ILE B 1 316 ? -25.708 20.317  -53.442 1.00 16.94  ? 296 ILE B CG1   1 
ATOM   4740 C  CG2   . ILE B 1 316 ? -27.024 18.186  -53.029 1.00 23.01  ? 296 ILE B CG2   1 
ATOM   4741 C  CD1   . ILE B 1 316 ? -26.080 21.086  -52.170 1.00 23.76  ? 296 ILE B CD1   1 
ATOM   4742 N  N     . ALA B 1 317 ? -27.655 16.810  -55.884 1.00 17.38  ? 297 ALA B N     1 
ATOM   4743 C  CA    . ALA B 1 317 ? -28.812 16.009  -56.281 1.00 16.55  ? 297 ALA B CA    1 
ATOM   4744 C  C     . ALA B 1 317 ? -29.353 15.197  -55.108 1.00 17.80  ? 297 ALA B C     1 
ATOM   4745 O  O     . ALA B 1 317 ? -28.654 14.953  -54.128 1.00 16.49  ? 297 ALA B O     1 
ATOM   4746 C  CB    . ALA B 1 317 ? -28.467 15.080  -57.449 1.00 18.92  ? 297 ALA B CB    1 
ATOM   4747 N  N     . PHE B 1 318 ? -30.618 14.768  -55.219 1.00 16.37  ? 298 PHE B N     1 
ATOM   4748 C  CA    . PHE B 1 318 ? -31.250 13.924  -54.208 1.00 16.52  ? 298 PHE B CA    1 
ATOM   4749 C  C     . PHE B 1 318 ? -31.941 12.754  -54.889 1.00 18.14  ? 298 PHE B C     1 
ATOM   4750 O  O     . PHE B 1 318 ? -32.770 12.959  -55.784 1.00 17.65  ? 298 PHE B O     1 
ATOM   4751 C  CB    . PHE B 1 318 ? -32.248 14.723  -53.361 1.00 19.21  ? 298 PHE B CB    1 
ATOM   4752 C  CG    . PHE B 1 318 ? -31.574 15.756  -52.510 1.00 16.15  ? 298 PHE B CG    1 
ATOM   4753 C  CD1   . PHE B 1 318 ? -31.090 15.422  -51.268 1.00 16.41  ? 298 PHE B CD1   1 
ATOM   4754 C  CD2   . PHE B 1 318 ? -31.369 17.039  -52.998 1.00 19.71  ? 298 PHE B CD2   1 
ATOM   4755 C  CE1   . PHE B 1 318 ? -30.404 16.367  -50.496 1.00 18.49  ? 298 PHE B CE1   1 
ATOM   4756 C  CE2   . PHE B 1 318 ? -30.692 17.990  -52.239 1.00 18.05  ? 298 PHE B CE2   1 
ATOM   4757 C  CZ    . PHE B 1 318 ? -30.221 17.646  -50.974 1.00 19.34  ? 298 PHE B CZ    1 
ATOM   4758 N  N     . GLN B 1 319 ? -31.591 11.538  -54.478 1.00 16.31  ? 299 GLN B N     1 
ATOM   4759 C  CA    . GLN B 1 319 ? -32.298 10.336  -54.919 1.00 16.51  ? 299 GLN B CA    1 
ATOM   4760 C  C     . GLN B 1 319 ? -33.268 9.841   -53.852 1.00 20.08  ? 299 GLN B C     1 
ATOM   4761 O  O     . GLN B 1 319 ? -32.972 9.882   -52.655 1.00 16.70  ? 299 GLN B O     1 
ATOM   4762 C  CB    . GLN B 1 319 ? -31.330 9.206   -55.274 1.00 17.53  ? 299 GLN B CB    1 
ATOM   4763 C  CG    . GLN B 1 319 ? -30.738 9.337   -56.647 1.00 21.14  ? 299 GLN B CG    1 
ATOM   4764 C  CD    . GLN B 1 319 ? -29.747 8.244   -56.936 1.00 23.80  ? 299 GLN B CD    1 
ATOM   4765 O  OE1   . GLN B 1 319 ? -28.690 8.196   -56.323 1.00 20.73  ? 299 GLN B OE1   1 
ATOM   4766 N  NE2   . GLN B 1 319 ? -30.078 7.358   -57.871 1.00 18.81  ? 299 GLN B NE2   1 
ATOM   4767 N  N     . THR B 1 320 ? -34.423 9.352   -54.300 1.00 16.75  ? 300 THR B N     1 
ATOM   4768 C  CA    . THR B 1 320 ? -35.380 8.746   -53.391 1.00 18.18  ? 300 THR B CA    1 
ATOM   4769 C  C     . THR B 1 320 ? -34.893 7.384   -52.920 1.00 18.13  ? 300 THR B C     1 
ATOM   4770 O  O     . THR B 1 320 ? -34.151 6.695   -53.619 1.00 22.21  ? 300 THR B O     1 
ATOM   4771 C  CB    . THR B 1 320 ? -36.710 8.538   -54.091 1.00 18.42  ? 300 THR B CB    1 
ATOM   4772 O  OG1   . THR B 1 320 ? -36.458 7.889   -55.344 1.00 23.13  ? 300 THR B OG1   1 
ATOM   4773 C  CG2   . THR B 1 320 ? -37.410 9.846   -54.314 1.00 23.50  ? 300 THR B CG2   1 
ATOM   4774 N  N     . GLY B 1 321 ? -35.305 6.999   -51.707 1.00 16.95  ? 301 GLY B N     1 
ATOM   4775 C  CA    . GLY B 1 321 ? -35.008 5.691   -51.171 1.00 17.11  ? 301 GLY B CA    1 
ATOM   4776 C  C     . GLY B 1 321 ? -36.267 4.950   -50.740 1.00 19.28  ? 301 GLY B C     1 
ATOM   4777 O  O     . GLY B 1 321 ? -37.370 5.511   -50.717 1.00 17.51  ? 301 GLY B O     1 
ATOM   4778 N  N     . GLU B 1 322 ? -36.075 3.688   -50.332 1.00 17.66  ? 302 GLU B N     1 
ATOM   4779 C  CA    . GLU B 1 322 ? -37.220 2.817   -50.048 1.00 18.05  ? 302 GLU B CA    1 
ATOM   4780 C  C     . GLU B 1 322 ? -38.029 3.297   -48.849 1.00 19.67  ? 302 GLU B C     1 
ATOM   4781 O  O     . GLU B 1 322 ? -39.250 3.089   -48.809 1.00 20.85  ? 302 GLU B O     1 
ATOM   4782 C  CB    . GLU B 1 322 ? -36.755 1.378   -49.812 1.00 18.90  ? 302 GLU B CB    1 
ATOM   4783 C  CG    . GLU B 1 322 ? -36.083 0.716   -51.029 1.00 19.95  ? 302 GLU B CG    1 
ATOM   4784 C  CD    . GLU B 1 322 ? -35.959 -0.790  -50.869 1.00 23.43  ? 302 GLU B CD    1 
ATOM   4785 O  OE1   . GLU B 1 322 ? -36.968 -1.494  -51.090 1.00 34.29  ? 302 GLU B OE1   1 
ATOM   4786 O  OE2   . GLU B 1 322 ? -34.877 -1.264  -50.482 1.00 32.35  ? 302 GLU B OE2   1 
ATOM   4787 N  N     . ALA B 1 323 ? -37.385 3.914   -47.852 1.00 20.09  ? 303 ALA B N     1 
ATOM   4788 C  CA    . ALA B 1 323 ? -38.160 4.398   -46.707 1.00 18.28  ? 303 ALA B CA    1 
ATOM   4789 C  C     . ALA B 1 323 ? -39.105 5.520   -47.119 1.00 20.73  ? 303 ALA B C     1 
ATOM   4790 O  O     . ALA B 1 323 ? -40.237 5.594   -46.623 1.00 20.15  ? 303 ALA B O     1 
ATOM   4791 C  CB    . ALA B 1 323 ? -37.225 4.847   -45.579 1.00 20.46  ? 303 ALA B CB    1 
ATOM   4792 N  N     . LEU B 1 324 ? -38.670 6.392   -48.035 1.00 18.73  ? 304 LEU B N     1 
ATOM   4793 C  CA    A LEU B 1 324 ? -39.572 7.430   -48.522 0.52 17.69  ? 304 LEU B CA    1 
ATOM   4794 C  CA    B LEU B 1 324 ? -39.547 7.436   -48.564 0.48 17.69  ? 304 LEU B CA    1 
ATOM   4795 C  C     . LEU B 1 324 ? -40.684 6.831   -49.375 1.00 20.46  ? 304 LEU B C     1 
ATOM   4796 O  O     . LEU B 1 324 ? -41.837 7.268   -49.282 1.00 19.37  ? 304 LEU B O     1 
ATOM   4797 C  CB    A LEU B 1 324 ? -38.791 8.500   -49.290 0.52 19.70  ? 304 LEU B CB    1 
ATOM   4798 C  CB    B LEU B 1 324 ? -38.731 8.410   -49.422 0.48 19.49  ? 304 LEU B CB    1 
ATOM   4799 C  CG    A LEU B 1 324 ? -39.625 9.741   -49.620 0.52 21.09  ? 304 LEU B CG    1 
ATOM   4800 C  CG    B LEU B 1 324 ? -39.532 9.431   -50.227 0.48 18.59  ? 304 LEU B CG    1 
ATOM   4801 C  CD1   A LEU B 1 324 ? -38.826 11.018  -49.450 0.52 23.07  ? 304 LEU B CD1   1 
ATOM   4802 C  CD1   B LEU B 1 324 ? -40.343 10.262  -49.272 0.48 17.57  ? 304 LEU B CD1   1 
ATOM   4803 C  CD2   A LEU B 1 324 ? -40.185 9.626   -51.026 0.52 17.58  ? 304 LEU B CD2   1 
ATOM   4804 C  CD2   B LEU B 1 324 ? -38.630 10.311  -51.065 0.48 19.92  ? 304 LEU B CD2   1 
ATOM   4805 N  N     . GLU B 1 325 ? -40.369 5.825   -50.187 1.00 19.33  ? 305 GLU B N     1 
ATOM   4806 C  CA    . GLU B 1 325 ? -41.409 5.144   -50.950 1.00 18.46  ? 305 GLU B CA    1 
ATOM   4807 C  C     . GLU B 1 325 ? -42.469 4.570   -50.020 1.00 22.32  ? 305 GLU B C     1 
ATOM   4808 O  O     . GLU B 1 325 ? -43.675 4.709   -50.277 1.00 21.18  ? 305 GLU B O     1 
ATOM   4809 C  CB    . GLU B 1 325 ? -40.788 4.047   -51.818 1.00 20.03  ? 305 GLU B CB    1 
ATOM   4810 C  CG    . GLU B 1 325 ? -41.815 3.239   -52.617 1.00 18.90  ? 305 GLU B CG    1 
ATOM   4811 C  CD    . GLU B 1 325 ? -41.182 2.154   -53.469 1.00 30.23  ? 305 GLU B CD    1 
ATOM   4812 O  OE1   . GLU B 1 325 ? -40.064 2.381   -53.964 1.00 24.00  ? 305 GLU B OE1   1 
ATOM   4813 O  OE2   . GLU B 1 325 ? -41.819 1.102   -53.699 1.00 28.42  ? 305 GLU B OE2   1 
ATOM   4814 N  N     . ARG B 1 326 ? -42.044 3.935   -48.921 1.00 20.01  ? 306 ARG B N     1 
ATOM   4815 C  CA    . ARG B 1 326 ? -43.018 3.360   -47.992 1.00 21.29  ? 306 ARG B CA    1 
ATOM   4816 C  C     . ARG B 1 326 ? -43.845 4.443   -47.311 1.00 22.56  ? 306 ARG B C     1 
ATOM   4817 O  O     . ARG B 1 326 ? -45.075 4.320   -47.213 1.00 20.25  ? 306 ARG B O     1 
ATOM   4818 C  CB    . ARG B 1 326 ? -42.310 2.487   -46.958 1.00 21.48  ? 306 ARG B CB    1 
ATOM   4819 C  CG    . ARG B 1 326 ? -43.236 1.592   -46.161 1.00 30.87  ? 306 ARG B CG    1 
ATOM   4820 C  CD    . ARG B 1 326 ? -43.985 0.622   -47.052 1.00 39.38  ? 306 ARG B CD    1 
ATOM   4821 N  NE    . ARG B 1 326 ? -44.664 -0.390  -46.256 1.00 50.89  ? 306 ARG B NE    1 
ATOM   4822 C  CZ    . ARG B 1 326 ? -44.228 -1.634  -46.116 1.00 53.01  ? 306 ARG B CZ    1 
ATOM   4823 N  NH1   . ARG B 1 326 ? -43.140 -2.058  -46.740 1.00 52.87  ? 306 ARG B NH1   1 
ATOM   4824 N  NH2   . ARG B 1 326 ? -44.901 -2.473  -45.334 1.00 61.39  ? 306 ARG B NH2   1 
ATOM   4825 N  N     . ILE B 1 327 ? -43.196 5.527   -46.873 1.00 20.61  ? 307 ILE B N     1 
ATOM   4826 C  CA    . ILE B 1 327 ? -43.899 6.612   -46.194 1.00 23.75  ? 307 ILE B CA    1 
ATOM   4827 C  C     . ILE B 1 327 ? -44.939 7.254   -47.108 1.00 20.45  ? 307 ILE B C     1 
ATOM   4828 O  O     . ILE B 1 327 ? -45.996 7.699   -46.641 1.00 23.84  ? 307 ILE B O     1 
ATOM   4829 C  CB    . ILE B 1 327 ? -42.872 7.638   -45.671 1.00 21.40  ? 307 ILE B CB    1 
ATOM   4830 C  CG1   . ILE B 1 327 ? -42.121 7.059   -44.470 1.00 20.70  ? 307 ILE B CG1   1 
ATOM   4831 C  CG2   . ILE B 1 327 ? -43.551 8.967   -45.295 1.00 21.01  ? 307 ILE B CG2   1 
ATOM   4832 C  CD1   . ILE B 1 327 ? -40.887 7.859   -44.087 1.00 18.47  ? 307 ILE B CD1   1 
ATOM   4833 N  N     . THR B 1 328 ? -44.670 7.316   -48.412 1.00 20.77  ? 308 THR B N     1 
ATOM   4834 C  CA    . THR B 1 328 ? -45.612 7.898   -49.357 1.00 21.30  ? 308 THR B CA    1 
ATOM   4835 C  C     . THR B 1 328 ? -46.511 6.848   -49.992 1.00 21.35  ? 308 THR B C     1 
ATOM   4836 O  O     . THR B 1 328 ? -47.214 7.156   -50.963 1.00 22.12  ? 308 THR B O     1 
ATOM   4837 C  CB    . THR B 1 328 ? -44.876 8.684   -50.453 1.00 24.98  ? 308 THR B CB    1 
ATOM   4838 O  OG1   . THR B 1 328 ? -44.066 7.803   -51.245 1.00 21.70  ? 308 THR B OG1   1 
ATOM   4839 C  CG2   . THR B 1 328 ? -43.995 9.778   -49.851 1.00 24.01  ? 308 THR B CG2   1 
ATOM   4840 N  N     . GLY B 1 329 ? -46.501 5.619   -49.473 1.00 22.37  ? 309 GLY B N     1 
ATOM   4841 C  CA    . GLY B 1 329 ? -47.351 4.571   -50.032 1.00 22.57  ? 309 GLY B CA    1 
ATOM   4842 C  C     . GLY B 1 329 ? -47.129 4.288   -51.504 1.00 29.16  ? 309 GLY B C     1 
ATOM   4843 O  O     . GLY B 1 329 ? -48.085 3.958   -52.217 1.00 28.89  ? 309 GLY B O     1 
ATOM   4844 N  N     . GLY B 1 330 ? -45.897 4.435   -51.990 1.00 22.28  ? 310 GLY B N     1 
ATOM   4845 C  CA    . GLY B 1 330 ? -45.566 4.184   -53.377 1.00 22.14  ? 310 GLY B CA    1 
ATOM   4846 C  C     . GLY B 1 330 ? -45.872 5.314   -54.331 1.00 21.28  ? 310 GLY B C     1 
ATOM   4847 O  O     . GLY B 1 330 ? -45.606 5.179   -55.536 1.00 24.99  ? 310 GLY B O     1 
ATOM   4848 N  N     . LYS B 1 331 ? -46.402 6.435   -53.842 1.00 21.72  ? 311 LYS B N     1 
ATOM   4849 C  CA    . LYS B 1 331 ? -46.674 7.550   -54.739 1.00 21.37  ? 311 LYS B CA    1 
ATOM   4850 C  C     . LYS B 1 331 ? -45.383 8.183   -55.227 1.00 24.97  ? 311 LYS B C     1 
ATOM   4851 O  O     . LYS B 1 331 ? -45.321 8.650   -56.367 1.00 25.45  ? 311 LYS B O     1 
ATOM   4852 C  CB    . LYS B 1 331 ? -47.577 8.577   -54.051 1.00 24.92  ? 311 LYS B CB    1 
ATOM   4853 C  CG    . LYS B 1 331 ? -48.987 8.041   -53.830 1.00 30.03  ? 311 LYS B CG    1 
ATOM   4854 C  CD    . LYS B 1 331 ? -49.992 9.143   -53.606 1.00 36.15  ? 311 LYS B CD    1 
ATOM   4855 C  CE    . LYS B 1 331 ? -51.354 8.560   -53.223 1.00 39.14  ? 311 LYS B CE    1 
ATOM   4856 N  NZ    . LYS B 1 331 ? -51.859 7.596   -54.238 1.00 52.46  ? 311 LYS B NZ    1 
ATOM   4857 N  N     . PHE B 1 332 ? -44.349 8.181   -54.394 1.00 20.46  ? 312 PHE B N     1 
ATOM   4858 C  CA    . PHE B 1 332 ? -42.976 8.381   -54.835 1.00 19.34  ? 312 PHE B CA    1 
ATOM   4859 C  C     . PHE B 1 332 ? -42.265 7.036   -54.728 1.00 21.06  ? 312 PHE B C     1 
ATOM   4860 O  O     . PHE B 1 332 ? -42.623 6.201   -53.893 1.00 20.34  ? 312 PHE B O     1 
ATOM   4861 C  CB    . PHE B 1 332 ? -42.245 9.437   -53.985 1.00 19.46  ? 312 PHE B CB    1 
ATOM   4862 C  CG    . PHE B 1 332 ? -42.686 10.864  -54.250 1.00 20.37  ? 312 PHE B CG    1 
ATOM   4863 C  CD1   . PHE B 1 332 ? -43.517 11.178  -55.319 1.00 22.92  ? 312 PHE B CD1   1 
ATOM   4864 C  CD2   . PHE B 1 332 ? -42.272 11.888  -53.413 1.00 22.90  ? 312 PHE B CD2   1 
ATOM   4865 C  CE1   . PHE B 1 332 ? -43.915 12.496  -55.556 1.00 24.41  ? 312 PHE B CE1   1 
ATOM   4866 C  CE2   . PHE B 1 332 ? -42.666 13.209  -53.645 1.00 25.72  ? 312 PHE B CE2   1 
ATOM   4867 C  CZ    . PHE B 1 332 ? -43.486 13.507  -54.721 1.00 20.85  ? 312 PHE B CZ    1 
ATOM   4868 N  N     . LYS B 1 333 ? -41.272 6.815   -55.590 1.00 20.64  ? 313 LYS B N     1 
ATOM   4869 C  CA    . LYS B 1 333 ? -40.664 5.501   -55.742 1.00 20.32  ? 313 LYS B CA    1 
ATOM   4870 C  C     . LYS B 1 333 ? -39.148 5.589   -55.660 1.00 20.55  ? 313 LYS B C     1 
ATOM   4871 O  O     . LYS B 1 333 ? -38.543 6.552   -56.146 1.00 21.49  ? 313 LYS B O     1 
ATOM   4872 C  CB    . LYS B 1 333 ? -41.042 4.877   -57.089 1.00 22.40  ? 313 LYS B CB    1 
ATOM   4873 C  CG    . LYS B 1 333 ? -42.482 4.368   -57.188 1.00 28.38  ? 313 LYS B CG    1 
ATOM   4874 C  CD    . LYS B 1 333 ? -42.788 3.298   -56.159 1.00 41.82  ? 313 LYS B CD    1 
ATOM   4875 C  CE    . LYS B 1 333 ? -43.912 2.391   -56.637 1.00 48.51  ? 313 LYS B CE    1 
ATOM   4876 N  NZ    . LYS B 1 333 ? -44.916 3.147   -57.430 1.00 50.27  ? 313 LYS B NZ    1 
ATOM   4877 N  N     . ALA B 1 334 ? -38.539 4.570   -55.055 1.00 19.48  ? 314 ALA B N     1 
ATOM   4878 C  CA    . ALA B 1 334 ? -37.107 4.339   -55.218 1.00 18.47  ? 314 ALA B CA    1 
ATOM   4879 C  C     . ALA B 1 334 ? -36.882 3.655   -56.560 1.00 21.43  ? 314 ALA B C     1 
ATOM   4880 O  O     . ALA B 1 334 ? -37.561 2.669   -56.877 1.00 22.74  ? 314 ALA B O     1 
ATOM   4881 C  CB    . ALA B 1 334 ? -36.571 3.471   -54.077 1.00 19.33  ? 314 ALA B CB    1 
ATOM   4882 N  N     . VAL B 1 335 ? -35.961 4.180   -57.358 1.00 18.16  ? 315 VAL B N     1 
ATOM   4883 C  CA    . VAL B 1 335 ? -35.787 3.762   -58.750 1.00 19.95  ? 315 VAL B CA    1 
ATOM   4884 C  C     . VAL B 1 335 ? -34.424 3.087   -58.894 1.00 20.77  ? 315 VAL B C     1 
ATOM   4885 O  O     . VAL B 1 335 ? -33.412 3.670   -58.494 1.00 21.51  ? 315 VAL B O     1 
ATOM   4886 C  CB    . VAL B 1 335 ? -35.924 4.949   -59.725 1.00 20.72  ? 315 VAL B CB    1 
ATOM   4887 C  CG1   . VAL B 1 335 ? -35.719 4.494   -61.172 1.00 20.48  ? 315 VAL B CG1   1 
ATOM   4888 C  CG2   . VAL B 1 335 ? -37.308 5.609   -59.560 1.00 20.14  ? 315 VAL B CG2   1 
ATOM   4889 N  N     . PRO B 1 336 ? -34.355 1.889   -59.471 1.00 18.61  ? 316 PRO B N     1 
ATOM   4890 C  CA    . PRO B 1 336 ? -33.081 1.152   -59.540 1.00 20.33  ? 316 PRO B CA    1 
ATOM   4891 C  C     . PRO B 1 336 ? -31.995 1.905   -60.302 1.00 20.41  ? 316 PRO B C     1 
ATOM   4892 O  O     . PRO B 1 336 ? -32.258 2.563   -61.311 1.00 20.05  ? 316 PRO B O     1 
ATOM   4893 C  CB    . PRO B 1 336 ? -33.471 -0.147  -60.261 1.00 23.35  ? 316 PRO B CB    1 
ATOM   4894 C  CG    . PRO B 1 336 ? -34.948 -0.295  -59.995 1.00 25.89  ? 316 PRO B CG    1 
ATOM   4895 C  CD    . PRO B 1 336 ? -35.491 1.100   -59.988 1.00 19.84  ? 316 PRO B CD    1 
ATOM   4896 N  N     . HIS B 1 337 ? -30.758 1.796   -59.813 1.00 19.34  ? 317 HIS B N     1 
ATOM   4897 C  CA    . HIS B 1 337 ? -29.653 2.544   -60.406 1.00 19.10  ? 317 HIS B CA    1 
ATOM   4898 C  C     . HIS B 1 337 ? -28.335 1.883   -60.023 1.00 19.13  ? 317 HIS B C     1 
ATOM   4899 O  O     . HIS B 1 337 ? -28.288 0.977   -59.191 1.00 20.54  ? 317 HIS B O     1 
ATOM   4900 C  CB    . HIS B 1 337 ? -29.677 4.010   -59.943 1.00 19.80  ? 317 HIS B CB    1 
ATOM   4901 C  CG    . HIS B 1 337 ? -29.548 4.170   -58.457 1.00 21.56  ? 317 HIS B CG    1 
ATOM   4902 N  ND1   . HIS B 1 337 ? -30.623 4.027   -57.605 1.00 17.80  ? 317 HIS B ND1   1 
ATOM   4903 C  CD2   . HIS B 1 337 ? -28.481 4.461   -57.674 1.00 19.98  ? 317 HIS B CD2   1 
ATOM   4904 C  CE1   . HIS B 1 337 ? -30.220 4.215   -56.358 1.00 17.51  ? 317 HIS B CE1   1 
ATOM   4905 N  NE2   . HIS B 1 337 ? -28.924 4.480   -56.371 1.00 17.87  ? 317 HIS B NE2   1 
ATOM   4906 N  N     . PHE B 1 338 ? -27.258 2.354   -60.650 1.00 18.81  ? 318 PHE B N     1 
ATOM   4907 C  CA    . PHE B 1 338 ? -25.914 1.930   -60.271 1.00 21.23  ? 318 PHE B CA    1 
ATOM   4908 C  C     . PHE B 1 338 ? -24.934 3.006   -60.700 1.00 22.73  ? 318 PHE B C     1 
ATOM   4909 O  O     . PHE B 1 338 ? -25.241 3.843   -61.546 1.00 19.56  ? 318 PHE B O     1 
ATOM   4910 C  CB    . PHE B 1 338 ? -25.543 0.564   -60.873 1.00 24.15  ? 318 PHE B CB    1 
ATOM   4911 C  CG    . PHE B 1 338 ? -25.496 0.539   -62.385 1.00 22.04  ? 318 PHE B CG    1 
ATOM   4912 C  CD1   . PHE B 1 338 ? -24.346 0.903   -63.079 1.00 25.73  ? 318 PHE B CD1   1 
ATOM   4913 C  CD2   . PHE B 1 338 ? -26.596 0.107   -63.109 1.00 25.80  ? 318 PHE B CD2   1 
ATOM   4914 C  CE1   . PHE B 1 338 ? -24.310 0.857   -64.473 1.00 27.35  ? 318 PHE B CE1   1 
ATOM   4915 C  CE2   . PHE B 1 338 ? -26.563 0.061   -64.495 1.00 29.37  ? 318 PHE B CE2   1 
ATOM   4916 C  CZ    . PHE B 1 338 ? -25.421 0.434   -65.175 1.00 27.79  ? 318 PHE B CZ    1 
ATOM   4917 N  N     . VAL B 1 339 ? -23.743 2.980   -60.106 1.00 23.00  ? 319 VAL B N     1 
ATOM   4918 C  CA    . VAL B 1 339 ? -22.696 3.937   -60.436 1.00 21.18  ? 319 VAL B CA    1 
ATOM   4919 C  C     . VAL B 1 339 ? -21.503 3.168   -60.991 1.00 24.38  ? 319 VAL B C     1 
ATOM   4920 O  O     . VAL B 1 339 ? -21.038 2.202   -60.374 1.00 25.30  ? 319 VAL B O     1 
ATOM   4921 C  CB    . VAL B 1 339 ? -22.291 4.780   -59.208 1.00 21.47  ? 319 VAL B CB    1 
ATOM   4922 C  CG1   . VAL B 1 339 ? -21.058 5.625   -59.510 1.00 22.56  ? 319 VAL B CG1   1 
ATOM   4923 C  CG2   . VAL B 1 339 ? -23.455 5.668   -58.749 1.00 20.29  ? 319 VAL B CG2   1 
ATOM   4924 N  N     . ARG B 1 340 ? -20.978 3.637   -62.124 1.00 21.64  ? 320 ARG B N     1 
ATOM   4925 C  CA    . ARG B 1 340 ? -19.793 3.080   -62.768 1.00 21.50  ? 320 ARG B CA    1 
ATOM   4926 C  C     . ARG B 1 340 ? -18.586 3.983   -62.558 1.00 26.91  ? 320 ARG B C     1 
ATOM   4927 O  O     . ARG B 1 340 ? -18.683 5.204   -62.699 1.00 23.90  ? 320 ARG B O     1 
ATOM   4928 C  CB    . ARG B 1 340 ? -20.006 2.921   -64.275 1.00 29.04  ? 320 ARG B CB    1 
ATOM   4929 C  CG    . ARG B 1 340 ? -20.585 1.605   -64.715 1.00 46.36  ? 320 ARG B CG    1 
ATOM   4930 C  CD    . ARG B 1 340 ? -20.757 1.607   -66.227 1.00 42.21  ? 320 ARG B CD    1 
ATOM   4931 N  NE    . ARG B 1 340 ? -19.476 1.739   -66.917 1.00 42.01  ? 320 ARG B NE    1 
ATOM   4932 C  CZ    . ARG B 1 340 ? -18.875 0.758   -67.577 1.00 56.35  ? 320 ARG B CZ    1 
ATOM   4933 N  NH1   . ARG B 1 340 ? -19.402 -0.455  -67.645 1.00 58.39  ? 320 ARG B NH1   1 
ATOM   4934 N  NH2   . ARG B 1 340 ? -17.716 0.997   -68.184 1.00 50.71  ? 320 ARG B NH2   1 
ATOM   4935 N  N     . GLY B 1 341 ? -17.448 3.371   -62.231 1.00 27.96  ? 321 GLY B N     1 
ATOM   4936 C  CA    . GLY B 1 341 ? -16.190 4.081   -62.182 1.00 31.67  ? 321 GLY B CA    1 
ATOM   4937 C  C     . GLY B 1 341 ? -15.541 4.184   -63.546 1.00 30.84  ? 321 GLY B C     1 
ATOM   4938 O  O     . GLY B 1 341 ? -16.095 3.780   -64.568 1.00 30.83  ? 321 GLY B O     1 
ATOM   4939 N  N     . ALA B 1 342 ? -14.356 4.796   -63.558 1.00 29.83  ? 322 ALA B N     1 
ATOM   4940 C  CA    . ALA B 1 342 ? -13.565 4.901   -64.772 1.00 33.79  ? 322 ALA B CA    1 
ATOM   4941 C  C     . ALA B 1 342 ? -12.776 3.616   -64.991 1.00 40.78  ? 322 ALA B C     1 
ATOM   4942 O  O     . ALA B 1 342 ? -12.216 3.045   -64.049 1.00 42.10  ? 322 ALA B O     1 
ATOM   4943 C  CB    . ALA B 1 342 ? -12.617 6.098   -64.692 1.00 37.59  ? 322 ALA B CB    1 
ATOM   4944 N  N     . ARG B 1 343 ? -12.707 3.180   -66.243 1.00 39.66  ? 323 ARG B N     1 
ATOM   4945 C  CA    . ARG B 1 343 ? -11.944 1.982   -66.559 1.00 45.61  ? 323 ARG B CA    1 
ATOM   4946 C  C     . ARG B 1 343 ? -10.454 2.227   -66.348 1.00 53.03  ? 323 ARG B C     1 
ATOM   4947 O  O     . ARG B 1 343 ? -9.944  3.323   -66.599 1.00 43.54  ? 323 ARG B O     1 
ATOM   4948 C  CB    . ARG B 1 343 ? -12.235 1.536   -67.991 1.00 41.81  ? 323 ARG B CB    1 
ATOM   4949 C  CG    . ARG B 1 343 ? -13.594 0.862   -68.127 1.00 49.47  ? 323 ARG B CG    1 
ATOM   4950 C  CD    . ARG B 1 343 ? -14.042 0.745   -69.574 1.00 44.75  ? 323 ARG B CD    1 
ATOM   4951 N  NE    . ARG B 1 343 ? -14.373 2.051   -70.132 1.00 41.23  ? 323 ARG B NE    1 
ATOM   4952 C  CZ    . ARG B 1 343 ? -14.716 2.259   -71.394 1.00 47.88  ? 323 ARG B CZ    1 
ATOM   4953 N  NH1   . ARG B 1 343 ? -14.788 1.264   -72.263 1.00 52.17  ? 323 ARG B NH1   1 
ATOM   4954 N  NH2   . ARG B 1 343 ? -14.996 3.496   -71.794 1.00 42.63  ? 323 ARG B NH2   1 
ATOM   4955 N  N     . ALA B 1 344 ? -9.759  1.183   -65.887 1.00 59.40  ? 324 ALA B N     1 
ATOM   4956 C  CA    . ALA B 1 344 ? -8.353  1.315   -65.514 1.00 64.91  ? 324 ALA B CA    1 
ATOM   4957 C  C     . ALA B 1 344 ? -7.510  1.833   -66.673 1.00 65.17  ? 324 ALA B C     1 
ATOM   4958 O  O     . ALA B 1 344 ? -6.550  2.582   -66.460 1.00 60.75  ? 324 ALA B O     1 
ATOM   4959 C  CB    . ALA B 1 344 ? -7.818  -0.026  -65.014 1.00 64.06  ? 324 ALA B CB    1 
ATOM   4960 N  N     . GLU B 1 345 ? -7.845  1.433   -67.907 1.00 51.42  ? 325 GLU B N     1 
ATOM   4961 C  CA    . GLU B 1 345 ? -7.159  1.965   -69.081 1.00 56.99  ? 325 GLU B CA    1 
ATOM   4962 C  C     . GLU B 1 345 ? -7.132  3.487   -69.063 1.00 64.23  ? 325 GLU B C     1 
ATOM   4963 O  O     . GLU B 1 345 ? -6.166  4.102   -69.529 1.00 71.82  ? 325 GLU B O     1 
ATOM   4964 C  CB    . GLU B 1 345 ? -7.829  1.442   -70.355 1.00 62.01  ? 325 GLU B CB    1 
ATOM   4965 C  CG    . GLU B 1 345 ? -7.373  2.111   -71.642 1.00 75.82  ? 325 GLU B CG    1 
ATOM   4966 C  CD    . GLU B 1 345 ? -8.149  1.629   -72.859 1.00 94.36  ? 325 GLU B CD    1 
ATOM   4967 O  OE1   . GLU B 1 345 ? -8.827  0.584   -72.759 1.00 94.15  ? 325 GLU B OE1   1 
ATOM   4968 O  OE2   . GLU B 1 345 ? -8.083  2.294   -73.915 1.00 93.83  ? 325 GLU B OE2   1 
ATOM   4969 N  N     . MET B 1 346 ? -8.176  4.109   -68.520 1.00 55.51  ? 326 MET B N     1 
ATOM   4970 C  CA    . MET B 1 346 ? -8.221  5.556   -68.389 1.00 65.08  ? 326 MET B CA    1 
ATOM   4971 C  C     . MET B 1 346 ? -7.672  6.024   -67.046 1.00 60.68  ? 326 MET B C     1 
ATOM   4972 O  O     . MET B 1 346 ? -7.137  7.136   -66.954 1.00 45.60  ? 326 MET B O     1 
ATOM   4973 C  CB    . MET B 1 346 ? -9.661  6.053   -68.545 1.00 58.50  ? 326 MET B CB    1 
ATOM   4974 C  CG    . MET B 1 346 ? -10.140 6.177   -69.987 1.00 61.05  ? 326 MET B CG    1 
ATOM   4975 S  SD    . MET B 1 346 ? -10.683 4.606   -70.684 1.00 73.89  ? 326 MET B SD    1 
ATOM   4976 C  CE    . MET B 1 346 ? -11.839 5.166   -71.933 1.00 48.71  ? 326 MET B CE    1 
ATOM   4977 N  N     . SER B 1 347 ? -7.801  5.194   -66.003 1.00 54.78  ? 327 SER B N     1 
ATOM   4978 C  CA    . SER B 1 347 ? -7.221  5.516   -64.700 1.00 45.89  ? 327 SER B CA    1 
ATOM   4979 C  C     . SER B 1 347 ? -5.695  5.494   -64.751 1.00 51.70  ? 327 SER B C     1 
ATOM   4980 O  O     . SER B 1 347 ? -5.038  6.304   -64.087 1.00 46.78  ? 327 SER B O     1 
ATOM   4981 C  CB    . SER B 1 347 ? -7.750  4.544   -63.641 1.00 50.04  ? 327 SER B CB    1 
ATOM   4982 O  OG    . SER B 1 347 ? -7.082  4.689   -62.398 1.00 49.23  ? 327 SER B OG    1 
ATOM   4983 N  N     . ALA B 1 348 ? -5.121  4.553   -65.507 1.00 61.33  ? 328 ALA B N     1 
ATOM   4984 C  CA    . ALA B 1 348 ? -3.682  4.506   -65.797 1.00 58.58  ? 328 ALA B CA    1 
ATOM   4985 C  C     . ALA B 1 348 ? -2.825  4.499   -64.532 1.00 57.73  ? 328 ALA B C     1 
ATOM   4986 O  O     . ALA B 1 348 ? -1.714  5.037   -64.517 1.00 63.97  ? 328 ALA B O     1 
ATOM   4987 C  CB    . ALA B 1 348 ? -3.274  5.662   -66.715 1.00 58.78  ? 328 ALA B CB    1 
ATOM   4988 N  N     . GLY B 1 349 ? -3.328  3.891   -63.458 1.00 53.88  ? 329 GLY B N     1 
ATOM   4989 C  CA    . GLY B 1 349 ? -2.586  3.837   -62.212 1.00 44.33  ? 329 GLY B CA    1 
ATOM   4990 C  C     . GLY B 1 349 ? -2.354  5.171   -61.541 1.00 50.36  ? 329 GLY B C     1 
ATOM   4991 O  O     . GLY B 1 349 ? -1.626  5.232   -60.544 1.00 50.47  ? 329 GLY B O     1 
ATOM   4992 N  N     . ARG B 1 350 ? -2.959  6.243   -62.045 1.00 45.57  ? 330 ARG B N     1 
ATOM   4993 C  CA    . ARG B 1 350 ? -2.774  7.574   -61.493 1.00 35.64  ? 330 ARG B CA    1 
ATOM   4994 C  C     . ARG B 1 350 ? -4.070  8.245   -61.069 1.00 26.13  ? 330 ARG B C     1 
ATOM   4995 O  O     . ARG B 1 350 ? -4.031  9.110   -60.198 1.00 25.16  ? 330 ARG B O     1 
ATOM   4996 C  CB    . ARG B 1 350 ? -2.054  8.483   -62.501 1.00 38.45  ? 330 ARG B CB    1 
ATOM   4997 C  CG    . ARG B 1 350 ? -2.747  8.599   -63.838 1.00 45.54  ? 330 ARG B CG    1 
ATOM   4998 C  CD    . ARG B 1 350 ? -2.016  9.571   -64.758 1.00 59.30  ? 330 ARG B CD    1 
ATOM   4999 N  NE    . ARG B 1 350 ? -2.726  9.731   -66.021 1.00 61.66  ? 330 ARG B NE    1 
ATOM   5000 C  CZ    . ARG B 1 350 ? -2.403  9.107   -67.144 1.00 74.40  ? 330 ARG B CZ    1 
ATOM   5001 N  NH1   . ARG B 1 350 ? -1.372  8.279   -67.202 1.00 72.83  ? 330 ARG B NH1   1 
ATOM   5002 N  NH2   . ARG B 1 350 ? -3.138  9.311   -68.235 1.00 85.73  ? 330 ARG B NH2   1 
ATOM   5003 N  N     . ILE B 1 351 ? -5.208  7.884   -61.656 1.00 27.25  ? 331 ILE B N     1 
ATOM   5004 C  CA    . ILE B 1 351 ? -6.448  8.625   -61.448 1.00 25.88  ? 331 ILE B CA    1 
ATOM   5005 C  C     . ILE B 1 351 ? -7.280  7.921   -60.386 1.00 23.72  ? 331 ILE B C     1 
ATOM   5006 O  O     . ILE B 1 351 ? -7.645  6.750   -60.538 1.00 30.66  ? 331 ILE B O     1 
ATOM   5007 C  CB    . ILE B 1 351 ? -7.254  8.761   -62.748 1.00 25.87  ? 331 ILE B CB    1 
ATOM   5008 C  CG1   . ILE B 1 351 ? -6.400  9.371   -63.852 1.00 33.66  ? 331 ILE B CG1   1 
ATOM   5009 C  CG2   . ILE B 1 351 ? -8.495  9.621   -62.484 1.00 29.04  ? 331 ILE B CG2   1 
ATOM   5010 C  CD1   . ILE B 1 351 ? -5.861  10.703  -63.509 1.00 34.60  ? 331 ILE B CD1   1 
ATOM   5011 N  N     . ALA B 1 352 ? -7.586  8.639   -59.316 1.00 21.64  ? 332 ALA B N     1 
ATOM   5012 C  CA    . ALA B 1 352 ? -8.481  8.168   -58.274 1.00 21.90  ? 332 ALA B CA    1 
ATOM   5013 C  C     . ALA B 1 352 ? -9.828  8.857   -58.429 1.00 22.21  ? 332 ALA B C     1 
ATOM   5014 O  O     . ALA B 1 352 ? -9.937  9.906   -59.075 1.00 20.44  ? 332 ALA B O     1 
ATOM   5015 C  CB    . ALA B 1 352 ? -7.904  8.454   -56.880 1.00 21.06  ? 332 ALA B CB    1 
ATOM   5016 N  N     . ARG B 1 353 ? -10.848 8.264   -57.800 1.00 20.03  ? 333 ARG B N     1 
ATOM   5017 C  CA    . ARG B 1 353 ? -12.212 8.799   -57.858 1.00 19.79  ? 333 ARG B CA    1 
ATOM   5018 C  C     . ARG B 1 353 ? -12.770 8.909   -56.450 1.00 19.33  ? 333 ARG B C     1 
ATOM   5019 O  O     . ARG B 1 353 ? -12.757 7.934   -55.703 1.00 20.90  ? 333 ARG B O     1 
ATOM   5020 C  CB    . ARG B 1 353 ? -13.143 7.922   -58.728 1.00 21.00  ? 333 ARG B CB    1 
ATOM   5021 C  CG    . ARG B 1 353 ? -14.633 8.353   -58.677 1.00 22.83  ? 333 ARG B CG    1 
ATOM   5022 C  CD    . ARG B 1 353 ? -15.541 7.471   -59.584 1.00 24.27  ? 333 ARG B CD    1 
ATOM   5023 N  NE    . ARG B 1 353 ? -15.384 6.027   -59.402 1.00 24.90  ? 333 ARG B NE    1 
ATOM   5024 C  CZ    . ARG B 1 353 ? -16.330 5.211   -58.943 1.00 23.59  ? 333 ARG B CZ    1 
ATOM   5025 N  NH1   . ARG B 1 353 ? -17.538 5.653   -58.629 1.00 25.24  ? 333 ARG B NH1   1 
ATOM   5026 N  NH2   . ARG B 1 353 ? -16.059 3.914   -58.807 1.00 28.20  ? 333 ARG B NH2   1 
ATOM   5027 N  N     . ASN B 1 354 ? -13.253 10.091  -56.086 1.00 18.46  ? 334 ASN B N     1 
ATOM   5028 C  CA    . ASN B 1 354 ? -13.792 10.344  -54.753 1.00 17.95  ? 334 ASN B CA    1 
ATOM   5029 C  C     . ASN B 1 354 ? -15.260 10.723  -54.861 1.00 19.28  ? 334 ASN B C     1 
ATOM   5030 O  O     . ASN B 1 354 ? -15.634 11.538  -55.712 1.00 17.85  ? 334 ASN B O     1 
ATOM   5031 C  CB    . ASN B 1 354 ? -13.001 11.448  -54.057 1.00 17.75  ? 334 ASN B CB    1 
ATOM   5032 C  CG    . ASN B 1 354 ? -11.555 11.061  -53.856 1.00 20.05  ? 334 ASN B CG    1 
ATOM   5033 O  OD1   . ASN B 1 354 ? -11.267 9.969   -53.376 1.00 18.96  ? 334 ASN B OD1   1 
ATOM   5034 N  ND2   . ASN B 1 354 ? -10.631 11.942  -54.247 1.00 20.61  ? 334 ASN B ND2   1 
ATOM   5035 N  N     . THR B 1 355 ? -16.091 10.161  -53.973 1.00 17.25  ? 335 THR B N     1 
ATOM   5036 C  CA    . THR B 1 355 ? -17.525 10.459  -54.026 1.00 19.11  ? 335 THR B CA    1 
ATOM   5037 C  C     . THR B 1 355 ? -18.073 10.723  -52.629 1.00 17.22  ? 335 THR B C     1 
ATOM   5038 O  O     . THR B 1 355 ? -17.528 10.262  -51.626 1.00 16.48  ? 335 THR B O     1 
ATOM   5039 C  CB    . THR B 1 355 ? -18.363 9.308   -54.643 1.00 17.84  ? 335 THR B CB    1 
ATOM   5040 O  OG1   . THR B 1 355 ? -18.371 8.172   -53.772 1.00 20.85  ? 335 THR B OG1   1 
ATOM   5041 C  CG2   . THR B 1 355 ? -17.759 8.858   -55.968 1.00 25.11  ? 335 THR B CG2   1 
ATOM   5042 N  N     . LEU B 1 356 ? -19.204 11.435  -52.578 1.00 19.82  ? 336 LEU B N     1 
ATOM   5043 C  CA    . LEU B 1 356 ? -19.924 11.665  -51.325 1.00 16.92  ? 336 LEU B CA    1 
ATOM   5044 C  C     . LEU B 1 356 ? -21.404 11.359  -51.491 1.00 16.92  ? 336 LEU B C     1 
ATOM   5045 O  O     . LEU B 1 356 ? -22.027 11.764  -52.481 1.00 19.54  ? 336 LEU B O     1 
ATOM   5046 C  CB    . LEU B 1 356 ? -19.754 13.102  -50.841 1.00 18.84  ? 336 LEU B CB    1 
ATOM   5047 C  CG    . LEU B 1 356 ? -20.554 13.501  -49.593 1.00 19.00  ? 336 LEU B CG    1 
ATOM   5048 C  CD1   . LEU B 1 356 ? -20.051 12.799  -48.341 1.00 20.75  ? 336 LEU B CD1   1 
ATOM   5049 C  CD2   . LEU B 1 356 ? -20.531 15.021  -49.393 1.00 20.02  ? 336 LEU B CD2   1 
ATOM   5050 N  N     . ALA B 1 357 ? -21.960 10.648  -50.512 1.00 15.75  ? 337 ALA B N     1 
ATOM   5051 C  CA    . ALA B 1 357 ? -23.402 10.433  -50.426 1.00 17.57  ? 337 ALA B CA    1 
ATOM   5052 C  C     . ALA B 1 357 ? -23.854 10.702  -49.001 1.00 16.98  ? 337 ALA B C     1 
ATOM   5053 O  O     . ALA B 1 357 ? -23.172 10.309  -48.058 1.00 17.21  ? 337 ALA B O     1 
ATOM   5054 C  CB    . ALA B 1 357 ? -23.778 9.004   -50.826 1.00 19.47  ? 337 ALA B CB    1 
ATOM   5055 N  N     . VAL B 1 358 ? -25.010 11.343  -48.832 1.00 15.36  ? 338 VAL B N     1 
ATOM   5056 C  CA    . VAL B 1 358 ? -25.579 11.596  -47.502 1.00 15.37  ? 338 VAL B CA    1 
ATOM   5057 C  C     . VAL B 1 358 ? -26.942 10.911  -47.492 1.00 15.93  ? 338 VAL B C     1 
ATOM   5058 O  O     . VAL B 1 358 ? -27.904 11.421  -48.079 1.00 17.72  ? 338 VAL B O     1 
ATOM   5059 C  CB    . VAL B 1 358 ? -25.705 13.095  -47.186 1.00 15.03  ? 338 VAL B CB    1 
ATOM   5060 C  CG1   . VAL B 1 358 ? -26.290 13.297  -45.783 1.00 17.12  ? 338 VAL B CG1   1 
ATOM   5061 C  CG2   . VAL B 1 358 ? -24.340 13.801  -47.275 1.00 16.14  ? 338 VAL B CG2   1 
ATOM   5062 N  N     . PHE B 1 359 ? -27.045 9.761   -46.837 1.00 15.48  ? 339 PHE B N     1 
ATOM   5063 C  CA    . PHE B 1 359 ? -28.297 8.994   -46.777 1.00 15.67  ? 339 PHE B CA    1 
ATOM   5064 C  C     . PHE B 1 359 ? -29.154 9.504   -45.623 1.00 15.62  ? 339 PHE B C     1 
ATOM   5065 O  O     . PHE B 1 359 ? -29.043 9.022   -44.487 1.00 17.00  ? 339 PHE B O     1 
ATOM   5066 C  CB    . PHE B 1 359 ? -27.999 7.502   -46.599 1.00 17.46  ? 339 PHE B CB    1 
ATOM   5067 C  CG    . PHE B 1 359 ? -27.083 6.930   -47.645 1.00 18.21  ? 339 PHE B CG    1 
ATOM   5068 C  CD1   . PHE B 1 359 ? -27.528 6.714   -48.936 1.00 16.16  ? 339 PHE B CD1   1 
ATOM   5069 C  CD2   . PHE B 1 359 ? -25.772 6.596   -47.330 1.00 19.58  ? 339 PHE B CD2   1 
ATOM   5070 C  CE1   . PHE B 1 359 ? -26.685 6.196   -49.911 1.00 17.34  ? 339 PHE B CE1   1 
ATOM   5071 C  CE2   . PHE B 1 359 ? -24.917 6.078   -48.305 1.00 17.92  ? 339 PHE B CE2   1 
ATOM   5072 C  CZ    . PHE B 1 359 ? -25.368 5.877   -49.587 1.00 19.75  ? 339 PHE B CZ    1 
ATOM   5073 N  N     . THR B 1 360 ? -30.029 10.487  -45.898 1.00 16.10  ? 340 THR B N     1 
ATOM   5074 C  CA    . THR B 1 360 ? -30.969 10.899  -44.865 1.00 15.63  ? 340 THR B CA    1 
ATOM   5075 C  C     . THR B 1 360 ? -32.056 9.838   -44.743 1.00 16.72  ? 340 THR B C     1 
ATOM   5076 O  O     . THR B 1 360 ? -32.579 9.332   -45.751 1.00 19.54  ? 340 THR B O     1 
ATOM   5077 C  CB    . THR B 1 360 ? -31.597 12.275  -45.138 1.00 16.76  ? 340 THR B CB    1 
ATOM   5078 O  OG1   . THR B 1 360 ? -32.565 12.217  -46.208 1.00 16.86  ? 340 THR B OG1   1 
ATOM   5079 C  CG2   . THR B 1 360 ? -30.535 13.335  -45.473 1.00 17.26  ? 340 THR B CG2   1 
ATOM   5080 N  N     . GLN B 1 361 ? -32.399 9.520   -43.497 1.00 16.06  ? 341 GLN B N     1 
ATOM   5081 C  CA    . GLN B 1 361 ? -33.287 8.408   -43.192 1.00 17.68  ? 341 GLN B CA    1 
ATOM   5082 C  C     . GLN B 1 361 ? -33.862 8.623   -41.792 1.00 19.89  ? 341 GLN B C     1 
ATOM   5083 O  O     . GLN B 1 361 ? -33.343 9.441   -41.025 1.00 20.12  ? 341 GLN B O     1 
ATOM   5084 C  CB    . GLN B 1 361 ? -32.532 7.067   -43.296 1.00 17.64  ? 341 GLN B CB    1 
ATOM   5085 C  CG    . GLN B 1 361 ? -31.220 7.016   -42.512 1.00 18.24  ? 341 GLN B CG    1 
ATOM   5086 C  CD    . GLN B 1 361 ? -30.265 5.967   -43.050 1.00 19.10  ? 341 GLN B CD    1 
ATOM   5087 O  OE1   . GLN B 1 361 ? -30.577 5.251   -44.012 1.00 19.94  ? 341 GLN B OE1   1 
ATOM   5088 N  NE2   . GLN B 1 361 ? -29.076 5.884   -42.445 1.00 19.24  ? 341 GLN B NE2   1 
ATOM   5089 N  N     . PRO B 1 362 ? -34.934 7.926   -41.436 1.00 18.19  ? 342 PRO B N     1 
ATOM   5090 C  CA    . PRO B 1 362 ? -35.608 8.216   -40.165 1.00 18.02  ? 342 PRO B CA    1 
ATOM   5091 C  C     . PRO B 1 362 ? -34.853 7.683   -38.957 1.00 19.61  ? 342 PRO B C     1 
ATOM   5092 O  O     . PRO B 1 362 ? -34.014 6.793   -39.057 1.00 21.47  ? 342 PRO B O     1 
ATOM   5093 C  CB    . PRO B 1 362 ? -36.960 7.491   -40.307 1.00 19.65  ? 342 PRO B CB    1 
ATOM   5094 C  CG    . PRO B 1 362 ? -37.072 7.125   -41.767 1.00 19.27  ? 342 PRO B CG    1 
ATOM   5095 C  CD    . PRO B 1 362 ? -35.671 6.922   -42.224 1.00 18.56  ? 342 PRO B CD    1 
ATOM   5096 N  N     . ASN B 1 363 ? -35.216 8.215   -37.790 1.00 21.91  ? 343 ASN B N     1 
ATOM   5097 C  CA    . ASN B 1 363 ? -34.819 7.565   -36.546 1.00 20.94  ? 343 ASN B CA    1 
ATOM   5098 C  C     . ASN B 1 363 ? -35.451 6.175   -36.476 1.00 19.48  ? 343 ASN B C     1 
ATOM   5099 O  O     . ASN B 1 363 ? -36.478 5.897   -37.104 1.00 21.61  ? 343 ASN B O     1 
ATOM   5100 C  CB    . ASN B 1 363 ? -35.240 8.409   -35.336 1.00 22.44  ? 343 ASN B CB    1 
ATOM   5101 C  CG    . ASN B 1 363 ? -34.356 9.630   -35.142 1.00 22.77  ? 343 ASN B CG    1 
ATOM   5102 O  OD1   . ASN B 1 363 ? -33.140 9.548   -35.256 1.00 22.21  ? 343 ASN B OD1   1 
ATOM   5103 N  ND2   . ASN B 1 363 ? -34.972 10.777  -34.886 1.00 25.40  ? 343 ASN B ND2   1 
ATOM   5104 N  N     . LEU B 1 364 ? -34.800 5.282   -35.723 1.00 23.00  ? 344 LEU B N     1 
ATOM   5105 C  CA    . LEU B 1 364 ? -35.193 3.875   -35.737 1.00 22.01  ? 344 LEU B CA    1 
ATOM   5106 C  C     . LEU B 1 364 ? -36.624 3.672   -35.253 1.00 21.17  ? 344 LEU B C     1 
ATOM   5107 O  O     . LEU B 1 364 ? -37.297 2.737   -35.694 1.00 22.52  ? 344 LEU B O     1 
ATOM   5108 C  CB    . LEU B 1 364 ? -34.216 3.065   -34.881 1.00 21.62  ? 344 LEU B CB    1 
ATOM   5109 C  CG    . LEU B 1 364 ? -32.779 3.095   -35.420 1.00 23.46  ? 344 LEU B CG    1 
ATOM   5110 C  CD1   . LEU B 1 364 ? -31.822 2.449   -34.450 1.00 27.84  ? 344 LEU B CD1   1 
ATOM   5111 C  CD2   . LEU B 1 364 ? -32.697 2.418   -36.779 1.00 28.51  ? 344 LEU B CD2   1 
ATOM   5112 N  N     . GLY B 1 365 ? -37.107 4.543   -34.365 1.00 23.62  ? 345 GLY B N     1 
ATOM   5113 C  CA    . GLY B 1 365 ? -38.451 4.443   -33.835 1.00 24.07  ? 345 GLY B CA    1 
ATOM   5114 C  C     . GLY B 1 365 ? -39.520 5.141   -34.641 1.00 24.57  ? 345 GLY B C     1 
ATOM   5115 O  O     . GLY B 1 365 ? -40.699 5.020   -34.304 1.00 28.09  ? 345 GLY B O     1 
ATOM   5116 N  N     . ASP B 1 366 ? -39.148 5.884   -35.688 1.00 23.11  ? 346 ASP B N     1 
ATOM   5117 C  CA    . ASP B 1 366 ? -40.133 6.552   -36.537 1.00 21.32  ? 346 ASP B CA    1 
ATOM   5118 C  C     . ASP B 1 366 ? -40.804 5.555   -37.473 1.00 23.54  ? 346 ASP B C     1 
ATOM   5119 O  O     . ASP B 1 366 ? -40.154 4.665   -38.024 1.00 24.64  ? 346 ASP B O     1 
ATOM   5120 C  CB    . ASP B 1 366 ? -39.490 7.663   -37.380 1.00 22.50  ? 346 ASP B CB    1 
ATOM   5121 C  CG    . ASP B 1 366 ? -38.997 8.834   -36.556 1.00 25.86  ? 346 ASP B CG    1 
ATOM   5122 O  OD1   . ASP B 1 366 ? -39.451 9.012   -35.410 1.00 33.51  ? 346 ASP B OD1   1 
ATOM   5123 O  OD2   . ASP B 1 366 ? -38.151 9.591   -37.072 1.00 34.68  ? 346 ASP B OD2   1 
ATOM   5124 N  N     . GLU B 1 367 ? -42.102 5.743   -37.699 1.00 22.26  ? 347 GLU B N     1 
ATOM   5125 C  CA    . GLU B 1 367 ? -42.850 4.845   -38.574 1.00 22.63  ? 347 GLU B CA    1 
ATOM   5126 C  C     . GLU B 1 367 ? -42.533 5.093   -40.047 1.00 27.45  ? 347 GLU B C     1 
ATOM   5127 O  O     . GLU B 1 367 ? -42.381 6.240   -40.483 1.00 27.66  ? 347 GLU B O     1 
ATOM   5128 C  CB    . GLU B 1 367 ? -44.356 5.002   -38.339 1.00 26.24  ? 347 GLU B CB    1 
ATOM   5129 C  CG    . GLU B 1 367 ? -44.789 4.514   -36.970 1.00 30.74  ? 347 GLU B CG    1 
ATOM   5130 C  CD    . GLU B 1 367 ? -46.297 4.473   -36.795 1.00 48.04  ? 347 GLU B CD    1 
ATOM   5131 O  OE1   . GLU B 1 367 ? -47.028 4.934   -37.693 1.00 44.76  ? 347 GLU B OE1   1 
ATOM   5132 O  OE2   . GLU B 1 367 ? -46.746 3.955   -35.753 1.00 46.06  ? 347 GLU B OE2   1 
ATOM   5133 N  N     . VAL B 1 368 ? -42.415 4.005   -40.814 1.00 24.81  ? 348 VAL B N     1 
ATOM   5134 C  CA    . VAL B 1 368 ? -42.325 4.099   -42.263 1.00 27.39  ? 348 VAL B CA    1 
ATOM   5135 C  C     . VAL B 1 368 ? -43.578 3.563   -42.942 1.00 26.19  ? 348 VAL B C     1 
ATOM   5136 O  O     . VAL B 1 368 ? -43.938 4.048   -44.021 1.00 25.93  ? 348 VAL B O     1 
ATOM   5137 C  CB    . VAL B 1 368 ? -41.067 3.391   -42.821 1.00 27.21  ? 348 VAL B CB    1 
ATOM   5138 C  CG1   . VAL B 1 368 ? -39.804 4.031   -42.273 1.00 27.09  ? 348 VAL B CG1   1 
ATOM   5139 C  CG2   . VAL B 1 368 ? -41.098 1.902   -42.517 1.00 32.77  ? 348 VAL B CG2   1 
ATOM   5140 N  N     . ASP B 1 369 ? -44.235 2.569   -42.359 1.00 29.79  ? 349 ASP B N     1 
ATOM   5141 C  CA    . ASP B 1 369 ? -45.538 2.098   -42.807 1.00 37.58  ? 349 ASP B CA    1 
ATOM   5142 C  C     . ASP B 1 369 ? -46.506 2.544   -41.721 1.00 32.60  ? 349 ASP B C     1 
ATOM   5143 O  O     . ASP B 1 369 ? -46.542 1.961   -40.634 1.00 34.82  ? 349 ASP B O     1 
ATOM   5144 C  CB    . ASP B 1 369 ? -45.538 0.585   -43.005 1.00 31.13  ? 349 ASP B CB    1 
ATOM   5145 C  CG    . ASP B 1 369 ? -46.826 0.075   -43.622 1.00 45.24  ? 349 ASP B CG    1 
ATOM   5146 O  OD1   . ASP B 1 369 ? -47.911 0.576   -43.265 1.00 42.18  ? 349 ASP B OD1   1 
ATOM   5147 O  OD2   . ASP B 1 369 ? -46.743 -0.829  -44.475 1.00 40.44  ? 349 ASP B OD2   1 
ATOM   5148 N  N     . MET B 1 370 ? -47.270 3.598   -42.005 1.00 35.49  ? 350 MET B N     1 
ATOM   5149 C  CA    A MET B 1 370 ? -48.157 4.162   -40.999 0.54 35.98  ? 350 MET B CA    1 
ATOM   5150 C  CA    B MET B 1 370 ? -48.164 4.177   -41.012 0.46 36.02  ? 350 MET B CA    1 
ATOM   5151 C  C     . MET B 1 370 ? -49.458 3.393   -40.850 1.00 40.23  ? 350 MET B C     1 
ATOM   5152 O  O     . MET B 1 370 ? -50.176 3.614   -39.870 1.00 52.26  ? 350 MET B O     1 
ATOM   5153 C  CB    A MET B 1 370 ? -48.464 5.618   -41.327 0.54 42.49  ? 350 MET B CB    1 
ATOM   5154 C  CB    B MET B 1 370 ? -48.486 5.633   -41.368 0.46 42.46  ? 350 MET B CB    1 
ATOM   5155 C  CG    A MET B 1 370 ? -47.418 6.573   -40.812 0.54 41.93  ? 350 MET B CG    1 
ATOM   5156 C  CG    B MET B 1 370 ? -47.537 6.659   -40.745 0.46 42.06  ? 350 MET B CG    1 
ATOM   5157 S  SD    A MET B 1 370 ? -47.443 8.077   -41.774 0.54 40.77  ? 350 MET B SD    1 
ATOM   5158 S  SD    B MET B 1 370 ? -45.919 6.766   -41.539 0.46 40.90  ? 350 MET B SD    1 
ATOM   5159 C  CE    A MET B 1 370 ? -46.457 7.600   -43.192 0.54 36.26  ? 350 MET B CE    1 
ATOM   5160 C  CE    B MET B 1 370 ? -46.330 7.693   -43.019 0.46 35.85  ? 350 MET B CE    1 
ATOM   5161 N  N     . GLU B 1 371 ? -49.775 2.501   -41.782 1.00 38.98  ? 351 GLU B N     1 
ATOM   5162 C  CA    . GLU B 1 371 ? -50.971 1.688   -41.611 1.00 47.31  ? 351 GLU B CA    1 
ATOM   5163 C  C     . GLU B 1 371 ? -50.681 0.516   -40.681 1.00 57.21  ? 351 GLU B C     1 
ATOM   5164 O  O     . GLU B 1 371 ? -51.456 0.233   -39.761 1.00 53.88  ? 351 GLU B O     1 
ATOM   5165 C  CB    . GLU B 1 371 ? -51.486 1.211   -42.971 1.00 59.84  ? 351 GLU B CB    1 
ATOM   5166 C  CG    . GLU B 1 371 ? -52.681 0.261   -42.893 1.00 73.33  ? 351 GLU B CG    1 
ATOM   5167 C  CD    . GLU B 1 371 ? -52.786 -0.665  -44.092 1.00 90.28  ? 351 GLU B CD    1 
ATOM   5168 O  OE1   . GLU B 1 371 ? -51.922 -0.580  -44.993 1.00 89.05  ? 351 GLU B OE1   1 
ATOM   5169 O  OE2   . GLU B 1 371 ? -53.753 -1.457  -44.145 1.00 89.79  ? 351 GLU B OE2   1 
ATOM   5170 N  N     . GLN B 1 372 ? -49.556 -0.165  -40.901 1.00 46.13  ? 352 GLN B N     1 
ATOM   5171 C  CA    . GLN B 1 372 ? -49.153 -1.306  -40.091 1.00 44.36  ? 352 GLN B CA    1 
ATOM   5172 C  C     . GLN B 1 372 ? -48.265 -0.918  -38.914 1.00 49.54  ? 352 GLN B C     1 
ATOM   5173 O  O     . GLN B 1 372 ? -47.974 -1.774  -38.071 1.00 42.85  ? 352 GLN B O     1 
ATOM   5174 C  CB    . GLN B 1 372 ? -48.431 -2.319  -40.980 1.00 48.78  ? 352 GLN B CB    1 
ATOM   5175 C  CG    . GLN B 1 372 ? -49.201 -2.617  -42.252 1.00 61.04  ? 352 GLN B CG    1 
ATOM   5176 C  CD    . GLN B 1 372 ? -48.699 -3.841  -42.981 1.00 73.41  ? 352 GLN B CD    1 
ATOM   5177 O  OE1   . GLN B 1 372 ? -48.371 -4.858  -42.365 1.00 68.18  ? 352 GLN B OE1   1 
ATOM   5178 N  NE2   . GLN B 1 372 ? -48.636 -3.752  -44.306 1.00 72.42  ? 352 GLN B NE2   1 
ATOM   5179 N  N     . HIS B 1 373 ? -47.836 0.346   -38.839 1.00 36.80  ? 353 HIS B N     1 
ATOM   5180 C  CA    . HIS B 1 373 ? -47.043 0.865   -37.726 1.00 37.85  ? 353 HIS B CA    1 
ATOM   5181 C  C     . HIS B 1 373 ? -45.673 0.194   -37.655 1.00 39.08  ? 353 HIS B C     1 
ATOM   5182 O  O     . HIS B 1 373 ? -45.133 -0.041  -36.573 1.00 40.16  ? 353 HIS B O     1 
ATOM   5183 C  CB    . HIS B 1 373 ? -47.797 0.732   -36.403 1.00 43.65  ? 353 HIS B CB    1 
ATOM   5184 C  CG    . HIS B 1 373 ? -49.142 1.384   -36.426 1.00 50.53  ? 353 HIS B CG    1 
ATOM   5185 N  ND1   . HIS B 1 373 ? -49.311 2.745   -36.285 1.00 52.00  ? 353 HIS B ND1   1 
ATOM   5186 C  CD2   . HIS B 1 373 ? -50.380 0.869   -36.626 1.00 54.06  ? 353 HIS B CD2   1 
ATOM   5187 C  CE1   . HIS B 1 373 ? -50.598 3.036   -36.367 1.00 53.07  ? 353 HIS B CE1   1 
ATOM   5188 N  NE2   . HIS B 1 373 ? -51.267 1.916   -36.578 1.00 51.37  ? 353 HIS B NE2   1 
ATOM   5189 N  N     . ILE B 1 374 ? -45.099 -0.084  -38.819 1.00 30.80  ? 354 ILE B N     1 
ATOM   5190 C  CA    . ILE B 1 374 ? -43.746 -0.621  -38.896 1.00 25.84  ? 354 ILE B CA    1 
ATOM   5191 C  C     . ILE B 1 374 ? -42.760 0.538   -38.840 1.00 27.24  ? 354 ILE B C     1 
ATOM   5192 O  O     . ILE B 1 374 ? -42.874 1.496   -39.614 1.00 27.95  ? 354 ILE B O     1 
ATOM   5193 C  CB    . ILE B 1 374 ? -43.567 -1.448  -40.178 1.00 31.44  ? 354 ILE B CB    1 
ATOM   5194 C  CG1   . ILE B 1 374 ? -44.527 -2.651  -40.165 1.00 32.21  ? 354 ILE B CG1   1 
ATOM   5195 C  CG2   . ILE B 1 374 ? -42.111 -1.868  -40.354 1.00 27.53  ? 354 ILE B CG2   1 
ATOM   5196 C  CD1   . ILE B 1 374 ? -44.597 -3.382  -41.483 1.00 33.21  ? 354 ILE B CD1   1 
ATOM   5197 N  N     . THR B 1 375 ? -41.797 0.456   -37.922 1.00 23.16  ? 355 THR B N     1 
ATOM   5198 C  CA    . THR B 1 375 ? -40.802 1.508   -37.745 1.00 22.94  ? 355 THR B CA    1 
ATOM   5199 C  C     . THR B 1 375 ? -39.624 1.329   -38.699 1.00 21.79  ? 355 THR B C     1 
ATOM   5200 O  O     . THR B 1 375 ? -39.459 0.292   -39.345 1.00 24.59  ? 355 THR B O     1 
ATOM   5201 C  CB    . THR B 1 375 ? -40.248 1.534   -36.324 1.00 26.91  ? 355 THR B CB    1 
ATOM   5202 O  OG1   . THR B 1 375 ? -39.511 0.325   -36.083 1.00 27.94  ? 355 THR B OG1   1 
ATOM   5203 C  CG2   . THR B 1 375 ? -41.363 1.690   -35.292 1.00 28.45  ? 355 THR B CG2   1 
ATOM   5204 N  N     . PHE B 1 376 ? -38.777 2.359   -38.759 1.00 22.04  ? 356 PHE B N     1 
ATOM   5205 C  CA    . PHE B 1 376 ? -37.605 2.269   -39.624 1.00 24.27  ? 356 PHE B CA    1 
ATOM   5206 C  C     . PHE B 1 376 ? -36.650 1.176   -39.152 1.00 23.36  ? 356 PHE B C     1 
ATOM   5207 O  O     . PHE B 1 376 ? -36.064 0.467   -39.976 1.00 23.91  ? 356 PHE B O     1 
ATOM   5208 C  CB    . PHE B 1 376 ? -36.880 3.617   -39.709 1.00 19.47  ? 356 PHE B CB    1 
ATOM   5209 C  CG    . PHE B 1 376 ? -35.679 3.595   -40.618 1.00 20.78  ? 356 PHE B CG    1 
ATOM   5210 C  CD1   . PHE B 1 376 ? -35.826 3.306   -41.968 1.00 20.99  ? 356 PHE B CD1   1 
ATOM   5211 C  CD2   . PHE B 1 376 ? -34.408 3.873   -40.126 1.00 20.19  ? 356 PHE B CD2   1 
ATOM   5212 C  CE1   . PHE B 1 376 ? -34.718 3.280   -42.812 1.00 20.22  ? 356 PHE B CE1   1 
ATOM   5213 C  CE2   . PHE B 1 376 ? -33.297 3.841   -40.972 1.00 22.70  ? 356 PHE B CE2   1 
ATOM   5214 C  CZ    . PHE B 1 376 ? -33.462 3.556   -42.312 1.00 20.61  ? 356 PHE B CZ    1 
ATOM   5215 N  N     . GLY B 1 377 ? -36.478 1.014   -37.837 1.00 23.21  ? 357 GLY B N     1 
ATOM   5216 C  CA    . GLY B 1 377 ? -35.628 -0.070  -37.355 1.00 24.74  ? 357 GLY B CA    1 
ATOM   5217 C  C     . GLY B 1 377 ? -36.158 -1.440  -37.747 1.00 26.87  ? 357 GLY B C     1 
ATOM   5218 O  O     . GLY B 1 377 ? -35.409 -2.307  -38.222 1.00 28.06  ? 357 GLY B O     1 
ATOM   5219 N  N     . GLU B 1 378 ? -37.466 -1.639  -37.588 1.00 25.34  ? 358 GLU B N     1 
ATOM   5220 C  CA    . GLU B 1 378 ? -38.093 -2.886  -38.013 1.00 26.18  ? 358 GLU B CA    1 
ATOM   5221 C  C     . GLU B 1 378 ? -37.941 -3.080  -39.517 1.00 26.42  ? 358 GLU B C     1 
ATOM   5222 O  O     . GLU B 1 378 ? -37.583 -4.169  -39.981 1.00 26.46  ? 358 GLU B O     1 
ATOM   5223 C  CB    . GLU B 1 378 ? -39.568 -2.875  -37.593 1.00 26.98  ? 358 GLU B CB    1 
ATOM   5224 C  CG    . GLU B 1 378 ? -39.728 -2.903  -36.059 1.00 27.80  ? 358 GLU B CG    1 
ATOM   5225 C  CD    . GLU B 1 378 ? -41.081 -2.411  -35.579 1.00 29.69  ? 358 GLU B CD    1 
ATOM   5226 O  OE1   . GLU B 1 378 ? -41.895 -1.962  -36.407 1.00 28.53  ? 358 GLU B OE1   1 
ATOM   5227 O  OE2   . GLU B 1 378 ? -41.316 -2.447  -34.354 1.00 41.87  ? 358 GLU B OE2   1 
ATOM   5228 N  N     . PHE B 1 379 ? -38.217 -2.024  -40.292 1.00 25.53  ? 359 PHE B N     1 
ATOM   5229 C  CA    . PHE B 1 379 ? -38.089 -2.062  -41.747 1.00 28.63  ? 359 PHE B CA    1 
ATOM   5230 C  C     . PHE B 1 379 ? -36.675 -2.452  -42.163 1.00 31.89  ? 359 PHE B C     1 
ATOM   5231 O  O     . PHE B 1 379 ? -36.485 -3.299  -43.047 1.00 28.01  ? 359 PHE B O     1 
ATOM   5232 C  CB    . PHE B 1 379 ? -38.479 -0.681  -42.291 1.00 25.37  ? 359 PHE B CB    1 
ATOM   5233 C  CG    . PHE B 1 379 ? -38.369 -0.521  -43.782 1.00 28.84  ? 359 PHE B CG    1 
ATOM   5234 C  CD1   . PHE B 1 379 ? -39.303 -1.093  -44.629 1.00 34.27  ? 359 PHE B CD1   1 
ATOM   5235 C  CD2   . PHE B 1 379 ? -37.371 0.273   -44.328 1.00 30.63  ? 359 PHE B CD2   1 
ATOM   5236 C  CE1   . PHE B 1 379 ? -39.218 -0.915  -45.998 1.00 40.03  ? 359 PHE B CE1   1 
ATOM   5237 C  CE2   . PHE B 1 379 ? -37.280 0.463   -45.697 1.00 31.34  ? 359 PHE B CE2   1 
ATOM   5238 C  CZ    . PHE B 1 379 ? -38.207 -0.132  -46.533 1.00 31.31  ? 359 PHE B CZ    1 
ATOM   5239 N  N     . ALA B 1 380 ? -35.671 -1.879  -41.499 1.00 26.53  ? 360 ALA B N     1 
ATOM   5240 C  CA    . ALA B 1 380 ? -34.283 -2.202  -41.809 1.00 31.11  ? 360 ALA B CA    1 
ATOM   5241 C  C     . ALA B 1 380 ? -33.964 -3.648  -41.483 1.00 29.30  ? 360 ALA B C     1 
ATOM   5242 O  O     . ALA B 1 380 ? -33.076 -4.239  -42.111 1.00 34.39  ? 360 ALA B O     1 
ATOM   5243 C  CB    . ALA B 1 380 ? -33.338 -1.279  -41.046 1.00 26.34  ? 360 ALA B CB    1 
ATOM   5244 N  N     . ARG B 1 381 ? -34.650 -4.223  -40.497 1.00 30.48  ? 361 ARG B N     1 
ATOM   5245 C  CA    . ARG B 1 381 ? -34.453 -5.629  -40.157 1.00 30.81  ? 361 ARG B CA    1 
ATOM   5246 C  C     . ARG B 1 381 ? -35.342 -6.591  -40.956 1.00 33.13  ? 361 ARG B C     1 
ATOM   5247 O  O     . ARG B 1 381 ? -35.349 -7.791  -40.662 1.00 32.76  ? 361 ARG B O     1 
ATOM   5248 C  CB    . ARG B 1 381 ? -34.687 -5.837  -38.659 1.00 33.29  ? 361 ARG B CB    1 
ATOM   5249 C  CG    . ARG B 1 381 ? -33.656 -5.153  -37.759 1.00 38.84  ? 361 ARG B CG    1 
ATOM   5250 C  CD    . ARG B 1 381 ? -32.405 -6.001  -37.629 1.00 49.07  ? 361 ARG B CD    1 
ATOM   5251 N  NE    . ARG B 1 381 ? -31.423 -5.423  -36.717 1.00 47.80  ? 361 ARG B NE    1 
ATOM   5252 C  CZ    . ARG B 1 381 ? -30.344 -4.763  -37.108 1.00 40.29  ? 361 ARG B CZ    1 
ATOM   5253 N  NH1   . ARG B 1 381 ? -30.087 -4.563  -38.390 1.00 48.63  ? 361 ARG B NH1   1 
ATOM   5254 N  NH2   . ARG B 1 381 ? -29.499 -4.297  -36.191 1.00 34.89  ? 361 ARG B NH2   1 
ATOM   5255 N  N     . GLY B 1 382 ? -36.090 -6.106  -41.947 1.00 30.71  ? 362 GLY B N     1 
ATOM   5256 C  CA    . GLY B 1 382 ? -36.873 -6.990  -42.793 1.00 29.00  ? 362 GLY B CA    1 
ATOM   5257 C  C     . GLY B 1 382 ? -38.253 -7.332  -42.281 1.00 35.74  ? 362 GLY B C     1 
ATOM   5258 O  O     . GLY B 1 382 ? -38.889 -8.247  -42.819 1.00 32.16  ? 362 GLY B O     1 
ATOM   5259 N  N     . ILE B 1 383 ? -38.722 -6.650  -41.249 1.00 30.23  ? 363 ILE B N     1 
ATOM   5260 C  CA    . ILE B 1 383 ? -40.031 -6.917  -40.661 1.00 26.79  ? 363 ILE B CA    1 
ATOM   5261 C  C     . ILE B 1 383 ? -41.119 -6.356  -41.566 1.00 30.24  ? 363 ILE B C     1 
ATOM   5262 O  O     . ILE B 1 383 ? -41.049 -5.195  -41.987 1.00 33.97  ? 363 ILE B O     1 
ATOM   5263 C  CB    . ILE B 1 383 ? -40.109 -6.315  -39.251 1.00 29.38  ? 363 ILE B CB    1 
ATOM   5264 C  CG1   . ILE B 1 383 ? -39.121 -7.043  -38.331 1.00 33.53  ? 363 ILE B CG1   1 
ATOM   5265 C  CG2   . ILE B 1 383 ? -41.538 -6.389  -38.709 1.00 31.32  ? 363 ILE B CG2   1 
ATOM   5266 C  CD1   . ILE B 1 383 ? -38.995 -6.433  -36.958 1.00 46.06  ? 363 ILE B CD1   1 
ATOM   5267 N  N     . VAL B 1 384 ? -42.126 -7.180  -41.875 1.00 30.08  ? 364 VAL B N     1 
ATOM   5268 C  CA    . VAL B 1 384 ? -43.227 -6.790  -42.752 1.00 30.19  ? 364 VAL B CA    1 
ATOM   5269 C  C     . VAL B 1 384 ? -44.594 -6.923  -42.091 1.00 30.40  ? 364 VAL B C     1 
ATOM   5270 O  O     . VAL B 1 384 ? -45.605 -6.600  -42.723 1.00 37.72  ? 364 VAL B O     1 
ATOM   5271 C  CB    . VAL B 1 384 ? -43.200 -7.575  -44.081 1.00 34.05  ? 364 VAL B CB    1 
ATOM   5272 C  CG1   . VAL B 1 384 ? -41.898 -7.312  -44.836 1.00 35.63  ? 364 VAL B CG1   1 
ATOM   5273 C  CG2   . VAL B 1 384 ? -43.378 -9.061  -43.824 1.00 37.74  ? 364 VAL B CG2   1 
ATOM   5274 N  N     . ALA B 1 385 ? -44.663 -7.374  -40.839 1.00 33.77  ? 365 ALA B N     1 
ATOM   5275 C  CA    . ALA B 1 385 ? -45.936 -7.496  -40.138 1.00 31.31  ? 365 ALA B CA    1 
ATOM   5276 C  C     . ALA B 1 385 ? -45.706 -7.253  -38.655 1.00 37.07  ? 365 ALA B C     1 
ATOM   5277 O  O     . ALA B 1 385 ? -44.630 -7.541  -38.127 1.00 39.51  ? 365 ALA B O     1 
ATOM   5278 C  CB    . ALA B 1 385 ? -46.575 -8.872  -40.356 1.00 33.96  ? 365 ALA B CB    1 
ATOM   5279 N  N     . LYS B 1 386 ? -46.721 -6.712  -37.985 1.00 39.49  ? 366 LYS B N     1 
ATOM   5280 C  CA    . LYS B 1 386 ? -46.553 -6.300  -36.599 1.00 38.11  ? 366 LYS B CA    1 
ATOM   5281 C  C     . LYS B 1 386 ? -47.901 -6.340  -35.889 1.00 35.99  ? 366 LYS B C     1 
ATOM   5282 O  O     . LYS B 1 386 ? -48.929 -6.007  -36.488 1.00 39.46  ? 366 LYS B O     1 
ATOM   5283 C  CB    . LYS B 1 386 ? -45.916 -4.906  -36.539 1.00 42.74  ? 366 LYS B CB    1 
ATOM   5284 C  CG    . LYS B 1 386 ? -45.547 -4.423  -35.156 1.00 50.76  ? 366 LYS B CG    1 
ATOM   5285 C  CD    . LYS B 1 386 ? -44.785 -3.111  -35.257 1.00 38.46  ? 366 LYS B CD    1 
ATOM   5286 C  CE    . LYS B 1 386 ? -44.558 -2.505  -33.896 1.00 45.16  ? 366 LYS B CE    1 
ATOM   5287 N  NZ    . LYS B 1 386 ? -43.727 -1.280  -34.005 1.00 46.99  ? 366 LYS B NZ    1 
ATOM   5288 N  N     . ASN B 1 387 ? -47.896 -6.753  -34.620 1.00 42.02  ? 367 ASN B N     1 
ATOM   5289 C  CA    . ASN B 1 387 ? -49.110 -6.693  -33.819 1.00 37.10  ? 367 ASN B CA    1 
ATOM   5290 C  C     . ASN B 1 387 ? -48.723 -6.540  -32.356 1.00 45.71  ? 367 ASN B C     1 
ATOM   5291 O  O     . ASN B 1 387 ? -47.603 -6.864  -31.950 1.00 45.77  ? 367 ASN B O     1 
ATOM   5292 C  CB    . ASN B 1 387 ? -50.006 -7.938  -33.987 1.00 40.96  ? 367 ASN B CB    1 
ATOM   5293 C  CG    . ASN B 1 387 ? -49.381 -9.217  -33.415 1.00 45.87  ? 367 ASN B CG    1 
ATOM   5294 O  OD1   . ASN B 1 387 ? -48.399 -9.740  -33.939 1.00 39.78  ? 367 ASN B OD1   1 
ATOM   5295 N  ND2   . ASN B 1 387 ? -49.989 -9.744  -32.345 1.00 39.19  ? 367 ASN B ND2   1 
ATOM   5296 N  N     . THR B 1 388 ? -49.658 -6.005  -31.574 1.00 48.79  ? 368 THR B N     1 
ATOM   5297 C  CA    . THR B 1 388 ? -49.466 -5.768  -30.151 1.00 58.09  ? 368 THR B CA    1 
ATOM   5298 C  C     . THR B 1 388 ? -50.366 -6.707  -29.361 1.00 57.83  ? 368 THR B C     1 
ATOM   5299 O  O     . THR B 1 388 ? -51.525 -6.927  -29.728 1.00 60.27  ? 368 THR B O     1 
ATOM   5300 C  CB    . THR B 1 388 ? -49.780 -4.314  -29.769 1.00 70.07  ? 368 THR B CB    1 
ATOM   5301 O  OG1   . THR B 1 388 ? -51.131 -4.001  -30.130 1.00 79.79  ? 368 THR B OG1   1 
ATOM   5302 C  CG2   . THR B 1 388 ? -48.835 -3.345  -30.470 1.00 64.60  ? 368 THR B CG2   1 
ATOM   5303 N  N     . VAL B 1 389 ? -49.824 -7.267  -28.282 1.00 47.57  ? 369 VAL B N     1 
ATOM   5304 C  CA    . VAL B 1 389 ? -50.564 -8.176  -27.422 1.00 50.74  ? 369 VAL B CA    1 
ATOM   5305 C  C     . VAL B 1 389 ? -50.614 -7.581  -26.019 1.00 53.26  ? 369 VAL B C     1 
ATOM   5306 O  O     . VAL B 1 389 ? -49.937 -6.601  -25.708 1.00 53.76  ? 369 VAL B O     1 
ATOM   5307 C  CB    . VAL B 1 389 ? -49.955 -9.594  -27.396 1.00 48.60  ? 369 VAL B CB    1 
ATOM   5308 C  CG1   . VAL B 1 389 ? -50.004 -10.226 -28.785 1.00 44.39  ? 369 VAL B CG1   1 
ATOM   5309 C  CG2   . VAL B 1 389 ? -48.528 -9.559  -26.842 1.00 45.88  ? 369 VAL B CG2   1 
ATOM   5310 N  N     . SER B 1 390 ? -51.431 -8.194  -25.170 1.00 43.00  ? 370 SER B N     1 
ATOM   5311 C  CA    . SER B 1 390 ? -51.572 -7.734  -23.798 1.00 49.13  ? 370 SER B CA    1 
ATOM   5312 C  C     . SER B 1 390 ? -50.747 -8.601  -22.846 1.00 51.02  ? 370 SER B C     1 
ATOM   5313 O  O     . SER B 1 390 ? -50.396 -9.734  -23.163 1.00 40.26  ? 370 SER B O     1 
ATOM   5314 C  CB    . SER B 1 390 ? -53.044 -7.740  -23.385 1.00 49.89  ? 370 SER B CB    1 
ATOM   5315 O  OG    . SER B 1 390 ? -53.193 -7.347  -22.032 1.00 57.44  ? 370 SER B OG    1 
ATOM   5316 O  OXT   . SER B 1 390 ? -50.407 -8.189  -21.736 1.00 60.23  ? 370 SER B OXT   1 
HETATM 5317 MN MN    . MN  C 2 .   ? -1.748  37.547  -23.754 1.00 18.39  ? 401 MN  A MN    1 
HETATM 5318 O  "O5'" . THM D 3 .   ? -0.970  41.535  -16.757 1.00 29.30  ? 402 THM A "O5'" 1 
HETATM 5319 C  "C5'" . THM D 3 .   ? -0.422  41.752  -18.049 1.00 29.72  ? 402 THM A "C5'" 1 
HETATM 5320 C  "C4'" . THM D 3 .   ? -0.737  40.580  -18.951 1.00 22.24  ? 402 THM A "C4'" 1 
HETATM 5321 O  "O4'" . THM D 3 .   ? -0.147  39.392  -18.381 1.00 21.12  ? 402 THM A "O4'" 1 
HETATM 5322 C  "C3'" . THM D 3 .   ? -2.228  40.275  -19.091 1.00 19.23  ? 402 THM A "C3'" 1 
HETATM 5323 O  "O3'" . THM D 3 .   ? -2.752  40.931  -20.248 1.00 25.23  ? 402 THM A "O3'" 1 
HETATM 5324 C  "C2'" . THM D 3 .   ? -2.248  38.762  -19.273 1.00 16.49  ? 402 THM A "C2'" 1 
HETATM 5325 C  "C1'" . THM D 3 .   ? -1.056  38.300  -18.442 1.00 18.46  ? 402 THM A "C1'" 1 
HETATM 5326 N  N1    . THM D 3 .   ? -1.362  37.877  -17.047 1.00 19.12  ? 402 THM A N1    1 
HETATM 5327 C  C2    . THM D 3 .   ? -0.366  37.195  -16.390 1.00 19.78  ? 402 THM A C2    1 
HETATM 5328 O  O2    . THM D 3 .   ? 0.699   36.894  -16.915 1.00 20.05  ? 402 THM A O2    1 
HETATM 5329 N  N3    . THM D 3 .   ? -0.647  36.894  -15.074 1.00 17.76  ? 402 THM A N3    1 
HETATM 5330 C  C4    . THM D 3 .   ? -1.796  37.208  -14.379 1.00 20.45  ? 402 THM A C4    1 
HETATM 5331 O  O4    . THM D 3 .   ? -1.891  36.915  -13.182 1.00 21.40  ? 402 THM A O4    1 
HETATM 5332 C  C5    . THM D 3 .   ? -2.807  37.920  -15.129 1.00 23.66  ? 402 THM A C5    1 
HETATM 5333 C  C5M   . THM D 3 .   ? -4.094  38.286  -14.451 1.00 24.88  ? 402 THM A C5M   1 
HETATM 5334 C  C6    . THM D 3 .   ? -2.546  38.212  -16.422 1.00 19.78  ? 402 THM A C6    1 
HETATM 5335 C  C1    . EDO E 4 .   ? -6.473  31.948  -30.248 1.00 39.65  ? 403 EDO A C1    1 
HETATM 5336 O  O1    . EDO E 4 .   ? -7.667  31.745  -31.016 1.00 41.78  ? 403 EDO A O1    1 
HETATM 5337 C  C2    . EDO E 4 .   ? -6.810  32.022  -28.761 1.00 39.07  ? 403 EDO A C2    1 
HETATM 5338 O  O2    . EDO E 4 .   ? -7.600  33.194  -28.508 1.00 34.31  ? 403 EDO A O2    1 
HETATM 5339 MN MN    . MN  F 2 .   ? -27.477 4.461   -54.650 1.00 18.46  ? 401 MN  B MN    1 
HETATM 5340 CL CL    . CL  G 5 .   ? -23.378 1.885   -48.503 1.00 23.40  ? 402 CL  B CL    1 
HETATM 5341 O  "O5'" . THM H 3 .   ? -28.265 -0.301  -48.030 1.00 33.00  ? 403 THM B "O5'" 1 
HETATM 5342 C  "C5'" . THM H 3 .   ? -28.752 -0.329  -49.365 1.00 29.69  ? 403 THM B "C5'" 1 
HETATM 5343 C  "C4'" . THM H 3 .   ? -28.387 0.948   -50.087 1.00 21.40  ? 403 THM B "C4'" 1 
HETATM 5344 O  "O4'" . THM H 3 .   ? -28.998 2.064   -49.399 1.00 19.13  ? 403 THM B "O4'" 1 
HETATM 5345 C  "C3'" . THM H 3 .   ? -26.889 1.248   -50.118 1.00 20.48  ? 403 THM B "C3'" 1 
HETATM 5346 O  "O3'" . THM H 3 .   ? -26.342 0.772   -51.349 1.00 24.15  ? 403 THM B "O3'" 1 
HETATM 5347 C  "C2'" . THM H 3 .   ? -26.854 2.768   -50.101 1.00 19.67  ? 403 THM B "C2'" 1 
HETATM 5348 C  "C1'" . THM H 3 .   ? -28.075 3.139   -49.269 1.00 19.57  ? 403 THM B "C1'" 1 
HETATM 5349 N  N1    . THM H 3 .   ? -27.811 3.350   -47.823 1.00 17.85  ? 403 THM B N1    1 
HETATM 5350 C  C2    . THM H 3 .   ? -28.789 3.998   -47.100 1.00 20.58  ? 403 THM B C2    1 
HETATM 5351 O  O2    . THM H 3 .   ? -29.826 4.402   -47.608 1.00 19.22  ? 403 THM B O2    1 
HETATM 5352 N  N3    . THM H 3 .   ? -28.522 4.144   -45.764 1.00 19.70  ? 403 THM B N3    1 
HETATM 5353 C  C4    . THM H 3 .   ? -27.399 3.706   -45.087 1.00 21.47  ? 403 THM B C4    1 
HETATM 5354 O  O4    . THM H 3 .   ? -27.315 3.863   -43.864 1.00 22.61  ? 403 THM B O4    1 
HETATM 5355 C  C5    . THM H 3 .   ? -26.404 3.036   -45.899 1.00 21.02  ? 403 THM B C5    1 
HETATM 5356 C  C5M   . THM H 3 .   ? -25.152 2.528   -45.239 1.00 22.91  ? 403 THM B C5M   1 
HETATM 5357 C  C6    . THM H 3 .   ? -26.654 2.901   -47.214 1.00 19.39  ? 403 THM B C6    1 
HETATM 5358 O  O6    . BU3 I 6 .   ? -23.613 8.958   -56.913 1.00 36.37  ? 404 BU3 B O6    1 
HETATM 5359 C  C3    . BU3 I 6 .   ? -23.182 9.979   -57.794 1.00 40.96  ? 404 BU3 B C3    1 
HETATM 5360 C  C4    . BU3 I 6 .   ? -24.276 10.334  -58.783 1.00 43.78  ? 404 BU3 B C4    1 
HETATM 5361 C  C2    . BU3 I 6 .   ? -21.872 9.579   -58.482 1.00 34.15  ? 404 BU3 B C2    1 
HETATM 5362 O  O5    . BU3 I 6 .   ? -20.896 9.246   -57.506 1.00 37.87  ? 404 BU3 B O5    1 
HETATM 5363 C  C1    . BU3 I 6 .   ? -21.374 10.633  -59.461 1.00 33.33  ? 404 BU3 B C1    1 
HETATM 5364 O  O     . HOH J 7 .   ? -29.403 29.643  -11.489 1.00 32.00  ? 501 HOH A O     1 
HETATM 5365 O  O     . HOH J 7 .   ? -0.118  22.464  1.663   1.00 44.76  ? 502 HOH A O     1 
HETATM 5366 O  O     . HOH J 7 .   ? 16.168  31.417  -34.056 1.00 50.51  ? 503 HOH A O     1 
HETATM 5367 O  O     . HOH J 7 .   ? -29.902 31.839  -8.618  1.00 48.74  ? 504 HOH A O     1 
HETATM 5368 O  O     C HOH J 7 .   ? 1.516   38.878  -13.104 0.50 21.30  ? 505 HOH A O     1 
HETATM 5369 O  O     . HOH J 7 .   ? -26.049 20.531  -24.749 1.00 45.34  ? 506 HOH A O     1 
HETATM 5370 O  O     . HOH J 7 .   ? -9.015  39.886  -1.346  1.00 42.61  ? 507 HOH A O     1 
HETATM 5371 O  O     . HOH J 7 .   ? -7.468  44.751  -12.349 1.00 46.73  ? 508 HOH A O     1 
HETATM 5372 O  O     . HOH J 7 .   ? 10.681  38.857  -0.825  1.00 39.97  ? 509 HOH A O     1 
HETATM 5373 O  O     . HOH J 7 .   ? -19.274 40.507  -31.945 1.00 38.95  ? 510 HOH A O     1 
HETATM 5374 O  O     . HOH J 7 .   ? 23.623  33.555  -14.390 1.00 42.29  ? 511 HOH A O     1 
HETATM 5375 O  O     . HOH J 7 .   ? 2.326   45.408  -2.785  1.00 45.83  ? 512 HOH A O     1 
HETATM 5376 O  O     . HOH J 7 .   ? -19.688 33.761  -40.851 1.00 37.03  ? 513 HOH A O     1 
HETATM 5377 O  O     . HOH J 7 .   ? -13.031 39.048  -13.236 1.00 24.81  ? 514 HOH A O     1 
HETATM 5378 O  O     . HOH J 7 .   ? -9.654  24.306  -4.759  1.00 41.32  ? 515 HOH A O     1 
HETATM 5379 O  O     . HOH J 7 .   ? 8.520   16.960  -31.174 1.00 28.47  ? 516 HOH A O     1 
HETATM 5380 O  O     . HOH J 7 .   ? -18.221 44.255  -7.538  1.00 47.89  ? 517 HOH A O     1 
HETATM 5381 O  O     . HOH J 7 .   ? 5.018   39.061  -36.413 1.00 45.14  ? 518 HOH A O     1 
HETATM 5382 O  O     . HOH J 7 .   ? -1.473  15.116  -12.911 1.00 49.05  ? 519 HOH A O     1 
HETATM 5383 O  O     . HOH J 7 .   ? -13.782 31.876  -1.155  1.00 43.56  ? 520 HOH A O     1 
HETATM 5384 O  O     . HOH J 7 .   ? -8.893  12.390  -26.979 1.00 47.59  ? 521 HOH A O     1 
HETATM 5385 O  O     . HOH J 7 .   ? -13.587 16.387  -14.345 1.00 40.10  ? 522 HOH A O     1 
HETATM 5386 O  O     . HOH J 7 .   ? -18.559 40.144  -27.420 1.00 40.18  ? 523 HOH A O     1 
HETATM 5387 O  O     . HOH J 7 .   ? -5.799  36.320  -41.336 1.00 33.12  ? 524 HOH A O     1 
HETATM 5388 O  O     . HOH J 7 .   ? -23.793 34.921  -23.758 1.00 22.00  ? 525 HOH A O     1 
HETATM 5389 O  O     . HOH J 7 .   ? -10.260 30.962  -38.059 1.00 45.49  ? 526 HOH A O     1 
HETATM 5390 O  O     . HOH J 7 .   ? 9.243   21.224  -33.996 1.00 42.39  ? 527 HOH A O     1 
HETATM 5391 O  O     . HOH J 7 .   ? -6.323  37.025  -6.302  1.00 31.42  ? 528 HOH A O     1 
HETATM 5392 O  O     . HOH J 7 .   ? 7.882   35.799  4.284   1.00 42.23  ? 529 HOH A O     1 
HETATM 5393 O  O     . HOH J 7 .   ? -17.238 16.340  -26.313 1.00 39.50  ? 530 HOH A O     1 
HETATM 5394 O  O     . HOH J 7 .   ? -19.013 28.825  -38.758 1.00 38.35  ? 531 HOH A O     1 
HETATM 5395 O  O     . HOH J 7 .   ? -15.969 20.322  -29.900 1.00 37.94  ? 532 HOH A O     1 
HETATM 5396 O  O     . HOH J 7 .   ? 25.226  31.027  -24.531 1.00 40.81  ? 533 HOH A O     1 
HETATM 5397 O  O     . HOH J 7 .   ? 3.065   42.445  -18.938 1.00 30.96  ? 534 HOH A O     1 
HETATM 5398 O  O     . HOH J 7 .   ? 16.895  27.691  -33.106 1.00 40.76  ? 535 HOH A O     1 
HETATM 5399 O  O     . HOH J 7 .   ? 16.941  20.685  -15.074 1.00 42.31  ? 536 HOH A O     1 
HETATM 5400 O  O     . HOH J 7 .   ? 3.685   20.728  -7.056  1.00 37.41  ? 537 HOH A O     1 
HETATM 5401 O  O     . HOH J 7 .   ? -4.766  14.160  -27.754 1.00 43.85  ? 538 HOH A O     1 
HETATM 5402 O  O     . HOH J 7 .   ? 12.416  44.008  -13.251 1.00 50.11  ? 539 HOH A O     1 
HETATM 5403 O  O     . HOH J 7 .   ? 7.226   28.926  -7.267  1.00 39.65  ? 540 HOH A O     1 
HETATM 5404 O  O     . HOH J 7 .   ? -1.606  35.274  -23.721 1.00 19.68  ? 541 HOH A O     1 
HETATM 5405 O  O     . HOH J 7 .   ? 1.455   12.289  -25.259 1.00 44.46  ? 542 HOH A O     1 
HETATM 5406 O  O     . HOH J 7 .   ? 10.428  38.397  -31.960 1.00 34.77  ? 543 HOH A O     1 
HETATM 5407 O  O     . HOH J 7 .   ? -29.047 23.993  -23.943 1.00 29.98  ? 544 HOH A O     1 
HETATM 5408 O  O     . HOH J 7 .   ? -7.290  18.336  -10.328 1.00 34.39  ? 545 HOH A O     1 
HETATM 5409 O  O     . HOH J 7 .   ? -11.788 36.493  -2.876  1.00 28.29  ? 546 HOH A O     1 
HETATM 5410 O  O     . HOH J 7 .   ? 6.249   34.731  3.048   1.00 42.31  ? 547 HOH A O     1 
HETATM 5411 O  O     . HOH J 7 .   ? -8.976  29.548  -31.770 1.00 31.67  ? 548 HOH A O     1 
HETATM 5412 O  O     . HOH J 7 .   ? -30.472 31.534  -26.178 1.00 37.23  ? 549 HOH A O     1 
HETATM 5413 O  O     . HOH J 7 .   ? -3.285  16.328  -29.472 1.00 29.64  ? 550 HOH A O     1 
HETATM 5414 O  O     . HOH J 7 .   ? 9.760   41.861  -24.083 1.00 38.34  ? 551 HOH A O     1 
HETATM 5415 O  O     . HOH J 7 .   ? -13.549 40.741  -19.138 1.00 31.94  ? 552 HOH A O     1 
HETATM 5416 O  O     . HOH J 7 .   ? 24.136  26.864  -16.738 1.00 27.32  ? 553 HOH A O     1 
HETATM 5417 O  O     . HOH J 7 .   ? 25.844  34.374  -17.021 1.00 41.04  ? 554 HOH A O     1 
HETATM 5418 O  O     . HOH J 7 .   ? -2.324  43.570  -20.511 1.00 35.83  ? 555 HOH A O     1 
HETATM 5419 O  O     . HOH J 7 .   ? 16.811  25.647  -9.295  1.00 39.27  ? 556 HOH A O     1 
HETATM 5420 O  O     . HOH J 7 .   ? -23.994 25.948  -30.822 1.00 23.38  ? 557 HOH A O     1 
HETATM 5421 O  O     . HOH J 7 .   ? 2.956   30.324  -1.651  1.00 34.26  ? 558 HOH A O     1 
HETATM 5422 O  O     . HOH J 7 .   ? 14.201  21.459  -15.207 1.00 26.63  ? 559 HOH A O     1 
HETATM 5423 O  O     . HOH J 7 .   ? -18.542 20.611  -33.290 1.00 33.86  ? 560 HOH A O     1 
HETATM 5424 O  O     . HOH J 7 .   ? 18.694  33.378  -27.241 1.00 38.22  ? 561 HOH A O     1 
HETATM 5425 O  O     . HOH J 7 .   ? -13.246 42.104  -16.768 1.00 40.11  ? 562 HOH A O     1 
HETATM 5426 O  O     . HOH J 7 .   ? -1.077  29.283  -37.575 1.00 22.27  ? 563 HOH A O     1 
HETATM 5427 O  O     . HOH J 7 .   ? -27.424 22.039  -22.522 1.00 38.69  ? 564 HOH A O     1 
HETATM 5428 O  O     . HOH J 7 .   ? -2.979  32.308  -4.507  1.00 19.44  ? 565 HOH A O     1 
HETATM 5429 O  O     . HOH J 7 .   ? 0.400   42.478  -10.767 1.00 38.98  ? 566 HOH A O     1 
HETATM 5430 O  O     . HOH J 7 .   ? -18.259 43.564  -40.406 1.00 46.18  ? 567 HOH A O     1 
HETATM 5431 O  O     . HOH J 7 .   ? -8.054  33.254  -40.689 1.00 28.43  ? 568 HOH A O     1 
HETATM 5432 O  O     . HOH J 7 .   ? -25.223 39.975  -39.437 1.00 42.84  ? 569 HOH A O     1 
HETATM 5433 O  O     . HOH J 7 .   ? -32.140 21.912  -21.615 1.00 35.94  ? 570 HOH A O     1 
HETATM 5434 O  O     . HOH J 7 .   ? -11.395 13.592  -24.253 1.00 30.83  ? 571 HOH A O     1 
HETATM 5435 O  O     . HOH J 7 .   ? 19.423  34.421  -15.535 1.00 28.59  ? 572 HOH A O     1 
HETATM 5436 O  O     . HOH J 7 .   ? -8.326  33.882  -6.502  1.00 28.26  ? 573 HOH A O     1 
HETATM 5437 O  O     . HOH J 7 .   ? -25.332 37.519  -17.828 1.00 37.22  ? 574 HOH A O     1 
HETATM 5438 O  O     . HOH J 7 .   ? 21.196  20.309  -18.733 1.00 47.50  ? 575 HOH A O     1 
HETATM 5439 O  O     . HOH J 7 .   ? 0.053   27.664  -35.697 1.00 27.99  ? 576 HOH A O     1 
HETATM 5440 O  O     . HOH J 7 .   ? -8.986  45.389  -38.409 1.00 41.41  ? 577 HOH A O     1 
HETATM 5441 O  O     . HOH J 7 .   ? 13.433  21.794  -10.453 1.00 33.03  ? 578 HOH A O     1 
HETATM 5442 O  O     . HOH J 7 .   ? -3.862  43.552  -26.162 1.00 24.57  ? 579 HOH A O     1 
HETATM 5443 O  O     . HOH J 7 .   ? -26.852 34.443  -25.882 1.00 27.31  ? 580 HOH A O     1 
HETATM 5444 O  O     . HOH J 7 .   ? 20.359  34.867  -7.528  1.00 41.90  ? 581 HOH A O     1 
HETATM 5445 O  O     . HOH J 7 .   ? 8.063   42.637  -31.416 1.00 39.41  ? 582 HOH A O     1 
HETATM 5446 O  O     . HOH J 7 .   ? 5.720   42.311  0.881   1.00 38.84  ? 583 HOH A O     1 
HETATM 5447 O  O     . HOH J 7 .   ? -8.470  41.848  -49.377 1.00 25.47  ? 584 HOH A O     1 
HETATM 5448 O  O     . HOH J 7 .   ? 13.477  33.507  -3.230  1.00 50.99  ? 585 HOH A O     1 
HETATM 5449 O  O     . HOH J 7 .   ? 1.737   26.549  -11.799 1.00 19.94  ? 586 HOH A O     1 
HETATM 5450 O  O     . HOH J 7 .   ? -0.147  26.333  -9.707  1.00 19.88  ? 587 HOH A O     1 
HETATM 5451 O  O     . HOH J 7 .   ? 1.483   34.049  0.685   1.00 31.39  ? 588 HOH A O     1 
HETATM 5452 O  O     . HOH J 7 .   ? -11.089 25.607  -31.925 1.00 23.78  ? 589 HOH A O     1 
HETATM 5453 O  O     . HOH J 7 .   ? 7.929   50.400  -13.910 1.00 45.57  ? 590 HOH A O     1 
HETATM 5454 O  O     . HOH J 7 .   ? -12.100 24.661  -37.545 1.00 34.63  ? 591 HOH A O     1 
HETATM 5455 O  O     . HOH J 7 .   ? -9.470  39.027  -25.370 1.00 34.54  ? 592 HOH A O     1 
HETATM 5456 O  O     . HOH J 7 .   ? 4.053   18.577  -11.322 1.00 41.12  ? 593 HOH A O     1 
HETATM 5457 O  O     . HOH J 7 .   ? 8.492   31.437  -33.667 1.00 22.91  ? 594 HOH A O     1 
HETATM 5458 O  O     . HOH J 7 .   ? -12.880 46.566  -46.757 1.00 42.17  ? 595 HOH A O     1 
HETATM 5459 O  O     . HOH J 7 .   ? -25.709 26.794  -35.345 1.00 36.63  ? 596 HOH A O     1 
HETATM 5460 O  O     . HOH J 7 .   ? 8.782   45.589  -13.404 1.00 34.55  ? 597 HOH A O     1 
HETATM 5461 O  O     . HOH J 7 .   ? -15.371 26.626  -32.418 1.00 19.69  ? 598 HOH A O     1 
HETATM 5462 O  O     . HOH J 7 .   ? 22.755  25.359  -14.819 1.00 32.96  ? 599 HOH A O     1 
HETATM 5463 O  O     . HOH J 7 .   ? -14.251 39.903  -9.734  1.00 21.96  ? 600 HOH A O     1 
HETATM 5464 O  O     . HOH J 7 .   ? -6.065  16.746  -14.772 1.00 28.24  ? 601 HOH A O     1 
HETATM 5465 O  O     . HOH J 7 .   ? 24.667  39.106  -5.826  1.00 48.97  ? 602 HOH A O     1 
HETATM 5466 O  O     . HOH J 7 .   ? -18.629 36.168  -30.974 1.00 28.92  ? 603 HOH A O     1 
HETATM 5467 O  O     . HOH J 7 .   ? 12.071  36.403  -1.322  1.00 37.61  ? 604 HOH A O     1 
HETATM 5468 O  O     . HOH J 7 .   ? 10.970  43.290  -22.021 1.00 59.16  ? 605 HOH A O     1 
HETATM 5469 O  O     . HOH J 7 .   ? -3.435  16.153  -15.199 1.00 41.81  ? 606 HOH A O     1 
HETATM 5470 O  O     . HOH J 7 .   ? 10.678  18.642  -21.269 1.00 27.26  ? 607 HOH A O     1 
HETATM 5471 O  O     . HOH J 7 .   ? -20.018 25.406  -9.536  1.00 29.88  ? 608 HOH A O     1 
HETATM 5472 O  O     . HOH J 7 .   ? -5.999  32.555  -33.568 1.00 25.64  ? 609 HOH A O     1 
HETATM 5473 O  O     . HOH J 7 .   ? 4.333   25.812  -2.943  1.00 32.59  ? 610 HOH A O     1 
HETATM 5474 O  O     . HOH J 7 .   ? 6.341   29.704  -32.930 1.00 21.23  ? 611 HOH A O     1 
HETATM 5475 O  O     . HOH J 7 .   ? -9.714  20.934  -5.051  1.00 35.97  ? 612 HOH A O     1 
HETATM 5476 O  O     . HOH J 7 .   ? -12.610 39.856  -36.091 1.00 22.62  ? 613 HOH A O     1 
HETATM 5477 O  O     . HOH J 7 .   ? -12.275 19.816  -27.531 1.00 20.83  ? 614 HOH A O     1 
HETATM 5478 O  O     . HOH J 7 .   ? 9.861   40.834  -2.459  1.00 39.00  ? 615 HOH A O     1 
HETATM 5479 O  O     . HOH J 7 .   ? -6.866  30.635  -24.957 1.00 23.14  ? 616 HOH A O     1 
HETATM 5480 O  O     . HOH J 7 .   ? -26.670 29.743  -17.450 1.00 23.35  ? 617 HOH A O     1 
HETATM 5481 O  O     . HOH J 7 .   ? -23.407 30.844  -8.484  1.00 37.06  ? 618 HOH A O     1 
HETATM 5482 O  O     . HOH J 7 .   ? 10.001  40.878  -27.716 1.00 37.72  ? 619 HOH A O     1 
HETATM 5483 O  O     . HOH J 7 .   ? 0.431   22.999  -35.158 1.00 30.99  ? 620 HOH A O     1 
HETATM 5484 O  O     . HOH J 7 .   ? -29.474 35.244  -17.936 1.00 43.29  ? 621 HOH A O     1 
HETATM 5485 O  O     . HOH J 7 .   ? 5.182   35.726  -25.947 1.00 23.97  ? 622 HOH A O     1 
HETATM 5486 O  O     . HOH J 7 .   ? 3.494   35.834  -28.465 1.00 20.76  ? 623 HOH A O     1 
HETATM 5487 O  O     . HOH J 7 .   ? 25.035  27.069  -12.367 1.00 31.64  ? 624 HOH A O     1 
HETATM 5488 O  O     . HOH J 7 .   ? -4.534  18.002  0.262   1.00 46.22  ? 625 HOH A O     1 
HETATM 5489 O  O     . HOH J 7 .   ? -12.173 27.768  -37.418 1.00 38.28  ? 626 HOH A O     1 
HETATM 5490 O  O     . HOH J 7 .   ? -20.144 20.381  -29.962 1.00 28.34  ? 627 HOH A O     1 
HETATM 5491 O  O     . HOH J 7 .   ? -3.720  34.239  0.900   1.00 24.72  ? 628 HOH A O     1 
HETATM 5492 O  O     . HOH J 7 .   ? -7.277  23.535  -27.870 1.00 18.70  ? 629 HOH A O     1 
HETATM 5493 O  O     . HOH J 7 .   ? -3.209  34.338  -8.559  1.00 20.01  ? 630 HOH A O     1 
HETATM 5494 O  O     . HOH J 7 .   ? -4.877  39.457  -21.382 1.00 27.83  ? 631 HOH A O     1 
HETATM 5495 O  O     . HOH J 7 .   ? 6.441   31.310  -38.256 1.00 38.09  ? 632 HOH A O     1 
HETATM 5496 O  O     . HOH J 7 .   ? 22.174  37.268  -24.223 1.00 47.52  ? 633 HOH A O     1 
HETATM 5497 O  O     . HOH J 7 .   ? -28.462 27.627  -13.284 1.00 29.46  ? 634 HOH A O     1 
HETATM 5498 O  O     . HOH J 7 .   ? 4.018   37.709  -24.069 1.00 21.68  ? 635 HOH A O     1 
HETATM 5499 O  O     . HOH J 7 .   ? 12.743  32.252  -34.061 1.00 33.92  ? 636 HOH A O     1 
HETATM 5500 O  O     . HOH J 7 .   ? -6.803  40.535  -47.627 1.00 32.33  ? 637 HOH A O     1 
HETATM 5501 O  O     . HOH J 7 .   ? -9.795  19.207  -28.496 1.00 26.14  ? 638 HOH A O     1 
HETATM 5502 O  O     . HOH J 7 .   ? -6.665  38.831  -40.533 1.00 25.42  ? 639 HOH A O     1 
HETATM 5503 O  O     . HOH J 7 .   ? -29.338 29.780  -34.857 1.00 36.88  ? 640 HOH A O     1 
HETATM 5504 O  O     . HOH J 7 .   ? -11.227 32.821  -35.943 1.00 26.99  ? 641 HOH A O     1 
HETATM 5505 O  O     . HOH J 7 .   ? -16.041 36.753  -30.417 1.00 21.78  ? 642 HOH A O     1 
HETATM 5506 O  O     . HOH J 7 .   ? 21.064  21.154  -21.067 1.00 35.14  ? 643 HOH A O     1 
HETATM 5507 O  O     . HOH J 7 .   ? 11.320  15.282  -19.768 1.00 43.55  ? 644 HOH A O     1 
HETATM 5508 O  O     . HOH J 7 .   ? 1.464   19.202  -7.424  1.00 37.71  ? 645 HOH A O     1 
HETATM 5509 O  O     . HOH J 7 .   ? -12.255 32.283  -8.344  1.00 19.57  ? 646 HOH A O     1 
HETATM 5510 O  O     . HOH J 7 .   ? -13.371 31.284  -40.385 1.00 37.10  ? 647 HOH A O     1 
HETATM 5511 O  O     . HOH J 7 .   ? -28.754 28.513  -16.148 1.00 24.10  ? 648 HOH A O     1 
HETATM 5512 O  O     . HOH J 7 .   ? 12.814  26.560  -8.748  1.00 27.37  ? 649 HOH A O     1 
HETATM 5513 O  O     . HOH J 7 .   ? 3.206   45.504  -26.206 1.00 34.09  ? 650 HOH A O     1 
HETATM 5514 O  O     . HOH J 7 .   ? -28.975 35.799  -36.298 1.00 49.87  ? 651 HOH A O     1 
HETATM 5515 O  O     . HOH J 7 .   ? -10.320 27.049  -4.748  1.00 31.05  ? 652 HOH A O     1 
HETATM 5516 O  O     . HOH J 7 .   ? -3.057  38.735  -11.193 1.00 29.97  ? 653 HOH A O     1 
HETATM 5517 O  O     . HOH J 7 .   ? 5.778   18.756  -34.724 1.00 47.69  ? 654 HOH A O     1 
HETATM 5518 O  O     . HOH J 7 .   ? -6.632  27.202  -5.463  1.00 19.86  ? 655 HOH A O     1 
HETATM 5519 O  O     . HOH J 7 .   ? -11.959 14.288  -20.225 1.00 38.97  ? 656 HOH A O     1 
HETATM 5520 O  O     . HOH J 7 .   ? -5.738  39.201  -17.935 1.00 19.73  ? 657 HOH A O     1 
HETATM 5521 O  O     . HOH J 7 .   ? -17.866 43.947  -33.843 1.00 47.76  ? 658 HOH A O     1 
HETATM 5522 O  O     . HOH J 7 .   ? -16.393 29.833  -3.240  1.00 37.14  ? 659 HOH A O     1 
HETATM 5523 O  O     . HOH J 7 .   ? 15.516  20.273  -17.505 1.00 34.76  ? 660 HOH A O     1 
HETATM 5524 O  O     . HOH J 7 .   ? 1.940   45.554  -37.607 1.00 42.14  ? 661 HOH A O     1 
HETATM 5525 O  O     . HOH J 7 .   ? -31.671 27.319  -15.110 1.00 29.22  ? 662 HOH A O     1 
HETATM 5526 O  O     C HOH J 7 .   ? -0.242  40.274  -14.276 0.51 20.87  ? 663 HOH A O     1 
HETATM 5527 O  O     . HOH J 7 .   ? 8.647   29.187  -3.991  1.00 43.61  ? 664 HOH A O     1 
HETATM 5528 O  O     . HOH J 7 .   ? -26.701 38.957  -5.179  1.00 55.11  ? 665 HOH A O     1 
HETATM 5529 O  O     . HOH J 7 .   ? 3.450   33.557  -3.765  1.00 28.29  ? 666 HOH A O     1 
HETATM 5530 O  O     . HOH J 7 .   ? 14.393  32.730  -5.818  1.00 30.99  ? 667 HOH A O     1 
HETATM 5531 O  O     . HOH J 7 .   ? -8.418  41.661  -26.500 1.00 31.47  ? 668 HOH A O     1 
HETATM 5532 O  O     . HOH J 7 .   ? 15.262  41.707  -21.659 1.00 43.32  ? 669 HOH A O     1 
HETATM 5533 O  O     . HOH J 7 .   ? -20.614 41.740  -27.358 1.00 45.80  ? 670 HOH A O     1 
HETATM 5534 O  O     . HOH J 7 .   ? -12.625 29.036  -2.062  1.00 44.47  ? 671 HOH A O     1 
HETATM 5535 O  O     . HOH J 7 .   ? -0.568  17.427  -11.130 1.00 28.40  ? 672 HOH A O     1 
HETATM 5536 O  O     . HOH J 7 .   ? -8.978  33.255  -21.562 1.00 23.07  ? 673 HOH A O     1 
HETATM 5537 O  O     . HOH J 7 .   ? -10.448 47.545  -8.099  1.00 44.47  ? 674 HOH A O     1 
HETATM 5538 O  O     . HOH J 7 .   ? 2.034   44.732  -21.803 1.00 34.23  ? 675 HOH A O     1 
HETATM 5539 O  O     . HOH J 7 .   ? -3.298  34.667  -26.290 1.00 27.15  ? 676 HOH A O     1 
HETATM 5540 O  O     . HOH J 7 .   ? -16.159 32.880  -18.320 1.00 27.72  ? 677 HOH A O     1 
HETATM 5541 O  O     . HOH J 7 .   ? -18.958 18.920  -8.514  1.00 42.92  ? 678 HOH A O     1 
HETATM 5542 O  O     . HOH J 7 .   ? 4.367   17.240  -15.680 1.00 30.12  ? 679 HOH A O     1 
HETATM 5543 O  O     . HOH J 7 .   ? -19.246 38.667  -30.113 1.00 38.18  ? 680 HOH A O     1 
HETATM 5544 O  O     . HOH J 7 .   ? -12.846 33.699  -25.922 1.00 25.84  ? 681 HOH A O     1 
HETATM 5545 O  O     . HOH J 7 .   ? 24.871  26.635  -28.956 1.00 34.83  ? 682 HOH A O     1 
HETATM 5546 O  O     . HOH J 7 .   ? -19.484 43.900  -37.950 1.00 37.84  ? 683 HOH A O     1 
HETATM 5547 O  O     . HOH J 7 .   ? -22.511 17.401  -6.297  1.00 27.38  ? 684 HOH A O     1 
HETATM 5548 O  O     . HOH J 7 .   ? -7.838  32.378  -35.609 1.00 37.72  ? 685 HOH A O     1 
HETATM 5549 O  O     . HOH J 7 .   ? -4.836  29.293  1.987   1.00 29.21  ? 686 HOH A O     1 
HETATM 5550 O  O     . HOH J 7 .   ? -7.560  14.875  -26.274 1.00 30.87  ? 687 HOH A O     1 
HETATM 5551 O  O     . HOH J 7 .   ? 17.921  36.669  -14.250 1.00 26.73  ? 688 HOH A O     1 
HETATM 5552 O  O     . HOH J 7 .   ? -12.424 11.880  -22.066 1.00 43.35  ? 689 HOH A O     1 
HETATM 5553 O  O     . HOH J 7 .   ? 7.032   23.077  -36.188 1.00 32.98  ? 690 HOH A O     1 
HETATM 5554 O  O     . HOH J 7 .   ? -3.773  9.908   -22.670 1.00 49.03  ? 691 HOH A O     1 
HETATM 5555 O  O     . HOH J 7 .   ? -6.392  34.815  -6.674  1.00 39.75  ? 692 HOH A O     1 
HETATM 5556 O  O     . HOH J 7 .   ? 2.215   33.720  -17.761 1.00 25.73  ? 693 HOH A O     1 
HETATM 5557 O  O     . HOH J 7 .   ? -25.260 39.062  -25.543 1.00 38.25  ? 694 HOH A O     1 
HETATM 5558 O  O     . HOH J 7 .   ? -21.106 31.908  -5.183  1.00 44.82  ? 695 HOH A O     1 
HETATM 5559 O  O     . HOH J 7 .   ? 25.003  29.769  -28.443 1.00 37.80  ? 696 HOH A O     1 
HETATM 5560 O  O     . HOH J 7 .   ? -5.742  41.167  -26.447 1.00 22.32  ? 697 HOH A O     1 
HETATM 5561 O  O     . HOH J 7 .   ? 18.396  19.614  -28.824 1.00 40.37  ? 698 HOH A O     1 
HETATM 5562 O  O     . HOH J 7 .   ? -21.649 25.419  -3.693  1.00 42.92  ? 699 HOH A O     1 
HETATM 5563 O  O     . HOH J 7 .   ? -8.278  23.182  -35.459 1.00 27.57  ? 700 HOH A O     1 
HETATM 5564 O  O     . HOH J 7 .   ? -8.724  34.598  -25.897 1.00 20.29  ? 701 HOH A O     1 
HETATM 5565 O  O     . HOH J 7 .   ? 18.901  26.495  -28.844 1.00 37.98  ? 702 HOH A O     1 
HETATM 5566 O  O     . HOH J 7 .   ? 20.687  25.419  -27.141 1.00 38.22  ? 703 HOH A O     1 
HETATM 5567 O  O     . HOH J 7 .   ? -30.472 38.428  -14.193 1.00 43.02  ? 704 HOH A O     1 
HETATM 5568 O  O     . HOH J 7 .   ? -25.170 18.784  -8.550  1.00 32.88  ? 705 HOH A O     1 
HETATM 5569 O  O     . HOH J 7 .   ? -28.452 22.120  -19.890 1.00 38.32  ? 706 HOH A O     1 
HETATM 5570 O  O     . HOH J 7 .   ? -4.712  35.321  -44.635 1.00 42.19  ? 707 HOH A O     1 
HETATM 5571 O  O     . HOH J 7 .   ? -6.966  27.812  1.587   1.00 31.10  ? 708 HOH A O     1 
HETATM 5572 O  O     . HOH J 7 .   ? -10.686 40.414  -48.285 1.00 46.14  ? 709 HOH A O     1 
HETATM 5573 O  O     . HOH J 7 .   ? -29.327 34.372  -20.465 1.00 51.65  ? 710 HOH A O     1 
HETATM 5574 O  O     . HOH J 7 .   ? -11.783 44.446  -39.118 1.00 34.65  ? 711 HOH A O     1 
HETATM 5575 O  O     . HOH J 7 .   ? -18.843 23.299  -8.968  1.00 24.42  ? 712 HOH A O     1 
HETATM 5576 O  O     . HOH J 7 .   ? -8.736  41.012  -22.334 1.00 47.89  ? 713 HOH A O     1 
HETATM 5577 O  O     . HOH J 7 .   ? -30.971 24.422  -21.790 1.00 33.21  ? 714 HOH A O     1 
HETATM 5578 O  O     . HOH J 7 .   ? -1.209  47.086  -23.343 1.00 51.22  ? 715 HOH A O     1 
HETATM 5579 O  O     . HOH J 7 .   ? -2.063  33.776  -45.055 1.00 33.79  ? 716 HOH A O     1 
HETATM 5580 O  O     . HOH J 7 .   ? -7.523  19.438  -7.822  1.00 32.70  ? 717 HOH A O     1 
HETATM 5581 O  O     . HOH J 7 .   ? -4.343  34.791  -22.953 1.00 28.43  ? 718 HOH A O     1 
HETATM 5582 O  O     . HOH J 7 .   ? -23.081 32.734  -6.964  1.00 43.48  ? 719 HOH A O     1 
HETATM 5583 O  O     . HOH J 7 .   ? -20.231 22.041  -19.840 1.00 30.75  ? 720 HOH A O     1 
HETATM 5584 O  O     . HOH J 7 .   ? -1.032  16.860  -19.010 1.00 31.27  ? 721 HOH A O     1 
HETATM 5585 O  O     . HOH J 7 .   ? 4.770   45.309  -20.522 1.00 42.54  ? 722 HOH A O     1 
HETATM 5586 O  O     . HOH J 7 .   ? 14.315  17.757  -14.423 1.00 51.31  ? 723 HOH A O     1 
HETATM 5587 O  O     . HOH J 7 .   ? 14.627  33.461  -32.332 1.00 34.21  ? 724 HOH A O     1 
HETATM 5588 O  O     . HOH J 7 .   ? 12.851  30.207  -5.434  1.00 42.92  ? 725 HOH A O     1 
HETATM 5589 O  O     . HOH J 7 .   ? -14.841 44.927  -40.549 1.00 51.55  ? 726 HOH A O     1 
HETATM 5590 O  O     . HOH J 7 .   ? 11.139  40.978  -19.134 1.00 38.73  ? 727 HOH A O     1 
HETATM 5591 O  O     . HOH J 7 .   ? 26.476  32.869  -20.318 1.00 38.52  ? 728 HOH A O     1 
HETATM 5592 O  O     . HOH J 7 .   ? -10.931 17.973  -9.254  1.00 38.31  ? 729 HOH A O     1 
HETATM 5593 O  O     . HOH J 7 .   ? 11.074  20.543  -9.532  1.00 48.21  ? 730 HOH A O     1 
HETATM 5594 O  O     . HOH J 7 .   ? 13.168  18.291  -21.860 1.00 34.43  ? 731 HOH A O     1 
HETATM 5595 O  O     . HOH J 7 .   ? -7.124  28.986  -33.589 1.00 33.77  ? 732 HOH A O     1 
HETATM 5596 O  O     . HOH J 7 .   ? -22.063 40.791  -15.011 1.00 36.82  ? 733 HOH A O     1 
HETATM 5597 O  O     . HOH J 7 .   ? -6.925  48.421  -44.793 1.00 34.96  ? 734 HOH A O     1 
HETATM 5598 O  O     . HOH J 7 .   ? 22.684  24.579  -10.212 1.00 34.26  ? 735 HOH A O     1 
HETATM 5599 O  O     . HOH J 7 .   ? 19.964  19.159  -23.136 1.00 43.87  ? 736 HOH A O     1 
HETATM 5600 O  O     . HOH J 7 .   ? 1.222   28.323  0.090   1.00 26.88  ? 737 HOH A O     1 
HETATM 5601 O  O     . HOH J 7 .   ? -2.066  15.513  -17.242 1.00 41.83  ? 738 HOH A O     1 
HETATM 5602 O  O     . HOH J 7 .   ? -30.877 38.135  -11.005 1.00 39.01  ? 739 HOH A O     1 
HETATM 5603 O  O     . HOH J 7 .   ? -21.828 17.485  -10.654 1.00 44.90  ? 740 HOH A O     1 
HETATM 5604 O  O     . HOH J 7 .   ? -24.935 24.935  -3.939  1.00 36.77  ? 741 HOH A O     1 
HETATM 5605 O  O     . HOH J 7 .   ? -25.934 36.453  -23.472 1.00 34.02  ? 742 HOH A O     1 
HETATM 5606 O  O     . HOH J 7 .   ? -2.365  15.507  -31.792 1.00 39.36  ? 743 HOH A O     1 
HETATM 5607 O  O     . HOH J 7 .   ? 6.752   33.308  -1.897  1.00 32.73  ? 744 HOH A O     1 
HETATM 5608 O  O     . HOH J 7 .   ? -3.433  37.238  -25.246 1.00 19.34  ? 745 HOH A O     1 
HETATM 5609 O  O     . HOH J 7 .   ? -8.013  37.130  -24.828 1.00 33.74  ? 746 HOH A O     1 
HETATM 5610 O  O     . HOH J 7 .   ? -11.145 23.131  -2.405  1.00 41.77  ? 747 HOH A O     1 
HETATM 5611 O  O     . HOH J 7 .   ? 7.009   9.686   -24.243 1.00 42.58  ? 748 HOH A O     1 
HETATM 5612 O  O     . HOH J 7 .   ? 8.385   13.805  -15.242 1.00 53.99  ? 749 HOH A O     1 
HETATM 5613 O  O     . HOH J 7 .   ? -10.643 32.377  -32.838 1.00 15.93  ? 750 HOH A O     1 
HETATM 5614 O  O     . HOH J 7 .   ? -14.552 43.436  -2.869  1.00 42.61  ? 751 HOH A O     1 
HETATM 5615 O  O     . HOH J 7 .   ? -11.984 30.175  0.823   1.00 45.74  ? 752 HOH A O     1 
HETATM 5616 O  O     . HOH J 7 .   ? -13.804 19.992  -6.413  1.00 44.56  ? 753 HOH A O     1 
HETATM 5617 O  O     . HOH J 7 .   ? -11.686 48.186  -48.656 1.00 38.95  ? 754 HOH A O     1 
HETATM 5618 O  O     . HOH J 7 .   ? -22.349 17.880  -14.088 1.00 55.62  ? 755 HOH A O     1 
HETATM 5619 O  O     . HOH J 7 .   ? -3.334  37.290  -22.207 1.00 19.84  ? 756 HOH A O     1 
HETATM 5620 O  O     . HOH J 7 .   ? 11.143  18.550  -31.247 1.00 30.12  ? 757 HOH A O     1 
HETATM 5621 O  O     . HOH J 7 .   ? -10.031 41.900  -16.928 1.00 41.78  ? 758 HOH A O     1 
HETATM 5622 O  O     . HOH J 7 .   ? -13.128 27.734  -33.904 1.00 30.37  ? 759 HOH A O     1 
HETATM 5623 O  O     . HOH J 7 .   ? -30.304 25.473  -12.691 1.00 39.93  ? 760 HOH A O     1 
HETATM 5624 O  O     . HOH J 7 .   ? -11.814 26.890  -2.820  1.00 38.76  ? 761 HOH A O     1 
HETATM 5625 O  O     . HOH J 7 .   ? 12.741  13.214  -18.904 1.00 51.93  ? 762 HOH A O     1 
HETATM 5626 O  O     . HOH J 7 .   ? 16.017  40.580  -19.714 1.00 48.87  ? 763 HOH A O     1 
HETATM 5627 O  O     . HOH J 7 .   ? 7.693   38.797  7.311   1.00 45.84  ? 764 HOH A O     1 
HETATM 5628 O  O     . HOH J 7 .   ? -6.667  40.399  -22.941 1.00 40.89  ? 765 HOH A O     1 
HETATM 5629 O  O     . HOH J 7 .   ? -15.514 45.224  -43.793 1.00 51.12  ? 766 HOH A O     1 
HETATM 5630 O  O     . HOH J 7 .   ? 1.243   18.817  -36.388 1.00 43.43  ? 767 HOH A O     1 
HETATM 5631 O  O     . HOH J 7 .   ? 21.390  22.765  -28.097 1.00 50.84  ? 768 HOH A O     1 
HETATM 5632 O  O     . HOH J 7 .   ? -31.113 31.474  -34.741 1.00 43.23  ? 769 HOH A O     1 
HETATM 5633 O  O     . HOH J 7 .   ? 9.582   40.763  -30.188 1.00 36.86  ? 770 HOH A O     1 
HETATM 5634 O  O     . HOH J 7 .   ? -18.214 29.353  -41.328 1.00 45.05  ? 771 HOH A O     1 
HETATM 5635 O  O     . HOH J 7 .   ? -10.548 22.605  -35.871 1.00 44.33  ? 772 HOH A O     1 
HETATM 5636 O  O     . HOH J 7 .   ? -6.321  33.549  -25.043 1.00 40.25  ? 773 HOH A O     1 
HETATM 5637 O  O     . HOH J 7 .   ? 26.342  28.523  -10.378 1.00 37.94  ? 774 HOH A O     1 
HETATM 5638 O  O     . HOH J 7 .   ? 11.113  23.672  -6.397  1.00 47.65  ? 775 HOH A O     1 
HETATM 5639 O  O     . HOH J 7 .   ? -10.992 29.365  -33.435 1.00 34.62  ? 776 HOH A O     1 
HETATM 5640 O  O     . HOH J 7 .   ? -2.004  41.247  -12.332 1.00 32.87  ? 777 HOH A O     1 
HETATM 5641 O  O     . HOH J 7 .   ? 1.547   17.129  -9.766  1.00 46.41  ? 778 HOH A O     1 
HETATM 5642 O  O     . HOH J 7 .   ? 2.699   46.694  -23.621 1.00 48.33  ? 779 HOH A O     1 
HETATM 5643 O  O     . HOH J 7 .   ? 7.373   16.789  -33.567 1.00 46.76  ? 780 HOH A O     1 
HETATM 5644 O  O     . HOH J 7 .   ? 10.013  51.834  -14.297 1.00 40.45  ? 781 HOH A O     1 
HETATM 5645 O  O     . HOH J 7 .   ? 21.048  32.975  -13.764 1.00 31.08  ? 782 HOH A O     1 
HETATM 5646 O  O     . HOH J 7 .   ? -0.727  36.343  8.022   1.00 46.67  ? 783 HOH A O     1 
HETATM 5647 O  O     . HOH J 7 .   ? 24.606  34.162  -11.277 1.00 44.97  ? 784 HOH A O     1 
HETATM 5648 O  O     . HOH J 7 .   ? 21.091  35.821  -17.267 1.00 37.36  ? 785 HOH A O     1 
HETATM 5649 O  O     . HOH J 7 .   ? -11.327 41.897  -20.370 1.00 37.67  ? 786 HOH A O     1 
HETATM 5650 O  O     . HOH J 7 .   ? 7.524   42.449  -2.560  1.00 42.54  ? 787 HOH A O     1 
HETATM 5651 O  O     . HOH J 7 .   ? -5.538  25.007  -37.054 1.00 46.38  ? 788 HOH A O     1 
HETATM 5652 O  O     . HOH J 7 .   ? 1.924   44.258  -17.396 1.00 42.79  ? 789 HOH A O     1 
HETATM 5653 O  O     . HOH J 7 .   ? -11.631 48.589  -3.582  1.00 55.61  ? 790 HOH A O     1 
HETATM 5654 O  O     . HOH J 7 .   ? -2.548  25.504  -37.721 1.00 44.23  ? 791 HOH A O     1 
HETATM 5655 O  O     . HOH J 7 .   ? -5.815  38.727  -24.698 1.00 29.53  ? 792 HOH A O     1 
HETATM 5656 O  O     . HOH J 7 .   ? -10.008 17.617  -30.838 1.00 35.78  ? 793 HOH A O     1 
HETATM 5657 O  O     . HOH J 7 .   ? 21.255  30.187  -28.974 1.00 49.82  ? 794 HOH A O     1 
HETATM 5658 O  O     . HOH J 7 .   ? -7.551  20.040  4.777   1.00 50.81  ? 795 HOH A O     1 
HETATM 5659 O  O     . HOH J 7 .   ? -28.794 22.578  -26.257 1.00 39.11  ? 796 HOH A O     1 
HETATM 5660 O  O     . HOH J 7 .   ? 14.184  22.672  -7.939  1.00 49.09  ? 797 HOH A O     1 
HETATM 5661 O  O     . HOH J 7 .   ? -5.162  41.794  -16.734 1.00 50.67  ? 798 HOH A O     1 
HETATM 5662 O  O     . HOH J 7 .   ? -14.165 18.607  -29.105 1.00 32.74  ? 799 HOH A O     1 
HETATM 5663 O  O     . HOH J 7 .   ? 10.067  21.540  -7.385  1.00 45.20  ? 800 HOH A O     1 
HETATM 5664 O  O     . HOH J 7 .   ? -26.370 23.634  -2.057  1.00 37.06  ? 801 HOH A O     1 
HETATM 5665 O  O     . HOH J 7 .   ? 1.513   15.817  -19.252 1.00 35.19  ? 802 HOH A O     1 
HETATM 5666 O  O     . HOH J 7 .   ? -5.713  33.899  2.807   1.00 30.43  ? 803 HOH A O     1 
HETATM 5667 O  O     . HOH J 7 .   ? 8.773   45.550  -16.066 1.00 51.07  ? 804 HOH A O     1 
HETATM 5668 O  O     . HOH J 7 .   ? -6.125  31.270  3.436   1.00 35.10  ? 805 HOH A O     1 
HETATM 5669 O  O     . HOH J 7 .   ? 8.610   31.843  -36.369 1.00 32.84  ? 806 HOH A O     1 
HETATM 5670 O  O     . HOH J 7 .   ? 14.422  16.492  -19.871 1.00 45.98  ? 807 HOH A O     1 
HETATM 5671 O  O     . HOH J 7 .   ? -11.002 23.759  -39.729 1.00 41.88  ? 808 HOH A O     1 
HETATM 5672 O  O     . HOH J 7 .   ? 3.195   33.403  -1.125  1.00 32.47  ? 809 HOH A O     1 
HETATM 5673 O  O     . HOH J 7 .   ? 17.898  18.153  -14.614 1.00 58.50  ? 810 HOH A O     1 
HETATM 5674 O  O     . HOH J 7 .   ? 5.350   22.951  -2.942  1.00 38.93  ? 811 HOH A O     1 
HETATM 5675 O  O     . HOH J 7 .   ? -24.737 24.965  -33.494 1.00 36.39  ? 812 HOH A O     1 
HETATM 5676 O  O     . HOH J 7 .   ? 15.893  17.948  -17.678 1.00 48.23  ? 813 HOH A O     1 
HETATM 5677 O  O     . HOH J 7 .   ? -8.881  36.384  2.370   1.00 48.70  ? 814 HOH A O     1 
HETATM 5678 O  O     . HOH J 7 .   ? 5.766   45.749  -26.113 1.00 49.79  ? 815 HOH A O     1 
HETATM 5679 O  O     . HOH J 7 .   ? 24.347  22.960  -14.545 1.00 57.38  ? 816 HOH A O     1 
HETATM 5680 O  O     . HOH J 7 .   ? -5.503  30.760  5.957   1.00 49.03  ? 817 HOH A O     1 
HETATM 5681 O  O     . HOH J 7 .   ? -5.796  35.868  4.999   1.00 38.45  ? 818 HOH A O     1 
HETATM 5682 O  O     . HOH J 7 .   ? 9.175   43.820  -28.868 1.00 44.22  ? 819 HOH A O     1 
HETATM 5683 O  O     . HOH J 7 .   ? 17.887  29.315  -6.834  1.00 44.63  ? 820 HOH A O     1 
HETATM 5684 O  O     . HOH J 7 .   ? 4.676   37.714  -42.780 1.00 49.87  ? 821 HOH A O     1 
HETATM 5685 O  O     . HOH K 7 .   ? -30.896 29.809  -54.305 1.00 40.78  ? 501 HOH B O     1 
HETATM 5686 O  O     . HOH K 7 .   ? -44.331 -4.700  -45.775 1.00 51.43  ? 502 HOH B O     1 
HETATM 5687 O  O     . HOH K 7 .   ? -22.620 8.411   -54.835 1.00 41.71  ? 503 HOH B O     1 
HETATM 5688 O  O     . HOH K 7 .   ? -36.289 10.845  -37.839 1.00 34.63  ? 504 HOH B O     1 
HETATM 5689 O  O     . HOH K 7 .   ? -46.045 25.120  -55.609 1.00 46.15  ? 505 HOH B O     1 
HETATM 5690 O  O     C HOH K 7 .   ? -30.614 2.054   -43.973 0.70 21.92  ? 506 HOH B O     1 
HETATM 5691 O  O     . HOH K 7 .   ? -4.814  10.422  -35.637 1.00 43.77  ? 507 HOH B O     1 
HETATM 5692 O  O     . HOH K 7 .   ? -39.834 26.251  -47.679 1.00 43.30  ? 508 HOH B O     1 
HETATM 5693 O  O     . HOH K 7 .   ? -37.433 25.732  -59.337 1.00 28.95  ? 509 HOH B O     1 
HETATM 5694 O  O     . HOH K 7 .   ? -19.431 15.318  -35.343 1.00 38.86  ? 510 HOH B O     1 
HETATM 5695 O  O     . HOH K 7 .   ? -53.933 13.669  -41.974 1.00 40.78  ? 511 HOH B O     1 
HETATM 5696 O  O     . HOH K 7 .   ? -31.948 8.803   -28.015 1.00 44.13  ? 512 HOH B O     1 
HETATM 5697 O  O     . HOH K 7 .   ? -17.947 26.701  -42.569 1.00 49.23  ? 513 HOH B O     1 
HETATM 5698 O  O     . HOH K 7 .   ? -22.201 11.155  -54.926 1.00 38.55  ? 514 HOH B O     1 
HETATM 5699 O  O     . HOH K 7 .   ? -20.961 16.440  -63.829 1.00 42.52  ? 515 HOH B O     1 
HETATM 5700 O  O     . HOH K 7 .   ? -5.057  16.073  -59.906 1.00 25.66  ? 516 HOH B O     1 
HETATM 5701 O  O     . HOH K 7 .   ? -32.682 19.518  -36.277 1.00 39.16  ? 517 HOH B O     1 
HETATM 5702 O  O     . HOH K 7 .   ? -34.918 5.022   -68.061 1.00 32.23  ? 518 HOH B O     1 
HETATM 5703 O  O     . HOH K 7 .   ? -24.178 20.542  -27.737 1.00 33.80  ? 519 HOH B O     1 
HETATM 5704 O  O     . HOH K 7 .   ? -25.676 25.565  -58.063 1.00 31.04  ? 520 HOH B O     1 
HETATM 5705 O  O     . HOH K 7 .   ? -21.239 2.912   -78.167 1.00 52.03  ? 521 HOH B O     1 
HETATM 5706 O  O     . HOH K 7 .   ? -39.447 -10.504 -43.924 1.00 32.71  ? 522 HOH B O     1 
HETATM 5707 O  O     . HOH K 7 .   ? -20.374 -0.415  -32.227 1.00 42.05  ? 523 HOH B O     1 
HETATM 5708 O  O     . HOH K 7 .   ? -22.965 3.050   -36.846 1.00 28.30  ? 524 HOH B O     1 
HETATM 5709 O  O     . HOH K 7 .   ? -13.209 21.569  -58.604 1.00 35.80  ? 525 HOH B O     1 
HETATM 5710 O  O     . HOH K 7 .   ? -21.007 6.241   -36.618 1.00 28.26  ? 526 HOH B O     1 
HETATM 5711 O  O     . HOH K 7 .   ? -17.286 27.989  -52.621 1.00 32.10  ? 527 HOH B O     1 
HETATM 5712 O  O     . HOH K 7 .   ? -43.337 19.846  -44.040 1.00 25.01  ? 528 HOH B O     1 
HETATM 5713 O  O     . HOH K 7 .   ? -27.794 14.340  -67.328 1.00 24.16  ? 529 HOH B O     1 
HETATM 5714 O  O     . HOH K 7 .   ? -19.646 4.204   -56.315 1.00 36.15  ? 530 HOH B O     1 
HETATM 5715 O  O     . HOH K 7 .   ? 4.498   30.144  -41.460 1.00 35.51  ? 531 HOH B O     1 
HETATM 5716 O  O     . HOH K 7 .   ? -53.297 14.311  -46.445 1.00 28.47  ? 532 HOH B O     1 
HETATM 5717 O  O     . HOH K 7 .   ? -52.690 7.201   -44.720 1.00 45.46  ? 533 HOH B O     1 
HETATM 5718 O  O     . HOH K 7 .   ? -27.618 6.672   -54.328 1.00 19.50  ? 534 HOH B O     1 
HETATM 5719 O  O     . HOH K 7 .   ? -14.892 -0.202  -48.250 1.00 30.78  ? 535 HOH B O     1 
HETATM 5720 O  O     . HOH K 7 .   ? -16.063 1.693   -43.655 1.00 20.62  ? 536 HOH B O     1 
HETATM 5721 O  O     . HOH K 7 .   ? -27.485 25.730  -41.262 1.00 45.48  ? 537 HOH B O     1 
HETATM 5722 O  O     . HOH K 7 .   ? -42.007 2.695   -60.332 1.00 44.03  ? 538 HOH B O     1 
HETATM 5723 O  O     . HOH K 7 .   ? -16.152 20.408  -35.190 1.00 34.06  ? 539 HOH B O     1 
HETATM 5724 O  O     . HOH K 7 .   ? -4.971  6.627   -53.504 1.00 24.53  ? 540 HOH B O     1 
HETATM 5725 O  O     . HOH K 7 .   ? -23.117 10.647  -63.776 1.00 26.56  ? 541 HOH B O     1 
HETATM 5726 O  O     . HOH K 7 .   ? -32.510 32.463  -51.833 1.00 44.60  ? 542 HOH B O     1 
HETATM 5727 O  O     . HOH K 7 .   ? -16.183 29.378  -50.099 1.00 48.30  ? 543 HOH B O     1 
HETATM 5728 O  O     . HOH K 7 .   ? -16.543 3.113   -67.118 1.00 40.04  ? 544 HOH B O     1 
HETATM 5729 O  O     . HOH K 7 .   ? -44.712 12.228  -64.064 1.00 36.11  ? 545 HOH B O     1 
HETATM 5730 O  O     . HOH K 7 .   ? -42.664 18.903  -39.546 1.00 40.00  ? 546 HOH B O     1 
HETATM 5731 O  O     . HOH K 7 .   ? -48.663 -5.565  -39.372 1.00 53.29  ? 547 HOH B O     1 
HETATM 5732 O  O     . HOH K 7 .   ? -39.938 1.062   -31.753 1.00 44.18  ? 548 HOH B O     1 
HETATM 5733 O  O     . HOH K 7 .   ? -8.470  23.927  -47.555 1.00 46.63  ? 549 HOH B O     1 
HETATM 5734 O  O     . HOH K 7 .   ? -32.234 -0.715  -50.267 1.00 27.19  ? 550 HOH B O     1 
HETATM 5735 O  O     . HOH K 7 .   ? -0.539  13.618  -41.121 1.00 39.67  ? 551 HOH B O     1 
HETATM 5736 O  O     . HOH K 7 .   ? -29.251 1.788   -72.295 1.00 44.40  ? 552 HOH B O     1 
HETATM 5737 O  O     . HOH K 7 .   ? -5.745  -0.231  -56.715 1.00 45.72  ? 553 HOH B O     1 
HETATM 5738 O  O     . HOH K 7 .   ? -41.425 -3.461  -43.966 1.00 47.71  ? 554 HOH B O     1 
HETATM 5739 O  O     . HOH K 7 .   ? -46.002 20.577  -44.342 1.00 39.17  ? 555 HOH B O     1 
HETATM 5740 O  O     . HOH K 7 .   ? -21.376 10.712  -66.013 1.00 34.82  ? 556 HOH B O     1 
HETATM 5741 O  O     . HOH K 7 .   ? 4.034   12.132  -57.970 1.00 40.00  ? 557 HOH B O     1 
HETATM 5742 O  O     . HOH K 7 .   ? -15.142 11.785  -70.231 1.00 47.33  ? 558 HOH B O     1 
HETATM 5743 O  O     . HOH K 7 .   ? -35.656 -2.745  -46.032 1.00 49.13  ? 559 HOH B O     1 
HETATM 5744 O  O     . HOH K 7 .   ? -25.636 5.410   -29.529 1.00 25.88  ? 560 HOH B O     1 
HETATM 5745 O  O     . HOH K 7 .   ? -44.408 0.762   -53.144 1.00 40.56  ? 561 HOH B O     1 
HETATM 5746 O  O     . HOH K 7 .   ? -16.030 8.362   -30.864 1.00 43.54  ? 562 HOH B O     1 
HETATM 5747 O  O     . HOH K 7 .   ? -46.981 21.357  -46.603 1.00 42.48  ? 563 HOH B O     1 
HETATM 5748 O  O     . HOH K 7 .   ? -0.242  17.571  -53.181 1.00 25.60  ? 564 HOH B O     1 
HETATM 5749 O  O     . HOH K 7 .   ? -48.452 6.782   -46.076 1.00 33.88  ? 565 HOH B O     1 
HETATM 5750 O  O     . HOH K 7 .   ? -3.143  21.178  -53.522 1.00 30.23  ? 566 HOH B O     1 
HETATM 5751 O  O     . HOH K 7 .   ? -45.924 15.416  -62.649 1.00 32.04  ? 567 HOH B O     1 
HETATM 5752 O  O     . HOH K 7 .   ? -49.494 5.991   -37.530 1.00 50.57  ? 568 HOH B O     1 
HETATM 5753 O  O     . HOH K 7 .   ? -35.834 4.338   -27.356 1.00 44.56  ? 569 HOH B O     1 
HETATM 5754 O  O     . HOH K 7 .   ? 2.593   13.858  -44.638 1.00 35.72  ? 570 HOH B O     1 
HETATM 5755 O  O     . HOH K 7 .   ? -17.602 3.375   -33.092 1.00 27.69  ? 571 HOH B O     1 
HETATM 5756 O  O     . HOH K 7 .   ? -29.377 16.478  -27.736 1.00 46.65  ? 572 HOH B O     1 
HETATM 5757 O  O     . HOH K 7 .   ? -47.347 9.563   -57.910 1.00 37.16  ? 573 HOH B O     1 
HETATM 5758 O  O     . HOH K 7 .   ? -18.962 22.748  -57.189 1.00 22.19  ? 574 HOH B O     1 
HETATM 5759 O  O     . HOH K 7 .   ? -53.867 1.263   -36.956 1.00 47.32  ? 575 HOH B O     1 
HETATM 5760 O  O     . HOH K 7 .   ? -37.310 0.312   -62.960 1.00 31.68  ? 576 HOH B O     1 
HETATM 5761 O  O     . HOH K 7 .   ? 0.253   5.864   -47.554 1.00 42.99  ? 577 HOH B O     1 
HETATM 5762 O  O     . HOH K 7 .   ? -28.999 15.752  -65.181 1.00 25.13  ? 578 HOH B O     1 
HETATM 5763 O  O     . HOH K 7 .   ? -2.038  7.150   -55.753 1.00 36.59  ? 579 HOH B O     1 
HETATM 5764 O  O     . HOH K 7 .   ? -16.512 21.884  -56.086 1.00 20.61  ? 580 HOH B O     1 
HETATM 5765 O  O     . HOH K 7 .   ? -26.322 7.623   -34.578 1.00 20.71  ? 581 HOH B O     1 
HETATM 5766 O  O     . HOH K 7 .   ? -17.608 14.450  -62.046 1.00 39.16  ? 582 HOH B O     1 
HETATM 5767 O  O     . HOH K 7 .   ? -30.858 14.118  -41.451 1.00 19.19  ? 583 HOH B O     1 
HETATM 5768 O  O     . HOH K 7 .   ? -50.858 21.056  -47.356 1.00 41.38  ? 584 HOH B O     1 
HETATM 5769 O  O     . HOH K 7 .   ? -17.991 17.124  -61.655 1.00 33.37  ? 585 HOH B O     1 
HETATM 5770 O  O     . HOH K 7 .   ? -33.522 13.757  -32.562 1.00 29.29  ? 586 HOH B O     1 
HETATM 5771 O  O     . HOH K 7 .   ? -2.298  27.785  -39.638 1.00 39.31  ? 587 HOH B O     1 
HETATM 5772 O  O     . HOH K 7 .   ? 0.475   12.731  -64.275 1.00 39.35  ? 588 HOH B O     1 
HETATM 5773 O  O     . HOH K 7 .   ? -33.127 4.410   -54.718 1.00 18.25  ? 589 HOH B O     1 
HETATM 5774 O  O     . HOH K 7 .   ? -28.972 14.148  -39.280 1.00 19.12  ? 590 HOH B O     1 
HETATM 5775 O  O     . HOH K 7 .   ? -53.982 10.748  -54.716 1.00 36.57  ? 591 HOH B O     1 
HETATM 5776 O  O     . HOH K 7 .   ? -18.287 10.518  -67.006 1.00 38.24  ? 592 HOH B O     1 
HETATM 5777 O  O     . HOH K 7 .   ? -25.943 7.528   -57.086 1.00 23.66  ? 593 HOH B O     1 
HETATM 5778 O  O     . HOH K 7 .   ? -23.422 -2.786  -60.252 1.00 47.81  ? 594 HOH B O     1 
HETATM 5779 O  O     . HOH K 7 .   ? -14.869 0.592   -40.169 1.00 24.04  ? 595 HOH B O     1 
HETATM 5780 O  O     . HOH K 7 .   ? -32.284 29.814  -61.594 1.00 36.77  ? 596 HOH B O     1 
HETATM 5781 O  O     . HOH K 7 .   ? -30.226 -5.949  -58.612 1.00 45.82  ? 597 HOH B O     1 
HETATM 5782 O  O     . HOH K 7 .   ? -51.856 15.639  -44.352 1.00 34.84  ? 598 HOH B O     1 
HETATM 5783 O  O     . HOH K 7 .   ? -18.827 1.345   -49.237 1.00 30.63  ? 599 HOH B O     1 
HETATM 5784 O  O     . HOH K 7 .   ? -32.674 6.711   -59.116 1.00 20.52  ? 600 HOH B O     1 
HETATM 5785 O  O     . HOH K 7 .   ? -6.764  7.635   -36.982 1.00 39.19  ? 601 HOH B O     1 
HETATM 5786 O  O     . HOH K 7 .   ? -16.970 7.956   -38.345 1.00 20.37  ? 602 HOH B O     1 
HETATM 5787 O  O     . HOH K 7 .   ? -24.485 2.205   -52.792 1.00 26.24  ? 603 HOH B O     1 
HETATM 5788 O  O     . HOH K 7 .   ? -14.347 25.731  -47.187 1.00 46.84  ? 604 HOH B O     1 
HETATM 5789 O  O     . HOH K 7 .   ? -13.560 15.608  -61.582 1.00 25.99  ? 605 HOH B O     1 
HETATM 5790 O  O     . HOH K 7 .   ? -15.287 24.002  -43.046 1.00 41.16  ? 606 HOH B O     1 
HETATM 5791 O  O     . HOH K 7 .   ? -19.950 11.970  -55.383 1.00 31.57  ? 607 HOH B O     1 
HETATM 5792 O  O     . HOH K 7 .   ? -22.261 -6.529  -34.715 1.00 51.29  ? 608 HOH B O     1 
HETATM 5793 O  O     . HOH K 7 .   ? -39.601 4.739   -62.875 1.00 22.41  ? 609 HOH B O     1 
HETATM 5794 O  O     . HOH K 7 .   ? -7.172  -0.070  -41.949 1.00 43.22  ? 610 HOH B O     1 
HETATM 5795 O  O     . HOH K 7 .   ? -1.856  19.259  -51.721 1.00 35.89  ? 611 HOH B O     1 
HETATM 5796 O  O     . HOH K 7 .   ? -3.042  15.596  -64.493 1.00 40.80  ? 612 HOH B O     1 
HETATM 5797 O  O     . HOH K 7 .   ? -26.066 6.051   -38.844 1.00 21.83  ? 613 HOH B O     1 
HETATM 5798 O  O     . HOH K 7 .   ? -40.277 31.692  -55.164 1.00 45.96  ? 614 HOH B O     1 
HETATM 5799 O  O     . HOH K 7 .   ? -29.660 -1.706  -42.213 1.00 36.14  ? 615 HOH B O     1 
HETATM 5800 O  O     C HOH K 7 .   ? -29.004 0.565   -45.496 0.70 24.41  ? 616 HOH B O     1 
HETATM 5801 O  O     . HOH K 7 .   ? -42.003 -0.999  -49.044 1.00 46.92  ? 617 HOH B O     1 
HETATM 5802 O  O     . HOH K 7 .   ? -22.832 24.311  -43.297 1.00 31.52  ? 618 HOH B O     1 
HETATM 5803 O  O     . HOH K 7 .   ? -28.258 18.548  -65.269 1.00 34.74  ? 619 HOH B O     1 
HETATM 5804 O  O     . HOH K 7 .   ? -33.234 21.891  -39.978 1.00 32.56  ? 620 HOH B O     1 
HETATM 5805 O  O     . HOH K 7 .   ? -30.699 5.603   -29.567 1.00 33.10  ? 621 HOH B O     1 
HETATM 5806 O  O     . HOH K 7 .   ? -21.710 18.447  -57.126 1.00 17.91  ? 622 HOH B O     1 
HETATM 5807 O  O     . HOH K 7 .   ? -22.624 12.801  -35.119 1.00 21.68  ? 623 HOH B O     1 
HETATM 5808 O  O     . HOH K 7 .   ? -39.604 23.244  -49.669 1.00 26.65  ? 624 HOH B O     1 
HETATM 5809 O  O     . HOH K 7 .   ? -37.509 11.847  -63.618 1.00 19.58  ? 625 HOH B O     1 
HETATM 5810 O  O     . HOH K 7 .   ? -32.248 9.464   -31.706 1.00 36.06  ? 626 HOH B O     1 
HETATM 5811 O  O     . HOH K 7 .   ? -38.884 0.494   -55.713 1.00 31.48  ? 627 HOH B O     1 
HETATM 5812 O  O     . HOH K 7 .   ? -18.305 2.259   -58.548 1.00 39.02  ? 628 HOH B O     1 
HETATM 5813 O  O     . HOH K 7 .   ? 1.635   10.121  -55.755 1.00 35.65  ? 629 HOH B O     1 
HETATM 5814 O  O     . HOH K 7 .   ? -42.140 9.810   -35.545 1.00 46.19  ? 630 HOH B O     1 
HETATM 5815 O  O     . HOH K 7 .   ? -0.465  20.235  -34.831 1.00 33.63  ? 631 HOH B O     1 
HETATM 5816 O  O     . HOH K 7 .   ? -35.285 13.425  -62.797 1.00 19.55  ? 632 HOH B O     1 
HETATM 5817 O  O     . HOH K 7 .   ? -17.785 16.568  -31.935 1.00 35.46  ? 633 HOH B O     1 
HETATM 5818 O  O     . HOH K 7 .   ? -32.564 -2.844  -57.992 1.00 29.73  ? 634 HOH B O     1 
HETATM 5819 O  O     . HOH K 7 .   ? -42.054 13.939  -38.336 1.00 28.41  ? 635 HOH B O     1 
HETATM 5820 O  O     . HOH K 7 .   ? -39.030 -0.505  -33.430 1.00 35.67  ? 636 HOH B O     1 
HETATM 5821 O  O     . HOH K 7 .   ? -8.258  23.143  -39.126 1.00 45.84  ? 637 HOH B O     1 
HETATM 5822 O  O     . HOH K 7 .   ? -25.428 -1.320  -57.874 1.00 27.35  ? 638 HOH B O     1 
HETATM 5823 O  O     . HOH K 7 .   ? -39.194 1.725   -58.985 1.00 32.05  ? 639 HOH B O     1 
HETATM 5824 O  O     . HOH K 7 .   ? -11.956 25.193  -55.033 1.00 26.62  ? 640 HOH B O     1 
HETATM 5825 O  O     . HOH K 7 .   ? -43.765 9.578   -62.171 1.00 25.55  ? 641 HOH B O     1 
HETATM 5826 O  O     . HOH K 7 .   ? -5.705  23.921  -54.185 1.00 39.02  ? 642 HOH B O     1 
HETATM 5827 O  O     . HOH K 7 .   ? -13.043 -3.228  -35.405 1.00 44.65  ? 643 HOH B O     1 
HETATM 5828 O  O     . HOH K 7 .   ? -20.024 15.659  -32.677 1.00 42.75  ? 644 HOH B O     1 
HETATM 5829 O  O     . HOH K 7 .   ? -27.232 -4.675  -56.130 1.00 42.66  ? 645 HOH B O     1 
HETATM 5830 O  O     . HOH K 7 .   ? -45.860 14.864  -38.769 1.00 39.73  ? 646 HOH B O     1 
HETATM 5831 O  O     . HOH K 7 .   ? -28.654 23.229  -39.724 1.00 24.47  ? 647 HOH B O     1 
HETATM 5832 O  O     . HOH K 7 .   ? -43.194 6.273   -33.785 1.00 48.04  ? 648 HOH B O     1 
HETATM 5833 O  O     . HOH K 7 .   ? -17.266 0.577   -61.747 1.00 44.97  ? 649 HOH B O     1 
HETATM 5834 O  O     . HOH K 7 .   ? 0.043   20.317  -49.988 1.00 42.31  ? 650 HOH B O     1 
HETATM 5835 O  O     . HOH K 7 .   ? -20.132 7.991   -51.468 1.00 18.62  ? 651 HOH B O     1 
HETATM 5836 O  O     . HOH K 7 .   ? -50.032 20.770  -49.835 1.00 39.03  ? 652 HOH B O     1 
HETATM 5837 O  O     . HOH K 7 .   ? -21.848 21.963  -39.076 1.00 31.54  ? 653 HOH B O     1 
HETATM 5838 O  O     . HOH K 7 .   ? -24.636 31.923  -50.966 1.00 48.60  ? 654 HOH B O     1 
HETATM 5839 O  O     . HOH K 7 .   ? -29.374 20.341  -64.143 1.00 35.42  ? 655 HOH B O     1 
HETATM 5840 O  O     . HOH K 7 .   ? -33.612 -9.339  -39.010 1.00 44.26  ? 656 HOH B O     1 
HETATM 5841 O  O     . HOH K 7 .   ? -9.118  15.017  -38.748 1.00 35.33  ? 657 HOH B O     1 
HETATM 5842 O  O     . HOH K 7 .   ? -22.772 5.164   -71.484 1.00 32.81  ? 658 HOH B O     1 
HETATM 5843 O  O     . HOH K 7 .   ? -10.075 17.048  -38.432 1.00 26.80  ? 659 HOH B O     1 
HETATM 5844 O  O     . HOH K 7 .   ? -26.416 -2.006  -52.033 1.00 40.97  ? 660 HOH B O     1 
HETATM 5845 O  O     . HOH K 7 .   ? -30.521 21.192  -36.514 1.00 36.06  ? 661 HOH B O     1 
HETATM 5846 O  O     . HOH K 7 .   ? -55.496 17.803  -52.876 1.00 31.79  ? 662 HOH B O     1 
HETATM 5847 O  O     . HOH K 7 .   ? -35.166 -3.170  -48.355 1.00 47.50  ? 663 HOH B O     1 
HETATM 5848 O  O     . HOH K 7 .   ? -18.790 8.211   -59.160 1.00 32.64  ? 664 HOH B O     1 
HETATM 5849 O  O     . HOH K 7 .   ? -18.817 12.934  -34.521 1.00 29.58  ? 665 HOH B O     1 
HETATM 5850 O  O     . HOH K 7 .   ? -31.303 7.658   -48.182 1.00 25.35  ? 666 HOH B O     1 
HETATM 5851 O  O     . HOH K 7 .   ? -41.240 3.661   -31.825 1.00 42.72  ? 667 HOH B O     1 
HETATM 5852 O  O     . HOH K 7 .   ? -45.570 25.983  -49.601 1.00 41.06  ? 668 HOH B O     1 
HETATM 5853 O  O     . HOH K 7 .   ? -13.058 5.239   -60.916 1.00 28.37  ? 669 HOH B O     1 
HETATM 5854 O  O     . HOH K 7 .   ? -8.096  8.386   -34.490 1.00 41.70  ? 670 HOH B O     1 
HETATM 5855 O  O     . HOH K 7 .   ? -38.450 22.099  -62.876 1.00 42.05  ? 671 HOH B O     1 
HETATM 5856 O  O     . HOH K 7 .   ? -29.865 11.654  -75.100 1.00 30.98  ? 672 HOH B O     1 
HETATM 5857 O  O     . HOH K 7 .   ? -24.873 24.102  -63.746 1.00 50.41  ? 673 HOH B O     1 
HETATM 5858 O  O     . HOH K 7 .   ? -21.045 26.870  -54.622 1.00 28.90  ? 674 HOH B O     1 
HETATM 5859 O  O     . HOH K 7 .   ? -22.033 20.922  -36.516 1.00 29.94  ? 675 HOH B O     1 
HETATM 5860 O  O     . HOH K 7 .   ? 1.434   2.407   -40.629 1.00 50.05  ? 676 HOH B O     1 
HETATM 5861 O  O     . HOH K 7 .   ? -19.129 25.725  -38.641 1.00 26.66  ? 677 HOH B O     1 
HETATM 5862 O  O     . HOH K 7 .   ? -16.952 27.033  -48.324 1.00 35.90  ? 678 HOH B O     1 
HETATM 5863 O  O     . HOH K 7 .   ? -26.980 25.761  -45.402 1.00 36.90  ? 679 HOH B O     1 
HETATM 5864 O  O     . HOH K 7 .   ? -41.959 10.961  -63.960 1.00 28.17  ? 680 HOH B O     1 
HETATM 5865 O  O     . HOH K 7 .   ? -20.552 10.993  -70.884 1.00 49.08  ? 681 HOH B O     1 
HETATM 5866 O  O     . HOH K 7 .   ? -43.403 23.271  -43.452 1.00 47.16  ? 682 HOH B O     1 
HETATM 5867 O  O     . HOH K 7 .   ? -21.876 -3.928  -43.915 1.00 45.82  ? 683 HOH B O     1 
HETATM 5868 O  O     . HOH K 7 .   ? -37.038 28.385  -45.862 1.00 45.03  ? 684 HOH B O     1 
HETATM 5869 O  O     . HOH K 7 .   ? -33.300 23.797  -44.127 1.00 29.32  ? 685 HOH B O     1 
HETATM 5870 O  O     . HOH K 7 .   ? -12.684 9.988   -32.838 1.00 37.24  ? 686 HOH B O     1 
HETATM 5871 O  O     . HOH K 7 .   ? -41.284 -1.729  -53.192 1.00 50.75  ? 687 HOH B O     1 
HETATM 5872 O  O     . HOH K 7 .   ? -22.341 11.694  -28.194 1.00 30.21  ? 688 HOH B O     1 
HETATM 5873 O  O     . HOH K 7 .   ? -40.501 0.741   -50.038 1.00 32.06  ? 689 HOH B O     1 
HETATM 5874 O  O     . HOH K 7 .   ? -23.220 4.444   -55.021 1.00 24.22  ? 690 HOH B O     1 
HETATM 5875 O  O     . HOH K 7 .   ? -26.329 1.801   -42.022 1.00 30.67  ? 691 HOH B O     1 
HETATM 5876 O  O     . HOH K 7 .   ? -34.206 6.429   -56.551 1.00 20.12  ? 692 HOH B O     1 
HETATM 5877 O  O     . HOH K 7 .   ? -38.565 -4.692  -44.600 1.00 48.28  ? 693 HOH B O     1 
HETATM 5878 O  O     . HOH K 7 .   ? -37.753 11.207  -34.014 1.00 51.80  ? 694 HOH B O     1 
HETATM 5879 O  O     . HOH K 7 .   ? -42.868 4.376   -67.387 1.00 41.98  ? 695 HOH B O     1 
HETATM 5880 O  O     . HOH K 7 .   ? -4.536  22.151  -37.601 1.00 47.40  ? 696 HOH B O     1 
HETATM 5881 O  O     . HOH K 7 .   ? 3.993   15.651  -58.620 1.00 40.42  ? 697 HOH B O     1 
HETATM 5882 O  O     . HOH K 7 .   ? -47.254 23.059  -57.595 1.00 33.19  ? 698 HOH B O     1 
HETATM 5883 O  O     . HOH K 7 .   ? -12.861 8.062   -47.938 1.00 23.90  ? 699 HOH B O     1 
HETATM 5884 O  O     . HOH K 7 .   ? -24.615 10.045  -27.878 1.00 31.49  ? 700 HOH B O     1 
HETATM 5885 O  O     . HOH K 7 .   ? -22.140 25.903  -56.490 1.00 39.21  ? 701 HOH B O     1 
HETATM 5886 O  O     . HOH K 7 .   ? 2.589   19.688  -50.897 1.00 34.23  ? 702 HOH B O     1 
HETATM 5887 O  O     . HOH K 7 .   ? -42.896 32.413  -50.768 1.00 43.35  ? 703 HOH B O     1 
HETATM 5888 O  O     . HOH K 7 .   ? 1.366   2.258   -43.802 1.00 45.90  ? 704 HOH B O     1 
HETATM 5889 O  O     . HOH K 7 .   ? -3.133  3.875   -47.019 1.00 46.25  ? 705 HOH B O     1 
HETATM 5890 O  O     . HOH K 7 .   ? -31.208 -2.891  -53.482 1.00 28.10  ? 706 HOH B O     1 
HETATM 5891 O  O     . HOH K 7 .   ? -25.403 25.074  -43.627 1.00 47.95  ? 707 HOH B O     1 
HETATM 5892 O  O     . HOH K 7 .   ? -36.279 6.626   -32.381 1.00 32.32  ? 708 HOH B O     1 
HETATM 5893 O  O     . HOH K 7 .   ? -36.171 20.355  -65.076 1.00 31.62  ? 709 HOH B O     1 
HETATM 5894 O  O     . HOH K 7 .   ? -19.736 12.591  -61.534 1.00 31.77  ? 710 HOH B O     1 
HETATM 5895 O  O     . HOH K 7 .   ? -26.731 26.825  -60.375 1.00 34.62  ? 711 HOH B O     1 
HETATM 5896 O  O     . HOH K 7 .   ? -32.697 6.620   -34.038 1.00 25.43  ? 712 HOH B O     1 
HETATM 5897 O  O     . HOH K 7 .   ? -20.474 20.439  -64.441 1.00 29.10  ? 713 HOH B O     1 
HETATM 5898 O  O     . HOH K 7 .   ? -31.168 -0.498  -71.422 1.00 34.48  ? 714 HOH B O     1 
HETATM 5899 O  O     . HOH K 7 .   ? -18.443 7.952   -61.478 1.00 33.19  ? 715 HOH B O     1 
HETATM 5900 O  O     . HOH K 7 .   ? -34.636 19.463  -66.341 1.00 41.64  ? 716 HOH B O     1 
HETATM 5901 O  O     . HOH K 7 .   ? -23.488 0.977   -57.853 1.00 23.93  ? 717 HOH B O     1 
HETATM 5902 O  O     . HOH K 7 .   ? -31.176 -2.835  -44.007 1.00 39.82  ? 718 HOH B O     1 
HETATM 5903 O  O     . HOH K 7 .   ? -28.086 10.149  -75.620 1.00 33.48  ? 719 HOH B O     1 
HETATM 5904 O  O     . HOH K 7 .   ? -1.419  14.537  -34.901 1.00 44.07  ? 720 HOH B O     1 
HETATM 5905 O  O     . HOH K 7 .   ? -10.585 6.222   -61.136 1.00 39.77  ? 721 HOH B O     1 
HETATM 5906 O  O     . HOH K 7 .   ? -22.430 13.055  -62.088 1.00 24.90  ? 722 HOH B O     1 
HETATM 5907 O  O     . HOH K 7 .   ? -33.652 -3.499  -52.164 1.00 41.04  ? 723 HOH B O     1 
HETATM 5908 O  O     . HOH K 7 .   ? -26.953 6.284   -77.359 1.00 47.01  ? 724 HOH B O     1 
HETATM 5909 O  O     . HOH K 7 .   ? -9.063  15.490  -32.855 1.00 35.53  ? 725 HOH B O     1 
HETATM 5910 O  O     . HOH K 7 .   ? -30.405 11.336  -29.638 1.00 30.18  ? 726 HOH B O     1 
HETATM 5911 O  O     . HOH K 7 .   ? -47.135 4.435   -44.945 1.00 32.11  ? 727 HOH B O     1 
HETATM 5912 O  O     . HOH K 7 .   ? -20.531 19.361  -34.824 1.00 28.91  ? 728 HOH B O     1 
HETATM 5913 O  O     . HOH K 7 .   ? -13.351 2.800   -59.871 1.00 36.86  ? 729 HOH B O     1 
HETATM 5914 O  O     . HOH K 7 .   ? -48.097 16.515  -58.234 1.00 38.51  ? 730 HOH B O     1 
HETATM 5915 O  O     . HOH K 7 .   ? -31.149 1.822   -75.098 1.00 48.99  ? 731 HOH B O     1 
HETATM 5916 O  O     . HOH K 7 .   ? -8.815  19.220  -48.867 1.00 24.33  ? 732 HOH B O     1 
HETATM 5917 O  O     . HOH K 7 .   ? -43.574 7.888   -36.052 1.00 33.28  ? 733 HOH B O     1 
HETATM 5918 O  O     . HOH K 7 .   ? -41.021 24.130  -52.021 1.00 31.32  ? 734 HOH B O     1 
HETATM 5919 O  O     . HOH K 7 .   ? -8.622  22.122  -58.976 1.00 42.03  ? 735 HOH B O     1 
HETATM 5920 O  O     . HOH K 7 .   ? -35.827 2.542   -24.305 1.00 47.75  ? 736 HOH B O     1 
HETATM 5921 O  O     . HOH K 7 .   ? -40.067 24.435  -59.580 1.00 30.10  ? 737 HOH B O     1 
HETATM 5922 O  O     . HOH K 7 .   ? -48.937 23.099  -51.512 1.00 42.65  ? 738 HOH B O     1 
HETATM 5923 O  O     . HOH K 7 .   ? -15.208 -3.631  -33.657 1.00 47.95  ? 739 HOH B O     1 
HETATM 5924 O  O     . HOH K 7 .   ? -30.068 -5.731  -61.623 1.00 44.57  ? 740 HOH B O     1 
HETATM 5925 O  O     . HOH K 7 .   ? -8.129  14.965  -29.684 1.00 39.77  ? 741 HOH B O     1 
HETATM 5926 O  O     . HOH K 7 .   ? -41.344 29.020  -47.182 1.00 51.91  ? 742 HOH B O     1 
HETATM 5927 O  O     . HOH K 7 .   ? -6.982  23.300  -43.441 1.00 53.11  ? 743 HOH B O     1 
HETATM 5928 O  O     . HOH K 7 .   ? -25.931 4.448   -53.078 1.00 19.57  ? 744 HOH B O     1 
HETATM 5929 O  O     . HOH K 7 .   ? -44.726 21.516  -46.246 1.00 39.18  ? 745 HOH B O     1 
HETATM 5930 O  O     . HOH K 7 .   ? -49.870 17.337  -56.193 1.00 37.67  ? 746 HOH B O     1 
HETATM 5931 O  O     . HOH K 7 .   ? -36.371 30.789  -58.518 1.00 39.23  ? 747 HOH B O     1 
HETATM 5932 O  O     . HOH K 7 .   ? -27.962 24.748  -47.540 1.00 30.08  ? 748 HOH B O     1 
HETATM 5933 O  O     . HOH K 7 .   ? -25.779 4.926   -56.039 1.00 20.11  ? 749 HOH B O     1 
HETATM 5934 O  O     . HOH K 7 .   ? -11.088 20.091  -35.476 1.00 43.05  ? 750 HOH B O     1 
HETATM 5935 O  O     . HOH K 7 .   ? -20.744 6.710   -55.365 1.00 18.87  ? 751 HOH B O     1 
HETATM 5936 O  O     . HOH K 7 .   ? -40.496 19.856  -38.463 1.00 43.33  ? 752 HOH B O     1 
HETATM 5937 O  O     . HOH K 7 .   ? -34.410 11.085  -31.728 1.00 49.21  ? 753 HOH B O     1 
HETATM 5938 O  O     . HOH K 7 .   ? -33.398 -3.536  -62.571 1.00 50.16  ? 754 HOH B O     1 
HETATM 5939 O  O     . HOH K 7 .   ? -15.564 15.284  -63.310 1.00 47.90  ? 755 HOH B O     1 
HETATM 5940 O  O     . HOH K 7 .   ? -20.657 23.131  -63.173 1.00 51.24  ? 756 HOH B O     1 
HETATM 5941 O  O     . HOH K 7 .   ? -2.906  20.022  -55.999 1.00 31.81  ? 757 HOH B O     1 
HETATM 5942 O  O     . HOH K 7 .   ? -42.138 23.308  -50.078 1.00 33.75  ? 758 HOH B O     1 
HETATM 5943 O  O     . HOH K 7 .   ? -35.028 32.384  -52.471 1.00 47.00  ? 759 HOH B O     1 
HETATM 5944 O  O     . HOH K 7 .   ? -24.866 7.116   -53.499 1.00 22.95  ? 760 HOH B O     1 
HETATM 5945 O  O     . HOH K 7 .   ? -19.870 28.920  -55.857 1.00 37.46  ? 761 HOH B O     1 
HETATM 5946 O  O     . HOH K 7 .   ? -50.563 19.947  -57.068 1.00 48.09  ? 762 HOH B O     1 
HETATM 5947 O  O     . HOH K 7 .   ? -36.262 16.970  -67.498 1.00 46.37  ? 763 HOH B O     1 
HETATM 5948 O  O     . HOH K 7 .   ? -2.789  5.000   -53.551 1.00 40.48  ? 764 HOH B O     1 
HETATM 5949 O  O     . HOH K 7 .   ? -6.185  18.753  -63.537 1.00 39.48  ? 765 HOH B O     1 
HETATM 5950 O  O     . HOH K 7 .   ? -11.188 15.305  -34.779 1.00 39.44  ? 766 HOH B O     1 
HETATM 5951 O  O     . HOH K 7 .   ? -25.757 17.665  -66.213 1.00 42.80  ? 767 HOH B O     1 
HETATM 5952 O  O     . HOH K 7 .   ? -25.164 11.294  -25.543 1.00 44.76  ? 768 HOH B O     1 
HETATM 5953 O  O     . HOH K 7 .   ? -16.583 21.973  -63.829 1.00 45.04  ? 769 HOH B O     1 
HETATM 5954 O  O     . HOH K 7 .   ? -58.151 12.171  -45.626 1.00 32.99  ? 770 HOH B O     1 
HETATM 5955 O  O     . HOH K 7 .   ? -46.367 8.461   -37.564 1.00 50.17  ? 771 HOH B O     1 
HETATM 5956 O  O     . HOH K 7 .   ? -22.269 25.605  -41.289 1.00 43.35  ? 772 HOH B O     1 
HETATM 5957 O  O     . HOH K 7 .   ? -38.690 2.321   -61.550 1.00 29.37  ? 773 HOH B O     1 
HETATM 5958 O  O     . HOH K 7 .   ? -45.378 1.088   -50.525 1.00 41.79  ? 774 HOH B O     1 
HETATM 5959 O  O     . HOH K 7 .   ? -0.291  7.612   -58.058 1.00 59.16  ? 775 HOH B O     1 
HETATM 5960 O  O     . HOH K 7 .   ? -24.649 -0.601  -47.304 1.00 45.69  ? 776 HOH B O     1 
HETATM 5961 O  O     . HOH K 7 .   ? -6.256  25.984  -48.272 1.00 50.13  ? 777 HOH B O     1 
HETATM 5962 O  O     . HOH K 7 .   ? -17.952 19.243  -31.032 1.00 35.46  ? 778 HOH B O     1 
HETATM 5963 O  O     . HOH K 7 .   ? -22.568 23.519  -35.670 1.00 37.15  ? 779 HOH B O     1 
HETATM 5964 O  O     . HOH K 7 .   ? -24.446 -1.374  -53.832 1.00 49.98  ? 780 HOH B O     1 
HETATM 5965 O  O     . HOH K 7 .   ? -18.626 10.229  -62.683 1.00 27.05  ? 781 HOH B O     1 
HETATM 5966 O  O     . HOH K 7 .   ? -32.161 -4.166  -55.703 1.00 37.60  ? 782 HOH B O     1 
HETATM 5967 O  O     . HOH K 7 .   ? -27.317 -0.646  -43.158 1.00 34.89  ? 783 HOH B O     1 
HETATM 5968 O  O     . HOH K 7 .   ? -31.231 -2.608  -48.900 1.00 41.38  ? 784 HOH B O     1 
HETATM 5969 O  O     . HOH K 7 .   ? -23.321 18.136  -66.129 1.00 43.01  ? 785 HOH B O     1 
HETATM 5970 O  O     . HOH K 7 .   ? -43.836 16.080  -37.336 1.00 51.98  ? 786 HOH B O     1 
HETATM 5971 O  O     . HOH K 7 .   ? -21.978 -0.096  -50.733 1.00 48.21  ? 787 HOH B O     1 
HETATM 5972 O  O     . HOH K 7 .   ? -18.686 -1.472  -47.734 1.00 49.83  ? 788 HOH B O     1 
HETATM 5973 O  O     . HOH K 7 .   ? -50.126 5.500   -47.892 1.00 35.56  ? 789 HOH B O     1 
HETATM 5974 O  O     . HOH K 7 .   ? -22.037 25.094  -37.899 1.00 35.86  ? 790 HOH B O     1 
HETATM 5975 O  O     . HOH K 7 .   ? -30.588 23.162  -37.911 1.00 42.45  ? 791 HOH B O     1 
HETATM 5976 O  O     . HOH K 7 .   ? -21.015 13.941  -64.329 1.00 52.47  ? 792 HOH B O     1 
HETATM 5977 O  O     . HOH K 7 .   ? -49.946 8.024   -44.070 1.00 36.70  ? 793 HOH B O     1 
HETATM 5978 O  O     . HOH K 7 .   ? -29.287 -3.109  -51.894 1.00 47.31  ? 794 HOH B O     1 
HETATM 5979 O  O     . HOH K 7 .   ? -26.458 16.447  -68.746 1.00 32.68  ? 795 HOH B O     1 
HETATM 5980 O  O     . HOH K 7 .   ? -0.458  18.974  -55.402 1.00 33.71  ? 796 HOH B O     1 
HETATM 5981 O  O     . HOH K 7 .   ? -36.885 -2.237  -33.496 1.00 41.91  ? 797 HOH B O     1 
HETATM 5982 O  O     . HOH K 7 .   ? -36.338 -4.641  -34.884 1.00 52.29  ? 798 HOH B O     1 
HETATM 5983 O  O     . HOH K 7 .   ? -23.316 7.991   -26.587 1.00 34.36  ? 799 HOH B O     1 
HETATM 5984 O  O     . HOH K 7 .   ? -27.723 25.696  -39.085 1.00 40.96  ? 800 HOH B O     1 
HETATM 5985 O  O     . HOH K 7 .   ? -23.678 5.284   -27.488 1.00 32.88  ? 801 HOH B O     1 
HETATM 5986 O  O     . HOH K 7 .   ? -22.870 1.925   -55.318 1.00 46.29  ? 802 HOH B O     1 
HETATM 5987 O  O     . HOH K 7 .   ? -43.743 24.878  -48.005 1.00 39.34  ? 803 HOH B O     1 
HETATM 5988 O  O     . HOH K 7 .   ? -4.067  17.543  -62.157 1.00 33.85  ? 804 HOH B O     1 
HETATM 5989 O  O     . HOH K 7 .   ? -48.997 7.068   -58.280 1.00 45.46  ? 805 HOH B O     1 
HETATM 5990 O  O     . HOH K 7 .   ? -30.320 25.772  -47.590 1.00 34.27  ? 806 HOH B O     1 
HETATM 5991 O  O     . HOH K 7 .   ? -32.565 6.526   -31.340 1.00 33.20  ? 807 HOH B O     1 
HETATM 5992 O  O     . HOH K 7 .   ? -32.042 26.206  -45.433 1.00 37.34  ? 808 HOH B O     1 
HETATM 5993 O  O     . HOH K 7 .   ? -15.038 23.291  -58.021 1.00 27.66  ? 809 HOH B O     1 
HETATM 5994 O  O     . HOH K 7 .   ? -13.140 14.647  -32.604 1.00 44.76  ? 810 HOH B O     1 
HETATM 5995 O  O     . HOH K 7 .   ? -31.051 16.264  -29.463 1.00 42.70  ? 811 HOH B O     1 
HETATM 5996 O  O     . HOH K 7 .   ? -17.619 24.206  -59.371 1.00 37.53  ? 812 HOH B O     1 
HETATM 5997 O  O     . HOH K 7 .   ? -39.160 -2.186  -55.270 1.00 47.71  ? 813 HOH B O     1 
HETATM 5998 O  O     . HOH K 7 .   ? -20.295 27.386  -58.085 1.00 41.98  ? 814 HOH B O     1 
HETATM 5999 O  O     . HOH K 7 .   ? -34.659 16.262  -31.828 1.00 44.26  ? 815 HOH B O     1 
HETATM 6000 O  O     . HOH K 7 .   ? -22.106 30.400  -56.476 1.00 46.40  ? 816 HOH B O     1 
HETATM 6001 O  O     . HOH K 7 .   ? -17.604 27.197  -45.757 1.00 41.16  ? 817 HOH B O     1 
HETATM 6002 O  O     . HOH K 7 .   ? 0.368   11.696  -42.773 1.00 36.16  ? 818 HOH B O     1 
HETATM 6003 O  O     . HOH K 7 .   ? 1.779   10.534  -64.444 1.00 49.48  ? 819 HOH B O     1 
HETATM 6004 O  O     . HOH K 7 .   ? -53.496 17.649  -43.876 1.00 49.01  ? 820 HOH B O     1 
HETATM 6005 O  O     . HOH K 7 .   ? -23.940 3.144   -25.594 1.00 47.76  ? 821 HOH B O     1 
HETATM 6006 O  O     . HOH K 7 .   ? -34.477 28.109  -45.731 1.00 41.55  ? 822 HOH B O     1 
HETATM 6007 O  O     . HOH K 7 .   ? 0.452   10.460  -40.645 1.00 46.34  ? 823 HOH B O     1 
HETATM 6008 O  O     . HOH K 7 .   ? -35.476 -3.217  -58.036 1.00 44.54  ? 824 HOH B O     1 
HETATM 6009 O  O     . HOH K 7 .   ? -31.523 13.777  -30.675 1.00 43.45  ? 825 HOH B O     1 
HETATM 6010 O  O     . HOH K 7 .   ? -24.140 8.695   -24.007 1.00 55.19  ? 826 HOH B O     1 
HETATM 6011 O  O     . HOH K 7 .   ? -2.189  19.593  -61.961 1.00 41.07  ? 827 HOH B O     1 
HETATM 6012 O  O     . HOH K 7 .   ? -47.240 30.179  -53.716 1.00 35.55  ? 828 HOH B O     1 
HETATM 6013 O  O     . HOH K 7 .   ? 3.728   18.647  -55.237 1.00 56.63  ? 829 HOH B O     1 
HETATM 6014 O  O     . HOH K 7 .   ? 2.678   8.527   -50.547 1.00 42.14  ? 830 HOH B O     1 
HETATM 6015 O  O     . HOH K 7 .   ? -60.245 11.209  -46.987 1.00 26.86  ? 831 HOH B O     1 
HETATM 6016 O  O     . HOH K 7 .   ? -24.615 16.283  -70.547 1.00 48.66  ? 832 HOH B O     1 
HETATM 6017 O  O     . HOH K 7 .   ? -17.392 2.066   -78.777 1.00 58.37  ? 833 HOH B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . GLY A 13  ? 0.9729 0.8125 0.8705 -0.0972 -0.0969 0.0728  -7  GLY A N     
2    C  CA    . GLY A 13  ? 0.8327 0.6830 0.7351 -0.0937 -0.0899 0.0714  -7  GLY A CA    
3    C  C     . GLY A 13  ? 0.8568 0.7287 0.7647 -0.0970 -0.0790 0.0712  -7  GLY A C     
4    O  O     . GLY A 13  ? 0.7859 0.6638 0.6883 -0.1079 -0.0779 0.0753  -7  GLY A O     
5    N  N     . LEU A 14  ? 0.6703 0.5539 0.5889 -0.0876 -0.0712 0.0661  -6  LEU A N     
6    C  CA    . LEU A 14  ? 0.5375 0.4412 0.4627 -0.0886 -0.0612 0.0648  -6  LEU A CA    
7    C  C     . LEU A 14  ? 0.5295 0.4411 0.4571 -0.0869 -0.0559 0.0640  -6  LEU A C     
8    O  O     . LEU A 14  ? 0.5772 0.5025 0.5054 -0.0923 -0.0501 0.0649  -6  LEU A O     
9    C  CB    . LEU A 14  ? 0.5356 0.4466 0.4704 -0.0799 -0.0563 0.0601  -6  LEU A CB    
10   C  CG    . LEU A 14  ? 0.5462 0.4474 0.4795 -0.0789 -0.0620 0.0597  -6  LEU A CG    
11   C  CD1   . LEU A 14  ? 0.6426 0.5510 0.5850 -0.0698 -0.0571 0.0549  -6  LEU A CD1   
12   C  CD2   . LEU A 14  ? 0.6716 0.5738 0.5990 -0.0899 -0.0645 0.0638  -6  LEU A CD2   
13   N  N     . VAL A 15  ? 0.4752 0.3790 0.4043 -0.0793 -0.0577 0.0619  -5  VAL A N     
14   C  CA    . VAL A 15  ? 0.4212 0.3311 0.3528 -0.0765 -0.0532 0.0608  -5  VAL A CA    
15   C  C     . VAL A 15  ? 0.4894 0.3852 0.4121 -0.0804 -0.0609 0.0642  -5  VAL A C     
16   O  O     . VAL A 15  ? 0.4923 0.3725 0.4103 -0.0801 -0.0695 0.0653  -5  VAL A O     
17   C  CB    . VAL A 15  ? 0.4938 0.4072 0.4350 -0.0646 -0.0491 0.0555  -5  VAL A CB    
18   C  CG1   . VAL A 15  ? 0.5254 0.4406 0.4684 -0.0610 -0.0467 0.0543  -5  VAL A CG1   
19   C  CG2   . VAL A 15  ? 0.4563 0.3845 0.4055 -0.0621 -0.0414 0.0528  -5  VAL A CG2   
20   N  N     . PRO A 16  ? 0.4418 0.3418 0.3615 -0.0845 -0.0588 0.0660  -4  PRO A N     
21   C  CA    . PRO A 16  ? 0.4751 0.3607 0.3857 -0.0882 -0.0668 0.0695  -4  PRO A CA    
22   C  C     . PRO A 16  ? 0.4726 0.3461 0.3865 -0.0780 -0.0719 0.0664  -4  PRO A C     
23   O  O     . PRO A 16  ? 0.4621 0.3423 0.3852 -0.0686 -0.0667 0.0616  -4  PRO A O     
24   C  CB    . PRO A 16  ? 0.4705 0.3664 0.3797 -0.0923 -0.0613 0.0704  -4  PRO A CB    
25   C  CG    . PRO A 16  ? 0.4226 0.3376 0.3369 -0.0951 -0.0521 0.0689  -4  PRO A CG    
26   C  CD    . PRO A 16  ? 0.3900 0.3078 0.3139 -0.0860 -0.0495 0.0647  -4  PRO A CD    
27   N  N     . ARG A 17  ? 0.5797 0.4353 0.4859 -0.0800 -0.0824 0.0690  -3  ARG A N     
28   C  CA    . ARG A 17  ? 0.7019 0.5454 0.6105 -0.0709 -0.0887 0.0659  -3  ARG A CA    
29   C  C     . ARG A 17  ? 0.6855 0.5295 0.5939 -0.0694 -0.0881 0.0660  -3  ARG A C     
30   O  O     . ARG A 17  ? 0.5990 0.4475 0.5018 -0.0773 -0.0860 0.0698  -3  ARG A O     
31   C  CB    . ARG A 17  ? 0.7059 0.5293 0.6061 -0.0737 -0.1012 0.0685  -3  ARG A CB    
32   C  CG    . ARG A 17  ? 0.7974 0.6166 0.7006 -0.0696 -0.1036 0.0657  -3  ARG A CG    
33   C  CD    . ARG A 17  ? 0.8806 0.6848 0.7728 -0.0785 -0.1134 0.0707  -3  ARG A CD    
34   N  NE    . ARG A 17  ? 0.9230 0.7096 0.8059 -0.0819 -0.1243 0.0742  -3  ARG A NE    
35   C  CZ    . ARG A 17  ? 0.8906 0.6630 0.7614 -0.0920 -0.1337 0.0801  -3  ARG A CZ    
36   N  NH1   . ARG A 17  ? 0.8961 0.6701 0.7627 -0.0999 -0.1333 0.0830  -3  ARG A NH1   
37   N  NH2   . ARG A 17  ? 0.8645 0.6203 0.7270 -0.0944 -0.1441 0.0831  -3  ARG A NH2   
38   N  N     . GLY A 18  ? 0.5289 0.3687 0.4434 -0.0592 -0.0902 0.0616  -2  GLY A N     
39   C  CA    . GLY A 18  ? 0.5248 0.3635 0.4392 -0.0571 -0.0910 0.0614  -2  GLY A CA    
40   C  C     . GLY A 18  ? 0.5597 0.4155 0.4809 -0.0550 -0.0800 0.0593  -2  GLY A C     
41   O  O     . GLY A 18  ? 0.5643 0.4316 0.4939 -0.0498 -0.0724 0.0556  -2  GLY A O     
42   N  N     . SER A 19  ? 0.5070 0.3640 0.4240 -0.0591 -0.0795 0.0618  -1  SER A N     
43   C  CA    . SER A 19  ? 0.4712 0.3430 0.3938 -0.0572 -0.0700 0.0598  -1  SER A CA    
44   C  C     . SER A 19  ? 0.4320 0.3172 0.3531 -0.0645 -0.0622 0.0616  -1  SER A C     
45   O  O     . SER A 19  ? 0.4474 0.3454 0.3738 -0.0625 -0.0540 0.0593  -1  SER A O     
46   C  CB    . SER A 19  ? 0.6016 0.4689 0.5204 -0.0581 -0.0730 0.0612  -1  SER A CB    
47   O  OG    . SER A 19  ? 0.7570 0.6147 0.6637 -0.0681 -0.0797 0.0670  -1  SER A OG    
48   N  N     . HIS A 20  ? 0.4653 0.3480 0.3796 -0.0729 -0.0646 0.0653  0   HIS A N     
49   C  CA    . HIS A 20  ? 0.4239 0.3204 0.3368 -0.0805 -0.0576 0.0667  0   HIS A CA    
50   C  C     . HIS A 20  ? 0.4668 0.3760 0.3899 -0.0747 -0.0498 0.0624  0   HIS A C     
51   O  O     . HIS A 20  ? 0.4628 0.3676 0.3906 -0.0685 -0.0516 0.0602  0   HIS A O     
52   C  CB    . HIS A 20  ? 0.4236 0.3136 0.3257 -0.0920 -0.0631 0.0721  0   HIS A CB    
53   C  CG    . HIS A 20  ? 0.3924 0.2672 0.2834 -0.0978 -0.0724 0.0768  0   HIS A CG    
54   N  ND1   . HIS A 20  ? 0.3881 0.2642 0.2757 -0.0999 -0.0717 0.0778  0   HIS A ND1   
55   C  CD2   . HIS A 20  ? 0.4577 0.3148 0.3403 -0.1017 -0.0833 0.0806  0   HIS A CD2   
56   C  CE1   . HIS A 20  ? 0.4382 0.2982 0.3155 -0.1050 -0.0817 0.0823  0   HIS A CE1   
57   N  NE2   . HIS A 20  ? 0.4577 0.3056 0.3317 -0.1062 -0.0891 0.0841  0   HIS A NE2   
58   N  N     . MET A 21  ? 0.3465 0.2714 0.2728 -0.0768 -0.0415 0.0611  1   MET A N     
59   C  CA    . MET A 21  ? 0.3387 0.2762 0.2750 -0.0708 -0.0340 0.0568  1   MET A CA    
60   C  C     . MET A 21  ? 0.3567 0.3038 0.2926 -0.0772 -0.0310 0.0577  1   MET A C     
61   O  O     . MET A 21  ? 0.3646 0.3154 0.2936 -0.0870 -0.0312 0.0608  1   MET A O     
62   C  CB    . MET A 21  ? 0.3754 0.3240 0.3170 -0.0672 -0.0270 0.0537  1   MET A CB    
63   C  CG    . MET A 21  ? 0.5246 0.4656 0.4661 -0.0623 -0.0296 0.0531  1   MET A CG    
64   S  SD    . MET A 21  ? 0.5034 0.4382 0.4530 -0.0507 -0.0311 0.0494  1   MET A SD    
65   C  CE    . MET A 21  ? 0.4423 0.3925 0.4020 -0.0451 -0.0216 0.0450  1   MET A CE    
66   N  N     . ALA A 22  ? 0.3128 0.2645 0.2559 -0.0721 -0.0283 0.0550  2   ALA A N     
67   C  CA    . ALA A 22  ? 0.3306 0.2943 0.2757 -0.0766 -0.0243 0.0547  2   ALA A CA    
68   C  C     . ALA A 22  ? 0.2654 0.2457 0.2164 -0.0754 -0.0162 0.0514  2   ALA A C     
69   O  O     . ALA A 22  ? 0.3134 0.2951 0.2690 -0.0686 -0.0134 0.0486  2   ALA A O     
70   C  CB    . ALA A 22  ? 0.3094 0.2719 0.2602 -0.0712 -0.0246 0.0528  2   ALA A CB    
71   N  N     . PRO A 23  ? 0.2931 0.2863 0.2441 -0.0819 -0.0125 0.0513  3   PRO A N     
72   C  CA    . PRO A 23  ? 0.2933 0.3030 0.2513 -0.0794 -0.0051 0.0470  3   PRO A CA    
73   C  C     . PRO A 23  ? 0.2986 0.3114 0.2668 -0.0693 -0.0022 0.0429  3   PRO A C     
74   O  O     . PRO A 23  ? 0.2865 0.2934 0.2565 -0.0664 -0.0047 0.0433  3   PRO A O     
75   C  CB    . PRO A 23  ? 0.3165 0.3393 0.2729 -0.0885 -0.0028 0.0475  3   PRO A CB    
76   C  CG    . PRO A 23  ? 0.4003 0.4121 0.3461 -0.0978 -0.0093 0.0532  3   PRO A CG    
77   C  CD    . PRO A 23  ? 0.3251 0.3191 0.2703 -0.0915 -0.0152 0.0547  3   PRO A CD    
78   N  N     . ILE A 24  ? 0.2720 0.2934 0.2462 -0.0640 0.0028  0.0389  4   ILE A N     
79   C  CA    . ILE A 24  ? 0.2357 0.2608 0.2190 -0.0551 0.0056  0.0351  4   ILE A CA    
80   C  C     . ILE A 24  ? 0.3424 0.3835 0.3315 -0.0563 0.0099  0.0319  4   ILE A C     
81   O  O     . ILE A 24  ? 0.3636 0.4158 0.3523 -0.0605 0.0130  0.0303  4   ILE A O     
82   C  CB    . ILE A 24  ? 0.2892 0.3122 0.2755 -0.0482 0.0074  0.0327  4   ILE A CB    
83   C  CG1   . ILE A 24  ? 0.3294 0.3375 0.3112 -0.0464 0.0030  0.0353  4   ILE A CG1   
84   C  CG2   . ILE A 24  ? 0.2899 0.3174 0.2849 -0.0402 0.0102  0.0290  4   ILE A CG2   
85   C  CD1   . ILE A 24  ? 0.3404 0.3469 0.3227 -0.0427 0.0044  0.0339  4   ILE A CD1   
86   N  N     . ALA A 25  ? 0.2855 0.3285 0.2801 -0.0526 0.0098  0.0306  5   ALA A N     
87   C  CA    . ALA A 25  ? 0.2444 0.3023 0.2458 -0.0524 0.0132  0.0271  5   ALA A CA    
88   C  C     . ALA A 25  ? 0.2897 0.3495 0.2994 -0.0428 0.0151  0.0232  5   ALA A C     
89   O  O     . ALA A 25  ? 0.2800 0.3292 0.2901 -0.0373 0.0132  0.0240  5   ALA A O     
90   C  CB    . ALA A 25  ? 0.2943 0.3533 0.2950 -0.0569 0.0111  0.0291  5   ALA A CB    
91   N  N     . GLN A 26  ? 0.3328 0.4064 0.3490 -0.0411 0.0186  0.0187  6   GLN A N     
92   C  CA    . GLN A 26  ? 0.3573 0.4328 0.3812 -0.0324 0.0197  0.0148  6   GLN A CA    
93   C  C     . GLN A 26  ? 0.2366 0.3150 0.2656 -0.0302 0.0185  0.0141  6   GLN A C     
94   O  O     . GLN A 26  ? 0.2943 0.3834 0.3254 -0.0345 0.0192  0.0132  6   GLN A O     
95   C  CB    . GLN A 26  ? 0.4490 0.5374 0.4776 -0.0308 0.0233  0.0096  6   GLN A CB    
96   C  CG    . GLN A 26  ? 0.6383 0.7298 0.6752 -0.0223 0.0237  0.0051  6   GLN A CG    
97   C  CD    . GLN A 26  ? 0.7182 0.7966 0.7542 -0.0162 0.0222  0.0061  6   GLN A CD    
98   O  OE1   . GLN A 26  ? 0.7717 0.8455 0.8039 -0.0164 0.0229  0.0067  6   GLN A OE1   
99   N  NE2   . GLN A 26  ? 0.5418 0.6144 0.5807 -0.0112 0.0201  0.0065  6   GLN A NE2   
100  N  N     . ALA A 27  ? 0.2678 0.3368 0.2983 -0.0242 0.0165  0.0147  7   ALA A N     
101  C  CA    . ALA A 27  ? 0.2923 0.3634 0.3276 -0.0216 0.0150  0.0140  7   ALA A CA    
102  C  C     . ALA A 27  ? 0.2254 0.3073 0.2692 -0.0166 0.0165  0.0088  7   ALA A C     
103  O  O     . ALA A 27  ? 0.2620 0.3447 0.3078 -0.0125 0.0179  0.0061  7   ALA A O     
104  C  CB    . ALA A 27  ? 0.2792 0.3370 0.3126 -0.0175 0.0124  0.0163  7   ALA A CB    
105  N  N     . VAL A 28  ? 0.2248 0.3147 0.2736 -0.0166 0.0158  0.0072  8   VAL A N     
106  C  CA    . VAL A 28  ? 0.2530 0.3521 0.3105 -0.0108 0.0160  0.0021  8   VAL A CA    
107  C  C     . VAL A 28  ? 0.2515 0.3397 0.3099 -0.0035 0.0139  0.0021  8   VAL A C     
108  O  O     . VAL A 28  ? 0.2271 0.3042 0.2819 -0.0027 0.0117  0.0057  8   VAL A O     
109  C  CB    . VAL A 28  ? 0.2345 0.3421 0.2968 -0.0121 0.0147  0.0012  8   VAL A CB    
110  C  CG1   . VAL A 28  ? 0.2365 0.3514 0.3082 -0.0048 0.0136  -0.0041 8   VAL A CG1   
111  C  CG2   . VAL A 28  ? 0.2476 0.3679 0.3093 -0.0202 0.0169  0.0009  8   VAL A CG2   
112  N  N     . THR A 29  ? 0.2316 0.3234 0.2946 0.0017  0.0145  -0.0022 9   THR A N     
113  C  CA    . THR A 29  ? 0.2180 0.2992 0.2810 0.0079  0.0123  -0.0021 9   THR A CA    
114  C  C     . THR A 29  ? 0.2686 0.3555 0.3396 0.0141  0.0101  -0.0069 9   THR A C     
115  O  O     . THR A 29  ? 0.2898 0.3893 0.3669 0.0153  0.0114  -0.0121 9   THR A O     
116  C  CB    . THR A 29  ? 0.2421 0.3189 0.3018 0.0085  0.0141  -0.0024 9   THR A CB    
117  O  OG1   . THR A 29  ? 0.2833 0.3544 0.3357 0.0031  0.0154  0.0020  9   THR A OG1   
118  C  CG2   . THR A 29  ? 0.2816 0.3472 0.3407 0.0141  0.0116  -0.0020 9   THR A CG2   
119  N  N     . VAL A 30  ? 0.2451 0.3229 0.3162 0.0179  0.0064  -0.0053 10  VAL A N     
120  C  CA    . VAL A 30  ? 0.2242 0.3042 0.3021 0.0243  0.0029  -0.0092 10  VAL A CA    
121  C  C     . VAL A 30  ? 0.2762 0.3421 0.3508 0.0283  -0.0001 -0.0074 10  VAL A C     
122  O  O     . VAL A 30  ? 0.2554 0.3109 0.3229 0.0259  0.0005  -0.0029 10  VAL A O     
123  C  CB    . VAL A 30  ? 0.2391 0.3229 0.3208 0.0245  0.0002  -0.0091 10  VAL A CB    
124  C  CG1   . VAL A 30  ? 0.2478 0.3469 0.3333 0.0200  0.0030  -0.0112 10  VAL A CG1   
125  C  CG2   . VAL A 30  ? 0.2633 0.3348 0.3382 0.0224  -0.0017 -0.0032 10  VAL A CG2   
126  N  N     . SER A 31  ? 0.2470 0.3129 0.3267 0.0343  -0.0037 -0.0113 11  SER A N     
127  C  CA    . SER A 31  ? 0.2844 0.3368 0.3609 0.0378  -0.0074 -0.0097 11  SER A CA    
128  C  C     . SER A 31  ? 0.2528 0.2975 0.3278 0.0387  -0.0120 -0.0065 11  SER A C     
129  O  O     . SER A 31  ? 0.2614 0.3123 0.3417 0.0403  -0.0144 -0.0084 11  SER A O     
130  C  CB    . SER A 31  ? 0.3360 0.3906 0.4181 0.0438  -0.0099 -0.0155 11  SER A CB    
131  O  OG    . SER A 31  ? 0.3271 0.3677 0.4058 0.0468  -0.0147 -0.0135 11  SER A OG    
132  N  N     . LEU A 32  ? 0.2629 0.2945 0.3305 0.0374  -0.0134 -0.0018 12  LEU A N     
133  C  CA    . LEU A 32  ? 0.2510 0.2744 0.3161 0.0381  -0.0182 0.0012  12  LEU A CA    
134  C  C     . LEU A 32  ? 0.3309 0.3535 0.4017 0.0439  -0.0243 -0.0024 12  LEU A C     
135  O  O     . LEU A 32  ? 0.2889 0.3094 0.3604 0.0450  -0.0286 -0.0014 12  LEU A O     
136  C  CB    . LEU A 32  ? 0.2964 0.3071 0.3527 0.0356  -0.0185 0.0061  12  LEU A CB    
137  C  CG    . LEU A 32  ? 0.2772 0.2786 0.3290 0.0351  -0.0233 0.0097  12  LEU A CG    
138  C  CD1   . LEU A 32  ? 0.2823 0.2876 0.3342 0.0328  -0.0231 0.0113  12  LEU A CD1   
139  C  CD2   . LEU A 32  ? 0.2927 0.2838 0.3360 0.0320  -0.0228 0.0140  12  LEU A CD2   
140  N  N     . ASN A 33  ? 0.2984 0.3219 0.3728 0.0480  -0.0253 -0.0066 13  ASN A N     
141  C  CA    . ASN A 33  ? 0.2964 0.3188 0.3767 0.0544  -0.0318 -0.0108 13  ASN A CA    
142  C  C     . ASN A 33  ? 0.3318 0.3670 0.4209 0.0567  -0.0328 -0.0149 13  ASN A C     
143  O  O     . ASN A 33  ? 0.3382 0.3707 0.4304 0.0603  -0.0391 -0.0158 13  ASN A O     
144  C  CB    . ASN A 33  ? 0.2974 0.3204 0.3809 0.0586  -0.0322 -0.0157 13  ASN A CB    
145  C  CG    . ASN A 33  ? 0.4179 0.4282 0.4930 0.0564  -0.0318 -0.0118 13  ASN A CG    
146  O  OD1   . ASN A 33  ? 0.4717 0.4697 0.5398 0.0542  -0.0349 -0.0065 13  ASN A OD1   
147  N  ND2   . ASN A 33  ? 0.4579 0.4717 0.5336 0.0565  -0.0280 -0.0145 13  ASN A ND2   
148  N  N     . ASP A 34  ? 0.3181 0.3674 0.4110 0.0542  -0.0269 -0.0173 14  ASP A N     
149  C  CA    . ASP A 34  ? 0.2997 0.3628 0.4010 0.0554  -0.0273 -0.0212 14  ASP A CA    
150  C  C     . ASP A 34  ? 0.3027 0.3633 0.4009 0.0518  -0.0284 -0.0163 14  ASP A C     
151  O  O     . ASP A 34  ? 0.3416 0.4082 0.4459 0.0541  -0.0319 -0.0186 14  ASP A O     
152  C  CB    . ASP A 34  ? 0.2974 0.3767 0.4030 0.0529  -0.0207 -0.0251 14  ASP A CB    
153  C  CG    . ASP A 34  ? 0.3817 0.4652 0.4915 0.0572  -0.0200 -0.0312 14  ASP A CG    
154  O  OD1   . ASP A 34  ? 0.4480 0.5296 0.5632 0.0641  -0.0257 -0.0356 14  ASP A OD1   
155  O  OD2   . ASP A 34  ? 0.3475 0.4361 0.4551 0.0538  -0.0144 -0.0317 14  ASP A OD2   
156  N  N     . LEU A 35  ? 0.2888 0.3408 0.3778 0.0463  -0.0257 -0.0100 15  LEU A N     
157  C  CA    . LEU A 35  ? 0.2671 0.3149 0.3523 0.0432  -0.0275 -0.0055 15  LEU A CA    
158  C  C     . LEU A 35  ? 0.3152 0.3526 0.3993 0.0469  -0.0349 -0.0043 15  LEU A C     
159  O  O     . LEU A 35  ? 0.3484 0.3873 0.4346 0.0472  -0.0384 -0.0038 15  LEU A O     
160  C  CB    . LEU A 35  ? 0.2616 0.3021 0.3372 0.0373  -0.0235 0.0002  15  LEU A CB    
161  C  CG    . LEU A 35  ? 0.2333 0.2825 0.3087 0.0326  -0.0173 0.0002  15  LEU A CG    
162  C  CD1   . LEU A 35  ? 0.2808 0.3207 0.3470 0.0283  -0.0143 0.0051  15  LEU A CD1   
163  C  CD2   . LEU A 35  ? 0.2402 0.2981 0.3187 0.0301  -0.0172 0.0000  15  LEU A CD2   
164  N  N     . LYS A 36  ? 0.3183 0.3446 0.3987 0.0492  -0.0378 -0.0035 16  LYS A N     
165  C  CA    . LYS A 36  ? 0.3216 0.3360 0.3993 0.0518  -0.0455 -0.0015 16  LYS A CA    
166  C  C     . LYS A 36  ? 0.3355 0.3551 0.4229 0.0585  -0.0517 -0.0071 16  LYS A C     
167  O  O     . LYS A 36  ? 0.3863 0.4006 0.4735 0.0600  -0.0581 -0.0057 16  LYS A O     
168  C  CB    . LYS A 36  ? 0.3663 0.3676 0.4372 0.0519  -0.0471 0.0008  16  LYS A CB    
169  C  CG    . LYS A 36  ? 0.4075 0.4025 0.4686 0.0455  -0.0424 0.0065  16  LYS A CG    
170  C  CD    . LYS A 36  ? 0.5453 0.5316 0.6015 0.0453  -0.0422 0.0076  16  LYS A CD    
171  C  CE    . LYS A 36  ? 0.6454 0.6182 0.6976 0.0472  -0.0501 0.0094  16  LYS A CE    
172  N  NZ    . LYS A 36  ? 0.6738 0.6380 0.7202 0.0457  -0.0496 0.0111  16  LYS A NZ    
173  N  N     . ASN A 37  ? 0.3557 0.3860 0.4518 0.0627  -0.0502 -0.0137 17  ASN A N     
174  C  CA    . ASN A 37  ? 0.3378 0.3738 0.4440 0.0699  -0.0564 -0.0201 17  ASN A CA    
175  C  C     . ASN A 37  ? 0.4143 0.4675 0.5295 0.0700  -0.0545 -0.0238 17  ASN A C     
176  O  O     . ASN A 37  ? 0.4402 0.5011 0.5653 0.0760  -0.0592 -0.0299 17  ASN A O     
177  C  CB    . ASN A 37  ? 0.3869 0.4249 0.4983 0.0755  -0.0571 -0.0263 17  ASN A CB    
178  C  CG    . ASN A 37  ? 0.5384 0.5919 0.6541 0.0738  -0.0486 -0.0304 17  ASN A CG    
179  O  OD1   . ASN A 37  ? 0.4768 0.5426 0.5946 0.0697  -0.0432 -0.0303 17  ASN A OD1   
180  N  ND2   . ASN A 37  ? 0.5370 0.5895 0.6536 0.0768  -0.0478 -0.0341 17  ASN A ND2   
181  N  N     . GLY A 38  ? 0.3552 0.4148 0.4673 0.0633  -0.0480 -0.0205 18  GLY A N     
182  C  CA    . GLY A 38  ? 0.4058 0.4809 0.5251 0.0620  -0.0462 -0.0231 18  GLY A CA    
183  C  C     . GLY A 38  ? 0.3868 0.4809 0.5161 0.0637  -0.0420 -0.0305 18  GLY A C     
184  O  O     . GLY A 38  ? 0.4418 0.5503 0.5795 0.0644  -0.0423 -0.0345 18  GLY A O     
185  N  N     . THR A 39  ? 0.3719 0.4672 0.5001 0.0638  -0.0378 -0.0326 19  THR A N     
186  C  CA    . THR A 39  ? 0.3504 0.4642 0.4874 0.0651  -0.0335 -0.0400 19  THR A CA    
187  C  C     . THR A 39  ? 0.3521 0.4726 0.4842 0.0572  -0.0249 -0.0375 19  THR A C     
188  O  O     . THR A 39  ? 0.4139 0.5483 0.5509 0.0569  -0.0206 -0.0428 19  THR A O     
189  C  CB    . THR A 39  ? 0.3724 0.4842 0.5131 0.0720  -0.0359 -0.0458 19  THR A CB    
190  O  OG1   . THR A 39  ? 0.4307 0.5275 0.5614 0.0698  -0.0343 -0.0409 19  THR A OG1   
191  C  CG2   . THR A 39  ? 0.4237 0.5292 0.5701 0.0803  -0.0455 -0.0491 19  THR A CG2   
192  N  N     . VAL A 40  ? 0.3501 0.4609 0.4725 0.0508  -0.0228 -0.0298 20  VAL A N     
193  C  CA    . VAL A 40  ? 0.3157 0.4320 0.4334 0.0434  -0.0157 -0.0272 20  VAL A CA    
194  C  C     . VAL A 40  ? 0.2884 0.4241 0.4132 0.0401  -0.0129 -0.0309 20  VAL A C     
195  O  O     . VAL A 40  ? 0.2905 0.4317 0.4204 0.0411  -0.0161 -0.0319 20  VAL A O     
196  C  CB    . VAL A 40  ? 0.3874 0.4895 0.4942 0.0379  -0.0149 -0.0189 20  VAL A CB    
197  C  CG1   . VAL A 40  ? 0.4473 0.5485 0.5544 0.0366  -0.0183 -0.0163 20  VAL A CG1   
198  C  CG2   . VAL A 40  ? 0.4075 0.5132 0.5091 0.0308  -0.0087 -0.0165 20  VAL A CG2   
199  N  N     . SER A 41  ? 0.3334 0.4797 0.4581 0.0360  -0.0072 -0.0329 21  SER A N     
200  C  CA    . SER A 41  ? 0.3085 0.4746 0.4390 0.0316  -0.0038 -0.0363 21  SER A CA    
201  C  C     . SER A 41  ? 0.3591 0.5235 0.4844 0.0240  -0.0030 -0.0302 21  SER A C     
202  O  O     . SER A 41  ? 0.3639 0.5170 0.4793 0.0188  -0.0010 -0.0239 21  SER A O     
203  C  CB    . SER A 41  ? 0.3501 0.5261 0.4797 0.0279  0.0021  -0.0391 21  SER A CB    
204  O  OG    . SER A 41  ? 0.3665 0.5588 0.4978 0.0205  0.0060  -0.0399 21  SER A OG    
205  N  N     . LEU A 42  ? 0.3733 0.5491 0.5054 0.0235  -0.0048 -0.0324 22  LEU A N     
206  C  CA    . LEU A 42  ? 0.3303 0.5057 0.4575 0.0157  -0.0040 -0.0271 22  LEU A CA    
207  C  C     . LEU A 42  ? 0.3463 0.5326 0.4705 0.0069  0.0018  -0.0265 22  LEU A C     
208  O  O     . LEU A 42  ? 0.2971 0.4778 0.4136 -0.0004 0.0027  -0.0207 22  LEU A O     
209  C  CB    . LEU A 42  ? 0.2993 0.4838 0.4344 0.0173  -0.0077 -0.0294 22  LEU A CB    
210  C  CG    . LEU A 42  ? 0.3243 0.4971 0.4614 0.0251  -0.0143 -0.0291 22  LEU A CG    
211  C  CD1   . LEU A 42  ? 0.3775 0.5594 0.5218 0.0256  -0.0181 -0.0308 22  LEU A CD1   
212  C  CD2   . LEU A 42  ? 0.3327 0.4831 0.4579 0.0239  -0.0157 -0.0214 22  LEU A CD2   
213  N  N     . GLU A 43  ? 0.2946 0.4957 0.4242 0.0073  0.0052  -0.0325 23  GLU A N     
214  C  CA    . GLU A 43  ? 0.3465 0.5560 0.4713 -0.0016 0.0106  -0.0314 23  GLU A CA    
215  C  C     . GLU A 43  ? 0.2526 0.4440 0.3653 -0.0047 0.0119  -0.0248 23  GLU A C     
216  O  O     . GLU A 43  ? 0.3035 0.4912 0.4082 -0.0131 0.0135  -0.0195 23  GLU A O     
217  C  CB    . GLU A 43  ? 0.3815 0.6102 0.5141 0.0001  0.0141  -0.0397 23  GLU A CB    
218  C  CG    . GLU A 43  ? 0.4805 0.7190 0.6077 -0.0097 0.0197  -0.0388 23  GLU A CG    
219  C  CD    . GLU A 43  ? 0.6602 0.9217 0.7961 -0.0089 0.0235  -0.0479 23  GLU A CD    
220  O  OE1   . GLU A 43  ? 0.6866 0.9548 0.8328 0.0005  0.0215  -0.0553 23  GLU A OE1   
221  O  OE2   . GLU A 43  ? 0.7464 1.0193 0.8786 -0.0178 0.0281  -0.0478 23  GLU A OE2   
222  N  N     . ALA A 44  ? 0.2871 0.4665 0.3983 0.0020  0.0108  -0.0252 24  ALA A N     
223  C  CA    . ALA A 44  ? 0.2388 0.4013 0.3394 -0.0002 0.0117  -0.0193 24  ALA A CA    
224  C  C     . ALA A 44  ? 0.3244 0.4720 0.4178 -0.0028 0.0090  -0.0124 24  ALA A C     
225  O  O     . ALA A 44  ? 0.2363 0.3753 0.3209 -0.0085 0.0103  -0.0073 24  ALA A O     
226  C  CB    . ALA A 44  ? 0.2751 0.4281 0.3761 0.0076  0.0105  -0.0212 24  ALA A CB    
227  N  N     . LEU A 45  ? 0.2546 0.3989 0.3516 0.0014  0.0050  -0.0123 25  LEU A N     
228  C  CA    . LEU A 45  ? 0.2413 0.3723 0.3316 -0.0010 0.0025  -0.0063 25  LEU A CA    
229  C  C     . LEU A 45  ? 0.2555 0.3913 0.3421 -0.0098 0.0039  -0.0034 25  LEU A C     
230  O  O     . LEU A 45  ? 0.2542 0.3783 0.3322 -0.0140 0.0036  0.0018  25  LEU A O     
231  C  CB    . LEU A 45  ? 0.2893 0.4173 0.3842 0.0047  -0.0022 -0.0071 25  LEU A CB    
232  C  CG    . LEU A 45  ? 0.2518 0.3644 0.3394 0.0037  -0.0050 -0.0015 25  LEU A CG    
233  C  CD1   . LEU A 45  ? 0.2353 0.3323 0.3159 0.0063  -0.0050 0.0013  25  LEU A CD1   
234  C  CD2   . LEU A 45  ? 0.2538 0.3667 0.3461 0.0076  -0.0097 -0.0025 25  LEU A CD2   
235  N  N     . GLU A 46  ? 0.2327 0.3861 0.3260 -0.0129 0.0051  -0.0070 26  GLU A N     
236  C  CA    . GLU A 46  ? 0.2575 0.4156 0.3466 -0.0224 0.0061  -0.0039 26  GLU A CA    
237  C  C     . GLU A 46  ? 0.2437 0.3995 0.3250 -0.0288 0.0094  -0.0013 26  GLU A C     
238  O  O     . GLU A 46  ? 0.2500 0.3990 0.3234 -0.0359 0.0088  0.0037  26  GLU A O     
239  C  CB    . GLU A 46  ? 0.2754 0.4546 0.3737 -0.0247 0.0068  -0.0085 26  GLU A CB    
240  C  CG    . GLU A 46  ? 0.3230 0.5062 0.4174 -0.0346 0.0066  -0.0050 26  GLU A CG    
241  C  CD    . GLU A 46  ? 0.4098 0.5983 0.4980 -0.0440 0.0102  -0.0032 26  GLU A CD    
242  O  OE1   . GLU A 46  ? 0.3463 0.5424 0.4363 -0.0430 0.0137  -0.0067 26  GLU A OE1   
243  O  OE2   . GLU A 46  ? 0.4350 0.6197 0.5162 -0.0525 0.0093  0.0016  26  GLU A OE2   
244  N  N     . GLU A 47  ? 0.2469 0.4073 0.3299 -0.0264 0.0123  -0.0046 27  GLU A N     
245  C  CA    . GLU A 47  ? 0.2371 0.3937 0.3120 -0.0322 0.0150  -0.0019 27  GLU A CA    
246  C  C     . GLU A 47  ? 0.2591 0.3945 0.3247 -0.0316 0.0129  0.0038  27  GLU A C     
247  O  O     . GLU A 47  ? 0.2720 0.4011 0.3294 -0.0379 0.0133  0.0078  27  GLU A O     
248  C  CB    . GLU A 47  ? 0.2679 0.4331 0.3464 -0.0291 0.0183  -0.0069 27  GLU A CB    
249  C  CG    . GLU A 47  ? 0.3501 0.5132 0.4203 -0.0358 0.0210  -0.0044 27  GLU A CG    
250  C  CD    . GLU A 47  ? 0.5417 0.7146 0.6155 -0.0331 0.0245  -0.0098 27  GLU A CD    
251  O  OE1   . GLU A 47  ? 0.6678 0.8521 0.7514 -0.0269 0.0250  -0.0162 27  GLU A OE1   
252  O  OE2   . GLU A 47  ? 0.5669 0.7357 0.6336 -0.0371 0.0264  -0.0077 27  GLU A OE2   
253  N  N     . ALA A 48  ? 0.2052 0.3300 0.2722 -0.0241 0.0104  0.0041  28  ALA A N     
254  C  CA    . ALA A 48  ? 0.2186 0.3249 0.2778 -0.0229 0.0087  0.0087  28  ALA A CA    
255  C  C     . ALA A 48  ? 0.2256 0.3235 0.2798 -0.0265 0.0057  0.0130  28  ALA A C     
256  O  O     . ALA A 48  ? 0.2441 0.3295 0.2905 -0.0288 0.0047  0.0168  28  ALA A O     
257  C  CB    . ALA A 48  ? 0.2177 0.3168 0.2797 -0.0141 0.0074  0.0071  28  ALA A CB    
258  N  N     . PHE A 49  ? 0.2155 0.3198 0.2742 -0.0269 0.0040  0.0120  29  PHE A N     
259  C  CA    . PHE A 49  ? 0.2277 0.3233 0.2824 -0.0288 0.0006  0.0155  29  PHE A CA    
260  C  C     . PHE A 49  ? 0.2238 0.3280 0.2786 -0.0364 -0.0001 0.0164  29  PHE A C     
261  O  O     . PHE A 49  ? 0.2498 0.3465 0.3007 -0.0386 -0.0031 0.0193  29  PHE A O     
262  C  CB    . PHE A 49  ? 0.2338 0.3264 0.2928 -0.0218 -0.0019 0.0141  29  PHE A CB    
263  C  CG    . PHE A 49  ? 0.2071 0.2874 0.2634 -0.0157 -0.0023 0.0147  29  PHE A CG    
264  C  CD1   . PHE A 49  ? 0.2102 0.2808 0.2600 -0.0165 -0.0011 0.0169  29  PHE A CD1   
265  C  CD2   . PHE A 49  ? 0.2405 0.3190 0.3007 -0.0095 -0.0044 0.0132  29  PHE A CD2   
266  C  CE1   . PHE A 49  ? 0.2447 0.3052 0.2924 -0.0113 -0.0014 0.0174  29  PHE A CE1   
267  C  CE2   . PHE A 49  ? 0.2495 0.3172 0.3069 -0.0048 -0.0050 0.0141  29  PHE A CE2   
268  C  CZ    . PHE A 49  ? 0.2218 0.2809 0.2729 -0.0058 -0.0033 0.0160  29  PHE A CZ    
269  N  N     . GLY A 50  ? 0.2544 0.3742 0.3132 -0.0407 0.0025  0.0140  30  GLY A N     
270  C  CA    . GLY A 50  ? 0.2808 0.4113 0.3407 -0.0482 0.0020  0.0144  30  GLY A CA    
271  C  C     . GLY A 50  ? 0.2827 0.4053 0.3325 -0.0575 0.0008  0.0196  30  GLY A C     
272  O  O     . GLY A 50  ? 0.2881 0.3962 0.3301 -0.0576 0.0000  0.0227  30  GLY A O     
273  N  N     . PRO A 51  ? 0.2854 0.4173 0.3352 -0.0655 0.0001  0.0204  31  PRO A N     
274  C  CA    . PRO A 51  ? 0.3236 0.4464 0.3631 -0.0750 -0.0023 0.0258  31  PRO A CA    
275  C  C     . PRO A 51  ? 0.3450 0.4647 0.3773 -0.0801 -0.0007 0.0279  31  PRO A C     
276  O  O     . PRO A 51  ? 0.4016 0.5067 0.4241 -0.0848 -0.0039 0.0326  31  PRO A O     
277  C  CB    . PRO A 51  ? 0.3737 0.5113 0.4163 -0.0828 -0.0027 0.0254  31  PRO A CB    
278  C  CG    . PRO A 51  ? 0.3640 0.5118 0.4177 -0.0753 -0.0023 0.0208  31  PRO A CG    
279  C  CD    . PRO A 51  ? 0.3095 0.4594 0.3686 -0.0662 0.0007  0.0167  31  PRO A CD    
280  N  N     . ASP A 52  ? 0.3239 0.4564 0.3605 -0.0794 0.0037  0.0243  32  ASP A N     
281  C  CA    . ASP A 52  ? 0.3390 0.4693 0.3687 -0.0843 0.0054  0.0261  32  ASP A CA    
282  C  C     . ASP A 52  ? 0.3212 0.4414 0.3505 -0.0759 0.0065  0.0252  32  ASP A C     
283  O  O     . ASP A 52  ? 0.3380 0.4580 0.3631 -0.0785 0.0084  0.0256  32  ASP A O     
284  C  CB    . ASP A 52  ? 0.3451 0.4974 0.3789 -0.0904 0.0098  0.0227  32  ASP A CB    
285  C  CG    . ASP A 52  ? 0.4797 0.6430 0.5131 -0.1004 0.0089  0.0240  32  ASP A CG    
286  O  OD1   . ASP A 52  ? 0.5393 0.6903 0.5635 -0.1075 0.0047  0.0297  32  ASP A OD1   
287  O  OD2   . ASP A 52  ? 0.5132 0.6972 0.5557 -0.1009 0.0119  0.0192  32  ASP A OD2   
288  N  N     . SER A 53  ? 0.2747 0.3864 0.3077 -0.0665 0.0052  0.0240  33  SER A N     
289  C  CA    . SER A 53  ? 0.2652 0.3696 0.2992 -0.0582 0.0064  0.0224  33  SER A CA    
290  C  C     . SER A 53  ? 0.2392 0.3241 0.2645 -0.0578 0.0035  0.0267  33  SER A C     
291  O  O     . SER A 53  ? 0.2700 0.3457 0.2884 -0.0630 0.0000  0.0306  33  SER A O     
292  C  CB    . SER A 53  ? 0.2607 0.3661 0.3029 -0.0487 0.0062  0.0191  33  SER A CB    
293  O  OG    . SER A 53  ? 0.2505 0.3431 0.2895 -0.0470 0.0024  0.0219  33  SER A OG    
294  N  N     . LEU A 54  ? 0.2147 0.2934 0.2406 -0.0510 0.0047  0.0255  34  LEU A N     
295  C  CA    . LEU A 54  ? 0.2068 0.2684 0.2265 -0.0482 0.0023  0.0282  34  LEU A CA    
296  C  C     . LEU A 54  ? 0.2322 0.2856 0.2537 -0.0419 0.0001  0.0280  34  LEU A C     
297  O  O     . LEU A 54  ? 0.2343 0.2747 0.2514 -0.0393 -0.0019 0.0296  34  LEU A O     
298  C  CB    . LEU A 54  ? 0.2303 0.2904 0.2502 -0.0443 0.0047  0.0268  34  LEU A CB    
299  C  CG    . LEU A 54  ? 0.2603 0.3267 0.2769 -0.0505 0.0068  0.0271  34  LEU A CG    
300  C  CD1   . LEU A 54  ? 0.2487 0.3148 0.2668 -0.0455 0.0094  0.0250  34  LEU A CD1   
301  C  CD2   . LEU A 54  ? 0.2869 0.3432 0.2939 -0.0579 0.0034  0.0319  34  LEU A CD2   
302  N  N     . GLY A 55  ? 0.2168 0.2780 0.2447 -0.0394 0.0003  0.0258  35  GLY A N     
303  C  CA    . GLY A 55  ? 0.2310 0.2847 0.2598 -0.0341 -0.0019 0.0258  35  GLY A CA    
304  C  C     . GLY A 55  ? 0.2064 0.2533 0.2359 -0.0268 -0.0011 0.0247  35  GLY A C     
305  O  O     . GLY A 55  ? 0.2274 0.2641 0.2540 -0.0239 -0.0031 0.0258  35  GLY A O     
306  N  N     . ILE A 56  ? 0.2050 0.2576 0.2381 -0.0240 0.0017  0.0224  36  ILE A N     
307  C  CA    . ILE A 56  ? 0.1974 0.2436 0.2308 -0.0179 0.0024  0.0216  36  ILE A CA    
308  C  C     . ILE A 56  ? 0.2229 0.2786 0.2630 -0.0141 0.0046  0.0180  36  ILE A C     
309  O  O     . ILE A 56  ? 0.2214 0.2878 0.2643 -0.0167 0.0066  0.0161  36  ILE A O     
310  C  CB    . ILE A 56  ? 0.2120 0.2492 0.2393 -0.0190 0.0027  0.0235  36  ILE A CB    
311  C  CG1   . ILE A 56  ? 0.2273 0.2577 0.2546 -0.0132 0.0031  0.0228  36  ILE A CG1   
312  C  CG2   . ILE A 56  ? 0.2282 0.2717 0.2547 -0.0231 0.0049  0.0232  36  ILE A CG2   
313  C  CD1   . ILE A 56  ? 0.2017 0.2222 0.2232 -0.0137 0.0025  0.0246  36  ILE A CD1   
314  N  N     . LEU A 57  ? 0.1939 0.2455 0.2361 -0.0081 0.0040  0.0169  37  LEU A N     
315  C  CA    . LEU A 57  ? 0.1791 0.2368 0.2273 -0.0034 0.0049  0.0134  37  LEU A CA    
316  C  C     . LEU A 57  ? 0.2483 0.2969 0.2940 0.0006  0.0051  0.0138  37  LEU A C     
317  O  O     . LEU A 57  ? 0.2177 0.2572 0.2602 0.0022  0.0034  0.0158  37  LEU A O     
318  C  CB    . LEU A 57  ? 0.1979 0.2598 0.2517 -0.0001 0.0026  0.0116  37  LEU A CB    
319  C  CG    . LEU A 57  ? 0.1882 0.2547 0.2485 0.0057  0.0021  0.0077  37  LEU A CG    
320  C  CD1   . LEU A 57  ? 0.2128 0.2940 0.2790 0.0047  0.0044  0.0034  37  LEU A CD1   
321  C  CD2   . LEU A 57  ? 0.2443 0.3095 0.3079 0.0095  -0.0016 0.0072  37  LEU A CD2   
322  N  N     . VAL A 58  ? 0.1906 0.2423 0.2379 0.0019  0.0071  0.0117  38  VAL A N     
323  C  CA    . VAL A 58  ? 0.1948 0.2386 0.2400 0.0054  0.0072  0.0120  38  VAL A CA    
324  C  C     . VAL A 58  ? 0.2209 0.2663 0.2712 0.0108  0.0056  0.0091  38  VAL A C     
325  O  O     . VAL A 58  ? 0.2513 0.3063 0.3075 0.0123  0.0059  0.0054  38  VAL A O     
326  C  CB    . VAL A 58  ? 0.2330 0.2779 0.2761 0.0035  0.0099  0.0115  38  VAL A CB    
327  C  CG1   . VAL A 58  ? 0.2388 0.2773 0.2810 0.0073  0.0099  0.0111  38  VAL A CG1   
328  C  CG2   . VAL A 58  ? 0.2521 0.2927 0.2892 -0.0016 0.0102  0.0148  38  VAL A CG2   
329  N  N     . VAL A 59  ? 0.2150 0.2512 0.2631 0.0136  0.0036  0.0106  39  VAL A N     
330  C  CA    . VAL A 59  ? 0.2421 0.2768 0.2937 0.0185  0.0009  0.0087  39  VAL A CA    
331  C  C     . VAL A 59  ? 0.2391 0.2674 0.2882 0.0203  0.0013  0.0087  39  VAL A C     
332  O  O     . VAL A 59  ? 0.2259 0.2463 0.2695 0.0188  0.0017  0.0117  39  VAL A O     
333  C  CB    . VAL A 59  ? 0.2030 0.2317 0.2530 0.0194  -0.0026 0.0108  39  VAL A CB    
334  C  CG1   . VAL A 59  ? 0.2148 0.2400 0.2673 0.0241  -0.0063 0.0094  39  VAL A CG1   
335  C  CG2   . VAL A 59  ? 0.2350 0.2699 0.2873 0.0174  -0.0031 0.0108  39  VAL A CG2   
336  N  N     . LYS A 60  ? 0.2344 0.2666 0.2877 0.0234  0.0012  0.0050  40  LYS A N     
337  C  CA    . LYS A 60  ? 0.2520 0.2783 0.3035 0.0254  0.0010  0.0046  40  LYS A CA    
338  C  C     . LYS A 60  ? 0.2629 0.2835 0.3160 0.0299  -0.0037 0.0036  40  LYS A C     
339  O  O     . LYS A 60  ? 0.2672 0.2888 0.3232 0.0316  -0.0067 0.0032  40  LYS A O     
340  C  CB    . LYS A 60  ? 0.2518 0.2855 0.3060 0.0257  0.0037  0.0009  40  LYS A CB    
341  C  CG    . LYS A 60  ? 0.3227 0.3662 0.3846 0.0294  0.0027  -0.0046 40  LYS A CG    
342  C  CD    . LYS A 60  ? 0.3618 0.4128 0.4256 0.0294  0.0057  -0.0086 40  LYS A CD    
343  C  CE    . LYS A 60  ? 0.4114 0.4727 0.4834 0.0339  0.0045  -0.0152 40  LYS A CE    
344  N  NZ    . LYS A 60  ? 0.6181 0.6878 0.6916 0.0337  0.0078  -0.0196 40  LYS A NZ    
345  N  N     . ASP A 61  ? 0.2926 0.3066 0.3438 0.0316  -0.0047 0.0034  41  ASP A N     
346  C  CA    . ASP A 61  ? 0.2716 0.2777 0.3228 0.0352  -0.0099 0.0031  41  ASP A CA    
347  C  C     . ASP A 61  ? 0.2959 0.2941 0.3423 0.0333  -0.0126 0.0077  41  ASP A C     
348  O  O     . ASP A 61  ? 0.3049 0.3000 0.3526 0.0356  -0.0173 0.0075  41  ASP A O     
349  C  CB    . ASP A 61  ? 0.3130 0.3251 0.3719 0.0402  -0.0131 -0.0021 41  ASP A CB    
350  C  CG    . ASP A 61  ? 0.3355 0.3562 0.3991 0.0423  -0.0105 -0.0074 41  ASP A CG    
351  O  OD1   . ASP A 61  ? 0.3779 0.3945 0.4385 0.0419  -0.0092 -0.0073 41  ASP A OD1   
352  O  OD2   . ASP A 61  ? 0.3386 0.3707 0.4089 0.0441  -0.0098 -0.0118 41  ASP A OD2   
353  N  N     . VAL A 62  ? 0.3083 0.3037 0.3491 0.0290  -0.0098 0.0114  42  VAL A N     
354  C  CA    . VAL A 62  ? 0.3518 0.3416 0.3878 0.0267  -0.0115 0.0153  42  VAL A CA    
355  C  C     . VAL A 62  ? 0.3376 0.3172 0.3688 0.0266  -0.0151 0.0175  42  VAL A C     
356  O  O     . VAL A 62  ? 0.3158 0.2925 0.3471 0.0281  -0.0157 0.0163  42  VAL A O     
357  C  CB    . VAL A 62  ? 0.3556 0.3471 0.3880 0.0227  -0.0073 0.0175  42  VAL A CB    
358  C  CG1   . VAL A 62  ? 0.3436 0.3441 0.3801 0.0222  -0.0047 0.0157  42  VAL A CG1   
359  C  CG2   . VAL A 62  ? 0.3348 0.3232 0.3636 0.0210  -0.0048 0.0185  42  VAL A CG2   
360  N  N     . PRO A 63  ? 0.2914 0.2654 0.3179 0.0246  -0.0178 0.0207  43  PRO A N     
361  C  CA    . PRO A 63  ? 0.3476 0.3117 0.3686 0.0235  -0.0216 0.0232  43  PRO A CA    
362  C  C     . PRO A 63  ? 0.3764 0.3383 0.3937 0.0209  -0.0186 0.0243  43  PRO A C     
363  O  O     . PRO A 63  ? 0.3345 0.3013 0.3515 0.0191  -0.0137 0.0243  43  PRO A O     
364  C  CB    . PRO A 63  ? 0.4341 0.3948 0.4498 0.0203  -0.0235 0.0267  43  PRO A CB    
365  C  CG    . PRO A 63  ? 0.3764 0.3438 0.3968 0.0219  -0.0230 0.0251  43  PRO A CG    
366  C  CD    . PRO A 63  ? 0.3293 0.3053 0.3548 0.0229  -0.0179 0.0223  43  PRO A CD    
367  N  N     . ALA A 64  ? 0.3944 0.3483 0.4086 0.0209  -0.0223 0.0253  44  ALA A N     
368  C  CA    . ALA A 64  ? 0.3629 0.3147 0.3742 0.0188  -0.0200 0.0260  44  ALA A CA    
369  C  C     . ALA A 64  ? 0.3752 0.3282 0.3811 0.0136  -0.0164 0.0289  44  ALA A C     
370  O  O     . ALA A 64  ? 0.3923 0.3480 0.3980 0.0122  -0.0126 0.0285  44  ALA A O     
371  C  CB    . ALA A 64  ? 0.4394 0.3812 0.4476 0.0191  -0.0256 0.0269  44  ALA A CB    
372  N  N     . GLU A 65  ? 0.3819 0.3334 0.3838 0.0109  -0.0177 0.0314  45  GLU A N     
373  C  CA    . GLU A 65  ? 0.3514 0.3051 0.3484 0.0062  -0.0145 0.0334  45  GLU A CA    
374  C  C     . GLU A 65  ? 0.3266 0.2887 0.3270 0.0068  -0.0093 0.0315  45  GLU A C     
375  O  O     . GLU A 65  ? 0.3300 0.2949 0.3278 0.0039  -0.0061 0.0319  45  GLU A O     
376  C  CB    . GLU A 65  ? 0.3940 0.3437 0.3850 0.0028  -0.0177 0.0365  45  GLU A CB    
377  C  CG    . GLU A 65  ? 0.4684 0.4199 0.4618 0.0050  -0.0193 0.0359  45  GLU A CG    
378  C  CD    . GLU A 65  ? 0.6124 0.5575 0.6070 0.0078  -0.0257 0.0362  45  GLU A CD    
379  O  OE1   . GLU A 65  ? 0.4964 0.4368 0.4925 0.0101  -0.0285 0.0354  45  GLU A OE1   
380  O  OE2   . GLU A 65  ? 0.6920 0.6364 0.6859 0.0080  -0.0283 0.0370  45  GLU A OE2   
381  N  N     . PHE A 66  ? 0.2726 0.2387 0.2787 0.0104  -0.0086 0.0291  46  PHE A N     
382  C  CA    . PHE A 66  ? 0.2367 0.2092 0.2451 0.0104  -0.0047 0.0278  46  PHE A CA    
383  C  C     . PHE A 66  ? 0.2854 0.2602 0.2934 0.0092  -0.0011 0.0272  46  PHE A C     
384  O  O     . PHE A 66  ? 0.2462 0.2236 0.2526 0.0075  0.0012  0.0272  46  PHE A O     
385  C  CB    . PHE A 66  ? 0.2800 0.2568 0.2943 0.0136  -0.0046 0.0255  46  PHE A CB    
386  C  CG    . PHE A 66  ? 0.2399 0.2221 0.2559 0.0130  -0.0011 0.0245  46  PHE A CG    
387  C  CD1   . PHE A 66  ? 0.2083 0.1918 0.2227 0.0116  -0.0008 0.0251  46  PHE A CD1   
388  C  CD2   . PHE A 66  ? 0.2484 0.2336 0.2668 0.0137  0.0014  0.0229  46  PHE A CD2   
389  C  CE1   . PHE A 66  ? 0.2259 0.2128 0.2412 0.0110  0.0015  0.0243  46  PHE A CE1   
390  C  CE2   . PHE A 66  ? 0.2190 0.2077 0.2380 0.0127  0.0036  0.0224  46  PHE A CE2   
391  C  CZ    . PHE A 66  ? 0.2332 0.2224 0.2507 0.0115  0.0035  0.0231  46  PHE A CZ    
392  N  N     . ALA A 67  ? 0.2827 0.2564 0.2923 0.0104  -0.0008 0.0263  47  ALA A N     
393  C  CA    . ALA A 67  ? 0.2713 0.2474 0.2812 0.0097  0.0023  0.0255  47  ALA A CA    
394  C  C     . ALA A 67  ? 0.2609 0.2371 0.2667 0.0064  0.0034  0.0268  47  ALA A C     
395  O  O     . ALA A 67  ? 0.2499 0.2298 0.2562 0.0059  0.0060  0.0258  47  ALA A O     
396  C  CB    . ALA A 67  ? 0.3281 0.3023 0.3395 0.0110  0.0018  0.0246  47  ALA A CB    
397  N  N     . GLU A 68  ? 0.2784 0.2506 0.2801 0.0040  0.0013  0.0288  48  GLU A N     
398  C  CA    . GLU A 68  ? 0.3208 0.2948 0.3186 0.0003  0.0029  0.0296  48  GLU A CA    
399  C  C     . GLU A 68  ? 0.2969 0.2749 0.2935 -0.0007 0.0042  0.0291  48  GLU A C     
400  O  O     . GLU A 68  ? 0.2898 0.2727 0.2863 -0.0017 0.0068  0.0277  48  GLU A O     
401  C  CB    . GLU A 68  ? 0.3604 0.3293 0.3531 -0.0033 0.0002  0.0322  48  GLU A CB    
402  C  CG    . GLU A 68  ? 0.4561 0.4287 0.4448 -0.0080 0.0022  0.0328  48  GLU A CG    
403  C  CD    . GLU A 68  ? 0.9318 0.8992 0.9143 -0.0128 -0.0006 0.0360  48  GLU A CD    
404  O  OE1   . GLU A 68  ? 0.9116 0.8714 0.8934 -0.0118 -0.0043 0.0374  48  GLU A OE1   
405  O  OE2   . GLU A 68  ? 0.9940 0.9649 0.9720 -0.0177 0.0006  0.0369  48  GLU A OE2   
406  N  N     . LEU A 69  ? 0.2551 0.2313 0.2512 0.0001  0.0021  0.0299  49  LEU A N     
407  C  CA    . LEU A 69  ? 0.2403 0.2197 0.2349 -0.0009 0.0030  0.0293  49  LEU A CA    
408  C  C     . LEU A 69  ? 0.2332 0.2171 0.2317 0.0014  0.0055  0.0267  49  LEU A C     
409  O  O     . LEU A 69  ? 0.2369 0.2246 0.2344 0.0005  0.0073  0.0251  49  LEU A O     
410  C  CB    . LEU A 69  ? 0.2237 0.2000 0.2174 -0.0004 -0.0001 0.0307  49  LEU A CB    
411  C  CG    . LEU A 69  ? 0.2479 0.2194 0.2359 -0.0036 -0.0033 0.0336  49  LEU A CG    
412  C  CD1   . LEU A 69  ? 0.2525 0.2204 0.2406 -0.0022 -0.0071 0.0347  49  LEU A CD1   
413  C  CD2   . LEU A 69  ? 0.3055 0.2800 0.2878 -0.0082 -0.0017 0.0341  49  LEU A CD2   
414  N  N     . ARG A 70  ? 0.2036 0.1870 0.2063 0.0043  0.0054  0.0260  50  ARG A N     
415  C  CA    . ARG A 70  ? 0.2069 0.1932 0.2125 0.0058  0.0071  0.0240  50  ARG A CA    
416  C  C     . ARG A 70  ? 0.2233 0.2119 0.2287 0.0052  0.0090  0.0227  50  ARG A C     
417  O  O     . ARG A 70  ? 0.2148 0.2060 0.2203 0.0055  0.0099  0.0208  50  ARG A O     
418  C  CB    . ARG A 70  ? 0.2361 0.2221 0.2455 0.0079  0.0068  0.0237  50  ARG A CB    
419  C  CG    . ARG A 70  ? 0.1950 0.1828 0.2063 0.0086  0.0080  0.0223  50  ARG A CG    
420  C  CD    . ARG A 70  ? 0.2052 0.1936 0.2193 0.0096  0.0082  0.0221  50  ARG A CD    
421  N  NE    . ARG A 70  ? 0.2211 0.2101 0.2356 0.0094  0.0089  0.0213  50  ARG A NE    
422  C  CZ    . ARG A 70  ? 0.2295 0.2182 0.2438 0.0094  0.0097  0.0207  50  ARG A CZ    
423  N  NH1   . ARG A 70  ? 0.2258 0.2141 0.2396 0.0093  0.0103  0.0209  50  ARG A NH1   
424  N  NH2   . ARG A 70  ? 0.2167 0.2051 0.2311 0.0093  0.0095  0.0201  50  ARG A NH2   
425  N  N     . HIS A 71  ? 0.2189 0.2066 0.2242 0.0046  0.0094  0.0233  51  HIS A N     
426  C  CA    . HIS A 71  ? 0.2660 0.2565 0.2719 0.0041  0.0111  0.0219  51  HIS A CA    
427  C  C     . HIS A 71  ? 0.2567 0.2512 0.2602 0.0021  0.0121  0.0208  51  HIS A C     
428  O  O     . HIS A 71  ? 0.2384 0.2369 0.2435 0.0029  0.0133  0.0182  51  HIS A O     
429  C  CB    . HIS A 71  ? 0.2290 0.2176 0.2346 0.0032  0.0110  0.0230  51  HIS A CB    
430  C  CG    . HIS A 71  ? 0.2718 0.2635 0.2785 0.0028  0.0125  0.0216  51  HIS A CG    
431  N  ND1   . HIS A 71  ? 0.3562 0.3470 0.3622 0.0012  0.0126  0.0224  51  HIS A ND1   
432  C  CD2   . HIS A 71  ? 0.3050 0.3004 0.3139 0.0040  0.0136  0.0192  51  HIS A CD2   
433  C  CE1   . HIS A 71  ? 0.3287 0.3233 0.3365 0.0012  0.0139  0.0207  51  HIS A CE1   
434  N  NE2   . HIS A 71  ? 0.3181 0.3156 0.3278 0.0032  0.0144  0.0186  51  HIS A NE2   
435  N  N     . ARG A 72  ? 0.2216 0.2154 0.2213 -0.0006 0.0114  0.0225  52  ARG A N     
436  C  CA    . ARG A 72  ? 0.2302 0.2291 0.2271 -0.0033 0.0127  0.0212  52  ARG A CA    
437  C  C     . ARG A 72  ? 0.2233 0.2249 0.2211 -0.0014 0.0130  0.0186  52  ARG A C     
438  O  O     . ARG A 72  ? 0.2256 0.2329 0.2244 -0.0011 0.0145  0.0153  52  ARG A O     
439  C  CB    . ARG A 72  ? 0.2953 0.2923 0.2867 -0.0075 0.0116  0.0241  52  ARG A CB    
440  C  CG    . ARG A 72  ? 0.4708 0.4652 0.4607 -0.0100 0.0110  0.0263  52  ARG A CG    
441  C  CD    . ARG A 72  ? 0.4991 0.4930 0.4824 -0.0157 0.0100  0.0288  52  ARG A CD    
442  N  NE    . ARG A 72  ? 0.6256 0.6146 0.6051 -0.0167 0.0073  0.0312  52  ARG A NE    
443  C  CZ    . ARG A 72  ? 0.8015 0.7936 0.7767 -0.0197 0.0076  0.0312  52  ARG A CZ    
444  N  NH1   . ARG A 72  ? 0.7087 0.7096 0.6831 -0.0220 0.0108  0.0285  52  ARG A NH1   
445  N  NH2   . ARG A 72  ? 0.5781 0.5648 0.5498 -0.0204 0.0045  0.0336  52  ARG A NH2   
446  N  N     . LEU A 73  ? 0.2218 0.2195 0.2196 0.0000  0.0113  0.0197  53  LEU A N     
447  C  CA    . LEU A 73  ? 0.2060 0.2057 0.2037 0.0011  0.0113  0.0175  53  LEU A CA    
448  C  C     . LEU A 73  ? 0.1898 0.1904 0.1914 0.0043  0.0115  0.0146  53  LEU A C     
449  O  O     . LEU A 73  ? 0.2094 0.2133 0.2114 0.0053  0.0117  0.0113  53  LEU A O     
450  C  CB    . LEU A 73  ? 0.1990 0.1947 0.1956 0.0013  0.0092  0.0194  53  LEU A CB    
451  C  CG    . LEU A 73  ? 0.1963 0.1940 0.1912 0.0014  0.0089  0.0172  53  LEU A CG    
452  C  CD1   . LEU A 73  ? 0.2380 0.2401 0.2285 -0.0018 0.0102  0.0163  53  LEU A CD1   
453  C  CD2   . LEU A 73  ? 0.2018 0.1958 0.1965 0.0020  0.0067  0.0189  53  LEU A CD2   
454  N  N     . LEU A 74  ? 0.1868 0.1844 0.1913 0.0059  0.0109  0.0156  54  LEU A N     
455  C  CA    . LEU A 74  ? 0.1899 0.1875 0.1973 0.0084  0.0105  0.0133  54  LEU A CA    
456  C  C     . LEU A 74  ? 0.2185 0.2208 0.2271 0.0088  0.0117  0.0104  54  LEU A C     
457  O  O     . LEU A 74  ? 0.2226 0.2262 0.2329 0.0109  0.0109  0.0071  54  LEU A O     
458  C  CB    . LEU A 74  ? 0.1901 0.1839 0.1994 0.0092  0.0097  0.0152  54  LEU A CB    
459  C  CG    . LEU A 74  ? 0.2111 0.2021 0.2200 0.0089  0.0085  0.0172  54  LEU A CG    
460  C  CD1   . LEU A 74  ? 0.2040 0.1932 0.2149 0.0093  0.0081  0.0184  54  LEU A CD1   
461  C  CD2   . LEU A 74  ? 0.2578 0.2483 0.2657 0.0092  0.0071  0.0161  54  LEU A CD2   
462  N  N     . SER A 75  ? 0.2073 0.2124 0.2151 0.0066  0.0134  0.0113  55  SER A N     
463  C  CA    A SER A 75  ? 0.2105 0.2220 0.2196 0.0064  0.0148  0.0081  55  SER A CA    
464  C  CA    B SER A 75  ? 0.2115 0.2230 0.2206 0.0064  0.0148  0.0082  55  SER A CA    
465  C  C     . SER A 75  ? 0.2464 0.2635 0.2545 0.0062  0.0155  0.0047  55  SER A C     
466  O  O     . SER A 75  ? 0.2047 0.2266 0.2156 0.0085  0.0155  0.0002  55  SER A O     
467  C  CB    A SER A 75  ? 0.2091 0.2226 0.2167 0.0031  0.0163  0.0101  55  SER A CB    
468  C  CB    B SER A 75  ? 0.2100 0.2234 0.2177 0.0031  0.0163  0.0102  55  SER A CB    
469  O  OG    A SER A 75  ? 0.2124 0.2215 0.2214 0.0037  0.0157  0.0123  55  SER A OG    
470  O  OG    B SER A 75  ? 0.1918 0.2130 0.2010 0.0024  0.0179  0.0070  55  SER A OG    
471  N  N     . TYR A 76  ? 0.2188 0.2355 0.2228 0.0038  0.0157  0.0063  56  TYR A N     
472  C  CA    . TYR A 76  ? 0.2000 0.2222 0.2024 0.0033  0.0164  0.0029  56  TYR A CA    
473  C  C     . TYR A 76  ? 0.1999 0.2208 0.2050 0.0077  0.0146  -0.0008 56  TYR A C     
474  O  O     . TYR A 76  ? 0.2079 0.2348 0.2138 0.0089  0.0150  -0.0058 56  TYR A O     
475  C  CB    . TYR A 76  ? 0.1969 0.2170 0.1940 0.0000  0.0161  0.0059  56  TYR A CB    
476  C  CG    . TYR A 76  ? 0.2034 0.2269 0.1960 -0.0053 0.0176  0.0081  56  TYR A CG    
477  C  CD1   . TYR A 76  ? 0.2120 0.2451 0.2032 -0.0079 0.0200  0.0048  56  TYR A CD1   
478  C  CD2   . TYR A 76  ? 0.2288 0.2460 0.2185 -0.0078 0.0163  0.0133  56  TYR A CD2   
479  C  CE1   . TYR A 76  ? 0.2305 0.2665 0.2166 -0.0140 0.0212  0.0073  56  TYR A CE1   
480  C  CE2   . TYR A 76  ? 0.2214 0.2400 0.2060 -0.0132 0.0168  0.0157  56  TYR A CE2   
481  C  CZ    . TYR A 76  ? 0.2302 0.2582 0.2128 -0.0167 0.0193  0.0131  56  TYR A CZ    
482  O  OH    . TYR A 76  ? 0.2531 0.2822 0.2297 -0.0231 0.0195  0.0160  56  TYR A OH    
483  N  N     . SER A 77  ? 0.1916 0.2049 0.1980 0.0098  0.0123  0.0012  57  SER A N     
484  C  CA    . SER A 77  ? 0.1928 0.2034 0.2011 0.0133  0.0098  -0.0019 57  SER A CA    
485  C  C     . SER A 77  ? 0.1946 0.2092 0.2068 0.0164  0.0093  -0.0067 57  SER A C     
486  O  O     . SER A 77  ? 0.1959 0.2124 0.2092 0.0191  0.0078  -0.0115 57  SER A O     
487  C  CB    . SER A 77  ? 0.1999 0.2023 0.2084 0.0140  0.0075  0.0016  57  SER A CB    
488  O  OG    . SER A 77  ? 0.2211 0.2196 0.2300 0.0163  0.0045  -0.0005 57  SER A OG    
489  N  N     . SER A 78  ? 0.2082 0.2240 0.2226 0.0162  0.0102  -0.0058 58  SER A N     
490  C  CA    . SER A 78  ? 0.1914 0.2120 0.2101 0.0191  0.0096  -0.0105 58  SER A CA    
491  C  C     . SER A 78  ? 0.1987 0.2304 0.2181 0.0185  0.0121  -0.0153 58  SER A C     
492  O  O     . SER A 78  ? 0.2232 0.2593 0.2457 0.0221  0.0109  -0.0213 58  SER A O     
493  C  CB    . SER A 78  ? 0.2095 0.2290 0.2301 0.0186  0.0099  -0.0080 58  SER A CB    
494  O  OG    . SER A 78  ? 0.2104 0.2212 0.2314 0.0202  0.0069  -0.0058 58  SER A OG    
495  N  N     . TYR A 79  ? 0.1962 0.2326 0.2124 0.0139  0.0154  -0.0129 59  TYR A N     
496  C  CA    . TYR A 79  ? 0.1939 0.2420 0.2100 0.0121  0.0181  -0.0172 59  TYR A CA    
497  C  C     . TYR A 79  ? 0.1980 0.2486 0.2133 0.0141  0.0174  -0.0219 59  TYR A C     
498  O  O     . TYR A 79  ? 0.2215 0.2807 0.2401 0.0167  0.0177  -0.0287 59  TYR A O     
499  C  CB    . TYR A 79  ? 0.2084 0.2590 0.2194 0.0058  0.0210  -0.0129 59  TYR A CB    
500  C  CG    . TYR A 79  ? 0.1927 0.2439 0.2043 0.0030  0.0221  -0.0097 59  TYR A CG    
501  C  CD1   . TYR A 79  ? 0.2380 0.2978 0.2539 0.0036  0.0234  -0.0135 59  TYR A CD1   
502  C  CD2   . TYR A 79  ? 0.2189 0.2625 0.2266 -0.0002 0.0218  -0.0033 59  TYR A CD2   
503  C  CE1   . TYR A 79  ? 0.2708 0.3310 0.2868 0.0006  0.0243  -0.0105 59  TYR A CE1   
504  C  CE2   . TYR A 79  ? 0.2552 0.2987 0.2630 -0.0028 0.0225  -0.0006 59  TYR A CE2   
505  C  CZ    . TYR A 79  ? 0.2549 0.3066 0.2665 -0.0026 0.0239  -0.0040 59  TYR A CZ    
506  O  OH    . TYR A 79  ? 0.3206 0.3718 0.3319 -0.0055 0.0244  -0.0012 59  TYR A OH    
507  N  N     . LEU A 80  ? 0.1987 0.2419 0.2099 0.0132  0.0162  -0.0186 60  LEU A N     
508  C  CA    . LEU A 80  ? 0.2025 0.2466 0.2123 0.0148  0.0152  -0.0224 60  LEU A CA    
509  C  C     . LEU A 80  ? 0.2560 0.2987 0.2705 0.0210  0.0119  -0.0282 60  LEU A C     
510  O  O     . LEU A 80  ? 0.2102 0.2600 0.2263 0.0234  0.0118  -0.0350 60  LEU A O     
511  C  CB    . LEU A 80  ? 0.2031 0.2379 0.2084 0.0132  0.0136  -0.0173 60  LEU A CB    
512  C  CG    . LEU A 80  ? 0.2074 0.2412 0.2106 0.0147  0.0120  -0.0205 60  LEU A CG    
513  C  CD1   . LEU A 80  ? 0.2577 0.3020 0.2579 0.0119  0.0150  -0.0241 60  LEU A CD1   
514  C  CD2   . LEU A 80  ? 0.2138 0.2380 0.2134 0.0129  0.0103  -0.0146 60  LEU A CD2   
515  N  N     . GLY A 81  ? 0.2437 0.2774 0.2606 0.0235  0.0087  -0.0258 61  GLY A N     
516  C  CA    . GLY A 81  ? 0.2398 0.2696 0.2602 0.0290  0.0044  -0.0304 61  GLY A CA    
517  C  C     . GLY A 81  ? 0.2745 0.3134 0.3005 0.0327  0.0043  -0.0375 61  GLY A C     
518  O  O     . GLY A 81  ? 0.2478 0.2846 0.2768 0.0379  0.0002  -0.0429 61  GLY A O     
519  N  N     . ASN A 82  ? 0.2144 0.2633 0.2417 0.0300  0.0084  -0.0377 62  ASN A N     
520  C  CA    . ASN A 82  ? 0.2131 0.2725 0.2464 0.0331  0.0087  -0.0445 62  ASN A CA    
521  C  C     . ASN A 82  ? 0.2497 0.3243 0.2831 0.0312  0.0129  -0.0500 62  ASN A C     
522  O  O     . ASN A 82  ? 0.2693 0.3557 0.3081 0.0329  0.0140  -0.0560 62  ASN A O     
523  C  CB    . ASN A 82  ? 0.2227 0.2822 0.2582 0.0315  0.0097  -0.0408 62  ASN A CB    
524  C  CG    . ASN A 82  ? 0.3275 0.3750 0.3647 0.0349  0.0048  -0.0384 62  ASN A CG    
525  O  OD1   . ASN A 82  ? 0.4330 0.4808 0.4751 0.0399  0.0012  -0.0433 62  ASN A OD1   
526  N  ND2   . ASN A 82  ? 0.2452 0.2821 0.2781 0.0321  0.0044  -0.0310 62  ASN A ND2   
527  N  N     . LEU A 83  ? 0.2579 0.3334 0.2856 0.0274  0.0151  -0.0484 63  LEU A N     
528  C  CA    . LEU A 83  ? 0.2492 0.3392 0.2760 0.0252  0.0188  -0.0539 63  LEU A CA    
529  C  C     . LEU A 83  ? 0.2971 0.3934 0.3293 0.0319  0.0165  -0.0642 63  LEU A C     
530  O  O     . LEU A 83  ? 0.2633 0.3494 0.2976 0.0376  0.0113  -0.0659 63  LEU A O     
531  C  CB    . LEU A 83  ? 0.2550 0.3423 0.2739 0.0202  0.0205  -0.0499 63  LEU A CB    
532  C  CG    . LEU A 83  ? 0.2863 0.3700 0.2994 0.0130  0.0230  -0.0409 63  LEU A CG    
533  C  CD1   . LEU A 83  ? 0.2979 0.3790 0.3035 0.0088  0.0237  -0.0379 63  LEU A CD1   
534  C  CD2   . LEU A 83  ? 0.2449 0.3405 0.2585 0.0083  0.0270  -0.0412 63  LEU A CD2   
535  N  N     . PRO A 84  ? 0.2785 0.3917 0.3131 0.0313  0.0199  -0.0716 64  PRO A N     
536  C  CA    . PRO A 84  ? 0.3235 0.4440 0.3638 0.0382  0.0176  -0.0825 64  PRO A CA    
537  C  C     . PRO A 84  ? 0.3412 0.4525 0.3777 0.0409  0.0144  -0.0838 64  PRO A C     
538  O  O     . PRO A 84  ? 0.3107 0.4177 0.3398 0.0358  0.0161  -0.0785 64  PRO A O     
539  C  CB    . PRO A 84  ? 0.3022 0.4440 0.3435 0.0347  0.0233  -0.0889 64  PRO A CB    
540  C  CG    . PRO A 84  ? 0.2716 0.4168 0.3107 0.0273  0.0273  -0.0817 64  PRO A CG    
541  C  CD    . PRO A 84  ? 0.2943 0.4214 0.3264 0.0240  0.0258  -0.0705 64  PRO A CD    
542  N  N     . LYS A 85  ? 0.3845 0.4925 0.4263 0.0490  0.0091  -0.0912 65  LYS A N     
543  C  CA    . LYS A 85  ? 0.3956 0.4936 0.4341 0.0520  0.0050  -0.0929 65  LYS A CA    
544  C  C     . LYS A 85  ? 0.3792 0.4870 0.4127 0.0484  0.0091  -0.0962 65  LYS A C     
545  O  O     . LYS A 85  ? 0.3794 0.4778 0.4070 0.0470  0.0075  -0.0931 65  LYS A O     
546  C  CB    . LYS A 85  ? 0.5194 0.6146 0.5648 0.0615  -0.0016 -0.1020 65  LYS A CB    
547  C  CG    . LYS A 85  ? 0.6922 0.7742 0.7340 0.0647  -0.0071 -0.1033 65  LYS A CG    
548  C  CD    . LYS A 85  ? 0.7977 0.8755 0.8459 0.0743  -0.0146 -0.1125 65  LYS A CD    
549  C  CE    . LYS A 85  ? 0.8358 0.8956 0.8794 0.0766  -0.0214 -0.1110 65  LYS A CE    
550  N  NZ    . LYS A 85  ? 0.7281 0.7903 0.7654 0.0734  -0.0186 -0.1118 65  LYS A NZ    
551  N  N     . SER A 86  ? 0.3740 0.5011 0.4095 0.0464  0.0142  -0.1025 66  SER A N     
552  C  CA    . SER A 86  ? 0.4035 0.5411 0.4333 0.0419  0.0185  -0.1054 66  SER A CA    
553  C  C     . SER A 86  ? 0.4444 0.5742 0.4645 0.0334  0.0210  -0.0942 66  SER A C     
554  O  O     . SER A 86  ? 0.4915 0.6193 0.5052 0.0310  0.0213  -0.0939 66  SER A O     
555  C  CB    . SER A 86  ? 0.5289 0.6898 0.5622 0.0397  0.0241  -0.1130 66  SER A CB    
556  O  OG    . SER A 86  ? 0.5629 0.7279 0.5967 0.0343  0.0275  -0.1069 66  SER A OG    
557  N  N     . GLU A 87  ? 0.3715 0.4965 0.3905 0.0289  0.0224  -0.0852 67  GLU A N     
558  C  CA    . GLU A 87  ? 0.3577 0.4744 0.3682 0.0216  0.0240  -0.0748 67  GLU A CA    
559  C  C     . GLU A 87  ? 0.2784 0.3764 0.2865 0.0241  0.0191  -0.0694 67  GLU A C     
560  O  O     . GLU A 87  ? 0.3636 0.4563 0.3649 0.0204  0.0192  -0.0652 67  GLU A O     
561  C  CB    . GLU A 87  ? 0.3869 0.5040 0.3971 0.0165  0.0265  -0.0676 67  GLU A CB    
562  C  CG    . GLU A 87  ? 0.4035 0.5386 0.4130 0.0108  0.0320  -0.0704 67  GLU A CG    
563  C  CD    . GLU A 87  ? 0.5946 0.7274 0.6020 0.0049  0.0339  -0.0620 67  GLU A CD    
564  O  OE1   . GLU A 87  ? 0.4576 0.5774 0.4594 0.0015  0.0326  -0.0530 67  GLU A OE1   
565  O  OE2   . GLU A 87  ? 0.5388 0.6827 0.5506 0.0038  0.0362  -0.0647 67  GLU A OE2   
566  N  N     . LEU A 88  ? 0.3209 0.4088 0.3343 0.0299  0.0146  -0.0692 68  LEU A N     
567  C  CA    . LEU A 88  ? 0.2845 0.3554 0.2954 0.0313  0.0100  -0.0637 68  LEU A CA    
568  C  C     . LEU A 88  ? 0.3269 0.3950 0.3355 0.0341  0.0072  -0.0687 68  LEU A C     
569  O  O     . LEU A 88  ? 0.3196 0.3774 0.3233 0.0321  0.0053  -0.0636 68  LEU A O     
570  C  CB    . LEU A 88  ? 0.3247 0.3859 0.3409 0.0360  0.0057  -0.0623 68  LEU A CB    
571  C  CG    . LEU A 88  ? 0.2984 0.3590 0.3162 0.0331  0.0078  -0.0559 68  LEU A CG    
572  C  CD1   . LEU A 88  ? 0.3267 0.3778 0.3490 0.0378  0.0031  -0.0553 68  LEU A CD1   
573  C  CD2   . LEU A 88  ? 0.3197 0.3740 0.3313 0.0268  0.0098  -0.0464 68  LEU A CD2   
574  N  N     . ASP A 89  ? 0.3224 0.4000 0.3346 0.0387  0.0068  -0.0791 69  ASP A N     
575  C  CA    . ASP A 89  ? 0.3069 0.3819 0.3168 0.0416  0.0039  -0.0847 69  ASP A CA    
576  C  C     . ASP A 89  ? 0.3600 0.4380 0.3618 0.0350  0.0073  -0.0814 69  ASP A C     
577  O  O     . ASP A 89  ? 0.3828 0.4521 0.3804 0.0354  0.0044  -0.0807 69  ASP A O     
578  C  CB    . ASP A 89  ? 0.3915 0.4786 0.4072 0.0478  0.0032  -0.0975 69  ASP A CB    
579  C  CG    . ASP A 89  ? 0.3986 0.4792 0.4220 0.0557  -0.0026 -0.1016 69  ASP A CG    
580  O  OD1   . ASP A 89  ? 0.5287 0.5937 0.5517 0.0563  -0.0069 -0.0947 69  ASP A OD1   
581  O  OD2   . ASP A 89  ? 0.5148 0.6061 0.5444 0.0613  -0.0033 -0.1121 69  ASP A OD2   
582  N  N     . ARG A 90  ? 0.3689 0.4582 0.3677 0.0287  0.0132  -0.0791 70  ARG A N     
583  C  CA    . ARG A 90  ? 0.3478 0.4388 0.3381 0.0217  0.0159  -0.0749 70  ARG A CA    
584  C  C     . ARG A 90  ? 0.4064 0.4822 0.3921 0.0185  0.0138  -0.0642 70  ARG A C     
585  O  O     . ARG A 90  ? 0.3813 0.4557 0.3600 0.0139  0.0144  -0.0610 70  ARG A O     
586  C  CB    . ARG A 90  ? 0.5112 0.6169 0.4987 0.0150  0.0220  -0.0743 70  ARG A CB    
587  C  CG    . ARG A 90  ? 0.6467 0.7706 0.6374 0.0167  0.0250  -0.0856 70  ARG A CG    
588  C  CD    . ARG A 90  ? 0.7198 0.8586 0.7063 0.0084  0.0310  -0.0844 70  ARG A CD    
589  N  NE    . ARG A 90  ? 1.0259 1.1839 1.0148 0.0095  0.0343  -0.0959 70  ARG A NE    
590  C  CZ    . ARG A 90  ? 1.0471 1.2126 1.0306 0.0073  0.0358  -0.1009 70  ARG A CZ    
591  N  NH1   . ARG A 90  ? 1.0169 1.1720 0.9920 0.0038  0.0342  -0.0952 70  ARG A NH1   
592  N  NH2   . ARG A 90  ? 0.9577 1.1421 0.9443 0.0088  0.0388  -0.1123 70  ARG A NH2   
593  N  N     . LEU A 91  ? 0.3238 0.3889 0.3132 0.0207  0.0111  -0.0590 71  LEU A N     
594  C  CA    . LEU A 91  ? 0.3270 0.3794 0.3130 0.0178  0.0092  -0.0495 71  LEU A CA    
595  C  C     . LEU A 91  ? 0.3155 0.3554 0.3022 0.0218  0.0038  -0.0495 71  LEU A C     
596  O  O     . LEU A 91  ? 0.3131 0.3430 0.2977 0.0198  0.0020  -0.0423 71  LEU A O     
597  C  CB    . LEU A 91  ? 0.3112 0.3604 0.3003 0.0167  0.0101  -0.0433 71  LEU A CB    
598  C  CG    . LEU A 91  ? 0.3228 0.3828 0.3110 0.0121  0.0150  -0.0422 71  LEU A CG    
599  C  CD1   . LEU A 91  ? 0.3621 0.4175 0.3534 0.0116  0.0151  -0.0364 71  LEU A CD1   
600  C  CD2   . LEU A 91  ? 0.3604 0.4231 0.3407 0.0052  0.0173  -0.0383 71  LEU A CD2   
601  N  N     . GLU A 92  ? 0.3581 0.3985 0.3473 0.0272  0.0010  -0.0576 72  GLU A N     
602  C  CA    . GLU A 92  ? 0.3999 0.4275 0.3890 0.0306  -0.0049 -0.0576 72  GLU A CA    
603  C  C     . GLU A 92  ? 0.4141 0.4401 0.3970 0.0281  -0.0055 -0.0578 72  GLU A C     
604  O  O     . GLU A 92  ? 0.4560 0.4923 0.4361 0.0266  -0.0025 -0.0625 72  GLU A O     
605  C  CB    . GLU A 92  ? 0.4223 0.4496 0.4169 0.0378  -0.0087 -0.0663 72  GLU A CB    
606  C  CG    . GLU A 92  ? 0.4711 0.4969 0.4716 0.0404  -0.0095 -0.0651 72  GLU A CG    
607  C  CD    . GLU A 92  ? 0.6591 0.6805 0.6646 0.0477  -0.0153 -0.0724 72  GLU A CD    
608  O  OE1   . GLU A 92  ? 0.6503 0.6667 0.6544 0.0509  -0.0196 -0.0773 72  GLU A OE1   
609  O  OE2   . GLU A 92  ? 0.6333 0.6561 0.6442 0.0505  -0.0159 -0.0734 72  GLU A OE2   
610  N  N     . ASN A 93  ? 0.3276 0.3414 0.3083 0.0272  -0.0093 -0.0525 73  ASN A N     
611  C  CA    . ASN A 93  ? 0.3375 0.3484 0.3124 0.0249  -0.0107 -0.0522 73  ASN A CA    
612  C  C     . ASN A 93  ? 0.3072 0.3049 0.2823 0.0277  -0.0172 -0.0522 73  ASN A C     
613  O  O     . ASN A 93  ? 0.3273 0.3161 0.3019 0.0254  -0.0192 -0.0450 73  ASN A O     
614  C  CB    . ASN A 93  ? 0.3702 0.3810 0.3407 0.0185  -0.0081 -0.0438 73  ASN A CB    
615  C  CG    . ASN A 93  ? 0.5158 0.5245 0.4801 0.0159  -0.0095 -0.0436 73  ASN A CG    
616  O  OD1   . ASN A 93  ? 0.4287 0.4322 0.3922 0.0186  -0.0134 -0.0478 73  ASN A OD1   
617  N  ND2   . ASN A 93  ? 0.5093 0.5214 0.4690 0.0105  -0.0068 -0.0386 73  ASN A ND2   
618  N  N     . GLU A 94  ? 0.3739 0.3708 0.3498 0.0325  -0.0205 -0.0605 74  GLU A N     
619  C  CA    . GLU A 94  ? 0.3546 0.3380 0.3301 0.0351  -0.0275 -0.0610 74  GLU A CA    
620  C  C     . GLU A 94  ? 0.3801 0.3575 0.3499 0.0311  -0.0293 -0.0570 74  GLU A C     
621  O  O     . GLU A 94  ? 0.3668 0.3325 0.3358 0.0303  -0.0341 -0.0528 74  GLU A O     
622  C  CB    . GLU A 94  ? 0.3791 0.3630 0.3569 0.0418  -0.0313 -0.0718 74  GLU A CB    
623  C  CG    . GLU A 94  ? 0.4819 0.4504 0.4591 0.0448  -0.0396 -0.0728 74  GLU A CG    
624  C  CD    . GLU A 94  ? 0.6232 0.5918 0.6027 0.0521  -0.0441 -0.0842 74  GLU A CD    
625  O  OE1   . GLU A 94  ? 0.5308 0.5131 0.5128 0.0547  -0.0400 -0.0918 74  GLU A OE1   
626  O  OE2   . GLU A 94  ? 0.7188 0.6739 0.6977 0.0550  -0.0518 -0.0858 74  GLU A OE2   
627  N  N     . LYS A 95  ? 0.3842 0.3695 0.3497 0.0282  -0.0258 -0.0581 75  LYS A N     
628  C  CA    . LYS A 95  ? 0.4248 0.4049 0.3848 0.0242  -0.0275 -0.0541 75  LYS A CA    
629  C  C     . LYS A 95  ? 0.4965 0.4714 0.4567 0.0197  -0.0272 -0.0438 75  LYS A C     
630  O  O     . LYS A 95  ? 0.4080 0.3744 0.3661 0.0177  -0.0310 -0.0400 75  LYS A O     
631  C  CB    . LYS A 95  ? 0.4637 0.4540 0.4186 0.0214  -0.0235 -0.0569 75  LYS A CB    
632  C  CG    . LYS A 95  ? 0.5233 0.5088 0.4723 0.0178  -0.0257 -0.0541 75  LYS A CG    
633  C  CD    . LYS A 95  ? 0.7540 0.7492 0.6974 0.0159  -0.0227 -0.0591 75  LYS A CD    
634  C  CE    . LYS A 95  ? 0.7649 0.7665 0.7045 0.0097  -0.0183 -0.0526 75  LYS A CE    
635  N  NZ    . LYS A 95  ? 0.6131 0.6062 0.5504 0.0059  -0.0209 -0.0441 75  LYS A NZ    
636  N  N     . ALA A 96  ? 0.4673 0.4472 0.4303 0.0182  -0.0231 -0.0396 76  ALA A N     
637  C  CA    . ALA A 96  ? 0.4026 0.3785 0.3667 0.0148  -0.0228 -0.0308 76  ALA A CA    
638  C  C     . ALA A 96  ? 0.4226 0.3898 0.3905 0.0165  -0.0264 -0.0286 76  ALA A C     
639  O  O     . ALA A 96  ? 0.3467 0.3121 0.3165 0.0141  -0.0257 -0.0221 76  ALA A O     
640  C  CB    . ALA A 96  ? 0.4240 0.4079 0.3891 0.0125  -0.0175 -0.0274 76  ALA A CB    
641  N  N     . LYS A 97  ? 0.3460 0.3077 0.3149 0.0205  -0.0306 -0.0340 77  LYS A N     
642  C  CA    . LYS A 97  ? 0.3666 0.3193 0.3381 0.0218  -0.0347 -0.0319 77  LYS A CA    
643  C  C     . LYS A 97  ? 0.2651 0.2217 0.2410 0.0224  -0.0314 -0.0296 77  LYS A C     
644  O  O     . LYS A 97  ? 0.3312 0.2822 0.3088 0.0212  -0.0331 -0.0249 77  LYS A O     
645  C  CB    . LYS A 97  ? 0.4221 0.3666 0.3916 0.0176  -0.0380 -0.0254 77  LYS A CB    
646  C  CG    . LYS A 97  ? 0.5267 0.4674 0.4916 0.0164  -0.0413 -0.0273 77  LYS A CG    
647  C  CD    . LYS A 97  ? 0.5517 0.4826 0.5150 0.0128  -0.0462 -0.0223 77  LYS A CD    
648  C  CE    . LYS A 97  ? 0.7196 0.6543 0.6830 0.0077  -0.0435 -0.0152 77  LYS A CE    
649  N  NZ    . LYS A 97  ? 0.7588 0.6955 0.7184 0.0057  -0.0436 -0.0157 77  LYS A NZ    
650  N  N     . TYR A 98  ? 0.3185 0.2853 0.2959 0.0238  -0.0267 -0.0329 78  TYR A N     
651  C  CA    . TYR A 98  ? 0.3047 0.2765 0.2862 0.0244  -0.0233 -0.0314 78  TYR A CA    
652  C  C     . TYR A 98  ? 0.2797 0.2514 0.2613 0.0200  -0.0207 -0.0230 78  TYR A C     
653  O  O     . TYR A 98  ? 0.3100 0.2824 0.2948 0.0202  -0.0192 -0.0205 78  TYR A O     
654  C  CB    . TYR A 98  ? 0.2972 0.2634 0.2822 0.0286  -0.0271 -0.0342 78  TYR A CB    
655  C  CG    . TYR A 98  ? 0.2916 0.2578 0.2773 0.0339  -0.0304 -0.0433 78  TYR A CG    
656  C  CD1   . TYR A 98  ? 0.3123 0.2899 0.3003 0.0367  -0.0268 -0.0500 78  TYR A CD1   
657  C  CD2   . TYR A 98  ? 0.3653 0.3204 0.3494 0.0359  -0.0373 -0.0455 78  TYR A CD2   
658  C  CE1   . TYR A 98  ? 0.4003 0.3791 0.3895 0.0420  -0.0299 -0.0593 78  TYR A CE1   
659  C  CE2   . TYR A 98  ? 0.3814 0.3360 0.3664 0.0415  -0.0409 -0.0546 78  TYR A CE2   
660  C  CZ    . TYR A 98  ? 0.4153 0.3823 0.4032 0.0448  -0.0371 -0.0617 78  TYR A CZ    
661  O  OH    . TYR A 98  ? 0.4816 0.4494 0.4711 0.0508  -0.0407 -0.0716 78  TYR A OH    
662  N  N     . LEU A 99  ? 0.2717 0.2425 0.2502 0.0164  -0.0205 -0.0191 79  LEU A N     
663  C  CA    . LEU A 99  ? 0.2660 0.2376 0.2451 0.0127  -0.0184 -0.0121 79  LEU A CA    
664  C  C     . LEU A 99  ? 0.2720 0.2516 0.2495 0.0107  -0.0139 -0.0110 79  LEU A C     
665  O  O     . LEU A 99  ? 0.2836 0.2637 0.2609 0.0078  -0.0127 -0.0057 79  LEU A O     
666  C  CB    . LEU A 99  ? 0.3045 0.2700 0.2817 0.0101  -0.0216 -0.0084 79  LEU A CB    
667  C  CG    . LEU A 99  ? 0.3079 0.2651 0.2863 0.0109  -0.0261 -0.0082 79  LEU A CG    
668  C  CD1   . LEU A 99  ? 0.3012 0.2530 0.2776 0.0076  -0.0295 -0.0049 79  LEU A CD1   
669  C  CD2   . LEU A 99  ? 0.3053 0.2622 0.2874 0.0109  -0.0249 -0.0052 79  LEU A CD2   
670  N  N     . THR A 100 ? 0.2596 0.2455 0.2359 0.0120  -0.0118 -0.0161 80  THR A N     
671  C  CA    . THR A 100 ? 0.2491 0.2430 0.2236 0.0096  -0.0075 -0.0154 80  THR A CA    
672  C  C     . THR A 100 ? 0.2572 0.2574 0.2344 0.0124  -0.0053 -0.0207 80  THR A C     
673  O  O     . THR A 100 ? 0.2864 0.2873 0.2646 0.0159  -0.0069 -0.0271 80  THR A O     
674  C  CB    . THR A 100 ? 0.3123 0.3096 0.2811 0.0071  -0.0070 -0.0168 80  THR A CB    
675  O  OG1   . THR A 100 ? 0.3174 0.3096 0.2842 0.0044  -0.0091 -0.0114 80  THR A OG1   
676  C  CG2   . THR A 100 ? 0.3716 0.3777 0.3377 0.0042  -0.0028 -0.0171 80  THR A CG2   
677  N  N     . GLY A 101 ? 0.2328 0.2375 0.2116 0.0110  -0.0020 -0.0184 81  GLY A N     
678  C  CA    . GLY A 101 ? 0.2320 0.2441 0.2138 0.0132  0.0003  -0.0233 81  GLY A CA    
679  C  C     . GLY A 101 ? 0.2477 0.2554 0.2350 0.0173  -0.0018 -0.0244 81  GLY A C     
680  O  O     . GLY A 101 ? 0.2365 0.2367 0.2252 0.0172  -0.0038 -0.0197 81  GLY A O     
681  N  N     . TRP A 102 ? 0.2325 0.2460 0.2230 0.0208  -0.0014 -0.0310 82  TRP A N     
682  C  CA    . TRP A 102 ? 0.2372 0.2478 0.2329 0.0245  -0.0032 -0.0323 82  TRP A CA    
683  C  C     . TRP A 102 ? 0.2790 0.2825 0.2762 0.0293  -0.0087 -0.0369 82  TRP A C     
684  O  O     . TRP A 102 ? 0.3099 0.3151 0.3056 0.0311  -0.0100 -0.0425 82  TRP A O     
685  C  CB    . TRP A 102 ? 0.2273 0.2489 0.2263 0.0256  0.0001  -0.0368 82  TRP A CB    
686  C  CG    . TRP A 102 ? 0.2644 0.2841 0.2691 0.0301  -0.0022 -0.0394 82  TRP A CG    
687  C  CD1   . TRP A 102 ? 0.3113 0.3328 0.3198 0.0357  -0.0051 -0.0473 82  TRP A CD1   
688  C  CD2   . TRP A 102 ? 0.2899 0.3057 0.2971 0.0297  -0.0023 -0.0346 82  TRP A CD2   
689  N  NE1   . TRP A 102 ? 0.3099 0.3279 0.3229 0.0385  -0.0074 -0.0471 82  TRP A NE1   
690  C  CE2   . TRP A 102 ? 0.3106 0.3254 0.3227 0.0347  -0.0054 -0.0393 82  TRP A CE2   
691  C  CE3   . TRP A 102 ? 0.2883 0.3011 0.2940 0.0257  -0.0003 -0.0270 82  TRP A CE3   
692  C  CZ2   . TRP A 102 ? 0.2886 0.2996 0.3036 0.0353  -0.0065 -0.0363 82  TRP A CZ2   
693  C  CZ3   . TRP A 102 ? 0.3163 0.3258 0.3251 0.0265  -0.0010 -0.0244 82  TRP A CZ3   
694  C  CH2   . TRP A 102 ? 0.2869 0.2955 0.3000 0.0310  -0.0040 -0.0288 82  TRP A CH2   
695  N  N     . SER A 103 ? 0.3006 0.2958 0.3003 0.0311  -0.0121 -0.0347 83  SER A N     
696  C  CA    . SER A 103 ? 0.3411 0.3288 0.3423 0.0357  -0.0181 -0.0393 83  SER A CA    
697  C  C     . SER A 103 ? 0.2757 0.2568 0.2799 0.0371  -0.0210 -0.0367 83  SER A C     
698  O  O     . SER A 103 ? 0.3101 0.2913 0.3146 0.0341  -0.0184 -0.0308 83  SER A O     
699  C  CB    . SER A 103 ? 0.3247 0.3030 0.3217 0.0346  -0.0222 -0.0378 83  SER A CB    
700  O  OG    . SER A 103 ? 0.3193 0.2909 0.3145 0.0305  -0.0225 -0.0297 83  SER A OG    
701  N  N     . LEU A 104 ? 0.3478 0.3230 0.3539 0.0419  -0.0267 -0.0416 84  LEU A N     
702  C  CA    . LEU A 104 ? 0.3326 0.3000 0.3409 0.0434  -0.0308 -0.0398 84  LEU A CA    
703  C  C     . LEU A 104 ? 0.3269 0.2798 0.3313 0.0419  -0.0372 -0.0359 84  LEU A C     
704  O  O     . LEU A 104 ? 0.3512 0.2986 0.3533 0.0434  -0.0413 -0.0391 84  LEU A O     
705  C  CB    . LEU A 104 ? 0.3665 0.3366 0.3797 0.0499  -0.0340 -0.0480 84  LEU A CB    
706  C  CG    . LEU A 104 ? 0.4504 0.4338 0.4687 0.0516  -0.0291 -0.0515 84  LEU A CG    
707  C  CD1   . LEU A 104 ? 0.4060 0.3900 0.4296 0.0586  -0.0341 -0.0600 84  LEU A CD1   
708  C  CD2   . LEU A 104 ? 0.4718 0.4552 0.4906 0.0479  -0.0261 -0.0444 84  LEU A CD2   
709  N  N     . GLY A 105 ? 0.3345 0.2814 0.3379 0.0387  -0.0380 -0.0293 85  GLY A N     
710  C  CA    . GLY A 105 ? 0.3787 0.3124 0.3780 0.0362  -0.0440 -0.0251 85  GLY A CA    
711  C  C     . GLY A 105 ? 0.4143 0.3414 0.4144 0.0365  -0.0477 -0.0229 85  GLY A C     
712  O  O     . GLY A 105 ? 0.4093 0.3423 0.4132 0.0385  -0.0452 -0.0241 85  GLY A O     
713  N  N     . LYS A 106 ? 0.4195 0.3340 0.4152 0.0338  -0.0540 -0.0193 86  LYS A N     
714  C  CA    . LYS A 106 ? 0.4941 0.4003 0.4892 0.0336  -0.0590 -0.0170 86  LYS A CA    
715  C  C     . LYS A 106 ? 0.5706 0.4700 0.5604 0.0263  -0.0601 -0.0089 86  LYS A C     
716  O  O     . LYS A 106 ? 0.4843 0.3806 0.4705 0.0225  -0.0608 -0.0064 86  LYS A O     
717  C  CB    . LYS A 106 ? 0.4797 0.3754 0.4746 0.0388  -0.0682 -0.0225 86  LYS A CB    
718  C  CG    . LYS A 106 ? 0.6236 0.5113 0.6184 0.0397  -0.0738 -0.0213 86  LYS A CG    
719  C  CD    . LYS A 106 ? 0.6724 0.5473 0.6660 0.0444  -0.0843 -0.0263 86  LYS A CD    
720  C  CE    . LYS A 106 ? 0.6726 0.5418 0.6682 0.0479  -0.0901 -0.0278 86  LYS A CE    
721  N  NZ    . LYS A 106 ? 0.6428 0.4986 0.6374 0.0532  -0.1013 -0.0332 86  LYS A NZ    
722  N  N     . GLU A 107 ? 0.4988 0.3967 0.4883 0.0241  -0.0602 -0.0051 87  GLU A N     
723  C  CA    . GLU A 107 ? 0.5086 0.4012 0.4931 0.0169  -0.0612 0.0022  87  GLU A CA    
724  C  C     . GLU A 107 ? 0.4909 0.3713 0.4721 0.0164  -0.0693 0.0035  87  GLU A C     
725  O  O     . GLU A 107 ? 0.5042 0.3853 0.4886 0.0205  -0.0702 0.0009  87  GLU A O     
726  C  CB    . GLU A 107 ? 0.5798 0.4837 0.5667 0.0140  -0.0529 0.0058  87  GLU A CB    
727  C  CG    . GLU A 107 ? 0.5039 0.4055 0.4871 0.0074  -0.0527 0.0122  87  GLU A CG    
728  C  CD    . GLU A 107 ? 0.3924 0.3059 0.3788 0.0061  -0.0444 0.0142  87  GLU A CD    
729  O  OE1   . GLU A 107 ? 0.3874 0.3091 0.3764 0.0066  -0.0392 0.0135  87  GLU A OE1   
730  O  OE2   . GLU A 107 ? 0.4195 0.3336 0.4058 0.0046  -0.0436 0.0163  87  GLU A OE2   
731  N  N     . THR A 108 ? 0.5862 0.4551 0.5607 0.0112  -0.0755 0.0075  88  THR A N     
732  C  CA    . THR A 108 ? 0.7421 0.5975 0.7120 0.0098  -0.0843 0.0094  88  THR A CA    
733  C  C     . THR A 108 ? 0.7938 0.6460 0.7572 0.0003  -0.0845 0.0174  88  THR A C     
734  O  O     . THR A 108 ? 0.6785 0.5357 0.6400 -0.0054 -0.0803 0.0210  88  THR A O     
735  C  CB    . THR A 108 ? 0.7624 0.6037 0.7291 0.0125  -0.0943 0.0061  88  THR A CB    
736  O  OG1   . THR A 108 ? 0.7796 0.6199 0.7432 0.0089  -0.0939 0.0075  88  THR A OG1   
737  C  CG2   . THR A 108 ? 0.7071 0.5511 0.6805 0.0226  -0.0955 -0.0028 88  THR A CG2   
738  N  N     . LEU A 109 ? 0.9269 0.7712 0.8869 -0.0015 -0.0895 0.0200  89  LEU A N     
739  C  CA    . LEU A 109 ? 0.9861 0.8277 0.9393 -0.0109 -0.0901 0.0273  89  LEU A CA    
740  C  C     . LEU A 109 ? 0.9257 0.7502 0.8698 -0.0164 -0.1007 0.0308  89  LEU A C     
741  O  O     . LEU A 109 ? 0.8971 0.7204 0.8360 -0.0240 -0.1009 0.0351  89  LEU A O     
742  C  CB    . LEU A 109 ? 0.9464 0.7904 0.9006 -0.0105 -0.0887 0.0285  89  LEU A CB    
743  C  CG    . LEU A 109 ? 1.0587 0.9039 1.0069 -0.0199 -0.0870 0.0354  89  LEU A CG    
744  C  CD1   . LEU A 109 ? 0.9488 0.8094 0.9000 -0.0233 -0.0765 0.0369  89  LEU A CD1   
745  C  CD2   . LEU A 109 ? 0.9256 0.7697 0.8739 -0.0187 -0.0879 0.0358  89  LEU A CD2   
746  N  N     . ASP A 115 ? 0.9482 0.8191 0.9303 0.0194  -0.0774 0.0049  95  ASP A N     
747  C  CA    . ASP A 115 ? 0.9412 0.8116 0.9284 0.0279  -0.0810 -0.0030 95  ASP A CA    
748  C  C     . ASP A 115 ? 0.9303 0.8168 0.9254 0.0325  -0.0724 -0.0075 95  ASP A C     
749  O  O     . ASP A 115 ? 0.9787 0.8687 0.9791 0.0384  -0.0734 -0.0128 95  ASP A O     
750  C  CB    . ASP A 115 ? 0.9434 0.8028 0.9299 0.0310  -0.0903 -0.0045 95  ASP A CB    
751  C  CG    . ASP A 115 ? 1.1082 0.9616 1.0976 0.0388  -0.0976 -0.0122 95  ASP A CG    
752  O  OD1   . ASP A 115 ? 1.0215 0.8772 1.0116 0.0405  -0.0963 -0.0156 95  ASP A OD1   
753  O  OD2   . ASP A 115 ? 1.2151 1.0616 1.2060 0.0433  -0.1050 -0.0153 95  ASP A OD2   
754  N  N     . ASN A 116 ? 0.5663 0.4625 0.5619 0.0295  -0.0643 -0.0055 96  ASN A N     
755  C  CA    . ASN A 116 ? 0.5914 0.5022 0.5926 0.0316  -0.0557 -0.0079 96  ASN A CA    
756  C  C     . ASN A 116 ? 0.4675 0.3847 0.4711 0.0347  -0.0529 -0.0128 96  ASN A C     
757  O  O     . ASN A 116 ? 0.5087 0.4218 0.5089 0.0326  -0.0543 -0.0117 96  ASN A O     
758  C  CB    . ASN A 116 ? 0.6029 0.5199 0.6027 0.0258  -0.0487 -0.0017 96  ASN A CB    
759  C  CG    . ASN A 116 ? 0.7395 0.6564 0.7394 0.0243  -0.0483 0.0011  96  ASN A CG    
760  O  OD1   . ASN A 116 ? 0.7999 0.7147 0.8022 0.0282  -0.0520 -0.0020 96  ASN A OD1   
761  N  ND2   . ASN A 116 ? 0.6619 0.5818 0.6596 0.0189  -0.0439 0.0065  96  ASN A ND2   
762  N  N     . LEU A 117 ? 0.3963 0.3241 0.4055 0.0392  -0.0490 -0.0181 97  LEU A N     
763  C  CA    . LEU A 117 ? 0.3784 0.3148 0.3897 0.0413  -0.0451 -0.0227 97  LEU A CA    
764  C  C     . LEU A 117 ? 0.3067 0.2527 0.3178 0.0371  -0.0367 -0.0187 97  LEU A C     
765  O  O     . LEU A 117 ? 0.3512 0.3019 0.3638 0.0354  -0.0328 -0.0159 97  LEU A O     
766  C  CB    . LEU A 117 ? 0.3588 0.3028 0.3761 0.0479  -0.0454 -0.0309 97  LEU A CB    
767  C  CG    . LEU A 117 ? 0.5056 0.4591 0.5252 0.0507  -0.0422 -0.0373 97  LEU A CG    
768  C  CD1   . LEU A 117 ? 0.4936 0.4381 0.5102 0.0525  -0.0482 -0.0402 97  LEU A CD1   
769  C  CD2   . LEU A 117 ? 0.5188 0.4828 0.5450 0.0561  -0.0412 -0.0449 97  LEU A CD2   
770  N  N     . LYS A 118 ? 0.2964 0.2443 0.3053 0.0352  -0.0343 -0.0182 98  LYS A N     
771  C  CA    . LYS A 118 ? 0.3151 0.2707 0.3234 0.0313  -0.0274 -0.0143 98  LYS A CA    
772  C  C     . LYS A 118 ? 0.3304 0.2927 0.3387 0.0323  -0.0246 -0.0180 98  LYS A C     
773  O  O     . LYS A 118 ? 0.4113 0.3691 0.4173 0.0328  -0.0277 -0.0197 98  LYS A O     
774  C  CB    . LYS A 118 ? 0.3935 0.3437 0.3980 0.0260  -0.0275 -0.0074 98  LYS A CB    
775  C  CG    . LYS A 118 ? 0.4493 0.3896 0.4499 0.0247  -0.0330 -0.0064 98  LYS A CG    
776  C  CD    . LYS A 118 ? 0.3752 0.3120 0.3727 0.0189  -0.0328 0.0004  98  LYS A CD    
777  C  CE    . LYS A 118 ? 0.4820 0.4103 0.4752 0.0163  -0.0377 0.0019  98  LYS A CE    
778  N  NZ    . LYS A 118 ? 0.4789 0.4064 0.4696 0.0102  -0.0367 0.0081  98  LYS A NZ    
779  N  N     . GLY A 119 ? 0.2726 0.2456 0.2830 0.0320  -0.0189 -0.0191 99  GLY A N     
780  C  CA    . GLY A 119 ? 0.2570 0.2372 0.2664 0.0316  -0.0156 -0.0216 99  GLY A CA    
781  C  C     . GLY A 119 ? 0.2290 0.2098 0.2352 0.0268  -0.0123 -0.0158 99  GLY A C     
782  O  O     . GLY A 119 ? 0.2340 0.2155 0.2405 0.0243  -0.0098 -0.0111 99  GLY A O     
783  N  N     . SER A 120 ? 0.2572 0.2373 0.2605 0.0259  -0.0127 -0.0164 100 SER A N     
784  C  CA    . SER A 120 ? 0.2205 0.2012 0.2210 0.0218  -0.0103 -0.0115 100 SER A CA    
785  C  C     . SER A 120 ? 0.2258 0.2146 0.2246 0.0208  -0.0068 -0.0135 100 SER A C     
786  O  O     . SER A 120 ? 0.2332 0.2254 0.2316 0.0229  -0.0072 -0.0191 100 SER A O     
787  C  CB    . SER A 120 ? 0.2714 0.2443 0.2691 0.0205  -0.0141 -0.0095 100 SER A CB    
788  O  OG    . SER A 120 ? 0.3391 0.3044 0.3372 0.0200  -0.0175 -0.0066 100 SER A OG    
789  N  N     . TYR A 121 ? 0.2135 0.2051 0.2110 0.0174  -0.0035 -0.0090 101 TYR A N     
790  C  CA    . TYR A 121 ? 0.2141 0.2118 0.2086 0.0150  -0.0008 -0.0094 101 TYR A CA    
791  C  C     . TYR A 121 ? 0.2139 0.2077 0.2056 0.0120  -0.0015 -0.0043 101 TYR A C     
792  O  O     . TYR A 121 ? 0.2102 0.2017 0.2030 0.0106  -0.0011 0.0004  101 TYR A O     
793  C  CB    . TYR A 121 ? 0.2265 0.2313 0.2215 0.0134  0.0031  -0.0089 101 TYR A CB    
794  C  CG    . TYR A 121 ? 0.2133 0.2236 0.2039 0.0100  0.0054  -0.0087 101 TYR A CG    
795  C  CD1   . TYR A 121 ? 0.2173 0.2346 0.2064 0.0104  0.0066  -0.0144 101 TYR A CD1   
796  C  CD2   . TYR A 121 ? 0.2125 0.2207 0.2001 0.0064  0.0059  -0.0032 101 TYR A CD2   
797  C  CE1   . TYR A 121 ? 0.2394 0.2617 0.2234 0.0065  0.0085  -0.0140 101 TYR A CE1   
798  C  CE2   . TYR A 121 ? 0.2382 0.2502 0.2208 0.0028  0.0072  -0.0026 101 TYR A CE2   
799  C  CZ    . TYR A 121 ? 0.2436 0.2625 0.2239 0.0025  0.0086  -0.0077 101 TYR A CZ    
800  O  OH    . TYR A 121 ? 0.2673 0.2901 0.2418 -0.0019 0.0099  -0.0068 101 TYR A OH    
801  N  N     . TYR A 122 ? 0.2181 0.2117 0.2064 0.0113  -0.0026 -0.0057 102 TYR A N     
802  C  CA    . TYR A 122 ? 0.2403 0.2305 0.2264 0.0087  -0.0039 -0.0015 102 TYR A CA    
803  C  C     . TYR A 122 ? 0.2300 0.2246 0.2119 0.0058  -0.0020 -0.0007 102 TYR A C     
804  O  O     . TYR A 122 ? 0.2240 0.2235 0.2033 0.0056  -0.0008 -0.0047 102 TYR A O     
805  C  CB    . TYR A 122 ? 0.2472 0.2322 0.2322 0.0096  -0.0075 -0.0030 102 TYR A CB    
806  C  CG    . TYR A 122 ? 0.2417 0.2202 0.2293 0.0110  -0.0106 -0.0024 102 TYR A CG    
807  C  CD1   . TYR A 122 ? 0.2880 0.2628 0.2764 0.0090  -0.0119 0.0024  102 TYR A CD1   
808  C  CD2   . TYR A 122 ? 0.2521 0.2283 0.2410 0.0142  -0.0125 -0.0067 102 TYR A CD2   
809  C  CE1   . TYR A 122 ? 0.2776 0.2468 0.2674 0.0092  -0.0147 0.0033  102 TYR A CE1   
810  C  CE2   . TYR A 122 ? 0.2865 0.2557 0.2767 0.0148  -0.0160 -0.0056 102 TYR A CE2   
811  C  CZ    . TYR A 122 ? 0.3126 0.2783 0.3027 0.0119  -0.0170 -0.0004 102 TYR A CZ    
812  O  OH    . TYR A 122 ? 0.3641 0.3231 0.3545 0.0115  -0.0205 0.0009  102 TYR A OH    
813  N  N     . ALA A 123 ? 0.2191 0.2119 0.2001 0.0034  -0.0023 0.0043  103 ALA A N     
814  C  CA    . ALA A 123 ? 0.2226 0.2174 0.1986 0.0002  -0.0019 0.0059  103 ALA A CA    
815  C  C     . ALA A 123 ? 0.2455 0.2360 0.2211 -0.0011 -0.0046 0.0100  103 ALA A C     
816  O  O     . ALA A 123 ? 0.2538 0.2418 0.2335 -0.0002 -0.0054 0.0128  103 ALA A O     
817  C  CB    . ALA A 123 ? 0.2421 0.2404 0.2169 -0.0020 0.0006  0.0079  103 ALA A CB    
818  N  N     . ASN A 124 ? 0.2279 0.2184 0.1989 -0.0031 -0.0059 0.0102  104 ASN A N     
819  C  CA    . ASN A 124 ? 0.2514 0.2387 0.2224 -0.0044 -0.0086 0.0142  104 ASN A CA    
820  C  C     . ASN A 124 ? 0.2343 0.2216 0.2045 -0.0062 -0.0083 0.0181  104 ASN A C     
821  O  O     . ASN A 124 ? 0.2413 0.2311 0.2087 -0.0077 -0.0063 0.0179  104 ASN A O     
822  C  CB    . ASN A 124 ? 0.2506 0.2371 0.2167 -0.0062 -0.0107 0.0135  104 ASN A CB    
823  C  CG    . ASN A 124 ? 0.2634 0.2529 0.2229 -0.0094 -0.0097 0.0135  104 ASN A CG    
824  O  OD1   . ASN A 124 ? 0.2754 0.2638 0.2326 -0.0118 -0.0106 0.0174  104 ASN A OD1   
825  N  ND2   . ASN A 124 ? 0.2478 0.2409 0.2037 -0.0098 -0.0082 0.0089  104 ASN A ND2   
826  N  N     . CYS A 125 ? 0.2293 0.2138 0.2020 -0.0060 -0.0108 0.0215  105 CYS A N     
827  C  CA    . CYS A 125 ? 0.2274 0.2105 0.2000 -0.0069 -0.0117 0.0250  105 CYS A CA    
828  C  C     . CYS A 125 ? 0.2444 0.2251 0.2127 -0.0092 -0.0152 0.0277  105 CYS A C     
829  O  O     . CYS A 125 ? 0.2472 0.2255 0.2175 -0.0087 -0.0179 0.0306  105 CYS A O     
830  C  CB    . CYS A 125 ? 0.2240 0.2065 0.2036 -0.0042 -0.0120 0.0263  105 CYS A CB    
831  S  SG    . CYS A 125 ? 0.2309 0.2154 0.2145 -0.0021 -0.0083 0.0239  105 CYS A SG    
832  N  N     . ALA A 126 ? 0.2444 0.2258 0.2068 -0.0115 -0.0156 0.0265  106 ALA A N     
833  C  CA    . ALA A 126 ? 0.2512 0.2301 0.2082 -0.0144 -0.0192 0.0292  106 ALA A CA    
834  C  C     . ALA A 126 ? 0.2618 0.2383 0.2150 -0.0169 -0.0203 0.0326  106 ALA A C     
835  O  O     . ALA A 126 ? 0.2795 0.2518 0.2304 -0.0181 -0.0246 0.0359  106 ALA A O     
836  C  CB    . ALA A 126 ? 0.2515 0.2323 0.2018 -0.0170 -0.0187 0.0268  106 ALA A CB    
837  N  N     . PHE A 127 ? 0.2487 0.2274 0.2010 -0.0177 -0.0169 0.0318  107 PHE A N     
838  C  CA    . PHE A 127 ? 0.2733 0.2492 0.2215 -0.0206 -0.0180 0.0351  107 PHE A CA    
839  C  C     . PHE A 127 ? 0.2795 0.2500 0.2323 -0.0182 -0.0219 0.0382  107 PHE A C     
840  O  O     . PHE A 127 ? 0.3091 0.2748 0.2575 -0.0207 -0.0251 0.0417  107 PHE A O     
841  C  CB    . PHE A 127 ? 0.2741 0.2541 0.2223 -0.0214 -0.0135 0.0333  107 PHE A CB    
842  C  CG    . PHE A 127 ? 0.2691 0.2506 0.2260 -0.0166 -0.0111 0.0313  107 PHE A CG    
843  C  CD1   . PHE A 127 ? 0.2711 0.2490 0.2325 -0.0145 -0.0125 0.0335  107 PHE A CD1   
844  C  CD2   . PHE A 127 ? 0.2714 0.2575 0.2317 -0.0143 -0.0078 0.0270  107 PHE A CD2   
845  C  CE1   . PHE A 127 ? 0.2306 0.2102 0.1992 -0.0107 -0.0103 0.0316  107 PHE A CE1   
846  C  CE2   . PHE A 127 ? 0.2890 0.2758 0.2563 -0.0105 -0.0061 0.0255  107 PHE A CE2   
847  C  CZ    . PHE A 127 ? 0.2982 0.2820 0.2695 -0.0090 -0.0071 0.0280  107 PHE A CZ    
848  N  N     . TYR A 128 ? 0.2779 0.2492 0.2391 -0.0135 -0.0219 0.0369  108 TYR A N     
849  C  CA    . TYR A 128 ? 0.2549 0.2227 0.2215 -0.0106 -0.0254 0.0387  108 TYR A CA    
850  C  C     . TYR A 128 ? 0.2521 0.2153 0.2155 -0.0117 -0.0313 0.0414  108 TYR A C     
851  O  O     . TYR A 128 ? 0.3100 0.2682 0.2736 -0.0111 -0.0354 0.0438  108 TYR A O     
852  C  CB    . TYR A 128 ? 0.2689 0.2403 0.2445 -0.0063 -0.0240 0.0363  108 TYR A CB    
853  C  CG    . TYR A 128 ? 0.2387 0.2088 0.2209 -0.0029 -0.0270 0.0370  108 TYR A CG    
854  C  CD1   . TYR A 128 ? 0.2618 0.2311 0.2469 -0.0012 -0.0260 0.0370  108 TYR A CD1   
855  C  CD2   . TYR A 128 ? 0.2764 0.2467 0.2622 -0.0012 -0.0309 0.0373  108 TYR A CD2   
856  C  CE1   . TYR A 128 ? 0.2643 0.2329 0.2555 0.0023  -0.0288 0.0369  108 TYR A CE1   
857  C  CE2   . TYR A 128 ? 0.3117 0.2821 0.3042 0.0024  -0.0337 0.0370  108 TYR A CE2   
858  C  CZ    . TYR A 128 ? 0.2845 0.2540 0.2797 0.0042  -0.0326 0.0366  108 TYR A CZ    
859  O  OH    . TYR A 128 ? 0.3039 0.2740 0.3060 0.0082  -0.0354 0.0356  108 TYR A OH    
860  N  N     . VAL A 129 ? 0.2917 0.2561 0.2524 -0.0131 -0.0321 0.0409  109 VAL A N     
861  C  CA    . VAL A 129 ? 0.3161 0.2763 0.2737 -0.0143 -0.0380 0.0434  109 VAL A CA    
862  C  C     . VAL A 129 ? 0.3407 0.2963 0.2875 -0.0197 -0.0402 0.0466  109 VAL A C     
863  O  O     . VAL A 129 ? 0.3775 0.3266 0.3214 -0.0206 -0.0461 0.0499  109 VAL A O     
864  C  CB    . VAL A 129 ? 0.3135 0.2769 0.2719 -0.0141 -0.0379 0.0416  109 VAL A CB    
865  C  CG1   . VAL A 129 ? 0.3849 0.3442 0.3394 -0.0157 -0.0441 0.0442  109 VAL A CG1   
866  C  CG2   . VAL A 129 ? 0.3018 0.2696 0.2705 -0.0097 -0.0364 0.0391  109 VAL A CG2   
867  N  N     . ASP A 130 ? 0.3321 0.2909 0.2727 -0.0235 -0.0358 0.0454  110 ASP A N     
868  C  CA    . ASP A 130 ? 0.3744 0.3306 0.3038 -0.0298 -0.0370 0.0481  110 ASP A CA    
869  C  C     . ASP A 130 ? 0.3507 0.3125 0.2779 -0.0321 -0.0309 0.0459  110 ASP A C     
870  O  O     . ASP A 130 ? 0.3585 0.3270 0.2867 -0.0316 -0.0262 0.0419  110 ASP A O     
871  C  CB    . ASP A 130 ? 0.3683 0.3247 0.2911 -0.0330 -0.0390 0.0483  110 ASP A CB    
872  C  CG    . ASP A 130 ? 0.4404 0.3960 0.3504 -0.0407 -0.0394 0.0506  110 ASP A CG    
873  O  OD1   . ASP A 130 ? 0.4462 0.4021 0.3523 -0.0441 -0.0374 0.0517  110 ASP A OD1   
874  O  OD2   . ASP A 130 ? 0.4830 0.4380 0.3866 -0.0438 -0.0416 0.0512  110 ASP A OD2   
875  N  N     . PRO A 131 ? 0.3944 0.3536 0.3189 -0.0345 -0.0310 0.0483  111 PRO A N     
876  C  CA    . PRO A 131 ? 0.4003 0.3657 0.3246 -0.0360 -0.0251 0.0459  111 PRO A CA    
877  C  C     . PRO A 131 ? 0.3592 0.3317 0.2761 -0.0409 -0.0214 0.0436  111 PRO A C     
878  O  O     . PRO A 131 ? 0.4103 0.3901 0.3289 -0.0409 -0.0160 0.0400  111 PRO A O     
879  C  CB    . PRO A 131 ? 0.4736 0.4333 0.3947 -0.0388 -0.0276 0.0498  111 PRO A CB    
880  C  CG    . PRO A 131 ? 0.5935 0.5442 0.5175 -0.0356 -0.0343 0.0529  111 PRO A CG    
881  C  CD    . PRO A 131 ? 0.5045 0.4547 0.4268 -0.0355 -0.0371 0.0530  111 PRO A CD    
882  N  N     . SER A 132 ? 0.3633 0.3343 0.2723 -0.0450 -0.0241 0.0451  112 SER A N     
883  C  CA    . SER A 132 ? 0.3787 0.3574 0.2804 -0.0500 -0.0205 0.0423  112 SER A CA    
884  C  C     . SER A 132 ? 0.4457 0.4307 0.3523 -0.0457 -0.0172 0.0365  112 SER A C     
885  O  O     . SER A 132 ? 0.3864 0.3791 0.2885 -0.0485 -0.0135 0.0326  112 SER A O     
886  C  CB    . SER A 132 ? 0.4495 0.4240 0.3395 -0.0569 -0.0249 0.0464  112 SER A CB    
887  O  OG    . SER A 132 ? 0.4901 0.4600 0.3813 -0.0543 -0.0291 0.0471  112 SER A OG    
888  N  N     . LEU A 133 ? 0.3304 0.3124 0.2456 -0.0393 -0.0185 0.0355  113 LEU A N     
889  C  CA    . LEU A 133 ? 0.3190 0.3049 0.2379 -0.0358 -0.0167 0.0307  113 LEU A CA    
890  C  C     . LEU A 133 ? 0.3199 0.3120 0.2452 -0.0321 -0.0116 0.0257  113 LEU A C     
891  O  O     . LEU A 133 ? 0.3548 0.3458 0.2864 -0.0291 -0.0107 0.0263  113 LEU A O     
892  C  CB    . LEU A 133 ? 0.3369 0.3173 0.2619 -0.0315 -0.0207 0.0322  113 LEU A CB    
893  C  CG    . LEU A 133 ? 0.3813 0.3559 0.3012 -0.0341 -0.0264 0.0363  113 LEU A CG    
894  C  CD1   . LEU A 133 ? 0.3828 0.3540 0.3106 -0.0292 -0.0298 0.0369  113 LEU A CD1   
895  C  CD2   . LEU A 133 ? 0.4376 0.4147 0.3483 -0.0386 -0.0264 0.0349  113 LEU A CD2   
896  N  N     . SER A 134 ? 0.2924 0.2907 0.2161 -0.0320 -0.0088 0.0203  114 SER A N     
897  C  CA    . SER A 134 ? 0.3026 0.3058 0.2329 -0.0275 -0.0051 0.0149  114 SER A CA    
898  C  C     . SER A 134 ? 0.3262 0.3260 0.2626 -0.0223 -0.0068 0.0128  114 SER A C     
899  O  O     . SER A 134 ? 0.2920 0.2938 0.2340 -0.0183 -0.0049 0.0088  114 SER A O     
900  C  CB    . SER A 134 ? 0.3621 0.3746 0.2880 -0.0296 -0.0014 0.0092  114 SER A CB    
901  O  OG    . SER A 134 ? 0.4486 0.4618 0.3695 -0.0308 -0.0027 0.0068  114 SER A OG    
902  N  N     . CYS A 135 ? 0.2884 0.2829 0.2236 -0.0226 -0.0107 0.0157  115 CYS A N     
903  C  CA    . CYS A 135 ? 0.3060 0.2972 0.2456 -0.0192 -0.0129 0.0145  115 CYS A CA    
904  C  C     . CYS A 135 ? 0.2753 0.2621 0.2114 -0.0214 -0.0173 0.0184  115 CYS A C     
905  O  O     . CYS A 135 ? 0.2728 0.2590 0.2024 -0.0256 -0.0185 0.0213  115 CYS A O     
906  C  CB    . CYS A 135 ? 0.2692 0.2637 0.2080 -0.0175 -0.0116 0.0082  115 CYS A CB    
907  S  SG    . CYS A 135 ? 0.3265 0.3263 0.2549 -0.0223 -0.0106 0.0052  115 CYS A SG    
908  N  N     . ALA A 136 ? 0.2624 0.2461 0.2027 -0.0190 -0.0199 0.0184  116 ALA A N     
909  C  CA    . ALA A 136 ? 0.2898 0.2700 0.2277 -0.0208 -0.0243 0.0216  116 ALA A CA    
910  C  C     . ALA A 136 ? 0.3190 0.3004 0.2475 -0.0247 -0.0248 0.0203  116 ALA A C     
911  O  O     . ALA A 136 ? 0.3045 0.2897 0.2300 -0.0249 -0.0222 0.0155  116 ALA A O     
912  C  CB    . ALA A 136 ? 0.3103 0.2885 0.2539 -0.0181 -0.0264 0.0208  116 ALA A CB    
913  N  N     . LYS A 137 ? 0.3333 0.3116 0.2572 -0.0278 -0.0286 0.0244  117 LYS A N     
914  C  CA    . LYS A 137 ? 0.3978 0.3768 0.3121 -0.0321 -0.0298 0.0237  117 LYS A CA    
915  C  C     . LYS A 137 ? 0.3578 0.3368 0.2731 -0.0304 -0.0308 0.0199  117 LYS A C     
916  O  O     . LYS A 137 ? 0.3662 0.3419 0.2869 -0.0281 -0.0339 0.0214  117 LYS A O     
917  C  CB    . LYS A 137 ? 0.4349 0.4091 0.3445 -0.0355 -0.0348 0.0294  117 LYS A CB    
918  C  CG    . LYS A 137 ? 0.5639 0.5360 0.4718 -0.0375 -0.0353 0.0336  117 LYS A CG    
919  C  CD    . LYS A 137 ? 0.6939 0.6594 0.5993 -0.0392 -0.0419 0.0392  117 LYS A CD    
920  C  CE    . LYS A 137 ? 0.6675 0.6292 0.5696 -0.0418 -0.0437 0.0436  117 LYS A CE    
921  N  NZ    . LYS A 137 ? 0.7670 0.7308 0.6578 -0.0484 -0.0416 0.0440  117 LYS A NZ    
922  N  N     . PRO A 138 ? 0.3352 0.3180 0.2454 -0.0313 -0.0284 0.0148  118 PRO A N     
923  C  CA    . PRO A 138 ? 0.3401 0.3220 0.2516 -0.0292 -0.0296 0.0107  118 PRO A CA    
924  C  C     . PRO A 138 ? 0.3632 0.3416 0.2698 -0.0318 -0.0342 0.0128  118 PRO A C     
925  O  O     . PRO A 138 ? 0.3811 0.3594 0.2801 -0.0362 -0.0357 0.0155  118 PRO A O     
926  C  CB    . PRO A 138 ? 0.3803 0.3679 0.2875 -0.0292 -0.0257 0.0039  118 PRO A CB    
927  C  CG    . PRO A 138 ? 0.4141 0.4060 0.3142 -0.0339 -0.0235 0.0055  118 PRO A CG    
928  C  CD    . PRO A 138 ? 0.3941 0.3829 0.2976 -0.0344 -0.0245 0.0120  118 PRO A CD    
929  N  N     . THR A 139 ? 0.3093 0.2846 0.2201 -0.0295 -0.0368 0.0117  119 THR A N     
930  C  CA    . THR A 139 ? 0.3461 0.3185 0.2529 -0.0317 -0.0413 0.0128  119 THR A CA    
931  C  C     . THR A 139 ? 0.3354 0.3069 0.2418 -0.0301 -0.0418 0.0073  119 THR A C     
932  O  O     . THR A 139 ? 0.3670 0.3391 0.2775 -0.0268 -0.0395 0.0033  119 THR A O     
933  C  CB    . THR A 139 ? 0.3498 0.3188 0.2628 -0.0311 -0.0455 0.0181  119 THR A CB    
934  O  OG1   . THR A 139 ? 0.3233 0.2916 0.2452 -0.0275 -0.0452 0.0170  119 THR A OG1   
935  C  CG2   . THR A 139 ? 0.3672 0.3360 0.2814 -0.0318 -0.0459 0.0232  119 THR A CG2   
936  N  N     . GLU A 140 ? 0.3270 0.2964 0.2281 -0.0325 -0.0454 0.0071  120 GLU A N     
937  C  CA    . GLU A 140 ? 0.3547 0.3219 0.2553 -0.0310 -0.0468 0.0021  120 GLU A CA    
938  C  C     . GLU A 140 ? 0.4168 0.3807 0.3266 -0.0278 -0.0481 0.0027  120 GLU A C     
939  O  O     . GLU A 140 ? 0.3947 0.3568 0.3060 -0.0252 -0.0476 -0.0020 120 GLU A O     
940  C  CB    . GLU A 140 ? 0.4073 0.3722 0.3015 -0.0343 -0.0511 0.0027  120 GLU A CB    
941  C  CG    . GLU A 140 ? 0.5178 0.4790 0.4118 -0.0329 -0.0535 -0.0019 120 GLU A CG    
942  C  CD    . GLU A 140 ? 0.8347 0.7935 0.7224 -0.0363 -0.0580 -0.0012 120 GLU A CD    
943  O  OE1   . GLU A 140 ? 0.8597 0.8190 0.7445 -0.0395 -0.0599 0.0037  120 GLU A OE1   
944  O  OE2   . GLU A 140 ? 1.0454 1.0011 0.9309 -0.0357 -0.0602 -0.0056 120 GLU A OE2   
945  N  N     . GLU A 141 ? 0.3541 0.3172 0.2700 -0.0280 -0.0498 0.0083  121 GLU A N     
946  C  CA    . GLU A 141 ? 0.3282 0.2891 0.2522 -0.0260 -0.0510 0.0092  121 GLU A CA    
947  C  C     . GLU A 141 ? 0.3425 0.3046 0.2716 -0.0228 -0.0471 0.0078  121 GLU A C     
948  O  O     . GLU A 141 ? 0.3840 0.3434 0.3166 -0.0211 -0.0476 0.0059  121 GLU A O     
949  C  CB    . GLU A 141 ? 0.3546 0.3163 0.2840 -0.0271 -0.0539 0.0148  121 GLU A CB    
950  C  CG    . GLU A 141 ? 0.4268 0.3877 0.3642 -0.0262 -0.0551 0.0158  121 GLU A CG    
951  C  CD    . GLU A 141 ? 0.4542 0.4179 0.3978 -0.0272 -0.0578 0.0203  121 GLU A CD    
952  O  OE1   . GLU A 141 ? 0.4998 0.4654 0.4430 -0.0273 -0.0584 0.0230  121 GLU A OE1   
953  O  OE2   . GLU A 141 ? 0.4824 0.4465 0.4312 -0.0278 -0.0597 0.0211  121 GLU A OE2   
954  N  N     . PHE A 142 ? 0.3221 0.2877 0.2513 -0.0224 -0.0437 0.0090  122 PHE A N     
955  C  CA    . PHE A 142 ? 0.3005 0.2675 0.2349 -0.0196 -0.0401 0.0083  122 PHE A CA    
956  C  C     . PHE A 142 ? 0.2870 0.2577 0.2169 -0.0194 -0.0361 0.0056  122 PHE A C     
957  O  O     . PHE A 142 ? 0.2950 0.2681 0.2225 -0.0214 -0.0350 0.0085  122 PHE A O     
958  C  CB    . PHE A 142 ? 0.3077 0.2758 0.2490 -0.0192 -0.0400 0.0134  122 PHE A CB    
959  C  CG    . PHE A 142 ? 0.3164 0.2830 0.2629 -0.0196 -0.0434 0.0158  122 PHE A CG    
960  C  CD1   . PHE A 142 ? 0.3570 0.3212 0.3063 -0.0188 -0.0442 0.0139  122 PHE A CD1   
961  C  CD2   . PHE A 142 ? 0.3319 0.3000 0.2808 -0.0209 -0.0461 0.0198  122 PHE A CD2   
962  C  CE1   . PHE A 142 ? 0.3339 0.2977 0.2878 -0.0202 -0.0471 0.0162  122 PHE A CE1   
963  C  CE2   . PHE A 142 ? 0.3836 0.3522 0.3380 -0.0215 -0.0489 0.0215  122 PHE A CE2   
964  C  CZ    . PHE A 142 ? 0.2915 0.2583 0.2482 -0.0215 -0.0491 0.0198  122 PHE A CZ    
965  N  N     . ASN A 143 ? 0.3005 0.2718 0.2299 -0.0171 -0.0341 0.0000  123 ASN A N     
966  C  CA    . ASN A 143 ? 0.3202 0.2969 0.2456 -0.0171 -0.0302 -0.0037 123 ASN A CA    
967  C  C     . ASN A 143 ? 0.3450 0.3223 0.2749 -0.0130 -0.0281 -0.0084 123 ASN A C     
968  O  O     . ASN A 143 ? 0.3511 0.3235 0.2857 -0.0106 -0.0303 -0.0087 123 ASN A O     
969  C  CB    . ASN A 143 ? 0.3578 0.3364 0.2748 -0.0194 -0.0308 -0.0075 123 ASN A CB    
970  C  CG    . ASN A 143 ? 0.4104 0.3847 0.3269 -0.0175 -0.0339 -0.0120 123 ASN A CG    
971  O  OD1   . ASN A 143 ? 0.4255 0.3992 0.3446 -0.0138 -0.0334 -0.0173 123 ASN A OD1   
972  N  ND2   . ASN A 143 ? 0.4059 0.3768 0.3190 -0.0200 -0.0377 -0.0100 123 ASN A ND2   
973  N  N     . PRO A 144 ? 0.3090 0.2923 0.2373 -0.0123 -0.0242 -0.0121 124 PRO A N     
974  C  CA    . PRO A 144 ? 0.3721 0.3564 0.3051 -0.0079 -0.0226 -0.0171 124 PRO A CA    
975  C  C     . PRO A 144 ? 0.3883 0.3686 0.3211 -0.0048 -0.0256 -0.0233 124 PRO A C     
976  O  O     . PRO A 144 ? 0.4203 0.3983 0.3579 -0.0008 -0.0262 -0.0263 124 PRO A O     
977  C  CB    . PRO A 144 ? 0.3681 0.3615 0.2985 -0.0088 -0.0180 -0.0203 124 PRO A CB    
978  C  CG    . PRO A 144 ? 0.3548 0.3500 0.2814 -0.0136 -0.0170 -0.0142 124 PRO A CG    
979  C  CD    . PRO A 144 ? 0.3255 0.3153 0.2487 -0.0159 -0.0211 -0.0110 124 PRO A CD    
980  N  N     . ASP A 145 ? 0.4187 0.3974 0.3461 -0.0063 -0.0281 -0.0253 125 ASP A N     
981  C  CA    . ASP A 145 ? 0.3877 0.3619 0.3148 -0.0030 -0.0315 -0.0317 125 ASP A CA    
982  C  C     . ASP A 145 ? 0.4466 0.4108 0.3772 -0.0024 -0.0363 -0.0283 125 ASP A C     
983  O  O     . ASP A 145 ? 0.5161 0.4749 0.4490 0.0010  -0.0391 -0.0322 125 ASP A O     
984  C  CB    . ASP A 145 ? 0.4248 0.4010 0.3443 -0.0048 -0.0323 -0.0360 125 ASP A CB    
985  C  CG    . ASP A 145 ? 0.5643 0.5514 0.4801 -0.0053 -0.0276 -0.0411 125 ASP A CG    
986  O  OD1   . ASP A 145 ? 0.6498 0.6418 0.5696 -0.0022 -0.0247 -0.0450 125 ASP A OD1   
987  O  OD2   . ASP A 145 ? 0.7584 0.7496 0.6671 -0.0093 -0.0268 -0.0412 125 ASP A OD2   
988  N  N     . ASN A 146 ? 0.3588 0.3206 0.2899 -0.0060 -0.0376 -0.0211 126 ASN A N     
989  C  CA    . ASN A 146 ? 0.3644 0.3183 0.2988 -0.0062 -0.0418 -0.0179 126 ASN A CA    
990  C  C     . ASN A 146 ? 0.3687 0.3224 0.3097 -0.0060 -0.0405 -0.0129 126 ASN A C     
991  O  O     . ASN A 146 ? 0.3954 0.3432 0.3392 -0.0059 -0.0436 -0.0114 126 ASN A O     
992  C  CB    . ASN A 146 ? 0.3469 0.2984 0.2784 -0.0101 -0.0451 -0.0142 126 ASN A CB    
993  C  CG    . ASN A 146 ? 0.3961 0.3528 0.3272 -0.0132 -0.0431 -0.0087 126 ASN A CG    
994  O  OD1   . ASN A 146 ? 0.4087 0.3705 0.3408 -0.0129 -0.0392 -0.0075 126 ASN A OD1   
995  N  ND2   . ASN A 146 ? 0.5119 0.4668 0.4415 -0.0163 -0.0463 -0.0053 126 ASN A ND2   
996  N  N     . PHE A 147 ? 0.3383 0.2981 0.2813 -0.0061 -0.0362 -0.0104 127 PHE A N     
997  C  CA    . PHE A 147 ? 0.3568 0.3168 0.3058 -0.0055 -0.0346 -0.0066 127 PHE A CA    
998  C  C     . PHE A 147 ? 0.3224 0.2877 0.2728 -0.0032 -0.0302 -0.0088 127 PHE A C     
999  O  O     . PHE A 147 ? 0.3052 0.2744 0.2576 -0.0042 -0.0274 -0.0051 127 PHE A O     
1000 C  CB    . PHE A 147 ? 0.3190 0.2806 0.2704 -0.0084 -0.0347 0.0000  127 PHE A CB    
1001 C  CG    . PHE A 147 ? 0.3327 0.2900 0.2851 -0.0105 -0.0389 0.0026  127 PHE A CG    
1002 C  CD1   . PHE A 147 ? 0.3600 0.3146 0.3171 -0.0107 -0.0401 0.0047  127 PHE A CD1   
1003 C  CD2   . PHE A 147 ? 0.3563 0.3127 0.3048 -0.0129 -0.0416 0.0029  127 PHE A CD2   
1004 C  CE1   . PHE A 147 ? 0.3967 0.3483 0.3546 -0.0135 -0.0438 0.0071  127 PHE A CE1   
1005 C  CE2   . PHE A 147 ? 0.3788 0.3321 0.3286 -0.0152 -0.0454 0.0053  127 PHE A CE2   
1006 C  CZ    . PHE A 147 ? 0.3981 0.3493 0.3527 -0.0157 -0.0465 0.0073  127 PHE A CZ    
1007 N  N     . PRO A 148 ? 0.3258 0.2911 0.2755 0.0000  -0.0300 -0.0151 128 PRO A N     
1008 C  CA    . PRO A 148 ? 0.3624 0.3340 0.3139 0.0021  -0.0258 -0.0177 128 PRO A CA    
1009 C  C     . PRO A 148 ? 0.3193 0.2902 0.2765 0.0029  -0.0244 -0.0139 128 PRO A C     
1010 O  O     . PRO A 148 ? 0.3448 0.3213 0.3034 0.0032  -0.0206 -0.0138 128 PRO A O     
1011 C  CB    . PRO A 148 ? 0.3605 0.3316 0.3114 0.0060  -0.0270 -0.0259 128 PRO A CB    
1012 C  CG    . PRO A 148 ? 0.3881 0.3495 0.3388 0.0067  -0.0326 -0.0261 128 PRO A CG    
1013 C  CD    . PRO A 148 ? 0.3688 0.3284 0.3169 0.0023  -0.0340 -0.0204 128 PRO A CD    
1014 N  N     . GLU A 149 ? 0.3399 0.3043 0.3000 0.0028  -0.0274 -0.0109 129 GLU A N     
1015 C  CA    . GLU A 149 ? 0.3358 0.2999 0.3010 0.0035  -0.0261 -0.0077 129 GLU A CA    
1016 C  C     . GLU A 149 ? 0.3216 0.2897 0.2885 0.0009  -0.0235 -0.0019 129 GLU A C     
1017 O  O     . GLU A 149 ? 0.3061 0.2751 0.2769 0.0014  -0.0218 0.0005  129 GLU A O     
1018 C  CB    . GLU A 149 ? 0.3792 0.3356 0.3462 0.0034  -0.0303 -0.0063 129 GLU A CB    
1019 C  CG    . GLU A 149 ? 0.4911 0.4447 0.4575 -0.0003 -0.0329 -0.0019 129 GLU A CG    
1020 C  CD    . GLU A 149 ? 0.5710 0.5209 0.5328 -0.0011 -0.0364 -0.0044 129 GLU A CD    
1021 O  OE1   . GLU A 149 ? 0.4260 0.3772 0.3846 0.0009  -0.0361 -0.0095 129 GLU A OE1   
1022 O  OE2   . GLU A 149 ? 0.7082 0.6545 0.6696 -0.0040 -0.0396 -0.0014 129 GLU A OE2   
1023 N  N     . TYR A 150 ? 0.3062 0.2763 0.2700 -0.0016 -0.0235 0.0002  130 TYR A N     
1024 C  CA    . TYR A 150 ? 0.2813 0.2544 0.2465 -0.0036 -0.0220 0.0052  130 TYR A CA    
1025 C  C     . TYR A 150 ? 0.2780 0.2555 0.2389 -0.0051 -0.0200 0.0051  130 TYR A C     
1026 O  O     . TYR A 150 ? 0.2907 0.2704 0.2526 -0.0060 -0.0182 0.0083  130 TYR A O     
1027 C  CB    . TYR A 150 ? 0.2792 0.2502 0.2455 -0.0058 -0.0251 0.0090  130 TYR A CB    
1028 C  CG    . TYR A 150 ? 0.2846 0.2525 0.2552 -0.0057 -0.0269 0.0103  130 TYR A CG    
1029 C  CD1   . TYR A 150 ? 0.2916 0.2609 0.2671 -0.0053 -0.0253 0.0128  130 TYR A CD1   
1030 C  CD2   . TYR A 150 ? 0.2923 0.2556 0.2613 -0.0067 -0.0305 0.0091  130 TYR A CD2   
1031 C  CE1   . TYR A 150 ? 0.3010 0.2681 0.2796 -0.0061 -0.0269 0.0141  130 TYR A CE1   
1032 C  CE2   . TYR A 150 ? 0.3580 0.3183 0.3300 -0.0077 -0.0325 0.0107  130 TYR A CE2   
1033 C  CZ    . TYR A 150 ? 0.3892 0.3517 0.3658 -0.0076 -0.0306 0.0132  130 TYR A CZ    
1034 O  OH    . TYR A 150 ? 0.3344 0.2945 0.3130 -0.0096 -0.0325 0.0150  130 TYR A OH    
1035 N  N     . LEU A 151 ? 0.2611 0.2395 0.2166 -0.0058 -0.0203 0.0015  131 LEU A N     
1036 C  CA    . LEU A 151 ? 0.2586 0.2406 0.2084 -0.0087 -0.0193 0.0023  131 LEU A CA    
1037 C  C     . LEU A 151 ? 0.2675 0.2551 0.2136 -0.0087 -0.0160 -0.0025 131 LEU A C     
1038 O  O     . LEU A 151 ? 0.2754 0.2665 0.2155 -0.0119 -0.0151 -0.0023 131 LEU A O     
1039 C  CB    . LEU A 151 ? 0.2924 0.2719 0.2379 -0.0108 -0.0227 0.0026  131 LEU A CB    
1040 C  CG    . LEU A 151 ? 0.2821 0.2572 0.2313 -0.0111 -0.0262 0.0067  131 LEU A CG    
1041 C  CD1   . LEU A 151 ? 0.2988 0.2719 0.2432 -0.0134 -0.0296 0.0066  131 LEU A CD1   
1042 C  CD2   . LEU A 151 ? 0.3167 0.2927 0.2695 -0.0119 -0.0259 0.0121  131 LEU A CD2   
1043 N  N     . SER A 152 ? 0.2894 0.2787 0.2390 -0.0053 -0.0143 -0.0069 132 SER A N     
1044 C  CA    . SER A 152 ? 0.2929 0.2895 0.2401 -0.0051 -0.0110 -0.0121 132 SER A CA    
1045 C  C     . SER A 152 ? 0.2673 0.2686 0.2141 -0.0077 -0.0076 -0.0088 132 SER A C     
1046 O  O     . SER A 152 ? 0.2842 0.2826 0.2350 -0.0074 -0.0077 -0.0041 132 SER A O     
1047 C  CB    . SER A 152 ? 0.2907 0.2876 0.2425 -0.0003 -0.0108 -0.0180 132 SER A CB    
1048 O  OG    . SER A 152 ? 0.3367 0.3285 0.2881 0.0020  -0.0145 -0.0215 132 SER A OG    
1049 N  N     . PRO A 153 ? 0.2863 0.2950 0.2280 -0.0105 -0.0048 -0.0113 133 PRO A N     
1050 C  CA    A PRO A 153 ? 0.2825 0.2953 0.2229 -0.0137 -0.0020 -0.0080 133 PRO A CA    
1051 C  CA    B PRO A 153 ? 0.2829 0.2958 0.2233 -0.0137 -0.0019 -0.0080 133 PRO A CA    
1052 C  C     . PRO A 153 ? 0.2644 0.2794 0.2115 -0.0105 0.0003  -0.0094 133 PRO A C     
1053 O  O     . PRO A 153 ? 0.2970 0.3143 0.2480 -0.0064 0.0008  -0.0152 133 PRO A O     
1054 C  CB    A PRO A 153 ? 0.3009 0.3224 0.2340 -0.0178 0.0006  -0.0116 133 PRO A CB    
1055 C  CB    B PRO A 153 ? 0.3011 0.3227 0.2343 -0.0177 0.0006  -0.0118 133 PRO A CB    
1056 C  CG    A PRO A 153 ? 0.2963 0.3200 0.2294 -0.0146 0.0001  -0.0190 133 PRO A CG    
1057 C  CG    B PRO A 153 ? 0.3173 0.3373 0.2467 -0.0175 -0.0017 -0.0147 133 PRO A CG    
1058 C  CD    A PRO A 153 ? 0.3222 0.3359 0.2582 -0.0117 -0.0043 -0.0169 133 PRO A CD    
1059 C  CD    B PRO A 153 ? 0.3217 0.3352 0.2576 -0.0117 -0.0044 -0.0167 133 PRO A CD    
1060 N  N     . ASN A 154 ? 0.2596 0.2733 0.2079 -0.0123 0.0010  -0.0042 134 ASN A N     
1061 C  CA    . ASN A 154 ? 0.2718 0.2876 0.2257 -0.0099 0.0032  -0.0050 134 ASN A CA    
1062 C  C     . ASN A 154 ? 0.2476 0.2737 0.2006 -0.0105 0.0069  -0.0108 134 ASN A C     
1063 O  O     . ASN A 154 ? 0.2897 0.3222 0.2364 -0.0148 0.0086  -0.0120 134 ASN A O     
1064 C  CB    . ASN A 154 ? 0.2421 0.2547 0.1964 -0.0122 0.0031  0.0016  134 ASN A CB    
1065 C  CG    . ASN A 154 ? 0.2381 0.2424 0.1964 -0.0101 0.0000  0.0059  134 ASN A CG    
1066 O  OD1   . ASN A 154 ? 0.2358 0.2371 0.1980 -0.0065 -0.0015 0.0040  134 ASN A OD1   
1067 N  ND2   . ASN A 154 ? 0.2597 0.2604 0.2168 -0.0123 -0.0014 0.0114  134 ASN A ND2   
1068 N  N     . LEU A 155 ? 0.2445 0.2729 0.2039 -0.0061 0.0079  -0.0147 135 LEU A N     
1069 C  CA    . LEU A 155 ? 0.2439 0.2831 0.2043 -0.0057 0.0113  -0.0210 135 LEU A CA    
1070 C  C     . LEU A 155 ? 0.2386 0.2795 0.2028 -0.0060 0.0132  -0.0186 135 LEU A C     
1071 O  O     . LEU A 155 ? 0.2789 0.3151 0.2493 -0.0018 0.0120  -0.0182 135 LEU A O     
1072 C  CB    . LEU A 155 ? 0.3123 0.3528 0.2773 0.0004  0.0101  -0.0288 135 LEU A CB    
1073 C  CG    . LEU A 155 ? 0.3740 0.4118 0.3358 0.0015  0.0076  -0.0321 135 LEU A CG    
1074 C  CD1   . LEU A 155 ? 0.3827 0.4200 0.3497 0.0082  0.0054  -0.0396 135 LEU A CD1   
1075 C  CD2   . LEU A 155 ? 0.4184 0.4654 0.3731 -0.0033 0.0102  -0.0345 135 LEU A CD2   
1076 N  N     . TRP A 156 ? 0.2751 0.3229 0.2354 -0.0114 0.0161  -0.0169 136 TRP A N     
1077 C  CA    . TRP A 156 ? 0.2889 0.3371 0.2519 -0.0125 0.0175  -0.0137 136 TRP A CA    
1078 C  C     . TRP A 156 ? 0.2865 0.3467 0.2528 -0.0118 0.0210  -0.0199 136 TRP A C     
1079 O  O     . TRP A 156 ? 0.3150 0.3856 0.2786 -0.0137 0.0233  -0.0253 136 TRP A O     
1080 C  CB    . TRP A 156 ? 0.2890 0.3351 0.2454 -0.0193 0.0176  -0.0068 136 TRP A CB    
1081 C  CG    . TRP A 156 ? 0.2659 0.3003 0.2202 -0.0195 0.0138  -0.0005 136 TRP A CG    
1082 C  CD1   . TRP A 156 ? 0.3113 0.3426 0.2595 -0.0224 0.0118  0.0016  136 TRP A CD1   
1083 C  CD2   . TRP A 156 ? 0.2681 0.2935 0.2270 -0.0166 0.0116  0.0039  136 TRP A CD2   
1084 N  NE1   . TRP A 156 ? 0.2975 0.3186 0.2468 -0.0211 0.0083  0.0070  136 TRP A NE1   
1085 C  CE2   . TRP A 156 ? 0.2933 0.3112 0.2492 -0.0176 0.0083  0.0083  136 TRP A CE2   
1086 C  CE3   . TRP A 156 ? 0.2680 0.2915 0.2332 -0.0133 0.0120  0.0043  136 TRP A CE3   
1087 C  CZ2   . TRP A 156 ? 0.3175 0.3271 0.2770 -0.0153 0.0056  0.0125  136 TRP A CZ2   
1088 C  CZ3   . TRP A 156 ? 0.2731 0.2881 0.2413 -0.0114 0.0095  0.0088  136 TRP A CZ3   
1089 C  CH2   . TRP A 156 ? 0.2702 0.2788 0.2358 -0.0123 0.0065  0.0125  136 TRP A CH2   
1090 N  N     . PRO A 157 ? 0.2803 0.3399 0.2526 -0.0092 0.0213  -0.0195 137 PRO A N     
1091 C  CA    . PRO A 157 ? 0.3184 0.3899 0.2940 -0.0093 0.0246  -0.0246 137 PRO A CA    
1092 C  C     . PRO A 157 ? 0.3753 0.4550 0.3443 -0.0174 0.0277  -0.0226 137 PRO A C     
1093 O  O     . PRO A 157 ? 0.3075 0.3811 0.2703 -0.0226 0.0267  -0.0156 137 PRO A O     
1094 C  CB    . PRO A 157 ? 0.3295 0.3959 0.3114 -0.0062 0.0237  -0.0221 137 PRO A CB    
1095 C  CG    . PRO A 157 ? 0.4058 0.4586 0.3887 -0.0028 0.0199  -0.0180 137 PRO A CG    
1096 C  CD    . PRO A 157 ? 0.2965 0.3451 0.2725 -0.0066 0.0189  -0.0143 137 PRO A CD    
1097 N  N     . GLN A 158 ? 0.3912 0.4854 0.3618 -0.0185 0.0311  -0.0289 138 GLN A N     
1098 C  CA    . GLN A 158 ? 0.4021 0.5059 0.3662 -0.0271 0.0343  -0.0275 138 GLN A CA    
1099 C  C     . GLN A 158 ? 0.2711 0.3693 0.2340 -0.0312 0.0339  -0.0200 138 GLN A C     
1100 O  O     . GLN A 158 ? 0.3216 0.4167 0.2912 -0.0271 0.0333  -0.0197 138 GLN A O     
1101 C  CB    . GLN A 158 ? 0.4572 0.5792 0.4250 -0.0270 0.0382  -0.0365 138 GLN A CB    
1102 C  CG    . GLN A 158 ? 0.4376 0.5661 0.4066 -0.0228 0.0384  -0.0450 138 GLN A CG    
1103 C  CD    . GLN A 158 ? 0.5768 0.7235 0.5517 -0.0206 0.0418  -0.0553 138 GLN A CD    
1104 O  OE1   . GLN A 158 ? 0.6764 0.8261 0.6594 -0.0164 0.0419  -0.0579 138 GLN A OE1   
1105 N  NE2   . GLN A 158 ? 0.6763 0.8357 0.6474 -0.0234 0.0444  -0.0615 138 GLN A NE2   
1106 N  N     . GLU A 159 ? 0.3174 0.4133 0.2711 -0.0394 0.0338  -0.0138 139 GLU A N     
1107 C  CA    . GLU A 159 ? 0.3001 0.3901 0.2518 -0.0437 0.0329  -0.0069 139 GLU A CA    
1108 C  C     . GLU A 159 ? 0.2640 0.3660 0.2200 -0.0452 0.0362  -0.0103 139 GLU A C     
1109 O  O     . GLU A 159 ? 0.3109 0.4079 0.2701 -0.0444 0.0354  -0.0071 139 GLU A O     
1110 C  CB    . GLU A 159 ? 0.3421 0.4275 0.2825 -0.0527 0.0313  0.0000  139 GLU A CB    
1111 C  CG    . GLU A 159 ? 0.3741 0.4562 0.3103 -0.0594 0.0306  0.0063  139 GLU A CG    
1112 C  CD    . GLU A 159 ? 0.4180 0.4854 0.3581 -0.0553 0.0270  0.0118  139 GLU A CD    
1113 O  OE1   . GLU A 159 ? 0.3872 0.4459 0.3319 -0.0483 0.0247  0.0120  139 GLU A OE1   
1114 O  OE2   . GLU A 159 ? 0.4931 0.5582 0.4315 -0.0594 0.0264  0.0157  139 GLU A OE2   
1115 N  N     . SER A 160 ? 0.2963 0.4149 0.2524 -0.0475 0.0401  -0.0172 140 SER A N     
1116 C  CA    . SER A 160 ? 0.3041 0.4354 0.2643 -0.0497 0.0433  -0.0205 140 SER A CA    
1117 C  C     . SER A 160 ? 0.3213 0.4524 0.2931 -0.0404 0.0428  -0.0249 140 SER A C     
1118 O  O     . SER A 160 ? 0.4026 0.5370 0.3780 -0.0414 0.0437  -0.0243 140 SER A O     
1119 C  CB    . SER A 160 ? 0.3604 0.5115 0.3187 -0.0542 0.0477  -0.0278 140 SER A CB    
1120 O  OG    . SER A 160 ? 0.4328 0.5890 0.3962 -0.0468 0.0481  -0.0361 140 SER A OG    
1121 N  N     . THR A 161 ? 0.3034 0.4301 0.2806 -0.0319 0.0410  -0.0291 141 THR A N     
1122 C  CA    . THR A 161 ? 0.3078 0.4331 0.2953 -0.0232 0.0397  -0.0332 141 THR A CA    
1123 C  C     . THR A 161 ? 0.2531 0.3611 0.2422 -0.0195 0.0360  -0.0265 141 THR A C     
1124 O  O     . THR A 161 ? 0.3191 0.4254 0.3153 -0.0146 0.0350  -0.0279 141 THR A O     
1125 C  CB    . THR A 161 ? 0.3678 0.4977 0.3603 -0.0159 0.0391  -0.0418 141 THR A CB    
1126 O  OG1   . THR A 161 ? 0.5242 0.6446 0.5115 -0.0154 0.0370  -0.0395 141 THR A OG1   
1127 C  CG2   . THR A 161 ? 0.5816 0.7317 0.5752 -0.0181 0.0431  -0.0504 141 THR A CG2   
1128 N  N     . LEU A 162 ? 0.2597 0.3554 0.2427 -0.0216 0.0338  -0.0199 142 LEU A N     
1129 C  CA    . LEU A 162 ? 0.2725 0.3532 0.2569 -0.0188 0.0306  -0.0137 142 LEU A CA    
1130 C  C     . LEU A 162 ? 0.2933 0.3662 0.2697 -0.0253 0.0295  -0.0058 142 LEU A C     
1131 O  O     . LEU A 162 ? 0.2424 0.3059 0.2154 -0.0251 0.0270  -0.0021 142 LEU A O     
1132 C  CB    . LEU A 162 ? 0.2493 0.3215 0.2364 -0.0122 0.0277  -0.0151 142 LEU A CB    
1133 C  CG    . LEU A 162 ? 0.2148 0.2749 0.2056 -0.0081 0.0249  -0.0110 142 LEU A CG    
1134 C  CD1   . LEU A 162 ? 0.2741 0.3374 0.2716 -0.0049 0.0253  -0.0135 142 LEU A CD1   
1135 C  CD2   . LEU A 162 ? 0.2531 0.3057 0.2453 -0.0031 0.0221  -0.0121 142 LEU A CD2   
1136 N  N     . PRO A 163 ? 0.2502 0.3265 0.2238 -0.0312 0.0308  -0.0029 143 PRO A N     
1137 C  CA    . PRO A 163 ? 0.2643 0.3335 0.2293 -0.0382 0.0291  0.0043  143 PRO A CA    
1138 C  C     . PRO A 163 ? 0.2285 0.2821 0.1938 -0.0353 0.0252  0.0101  143 PRO A C     
1139 O  O     . PRO A 163 ? 0.2422 0.2917 0.2134 -0.0311 0.0245  0.0104  143 PRO A O     
1140 C  CB    . PRO A 163 ? 0.2836 0.3600 0.2468 -0.0445 0.0311  0.0052  143 PRO A CB    
1141 C  CG    . PRO A 163 ? 0.3417 0.4254 0.3144 -0.0391 0.0330  -0.0002 143 PRO A CG    
1142 C  CD    . PRO A 163 ? 0.2801 0.3680 0.2578 -0.0324 0.0336  -0.0067 143 PRO A CD    
1143 N  N     . GLY A 164 ? 0.2531 0.2988 0.2122 -0.0377 0.0225  0.0144  144 GLY A N     
1144 C  CA    . GLY A 164 ? 0.2640 0.2961 0.2231 -0.0354 0.0185  0.0196  144 GLY A CA    
1145 C  C     . GLY A 164 ? 0.2853 0.3123 0.2499 -0.0282 0.0171  0.0181  144 GLY A C     
1146 O  O     . GLY A 164 ? 0.2506 0.2677 0.2160 -0.0260 0.0141  0.0218  144 GLY A O     
1147 N  N     . PHE A 165 ? 0.2532 0.2865 0.2215 -0.0245 0.0190  0.0126  145 PHE A N     
1148 C  CA    . PHE A 165 ? 0.2183 0.2464 0.1916 -0.0181 0.0175  0.0112  145 PHE A CA    
1149 C  C     . PHE A 165 ? 0.2331 0.2539 0.2026 -0.0187 0.0145  0.0146  145 PHE A C     
1150 O  O     . PHE A 165 ? 0.2184 0.2315 0.1907 -0.0154 0.0121  0.0170  145 PHE A O     
1151 C  CB    . PHE A 165 ? 0.2162 0.2520 0.1933 -0.0145 0.0193  0.0045  145 PHE A CB    
1152 C  CG    . PHE A 165 ? 0.2129 0.2430 0.1939 -0.0089 0.0172  0.0031  145 PHE A CG    
1153 C  CD1   . PHE A 165 ? 0.2463 0.2706 0.2325 -0.0049 0.0159  0.0042  145 PHE A CD1   
1154 C  CD2   . PHE A 165 ? 0.2580 0.2886 0.2368 -0.0083 0.0164  0.0009  145 PHE A CD2   
1155 C  CE1   . PHE A 165 ? 0.2657 0.2850 0.2548 -0.0008 0.0137  0.0033  145 PHE A CE1   
1156 C  CE2   . PHE A 165 ? 0.2848 0.3097 0.2667 -0.0038 0.0141  -0.0001 145 PHE A CE2   
1157 C  CZ    . PHE A 165 ? 0.2424 0.2617 0.2293 -0.0003 0.0127  0.0012  145 PHE A CZ    
1158 N  N     . LYS A 166 ? 0.2280 0.2518 0.1910 -0.0229 0.0146  0.0146  146 LYS A N     
1159 C  CA    . LYS A 166 ? 0.2312 0.2485 0.1907 -0.0233 0.0116  0.0173  146 LYS A CA    
1160 C  C     . LYS A 166 ? 0.2332 0.2409 0.1909 -0.0245 0.0080  0.0234  146 LYS A C     
1161 O  O     . LYS A 166 ? 0.2456 0.2470 0.2063 -0.0209 0.0054  0.0247  146 LYS A O     
1162 C  CB    . LYS A 166 ? 0.2459 0.2687 0.1981 -0.0282 0.0123  0.0161  146 LYS A CB    
1163 C  CG    . LYS A 166 ? 0.2679 0.2841 0.2157 -0.0290 0.0089  0.0190  146 LYS A CG    
1164 C  CD    . LYS A 166 ? 0.2755 0.2983 0.2161 -0.0335 0.0101  0.0166  146 LYS A CD    
1165 C  CE    . LYS A 166 ? 0.3671 0.3835 0.3029 -0.0346 0.0064  0.0195  146 LYS A CE    
1166 N  NZ    . LYS A 166 ? 0.3669 0.3751 0.2974 -0.0389 0.0026  0.0263  146 LYS A NZ    
1167 N  N     . PRO A 167 ? 0.2570 0.2631 0.2102 -0.0293 0.0073  0.0269  147 PRO A N     
1168 C  CA    . PRO A 167 ? 0.2786 0.2744 0.2308 -0.0293 0.0030  0.0321  147 PRO A CA    
1169 C  C     . PRO A 167 ? 0.2863 0.2783 0.2466 -0.0234 0.0026  0.0317  147 PRO A C     
1170 O  O     . PRO A 167 ? 0.2596 0.2447 0.2217 -0.0209 -0.0008 0.0340  147 PRO A O     
1171 C  CB    . PRO A 167 ? 0.3127 0.3077 0.2582 -0.0360 0.0023  0.0354  147 PRO A CB    
1172 C  CG    . PRO A 167 ? 0.3423 0.3485 0.2882 -0.0383 0.0073  0.0315  147 PRO A CG    
1173 C  CD    . PRO A 167 ? 0.2743 0.2873 0.2223 -0.0355 0.0097  0.0266  147 PRO A CD    
1174 N  N     . THR A 168 ? 0.2268 0.2237 0.1921 -0.0212 0.0058  0.0288  148 THR A N     
1175 C  CA    . THR A 168 ? 0.2200 0.2137 0.1923 -0.0161 0.0056  0.0284  148 THR A CA    
1176 C  C     . THR A 168 ? 0.2638 0.2562 0.2403 -0.0115 0.0048  0.0269  148 THR A C     
1177 O  O     . THR A 168 ? 0.2444 0.2320 0.2244 -0.0087 0.0028  0.0283  148 THR A O     
1178 C  CB    . THR A 168 ? 0.2157 0.2151 0.1920 -0.0149 0.0089  0.0254  148 THR A CB    
1179 O  OG1   . THR A 168 ? 0.2497 0.2512 0.2219 -0.0198 0.0097  0.0267  148 THR A OG1   
1180 C  CG2   . THR A 168 ? 0.2555 0.2513 0.2378 -0.0104 0.0085  0.0254  148 THR A CG2   
1181 N  N     . PHE A 169 ? 0.2361 0.2333 0.2124 -0.0111 0.0063  0.0237  149 PHE A N     
1182 C  CA    . PHE A 169 ? 0.2141 0.2097 0.1933 -0.0077 0.0052  0.0224  149 PHE A CA    
1183 C  C     . PHE A 169 ? 0.2632 0.2535 0.2404 -0.0083 0.0018  0.0256  149 PHE A C     
1184 O  O     . PHE A 169 ? 0.2281 0.2154 0.2094 -0.0054 0.0001  0.0263  149 PHE A O     
1185 C  CB    . PHE A 169 ? 0.2143 0.2153 0.1921 -0.0078 0.0068  0.0183  149 PHE A CB    
1186 C  CG    . PHE A 169 ? 0.2167 0.2163 0.1978 -0.0042 0.0058  0.0162  149 PHE A CG    
1187 C  CD1   . PHE A 169 ? 0.2260 0.2220 0.2057 -0.0043 0.0032  0.0179  149 PHE A CD1   
1188 C  CD2   . PHE A 169 ? 0.2136 0.2150 0.1989 -0.0010 0.0068  0.0127  149 PHE A CD2   
1189 C  CE1   . PHE A 169 ? 0.2237 0.2182 0.2060 -0.0018 0.0021  0.0162  149 PHE A CE1   
1190 C  CE2   . PHE A 169 ? 0.2441 0.2430 0.2315 0.0016  0.0052  0.0111  149 PHE A CE2   
1191 C  CZ    . PHE A 169 ? 0.2240 0.2196 0.2098 0.0010  0.0029  0.0130  149 PHE A CZ    
1192 N  N     . GLU A 170 ? 0.2252 0.2148 0.1960 -0.0124 0.0004  0.0276  150 GLU A N     
1193 C  CA    . GLU A 170 ? 0.2268 0.2110 0.1954 -0.0129 -0.0036 0.0307  150 GLU A CA    
1194 C  C     . GLU A 170 ? 0.2304 0.2090 0.2021 -0.0111 -0.0063 0.0333  150 GLU A C     
1195 O  O     . GLU A 170 ? 0.2568 0.2327 0.2319 -0.0084 -0.0089 0.0340  150 GLU A O     
1196 C  CB    . GLU A 170 ? 0.2463 0.2301 0.2063 -0.0183 -0.0049 0.0326  150 GLU A CB    
1197 C  CG    . GLU A 170 ? 0.2666 0.2559 0.2236 -0.0197 -0.0029 0.0295  150 GLU A CG    
1198 C  CD    . GLU A 170 ? 0.5067 0.4970 0.4544 -0.0259 -0.0036 0.0311  150 GLU A CD    
1199 O  OE1   . GLU A 170 ? 0.6343 0.6228 0.5775 -0.0300 -0.0044 0.0342  150 GLU A OE1   
1200 O  OE2   . GLU A 170 ? 0.4843 0.4772 0.4288 -0.0269 -0.0034 0.0294  150 GLU A OE2   
1201 N  N     . ASP A 171 ? 0.2445 0.2219 0.2156 -0.0123 -0.0058 0.0345  151 ASP A N     
1202 C  CA    . ASP A 171 ? 0.2723 0.2439 0.2459 -0.0104 -0.0089 0.0366  151 ASP A CA    
1203 C  C     . ASP A 171 ? 0.2304 0.2035 0.2122 -0.0052 -0.0079 0.0345  151 ASP A C     
1204 O  O     . ASP A 171 ? 0.2376 0.2077 0.2229 -0.0025 -0.0108 0.0351  151 ASP A O     
1205 C  CB    . ASP A 171 ? 0.2505 0.2202 0.2214 -0.0131 -0.0086 0.0381  151 ASP A CB    
1206 C  CG    . ASP A 171 ? 0.3509 0.3174 0.3128 -0.0191 -0.0110 0.0413  151 ASP A CG    
1207 O  OD1   . ASP A 171 ? 0.3492 0.3138 0.3071 -0.0207 -0.0136 0.0427  151 ASP A OD1   
1208 O  OD2   . ASP A 171 ? 0.3817 0.3474 0.3402 -0.0225 -0.0106 0.0427  151 ASP A OD2   
1209 N  N     . LEU A 172 ? 0.2171 0.1950 0.2022 -0.0039 -0.0040 0.0318  152 LEU A N     
1210 C  CA    . LEU A 172 ? 0.2071 0.1863 0.1988 0.0000  -0.0031 0.0302  152 LEU A CA    
1211 C  C     . LEU A 172 ? 0.2420 0.2221 0.2359 0.0015  -0.0045 0.0296  152 LEU A C     
1212 O  O     . LEU A 172 ? 0.2140 0.1940 0.2125 0.0039  -0.0057 0.0294  152 LEU A O     
1213 C  CB    . LEU A 172 ? 0.2107 0.1936 0.2045 0.0007  0.0005  0.0278  152 LEU A CB    
1214 C  CG    . LEU A 172 ? 0.2111 0.1951 0.2107 0.0038  0.0013  0.0265  152 LEU A CG    
1215 C  CD1   . LEU A 172 ? 0.2322 0.2142 0.2350 0.0055  -0.0002 0.0274  152 LEU A CD1   
1216 C  CD2   . LEU A 172 ? 0.2001 0.1865 0.2009 0.0042  0.0040  0.0246  152 LEU A CD2   
1217 N  N     . CYS A 173 ? 0.2174 0.1988 0.2080 -0.0001 -0.0042 0.0290  153 CYS A N     
1218 C  CA    . CYS A 173 ? 0.2209 0.2027 0.2130 0.0008  -0.0059 0.0287  153 CYS A CA    
1219 C  C     . CYS A 173 ? 0.2533 0.2321 0.2457 0.0012  -0.0098 0.0308  153 CYS A C     
1220 O  O     . CYS A 173 ? 0.2292 0.2092 0.2262 0.0032  -0.0112 0.0304  153 CYS A O     
1221 C  CB    . CYS A 173 ? 0.2312 0.2145 0.2191 -0.0010 -0.0053 0.0275  153 CYS A CB    
1222 S  SG    . CYS A 173 ? 0.2458 0.2324 0.2352 0.0001  -0.0020 0.0238  153 CYS A SG    
1223 N  N     . ARG A 174 ? 0.2208 0.1960 0.2086 -0.0009 -0.0119 0.0330  154 ARG A N     
1224 C  CA    . ARG A 174 ? 0.2250 0.1961 0.2129 -0.0002 -0.0167 0.0350  154 ARG A CA    
1225 C  C     . ARG A 174 ? 0.2556 0.2266 0.2503 0.0036  -0.0178 0.0342  154 ARG A C     
1226 O  O     . ARG A 174 ? 0.2392 0.2107 0.2381 0.0060  -0.0207 0.0338  154 ARG A O     
1227 C  CB    . ARG A 174 ? 0.2752 0.2410 0.2557 -0.0037 -0.0194 0.0379  154 ARG A CB    
1228 C  CG    . ARG A 174 ? 0.3086 0.2686 0.2888 -0.0029 -0.0256 0.0401  154 ARG A CG    
1229 C  CD    . ARG A 174 ? 0.3223 0.2757 0.2933 -0.0075 -0.0290 0.0437  154 ARG A CD    
1230 N  NE    . ARG A 174 ? 0.3257 0.2816 0.2898 -0.0121 -0.0271 0.0442  154 ARG A NE    
1231 C  CZ    . ARG A 174 ? 0.3595 0.3154 0.3211 -0.0131 -0.0291 0.0447  154 ARG A CZ    
1232 N  NH1   . ARG A 174 ? 0.3805 0.3344 0.3464 -0.0099 -0.0333 0.0448  154 ARG A NH1   
1233 N  NH2   . ARG A 174 ? 0.3553 0.3141 0.3104 -0.0173 -0.0269 0.0445  154 ARG A NH2   
1234 N  N     . LEU A 175 ? 0.2309 0.2020 0.2270 0.0043  -0.0156 0.0336  155 LEU A N     
1235 C  CA    . LEU A 175 ? 0.2259 0.1978 0.2283 0.0079  -0.0162 0.0322  155 LEU A CA    
1236 C  C     . LEU A 175 ? 0.2283 0.2063 0.2369 0.0100  -0.0144 0.0299  155 LEU A C     
1237 O  O     . LEU A 175 ? 0.2316 0.2116 0.2455 0.0127  -0.0166 0.0287  155 LEU A O     
1238 C  CB    . LEU A 175 ? 0.2156 0.1867 0.2176 0.0076  -0.0136 0.0319  155 LEU A CB    
1239 C  CG    . LEU A 175 ? 0.2658 0.2370 0.2731 0.0110  -0.0140 0.0303  155 LEU A CG    
1240 C  CD1   . LEU A 175 ? 0.2795 0.2476 0.2839 0.0095  -0.0129 0.0310  155 LEU A CD1   
1241 C  CD2   . LEU A 175 ? 0.2794 0.2574 0.2928 0.0130  -0.0109 0.0276  155 LEU A CD2   
1242 N  N     . ILE A 176 ? 0.2176 0.1990 0.2257 0.0087  -0.0109 0.0290  156 ILE A N     
1243 C  CA    . ILE A 176 ? 0.2095 0.1960 0.2224 0.0097  -0.0095 0.0273  156 ILE A CA    
1244 C  C     . ILE A 176 ? 0.2289 0.2168 0.2431 0.0098  -0.0123 0.0275  156 ILE A C     
1245 O  O     . ILE A 176 ? 0.2164 0.2090 0.2362 0.0112  -0.0127 0.0262  156 ILE A O     
1246 C  CB    . ILE A 176 ? 0.2154 0.2032 0.2266 0.0082  -0.0062 0.0266  156 ILE A CB    
1247 C  CG1   . ILE A 176 ? 0.1926 0.1801 0.2041 0.0086  -0.0037 0.0260  156 ILE A CG1   
1248 C  CG2   . ILE A 176 ? 0.2283 0.2199 0.2426 0.0080  -0.0058 0.0256  156 ILE A CG2   
1249 C  CD1   . ILE A 176 ? 0.2509 0.2388 0.2605 0.0075  -0.0012 0.0252  156 ILE A CD1   
1250 N  N     . ILE A 177 ? 0.2044 0.1892 0.2137 0.0080  -0.0141 0.0290  157 ILE A N     
1251 C  CA    . ILE A 177 ? 0.2069 0.1928 0.2172 0.0080  -0.0171 0.0293  157 ILE A CA    
1252 C  C     . ILE A 177 ? 0.2178 0.2034 0.2321 0.0106  -0.0211 0.0293  157 ILE A C     
1253 O  O     . ILE A 177 ? 0.2210 0.2107 0.2401 0.0118  -0.0229 0.0282  157 ILE A O     
1254 C  CB    . ILE A 177 ? 0.2116 0.1940 0.2149 0.0052  -0.0182 0.0307  157 ILE A CB    
1255 C  CG1   . ILE A 177 ? 0.2327 0.2165 0.2334 0.0035  -0.0148 0.0296  157 ILE A CG1   
1256 C  CG2   . ILE A 177 ? 0.2148 0.1977 0.2189 0.0052  -0.0221 0.0313  157 ILE A CG2   
1257 C  CD1   . ILE A 177 ? 0.2260 0.2074 0.2193 0.0008  -0.0150 0.0301  157 ILE A CD1   
1258 N  N     . ASP A 178 ? 0.2137 0.1944 0.2262 0.0114  -0.0230 0.0303  158 ASP A N     
1259 C  CA    . ASP A 178 ? 0.2163 0.1959 0.2332 0.0147  -0.0275 0.0297  158 ASP A CA    
1260 C  C     . ASP A 178 ? 0.2538 0.2412 0.2795 0.0179  -0.0259 0.0263  158 ASP A C     
1261 O  O     . ASP A 178 ? 0.2398 0.2314 0.2714 0.0204  -0.0288 0.0245  158 ASP A O     
1262 C  CB    . ASP A 178 ? 0.2454 0.2179 0.2588 0.0150  -0.0295 0.0310  158 ASP A CB    
1263 C  CG    . ASP A 178 ? 0.2700 0.2346 0.2748 0.0116  -0.0329 0.0346  158 ASP A CG    
1264 O  OD1   . ASP A 178 ? 0.2850 0.2492 0.2870 0.0100  -0.0349 0.0358  158 ASP A OD1   
1265 O  OD2   . ASP A 178 ? 0.3223 0.2811 0.3224 0.0102  -0.0337 0.0363  158 ASP A OD2   
1266 N  N     . VAL A 179 ? 0.2213 0.2116 0.2481 0.0175  -0.0213 0.0251  159 VAL A N     
1267 C  CA    . VAL A 179 ? 0.2124 0.2109 0.2466 0.0195  -0.0194 0.0220  159 VAL A CA    
1268 C  C     . VAL A 179 ? 0.2523 0.2576 0.2892 0.0180  -0.0185 0.0213  159 VAL A C     
1269 O  O     . VAL A 179 ? 0.2155 0.2284 0.2591 0.0196  -0.0192 0.0188  159 VAL A O     
1270 C  CB    . VAL A 179 ? 0.2091 0.2085 0.2428 0.0189  -0.0150 0.0213  159 VAL A CB    
1271 C  CG1   . VAL A 179 ? 0.2409 0.2495 0.2816 0.0202  -0.0129 0.0180  159 VAL A CG1   
1272 C  CG2   . VAL A 179 ? 0.2149 0.2077 0.2461 0.0203  -0.0163 0.0219  159 VAL A CG2   
1273 N  N     . ALA A 180 ? 0.2222 0.2252 0.2540 0.0147  -0.0171 0.0233  160 ALA A N     
1274 C  CA    . ALA A 180 ? 0.1960 0.2039 0.2293 0.0127  -0.0169 0.0230  160 ALA A CA    
1275 C  C     . ALA A 180 ? 0.2295 0.2400 0.2664 0.0141  -0.0211 0.0225  160 ALA A C     
1276 O  O     . ALA A 180 ? 0.2177 0.2357 0.2596 0.0137  -0.0212 0.0210  160 ALA A O     
1277 C  CB    . ALA A 180 ? 0.2096 0.2131 0.2363 0.0095  -0.0158 0.0249  160 ALA A CB    
1278 N  N     . VAL A 181 ? 0.2145 0.2188 0.2487 0.0155  -0.0250 0.0239  161 VAL A N     
1279 C  CA    . VAL A 181 ? 0.2161 0.2218 0.2536 0.0172  -0.0299 0.0235  161 VAL A CA    
1280 C  C     . VAL A 181 ? 0.2362 0.2497 0.2831 0.0211  -0.0310 0.0199  161 VAL A C     
1281 O  O     . VAL A 181 ? 0.2215 0.2422 0.2743 0.0220  -0.0331 0.0181  161 VAL A O     
1282 C  CB    . VAL A 181 ? 0.2152 0.2113 0.2468 0.0175  -0.0344 0.0261  161 VAL A CB    
1283 C  CG1   . VAL A 181 ? 0.2493 0.2459 0.2849 0.0202  -0.0406 0.0255  161 VAL A CG1   
1284 C  CG2   . VAL A 181 ? 0.2628 0.2537 0.2856 0.0133  -0.0332 0.0289  161 VAL A CG2   
1285 N  N     . LEU A 182 ? 0.2285 0.2415 0.2772 0.0235  -0.0298 0.0184  162 LEU A N     
1286 C  CA    . LEU A 182 ? 0.2477 0.2694 0.3058 0.0275  -0.0304 0.0140  162 LEU A CA    
1287 C  C     . LEU A 182 ? 0.2240 0.2578 0.2870 0.0254  -0.0260 0.0117  162 LEU A C     
1288 O  O     . LEU A 182 ? 0.2147 0.2589 0.2859 0.0274  -0.0269 0.0080  162 LEU A O     
1289 C  CB    . LEU A 182 ? 0.2228 0.2405 0.2811 0.0305  -0.0304 0.0127  162 LEU A CB    
1290 C  CG    . LEU A 182 ? 0.2463 0.2523 0.3002 0.0324  -0.0359 0.0148  162 LEU A CG    
1291 C  CD1   . LEU A 182 ? 0.2727 0.2737 0.3255 0.0343  -0.0355 0.0140  162 LEU A CD1   
1292 C  CD2   . LEU A 182 ? 0.2993 0.3063 0.3586 0.0364  -0.0426 0.0129  162 LEU A CD2   
1293 N  N     . VAL A 183 ? 0.2038 0.2366 0.2620 0.0212  -0.0213 0.0136  163 VAL A N     
1294 C  CA    . VAL A 183 ? 0.1897 0.2324 0.2509 0.0181  -0.0178 0.0122  163 VAL A CA    
1295 C  C     . VAL A 183 ? 0.2196 0.2671 0.2828 0.0161  -0.0198 0.0126  163 VAL A C     
1296 O  O     . VAL A 183 ? 0.1994 0.2584 0.2689 0.0152  -0.0191 0.0100  163 VAL A O     
1297 C  CB    . VAL A 183 ? 0.1875 0.2259 0.2422 0.0141  -0.0137 0.0146  163 VAL A CB    
1298 C  CG1   . VAL A 183 ? 0.2083 0.2551 0.2646 0.0098  -0.0111 0.0142  163 VAL A CG1   
1299 C  CG2   . VAL A 183 ? 0.1983 0.2339 0.2521 0.0159  -0.0115 0.0139  163 VAL A CG2   
1300 N  N     . ALA A 184 ? 0.2222 0.2614 0.2797 0.0149  -0.0222 0.0156  164 ALA A N     
1301 C  CA    . ALA A 184 ? 0.1956 0.2380 0.2543 0.0132  -0.0248 0.0161  164 ALA A CA    
1302 C  C     . ALA A 184 ? 0.2205 0.2706 0.2879 0.0170  -0.0286 0.0130  164 ALA A C     
1303 O  O     . ALA A 184 ? 0.2211 0.2803 0.2933 0.0156  -0.0293 0.0116  164 ALA A O     
1304 C  CB    . ALA A 184 ? 0.2198 0.2514 0.2705 0.0120  -0.0272 0.0195  164 ALA A CB    
1305 N  N     . ARG A 185 ? 0.1996 0.2458 0.2687 0.0219  -0.0316 0.0118  165 ARG A N     
1306 C  CA    . ARG A 185 ? 0.2109 0.2639 0.2889 0.0266  -0.0360 0.0081  165 ARG A CA    
1307 C  C     . ARG A 185 ? 0.2096 0.2781 0.2970 0.0273  -0.0330 0.0032  165 ARG A C     
1308 O  O     . ARG A 185 ? 0.1974 0.2768 0.2927 0.0285  -0.0351 0.0001  165 ARG A O     
1309 C  CB    . ARG A 185 ? 0.2436 0.2877 0.3209 0.0317  -0.0401 0.0078  165 ARG A CB    
1310 C  CG    . ARG A 185 ? 0.2712 0.3211 0.3581 0.0376  -0.0456 0.0033  165 ARG A CG    
1311 C  CD    . ARG A 185 ? 0.2985 0.3373 0.3834 0.0422  -0.0502 0.0034  165 ARG A CD    
1312 N  NE    . ARG A 185 ? 0.3399 0.3641 0.4147 0.0400  -0.0537 0.0089  165 ARG A NE    
1313 C  CZ    . ARG A 185 ? 0.5046 0.5166 0.5744 0.0418  -0.0576 0.0107  165 ARG A CZ    
1314 N  NH1   . ARG A 185 ? 0.4271 0.4385 0.5011 0.0464  -0.0592 0.0074  165 ARG A NH1   
1315 N  NH2   . ARG A 185 ? 0.4077 0.4080 0.4676 0.0385  -0.0601 0.0159  165 ARG A NH2   
1316 N  N     . ALA A 186 ? 0.2460 0.3165 0.3325 0.0262  -0.0281 0.0023  166 ALA A N     
1317 C  CA    . ALA A 186 ? 0.2208 0.3068 0.3150 0.0256  -0.0247 -0.0022 166 ALA A CA    
1318 C  C     . ALA A 186 ? 0.1880 0.2827 0.2826 0.0196  -0.0226 -0.0012 166 ALA A C     
1319 O  O     . ALA A 186 ? 0.1941 0.3037 0.2969 0.0193  -0.0223 -0.0052 166 ALA A O     
1320 C  CB    . ALA A 186 ? 0.2267 0.3118 0.3184 0.0250  -0.0201 -0.0027 166 ALA A CB    
1321 N  N     . CYS A 187 ? 0.1963 0.2822 0.2820 0.0146  -0.0213 0.0037  167 CYS A N     
1322 C  CA    . CYS A 187 ? 0.2218 0.3133 0.3067 0.0086  -0.0203 0.0052  167 CYS A CA    
1323 C  C     . CYS A 187 ? 0.2506 0.3480 0.3412 0.0099  -0.0247 0.0039  167 CYS A C     
1324 O  O     . CYS A 187 ? 0.2155 0.3254 0.3111 0.0065  -0.0240 0.0022  167 CYS A O     
1325 C  CB    . CYS A 187 ? 0.2075 0.2864 0.2819 0.0043  -0.0195 0.0103  167 CYS A CB    
1326 S  SG    . CYS A 187 ? 0.2249 0.2982 0.2930 0.0019  -0.0146 0.0118  167 CYS A SG    
1327 N  N     . ASP A 188 ? 0.1932 0.2820 0.2829 0.0143  -0.0294 0.0047  168 ASP A N     
1328 C  CA    . ASP A 188 ? 0.1960 0.2896 0.2912 0.0161  -0.0343 0.0033  168 ASP A CA    
1329 C  C     . ASP A 188 ? 0.2196 0.3293 0.3272 0.0199  -0.0350 -0.0028 168 ASP A C     
1330 O  O     . ASP A 188 ? 0.2082 0.3290 0.3223 0.0189  -0.0368 -0.0049 168 ASP A O     
1331 C  CB    . ASP A 188 ? 0.2245 0.3050 0.3158 0.0202  -0.0397 0.0055  168 ASP A CB    
1332 C  CG    . ASP A 188 ? 0.2606 0.3284 0.3410 0.0161  -0.0400 0.0108  168 ASP A CG    
1333 O  OD1   . ASP A 188 ? 0.2223 0.2922 0.2998 0.0108  -0.0379 0.0125  168 ASP A OD1   
1334 O  OD2   . ASP A 188 ? 0.2409 0.2967 0.3154 0.0181  -0.0426 0.0132  168 ASP A OD2   
1335 N  N     . ARG A 189 ? 0.2063 0.3179 0.3177 0.0245  -0.0341 -0.0063 169 ARG A N     
1336 C  CA    . ARG A 189 ? 0.2129 0.3413 0.3367 0.0284  -0.0346 -0.0132 169 ARG A CA    
1337 C  C     . ARG A 189 ? 0.2145 0.3598 0.3422 0.0222  -0.0297 -0.0151 169 ARG A C     
1338 O  O     . ARG A 189 ? 0.1887 0.3494 0.3258 0.0226  -0.0309 -0.0193 169 ARG A O     
1339 C  CB    . ARG A 189 ? 0.2599 0.3873 0.3862 0.0339  -0.0338 -0.0168 169 ARG A CB    
1340 C  CG    . ARG A 189 ? 0.3480 0.4613 0.4727 0.0405  -0.0399 -0.0162 169 ARG A CG    
1341 C  CD    . ARG A 189 ? 0.3985 0.5097 0.5241 0.0446  -0.0385 -0.0191 169 ARG A CD    
1342 N  NE    . ARG A 189 ? 0.5162 0.6460 0.6520 0.0461  -0.0353 -0.0262 169 ARG A NE    
1343 C  CZ    . ARG A 189 ? 0.4048 0.5381 0.5408 0.0464  -0.0309 -0.0288 169 ARG A CZ    
1344 N  NH1   . ARG A 189 ? 0.3473 0.4670 0.4744 0.0454  -0.0291 -0.0249 169 ARG A NH1   
1345 N  NH2   . ARG A 189 ? 0.4096 0.5616 0.5550 0.0474  -0.0281 -0.0357 169 ARG A NH2   
1346 N  N     . PHE A 190 ? 0.2317 0.3741 0.3519 0.0161  -0.0243 -0.0118 170 PHE A N     
1347 C  CA    . PHE A 190 ? 0.1928 0.3491 0.3145 0.0088  -0.0201 -0.0125 170 PHE A CA    
1348 C  C     . PHE A 190 ? 0.1862 0.3459 0.3082 0.0043  -0.0225 -0.0104 170 PHE A C     
1349 O  O     . PHE A 190 ? 0.1903 0.3672 0.3201 0.0018  -0.0219 -0.0139 170 PHE A O     
1350 C  CB    . PHE A 190 ? 0.1877 0.3361 0.2994 0.0030  -0.0154 -0.0082 170 PHE A CB    
1351 C  CG    . PHE A 190 ? 0.2159 0.3743 0.3261 -0.0060 -0.0120 -0.0071 170 PHE A CG    
1352 C  CD1   . PHE A 190 ? 0.2606 0.4349 0.3755 -0.0088 -0.0079 -0.0110 170 PHE A CD1   
1353 C  CD2   . PHE A 190 ? 0.2680 0.4196 0.3714 -0.0121 -0.0132 -0.0021 170 PHE A CD2   
1354 C  CE1   . PHE A 190 ? 0.2218 0.4053 0.3344 -0.0181 -0.0051 -0.0096 170 PHE A CE1   
1355 C  CE2   . PHE A 190 ? 0.2785 0.4382 0.3798 -0.0209 -0.0108 -0.0007 170 PHE A CE2   
1356 C  CZ    . PHE A 190 ? 0.2390 0.4147 0.3446 -0.0243 -0.0068 -0.0042 170 PHE A CZ    
1357 N  N     . ALA A 191 ? 0.1909 0.3350 0.3045 0.0032  -0.0251 -0.0050 171 ALA A N     
1358 C  CA    . ALA A 191 ? 0.1923 0.3377 0.3047 -0.0016 -0.0274 -0.0026 171 ALA A CA    
1359 C  C     . ALA A 191 ? 0.2174 0.3727 0.3399 0.0027  -0.0322 -0.0065 171 ALA A C     
1360 O  O     . ALA A 191 ? 0.2257 0.3924 0.3524 -0.0015 -0.0328 -0.0073 171 ALA A O     
1361 C  CB    . ALA A 191 ? 0.2419 0.3681 0.3428 -0.0031 -0.0292 0.0033  171 ALA A CB    
1362 N  N     . GLU A 192 ? 0.1932 0.3439 0.3194 0.0109  -0.0360 -0.0087 172 GLU A N     
1363 C  CA    . GLU A 192 ? 0.1953 0.3547 0.3316 0.0160  -0.0414 -0.0128 172 GLU A CA    
1364 C  C     . GLU A 192 ? 0.1926 0.3749 0.3414 0.0163  -0.0393 -0.0197 172 GLU A C     
1365 O  O     . GLU A 192 ? 0.2051 0.3997 0.3627 0.0172  -0.0425 -0.0229 172 GLU A O     
1366 C  CB    . GLU A 192 ? 0.2448 0.3929 0.3817 0.0245  -0.0464 -0.0137 172 GLU A CB    
1367 C  CG    . GLU A 192 ? 0.2190 0.3465 0.3444 0.0241  -0.0497 -0.0073 172 GLU A CG    
1368 C  CD    . GLU A 192 ? 0.3496 0.4638 0.4721 0.0304  -0.0529 -0.0069 172 GLU A CD    
1369 O  OE1   . GLU A 192 ? 0.3392 0.4596 0.4701 0.0365  -0.0545 -0.0121 172 GLU A OE1   
1370 O  OE2   . GLU A 192 ? 0.2680 0.3659 0.3798 0.0290  -0.0538 -0.0017 172 GLU A OE2   
1371 N  N     . LYS A 193 ? 0.2009 0.3902 0.3508 0.0153  -0.0338 -0.0222 173 LYS A N     
1372 C  CA    . LYS A 193 ? 0.2158 0.4287 0.3771 0.0145  -0.0311 -0.0290 173 LYS A CA    
1373 C  C     . LYS A 193 ? 0.2036 0.4280 0.3632 0.0041  -0.0271 -0.0272 173 LYS A C     
1374 O  O     . LYS A 193 ? 0.2010 0.4460 0.3707 0.0025  -0.0267 -0.0321 173 LYS A O     
1375 C  CB    . LYS A 193 ? 0.2153 0.4322 0.3783 0.0174  -0.0269 -0.0330 173 LYS A CB    
1376 C  CG    . LYS A 193 ? 0.2814 0.5238 0.4554 0.0162  -0.0230 -0.0406 173 LYS A CG    
1377 C  CD    . LYS A 193 ? 0.3634 0.6068 0.5380 0.0200  -0.0196 -0.0444 173 LYS A CD    
1378 C  CE    . LYS A 193 ? 0.5017 0.7713 0.6880 0.0200  -0.0159 -0.0533 173 LYS A CE    
1379 N  NZ    . LYS A 193 ? 0.6684 0.9505 0.8510 0.0084  -0.0097 -0.0514 173 LYS A NZ    
1380 N  N     . GLN A 194 ? 0.2272 0.4387 0.3744 -0.0032 -0.0248 -0.0201 174 GLN A N     
1381 C  CA    . GLN A 194 ? 0.2242 0.4450 0.3682 -0.0138 -0.0209 -0.0181 174 GLN A CA    
1382 C  C     . GLN A 194 ? 0.2580 0.4731 0.3967 -0.0199 -0.0236 -0.0131 174 GLN A C     
1383 O  O     . GLN A 194 ? 0.2369 0.4621 0.3747 -0.0289 -0.0215 -0.0121 174 GLN A O     
1384 C  CB    . GLN A 194 ? 0.1866 0.3985 0.3204 -0.0186 -0.0160 -0.0144 174 GLN A CB    
1385 C  CG    . GLN A 194 ? 0.1839 0.4015 0.3213 -0.0143 -0.0124 -0.0189 174 GLN A CG    
1386 C  CD    . GLN A 194 ? 0.2861 0.5289 0.4325 -0.0180 -0.0086 -0.0250 174 GLN A CD    
1387 O  OE1   . GLN A 194 ? 0.3091 0.5638 0.4565 -0.0259 -0.0076 -0.0244 174 GLN A OE1   
1388 N  NE2   . GLN A 194 ? 0.2692 0.5206 0.4219 -0.0125 -0.0063 -0.0309 174 GLN A NE2   
1389 N  N     . ILE A 195 ? 0.2102 0.4097 0.3448 -0.0160 -0.0284 -0.0099 175 ILE A N     
1390 C  CA    . ILE A 195 ? 0.1957 0.3869 0.3236 -0.0216 -0.0311 -0.0048 175 ILE A CA    
1391 C  C     . ILE A 195 ? 0.2002 0.3954 0.3353 -0.0173 -0.0368 -0.0068 175 ILE A C     
1392 O  O     . ILE A 195 ? 0.2068 0.3917 0.3420 -0.0097 -0.0407 -0.0069 175 ILE A O     
1393 C  CB    . ILE A 195 ? 0.2279 0.3956 0.3424 -0.0219 -0.0316 0.0012  175 ILE A CB    
1394 C  CG1   . ILE A 195 ? 0.2136 0.3772 0.3213 -0.0260 -0.0265 0.0031  175 ILE A CG1   
1395 C  CG2   . ILE A 195 ? 0.2206 0.3803 0.3286 -0.0270 -0.0348 0.0055  175 ILE A CG2   
1396 C  CD1   . ILE A 195 ? 0.2179 0.3598 0.3135 -0.0255 -0.0268 0.0081  175 ILE A CD1   
1397 N  N     . ALA A 196 ? 0.1986 0.4081 0.3391 -0.0225 -0.0378 -0.0081 176 ALA A N     
1398 C  CA    . ALA A 196 ? 0.2005 0.4141 0.3479 -0.0189 -0.0436 -0.0099 176 ALA A CA    
1399 C  C     . ALA A 196 ? 0.2073 0.4001 0.3442 -0.0189 -0.0478 -0.0041 176 ALA A C     
1400 O  O     . ALA A 196 ? 0.2726 0.4556 0.3991 -0.0258 -0.0466 0.0009  176 ALA A O     
1401 C  CB    . ALA A 196 ? 0.2431 0.4772 0.3981 -0.0255 -0.0434 -0.0123 176 ALA A CB    
1402 N  N     . GLY A 197 ? 0.2294 0.4155 0.3687 -0.0113 -0.0531 -0.0049 177 GLY A N     
1403 C  CA    . GLY A 197 ? 0.2243 0.3920 0.3539 -0.0111 -0.0573 0.0001  177 GLY A CA    
1404 C  C     . GLY A 197 ? 0.2641 0.4119 0.3824 -0.0089 -0.0560 0.0039  177 GLY A C     
1405 O  O     . GLY A 197 ? 0.2888 0.4218 0.3985 -0.0091 -0.0591 0.0078  177 GLY A O     
1406 N  N     . TYR A 198 ? 0.2475 0.3952 0.3656 -0.0073 -0.0515 0.0028  178 TYR A N     
1407 C  CA    . TYR A 198 ? 0.2087 0.3389 0.3167 -0.0053 -0.0500 0.0060  178 TYR A CA    
1408 C  C     . TYR A 198 ? 0.2467 0.3663 0.3538 0.0017  -0.0552 0.0064  178 TYR A C     
1409 O  O     . TYR A 198 ? 0.2443 0.3713 0.3607 0.0075  -0.0587 0.0025  178 TYR A O     
1410 C  CB    . TYR A 198 ? 0.2033 0.3377 0.3132 -0.0042 -0.0447 0.0039  178 TYR A CB    
1411 C  CG    . TYR A 198 ? 0.2030 0.3212 0.3031 -0.0030 -0.0425 0.0071  178 TYR A CG    
1412 C  CD1   . TYR A 198 ? 0.2234 0.3330 0.3138 -0.0087 -0.0394 0.0110  178 TYR A CD1   
1413 C  CD2   . TYR A 198 ? 0.2029 0.3149 0.3039 0.0039  -0.0438 0.0059  178 TYR A CD2   
1414 C  CE1   . TYR A 198 ? 0.2029 0.2991 0.2852 -0.0073 -0.0373 0.0133  178 TYR A CE1   
1415 C  CE2   . TYR A 198 ? 0.2267 0.3250 0.3190 0.0046  -0.0416 0.0087  178 TYR A CE2   
1416 C  CZ    . TYR A 198 ? 0.2522 0.3435 0.3357 -0.0009 -0.0382 0.0122  178 TYR A CZ    
1417 O  OH    . TYR A 198 ? 0.2559 0.3348 0.3316 0.0001  -0.0361 0.0144  178 TYR A OH    
1418 N  N     . PRO A 199 ? 0.2349 0.3374 0.3308 0.0012  -0.0561 0.0108  179 PRO A N     
1419 C  CA    . PRO A 199 ? 0.2649 0.3566 0.3583 0.0068  -0.0612 0.0117  179 PRO A CA    
1420 C  C     . PRO A 199 ? 0.2403 0.3292 0.3354 0.0120  -0.0598 0.0100  179 PRO A C     
1421 O  O     . PRO A 199 ? 0.2533 0.3365 0.3426 0.0105  -0.0550 0.0115  179 PRO A O     
1422 C  CB    . PRO A 199 ? 0.3040 0.3802 0.3842 0.0031  -0.0613 0.0166  179 PRO A CB    
1423 C  CG    . PRO A 199 ? 0.4070 0.4858 0.4838 -0.0036 -0.0571 0.0179  179 PRO A CG    
1424 C  CD    . PRO A 199 ? 0.2982 0.3906 0.3831 -0.0045 -0.0530 0.0148  179 PRO A CD    
1425 N  N     . ALA A 200 ? 0.3116 0.4043 0.4147 0.0183  -0.0644 0.0068  180 ALA A N     
1426 C  CA    . ALA A 200 ? 0.2877 0.3779 0.3930 0.0237  -0.0639 0.0047  180 ALA A CA    
1427 C  C     . ALA A 200 ? 0.2840 0.3568 0.3772 0.0230  -0.0629 0.0092  180 ALA A C     
1428 O  O     . ALA A 200 ? 0.2946 0.3559 0.3797 0.0217  -0.0664 0.0130  180 ALA A O     
1429 C  CB    . ALA A 200 ? 0.3576 0.4508 0.4718 0.0309  -0.0709 0.0009  180 ALA A CB    
1430 N  N     . GLY A 201 ? 0.2164 0.2878 0.3081 0.0234  -0.0581 0.0087  181 GLY A N     
1431 C  CA    . GLY A 201 ? 0.2672 0.3238 0.3488 0.0233  -0.0572 0.0123  181 GLY A CA    
1432 C  C     . GLY A 201 ? 0.3161 0.3647 0.3869 0.0174  -0.0538 0.0166  181 GLY A C     
1433 O  O     . GLY A 201 ? 0.2494 0.2861 0.3115 0.0170  -0.0538 0.0196  181 GLY A O     
1434 N  N     . TYR A 202 ? 0.2374 0.2926 0.3087 0.0129  -0.0510 0.0167  182 TYR A N     
1435 C  CA    . TYR A 202 ? 0.2206 0.2678 0.2820 0.0078  -0.0494 0.0203  182 TYR A CA    
1436 C  C     . TYR A 202 ? 0.2629 0.3024 0.3172 0.0066  -0.0446 0.0219  182 TYR A C     
1437 O  O     . TYR A 202 ? 0.2575 0.2866 0.3028 0.0053  -0.0449 0.0245  182 TYR A O     
1438 C  CB    . TYR A 202 ? 0.2392 0.2946 0.3027 0.0031  -0.0479 0.0199  182 TYR A CB    
1439 C  CG    . TYR A 202 ? 0.2247 0.2714 0.2786 -0.0015 -0.0478 0.0230  182 TYR A CG    
1440 C  CD1   . TYR A 202 ? 0.2811 0.3214 0.3304 -0.0016 -0.0522 0.0247  182 TYR A CD1   
1441 C  CD2   . TYR A 202 ? 0.2402 0.2848 0.2894 -0.0055 -0.0436 0.0239  182 TYR A CD2   
1442 C  CE1   . TYR A 202 ? 0.3133 0.3460 0.3537 -0.0054 -0.0521 0.0269  182 TYR A CE1   
1443 C  CE2   . TYR A 202 ? 0.2505 0.2870 0.2912 -0.0090 -0.0440 0.0260  182 TYR A CE2   
1444 C  CZ    . TYR A 202 ? 0.2587 0.2897 0.2952 -0.0088 -0.0480 0.0272  182 TYR A CZ    
1445 O  OH    . TYR A 202 ? 0.3081 0.3315 0.3362 -0.0120 -0.0484 0.0286  182 TYR A OH    
1446 N  N     . LEU A 203 ? 0.2093 0.2546 0.2671 0.0065  -0.0402 0.0202  183 LEU A N     
1447 C  CA    . LEU A 203 ? 0.2073 0.2458 0.2586 0.0050  -0.0359 0.0216  183 LEU A CA    
1448 C  C     . LEU A 203 ? 0.2198 0.2495 0.2673 0.0084  -0.0367 0.0225  183 LEU A C     
1449 O  O     . LEU A 203 ? 0.2368 0.2580 0.2765 0.0069  -0.0350 0.0246  183 LEU A O     
1450 C  CB    . LEU A 203 ? 0.2235 0.2700 0.2792 0.0039  -0.0315 0.0197  183 LEU A CB    
1451 C  CG    . LEU A 203 ? 0.2184 0.2708 0.2743 -0.0015 -0.0297 0.0199  183 LEU A CG    
1452 C  CD1   . LEU A 203 ? 0.2361 0.2994 0.2980 -0.0025 -0.0263 0.0175  183 LEU A CD1   
1453 C  CD2   . LEU A 203 ? 0.2458 0.2882 0.2923 -0.0050 -0.0282 0.0226  183 LEU A CD2   
1454 N  N     . GLU A 204 ? 0.2177 0.2494 0.2708 0.0128  -0.0397 0.0208  184 GLU A N     
1455 C  CA    . GLU A 204 ? 0.2146 0.2369 0.2635 0.0155  -0.0415 0.0221  184 GLU A CA    
1456 C  C     . GLU A 204 ? 0.2495 0.2619 0.2894 0.0134  -0.0444 0.0256  184 GLU A C     
1457 O  O     . GLU A 204 ? 0.2505 0.2548 0.2828 0.0122  -0.0430 0.0277  184 GLU A O     
1458 C  CB    . GLU A 204 ? 0.2821 0.3073 0.3385 0.0208  -0.0456 0.0195  184 GLU A CB    
1459 C  CG    . GLU A 204 ? 0.2462 0.2607 0.2978 0.0231  -0.0482 0.0211  184 GLU A CG    
1460 C  CD    . GLU A 204 ? 0.3901 0.4056 0.4488 0.0288  -0.0537 0.0184  184 GLU A CD    
1461 O  OE1   . GLU A 204 ? 0.3705 0.3971 0.4392 0.0316  -0.0544 0.0143  184 GLU A OE1   
1462 O  OE2   . GLU A 204 ? 0.3210 0.3262 0.3752 0.0304  -0.0577 0.0201  184 GLU A OE2   
1463 N  N     . GLY A 205 ? 0.2472 0.2610 0.2878 0.0127  -0.0483 0.0260  185 GLY A N     
1464 C  CA    . GLY A 205 ? 0.2361 0.2411 0.2677 0.0103  -0.0512 0.0291  185 GLY A CA    
1465 C  C     . GLY A 205 ? 0.3295 0.3313 0.3534 0.0061  -0.0469 0.0304  185 GLY A C     
1466 O  O     . GLY A 205 ? 0.3106 0.3047 0.3259 0.0043  -0.0468 0.0324  185 GLY A O     
1467 N  N     . VAL A 206 ? 0.2608 0.2685 0.2876 0.0043  -0.0434 0.0290  186 VAL A N     
1468 C  CA    . VAL A 206 ? 0.2809 0.2852 0.3010 0.0008  -0.0401 0.0297  186 VAL A CA    
1469 C  C     . VAL A 206 ? 0.2829 0.2824 0.2986 0.0011  -0.0363 0.0300  186 VAL A C     
1470 O  O     . VAL A 206 ? 0.3079 0.3017 0.3159 -0.0007 -0.0354 0.0309  186 VAL A O     
1471 C  CB    . VAL A 206 ? 0.2974 0.3083 0.3216 -0.0014 -0.0381 0.0284  186 VAL A CB    
1472 C  CG1   . VAL A 206 ? 0.4154 0.4224 0.4342 -0.0037 -0.0344 0.0285  186 VAL A CG1   
1473 C  CG2   . VAL A 206 ? 0.3257 0.3392 0.3509 -0.0032 -0.0419 0.0286  186 VAL A CG2   
1474 N  N     . VAL A 207 ? 0.2233 0.2257 0.2439 0.0034  -0.0342 0.0290  187 VAL A N     
1475 C  CA    . VAL A 207 ? 0.2475 0.2459 0.2645 0.0037  -0.0307 0.0292  187 VAL A CA    
1476 C  C     . VAL A 207 ? 0.2902 0.2819 0.3017 0.0042  -0.0328 0.0310  187 VAL A C     
1477 O  O     . VAL A 207 ? 0.2860 0.2733 0.2910 0.0025  -0.0307 0.0317  187 VAL A O     
1478 C  CB    . VAL A 207 ? 0.2349 0.2384 0.2584 0.0057  -0.0281 0.0276  187 VAL A CB    
1479 C  CG1   . VAL A 207 ? 0.2627 0.2618 0.2826 0.0062  -0.0251 0.0279  187 VAL A CG1   
1480 C  CG2   . VAL A 207 ? 0.2642 0.2739 0.2913 0.0038  -0.0259 0.0263  187 VAL A CG2   
1481 N  N     . LYS A 208 ? 0.2459 0.2368 0.2599 0.0062  -0.0373 0.0315  188 LYS A N     
1482 C  CA    . LYS A 208 ? 0.2873 0.2709 0.2958 0.0063  -0.0400 0.0336  188 LYS A CA    
1483 C  C     . LYS A 208 ? 0.2858 0.2642 0.2849 0.0026  -0.0413 0.0358  188 LYS A C     
1484 O  O     . LYS A 208 ? 0.2922 0.2649 0.2843 0.0008  -0.0415 0.0377  188 LYS A O     
1485 C  CB    . LYS A 208 ? 0.3438 0.3271 0.3575 0.0097  -0.0457 0.0335  188 LYS A CB    
1486 C  CG    . LYS A 208 ? 0.4620 0.4365 0.4703 0.0098  -0.0499 0.0359  188 LYS A CG    
1487 C  CD    . LYS A 208 ? 0.4952 0.4688 0.5088 0.0135  -0.0569 0.0355  188 LYS A CD    
1488 C  CE    . LYS A 208 ? 0.6110 0.5928 0.6360 0.0183  -0.0560 0.0315  188 LYS A CE    
1489 N  NZ    . LYS A 208 ? 0.6757 0.6568 0.7067 0.0228  -0.0632 0.0301  188 LYS A NZ    
1490 N  N     . THR A 209 ? 0.2533 0.2336 0.2516 0.0010  -0.0421 0.0355  189 THR A N     
1491 C  CA    . THR A 209 ? 0.2550 0.2311 0.2445 -0.0025 -0.0437 0.0371  189 THR A CA    
1492 C  C     . THR A 209 ? 0.2650 0.2423 0.2504 -0.0049 -0.0392 0.0357  189 THR A C     
1493 O  O     . THR A 209 ? 0.2950 0.2700 0.2732 -0.0077 -0.0399 0.0361  189 THR A O     
1494 C  CB    . THR A 209 ? 0.3148 0.2912 0.3055 -0.0026 -0.0490 0.0379  189 THR A CB    
1495 O  OG1   . THR A 209 ? 0.2945 0.2774 0.2917 -0.0019 -0.0478 0.0358  189 THR A OG1   
1496 C  CG2   . THR A 209 ? 0.3499 0.3245 0.3447 0.0004  -0.0544 0.0389  189 THR A CG2   
1497 N  N     . SER A 210 ? 0.2582 0.2389 0.2477 -0.0038 -0.0350 0.0337  190 SER A N     
1498 C  CA    . SER A 210 ? 0.2753 0.2565 0.2617 -0.0054 -0.0318 0.0319  190 SER A CA    
1499 C  C     . SER A 210 ? 0.2657 0.2441 0.2445 -0.0071 -0.0294 0.0316  190 SER A C     
1500 O  O     . SER A 210 ? 0.2796 0.2573 0.2580 -0.0066 -0.0277 0.0322  190 SER A O     
1501 C  CB    . SER A 210 ? 0.2350 0.2196 0.2273 -0.0040 -0.0287 0.0302  190 SER A CB    
1502 O  OG    . SER A 210 ? 0.2495 0.2331 0.2384 -0.0051 -0.0263 0.0283  190 SER A OG    
1503 N  N     . THR A 211 ? 0.2415 0.2193 0.2148 -0.0091 -0.0291 0.0302  191 THR A N     
1504 C  CA    . THR A 211 ? 0.2668 0.2443 0.2340 -0.0105 -0.0260 0.0285  191 THR A CA    
1505 C  C     . THR A 211 ? 0.2654 0.2444 0.2342 -0.0093 -0.0231 0.0250  191 THR A C     
1506 O  O     . THR A 211 ? 0.2932 0.2730 0.2578 -0.0099 -0.0207 0.0225  191 THR A O     
1507 C  CB    . THR A 211 ? 0.3610 0.3371 0.3198 -0.0138 -0.0278 0.0289  191 THR A CB    
1508 O  OG1   . THR A 211 ? 0.3777 0.3535 0.3362 -0.0142 -0.0301 0.0279  191 THR A OG1   
1509 C  CG2   . THR A 211 ? 0.3554 0.3287 0.3114 -0.0154 -0.0311 0.0327  191 THR A CG2   
1510 N  N     . THR A 212 ? 0.2521 0.2316 0.2266 -0.0078 -0.0237 0.0246  192 THR A N     
1511 C  CA    . THR A 212 ? 0.2507 0.2299 0.2265 -0.0069 -0.0221 0.0217  192 THR A CA    
1512 C  C     . THR A 212 ? 0.2418 0.2221 0.2227 -0.0050 -0.0197 0.0217  192 THR A C     
1513 O  O     . THR A 212 ? 0.2472 0.2265 0.2285 -0.0041 -0.0185 0.0193  192 THR A O     
1514 C  CB    . THR A 212 ? 0.2935 0.2717 0.2710 -0.0076 -0.0248 0.0215  192 THR A CB    
1515 O  OG1   . THR A 212 ? 0.3075 0.2880 0.2915 -0.0072 -0.0256 0.0238  192 THR A OG1   
1516 C  CG2   . THR A 212 ? 0.3318 0.3089 0.3046 -0.0095 -0.0276 0.0217  192 THR A CG2   
1517 N  N     . THR A 213 ? 0.2243 0.2061 0.2090 -0.0043 -0.0194 0.0240  193 THR A N     
1518 C  CA    . THR A 213 ? 0.2182 0.2011 0.2071 -0.0027 -0.0169 0.0239  193 THR A CA    
1519 C  C     . THR A 213 ? 0.2182 0.2005 0.2043 -0.0021 -0.0141 0.0216  193 THR A C     
1520 O  O     . THR A 213 ? 0.2442 0.2267 0.2258 -0.0029 -0.0134 0.0210  193 THR A O     
1521 C  CB    . THR A 213 ? 0.2357 0.2197 0.2273 -0.0018 -0.0171 0.0261  193 THR A CB    
1522 O  OG1   . THR A 213 ? 0.2155 0.2015 0.2116 -0.0016 -0.0195 0.0272  193 THR A OG1   
1523 C  CG2   . THR A 213 ? 0.2357 0.2206 0.2303 -0.0003 -0.0142 0.0258  193 THR A CG2   
1524 N  N     . LYS A 214 ? 0.2152 0.1973 0.2040 -0.0009 -0.0129 0.0203  194 LYS A N     
1525 C  CA    . LYS A 214 ? 0.2244 0.2060 0.2113 0.0001  -0.0111 0.0173  194 LYS A CA    
1526 C  C     . LYS A 214 ? 0.2386 0.2211 0.2290 0.0015  -0.0089 0.0177  194 LYS A C     
1527 O  O     . LYS A 214 ? 0.2266 0.2087 0.2206 0.0017  -0.0093 0.0188  194 LYS A O     
1528 C  CB    . LYS A 214 ? 0.2599 0.2387 0.2458 0.0005  -0.0129 0.0148  194 LYS A CB    
1529 C  CG    . LYS A 214 ? 0.3508 0.3290 0.3360 0.0024  -0.0118 0.0110  194 LYS A CG    
1530 C  CD    . LYS A 214 ? 0.3502 0.3296 0.3312 0.0027  -0.0117 0.0075  194 LYS A CD    
1531 C  CE    . LYS A 214 ? 0.4152 0.3912 0.3937 0.0021  -0.0150 0.0062  194 LYS A CE    
1532 N  NZ    . LYS A 214 ? 0.3546 0.3330 0.3284 0.0019  -0.0144 0.0027  194 LYS A NZ    
1533 N  N     . ALA A 215 ? 0.2148 0.1990 0.2040 0.0020  -0.0066 0.0166  195 ALA A N     
1534 C  CA    . ALA A 215 ? 0.2064 0.1914 0.1986 0.0032  -0.0046 0.0166  195 ALA A CA    
1535 C  C     . ALA A 215 ? 0.2371 0.2218 0.2292 0.0048  -0.0040 0.0131  195 ALA A C     
1536 O  O     . ALA A 215 ? 0.2443 0.2302 0.2337 0.0051  -0.0040 0.0100  195 ALA A O     
1537 C  CB    . ALA A 215 ? 0.2305 0.2174 0.2217 0.0025  -0.0029 0.0181  195 ALA A CB    
1538 N  N     . ARG A 216 ? 0.2042 0.1877 0.1995 0.0060  -0.0038 0.0132  196 ARG A N     
1539 C  CA    . ARG A 216 ? 0.2052 0.1876 0.2011 0.0079  -0.0042 0.0100  196 ARG A CA    
1540 C  C     . ARG A 216 ? 0.2015 0.1855 0.1998 0.0088  -0.0021 0.0104  196 ARG A C     
1541 O  O     . ARG A 216 ? 0.1985 0.1816 0.1990 0.0083  -0.0019 0.0130  196 ARG A O     
1542 C  CB    . ARG A 216 ? 0.2260 0.2033 0.2222 0.0080  -0.0073 0.0100  196 ARG A CB    
1543 C  CG    . ARG A 216 ? 0.2233 0.1979 0.2201 0.0104  -0.0089 0.0067  196 ARG A CG    
1544 C  CD    . ARG A 216 ? 0.3282 0.2966 0.3248 0.0095  -0.0125 0.0080  196 ARG A CD    
1545 N  NE    . ARG A 216 ? 0.3979 0.3666 0.3963 0.0078  -0.0114 0.0115  196 ARG A NE    
1546 C  CZ    . ARG A 216 ? 0.4966 0.4616 0.4946 0.0055  -0.0137 0.0138  196 ARG A CZ    
1547 N  NH1   . ARG A 216 ? 0.5316 0.4911 0.5271 0.0044  -0.0177 0.0135  196 ARG A NH1   
1548 N  NH2   . ARG A 216 ? 0.3322 0.2992 0.3319 0.0038  -0.0121 0.0165  196 ARG A NH2   
1549 N  N     . LEU A 217 ? 0.2074 0.1947 0.2055 0.0100  -0.0006 0.0074  197 LEU A N     
1550 C  CA    . LEU A 217 ? 0.2145 0.2036 0.2148 0.0109  0.0012  0.0071  197 LEU A CA    
1551 C  C     . LEU A 217 ? 0.2048 0.1919 0.2068 0.0135  -0.0008 0.0037  197 LEU A C     
1552 O  O     . LEU A 217 ? 0.2463 0.2347 0.2476 0.0152  -0.0017 -0.0005 197 LEU A O     
1553 C  CB    . LEU A 217 ? 0.2289 0.2238 0.2280 0.0099  0.0039  0.0061  197 LEU A CB    
1554 C  CG    . LEU A 217 ? 0.2581 0.2557 0.2592 0.0100  0.0060  0.0062  197 LEU A CG    
1555 C  CD1   . LEU A 217 ? 0.2259 0.2208 0.2279 0.0088  0.0063  0.0106  197 LEU A CD1   
1556 C  CD2   . LEU A 217 ? 0.2589 0.2628 0.2579 0.0082  0.0084  0.0047  197 LEU A CD2   
1557 N  N     . LEU A 218 ? 0.1994 0.1831 0.2032 0.0140  -0.0019 0.0052  198 LEU A N     
1558 C  CA    . LEU A 218 ? 0.2121 0.1918 0.2169 0.0162  -0.0050 0.0027  198 LEU A CA    
1559 C  C     . LEU A 218 ? 0.2152 0.1970 0.2227 0.0177  -0.0040 0.0015  198 LEU A C     
1560 O  O     . LEU A 218 ? 0.2424 0.2254 0.2507 0.0163  -0.0020 0.0045  198 LEU A O     
1561 C  CB    . LEU A 218 ? 0.2266 0.1997 0.2304 0.0145  -0.0080 0.0059  198 LEU A CB    
1562 C  CG    . LEU A 218 ? 0.3630 0.3292 0.3663 0.0157  -0.0125 0.0047  198 LEU A CG    
1563 C  CD1   . LEU A 218 ? 0.3183 0.2820 0.3206 0.0181  -0.0157 0.0004  198 LEU A CD1   
1564 C  CD2   . LEU A 218 ? 0.4099 0.3712 0.4114 0.0122  -0.0145 0.0089  198 LEU A CD2   
1565 N  N     . HIS A 219 ? 0.2513 0.2332 0.2602 0.0209  -0.0060 -0.0030 199 HIS A N     
1566 C  CA    . HIS A 219 ? 0.2318 0.2160 0.2437 0.0229  -0.0058 -0.0050 199 HIS A CA    
1567 C  C     . HIS A 219 ? 0.2493 0.2265 0.2618 0.0255  -0.0111 -0.0069 199 HIS A C     
1568 O  O     . HIS A 219 ? 0.2753 0.2509 0.2881 0.0283  -0.0142 -0.0113 199 HIS A O     
1569 C  CB    . HIS A 219 ? 0.2168 0.2099 0.2305 0.0245  -0.0033 -0.0098 199 HIS A CB    
1570 C  CG    . HIS A 219 ? 0.2203 0.2171 0.2379 0.0269  -0.0034 -0.0127 199 HIS A CG    
1571 N  ND1   . HIS A 219 ? 0.1967 0.1959 0.2155 0.0252  -0.0009 -0.0100 199 HIS A ND1   
1572 C  CD2   . HIS A 219 ? 0.2271 0.2256 0.2479 0.0310  -0.0060 -0.0185 199 HIS A CD2   
1573 C  CE1   . HIS A 219 ? 0.1972 0.1999 0.2196 0.0279  -0.0018 -0.0138 199 HIS A CE1   
1574 N  NE2   . HIS A 219 ? 0.2161 0.2186 0.2401 0.0316  -0.0049 -0.0190 199 HIS A NE2   
1575 N  N     . TYR A 220 ? 0.2131 0.1856 0.2255 0.0244  -0.0126 -0.0037 200 TYR A N     
1576 C  CA    . TYR A 220 ? 0.2509 0.2166 0.2637 0.0266  -0.0180 -0.0052 200 TYR A CA    
1577 C  C     . TYR A 220 ? 0.2464 0.2170 0.2634 0.0302  -0.0179 -0.0094 200 TYR A C     
1578 O  O     . TYR A 220 ? 0.2453 0.2211 0.2640 0.0291  -0.0143 -0.0080 200 TYR A O     
1579 C  CB    . TYR A 220 ? 0.2734 0.2326 0.2837 0.0233  -0.0196 0.0000  200 TYR A CB    
1580 C  CG    . TYR A 220 ? 0.3030 0.2563 0.3092 0.0196  -0.0214 0.0038  200 TYR A CG    
1581 C  CD1   . TYR A 220 ? 0.3125 0.2697 0.3179 0.0165  -0.0173 0.0070  200 TYR A CD1   
1582 C  CD2   . TYR A 220 ? 0.3662 0.3099 0.3695 0.0191  -0.0276 0.0043  200 TYR A CD2   
1583 C  CE1   . TYR A 220 ? 0.3441 0.2973 0.3464 0.0129  -0.0189 0.0102  200 TYR A CE1   
1584 C  CE2   . TYR A 220 ? 0.3259 0.2647 0.3253 0.0150  -0.0293 0.0080  200 TYR A CE2   
1585 C  CZ    . TYR A 220 ? 0.3316 0.2759 0.3308 0.0119  -0.0247 0.0108  200 TYR A CZ    
1586 O  OH    . TYR A 220 ? 0.4124 0.3532 0.4083 0.0076  -0.0263 0.0140  200 TYR A OH    
1587 N  N     . PHE A 221 ? 0.2509 0.2205 0.2699 0.0345  -0.0219 -0.0151 201 PHE A N     
1588 C  CA    . PHE A 221 ? 0.2454 0.2204 0.2693 0.0386  -0.0225 -0.0201 201 PHE A CA    
1589 C  C     . PHE A 221 ? 0.3073 0.2756 0.3314 0.0389  -0.0265 -0.0180 201 PHE A C     
1590 O  O     . PHE A 221 ? 0.3400 0.2974 0.3604 0.0375  -0.0313 -0.0149 201 PHE A O     
1591 C  CB    . PHE A 221 ? 0.2691 0.2451 0.2955 0.0438  -0.0262 -0.0276 201 PHE A CB    
1592 C  CG    . PHE A 221 ? 0.2566 0.2420 0.2833 0.0437  -0.0217 -0.0310 201 PHE A CG    
1593 C  CD1   . PHE A 221 ? 0.2501 0.2486 0.2807 0.0447  -0.0172 -0.0352 201 PHE A CD1   
1594 C  CD2   . PHE A 221 ? 0.2626 0.2442 0.2852 0.0419  -0.0218 -0.0296 201 PHE A CD2   
1595 C  CE1   . PHE A 221 ? 0.2765 0.2840 0.3066 0.0438  -0.0131 -0.0381 201 PHE A CE1   
1596 C  CE2   . PHE A 221 ? 0.2353 0.2257 0.2576 0.0415  -0.0178 -0.0327 201 PHE A CE2   
1597 C  CZ    . PHE A 221 ? 0.2854 0.2885 0.3111 0.0423  -0.0134 -0.0367 201 PHE A CZ    
1598 N  N     . PRO A 222 ? 0.2612 0.2356 0.2891 0.0401  -0.0248 -0.0195 202 PRO A N     
1599 C  CA    . PRO A 222 ? 0.2879 0.2560 0.3160 0.0406  -0.0291 -0.0178 202 PRO A CA    
1600 C  C     . PRO A 222 ? 0.3874 0.3469 0.4161 0.0450  -0.0374 -0.0216 202 PRO A C     
1601 O  O     . PRO A 222 ? 0.3838 0.3462 0.4155 0.0494  -0.0392 -0.0278 202 PRO A O     
1602 C  CB    . PRO A 222 ? 0.3335 0.3120 0.3666 0.0418  -0.0255 -0.0202 202 PRO A CB    
1603 C  CG    . PRO A 222 ? 0.2971 0.2855 0.3304 0.0394  -0.0184 -0.0199 202 PRO A CG    
1604 C  CD    . PRO A 222 ? 0.2677 0.2551 0.2992 0.0401  -0.0188 -0.0219 202 PRO A CD    
1605 N  N     . GLU A 223 ? 0.3757 0.3244 0.4011 0.0436  -0.0428 -0.0179 203 GLU A N     
1606 C  CA    . GLU A 223 ? 0.4993 0.4379 0.5246 0.0476  -0.0519 -0.0211 203 GLU A CA    
1607 C  C     . GLU A 223 ? 0.4160 0.3488 0.4410 0.0476  -0.0565 -0.0191 203 GLU A C     
1608 O  O     . GLU A 223 ? 0.3782 0.3111 0.4004 0.0429  -0.0533 -0.0135 203 GLU A O     
1609 C  CB    . GLU A 223 ? 0.5581 0.4851 0.5771 0.0451  -0.0561 -0.0181 203 GLU A CB    
1610 C  CG    . GLU A 223 ? 0.7645 0.6798 0.7829 0.0494  -0.0663 -0.0218 203 GLU A CG    
1611 C  CD    . GLU A 223 ? 0.9035 0.8054 0.9143 0.0451  -0.0713 -0.0171 203 GLU A CD    
1612 O  OE1   . GLU A 223 ? 0.9593 0.8608 0.9652 0.0384  -0.0672 -0.0105 203 GLU A OE1   
1613 O  OE2   . GLU A 223 ? 1.0823 0.9743 1.0920 0.0485  -0.0795 -0.0205 203 GLU A OE2   
1614 N  N     . GLU A 224 ? 0.6013 0.5294 0.6295 0.0533  -0.0641 -0.0242 204 GLU A N     
1615 C  CA    . GLU A 224 ? 0.5983 0.5207 0.6267 0.0541  -0.0697 -0.0232 204 GLU A CA    
1616 C  C     . GLU A 224 ? 0.5456 0.4504 0.5660 0.0510  -0.0782 -0.0181 204 GLU A C     
1617 O  O     . GLU A 224 ? 0.5634 0.4594 0.5806 0.0514  -0.0831 -0.0187 204 GLU A O     
1618 C  CB    . GLU A 224 ? 0.6695 0.5966 0.7062 0.0623  -0.0741 -0.0318 204 GLU A CB    
1619 C  CG    . GLU A 224 ? 0.6596 0.6052 0.7041 0.0650  -0.0661 -0.0373 204 GLU A CG    
1620 C  CD    . GLU A 224 ? 0.9778 0.9294 1.0309 0.0734  -0.0707 -0.0471 204 GLU A CD    
1621 O  OE1   . GLU A 224 ? 0.9784 0.9231 1.0333 0.0768  -0.0786 -0.0487 204 GLU A OE1   
1622 O  OE2   . GLU A 224 ? 1.0780 1.0414 1.1360 0.0764  -0.0666 -0.0535 204 GLU A OE2   
1623 N  N     . ALA A 225 ? 0.6210 0.5207 0.6379 0.0473  -0.0801 -0.0131 205 ALA A N     
1624 C  CA    . ALA A 225 ? 0.7234 0.6068 0.7314 0.0426  -0.0878 -0.0072 205 ALA A CA    
1625 C  C     . ALA A 225 ? 0.7471 0.6173 0.7545 0.0474  -0.0996 -0.0109 205 ALA A C     
1626 O  O     . ALA A 225 ? 0.7529 0.6249 0.7670 0.0547  -0.1041 -0.0174 205 ALA A O     
1627 C  CB    . ALA A 225 ? 0.7476 0.6293 0.7527 0.0387  -0.0881 -0.0024 205 ALA A CB    
1628 N  N     . CYS A 246 ? 0.8145 0.6586 0.7468 -0.0508 -0.0918 0.0423  226 CYS A N     
1629 C  CA    . CYS A 246 ? 0.7750 0.6364 0.7118 -0.0542 -0.0825 0.0446  226 CYS A CA    
1630 C  C     . CYS A 246 ? 0.7554 0.6266 0.6996 -0.0467 -0.0754 0.0414  226 CYS A C     
1631 O  O     . CYS A 246 ? 0.6543 0.5277 0.6035 -0.0384 -0.0731 0.0364  226 CYS A O     
1632 C  CB    . CYS A 246 ? 0.8481 0.7191 0.7880 -0.0560 -0.0785 0.0444  226 CYS A CB    
1633 S  SG    . CYS A 246 ? 0.7263 0.6174 0.6708 -0.0618 -0.0691 0.0475  226 CYS A SG    
1634 N  N     . ALA A 247 ? 0.5113 0.3884 0.4555 -0.0500 -0.0719 0.0442  227 ALA A N     
1635 C  CA    . ALA A 247 ? 0.5415 0.4268 0.4919 -0.0435 -0.0657 0.0415  227 ALA A CA    
1636 C  C     . ALA A 247 ? 0.4665 0.3680 0.4242 -0.0415 -0.0568 0.0401  227 ALA A C     
1637 O  O     . ALA A 247 ? 0.4449 0.3522 0.4082 -0.0346 -0.0521 0.0368  227 ALA A O     
1638 C  CB    . ALA A 247 ? 0.6353 0.5198 0.5827 -0.0475 -0.0660 0.0447  227 ALA A CB    
1639 N  N     . THR A 248 ? 0.3846 0.2935 0.3422 -0.0474 -0.0546 0.0425  228 THR A N     
1640 C  CA    . THR A 248 ? 0.3474 0.2712 0.3121 -0.0454 -0.0470 0.0411  228 THR A CA    
1641 C  C     . THR A 248 ? 0.3469 0.2712 0.3141 -0.0415 -0.0471 0.0384  228 THR A C     
1642 O  O     . THR A 248 ? 0.3770 0.2915 0.3402 -0.0421 -0.0527 0.0381  228 THR A O     
1643 C  CB    . THR A 248 ? 0.3028 0.2371 0.2675 -0.0534 -0.0441 0.0444  228 THR A CB    
1644 O  OG1   . THR A 248 ? 0.3868 0.3158 0.3462 -0.0603 -0.0491 0.0470  228 THR A OG1   
1645 C  CG2   . THR A 248 ? 0.3481 0.2842 0.3104 -0.0574 -0.0430 0.0468  228 THR A CG2   
1646 N  N     . HIS A 249 ? 0.3068 0.2423 0.2803 -0.0378 -0.0409 0.0366  229 HIS A N     
1647 C  CA    . HIS A 249 ? 0.3231 0.2615 0.2991 -0.0354 -0.0402 0.0347  229 HIS A CA    
1648 C  C     . HIS A 249 ? 0.2881 0.2405 0.2695 -0.0367 -0.0347 0.0353  229 HIS A C     
1649 O  O     . HIS A 249 ? 0.2745 0.2346 0.2586 -0.0379 -0.0309 0.0362  229 HIS A O     
1650 C  CB    . HIS A 249 ? 0.3120 0.2475 0.2899 -0.0274 -0.0395 0.0305  229 HIS A CB    
1651 C  CG    . HIS A 249 ? 0.2924 0.2358 0.2753 -0.0228 -0.0338 0.0291  229 HIS A CG    
1652 N  ND1   . HIS A 249 ? 0.2770 0.2179 0.2597 -0.0208 -0.0333 0.0287  229 HIS A ND1   
1653 C  CD2   . HIS A 249 ? 0.2541 0.2070 0.2418 -0.0202 -0.0288 0.0282  229 HIS A CD2   
1654 C  CE1   . HIS A 249 ? 0.2606 0.2095 0.2479 -0.0173 -0.0280 0.0275  229 HIS A CE1   
1655 N  NE2   . HIS A 249 ? 0.2748 0.2304 0.2649 -0.0168 -0.0254 0.0272  229 HIS A NE2   
1656 N  N     . LEU A 250 ? 0.2796 0.2350 0.2627 -0.0361 -0.0346 0.0345  230 LEU A N     
1657 C  CA    . LEU A 250 ? 0.2619 0.2297 0.2510 -0.0354 -0.0302 0.0341  230 LEU A CA    
1658 C  C     . LEU A 250 ? 0.2469 0.2146 0.2384 -0.0285 -0.0285 0.0312  230 LEU A C     
1659 O  O     . LEU A 250 ? 0.2893 0.2493 0.2777 -0.0264 -0.0314 0.0296  230 LEU A O     
1660 C  CB    . LEU A 250 ? 0.2961 0.2679 0.2852 -0.0407 -0.0320 0.0356  230 LEU A CB    
1661 C  CG    . LEU A 250 ? 0.3559 0.3292 0.3421 -0.0492 -0.0339 0.0387  230 LEU A CG    
1662 C  CD1   . LEU A 250 ? 0.3641 0.3407 0.3502 -0.0540 -0.0361 0.0397  230 LEU A CD1   
1663 C  CD2   . LEU A 250 ? 0.3138 0.2987 0.3041 -0.0506 -0.0291 0.0391  230 LEU A CD2   
1664 N  N     . ASP A 251 ? 0.2391 0.2152 0.2357 -0.0254 -0.0240 0.0303  231 ASP A N     
1665 C  CA    . ASP A 251 ? 0.2361 0.2128 0.2343 -0.0203 -0.0227 0.0283  231 ASP A CA    
1666 C  C     . ASP A 251 ? 0.2697 0.2489 0.2684 -0.0219 -0.0244 0.0285  231 ASP A C     
1667 O  O     . ASP A 251 ? 0.2421 0.2274 0.2430 -0.0258 -0.0246 0.0300  231 ASP A O     
1668 C  CB    . ASP A 251 ? 0.2268 0.2106 0.2297 -0.0169 -0.0184 0.0276  231 ASP A CB    
1669 C  CG    . ASP A 251 ? 0.2263 0.2073 0.2286 -0.0144 -0.0167 0.0270  231 ASP A CG    
1670 O  OD1   . ASP A 251 ? 0.2356 0.2098 0.2343 -0.0154 -0.0188 0.0271  231 ASP A OD1   
1671 O  OD2   . ASP A 251 ? 0.2444 0.2295 0.2497 -0.0114 -0.0136 0.0263  231 ASP A OD2   
1672 N  N     . HIS A 252 ? 0.2498 0.2249 0.2465 -0.0190 -0.0257 0.0268  232 HIS A N     
1673 C  CA    A HIS A 252 ? 0.2281 0.2042 0.2243 -0.0210 -0.0280 0.0272  232 HIS A CA    
1674 C  CA    B HIS A 252 ? 0.2283 0.2036 0.2241 -0.0205 -0.0280 0.0269  232 HIS A CA    
1675 C  C     . HIS A 252 ? 0.2649 0.2480 0.2650 -0.0188 -0.0262 0.0269  232 HIS A C     
1676 O  O     . HIS A 252 ? 0.2586 0.2446 0.2596 -0.0208 -0.0280 0.0275  232 HIS A O     
1677 C  CB    A HIS A 252 ? 0.3052 0.2721 0.2959 -0.0205 -0.0316 0.0255  232 HIS A CB    
1678 C  CB    B HIS A 252 ? 0.3096 0.2763 0.3004 -0.0184 -0.0306 0.0247  232 HIS A CB    
1679 C  CG    A HIS A 252 ? 0.3068 0.2722 0.2962 -0.0159 -0.0305 0.0229  232 HIS A CG    
1680 C  CG    B HIS A 252 ? 0.2553 0.2208 0.2441 -0.0201 -0.0336 0.0245  232 HIS A CG    
1681 N  ND1   A HIS A 252 ? 0.3022 0.2627 0.2894 -0.0125 -0.0302 0.0204  232 HIS A ND1   
1682 N  ND1   B HIS A 252 ? 0.3532 0.3154 0.3397 -0.0247 -0.0374 0.0257  232 HIS A ND1   
1683 C  CD2   A HIS A 252 ? 0.2707 0.2390 0.2603 -0.0145 -0.0301 0.0223  232 HIS A CD2   
1684 C  CD2   B HIS A 252 ? 0.2677 0.2343 0.2558 -0.0181 -0.0335 0.0232  232 HIS A CD2   
1685 C  CE1   A HIS A 252 ? 0.2948 0.2562 0.2807 -0.0096 -0.0290 0.0183  232 HIS A CE1   
1686 C  CE1   B HIS A 252 ? 0.2775 0.2391 0.2625 -0.0252 -0.0395 0.0251  232 HIS A CE1   
1687 N  NE2   A HIS A 252 ? 0.3018 0.2674 0.2888 -0.0110 -0.0290 0.0197  232 HIS A NE2   
1688 N  NE2   B HIS A 252 ? 0.3775 0.3418 0.3633 -0.0212 -0.0372 0.0236  232 HIS A NE2   
1689 N  N     . GLY A 253 ? 0.2485 0.2346 0.2510 -0.0151 -0.0231 0.0263  233 GLY A N     
1690 C  CA    . GLY A 253 ? 0.2344 0.2255 0.2400 -0.0129 -0.0222 0.0262  233 GLY A CA    
1691 C  C     . GLY A 253 ? 0.2205 0.2206 0.2324 -0.0136 -0.0212 0.0270  233 GLY A C     
1692 O  O     . GLY A 253 ? 0.2346 0.2389 0.2485 -0.0172 -0.0217 0.0277  233 GLY A O     
1693 N  N     . CYS A 254 ? 0.2295 0.2330 0.2446 -0.0103 -0.0200 0.0266  234 CYS A N     
1694 C  CA    . CYS A 254 ? 0.2129 0.2253 0.2348 -0.0099 -0.0195 0.0263  234 CYS A CA    
1695 C  C     . CYS A 254 ? 0.1998 0.2150 0.2243 -0.0086 -0.0164 0.0258  234 CYS A C     
1696 O  O     . CYS A 254 ? 0.2230 0.2440 0.2504 -0.0110 -0.0152 0.0256  234 CYS A O     
1697 C  CB    . CYS A 254 ? 0.2072 0.2210 0.2313 -0.0068 -0.0211 0.0261  234 CYS A CB    
1698 S  SG    . CYS A 254 ? 0.2631 0.2763 0.2856 -0.0086 -0.0251 0.0267  234 CYS A SG    
1699 N  N     . LEU A 255 ? 0.2105 0.2219 0.2338 -0.0052 -0.0151 0.0255  235 LEU A N     
1700 C  CA    . LEU A 255 ? 0.1947 0.2082 0.2203 -0.0037 -0.0124 0.0248  235 LEU A CA    
1701 C  C     . LEU A 255 ? 0.1948 0.2009 0.2156 -0.0024 -0.0110 0.0251  235 LEU A C     
1702 O  O     . LEU A 255 ? 0.2135 0.2155 0.2316 -0.0006 -0.0117 0.0252  235 LEU A O     
1703 C  CB    . LEU A 255 ? 0.1926 0.2109 0.2235 -0.0003 -0.0125 0.0237  235 LEU A CB    
1704 C  CG    . LEU A 255 ? 0.2036 0.2316 0.2413 -0.0006 -0.0136 0.0224  235 LEU A CG    
1705 C  CD1   . LEU A 255 ? 0.1986 0.2285 0.2405 0.0037  -0.0155 0.0211  235 LEU A CD1   
1706 C  CD2   . LEU A 255 ? 0.1914 0.2267 0.2323 -0.0026 -0.0108 0.0212  235 LEU A CD2   
1707 N  N     . THR A 256 ? 0.1938 0.1989 0.2136 -0.0035 -0.0093 0.0250  236 THR A N     
1708 C  CA    . THR A 256 ? 0.1938 0.1930 0.2099 -0.0021 -0.0081 0.0249  236 THR A CA    
1709 C  C     . THR A 256 ? 0.2042 0.2054 0.2227 0.0000  -0.0058 0.0244  236 THR A C     
1710 O  O     . THR A 256 ? 0.2134 0.2181 0.2342 -0.0010 -0.0045 0.0242  236 THR A O     
1711 C  CB    . THR A 256 ? 0.1963 0.1915 0.2091 -0.0045 -0.0086 0.0251  236 THR A CB    
1712 O  OG1   . THR A 256 ? 0.2035 0.1963 0.2139 -0.0066 -0.0113 0.0253  236 THR A OG1   
1713 C  CG2   . THR A 256 ? 0.1964 0.1863 0.2063 -0.0025 -0.0077 0.0242  236 THR A CG2   
1714 N  N     . GLY A 257 ? 0.1901 0.1888 0.2075 0.0024  -0.0055 0.0243  237 GLY A N     
1715 C  CA    . GLY A 257 ? 0.1918 0.1909 0.2107 0.0043  -0.0037 0.0240  237 GLY A CA    
1716 C  C     . GLY A 257 ? 0.2037 0.1994 0.2199 0.0041  -0.0020 0.0237  237 GLY A C     
1717 O  O     . GLY A 257 ? 0.2151 0.2071 0.2278 0.0038  -0.0024 0.0235  237 GLY A O     
1718 N  N     . LEU A 258 ? 0.1888 0.1862 0.2069 0.0045  -0.0004 0.0234  238 LEU A N     
1719 C  CA    . LEU A 258 ? 0.1900 0.1847 0.2061 0.0042  0.0008  0.0232  238 LEU A CA    
1720 C  C     . LEU A 258 ? 0.2441 0.2391 0.2613 0.0059  0.0025  0.0228  238 LEU A C     
1721 O  O     . LEU A 258 ? 0.2246 0.2230 0.2448 0.0066  0.0030  0.0225  238 LEU A O     
1722 C  CB    . LEU A 258 ? 0.2122 0.2081 0.2285 0.0017  0.0007  0.0235  238 LEU A CB    
1723 C  CG    . LEU A 258 ? 0.2493 0.2449 0.2644 -0.0010 -0.0013 0.0241  238 LEU A CG    
1724 C  CD1   . LEU A 258 ? 0.3194 0.3173 0.3345 -0.0044 -0.0013 0.0249  238 LEU A CD1   
1725 C  CD2   . LEU A 258 ? 0.2380 0.2274 0.2492 -0.0007 -0.0031 0.0238  238 LEU A CD2   
1726 N  N     . THR A 259 ? 0.2447 0.2366 0.2596 0.0064  0.0032  0.0225  239 THR A N     
1727 C  CA    . THR A 259 ? 0.2630 0.2549 0.2786 0.0074  0.0048  0.0223  239 THR A CA    
1728 C  C     . THR A 259 ? 0.2313 0.2229 0.2468 0.0063  0.0052  0.0221  239 THR A C     
1729 O  O     . THR A 259 ? 0.2250 0.2148 0.2389 0.0050  0.0040  0.0222  239 THR A O     
1730 C  CB    . THR A 259 ? 0.2370 0.2268 0.2505 0.0081  0.0053  0.0220  239 THR A CB    
1731 O  OG1   . THR A 259 ? 0.2587 0.2469 0.2704 0.0080  0.0051  0.0209  239 THR A OG1   
1732 C  CG2   . THR A 259 ? 0.2559 0.2452 0.2680 0.0082  0.0045  0.0226  239 THR A CG2   
1733 N  N     . SER A 260 ? 0.2250 0.2177 0.2416 0.0067  0.0066  0.0219  240 SER A N     
1734 C  CA    . SER A 260 ? 0.2390 0.2303 0.2545 0.0057  0.0068  0.0219  240 SER A CA    
1735 C  C     . SER A 260 ? 0.2110 0.1988 0.2246 0.0067  0.0062  0.0212  240 SER A C     
1736 O  O     . SER A 260 ? 0.2642 0.2520 0.2777 0.0080  0.0067  0.0207  240 SER A O     
1737 C  CB    . SER A 260 ? 0.2753 0.2686 0.2920 0.0060  0.0083  0.0215  240 SER A CB    
1738 O  OG    . SER A 260 ? 0.3122 0.3042 0.3291 0.0078  0.0090  0.0211  240 SER A OG    
1739 N  N     . ALA A 261 ? 0.2163 0.2015 0.2285 0.0060  0.0050  0.0212  241 ALA A N     
1740 C  CA    . ALA A 261 ? 0.2204 0.2030 0.2318 0.0075  0.0039  0.0198  241 ALA A CA    
1741 C  C     . ALA A 261 ? 0.2582 0.2420 0.2706 0.0087  0.0055  0.0190  241 ALA A C     
1742 O  O     . ALA A 261 ? 0.2252 0.2099 0.2382 0.0081  0.0065  0.0198  241 ALA A O     
1743 C  CB    . ALA A 261 ? 0.2679 0.2463 0.2775 0.0066  0.0010  0.0198  241 ALA A CB    
1744 N  N     . MET A 262 ? 0.2185 0.2029 0.2311 0.0102  0.0056  0.0173  242 MET A N     
1745 C  CA    . MET A 262 ? 0.1997 0.1859 0.2134 0.0111  0.0068  0.0163  242 MET A CA    
1746 C  C     . MET A 262 ? 0.2511 0.2357 0.2652 0.0125  0.0048  0.0143  242 MET A C     
1747 O  O     . MET A 262 ? 0.2561 0.2407 0.2703 0.0138  0.0034  0.0122  242 MET A O     
1748 C  CB    . MET A 262 ? 0.2230 0.2123 0.2366 0.0111  0.0085  0.0156  242 MET A CB    
1749 C  CG    . MET A 262 ? 0.2309 0.2229 0.2455 0.0114  0.0097  0.0144  242 MET A CG    
1750 S  SD    . MET A 262 ? 0.2849 0.2817 0.2985 0.0104  0.0113  0.0131  242 MET A SD    
1751 C  CE    . MET A 262 ? 0.2729 0.2730 0.2876 0.0095  0.0127  0.0125  242 MET A CE    
1752 N  N     . PHE A 263 ? 0.2088 0.1923 0.2233 0.0124  0.0043  0.0146  243 PHE A N     
1753 C  CA    . PHE A 263 ? 0.2057 0.1879 0.2212 0.0142  0.0019  0.0124  243 PHE A CA    
1754 C  C     . PHE A 263 ? 0.2279 0.2150 0.2457 0.0153  0.0037  0.0105  243 PHE A C     
1755 O  O     . PHE A 263 ? 0.2183 0.2075 0.2362 0.0139  0.0061  0.0119  243 PHE A O     
1756 C  CB    . PHE A 263 ? 0.2204 0.1981 0.2346 0.0132  -0.0005 0.0139  243 PHE A CB    
1757 C  CG    . PHE A 263 ? 0.2170 0.1898 0.2284 0.0116  -0.0031 0.0156  243 PHE A CG    
1758 C  CD1   . PHE A 263 ? 0.2267 0.1946 0.2372 0.0127  -0.0074 0.0144  243 PHE A CD1   
1759 C  CD2   . PHE A 263 ? 0.2524 0.2258 0.2622 0.0087  -0.0015 0.0182  243 PHE A CD2   
1760 C  CE1   . PHE A 263 ? 0.2525 0.2153 0.2597 0.0104  -0.0103 0.0163  243 PHE A CE1   
1761 C  CE2   . PHE A 263 ? 0.2586 0.2284 0.2657 0.0063  -0.0038 0.0199  243 PHE A CE2   
1762 C  CZ    . PHE A 263 ? 0.3016 0.2657 0.3070 0.0068  -0.0082 0.0193  243 PHE A CZ    
1763 N  N     . VAL A 264 ? 0.2357 0.2251 0.2555 0.0176  0.0024  0.0071  244 VAL A N     
1764 C  CA    . VAL A 264 ? 0.2393 0.2352 0.2617 0.0182  0.0042  0.0046  244 VAL A CA    
1765 C  C     . VAL A 264 ? 0.1933 0.1895 0.2186 0.0210  0.0012  0.0014  244 VAL A C     
1766 O  O     . VAL A 264 ? 0.2347 0.2282 0.2606 0.0235  -0.0021 -0.0010 244 VAL A O     
1767 C  CB    . VAL A 264 ? 0.2303 0.2319 0.2530 0.0182  0.0062  0.0023  244 VAL A CB    
1768 C  CG1   . VAL A 264 ? 0.2170 0.2267 0.2419 0.0177  0.0085  0.0001  244 VAL A CG1   
1769 C  CG2   . VAL A 264 ? 0.2863 0.2866 0.3059 0.0158  0.0081  0.0055  244 VAL A CG2   
1770 N  N     . ASP A 265 ? 0.2155 0.2146 0.2426 0.0208  0.0020  0.0011  245 ASP A N     
1771 C  CA    . ASP A 265 ? 0.2404 0.2416 0.2713 0.0237  -0.0008 -0.0025 245 ASP A CA    
1772 C  C     . ASP A 265 ? 0.2421 0.2532 0.2764 0.0248  0.0013  -0.0070 245 ASP A C     
1773 O  O     . ASP A 265 ? 0.2292 0.2468 0.2643 0.0226  0.0046  -0.0068 245 ASP A O     
1774 C  CB    . ASP A 265 ? 0.2290 0.2292 0.2602 0.0227  -0.0011 -0.0008 245 ASP A CB    
1775 C  CG    . ASP A 265 ? 0.2595 0.2620 0.2949 0.0258  -0.0044 -0.0046 245 ASP A CG    
1776 O  OD1   . ASP A 265 ? 0.2624 0.2693 0.3014 0.0290  -0.0058 -0.0093 245 ASP A OD1   
1777 O  OD2   . ASP A 265 ? 0.3413 0.3410 0.3765 0.0252  -0.0058 -0.0030 245 ASP A OD2   
1778 N  N     . GLU A 266 ? 0.2460 0.2585 0.2820 0.0279  -0.0006 -0.0111 246 GLU A N     
1779 C  CA    . GLU A 266 ? 0.2134 0.2364 0.2522 0.0286  0.0017  -0.0159 246 GLU A CA    
1780 C  C     . GLU A 266 ? 0.2366 0.2679 0.2812 0.0311  0.0009  -0.0208 246 GLU A C     
1781 O  O     . GLU A 266 ? 0.2693 0.3117 0.3166 0.0311  0.0035  -0.0251 246 GLU A O     
1782 C  CB    . GLU A 266 ? 0.2152 0.2371 0.2537 0.0312  0.0000  -0.0190 246 GLU A CB    
1783 C  CG    . GLU A 266 ? 0.2019 0.2186 0.2350 0.0281  0.0017  -0.0145 246 GLU A CG    
1784 C  CD    . GLU A 266 ? 0.2121 0.2274 0.2443 0.0300  0.0001  -0.0173 246 GLU A CD    
1785 O  OE1   . GLU A 266 ? 0.2410 0.2560 0.2760 0.0343  -0.0036 -0.0222 246 GLU A OE1   
1786 O  OE2   . GLU A 266 ? 0.2272 0.2411 0.2555 0.0273  0.0021  -0.0145 246 GLU A OE2   
1787 N  N     . ALA A 267 ? 0.2557 0.2824 0.3021 0.0330  -0.0026 -0.0205 247 ALA A N     
1788 C  CA    . ALA A 267 ? 0.2634 0.2984 0.3153 0.0346  -0.0030 -0.0243 247 ALA A CA    
1789 C  C     . ALA A 267 ? 0.2886 0.3284 0.3394 0.0298  0.0014  -0.0210 247 ALA A C     
1790 O  O     . ALA A 267 ? 0.3181 0.3694 0.3725 0.0288  0.0039  -0.0242 247 ALA A O     
1791 C  CB    . ALA A 267 ? 0.2897 0.3175 0.3436 0.0383  -0.0091 -0.0251 247 ALA A CB    
1792 N  N     . ALA A 268 ? 0.2541 0.2855 0.3000 0.0266  0.0022  -0.0148 248 ALA A N     
1793 C  CA    . ALA A 268 ? 0.2825 0.3163 0.3267 0.0222  0.0056  -0.0114 248 ALA A CA    
1794 C  C     . ALA A 268 ? 0.3324 0.3723 0.3744 0.0183  0.0100  -0.0107 248 ALA A C     
1795 O  O     . ALA A 268 ? 0.3077 0.3547 0.3503 0.0151  0.0126  -0.0108 248 ALA A O     
1796 C  CB    . ALA A 268 ? 0.3399 0.3631 0.3797 0.0204  0.0048  -0.0059 248 ALA A CB    
1797 N  N     . THR A 269 ? 0.2544 0.2912 0.2933 0.0181  0.0107  -0.0097 249 THR A N     
1798 C  CA    . THR A 269 ? 0.2786 0.3203 0.3146 0.0143  0.0143  -0.0088 249 THR A CA    
1799 C  C     . THR A 269 ? 0.2794 0.3255 0.3165 0.0167  0.0141  -0.0132 249 THR A C     
1800 O  O     . THR A 269 ? 0.2273 0.2670 0.2619 0.0177  0.0130  -0.0119 249 THR A O     
1801 C  CB    . THR A 269 ? 0.2551 0.2883 0.2856 0.0114  0.0151  -0.0030 249 THR A CB    
1802 O  OG1   . THR A 269 ? 0.2597 0.2850 0.2888 0.0139  0.0130  -0.0020 249 THR A OG1   
1803 C  CG2   . THR A 269 ? 0.2357 0.2644 0.2651 0.0096  0.0150  0.0005  249 THR A CG2   
1804 N  N     . PRO A 270 ? 0.2195 0.2772 0.2608 0.0176  0.0151  -0.0188 250 PRO A N     
1805 C  CA    . PRO A 270 ? 0.1826 0.2452 0.2259 0.0208  0.0145  -0.0243 250 PRO A CA    
1806 C  C     . PRO A 270 ? 0.2312 0.2932 0.2691 0.0176  0.0168  -0.0223 250 PRO A C     
1807 O  O     . PRO A 270 ? 0.2313 0.2963 0.2655 0.0122  0.0199  -0.0191 250 PRO A O     
1808 C  CB    . PRO A 270 ? 0.2551 0.3328 0.3039 0.0212  0.0161  -0.0306 250 PRO A CB    
1809 C  CG    . PRO A 270 ? 0.2865 0.3642 0.3376 0.0204  0.0155  -0.0290 250 PRO A CG    
1810 C  CD    . PRO A 270 ? 0.2854 0.3526 0.3307 0.0163  0.0163  -0.0211 250 PRO A CD    
1811 N  N     . PRO A 271 ? 0.2197 0.2774 0.2569 0.0207  0.0148  -0.0240 251 PRO A N     
1812 C  CA    . PRO A 271 ? 0.2635 0.3199 0.2955 0.0180  0.0165  -0.0221 251 PRO A CA    
1813 C  C     . PRO A 271 ? 0.2544 0.3237 0.2867 0.0165  0.0193  -0.0272 251 PRO A C     
1814 O  O     . PRO A 271 ? 0.2350 0.3060 0.2673 0.0188  0.0186  -0.0312 251 PRO A O     
1815 C  CB    . PRO A 271 ? 0.2887 0.3350 0.3203 0.0221  0.0127  -0.0221 251 PRO A CB    
1816 C  CG    . PRO A 271 ? 0.2676 0.3151 0.3050 0.0276  0.0092  -0.0275 251 PRO A CG    
1817 C  CD    . PRO A 271 ? 0.2420 0.2940 0.2826 0.0267  0.0102  -0.0272 251 PRO A CD    
1818 N  N     . VAL A 272 ? 0.2109 0.2899 0.2434 0.0123  0.0225  -0.0274 252 VAL A N     
1819 C  CA    . VAL A 272 ? 0.2357 0.3299 0.2690 0.0100  0.0257  -0.0328 252 VAL A CA    
1820 C  C     . VAL A 272 ? 0.2226 0.3190 0.2491 0.0018  0.0290  -0.0277 252 VAL A C     
1821 O  O     . VAL A 272 ? 0.2926 0.3854 0.3174 -0.0017 0.0294  -0.0227 252 VAL A O     
1822 C  CB    . VAL A 272 ? 0.2691 0.3748 0.3099 0.0124  0.0259  -0.0388 252 VAL A CB    
1823 C  CG1   . VAL A 272 ? 0.2564 0.3800 0.2978 0.0083  0.0301  -0.0438 252 VAL A CG1   
1824 C  CG2   . VAL A 272 ? 0.2162 0.3196 0.2633 0.0207  0.0218  -0.0447 252 VAL A CG2   
1825 N  N     . VAL A 273 ? 0.2298 0.3317 0.2521 -0.0012 0.0310  -0.0291 253 VAL A N     
1826 C  CA    . VAL A 273 ? 0.2874 0.3908 0.3020 -0.0095 0.0334  -0.0242 253 VAL A CA    
1827 C  C     . VAL A 273 ? 0.3271 0.4452 0.3428 -0.0147 0.0367  -0.0266 253 VAL A C     
1828 O  O     . VAL A 273 ? 0.3127 0.4455 0.3311 -0.0147 0.0390  -0.0336 253 VAL A O     
1829 C  CB    . VAL A 273 ? 0.3128 0.4172 0.3221 -0.0112 0.0341  -0.0250 253 VAL A CB    
1830 C  CG1   . VAL A 273 ? 0.3772 0.4832 0.3779 -0.0204 0.0361  -0.0199 253 VAL A CG1   
1831 C  CG2   . VAL A 273 ? 0.3493 0.4392 0.3576 -0.0067 0.0308  -0.0221 253 VAL A CG2   
1832 N  N     . ASN A 274 ? 0.3645 0.4790 0.3782 -0.0190 0.0367  -0.0213 254 ASN A N     
1833 C  CA    . ASN A 274 ? 0.5157 0.6431 0.5300 -0.0247 0.0394  -0.0227 254 ASN A CA    
1834 C  C     . ASN A 274 ? 0.5661 0.6881 0.5719 -0.0336 0.0397  -0.0149 254 ASN A C     
1835 O  O     . ASN A 274 ? 0.7027 0.8095 0.7042 -0.0336 0.0371  -0.0085 254 ASN A O     
1836 C  CB    . ASN A 274 ? 0.4448 0.5745 0.4675 -0.0200 0.0384  -0.0255 254 ASN A CB    
1837 C  CG    . ASN A 274 ? 0.4094 0.5540 0.4340 -0.0255 0.0412  -0.0278 254 ASN A CG    
1838 O  OD1   . ASN A 274 ? 0.4283 0.5870 0.4507 -0.0309 0.0444  -0.0308 254 ASN A OD1   
1839 N  ND2   . ASN A 274 ? 0.4030 0.5453 0.4314 -0.0245 0.0399  -0.0264 254 ASN A ND2   
1840 N  N     . GLY A 279 ? 0.6906 0.7711 0.6341 -0.0852 0.0300  0.0261  259 GLY A N     
1841 C  CA    . GLY A 279 ? 0.7891 0.8585 0.7398 -0.0761 0.0277  0.0264  259 GLY A CA    
1842 C  C     . GLY A 279 ? 0.8096 0.8721 0.7643 -0.0671 0.0267  0.0248  259 GLY A C     
1843 O  O     . GLY A 279 ? 0.7482 0.8184 0.7040 -0.0653 0.0290  0.0208  259 GLY A O     
1844 N  N     . SER A 280 ? 0.8671 0.9155 0.8241 -0.0615 0.0232  0.0277  260 SER A N     
1845 C  CA    . SER A 280 ? 1.0587 1.1004 1.0197 -0.0534 0.0220  0.0266  260 SER A CA    
1846 C  C     . SER A 280 ? 0.9066 0.9545 0.8778 -0.0454 0.0245  0.0208  260 SER A C     
1847 O  O     . SER A 280 ? 0.8785 0.9333 0.8541 -0.0452 0.0264  0.0183  260 SER A O     
1848 C  CB    . SER A 280 ? 1.0481 1.0733 1.0071 -0.0513 0.0172  0.0317  260 SER A CB    
1849 O  OG    . SER A 280 ? 1.1081 1.1292 1.0701 -0.0502 0.0162  0.0328  260 SER A OG    
1850 N  N     . LEU A 281 ? 0.7035 0.7481 0.6780 -0.0389 0.0240  0.0189  261 LEU A N     
1851 C  CA    . LEU A 281 ? 0.6615 0.7104 0.6446 -0.0316 0.0255  0.0137  261 LEU A CA    
1852 C  C     . LEU A 281 ? 0.5223 0.5609 0.5093 -0.0265 0.0232  0.0157  261 LEU A C     
1853 O  O     . LEU A 281 ? 0.6053 0.6343 0.5912 -0.0241 0.0208  0.0184  261 LEU A O     
1854 C  CB    . LEU A 281 ? 0.4825 0.5331 0.4665 -0.0279 0.0258  0.0105  261 LEU A CB    
1855 C  CG    . LEU A 281 ? 0.3624 0.4169 0.3544 -0.0206 0.0266  0.0049  261 LEU A CG    
1856 C  CD1   . LEU A 281 ? 0.4498 0.5168 0.4464 -0.0210 0.0291  0.0000  261 LEU A CD1   
1857 C  CD2   . LEU A 281 ? 0.4018 0.4576 0.3936 -0.0179 0.0265  0.0019  261 LEU A CD2   
1858 N  N     . PRO A 282 ? 0.4671 0.5082 0.4589 -0.0248 0.0239  0.0142  262 PRO A N     
1859 C  CA    . PRO A 282 ? 0.4473 0.4789 0.4418 -0.0209 0.0219  0.0163  262 PRO A CA    
1860 C  C     . PRO A 282 ? 0.4931 0.5218 0.4922 -0.0142 0.0212  0.0141  262 PRO A C     
1861 O  O     . PRO A 282 ? 0.3748 0.4097 0.3769 -0.0116 0.0224  0.0099  262 PRO A O     
1862 C  CB    . PRO A 282 ? 0.3788 0.4156 0.3767 -0.0217 0.0230  0.0148  262 PRO A CB    
1863 C  CG    . PRO A 282 ? 0.6048 0.6551 0.6054 -0.0224 0.0257  0.0097  262 PRO A CG    
1864 C  CD    . PRO A 282 ? 0.4949 0.5483 0.4899 -0.0265 0.0266  0.0102  262 PRO A CD    
1865 N  N     . PRO A 283 ? 0.4135 0.4327 0.4131 -0.0114 0.0192  0.0167  263 PRO A N     
1866 C  CA    . PRO A 283 ? 0.3607 0.3772 0.3645 -0.0059 0.0185  0.0149  263 PRO A CA    
1867 C  C     . PRO A 283 ? 0.3600 0.3800 0.3688 -0.0031 0.0190  0.0120  263 PRO A C     
1868 O  O     . PRO A 283 ? 0.3838 0.4069 0.3935 -0.0049 0.0197  0.0118  263 PRO A O     
1869 C  CB    . PRO A 283 ? 0.4270 0.4343 0.4298 -0.0048 0.0164  0.0184  263 PRO A CB    
1870 C  CG    . PRO A 283 ? 0.4868 0.4914 0.4867 -0.0085 0.0159  0.0212  263 PRO A CG    
1871 C  CD    . PRO A 283 ? 0.5191 0.5298 0.5153 -0.0134 0.0171  0.0211  263 PRO A CD    
1872 N  N     . LEU A 284 ? 0.3108 0.3300 0.3227 0.0011  0.0182  0.0097  264 LEU A N     
1873 C  CA    . LEU A 284 ? 0.2266 0.2472 0.2430 0.0043  0.0176  0.0070  264 LEU A CA    
1874 C  C     . LEU A 284 ? 0.2614 0.2747 0.2782 0.0055  0.0162  0.0097  264 LEU A C     
1875 O  O     . LEU A 284 ? 0.2726 0.2804 0.2871 0.0047  0.0158  0.0128  264 LEU A O     
1876 C  CB    . LEU A 284 ? 0.2268 0.2490 0.2455 0.0079  0.0165  0.0034  264 LEU A CB    
1877 C  CG    . LEU A 284 ? 0.2206 0.2516 0.2393 0.0070  0.0180  -0.0003 264 LEU A CG    
1878 C  CD1   . LEU A 284 ? 0.2605 0.2909 0.2806 0.0107  0.0164  -0.0037 264 LEU A CD1   
1879 C  CD2   . LEU A 284 ? 0.2266 0.2667 0.2485 0.0063  0.0194  -0.0036 264 LEU A CD2   
1880 N  N     . GLY A 285 ? 0.2651 0.2790 0.2849 0.0074  0.0154  0.0082  265 GLY A N     
1881 C  CA    . GLY A 285 ? 0.3058 0.3138 0.3256 0.0080  0.0144  0.0104  265 GLY A CA    
1882 C  C     . GLY A 285 ? 0.2105 0.2130 0.2300 0.0101  0.0127  0.0112  265 GLY A C     
1883 O  O     . GLY A 285 ? 0.3063 0.3085 0.3273 0.0123  0.0111  0.0091  265 GLY A O     
1884 N  N     . GLU A 286 ? 0.2403 0.2383 0.2578 0.0092  0.0128  0.0139  266 GLU A N     
1885 C  CA    . GLU A 286 ? 0.2479 0.2419 0.2651 0.0104  0.0115  0.0147  266 GLU A CA    
1886 C  C     . GLU A 286 ? 0.2440 0.2357 0.2616 0.0106  0.0106  0.0152  266 GLU A C     
1887 O  O     . GLU A 286 ? 0.2823 0.2736 0.2996 0.0097  0.0114  0.0160  266 GLU A O     
1888 C  CB    . GLU A 286 ? 0.2819 0.2737 0.2975 0.0095  0.0120  0.0168  266 GLU A CB    
1889 C  CG    . GLU A 286 ? 0.2228 0.2121 0.2383 0.0100  0.0110  0.0175  266 GLU A CG    
1890 C  CD    . GLU A 286 ? 0.2615 0.2502 0.2764 0.0096  0.0111  0.0187  266 GLU A CD    
1891 O  OE1   . GLU A 286 ? 0.3006 0.2897 0.3149 0.0092  0.0117  0.0193  266 GLU A OE1   
1892 O  OE2   . GLU A 286 ? 0.2490 0.2368 0.2637 0.0096  0.0102  0.0190  266 GLU A OE2   
1893 N  N     . LEU A 287 ? 0.2326 0.2220 0.2503 0.0116  0.0086  0.0147  267 LEU A N     
1894 C  CA    . LEU A 287 ? 0.2287 0.2152 0.2456 0.0111  0.0073  0.0155  267 LEU A CA    
1895 C  C     . LEU A 287 ? 0.2541 0.2394 0.2693 0.0096  0.0085  0.0175  267 LEU A C     
1896 O  O     . LEU A 287 ? 0.2424 0.2273 0.2570 0.0092  0.0085  0.0182  267 LEU A O     
1897 C  CB    . LEU A 287 ? 0.2468 0.2300 0.2632 0.0119  0.0040  0.0150  267 LEU A CB    
1898 C  CG    . LEU A 287 ? 0.3311 0.3154 0.3498 0.0144  0.0020  0.0121  267 LEU A CG    
1899 C  CD1   . LEU A 287 ? 0.3808 0.3596 0.3982 0.0150  -0.0024 0.0121  267 LEU A CD1   
1900 C  CD2   . LEU A 287 ? 0.3983 0.3866 0.4194 0.0149  0.0029  0.0107  267 LEU A CD2   
1901 N  N     . PRO A 288 ? 0.2621 0.2473 0.2768 0.0087  0.0093  0.0181  268 PRO A N     
1902 C  CA    . PRO A 288 ? 0.2988 0.2841 0.3125 0.0077  0.0105  0.0190  268 PRO A CA    
1903 C  C     . PRO A 288 ? 0.2353 0.2198 0.2475 0.0063  0.0096  0.0198  268 PRO A C     
1904 O  O     . PRO A 288 ? 0.2603 0.2465 0.2727 0.0058  0.0106  0.0200  268 PRO A O     
1905 C  CB    . PRO A 288 ? 0.2825 0.2675 0.2956 0.0071  0.0109  0.0188  268 PRO A CB    
1906 C  CG    . PRO A 288 ? 0.2810 0.2665 0.2955 0.0078  0.0107  0.0181  268 PRO A CG    
1907 C  CD    . PRO A 288 ? 0.3158 0.3015 0.3312 0.0088  0.0093  0.0174  268 PRO A CD    
1908 N  N     . THR A 289 ? 0.2500 0.2318 0.2606 0.0055  0.0072  0.0202  269 THR A N     
1909 C  CA    . THR A 289 ? 0.2751 0.2552 0.2829 0.0031  0.0057  0.0215  269 THR A CA    
1910 C  C     . THR A 289 ? 0.2494 0.2256 0.2565 0.0036  0.0025  0.0216  269 THR A C     
1911 O  O     . THR A 289 ? 0.2786 0.2532 0.2870 0.0057  0.0007  0.0204  269 THR A O     
1912 C  CB    . THR A 289 ? 0.4201 0.3992 0.4252 0.0007  0.0051  0.0223  269 THR A CB    
1913 O  OG1   . THR A 289 ? 0.4084 0.3912 0.4143 0.0007  0.0081  0.0215  269 THR A OG1   
1914 C  CG2   . THR A 289 ? 0.4088 0.3863 0.4100 -0.0030 0.0034  0.0241  269 THR A CG2   
1915 N  N     . SER A 290 ? 0.2796 0.2546 0.2850 0.0017  0.0013  0.0227  270 SER A N     
1916 C  CA    . SER A 290 ? 0.2640 0.2341 0.2681 0.0022  -0.0025 0.0228  270 SER A CA    
1917 C  C     . SER A 290 ? 0.2856 0.2503 0.2874 0.0017  -0.0065 0.0232  270 SER A C     
1918 O  O     . SER A 290 ? 0.3002 0.2640 0.2990 -0.0013 -0.0068 0.0249  270 SER A O     
1919 C  CB    . SER A 290 ? 0.2641 0.2332 0.2659 -0.0008 -0.0035 0.0244  270 SER A CB    
1920 O  OG    . SER A 290 ? 0.2812 0.2436 0.2805 -0.0011 -0.0082 0.0247  270 SER A OG    
1921 N  N     . PRO A 291 ? 0.2708 0.2319 0.2738 0.0046  -0.0099 0.0214  271 PRO A N     
1922 C  CA    . PRO A 291 ? 0.2866 0.2415 0.2875 0.0046  -0.0149 0.0217  271 PRO A CA    
1923 C  C     . PRO A 291 ? 0.3106 0.2581 0.3060 0.0008  -0.0195 0.0244  271 PRO A C     
1924 O  O     . PRO A 291 ? 0.3377 0.2789 0.3299 -0.0002 -0.0242 0.0254  271 PRO A O     
1925 C  CB    . PRO A 291 ? 0.3368 0.2913 0.3417 0.0096  -0.0171 0.0181  271 PRO A CB    
1926 C  CG    . PRO A 291 ? 0.2831 0.2402 0.2895 0.0106  -0.0151 0.0170  271 PRO A CG    
1927 C  CD    . PRO A 291 ? 0.3251 0.2877 0.3314 0.0082  -0.0097 0.0188  271 PRO A CD    
1928 N  N     . ASP A 292 ? 0.3028 0.2504 0.2965 -0.0015 -0.0188 0.0256  272 ASP A N     
1929 C  CA    . ASP A 292 ? 0.2929 0.2334 0.2809 -0.0058 -0.0235 0.0284  272 ASP A CA    
1930 C  C     . ASP A 292 ? 0.3445 0.2901 0.3306 -0.0105 -0.0198 0.0306  272 ASP A C     
1931 O  O     . ASP A 292 ? 0.2954 0.2445 0.2839 -0.0097 -0.0176 0.0298  272 ASP A O     
1932 C  CB    . ASP A 292 ? 0.2878 0.2219 0.2759 -0.0032 -0.0284 0.0269  272 ASP A CB    
1933 C  CG    . ASP A 292 ? 0.3682 0.2933 0.3497 -0.0081 -0.0342 0.0300  272 ASP A CG    
1934 O  OD1   . ASP A 292 ? 0.3360 0.2610 0.3126 -0.0143 -0.0339 0.0336  272 ASP A OD1   
1935 O  OD2   . ASP A 292 ? 0.3301 0.2481 0.3109 -0.0061 -0.0394 0.0288  272 ASP A OD2   
1936 N  N     . PRO A 293 ? 0.2991 0.2459 0.2812 -0.0157 -0.0191 0.0331  273 PRO A N     
1937 C  CA    . PRO A 293 ? 0.3498 0.3037 0.3310 -0.0201 -0.0152 0.0344  273 PRO A CA    
1938 C  C     . PRO A 293 ? 0.3635 0.3148 0.3420 -0.0235 -0.0177 0.0360  273 PRO A C     
1939 O  O     . PRO A 293 ? 0.3394 0.2979 0.3190 -0.0259 -0.0142 0.0363  273 PRO A O     
1940 C  CB    . PRO A 293 ? 0.3320 0.2874 0.3086 -0.0253 -0.0148 0.0364  273 PRO A CB    
1941 C  CG    . PRO A 293 ? 0.4267 0.3720 0.3993 -0.0253 -0.0207 0.0377  273 PRO A CG    
1942 C  CD    . PRO A 293 ? 0.3683 0.3112 0.3465 -0.0178 -0.0217 0.0346  273 PRO A CD    
1943 N  N     . LYS A 294 ? 0.2993 0.2404 0.2746 -0.0236 -0.0240 0.0370  274 LYS A N     
1944 C  CA    . LYS A 294 ? 0.2882 0.2256 0.2607 -0.0266 -0.0269 0.0384  274 LYS A CA    
1945 C  C     . LYS A 294 ? 0.3221 0.2613 0.2998 -0.0214 -0.0256 0.0356  274 LYS A C     
1946 O  O     . LYS A 294 ? 0.3064 0.2442 0.2826 -0.0238 -0.0271 0.0365  274 LYS A O     
1947 C  CB    . LYS A 294 ? 0.3114 0.2357 0.2775 -0.0291 -0.0353 0.0406  274 LYS A CB    
1948 C  CG    . LYS A 294 ? 0.4841 0.4052 0.4423 -0.0372 -0.0378 0.0448  274 LYS A CG    
1949 C  CD    . LYS A 294 ? 0.3679 0.2744 0.3187 -0.0406 -0.0472 0.0476  274 LYS A CD    
1950 C  CE    . LYS A 294 ? 0.4261 0.3306 0.3719 -0.0474 -0.0493 0.0505  274 LYS A CE    
1951 N  NZ    . LYS A 294 ? 0.4382 0.3277 0.3748 -0.0527 -0.0589 0.0543  274 LYS A NZ    
1952 N  N     . ALA A 295 ? 0.2682 0.2104 0.2514 -0.0149 -0.0230 0.0323  275 ALA A N     
1953 C  CA    . ALA A 295 ? 0.2780 0.2230 0.2655 -0.0108 -0.0212 0.0298  275 ALA A CA    
1954 C  C     . ALA A 295 ? 0.2981 0.2523 0.2879 -0.0127 -0.0160 0.0303  275 ALA A C     
1955 O  O     . ALA A 295 ? 0.2789 0.2394 0.2693 -0.0147 -0.0124 0.0311  275 ALA A O     
1956 C  CB    . ALA A 295 ? 0.2811 0.2283 0.2735 -0.0045 -0.0194 0.0263  275 ALA A CB    
1957 N  N     . GLY A 296 ? 0.2632 0.2183 0.2544 -0.0118 -0.0159 0.0295  276 GLY A N     
1958 C  CA    . GLY A 296 ? 0.2583 0.2220 0.2526 -0.0123 -0.0115 0.0294  276 GLY A CA    
1959 C  C     . GLY A 296 ? 0.2632 0.2267 0.2557 -0.0159 -0.0131 0.0307  276 GLY A C     
1960 O  O     . GLY A 296 ? 0.2554 0.2112 0.2445 -0.0170 -0.0178 0.0314  276 GLY A O     
1961 N  N     . LEU A 297 ? 0.2488 0.2210 0.2440 -0.0174 -0.0095 0.0309  277 LEU A N     
1962 C  CA    . LEU A 297 ? 0.2540 0.2285 0.2489 -0.0205 -0.0103 0.0318  277 LEU A CA    
1963 C  C     . LEU A 297 ? 0.2591 0.2354 0.2502 -0.0278 -0.0113 0.0345  277 LEU A C     
1964 O  O     . LEU A 297 ? 0.2618 0.2439 0.2532 -0.0300 -0.0087 0.0348  277 LEU A O     
1965 C  CB    . LEU A 297 ? 0.2449 0.2284 0.2453 -0.0180 -0.0062 0.0302  277 LEU A CB    
1966 C  CG    . LEU A 297 ? 0.2550 0.2439 0.2565 -0.0211 -0.0061 0.0308  277 LEU A CG    
1967 C  CD1   . LEU A 297 ? 0.2658 0.2481 0.2650 -0.0213 -0.0099 0.0312  277 LEU A CD1   
1968 C  CD2   . LEU A 297 ? 0.2853 0.2826 0.2927 -0.0176 -0.0025 0.0288  277 LEU A CD2   
1969 N  N     . TYR A 298 ? 0.2349 0.2064 0.2222 -0.0318 -0.0152 0.0363  278 TYR A N     
1970 C  CA    . TYR A 298 ? 0.2648 0.2375 0.2475 -0.0399 -0.0168 0.0392  278 TYR A CA    
1971 C  C     . TYR A 298 ? 0.3074 0.2851 0.2914 -0.0429 -0.0168 0.0396  278 TYR A C     
1972 O  O     . TYR A 298 ? 0.2706 0.2432 0.2550 -0.0402 -0.0191 0.0389  278 TYR A O     
1973 C  CB    . TYR A 298 ? 0.2701 0.2298 0.2453 -0.0432 -0.0231 0.0418  278 TYR A CB    
1974 C  CG    . TYR A 298 ? 0.2622 0.2176 0.2357 -0.0417 -0.0237 0.0419  278 TYR A CG    
1975 C  CD1   . TYR A 298 ? 0.2778 0.2283 0.2540 -0.0343 -0.0241 0.0393  278 TYR A CD1   
1976 C  CD2   . TYR A 298 ? 0.2767 0.2333 0.2454 -0.0480 -0.0239 0.0445  278 TYR A CD2   
1977 C  CE1   . TYR A 298 ? 0.2786 0.2257 0.2535 -0.0329 -0.0248 0.0393  278 TYR A CE1   
1978 C  CE2   . TYR A 298 ? 0.2800 0.2324 0.2468 -0.0468 -0.0248 0.0447  278 TYR A CE2   
1979 C  CZ    . TYR A 298 ? 0.3269 0.2743 0.2970 -0.0391 -0.0253 0.0421  278 TYR A CZ    
1980 O  OH    . TYR A 298 ? 0.3438 0.2875 0.3123 -0.0379 -0.0264 0.0422  278 TYR A OH    
1981 N  N     . ILE A 299 ? 0.2392 0.2274 0.2239 -0.0485 -0.0143 0.0404  279 ILE A N     
1982 C  CA    . ILE A 299 ? 0.2555 0.2510 0.2426 -0.0513 -0.0137 0.0403  279 ILE A CA    
1983 C  C     . ILE A 299 ? 0.2616 0.2590 0.2431 -0.0613 -0.0157 0.0435  279 ILE A C     
1984 O  O     . ILE A 299 ? 0.2965 0.2979 0.2753 -0.0660 -0.0144 0.0446  279 ILE A O     
1985 C  CB    . ILE A 299 ? 0.2234 0.2330 0.2189 -0.0475 -0.0082 0.0371  279 ILE A CB    
1986 C  CG1   . ILE A 299 ? 0.2487 0.2548 0.2484 -0.0385 -0.0069 0.0346  279 ILE A CG1   
1987 C  CG2   . ILE A 299 ? 0.2295 0.2471 0.2281 -0.0501 -0.0080 0.0368  279 ILE A CG2   
1988 C  CD1   . ILE A 299 ? 0.2569 0.2741 0.2641 -0.0340 -0.0025 0.0315  279 ILE A CD1   
1989 N  N     . LYS A 300 ? 0.2817 0.2761 0.2609 -0.0651 -0.0192 0.0451  280 LYS A N     
1990 C  CA    . LYS A 300 ? 0.2757 0.2718 0.2491 -0.0757 -0.0216 0.0485  280 LYS A CA    
1991 C  C     . LYS A 300 ? 0.4018 0.4128 0.3810 -0.0781 -0.0184 0.0471  280 LYS A C     
1992 O  O     . LYS A 300 ? 0.4399 0.4487 0.4203 -0.0773 -0.0206 0.0470  280 LYS A O     
1993 C  CB    . LYS A 300 ? 0.3862 0.3660 0.3517 -0.0789 -0.0291 0.0517  280 LYS A CB    
1994 C  CG    . LYS A 300 ? 0.4310 0.4110 0.3893 -0.0908 -0.0324 0.0558  280 LYS A CG    
1995 C  CD    . LYS A 300 ? 0.6180 0.5827 0.5697 -0.0935 -0.0401 0.0584  280 LYS A CD    
1996 C  CE    . LYS A 300 ? 0.6937 0.6404 0.6374 -0.0935 -0.0466 0.0606  280 LYS A CE    
1997 N  NZ    . LYS A 300 ? 0.9328 0.8649 0.8690 -0.0981 -0.0549 0.0634  280 LYS A NZ    
1998 N  N     . SER A 301 ? 0.3839 0.4103 0.3666 -0.0811 -0.0135 0.0457  281 SER A N     
1999 C  CA    . SER A 301 ? 0.4323 0.4747 0.4212 -0.0837 -0.0106 0.0438  281 SER A CA    
2000 C  C     . SER A 301 ? 0.6028 0.6449 0.5854 -0.0946 -0.0142 0.0476  281 SER A C     
2001 O  O     . SER A 301 ? 0.4740 0.5030 0.4471 -0.1002 -0.0192 0.0518  281 SER A O     
2002 C  CB    . SER A 301 ? 0.5540 0.6137 0.5485 -0.0838 -0.0046 0.0405  281 SER A CB    
2003 O  OG    . SER A 301 ? 0.5138 0.5778 0.5019 -0.0938 -0.0044 0.0430  281 SER A OG    
2004 N  N     . ARG A 302 ? 0.4897 0.5467 0.4774 -0.0981 -0.0121 0.0461  282 ARG A N     
2005 C  CA    . ARG A 302 ? 0.4838 0.5417 0.4656 -0.1093 -0.0154 0.0497  282 ARG A CA    
2006 C  C     . ARG A 302 ? 0.6167 0.6781 0.5908 -0.1202 -0.0153 0.0528  282 ARG A C     
2007 O  O     . ARG A 302 ? 0.5432 0.6029 0.5103 -0.1309 -0.0189 0.0568  282 ARG A O     
2008 C  CB    . ARG A 302 ? 0.6197 0.6943 0.6096 -0.1106 -0.0131 0.0471  282 ARG A CB    
2009 C  CG    . ARG A 302 ? 0.7473 0.8129 0.7392 -0.1053 -0.0167 0.0470  282 ARG A CG    
2010 C  CD    . ARG A 302 ? 0.9252 1.0053 0.9238 -0.1079 -0.0158 0.0453  282 ARG A CD    
2011 N  NE    . ARG A 302 ? 1.1371 1.2246 1.1308 -0.1209 -0.0170 0.0482  282 ARG A NE    
2012 C  CZ    . ARG A 302 ? 1.1278 1.2298 1.1264 -0.1256 -0.0163 0.0471  282 ARG A CZ    
2013 N  NH1   . ARG A 302 ? 0.8194 0.9294 0.8279 -0.1182 -0.0149 0.0432  282 ARG A NH1   
2014 N  NH2   . ARG A 302 ? 0.8913 0.9996 0.8844 -0.1385 -0.0176 0.0503  282 ARG A NH2   
2015 N  N     . THR A 303 ? 0.5720 0.6377 0.5466 -0.1184 -0.0116 0.0513  283 THR A N     
2016 C  CA    . THR A 303 ? 0.4935 0.5592 0.4589 -0.1287 -0.0123 0.0547  283 THR A CA    
2017 C  C     . THR A 303 ? 0.5622 0.6049 0.5155 -0.1327 -0.0201 0.0605  283 THR A C     
2018 O  O     . THR A 303 ? 0.5305 0.5706 0.4741 -0.1435 -0.0226 0.0648  283 THR A O     
2019 C  CB    . THR A 303 ? 0.5311 0.6041 0.4994 -0.1247 -0.0071 0.0517  283 THR A CB    
2020 O  OG1   . THR A 303 ? 0.6097 0.6667 0.5776 -0.1150 -0.0090 0.0515  283 THR A OG1   
2021 C  CG2   . THR A 303 ? 0.6442 0.7384 0.6249 -0.1192 -0.0003 0.0452  283 THR A CG2   
2022 N  N     . GLY A 304 ? 0.4940 0.5203 0.4477 -0.1243 -0.0241 0.0605  284 GLY A N     
2023 C  CA    . GLY A 304 ? 0.4107 0.4150 0.3543 -0.1264 -0.0321 0.0650  284 GLY A CA    
2024 C  C     . GLY A 304 ? 0.4330 0.4261 0.3727 -0.1223 -0.0334 0.0655  284 GLY A C     
2025 O  O     . GLY A 304 ? 0.5242 0.4984 0.4564 -0.1226 -0.0406 0.0685  284 GLY A O     
2026 N  N     . GLN A 305 ? 0.3450 0.3492 0.2897 -0.1187 -0.0272 0.0625  285 GLN A N     
2027 C  CA    . GLN A 305 ? 0.3507 0.3460 0.2926 -0.1145 -0.0279 0.0627  285 GLN A CA    
2028 C  C     . GLN A 305 ? 0.4175 0.4142 0.3692 -0.1012 -0.0240 0.0578  285 GLN A C     
2029 O  O     . GLN A 305 ? 0.4195 0.4287 0.3802 -0.0964 -0.0190 0.0540  285 GLN A O     
2030 C  CB    . GLN A 305 ? 0.4707 0.4759 0.4085 -0.1223 -0.0248 0.0638  285 GLN A CB    
2031 C  CG    . GLN A 305 ? 0.5148 0.5137 0.4404 -0.1362 -0.0305 0.0699  285 GLN A CG    
2032 C  CD    . GLN A 305 ? 0.5911 0.5986 0.5104 -0.1458 -0.0282 0.0717  285 GLN A CD    
2033 O  OE1   . GLN A 305 ? 0.6240 0.6515 0.5491 -0.1468 -0.0208 0.0682  285 GLN A OE1   
2034 N  NE2   . GLN A 305 ? 0.4784 0.4708 0.3855 -0.1530 -0.0350 0.0771  285 GLN A NE2   
2035 N  N     . THR A 306 ? 0.3356 0.3185 0.2850 -0.0954 -0.0271 0.0580  286 THR A N     
2036 C  CA    . THR A 306 ? 0.3498 0.3310 0.3067 -0.0835 -0.0247 0.0540  286 THR A CA    
2037 C  C     . THR A 306 ? 0.3543 0.3425 0.3143 -0.0800 -0.0197 0.0518  286 THR A C     
2038 O  O     . THR A 306 ? 0.3543 0.3387 0.3081 -0.0845 -0.0213 0.0540  286 THR A O     
2039 C  CB    . THR A 306 ? 0.3626 0.3253 0.3158 -0.0790 -0.0313 0.0548  286 THR A CB    
2040 O  OG1   . THR A 306 ? 0.4413 0.3974 0.3914 -0.0822 -0.0361 0.0565  286 THR A OG1   
2041 C  CG2   . THR A 306 ? 0.3415 0.3034 0.3021 -0.0675 -0.0287 0.0507  286 THR A CG2   
2042 N  N     . VAL A 307 ? 0.2709 0.2683 0.2401 -0.0722 -0.0143 0.0475  287 VAL A N     
2043 C  CA    . VAL A 307 ? 0.2858 0.2895 0.2586 -0.0679 -0.0097 0.0449  287 VAL A CA    
2044 C  C     . VAL A 307 ? 0.2659 0.2639 0.2440 -0.0575 -0.0091 0.0422  287 VAL A C     
2045 O  O     . VAL A 307 ? 0.2687 0.2640 0.2502 -0.0531 -0.0101 0.0412  287 VAL A O     
2046 C  CB    . VAL A 307 ? 0.2956 0.3179 0.2745 -0.0693 -0.0034 0.0419  287 VAL A CB    
2047 C  CG1   . VAL A 307 ? 0.3320 0.3616 0.3052 -0.0805 -0.0035 0.0443  287 VAL A CG1   
2048 C  CG2   . VAL A 307 ? 0.2771 0.3061 0.2638 -0.0647 -0.0016 0.0392  287 VAL A CG2   
2049 N  N     . GLN A 308 ? 0.2364 0.2332 0.2150 -0.0539 -0.0075 0.0411  288 GLN A N     
2050 C  CA    . GLN A 308 ? 0.2314 0.2250 0.2152 -0.0448 -0.0063 0.0384  288 GLN A CA    
2051 C  C     . GLN A 308 ? 0.3045 0.3104 0.2960 -0.0407 -0.0008 0.0349  288 GLN A C     
2052 O  O     . GLN A 308 ? 0.2972 0.3134 0.2899 -0.0436 0.0026  0.0338  288 GLN A O     
2053 C  CB    . GLN A 308 ? 0.2368 0.2236 0.2178 -0.0430 -0.0074 0.0388  288 GLN A CB    
2054 C  CG    . GLN A 308 ? 0.2693 0.2507 0.2543 -0.0346 -0.0074 0.0366  288 GLN A CG    
2055 C  CD    . GLN A 308 ? 0.3319 0.3082 0.3148 -0.0331 -0.0083 0.0367  288 GLN A CD    
2056 O  OE1   . GLN A 308 ? 0.3314 0.3114 0.3119 -0.0367 -0.0068 0.0374  288 GLN A OE1   
2057 N  NE2   . GLN A 308 ? 0.3392 0.3073 0.3227 -0.0280 -0.0109 0.0359  288 GLN A NE2   
2058 N  N     . VAL A 309 ? 0.2508 0.2555 0.2473 -0.0340 -0.0001 0.0329  289 VAL A N     
2059 C  CA    . VAL A 309 ? 0.2268 0.2413 0.2303 -0.0298 0.0039  0.0297  289 VAL A CA    
2060 C  C     . VAL A 309 ? 0.2692 0.2788 0.2754 -0.0227 0.0045  0.0282  289 VAL A C     
2061 O  O     . VAL A 309 ? 0.2839 0.2855 0.2890 -0.0200 0.0022  0.0287  289 VAL A O     
2062 C  CB    . VAL A 309 ? 0.2410 0.2609 0.2481 -0.0300 0.0039  0.0291  289 VAL A CB    
2063 C  CG1   . VAL A 309 ? 0.2949 0.3230 0.3093 -0.0246 0.0070  0.0256  289 VAL A CG1   
2064 C  CG2   . VAL A 309 ? 0.2771 0.3035 0.2818 -0.0377 0.0037  0.0305  289 VAL A CG2   
2065 N  N     . LYS A 310 ? 0.2507 0.2656 0.2603 -0.0198 0.0076  0.0259  290 LYS A N     
2066 C  CA    . LYS A 310 ? 0.2628 0.2734 0.2742 -0.0141 0.0082  0.0248  290 LYS A CA    
2067 C  C     . LYS A 310 ? 0.2944 0.3094 0.3113 -0.0096 0.0097  0.0225  290 LYS A C     
2068 O  O     . LYS A 310 ? 0.3247 0.3480 0.3451 -0.0100 0.0110  0.0209  290 LYS A O     
2069 C  CB    . LYS A 310 ? 0.3236 0.3347 0.3338 -0.0143 0.0097  0.0242  290 LYS A CB    
2070 C  CG    . LYS A 310 ? 0.3382 0.3428 0.3423 -0.0182 0.0073  0.0267  290 LYS A CG    
2071 C  CD    . LYS A 310 ? 0.5215 0.5268 0.5242 -0.0186 0.0086  0.0262  290 LYS A CD    
2072 C  CE    . LYS A 310 ? 0.5145 0.5127 0.5107 -0.0228 0.0055  0.0289  290 LYS A CE    
2073 N  NZ    . LYS A 310 ? 0.5111 0.4993 0.5061 -0.0198 0.0020  0.0298  290 LYS A NZ    
2074 N  N     . ILE A 311 ? 0.2551 0.2645 0.2725 -0.0055 0.0090  0.0224  291 ILE A N     
2075 C  CA    . ILE A 311 ? 0.2421 0.2533 0.2635 -0.0014 0.0096  0.0208  291 ILE A CA    
2076 C  C     . ILE A 311 ? 0.2290 0.2387 0.2510 0.0014  0.0109  0.0198  291 ILE A C     
2077 O  O     . ILE A 311 ? 0.2346 0.2385 0.2541 0.0021  0.0104  0.0206  291 ILE A O     
2078 C  CB    . ILE A 311 ? 0.2531 0.2592 0.2736 0.0002  0.0078  0.0217  291 ILE A CB    
2079 C  CG1   . ILE A 311 ? 0.3391 0.3457 0.3584 -0.0028 0.0062  0.0228  291 ILE A CG1   
2080 C  CG2   . ILE A 311 ? 0.2537 0.2611 0.2773 0.0037  0.0079  0.0206  291 ILE A CG2   
2081 C  CD1   . ILE A 311 ? 0.3732 0.3746 0.3910 -0.0015 0.0043  0.0234  291 ILE A CD1   
2082 N  N     . PRO A 312 ? 0.2277 0.2424 0.2531 0.0033  0.0121  0.0176  292 PRO A N     
2083 C  CA    . PRO A 312 ? 0.2426 0.2548 0.2683 0.0059  0.0127  0.0166  292 PRO A CA    
2084 C  C     . PRO A 312 ? 0.2509 0.2568 0.2757 0.0083  0.0114  0.0177  292 PRO A C     
2085 O  O     . PRO A 312 ? 0.2442 0.2494 0.2697 0.0091  0.0102  0.0182  292 PRO A O     
2086 C  CB    . PRO A 312 ? 0.2576 0.2763 0.2878 0.0080  0.0134  0.0135  292 PRO A CB    
2087 C  CG    . PRO A 312 ? 0.3348 0.3615 0.3666 0.0052  0.0142  0.0127  292 PRO A CG    
2088 C  CD    . PRO A 312 ? 0.2967 0.3200 0.3262 0.0031  0.0128  0.0155  292 PRO A CD    
2089 N  N     . ARG A 313 ? 0.2340 0.2358 0.2569 0.0089  0.0118  0.0180  293 ARG A N     
2090 C  CA    . ARG A 313 ? 0.2457 0.2427 0.2672 0.0100  0.0109  0.0191  293 ARG A CA    
2091 C  C     . ARG A 313 ? 0.2403 0.2365 0.2632 0.0120  0.0097  0.0188  293 ARG A C     
2092 O  O     . ARG A 313 ? 0.2513 0.2445 0.2725 0.0120  0.0087  0.0200  293 ARG A O     
2093 C  CB    . ARG A 313 ? 0.2826 0.2768 0.3025 0.0100  0.0116  0.0192  293 ARG A CB    
2094 C  CG    . ARG A 313 ? 0.2822 0.2729 0.3003 0.0103  0.0111  0.0200  293 ARG A CG    
2095 C  CD    . ARG A 313 ? 0.2793 0.2686 0.2963 0.0099  0.0118  0.0199  293 ARG A CD    
2096 N  NE    . ARG A 313 ? 0.3171 0.3066 0.3334 0.0089  0.0117  0.0200  293 ARG A NE    
2097 C  CZ    . ARG A 313 ? 0.3953 0.3839 0.4108 0.0084  0.0118  0.0198  293 ARG A CZ    
2098 N  NH1   . ARG A 313 ? 0.5266 0.5148 0.5423 0.0088  0.0123  0.0194  293 ARG A NH1   
2099 N  NH2   . ARG A 313 ? 0.3840 0.3716 0.3984 0.0074  0.0107  0.0201  293 ARG A NH2   
2100 N  N     . ASP A 314 ? 0.2374 0.2361 0.2632 0.0137  0.0094  0.0171  294 ASP A N     
2101 C  CA    . ASP A 314 ? 0.2359 0.2327 0.2630 0.0160  0.0071  0.0167  294 ASP A CA    
2102 C  C     . ASP A 314 ? 0.2281 0.2283 0.2578 0.0167  0.0058  0.0162  294 ASP A C     
2103 O  O     . ASP A 314 ? 0.3199 0.3189 0.3514 0.0189  0.0033  0.0155  294 ASP A O     
2104 C  CB    . ASP A 314 ? 0.2777 0.2745 0.3069 0.0184  0.0065  0.0144  294 ASP A CB    
2105 C  CG    . ASP A 314 ? 0.2583 0.2626 0.2913 0.0191  0.0079  0.0113  294 ASP A CG    
2106 O  OD1   . ASP A 314 ? 0.2821 0.2912 0.3152 0.0168  0.0098  0.0115  294 ASP A OD1   
2107 O  OD2   . ASP A 314 ? 0.3250 0.3303 0.3608 0.0219  0.0069  0.0085  294 ASP A OD2   
2108 N  N     . CYS A 315 ? 0.2312 0.2350 0.2610 0.0147  0.0069  0.0167  295 CYS A N     
2109 C  CA    . CYS A 315 ? 0.2418 0.2499 0.2744 0.0148  0.0058  0.0161  295 CYS A CA    
2110 C  C     . CYS A 315 ? 0.2429 0.2482 0.2727 0.0130  0.0050  0.0183  295 CYS A C     
2111 O  O     . CYS A 315 ? 0.2409 0.2423 0.2670 0.0116  0.0057  0.0198  295 CYS A O     
2112 C  CB    . CYS A 315 ? 0.2693 0.2853 0.3046 0.0133  0.0075  0.0143  295 CYS A CB    
2113 S  SG    . CYS A 315 ? 0.2754 0.2973 0.3151 0.0158  0.0084  0.0104  295 CYS A SG    
2114 N  N     . ILE A 316 ? 0.2021 0.2100 0.2340 0.0133  0.0034  0.0181  296 ILE A N     
2115 C  CA    . ILE A 316 ? 0.1917 0.1981 0.2212 0.0115  0.0026  0.0198  296 ILE A CA    
2116 C  C     . ILE A 316 ? 0.2323 0.2452 0.2645 0.0096  0.0029  0.0190  296 ILE A C     
2117 O  O     . ILE A 316 ? 0.2575 0.2766 0.2943 0.0108  0.0025  0.0171  296 ILE A O     
2118 C  CB    . ILE A 316 ? 0.2196 0.2227 0.2484 0.0128  -0.0002 0.0206  296 ILE A CB    
2119 C  CG1   . ILE A 316 ? 0.2350 0.2320 0.2606 0.0137  -0.0007 0.0216  296 ILE A CG1   
2120 C  CG2   . ILE A 316 ? 0.2509 0.2527 0.2769 0.0108  -0.0010 0.0220  296 ILE A CG2   
2121 C  CD1   . ILE A 316 ? 0.2992 0.2927 0.3238 0.0148  -0.0041 0.0225  296 ILE A CD1   
2122 N  N     . ALA A 317 ? 0.2059 0.2176 0.2352 0.0066  0.0032  0.0203  297 ALA A N     
2123 C  CA    . ALA A 317 ? 0.2074 0.2249 0.2384 0.0039  0.0031  0.0201  297 ALA A CA    
2124 C  C     . ALA A 317 ? 0.2090 0.2249 0.2389 0.0030  0.0009  0.0212  297 ALA A C     
2125 O  O     . ALA A 317 ? 0.2210 0.2307 0.2476 0.0038  -0.0001 0.0222  297 ALA A O     
2126 C  CB    . ALA A 317 ? 0.2723 0.2894 0.3004 0.0003  0.0043  0.0210  297 ALA A CB    
2127 N  N     . PHE A 318 ? 0.2001 0.2224 0.2329 0.0011  0.0003  0.0207  298 PHE A N     
2128 C  CA    . PHE A 318 ? 0.2187 0.2402 0.2508 -0.0001 -0.0020 0.0216  298 PHE A CA    
2129 C  C     . PHE A 318 ? 0.2296 0.2545 0.2609 -0.0048 -0.0021 0.0223  298 PHE A C     
2130 O  O     . PHE A 318 ? 0.2109 0.2444 0.2458 -0.0067 -0.0009 0.0212  298 PHE A O     
2131 C  CB    . PHE A 318 ? 0.1835 0.2094 0.2204 0.0027  -0.0036 0.0203  298 PHE A CB    
2132 C  CG    . PHE A 318 ? 0.1962 0.2167 0.2323 0.0065  -0.0046 0.0203  298 PHE A CG    
2133 C  CD1   . PHE A 318 ? 0.2032 0.2171 0.2351 0.0067  -0.0064 0.0220  298 PHE A CD1   
2134 C  CD2   . PHE A 318 ? 0.1906 0.2121 0.2292 0.0093  -0.0038 0.0188  298 PHE A CD2   
2135 C  CE1   . PHE A 318 ? 0.2217 0.2303 0.2516 0.0091  -0.0074 0.0225  298 PHE A CE1   
2136 C  CE2   . PHE A 318 ? 0.2224 0.2377 0.2592 0.0121  -0.0052 0.0194  298 PHE A CE2   
2137 C  CZ    . PHE A 318 ? 0.2365 0.2455 0.2688 0.0116  -0.0070 0.0214  298 PHE A CZ    
2138 N  N     . GLN A 319 ? 0.1960 0.2145 0.2225 -0.0071 -0.0037 0.0240  299 GLN A N     
2139 C  CA    . GLN A 319 ? 0.1916 0.2115 0.2164 -0.0121 -0.0049 0.0251  299 GLN A CA    
2140 C  C     . GLN A 319 ? 0.1934 0.2147 0.2191 -0.0129 -0.0072 0.0254  299 GLN A C     
2141 O  O     . GLN A 319 ? 0.2246 0.2411 0.2489 -0.0103 -0.0086 0.0254  299 GLN A O     
2142 C  CB    . GLN A 319 ? 0.2217 0.2324 0.2403 -0.0141 -0.0061 0.0267  299 GLN A CB    
2143 C  CG    . GLN A 319 ? 0.2105 0.2207 0.2277 -0.0152 -0.0044 0.0269  299 GLN A CG    
2144 C  CD    . GLN A 319 ? 0.2465 0.2469 0.2579 -0.0165 -0.0065 0.0281  299 GLN A CD    
2145 O  OE1   . GLN A 319 ? 0.2717 0.2658 0.2814 -0.0130 -0.0071 0.0275  299 GLN A OE1   
2146 N  NE2   . GLN A 319 ? 0.2362 0.2356 0.2445 -0.0217 -0.0080 0.0298  299 GLN A NE2   
2147 N  N     . THR A 320 ? 0.2135 0.2419 0.2412 -0.0171 -0.0077 0.0255  300 THR A N     
2148 C  CA    . THR A 320 ? 0.2180 0.2478 0.2463 -0.0186 -0.0102 0.0259  300 THR A CA    
2149 C  C     . THR A 320 ? 0.2326 0.2525 0.2542 -0.0213 -0.0129 0.0278  300 THR A C     
2150 O  O     . THR A 320 ? 0.2560 0.2709 0.2733 -0.0242 -0.0132 0.0290  300 THR A O     
2151 C  CB    . THR A 320 ? 0.2588 0.3003 0.2915 -0.0228 -0.0098 0.0254  300 THR A CB    
2152 O  OG1   . THR A 320 ? 0.2984 0.3411 0.3284 -0.0277 -0.0085 0.0264  300 THR A OG1   
2153 C  CG2   . THR A 320 ? 0.2430 0.2949 0.2836 -0.0189 -0.0082 0.0225  300 THR A CG2   
2154 N  N     . GLY A 321 ? 0.2184 0.2355 0.2391 -0.0205 -0.0153 0.0279  301 GLY A N     
2155 C  CA    . GLY A 321 ? 0.2248 0.2331 0.2396 -0.0227 -0.0183 0.0289  301 GLY A CA    
2156 C  C     . GLY A 321 ? 0.2468 0.2583 0.2621 -0.0267 -0.0209 0.0297  301 GLY A C     
2157 O  O     . GLY A 321 ? 0.2459 0.2675 0.2668 -0.0274 -0.0204 0.0291  301 GLY A O     
2158 N  N     . GLU A 322 ? 0.2197 0.2227 0.2293 -0.0291 -0.0242 0.0305  302 GLU A N     
2159 C  CA    . GLU A 322 ? 0.2244 0.2293 0.2334 -0.0340 -0.0271 0.0316  302 GLU A CA    
2160 C  C     . GLU A 322 ? 0.2535 0.2635 0.2662 -0.0319 -0.0279 0.0307  302 GLU A C     
2161 O  O     . GLU A 322 ? 0.2396 0.2565 0.2551 -0.0356 -0.0292 0.0312  302 GLU A O     
2162 C  CB    . GLU A 322 ? 0.2619 0.2549 0.2636 -0.0363 -0.0311 0.0324  302 GLU A CB    
2163 C  CG    . GLU A 322 ? 0.3191 0.3058 0.3165 -0.0392 -0.0319 0.0336  302 GLU A CG    
2164 C  CD    . GLU A 322 ? 0.3760 0.3512 0.3664 -0.0425 -0.0372 0.0344  302 GLU A CD    
2165 O  OE1   . GLU A 322 ? 0.4756 0.4522 0.4647 -0.0486 -0.0398 0.0363  302 GLU A OE1   
2166 O  OE2   . GLU A 322 ? 0.4346 0.3997 0.4212 -0.0388 -0.0389 0.0329  302 GLU A OE2   
2167 N  N     . ALA A 323 ? 0.2249 0.2316 0.2373 -0.0266 -0.0274 0.0295  303 ALA A N     
2168 C  CA    . ALA A 323 ? 0.2654 0.2762 0.2807 -0.0250 -0.0288 0.0290  303 ALA A CA    
2169 C  C     . ALA A 323 ? 0.2485 0.2714 0.2720 -0.0241 -0.0272 0.0283  303 ALA A C     
2170 O  O     . ALA A 323 ? 0.2261 0.2554 0.2534 -0.0252 -0.0291 0.0281  303 ALA A O     
2171 C  CB    . ALA A 323 ? 0.2396 0.2440 0.2518 -0.0203 -0.0288 0.0282  303 ALA A CB    
2172 N  N     . LEU A 324 ? 0.2274 0.2538 0.2540 -0.0219 -0.0241 0.0276  304 LEU A N     
2173 C  CA    . LEU A 324 ? 0.2497 0.2881 0.2844 -0.0207 -0.0228 0.0261  304 LEU A CA    
2174 C  C     . LEU A 324 ? 0.2378 0.2857 0.2756 -0.0264 -0.0226 0.0261  304 LEU A C     
2175 O  O     . LEU A 324 ? 0.2341 0.2931 0.2787 -0.0266 -0.0232 0.0246  304 LEU A O     
2176 C  CB    . LEU A 324 ? 0.2562 0.2953 0.2928 -0.0171 -0.0196 0.0250  304 LEU A CB    
2177 C  CG    . LEU A 324 ? 0.2589 0.3099 0.3041 -0.0147 -0.0183 0.0225  304 LEU A CG    
2178 C  CD1   . LEU A 324 ? 0.3180 0.3654 0.3640 -0.0090 -0.0172 0.0216  304 LEU A CD1   
2179 C  CD2   . LEU A 324 ? 0.3125 0.3729 0.3605 -0.0189 -0.0158 0.0218  304 LEU A CD2   
2180 N  N     . GLU A 325 ? 0.2339 0.2780 0.2667 -0.0314 -0.0222 0.0278  305 GLU A N     
2181 C  CA    . GLU A 325 ? 0.2591 0.3114 0.2931 -0.0384 -0.0226 0.0285  305 GLU A CA    
2182 C  C     . GLU A 325 ? 0.2902 0.3451 0.3254 -0.0408 -0.0259 0.0288  305 GLU A C     
2183 O  O     . GLU A 325 ? 0.2480 0.3159 0.2892 -0.0436 -0.0258 0.0278  305 GLU A O     
2184 C  CB    . GLU A 325 ? 0.2614 0.3052 0.2877 -0.0436 -0.0230 0.0310  305 GLU A CB    
2185 C  CG    . GLU A 325 ? 0.2632 0.3137 0.2888 -0.0523 -0.0240 0.0325  305 GLU A CG    
2186 C  CD    . GLU A 325 ? 0.3720 0.4123 0.3891 -0.0577 -0.0256 0.0354  305 GLU A CD    
2187 O  OE1   . GLU A 325 ? 0.3102 0.3439 0.3244 -0.0552 -0.0242 0.0355  305 GLU A OE1   
2188 O  OE2   . GLU A 325 ? 0.4151 0.4533 0.4281 -0.0647 -0.0288 0.0376  305 GLU A OE2   
2189 N  N     . ARG A 326 ? 0.2496 0.2933 0.2793 -0.0396 -0.0289 0.0299  306 ARG A N     
2190 C  CA    . ARG A 326 ? 0.2516 0.2972 0.2819 -0.0421 -0.0323 0.0303  306 ARG A CA    
2191 C  C     . ARG A 326 ? 0.2734 0.3289 0.3118 -0.0378 -0.0325 0.0282  306 ARG A C     
2192 O  O     . ARG A 326 ? 0.2494 0.3148 0.2927 -0.0407 -0.0340 0.0276  306 ARG A O     
2193 C  CB    . ARG A 326 ? 0.2649 0.2960 0.2871 -0.0413 -0.0354 0.0313  306 ARG A CB    
2194 C  CG    . ARG A 326 ? 0.4567 0.4870 0.4770 -0.0457 -0.0395 0.0323  306 ARG A CG    
2195 C  CD    . ARG A 326 ? 0.6156 0.6483 0.6340 -0.0539 -0.0405 0.0341  306 ARG A CD    
2196 N  NE    . ARG A 326 ? 0.7976 0.8262 0.8122 -0.0584 -0.0450 0.0353  306 ARG A NE    
2197 C  CZ    . ARG A 326 ? 0.7485 0.7640 0.7547 -0.0614 -0.0483 0.0367  306 ARG A CZ    
2198 N  NH1   . ARG A 326 ? 0.7670 0.7725 0.7679 -0.0604 -0.0478 0.0370  306 ARG A NH1   
2199 N  NH2   . ARG A 326 ? 0.6679 0.6800 0.6709 -0.0653 -0.0526 0.0375  306 ARG A NH2   
2200 N  N     . ILE A 327 ? 0.2321 0.2851 0.2721 -0.0311 -0.0314 0.0269  307 ILE A N     
2201 C  CA    . ILE A 327 ? 0.2413 0.3017 0.2885 -0.0266 -0.0326 0.0250  307 ILE A CA    
2202 C  C     . ILE A 327 ? 0.2216 0.2982 0.2784 -0.0272 -0.0310 0.0225  307 ILE A C     
2203 O  O     . ILE A 327 ? 0.2460 0.3318 0.3099 -0.0257 -0.0332 0.0206  307 ILE A O     
2204 C  CB    . ILE A 327 ? 0.2526 0.3056 0.2983 -0.0201 -0.0321 0.0246  307 ILE A CB    
2205 C  CG1   . ILE A 327 ? 0.2345 0.2748 0.2720 -0.0195 -0.0343 0.0263  307 ILE A CG1   
2206 C  CG2   . ILE A 327 ? 0.2318 0.2924 0.2855 -0.0150 -0.0333 0.0223  307 ILE A CG2   
2207 C  CD1   . ILE A 327 ? 0.2345 0.2665 0.2683 -0.0149 -0.0331 0.0264  307 ILE A CD1   
2208 N  N     . THR A 328 ? 0.2221 0.3032 0.2796 -0.0294 -0.0274 0.0220  308 THR A N     
2209 C  CA    . THR A 328 ? 0.2353 0.3332 0.3017 -0.0305 -0.0253 0.0190  308 THR A CA    
2210 C  C     . THR A 328 ? 0.2825 0.3890 0.3489 -0.0390 -0.0252 0.0199  308 THR A C     
2211 O  O     . THR A 328 ? 0.2736 0.3948 0.3460 -0.0416 -0.0226 0.0176  308 THR A O     
2212 C  CB    . THR A 328 ? 0.2334 0.3331 0.3009 -0.0281 -0.0213 0.0176  308 THR A CB    
2213 O  OG1   . THR A 328 ? 0.2469 0.3386 0.3063 -0.0329 -0.0195 0.0204  308 THR A OG1   
2214 C  CG2   . THR A 328 ? 0.2191 0.3108 0.2869 -0.0201 -0.0217 0.0167  308 THR A CG2   
2215 N  N     . GLY A 329 ? 0.2462 0.3442 0.3058 -0.0437 -0.0279 0.0231  309 GLY A N     
2216 C  CA    . GLY A 329 ? 0.2409 0.3455 0.2994 -0.0527 -0.0286 0.0245  309 GLY A CA    
2217 C  C     . GLY A 329 ? 0.2549 0.3629 0.3106 -0.0585 -0.0254 0.0254  309 GLY A C     
2218 O  O     . GLY A 329 ? 0.2902 0.4108 0.3485 -0.0657 -0.0246 0.0252  309 GLY A O     
2219 N  N     . GLY A 330 ? 0.2437 0.3410 0.2940 -0.0561 -0.0236 0.0265  310 GLY A N     
2220 C  CA    . GLY A 330 ? 0.2484 0.3470 0.2950 -0.0614 -0.0210 0.0277  310 GLY A CA    
2221 C  C     . GLY A 330 ? 0.2590 0.3728 0.3131 -0.0600 -0.0166 0.0242  310 GLY A C     
2222 O  O     . GLY A 330 ? 0.3190 0.4352 0.3699 -0.0649 -0.0142 0.0251  310 GLY A O     
2223 N  N     . LYS A 331 ? 0.2721 0.3961 0.3358 -0.0534 -0.0158 0.0201  311 LYS A N     
2224 C  CA    . LYS A 331 ? 0.2879 0.4265 0.3592 -0.0510 -0.0119 0.0159  311 LYS A CA    
2225 C  C     . LYS A 331 ? 0.3219 0.4512 0.3897 -0.0464 -0.0096 0.0160  311 LYS A C     
2226 O  O     . LYS A 331 ? 0.2780 0.4161 0.3479 -0.0476 -0.0061 0.0139  311 LYS A O     
2227 C  CB    . LYS A 331 ? 0.2605 0.4111 0.3431 -0.0445 -0.0128 0.0111  311 LYS A CB    
2228 C  CG    . LYS A 331 ? 0.3020 0.4668 0.3901 -0.0497 -0.0143 0.0099  311 LYS A CG    
2229 C  CD    . LYS A 331 ? 0.3207 0.5022 0.4220 -0.0434 -0.0144 0.0038  311 LYS A CD    
2230 C  CE    . LYS A 331 ? 0.3614 0.5570 0.4689 -0.0478 -0.0165 0.0024  311 LYS A CE    
2231 N  NZ    . LYS A 331 ? 0.4541 0.6609 0.5593 -0.0590 -0.0139 0.0035  311 LYS A NZ    
2232 N  N     . PHE A 332 ? 0.2094 0.3222 0.2721 -0.0414 -0.0115 0.0181  312 PHE A N     
2233 C  CA    . PHE A 332 ? 0.2476 0.3488 0.3044 -0.0391 -0.0099 0.0195  312 PHE A CA    
2234 C  C     . PHE A 332 ? 0.2516 0.3380 0.2982 -0.0437 -0.0121 0.0240  312 PHE A C     
2235 O  O     . PHE A 332 ? 0.2691 0.3505 0.3130 -0.0458 -0.0153 0.0257  312 PHE A O     
2236 C  CB    . PHE A 332 ? 0.2268 0.3211 0.2858 -0.0300 -0.0103 0.0180  312 PHE A CB    
2237 C  CG    . PHE A 332 ? 0.2479 0.3541 0.3161 -0.0246 -0.0086 0.0133  312 PHE A CG    
2238 C  CD1   . PHE A 332 ? 0.2333 0.3559 0.3074 -0.0276 -0.0059 0.0102  312 PHE A CD1   
2239 C  CD2   . PHE A 332 ? 0.2795 0.3801 0.3500 -0.0167 -0.0097 0.0119  312 PHE A CD2   
2240 C  CE1   . PHE A 332 ? 0.2530 0.3865 0.3359 -0.0220 -0.0046 0.0051  312 PHE A CE1   
2241 C  CE2   . PHE A 332 ? 0.2283 0.3382 0.3070 -0.0114 -0.0090 0.0074  312 PHE A CE2   
2242 C  CZ    . PHE A 332 ? 0.2248 0.3513 0.3100 -0.0136 -0.0064 0.0036  312 PHE A CZ    
2243 N  N     . LYS A 333 ? 0.2633 0.3425 0.3041 -0.0452 -0.0107 0.0256  313 LYS A N     
2244 C  CA    . LYS A 333 ? 0.2617 0.3278 0.2930 -0.0501 -0.0132 0.0294  313 LYS A CA    
2245 C  C     . LYS A 333 ? 0.2323 0.2843 0.2587 -0.0450 -0.0133 0.0302  313 LYS A C     
2246 O  O     . LYS A 333 ? 0.2913 0.3450 0.3200 -0.0411 -0.0104 0.0287  313 LYS A O     
2247 C  CB    . LYS A 333 ? 0.3623 0.4330 0.3899 -0.0589 -0.0124 0.0313  313 LYS A CB    
2248 C  CG    . LYS A 333 ? 0.4571 0.5390 0.4865 -0.0666 -0.0133 0.0318  313 LYS A CG    
2249 C  CD    . LYS A 333 ? 0.5577 0.6300 0.5830 -0.0684 -0.0180 0.0341  313 LYS A CD    
2250 C  CE    . LYS A 333 ? 0.6691 0.7465 0.6914 -0.0789 -0.0201 0.0365  313 LYS A CE    
2251 N  NZ    . LYS A 333 ? 0.7592 0.8192 0.7706 -0.0836 -0.0247 0.0407  313 LYS A NZ    
2252 N  N     . ALA A 334 ? 0.2282 0.2668 0.2482 -0.0454 -0.0167 0.0322  314 ALA A N     
2253 C  CA    . ALA A 334 ? 0.2420 0.2678 0.2565 -0.0425 -0.0172 0.0330  314 ALA A CA    
2254 C  C     . ALA A 334 ? 0.2741 0.2968 0.2832 -0.0487 -0.0178 0.0353  314 ALA A C     
2255 O  O     . ALA A 334 ? 0.3181 0.3407 0.3237 -0.0558 -0.0203 0.0374  314 ALA A O     
2256 C  CB    . ALA A 334 ? 0.2752 0.2888 0.2851 -0.0404 -0.0208 0.0335  314 ALA A CB    
2257 N  N     . VAL A 335 ? 0.2399 0.2603 0.2481 -0.0465 -0.0158 0.0350  315 VAL A N     
2258 C  CA    . VAL A 335 ? 0.2591 0.2779 0.2624 -0.0523 -0.0160 0.0371  315 VAL A CA    
2259 C  C     . VAL A 335 ? 0.2473 0.2505 0.2441 -0.0505 -0.0191 0.0383  315 VAL A C     
2260 O  O     . VAL A 335 ? 0.2878 0.2868 0.2861 -0.0435 -0.0180 0.0365  315 VAL A O     
2261 C  CB    . VAL A 335 ? 0.2340 0.2639 0.2416 -0.0518 -0.0113 0.0355  315 VAL A CB    
2262 C  CG1   . VAL A 335 ? 0.2642 0.2922 0.2657 -0.0585 -0.0118 0.0379  315 VAL A CG1   
2263 C  CG2   . VAL A 335 ? 0.2844 0.3306 0.2993 -0.0531 -0.0086 0.0333  315 VAL A CG2   
2264 N  N     . PRO A 336 ? 0.2784 0.2730 0.2680 -0.0565 -0.0234 0.0412  316 PRO A N     
2265 C  CA    . PRO A 336 ? 0.2731 0.2524 0.2569 -0.0543 -0.0273 0.0419  316 PRO A CA    
2266 C  C     . PRO A 336 ? 0.2773 0.2558 0.2616 -0.0507 -0.0248 0.0411  316 PRO A C     
2267 O  O     . PRO A 336 ? 0.2729 0.2595 0.2582 -0.0538 -0.0218 0.0417  316 PRO A O     
2268 C  CB    . PRO A 336 ? 0.3054 0.2774 0.2814 -0.0630 -0.0326 0.0455  316 PRO A CB    
2269 C  CG    . PRO A 336 ? 0.3879 0.3696 0.3656 -0.0688 -0.0320 0.0465  316 PRO A CG    
2270 C  CD    . PRO A 336 ? 0.2737 0.2719 0.2599 -0.0660 -0.0254 0.0440  316 PRO A CD    
2271 N  N     . HIS A 337 ? 0.2627 0.2320 0.2463 -0.0445 -0.0263 0.0395  317 HIS A N     
2272 C  CA    . HIS A 337 ? 0.2600 0.2285 0.2446 -0.0405 -0.0240 0.0385  317 HIS A CA    
2273 C  C     . HIS A 337 ? 0.3005 0.2567 0.2824 -0.0356 -0.0276 0.0371  317 HIS A C     
2274 O  O     . HIS A 337 ? 0.2905 0.2399 0.2706 -0.0343 -0.0313 0.0363  317 HIS A O     
2275 C  CB    . HIS A 337 ? 0.2531 0.2323 0.2449 -0.0354 -0.0182 0.0360  317 HIS A CB    
2276 C  CG    . HIS A 337 ? 0.2392 0.2177 0.2340 -0.0298 -0.0178 0.0337  317 HIS A CG    
2277 N  ND1   . HIS A 337 ? 0.2463 0.2291 0.2431 -0.0308 -0.0181 0.0336  317 HIS A ND1   
2278 C  CD2   . HIS A 337 ? 0.2422 0.2166 0.2381 -0.0236 -0.0173 0.0316  317 HIS A CD2   
2279 C  CE1   . HIS A 337 ? 0.2509 0.2316 0.2493 -0.0255 -0.0178 0.0316  317 HIS A CE1   
2280 N  NE2   . HIS A 337 ? 0.2245 0.2005 0.2223 -0.0213 -0.0173 0.0303  317 HIS A NE2   
2281 N  N     . PHE A 338 ? 0.2768 0.2310 0.2589 -0.0327 -0.0267 0.0364  318 PHE A N     
2282 C  CA    . PHE A 338 ? 0.3062 0.2513 0.2875 -0.0270 -0.0294 0.0341  318 PHE A CA    
2283 C  C     . PHE A 338 ? 0.2982 0.2466 0.2825 -0.0230 -0.0258 0.0328  318 PHE A C     
2284 O  O     . PHE A 338 ? 0.2613 0.2166 0.2469 -0.0252 -0.0223 0.0340  318 PHE A O     
2285 C  CB    . PHE A 338 ? 0.2968 0.2288 0.2716 -0.0297 -0.0366 0.0355  318 PHE A CB    
2286 C  CG    . PHE A 338 ? 0.3462 0.2755 0.3169 -0.0344 -0.0382 0.0385  318 PHE A CG    
2287 C  CD1   . PHE A 338 ? 0.4245 0.3497 0.3952 -0.0308 -0.0390 0.0375  318 PHE A CD1   
2288 C  CD2   . PHE A 338 ? 0.3884 0.3194 0.3549 -0.0429 -0.0392 0.0423  318 PHE A CD2   
2289 C  CE1   . PHE A 338 ? 0.4418 0.3639 0.4081 -0.0355 -0.0409 0.0404  318 PHE A CE1   
2290 C  CE2   . PHE A 338 ? 0.4024 0.3310 0.3642 -0.0481 -0.0408 0.0453  318 PHE A CE2   
2291 C  CZ    . PHE A 338 ? 0.3611 0.2848 0.3226 -0.0443 -0.0417 0.0444  318 PHE A CZ    
2292 N  N     . VAL A 339 ? 0.2758 0.2201 0.2614 -0.0171 -0.0266 0.0299  319 VAL A N     
2293 C  CA    . VAL A 339 ? 0.2657 0.2125 0.2541 -0.0132 -0.0238 0.0284  319 VAL A CA    
2294 C  C     . VAL A 339 ? 0.3125 0.2496 0.2981 -0.0113 -0.0287 0.0274  319 VAL A C     
2295 O  O     . VAL A 339 ? 0.3252 0.2552 0.3093 -0.0093 -0.0332 0.0256  319 VAL A O     
2296 C  CB    . VAL A 339 ? 0.2707 0.2234 0.2639 -0.0078 -0.0197 0.0254  319 VAL A CB    
2297 C  CG1   . VAL A 339 ? 0.2851 0.2392 0.2806 -0.0040 -0.0176 0.0237  319 VAL A CG1   
2298 C  CG2   . VAL A 339 ? 0.2871 0.2487 0.2832 -0.0092 -0.0154 0.0263  319 VAL A CG2   
2299 N  N     . ARG A 340 ? 0.2653 0.2024 0.2505 -0.0120 -0.0282 0.0285  320 ARG A N     
2300 C  CA    . ARG A 340 ? 0.3171 0.2460 0.3005 -0.0098 -0.0328 0.0275  320 ARG A CA    
2301 C  C     . ARG A 340 ? 0.3003 0.2342 0.2886 -0.0043 -0.0292 0.0245  320 ARG A C     
2302 O  O     . ARG A 340 ? 0.3016 0.2431 0.2922 -0.0047 -0.0241 0.0252  320 ARG A O     
2303 C  CB    . ARG A 340 ? 0.4096 0.3349 0.3882 -0.0154 -0.0350 0.0313  320 ARG A CB    
2304 C  CG    . ARG A 340 ? 0.5656 0.4818 0.5375 -0.0212 -0.0413 0.0345  320 ARG A CG    
2305 C  CD    . ARG A 340 ? 0.3902 0.3057 0.3576 -0.0271 -0.0419 0.0382  320 ARG A CD    
2306 N  NE    . ARG A 340 ? 0.3919 0.3025 0.3590 -0.0242 -0.0443 0.0374  320 ARG A NE    
2307 C  CZ    . ARG A 340 ? 0.4328 0.3316 0.3940 -0.0265 -0.0517 0.0393  320 ARG A CZ    
2308 N  NH1   . ARG A 340 ? 0.4713 0.3614 0.4258 -0.0322 -0.0576 0.0424  320 ARG A NH1   
2309 N  NH2   . ARG A 340 ? 0.3795 0.2750 0.3411 -0.0235 -0.0537 0.0384  320 ARG A NH2   
2310 N  N     . GLY A 341 ? 0.2908 0.2204 0.2805 0.0008  -0.0323 0.0209  321 GLY A N     
2311 C  CA    . GLY A 341 ? 0.2946 0.2287 0.2885 0.0052  -0.0297 0.0182  321 GLY A CA    
2312 C  C     . GLY A 341 ? 0.3252 0.2553 0.3173 0.0040  -0.0322 0.0199  321 GLY A C     
2313 O  O     . GLY A 341 ? 0.3548 0.2782 0.3418 -0.0005 -0.0362 0.0232  321 GLY A O     
2314 N  N     . ALA A 342 ? 0.2825 0.2167 0.2784 0.0076  -0.0302 0.0175  322 ALA A N     
2315 C  CA    . ALA A 342 ? 0.2812 0.2119 0.2757 0.0070  -0.0326 0.0187  322 ALA A CA    
2316 C  C     . ALA A 342 ? 0.3668 0.2873 0.3597 0.0093  -0.0406 0.0170  322 ALA A C     
2317 O  O     . ALA A 342 ? 0.3485 0.2678 0.3440 0.0140  -0.0430 0.0127  322 ALA A O     
2318 C  CB    . ALA A 342 ? 0.3024 0.2409 0.3017 0.0100  -0.0280 0.0167  322 ALA A CB    
2319 N  N     . ARG A 343 ? 0.3153 0.2283 0.3035 0.0059  -0.0452 0.0201  323 ARG A N     
2320 C  CA    . ARG A 343 ? 0.3480 0.2499 0.3342 0.0081  -0.0540 0.0188  323 ARG A CA    
2321 C  C     . ARG A 343 ? 0.3529 0.2580 0.3452 0.0150  -0.0546 0.0138  323 ARG A C     
2322 O  O     . ARG A 343 ? 0.3522 0.2659 0.3482 0.0158  -0.0491 0.0133  323 ARG A O     
2323 C  CB    . ARG A 343 ? 0.3840 0.2771 0.3627 0.0020  -0.0588 0.0240  323 ARG A CB    
2324 C  CG    . ARG A 343 ? 0.4086 0.2964 0.3805 -0.0050 -0.0607 0.0285  323 ARG A CG    
2325 C  CD    . ARG A 343 ? 0.4633 0.3463 0.4276 -0.0127 -0.0631 0.0340  323 ARG A CD    
2326 N  NE    . ARG A 343 ? 0.4206 0.3146 0.3861 -0.0154 -0.0552 0.0356  323 ARG A NE    
2327 C  CZ    . ARG A 343 ? 0.4762 0.3694 0.4361 -0.0218 -0.0554 0.0397  323 ARG A CZ    
2328 N  NH1   . ARG A 343 ? 0.4664 0.3479 0.4183 -0.0268 -0.0632 0.0432  323 ARG A NH1   
2329 N  NH2   . ARG A 343 ? 0.3624 0.2665 0.3242 -0.0234 -0.0480 0.0401  323 ARG A NH2   
2330 N  N     . ALA A 344 ? 0.4326 0.3309 0.4264 0.0199  -0.0615 0.0097  324 ALA A N     
2331 C  CA    . ALA A 344 ? 0.4439 0.3469 0.4446 0.0270  -0.0622 0.0038  324 ALA A CA    
2332 C  C     . ALA A 344 ? 0.4144 0.3179 0.4156 0.0265  -0.0627 0.0052  324 ALA A C     
2333 O  O     . ALA A 344 ? 0.4060 0.3190 0.4133 0.0301  -0.0589 0.0019  324 ALA A O     
2334 C  CB    . ALA A 344 ? 0.4575 0.3518 0.4593 0.0324  -0.0710 -0.0010 324 ALA A CB    
2335 N  N     . GLU A 345 ? 0.4109 0.3045 0.4052 0.0215  -0.0676 0.0104  325 GLU A N     
2336 C  CA    . GLU A 345 ? 0.4473 0.3413 0.4412 0.0203  -0.0679 0.0122  325 GLU A CA    
2337 C  C     . GLU A 345 ? 0.4471 0.3542 0.4443 0.0190  -0.0581 0.0128  325 GLU A C     
2338 O  O     . GLU A 345 ? 0.4409 0.3527 0.4418 0.0212  -0.0569 0.0112  325 GLU A O     
2339 C  CB    . GLU A 345 ? 0.5866 0.4693 0.5709 0.0131  -0.0731 0.0186  325 GLU A CB    
2340 C  CG    . GLU A 345 ? 0.7030 0.5871 0.6855 0.0104  -0.0721 0.0214  325 GLU A CG    
2341 C  CD    . GLU A 345 ? 0.8436 0.7184 0.8158 0.0020  -0.0759 0.0280  325 GLU A CD    
2342 O  OE1   . GLU A 345 ? 0.9619 0.8271 0.9282 -0.0014 -0.0814 0.0304  325 GLU A OE1   
2343 O  OE2   . GLU A 345 ? 0.7432 0.6208 0.7128 -0.0017 -0.0734 0.0308  325 GLU A OE2   
2344 N  N     . MET A 346 ? 0.4014 0.3142 0.3976 0.0157  -0.0515 0.0149  326 MET A N     
2345 C  CA    . MET A 346 ? 0.3870 0.3109 0.3859 0.0145  -0.0430 0.0154  326 MET A CA    
2346 C  C     . MET A 346 ? 0.3389 0.2728 0.3449 0.0193  -0.0380 0.0108  326 MET A C     
2347 O  O     . MET A 346 ? 0.3759 0.3179 0.3851 0.0198  -0.0328 0.0101  326 MET A O     
2348 C  CB    . MET A 346 ? 0.3434 0.2686 0.3376 0.0083  -0.0389 0.0200  326 MET A CB    
2349 C  CG    . MET A 346 ? 0.6125 0.5343 0.6011 0.0029  -0.0399 0.0243  326 MET A CG    
2350 S  SD    . MET A 346 ? 0.9407 0.8481 0.9209 -0.0013 -0.0496 0.0279  326 MET A SD    
2351 C  CE    . MET A 346 ? 0.4767 0.3818 0.4543 -0.0040 -0.0498 0.0291  326 MET A CE    
2352 N  N     . SER A 347 ? 0.3598 0.2931 0.3677 0.0224  -0.0395 0.0076  327 SER A N     
2353 C  CA    . SER A 347 ? 0.3399 0.2831 0.3540 0.0267  -0.0353 0.0027  327 SER A CA    
2354 C  C     . SER A 347 ? 0.3604 0.3072 0.3798 0.0313  -0.0372 -0.0017 327 SER A C     
2355 O  O     . SER A 347 ? 0.3395 0.2966 0.3635 0.0326  -0.0321 -0.0040 327 SER A O     
2356 C  CB    . SER A 347 ? 0.3611 0.3030 0.3756 0.0290  -0.0369 -0.0002 327 SER A CB    
2357 O  OG    . SER A 347 ? 0.3838 0.3356 0.4041 0.0331  -0.0334 -0.0055 327 SER A OG    
2358 N  N     . ALA A 348 ? 0.3438 0.2822 0.3625 0.0335  -0.0449 -0.0027 328 ALA A N     
2359 C  CA    . ALA A 348 ? 0.4063 0.3474 0.4303 0.0378  -0.0478 -0.0067 328 ALA A CA    
2360 C  C     . ALA A 348 ? 0.4463 0.3985 0.4779 0.0433  -0.0454 -0.0138 328 ALA A C     
2361 O  O     . ALA A 348 ? 0.4160 0.3765 0.4530 0.0455  -0.0437 -0.0169 328 ALA A O     
2362 C  CB    . ALA A 348 ? 0.4292 0.3738 0.4528 0.0349  -0.0445 -0.0036 328 ALA A CB    
2363 N  N     . GLY A 349 ? 0.3890 0.3417 0.4210 0.0450  -0.0452 -0.0165 329 GLY A N     
2364 C  CA    . GLY A 349 ? 0.3940 0.3578 0.4324 0.0495  -0.0426 -0.0235 329 GLY A CA    
2365 C  C     . GLY A 349 ? 0.3474 0.3245 0.3881 0.0471  -0.0337 -0.0233 329 GLY A C     
2366 O  O     . GLY A 349 ? 0.3716 0.3595 0.4174 0.0500  -0.0311 -0.0290 329 GLY A O     
2367 N  N     . ARG A 350 ? 0.2952 0.2719 0.3321 0.0418  -0.0292 -0.0171 330 ARG A N     
2368 C  CA    . ARG A 350 ? 0.2712 0.2587 0.3096 0.0393  -0.0217 -0.0165 330 ARG A CA    
2369 C  C     . ARG A 350 ? 0.2534 0.2401 0.2871 0.0348  -0.0170 -0.0118 330 ARG A C     
2370 O  O     . ARG A 350 ? 0.2676 0.2626 0.3022 0.0333  -0.0117 -0.0122 330 ARG A O     
2371 C  CB    . ARG A 350 ? 0.3499 0.3397 0.3893 0.0376  -0.0204 -0.0144 330 ARG A CB    
2372 C  CG    . ARG A 350 ? 0.6015 0.5878 0.6437 0.0409  -0.0265 -0.0166 330 ARG A CG    
2373 C  CD    . ARG A 350 ? 0.4853 0.4757 0.5288 0.0390  -0.0243 -0.0150 330 ARG A CD    
2374 N  NE    . ARG A 350 ? 0.6030 0.5922 0.6418 0.0337  -0.0195 -0.0091 330 ARG A NE    
2375 C  CZ    . ARG A 350 ? 0.7111 0.6915 0.7445 0.0306  -0.0210 -0.0041 330 ARG A CZ    
2376 N  NH1   . ARG A 350 ? 0.6554 0.6264 0.6864 0.0315  -0.0273 -0.0032 330 ARG A NH1   
2377 N  NH2   . ARG A 350 ? 0.5750 0.5561 0.6052 0.0265  -0.0163 0.0000  330 ARG A NH2   
2378 N  N     . ILE A 351 ? 0.2603 0.2377 0.2890 0.0322  -0.0188 -0.0071 331 ILE A N     
2379 C  CA    . ILE A 351 ? 0.2131 0.1904 0.2380 0.0279  -0.0144 -0.0025 331 ILE A CA    
2380 C  C     . ILE A 351 ? 0.2284 0.2037 0.2515 0.0279  -0.0148 -0.0029 331 ILE A C     
2381 O  O     . ILE A 351 ? 0.2892 0.2567 0.3101 0.0286  -0.0196 -0.0029 331 ILE A O     
2382 C  CB    . ILE A 351 ? 0.2398 0.2108 0.2608 0.0243  -0.0151 0.0027  331 ILE A CB    
2383 C  CG1   . ILE A 351 ? 0.2781 0.2513 0.3008 0.0244  -0.0149 0.0027  331 ILE A CG1   
2384 C  CG2   . ILE A 351 ? 0.2799 0.2523 0.2982 0.0206  -0.0106 0.0064  331 ILE A CG2   
2385 C  CD1   . ILE A 351 ? 0.3172 0.2847 0.3359 0.0209  -0.0158 0.0072  331 ILE A CD1   
2386 N  N     . ALA A 352 ? 0.2118 0.1936 0.2351 0.0268  -0.0100 -0.0031 332 ALA A N     
2387 C  CA    . ALA A 352 ? 0.2221 0.2032 0.2434 0.0262  -0.0094 -0.0031 332 ALA A CA    
2388 C  C     . ALA A 352 ? 0.2433 0.2222 0.2612 0.0221  -0.0070 0.0021  332 ALA A C     
2389 O  O     . ALA A 352 ? 0.2211 0.2010 0.2388 0.0201  -0.0047 0.0050  332 ALA A O     
2390 C  CB    . ALA A 352 ? 0.2293 0.2195 0.2528 0.0272  -0.0060 -0.0067 332 ALA A CB    
2391 N  N     . ARG A 353 ? 0.2212 0.1975 0.2369 0.0212  -0.0076 0.0030  333 ARG A N     
2392 C  CA    . ARG A 353 ? 0.2225 0.1977 0.2357 0.0177  -0.0057 0.0073  333 ARG A CA    
2393 C  C     . ARG A 353 ? 0.2018 0.1801 0.2144 0.0173  -0.0037 0.0068  333 ARG A C     
2394 O  O     . ARG A 353 ? 0.2561 0.2329 0.2681 0.0187  -0.0058 0.0045  333 ARG A O     
2395 C  CB    . ARG A 353 ? 0.2187 0.1865 0.2290 0.0158  -0.0093 0.0099  333 ARG A CB    
2396 C  CG    . ARG A 353 ? 0.2270 0.1953 0.2355 0.0122  -0.0072 0.0137  333 ARG A CG    
2397 C  CD    . ARG A 353 ? 0.2516 0.2135 0.2568 0.0094  -0.0110 0.0160  333 ARG A CD    
2398 N  NE    . ARG A 353 ? 0.2993 0.2633 0.3034 0.0056  -0.0090 0.0192  333 ARG A NE    
2399 C  CZ    . ARG A 353 ? 0.3457 0.3110 0.3493 0.0042  -0.0085 0.0200  333 ARG A CZ    
2400 N  NH1   . ARG A 353 ? 0.3089 0.2731 0.3125 0.0060  -0.0097 0.0181  333 ARG A NH1   
2401 N  NH2   . ARG A 353 ? 0.3329 0.3010 0.3361 0.0009  -0.0069 0.0224  333 ARG A NH2   
2402 N  N     . ASN A 354 ? 0.1897 0.1718 0.2021 0.0155  -0.0001 0.0090  334 ASN A N     
2403 C  CA    . ASN A 354 ? 0.2208 0.2057 0.2322 0.0148  0.0016  0.0089  334 ASN A CA    
2404 C  C     . ASN A 354 ? 0.2203 0.2039 0.2306 0.0125  0.0022  0.0125  334 ASN A C     
2405 O  O     . ASN A 354 ? 0.1954 0.1791 0.2062 0.0114  0.0033  0.0147  334 ASN A O     
2406 C  CB    . ASN A 354 ? 0.2016 0.1924 0.2137 0.0146  0.0047  0.0079  334 ASN A CB    
2407 C  CG    . ASN A 354 ? 0.2009 0.1955 0.2149 0.0168  0.0045  0.0037  334 ASN A CG    
2408 O  OD1   . ASN A 354 ? 0.2359 0.2304 0.2502 0.0188  0.0026  0.0003  334 ASN A OD1   
2409 N  ND2   . ASN A 354 ? 0.2255 0.2234 0.2412 0.0166  0.0061  0.0035  334 ASN A ND2   
2410 N  N     . THR A 355 ? 0.2193 0.2021 0.2280 0.0119  0.0013  0.0126  335 THR A N     
2411 C  CA    . THR A 355 ? 0.2374 0.2202 0.2457 0.0100  0.0017  0.0154  335 THR A CA    
2412 C  C     . THR A 355 ? 0.2460 0.2303 0.2529 0.0097  0.0019  0.0151  335 THR A C     
2413 O  O     . THR A 355 ? 0.2093 0.1938 0.2149 0.0106  0.0013  0.0127  335 THR A O     
2414 C  CB    . THR A 355 ? 0.2719 0.2512 0.2797 0.0085  -0.0006 0.0168  335 THR A CB    
2415 O  OG1   . THR A 355 ? 0.2653 0.2411 0.2715 0.0092  -0.0035 0.0151  335 THR A OG1   
2416 C  CG2   . THR A 355 ? 0.3475 0.3257 0.3558 0.0077  -0.0007 0.0181  335 THR A CG2   
2417 N  N     . LEU A 356 ? 0.2253 0.2105 0.2324 0.0084  0.0024  0.0174  336 LEU A N     
2418 C  CA    . LEU A 356 ? 0.2143 0.2001 0.2199 0.0077  0.0019  0.0178  336 LEU A CA    
2419 C  C     . LEU A 356 ? 0.2128 0.1980 0.2193 0.0066  0.0004  0.0195  336 LEU A C     
2420 O  O     . LEU A 356 ? 0.2298 0.2163 0.2386 0.0061  0.0008  0.0209  336 LEU A O     
2421 C  CB    . LEU A 356 ? 0.2087 0.1964 0.2137 0.0072  0.0032  0.0190  336 LEU A CB    
2422 C  CG    . LEU A 356 ? 0.1977 0.1855 0.2006 0.0062  0.0021  0.0200  336 LEU A CG    
2423 C  CD1   . LEU A 356 ? 0.2315 0.2198 0.2312 0.0059  0.0020  0.0179  336 LEU A CD1   
2424 C  CD2   . LEU A 356 ? 0.2593 0.2472 0.2615 0.0055  0.0023  0.0220  336 LEU A CD2   
2425 N  N     . ALA A 357 ? 0.1929 0.1770 0.1977 0.0060  -0.0014 0.0190  337 ALA A N     
2426 C  CA    . ALA A 357 ? 0.1936 0.1780 0.1991 0.0045  -0.0029 0.0205  337 ALA A CA    
2427 C  C     . ALA A 357 ? 0.2153 0.2002 0.2191 0.0043  -0.0037 0.0206  337 ALA A C     
2428 O  O     . ALA A 357 ? 0.2104 0.1944 0.2113 0.0046  -0.0038 0.0191  337 ALA A O     
2429 C  CB    . ALA A 357 ? 0.2339 0.2152 0.2385 0.0033  -0.0051 0.0201  337 ALA A CB    
2430 N  N     . VAL A 358 ? 0.1950 0.1819 0.2005 0.0037  -0.0044 0.0222  338 VAL A N     
2431 C  CA    . VAL A 358 ? 0.1975 0.1845 0.2013 0.0032  -0.0058 0.0228  338 VAL A CA    
2432 C  C     . VAL A 358 ? 0.1985 0.1865 0.2038 0.0019  -0.0080 0.0234  338 VAL A C     
2433 O  O     . VAL A 358 ? 0.2028 0.1940 0.2120 0.0018  -0.0082 0.0243  338 VAL A O     
2434 C  CB    . VAL A 358 ? 0.1970 0.1850 0.2016 0.0039  -0.0057 0.0242  338 VAL A CB    
2435 C  CG1   . VAL A 358 ? 0.2302 0.2173 0.2321 0.0031  -0.0079 0.0250  338 VAL A CG1   
2436 C  CG2   . VAL A 358 ? 0.2037 0.1909 0.2067 0.0044  -0.0037 0.0238  338 VAL A CG2   
2437 N  N     . PHE A 359 ? 0.2020 0.1877 0.2043 0.0009  -0.0095 0.0226  339 PHE A N     
2438 C  CA    . PHE A 359 ? 0.2039 0.1900 0.2069 -0.0009 -0.0119 0.0232  339 PHE A CA    
2439 C  C     . PHE A 359 ? 0.2054 0.1931 0.2084 -0.0011 -0.0135 0.0241  339 PHE A C     
2440 O  O     . PHE A 359 ? 0.2160 0.2014 0.2150 -0.0016 -0.0148 0.0235  339 PHE A O     
2441 C  CB    . PHE A 359 ? 0.2236 0.2054 0.2231 -0.0018 -0.0135 0.0217  339 PHE A CB    
2442 C  CG    . PHE A 359 ? 0.2178 0.1968 0.2169 -0.0013 -0.0129 0.0206  339 PHE A CG    
2443 C  CD1   . PHE A 359 ? 0.2262 0.2054 0.2273 -0.0030 -0.0132 0.0219  339 PHE A CD1   
2444 C  CD2   . PHE A 359 ? 0.2518 0.2282 0.2485 0.0007  -0.0123 0.0182  339 PHE A CD2   
2445 C  CE1   . PHE A 359 ? 0.2170 0.1927 0.2171 -0.0027 -0.0134 0.0212  339 PHE A CE1   
2446 C  CE2   . PHE A 359 ? 0.2565 0.2300 0.2532 0.0016  -0.0125 0.0170  339 PHE A CE2   
2447 C  CZ    . PHE A 359 ? 0.2368 0.2093 0.2350 -0.0001 -0.0133 0.0188  339 PHE A CZ    
2448 N  N     . THR A 360 ? 0.2035 0.1951 0.2107 -0.0006 -0.0137 0.0252  340 THR A N     
2449 C  CA    . THR A 360 ? 0.2072 0.1999 0.2147 -0.0007 -0.0162 0.0261  340 THR A CA    
2450 C  C     . THR A 360 ? 0.2209 0.2150 0.2291 -0.0028 -0.0184 0.0261  340 THR A C     
2451 O  O     . THR A 360 ? 0.2401 0.2369 0.2511 -0.0043 -0.0180 0.0260  340 THR A O     
2452 C  CB    . THR A 360 ? 0.2056 0.2018 0.2180 0.0012  -0.0167 0.0266  340 THR A CB    
2453 O  OG1   . THR A 360 ? 0.2004 0.2026 0.2187 0.0009  -0.0164 0.0261  340 THR A OG1   
2454 C  CG2   . THR A 360 ? 0.2271 0.2215 0.2389 0.0030  -0.0148 0.0267  340 THR A CG2   
2455 N  N     . GLN A 361 ? 0.2124 0.2046 0.2174 -0.0036 -0.0207 0.0264  341 GLN A N     
2456 C  CA    . GLN A 361 ? 0.2628 0.2552 0.2672 -0.0059 -0.0231 0.0263  341 GLN A CA    
2457 C  C     . GLN A 361 ? 0.2313 0.2229 0.2335 -0.0061 -0.0259 0.0270  341 GLN A C     
2458 O  O     . GLN A 361 ? 0.2275 0.2172 0.2271 -0.0049 -0.0260 0.0275  341 GLN A O     
2459 C  CB    . GLN A 361 ? 0.2346 0.2222 0.2346 -0.0072 -0.0228 0.0251  341 GLN A CB    
2460 C  CG    . GLN A 361 ? 0.2353 0.2185 0.2299 -0.0058 -0.0217 0.0236  341 GLN A CG    
2461 C  CD    . GLN A 361 ? 0.2524 0.2318 0.2447 -0.0056 -0.0211 0.0216  341 GLN A CD    
2462 O  OE1   . GLN A 361 ? 0.2795 0.2580 0.2734 -0.0069 -0.0218 0.0219  341 GLN A OE1   
2463 N  NE2   . GLN A 361 ? 0.2395 0.2168 0.2279 -0.0042 -0.0200 0.0195  341 GLN A NE2   
2464 N  N     . PRO A 362 ? 0.2207 0.2137 0.2236 -0.0081 -0.0286 0.0272  342 PRO A N     
2465 C  CA    . PRO A 362 ? 0.2524 0.2450 0.2536 -0.0084 -0.0318 0.0280  342 PRO A CA    
2466 C  C     . PRO A 362 ? 0.2572 0.2441 0.2504 -0.0092 -0.0324 0.0274  342 PRO A C     
2467 O  O     . PRO A 362 ? 0.2586 0.2422 0.2479 -0.0096 -0.0308 0.0258  342 PRO A O     
2468 C  CB    . PRO A 362 ? 0.2535 0.2500 0.2581 -0.0107 -0.0343 0.0281  342 PRO A CB    
2469 C  CG    . PRO A 362 ? 0.2215 0.2218 0.2306 -0.0116 -0.0321 0.0278  342 PRO A CG    
2470 C  CD    . PRO A 362 ? 0.2394 0.2348 0.2448 -0.0107 -0.0291 0.0271  342 PRO A CD    
2471 N  N     . ASN A 363 ? 0.2586 0.2447 0.2492 -0.0094 -0.0350 0.0285  343 ASN A N     
2472 C  CA    . ASN A 363 ? 0.2802 0.2621 0.2631 -0.0111 -0.0361 0.0278  343 ASN A CA    
2473 C  C     . ASN A 363 ? 0.2616 0.2429 0.2438 -0.0130 -0.0379 0.0267  343 ASN A C     
2474 O  O     . ASN A 363 ? 0.2603 0.2448 0.2478 -0.0138 -0.0393 0.0273  343 ASN A O     
2475 C  CB    . ASN A 363 ? 0.2673 0.2482 0.2470 -0.0116 -0.0392 0.0296  343 ASN A CB    
2476 C  CG    . ASN A 363 ? 0.3088 0.2881 0.2860 -0.0108 -0.0377 0.0307  343 ASN A CG    
2477 O  OD1   . ASN A 363 ? 0.2981 0.2764 0.2722 -0.0107 -0.0343 0.0294  343 ASN A OD1   
2478 N  ND2   . ASN A 363 ? 0.3224 0.3014 0.3010 -0.0101 -0.0408 0.0330  343 ASN A ND2   
2479 N  N     . LEU A 364 ? 0.3069 0.2843 0.2825 -0.0140 -0.0379 0.0247  344 LEU A N     
2480 C  CA    . LEU A 364 ? 0.2789 0.2540 0.2532 -0.0156 -0.0397 0.0231  344 LEU A CA    
2481 C  C     . LEU A 364 ? 0.3716 0.3483 0.3474 -0.0178 -0.0437 0.0247  344 LEU A C     
2482 O  O     . LEU A 364 ? 0.2977 0.2742 0.2752 -0.0196 -0.0454 0.0246  344 LEU A O     
2483 C  CB    . LEU A 364 ? 0.2646 0.2355 0.2315 -0.0156 -0.0393 0.0199  344 LEU A CB    
2484 C  CG    . LEU A 364 ? 0.3070 0.2771 0.2733 -0.0134 -0.0356 0.0176  344 LEU A CG    
2485 C  CD1   . LEU A 364 ? 0.3244 0.2923 0.2838 -0.0130 -0.0351 0.0136  344 LEU A CD1   
2486 C  CD2   . LEU A 364 ? 0.3259 0.2944 0.2962 -0.0128 -0.0354 0.0171  344 LEU A CD2   
2487 N  N     . GLY A 365 ? 0.2977 0.2759 0.2728 -0.0178 -0.0456 0.0264  345 GLY A N     
2488 C  CA    . GLY A 365 ? 0.2889 0.2690 0.2658 -0.0196 -0.0498 0.0278  345 GLY A CA    
2489 C  C     . GLY A 365 ? 0.3512 0.3378 0.3373 -0.0189 -0.0507 0.0294  345 GLY A C     
2490 O  O     . GLY A 365 ? 0.3353 0.3250 0.3243 -0.0204 -0.0542 0.0301  345 GLY A O     
2491 N  N     . ASP A 366 ? 0.2872 0.2767 0.2783 -0.0167 -0.0477 0.0295  346 ASP A N     
2492 C  CA    . ASP A 366 ? 0.2793 0.2763 0.2796 -0.0158 -0.0482 0.0301  346 ASP A CA    
2493 C  C     . ASP A 366 ? 0.2798 0.2808 0.2840 -0.0185 -0.0479 0.0296  346 ASP A C     
2494 O  O     . ASP A 366 ? 0.2964 0.2939 0.2975 -0.0199 -0.0460 0.0289  346 ASP A O     
2495 C  CB    . ASP A 366 ? 0.2631 0.2617 0.2669 -0.0128 -0.0449 0.0301  346 ASP A CB    
2496 C  CG    . ASP A 366 ? 0.3686 0.3634 0.3691 -0.0106 -0.0456 0.0310  346 ASP A CG    
2497 O  OD1   . ASP A 366 ? 0.3941 0.3867 0.3913 -0.0111 -0.0492 0.0321  346 ASP A OD1   
2498 O  OD2   . ASP A 366 ? 0.3606 0.3545 0.3613 -0.0087 -0.0426 0.0309  346 ASP A OD2   
2499 N  N     . GLU A 367 ? 0.2761 0.2849 0.2872 -0.0193 -0.0501 0.0298  347 GLU A N     
2500 C  CA    . GLU A 367 ? 0.3046 0.3185 0.3193 -0.0230 -0.0498 0.0296  347 GLU A CA    
2501 C  C     . GLU A 367 ? 0.2863 0.3045 0.3054 -0.0226 -0.0458 0.0291  347 GLU A C     
2502 O  O     . GLU A 367 ? 0.3020 0.3241 0.3258 -0.0191 -0.0442 0.0286  347 GLU A O     
2503 C  CB    . GLU A 367 ? 0.2782 0.3011 0.2997 -0.0243 -0.0531 0.0296  347 GLU A CB    
2504 C  CG    . GLU A 367 ? 0.3140 0.3326 0.3308 -0.0257 -0.0575 0.0303  347 GLU A CG    
2505 C  CD    . GLU A 367 ? 0.4123 0.4402 0.4359 -0.0276 -0.0610 0.0302  347 GLU A CD    
2506 O  OE1   . GLU A 367 ? 0.4652 0.5039 0.4978 -0.0274 -0.0600 0.0292  347 GLU A OE1   
2507 O  OE2   . GLU A 367 ? 0.5477 0.5726 0.5677 -0.0293 -0.0648 0.0307  347 GLU A OE2   
2508 N  N     . VAL A 368 ? 0.2547 0.2713 0.2716 -0.0263 -0.0448 0.0294  348 VAL A N     
2509 C  CA    . VAL A 368 ? 0.2315 0.2529 0.2522 -0.0273 -0.0415 0.0292  348 VAL A CA    
2510 C  C     . VAL A 368 ? 0.3128 0.3432 0.3380 -0.0325 -0.0424 0.0296  348 VAL A C     
2511 O  O     . VAL A 368 ? 0.2800 0.3195 0.3111 -0.0331 -0.0400 0.0290  348 VAL A O     
2512 C  CB    . VAL A 368 ? 0.3181 0.3302 0.3323 -0.0277 -0.0396 0.0294  348 VAL A CB    
2513 C  CG1   . VAL A 368 ? 0.3262 0.3321 0.3370 -0.0227 -0.0380 0.0287  348 VAL A CG1   
2514 C  CG2   . VAL A 368 ? 0.3662 0.3707 0.3739 -0.0316 -0.0424 0.0299  348 VAL A CG2   
2515 N  N     . ASP A 369 ? 0.3332 0.3617 0.3556 -0.0366 -0.0457 0.0303  349 ASP A N     
2516 C  CA    . ASP A 369 ? 0.4170 0.4554 0.4440 -0.0420 -0.0470 0.0307  349 ASP A CA    
2517 C  C     . ASP A 369 ? 0.3785 0.4228 0.4100 -0.0406 -0.0501 0.0301  349 ASP A C     
2518 O  O     . ASP A 369 ? 0.3442 0.3813 0.3706 -0.0410 -0.0534 0.0306  349 ASP A O     
2519 C  CB    . ASP A 369 ? 0.4159 0.4472 0.4361 -0.0484 -0.0492 0.0324  349 ASP A CB    
2520 C  CG    . ASP A 369 ? 0.4022 0.4442 0.4265 -0.0554 -0.0503 0.0332  349 ASP A CG    
2521 O  OD1   . ASP A 369 ? 0.3964 0.4496 0.4278 -0.0554 -0.0512 0.0322  349 ASP A OD1   
2522 O  OD2   . ASP A 369 ? 0.5036 0.5430 0.5240 -0.0612 -0.0504 0.0348  349 ASP A OD2   
2523 N  N     . MET A 370 ? 0.3640 0.4212 0.4050 -0.0387 -0.0493 0.0285  350 MET A N     
2524 C  CA    . MET A 370 ? 0.4333 0.4957 0.4793 -0.0361 -0.0527 0.0276  350 MET A CA    
2525 C  C     . MET A 370 ? 0.4171 0.4879 0.4664 -0.0415 -0.0556 0.0276  350 MET A C     
2526 O  O     . MET A 370 ? 0.4521 0.5263 0.5049 -0.0398 -0.0593 0.0270  350 MET A O     
2527 C  CB    . MET A 370 ? 0.3905 0.4621 0.4455 -0.0304 -0.0514 0.0252  350 MET A CB    
2528 C  CG    . MET A 370 ? 0.6170 0.6788 0.6680 -0.0248 -0.0500 0.0254  350 MET A CG    
2529 S  SD    . MET A 370 ? 0.6520 0.7225 0.7129 -0.0180 -0.0495 0.0226  350 MET A SD    
2530 C  CE    . MET A 370 ? 0.4181 0.4894 0.4786 -0.0183 -0.0435 0.0221  350 MET A CE    
2531 N  N     . GLU A 371 ? 0.3950 0.4689 0.4431 -0.0482 -0.0545 0.0286  351 GLU A N     
2532 C  CA    . GLU A 371 ? 0.4340 0.5141 0.4835 -0.0546 -0.0576 0.0292  351 GLU A CA    
2533 C  C     . GLU A 371 ? 0.4942 0.5601 0.5336 -0.0573 -0.0612 0.0313  351 GLU A C     
2534 O  O     . GLU A 371 ? 0.4963 0.5633 0.5363 -0.0584 -0.0652 0.0314  351 GLU A O     
2535 C  CB    . GLU A 371 ? 0.4576 0.5470 0.5091 -0.0618 -0.0552 0.0297  351 GLU A CB    
2536 C  CG    . GLU A 371 ? 0.6647 0.7582 0.7153 -0.0700 -0.0586 0.0310  351 GLU A CG    
2537 C  CD    . GLU A 371 ? 0.8696 0.9624 0.9153 -0.0788 -0.0575 0.0333  351 GLU A CD    
2538 O  OE1   . GLU A 371 ? 0.9056 0.9951 0.9487 -0.0783 -0.0541 0.0337  351 GLU A OE1   
2539 O  OE2   . GLU A 371 ? 0.9101 1.0046 0.9536 -0.0864 -0.0606 0.0349  351 GLU A OE2   
2540 N  N     . GLN A 372 ? 0.3958 0.4484 0.4262 -0.0583 -0.0603 0.0327  352 GLN A N     
2541 C  CA    . GLN A 372 ? 0.4049 0.4437 0.4257 -0.0603 -0.0638 0.0338  352 GLN A CA    
2542 C  C     . GLN A 372 ? 0.4612 0.4899 0.4772 -0.0539 -0.0644 0.0330  352 GLN A C     
2543 O  O     . GLN A 372 ? 0.4077 0.4257 0.4159 -0.0549 -0.0673 0.0332  352 GLN A O     
2544 C  CB    . GLN A 372 ? 0.4641 0.4931 0.4774 -0.0645 -0.0635 0.0352  352 GLN A CB    
2545 C  CG    . GLN A 372 ? 0.5847 0.6224 0.6008 -0.0718 -0.0626 0.0366  352 GLN A CG    
2546 C  CD    . GLN A 372 ? 0.6093 0.6348 0.6163 -0.0775 -0.0648 0.0386  352 GLN A CD    
2547 O  OE1   . GLN A 372 ? 0.5858 0.5992 0.5854 -0.0786 -0.0690 0.0390  352 GLN A OE1   
2548 N  NE2   . GLN A 372 ? 0.7470 0.7747 0.7539 -0.0810 -0.0624 0.0398  352 GLN A NE2   
2549 N  N     . HIS A 373 ? 0.3468 0.3789 0.3670 -0.0479 -0.0619 0.0319  353 HIS A N     
2550 C  CA    . HIS A 373 ? 0.3379 0.3619 0.3537 -0.0425 -0.0624 0.0314  353 HIS A CA    
2551 C  C     . HIS A 373 ? 0.3778 0.3887 0.3843 -0.0418 -0.0611 0.0313  353 HIS A C     
2552 O  O     . HIS A 373 ? 0.3891 0.3916 0.3888 -0.0404 -0.0628 0.0308  353 HIS A O     
2553 C  CB    . HIS A 373 ? 0.4275 0.4512 0.4423 -0.0428 -0.0669 0.0316  353 HIS A CB    
2554 C  CG    . HIS A 373 ? 0.3889 0.4259 0.4136 -0.0429 -0.0687 0.0312  353 HIS A CG    
2555 N  ND1   . HIS A 373 ? 0.5010 0.5444 0.5326 -0.0376 -0.0682 0.0303  353 HIS A ND1   
2556 C  CD2   . HIS A 373 ? 0.5957 0.6413 0.6251 -0.0474 -0.0714 0.0314  353 HIS A CD2   
2557 C  CE1   . HIS A 373 ? 0.4449 0.5004 0.4853 -0.0384 -0.0705 0.0294  353 HIS A CE1   
2558 N  NE2   . HIS A 373 ? 0.4428 0.5006 0.4823 -0.0445 -0.0722 0.0301  353 HIS A NE2   
2559 N  N     . ILE A 374 ? 0.3321 0.3419 0.3384 -0.0428 -0.0582 0.0314  354 ILE A N     
2560 C  CA    . ILE A 374 ? 0.2966 0.2949 0.2953 -0.0413 -0.0570 0.0307  354 ILE A CA    
2561 C  C     . ILE A 374 ? 0.3663 0.3641 0.3657 -0.0355 -0.0535 0.0299  354 ILE A C     
2562 O  O     . ILE A 374 ? 0.3095 0.3147 0.3153 -0.0336 -0.0508 0.0301  354 ILE A O     
2563 C  CB    . ILE A 374 ? 0.2934 0.2899 0.2912 -0.0450 -0.0561 0.0315  354 ILE A CB    
2564 C  CG1   . ILE A 374 ? 0.3617 0.3573 0.3575 -0.0518 -0.0601 0.0328  354 ILE A CG1   
2565 C  CG2   . ILE A 374 ? 0.3106 0.2960 0.3020 -0.0424 -0.0550 0.0303  354 ILE A CG2   
2566 C  CD1   . ILE A 374 ? 0.4023 0.3973 0.3973 -0.0568 -0.0597 0.0342  354 ILE A CD1   
2567 N  N     . THR A 375 ? 0.2931 0.2827 0.2860 -0.0328 -0.0537 0.0287  355 THR A N     
2568 C  CA    . THR A 375 ? 0.3117 0.3004 0.3040 -0.0282 -0.0508 0.0280  355 THR A CA    
2569 C  C     . THR A 375 ? 0.2954 0.2803 0.2863 -0.0268 -0.0475 0.0272  355 THR A C     
2570 O  O     . THR A 375 ? 0.2999 0.2807 0.2886 -0.0291 -0.0482 0.0269  355 THR A O     
2571 C  CB    . THR A 375 ? 0.3430 0.3258 0.3285 -0.0267 -0.0521 0.0270  355 THR A CB    
2572 O  OG1   . THR A 375 ? 0.3692 0.3440 0.3480 -0.0276 -0.0529 0.0250  355 THR A OG1   
2573 C  CG2   . THR A 375 ? 0.3539 0.3395 0.3399 -0.0281 -0.0559 0.0280  355 THR A CG2   
2574 N  N     . PHE A 376 ? 0.3275 0.3131 0.3192 -0.0231 -0.0444 0.0269  356 PHE A N     
2575 C  CA    . PHE A 376 ? 0.2643 0.2467 0.2549 -0.0215 -0.0414 0.0260  356 PHE A CA    
2576 C  C     . PHE A 376 ? 0.2885 0.2624 0.2720 -0.0213 -0.0423 0.0237  356 PHE A C     
2577 O  O     . PHE A 376 ? 0.2930 0.2628 0.2754 -0.0217 -0.0420 0.0230  356 PHE A O     
2578 C  CB    . PHE A 376 ? 0.2398 0.2247 0.2325 -0.0179 -0.0382 0.0261  356 PHE A CB    
2579 C  CG    . PHE A 376 ? 0.2547 0.2370 0.2466 -0.0162 -0.0351 0.0251  356 PHE A CG    
2580 C  CD1   . PHE A 376 ? 0.2510 0.2345 0.2459 -0.0176 -0.0341 0.0257  356 PHE A CD1   
2581 C  CD2   . PHE A 376 ? 0.3001 0.2792 0.2882 -0.0136 -0.0332 0.0237  356 PHE A CD2   
2582 C  CE1   . PHE A 376 ? 0.2707 0.2516 0.2649 -0.0160 -0.0316 0.0248  356 PHE A CE1   
2583 C  CE2   . PHE A 376 ? 0.3034 0.2807 0.2914 -0.0119 -0.0305 0.0226  356 PHE A CE2   
2584 C  CZ    . PHE A 376 ? 0.3257 0.3035 0.3168 -0.0129 -0.0299 0.0232  356 PHE A CZ    
2585 N  N     . GLY A 377 ? 0.3344 0.3053 0.3130 -0.0207 -0.0438 0.0224  357 GLY A N     
2586 C  CA    . GLY A 377 ? 0.3623 0.3260 0.3345 -0.0202 -0.0449 0.0193  357 GLY A CA    
2587 C  C     . GLY A 377 ? 0.3358 0.2945 0.3065 -0.0231 -0.0485 0.0190  357 GLY A C     
2588 O  O     . GLY A 377 ? 0.3929 0.3454 0.3610 -0.0223 -0.0492 0.0169  357 GLY A O     
2589 N  N     . GLU A 378 ? 0.3412 0.3023 0.3136 -0.0266 -0.0513 0.0211  358 GLU A N     
2590 C  CA    . GLU A 378 ? 0.3847 0.3412 0.3555 -0.0306 -0.0551 0.0216  358 GLU A CA    
2591 C  C     . GLU A 378 ? 0.4001 0.3563 0.3736 -0.0319 -0.0541 0.0229  358 GLU A C     
2592 O  O     . GLU A 378 ? 0.3511 0.2993 0.3209 -0.0331 -0.0566 0.0220  358 GLU A O     
2593 C  CB    . GLU A 378 ? 0.3512 0.3126 0.3244 -0.0345 -0.0578 0.0238  358 GLU A CB    
2594 C  CG    . GLU A 378 ? 0.3655 0.3252 0.3345 -0.0341 -0.0602 0.0225  358 GLU A CG    
2595 C  CD    . GLU A 378 ? 0.4318 0.3986 0.4047 -0.0368 -0.0621 0.0248  358 GLU A CD    
2596 O  OE1   . GLU A 378 ? 0.3990 0.3736 0.3787 -0.0383 -0.0612 0.0270  358 GLU A OE1   
2597 O  OE2   . GLU A 378 ? 0.4837 0.4484 0.4527 -0.0373 -0.0648 0.0241  358 GLU A OE2   
2598 N  N     . PHE A 379 ? 0.3766 0.3411 0.3562 -0.0318 -0.0507 0.0250  359 PHE A N     
2599 C  CA    . PHE A 379 ? 0.3155 0.2811 0.2976 -0.0333 -0.0493 0.0264  359 PHE A CA    
2600 C  C     . PHE A 379 ? 0.3396 0.2974 0.3182 -0.0303 -0.0485 0.0244  359 PHE A C     
2601 O  O     . PHE A 379 ? 0.3759 0.3283 0.3525 -0.0325 -0.0503 0.0249  359 PHE A O     
2602 C  CB    . PHE A 379 ? 0.3170 0.2934 0.3063 -0.0322 -0.0454 0.0278  359 PHE A CB    
2603 C  CG    . PHE A 379 ? 0.3564 0.3360 0.3488 -0.0339 -0.0433 0.0291  359 PHE A CG    
2604 C  CD1   . PHE A 379 ? 0.4725 0.4551 0.4659 -0.0397 -0.0449 0.0311  359 PHE A CD1   
2605 C  CD2   . PHE A 379 ? 0.3909 0.3714 0.3850 -0.0301 -0.0395 0.0285  359 PHE A CD2   
2606 C  CE1   . PHE A 379 ? 0.5432 0.5295 0.5389 -0.0420 -0.0428 0.0324  359 PHE A CE1   
2607 C  CE2   . PHE A 379 ? 0.4701 0.4539 0.4667 -0.0318 -0.0376 0.0297  359 PHE A CE2   
2608 C  CZ    . PHE A 379 ? 0.4729 0.4597 0.4701 -0.0378 -0.0391 0.0316  359 PHE A CZ    
2609 N  N     . ALA A 380 ? 0.3309 0.2882 0.3085 -0.0254 -0.0462 0.0220  360 ALA A N     
2610 C  CA    . ALA A 380 ? 0.3368 0.2883 0.3118 -0.0219 -0.0453 0.0193  360 ALA A CA    
2611 C  C     . ALA A 380 ? 0.4150 0.3565 0.3843 -0.0221 -0.0498 0.0166  360 ALA A C     
2612 O  O     . ALA A 380 ? 0.5236 0.4589 0.4911 -0.0204 -0.0508 0.0148  360 ALA A O     
2613 C  CB    . ALA A 380 ? 0.4155 0.3702 0.3905 -0.0175 -0.0417 0.0173  360 ALA A CB    
2614 N  N     . ARG A 381 ? 0.4257 0.3650 0.3919 -0.0240 -0.0531 0.0161  361 ARG A N     
2615 C  CA    . ARG A 381 ? 0.4203 0.3493 0.3809 -0.0242 -0.0581 0.0133  361 ARG A CA    
2616 C  C     . ARG A 381 ? 0.4788 0.4023 0.4382 -0.0296 -0.0626 0.0161  361 ARG A C     
2617 O  O     . ARG A 381 ? 0.5529 0.4669 0.5074 -0.0307 -0.0679 0.0144  361 ARG A O     
2618 C  CB    . ARG A 381 ? 0.4988 0.4275 0.4560 -0.0239 -0.0597 0.0110  361 ARG A CB    
2619 C  CG    . ARG A 381 ? 0.4991 0.4316 0.4554 -0.0192 -0.0560 0.0076  361 ARG A CG    
2620 C  CD    . ARG A 381 ? 0.6622 0.5881 0.6150 -0.0151 -0.0572 0.0020  361 ARG A CD    
2621 N  NE    . ARG A 381 ? 0.5753 0.5062 0.5271 -0.0113 -0.0534 -0.0017 361 ARG A NE    
2622 C  CZ    . ARG A 381 ? 0.5298 0.4644 0.4840 -0.0081 -0.0494 -0.0029 361 ARG A CZ    
2623 N  NH1   . ARG A 381 ? 0.5811 0.5149 0.5391 -0.0079 -0.0487 -0.0007 361 ARG A NH1   
2624 N  NH2   . ARG A 381 ? 0.4025 0.3422 0.3551 -0.0056 -0.0461 -0.0063 361 ARG A NH2   
2625 N  N     . GLY A 382 ? 0.4505 0.3796 0.4140 -0.0331 -0.0609 0.0202  362 GLY A N     
2626 C  CA    . GLY A 382 ? 0.4574 0.3824 0.4193 -0.0391 -0.0646 0.0233  362 GLY A CA    
2627 C  C     . GLY A 382 ? 0.3992 0.3278 0.3614 -0.0452 -0.0670 0.0260  362 GLY A C     
2628 O  O     . GLY A 382 ? 0.4281 0.3530 0.3881 -0.0513 -0.0707 0.0287  362 GLY A O     
2629 N  N     . ILE A 383 ? 0.3763 0.3121 0.3410 -0.0441 -0.0653 0.0256  363 ILE A N     
2630 C  CA    . ILE A 383 ? 0.3529 0.2932 0.3186 -0.0496 -0.0677 0.0279  363 ILE A CA    
2631 C  C     . ILE A 383 ? 0.5011 0.4528 0.4730 -0.0536 -0.0648 0.0314  363 ILE A C     
2632 O  O     . ILE A 383 ? 0.4233 0.3841 0.4010 -0.0503 -0.0600 0.0313  363 ILE A O     
2633 C  CB    . ILE A 383 ? 0.4159 0.3602 0.3823 -0.0468 -0.0671 0.0263  363 ILE A CB    
2634 C  CG1   . ILE A 383 ? 0.4455 0.3789 0.4048 -0.0441 -0.0704 0.0226  363 ILE A CG1   
2635 C  CG2   . ILE A 383 ? 0.3941 0.3463 0.3638 -0.0518 -0.0686 0.0288  363 ILE A CG2   
2636 C  CD1   . ILE A 383 ? 0.5617 0.4983 0.5204 -0.0414 -0.0697 0.0208  363 ILE A CD1   
2637 N  N     . VAL A 384 ? 0.4328 0.3848 0.4037 -0.0609 -0.0680 0.0341  364 VAL A N     
2638 C  CA    . VAL A 384 ? 0.4492 0.4134 0.4259 -0.0657 -0.0653 0.0368  364 VAL A CA    
2639 C  C     . VAL A 384 ? 0.4602 0.4333 0.4400 -0.0710 -0.0670 0.0383  364 VAL A C     
2640 O  O     . VAL A 384 ? 0.5395 0.5253 0.5252 -0.0748 -0.0647 0.0398  364 VAL A O     
2641 C  CB    . VAL A 384 ? 0.4559 0.4149 0.4289 -0.0709 -0.0668 0.0392  364 VAL A CB    
2642 C  CG1   . VAL A 384 ? 0.4751 0.4269 0.4462 -0.0653 -0.0649 0.0377  364 VAL A CG1   
2643 C  CG2   . VAL A 384 ? 0.4674 0.4148 0.4327 -0.0772 -0.0737 0.0406  364 VAL A CG2   
2644 N  N     . ALA A 385 ? 0.4449 0.4125 0.4212 -0.0712 -0.0710 0.0374  365 ALA A N     
2645 C  CA    . ALA A 385 ? 0.4571 0.4328 0.4363 -0.0760 -0.0731 0.0385  365 ALA A CA    
2646 C  C     . ALA A 385 ? 0.4607 0.4320 0.4378 -0.0720 -0.0752 0.0364  365 ALA A C     
2647 O  O     . ALA A 385 ? 0.4739 0.4329 0.4445 -0.0684 -0.0771 0.0343  365 ALA A O     
2648 C  CB    . ALA A 385 ? 0.5886 0.5600 0.5632 -0.0854 -0.0779 0.0413  365 ALA A CB    
2649 N  N     . LYS A 386 ? 0.4524 0.4343 0.4349 -0.0728 -0.0752 0.0366  366 LYS A N     
2650 C  CA    . LYS A 386 ? 0.4397 0.4190 0.4205 -0.0690 -0.0770 0.0348  366 LYS A CA    
2651 C  C     . LYS A 386 ? 0.6069 0.5956 0.5920 -0.0732 -0.0796 0.0359  366 LYS A C     
2652 O  O     . LYS A 386 ? 0.5945 0.5972 0.5879 -0.0751 -0.0775 0.0369  366 LYS A O     
2653 C  CB    . LYS A 386 ? 0.4998 0.4829 0.4841 -0.0612 -0.0727 0.0332  366 LYS A CB    
2654 C  CG    . LYS A 386 ? 0.5393 0.5193 0.5208 -0.0574 -0.0741 0.0315  366 LYS A CG    
2655 C  CD    . LYS A 386 ? 0.4683 0.4509 0.4522 -0.0507 -0.0700 0.0304  366 LYS A CD    
2656 C  CE    . LYS A 386 ? 0.4302 0.4115 0.4115 -0.0477 -0.0714 0.0294  366 LYS A CE    
2657 N  NZ    . LYS A 386 ? 0.4754 0.4580 0.4578 -0.0422 -0.0678 0.0288  366 LYS A NZ    
2658 N  N     . ASN A 387 ? 0.6673 0.6488 0.6469 -0.0747 -0.0841 0.0353  367 ASN A N     
2659 C  CA    . ASN A 387 ? 0.7976 0.7868 0.7806 -0.0778 -0.0871 0.0360  367 ASN A CA    
2660 C  C     . ASN A 387 ? 0.9059 0.8844 0.8812 -0.0772 -0.0916 0.0346  367 ASN A C     
2661 O  O     . ASN A 387 ? 0.8784 0.8495 0.8491 -0.0715 -0.0907 0.0324  367 ASN A O     
2662 C  CB    . ASN A 387 ? 0.9264 0.9235 0.9129 -0.0864 -0.0888 0.0384  367 ASN A CB    
2663 C  CG    . ASN A 387 ? 1.0771 1.0615 1.0549 -0.0925 -0.0925 0.0397  367 ASN A CG    
2664 O  OD1   . ASN A 387 ? 1.0900 1.0607 1.0595 -0.0921 -0.0966 0.0386  367 ASN A OD1   
2665 N  ND2   . ASN A 387 ? 0.9521 0.9406 0.9313 -0.0982 -0.0915 0.0419  367 ASN A ND2   
2666 N  N     . MET B 21  ? 0.5941 0.6032 0.4745 -0.0420 0.0138  -0.0657 1   MET B N     
2667 C  CA    . MET B 21  ? 0.5088 0.5121 0.3946 -0.0417 0.0121  -0.0569 1   MET B CA    
2668 C  C     . MET B 21  ? 0.5609 0.5510 0.4479 -0.0413 0.0068  -0.0507 1   MET B C     
2669 O  O     . MET B 21  ? 0.5215 0.5075 0.4020 -0.0449 0.0041  -0.0498 1   MET B O     
2670 C  CB    . MET B 21  ? 0.5216 0.5307 0.4018 -0.0489 0.0138  -0.0511 1   MET B CB    
2671 C  CG    . MET B 21  ? 0.5917 0.6155 0.4696 -0.0512 0.0193  -0.0565 1   MET B CG    
2672 S  SD    . MET B 21  ? 0.5781 0.6076 0.4681 -0.0439 0.0225  -0.0599 1   MET B SD    
2673 C  CE    . MET B 21  ? 0.5662 0.5893 0.4587 -0.0463 0.0206  -0.0485 1   MET B CE    
2674 N  N     . ALA B 22  ? 0.4293 0.4134 0.3246 -0.0374 0.0053  -0.0465 2   ALA B N     
2675 C  CA    . ALA B 22  ? 0.4584 0.4322 0.3553 -0.0378 0.0006  -0.0401 2   ALA B CA    
2676 C  C     . ALA B 22  ? 0.4273 0.4009 0.3197 -0.0438 -0.0008 -0.0325 2   ALA B C     
2677 O  O     . ALA B 22  ? 0.3992 0.3791 0.2897 -0.0465 0.0017  -0.0308 2   ALA B O     
2678 C  CB    . ALA B 22  ? 0.4830 0.4517 0.3897 -0.0324 -0.0004 -0.0380 2   ALA B CB    
2679 N  N     . PRO B 23  ? 0.3733 0.3397 0.2640 -0.0460 -0.0053 -0.0279 3   PRO B N     
2680 C  CA    . PRO B 23  ? 0.3946 0.3595 0.2821 -0.0507 -0.0078 -0.0206 3   PRO B CA    
2681 C  C     . PRO B 23  ? 0.3735 0.3385 0.2685 -0.0483 -0.0072 -0.0163 3   PRO B C     
2682 O  O     . PRO B 23  ? 0.3497 0.3124 0.2531 -0.0432 -0.0069 -0.0168 3   PRO B O     
2683 C  CB    . PRO B 23  ? 0.4173 0.3745 0.3044 -0.0516 -0.0130 -0.0177 3   PRO B CB    
2684 C  CG    . PRO B 23  ? 0.4947 0.4499 0.3815 -0.0492 -0.0128 -0.0237 3   PRO B CG    
2685 C  CD    . PRO B 23  ? 0.4539 0.4128 0.3462 -0.0441 -0.0088 -0.0289 3   PRO B CD    
2686 N  N     . ILE B 24  ? 0.3266 0.2934 0.2180 -0.0523 -0.0076 -0.0118 4   ILE B N     
2687 C  CA    . ILE B 24  ? 0.3392 0.3055 0.2368 -0.0504 -0.0077 -0.0074 4   ILE B CA    
2688 C  C     . ILE B 24  ? 0.3867 0.3462 0.2862 -0.0510 -0.0132 -0.0014 4   ILE B C     
2689 O  O     . ILE B 24  ? 0.3660 0.3226 0.2587 -0.0555 -0.0169 0.0012  4   ILE B O     
2690 C  CB    . ILE B 24  ? 0.3765 0.3487 0.2695 -0.0543 -0.0051 -0.0063 4   ILE B CB    
2691 C  CG1   . ILE B 24  ? 0.4258 0.3963 0.3250 -0.0524 -0.0059 -0.0016 4   ILE B CG1   
2692 C  CG2   . ILE B 24  ? 0.4690 0.4411 0.3505 -0.0618 -0.0074 -0.0038 4   ILE B CG2   
2693 C  CD1   . ILE B 24  ? 0.5536 0.5311 0.4524 -0.0535 -0.0018 -0.0025 4   ILE B CD1   
2694 N  N     . ALA B 25  ? 0.3344 0.2915 0.2430 -0.0465 -0.0139 0.0003  5   ALA B N     
2695 C  CA    . ALA B 25  ? 0.3068 0.2593 0.2190 -0.0463 -0.0188 0.0050  5   ALA B CA    
2696 C  C     . ALA B 25  ? 0.3531 0.3059 0.2692 -0.0452 -0.0192 0.0087  5   ALA B C     
2697 O  O     . ALA B 25  ? 0.3618 0.3179 0.2816 -0.0429 -0.0153 0.0075  5   ALA B O     
2698 C  CB    . ALA B 25  ? 0.3411 0.2911 0.2607 -0.0425 -0.0199 0.0040  5   ALA B CB    
2699 N  N     . GLN B 26  ? 0.3102 0.2592 0.2255 -0.0469 -0.0243 0.0130  6   GLN B N     
2700 C  CA    . GLN B 26  ? 0.3014 0.2494 0.2202 -0.0457 -0.0259 0.0165  6   GLN B CA    
2701 C  C     . GLN B 26  ? 0.2970 0.2449 0.2267 -0.0405 -0.0269 0.0167  6   GLN B C     
2702 O  O     . GLN B 26  ? 0.3416 0.2876 0.2740 -0.0399 -0.0305 0.0172  6   GLN B O     
2703 C  CB    . GLN B 26  ? 0.3720 0.3153 0.2843 -0.0498 -0.0319 0.0208  6   GLN B CB    
2704 C  CG    . GLN B 26  ? 0.4035 0.3442 0.3197 -0.0482 -0.0352 0.0242  6   GLN B CG    
2705 C  CD    . GLN B 26  ? 0.4075 0.3509 0.3222 -0.0490 -0.0313 0.0245  6   GLN B CD    
2706 O  OE1   . GLN B 26  ? 0.4279 0.3723 0.3337 -0.0542 -0.0300 0.0250  6   GLN B OE1   
2707 N  NE2   . GLN B 26  ? 0.4268 0.3721 0.3501 -0.0443 -0.0292 0.0239  6   GLN B NE2   
2708 N  N     . ALA B 27  ? 0.2804 0.2308 0.2161 -0.0373 -0.0237 0.0163  7   ALA B N     
2709 C  CA    . ALA B 27  ? 0.2677 0.2190 0.2131 -0.0329 -0.0243 0.0164  7   ALA B CA    
2710 C  C     . ALA B 27  ? 0.2672 0.2162 0.2153 -0.0323 -0.0296 0.0195  7   ALA B C     
2711 O  O     . ALA B 27  ? 0.2998 0.2462 0.2432 -0.0343 -0.0320 0.0219  7   ALA B O     
2712 C  CB    . ALA B 27  ? 0.3028 0.2571 0.2530 -0.0299 -0.0196 0.0152  7   ALA B CB    
2713 N  N     . VAL B 28  ? 0.2641 0.2143 0.2197 -0.0295 -0.0317 0.0192  8   VAL B N     
2714 C  CA    . VAL B 28  ? 0.2790 0.2286 0.2394 -0.0275 -0.0366 0.0209  8   VAL B CA    
2715 C  C     . VAL B 28  ? 0.3110 0.2609 0.2736 -0.0256 -0.0351 0.0218  8   VAL B C     
2716 O  O     . VAL B 28  ? 0.2927 0.2460 0.2591 -0.0236 -0.0302 0.0204  8   VAL B O     
2717 C  CB    . VAL B 28  ? 0.2765 0.2301 0.2459 -0.0248 -0.0377 0.0194  8   VAL B CB    
2718 C  CG1   . VAL B 28  ? 0.3156 0.2702 0.2916 -0.0216 -0.0423 0.0200  8   VAL B CG1   
2719 C  CG2   . VAL B 28  ? 0.3316 0.2843 0.2985 -0.0271 -0.0401 0.0189  8   VAL B CG2   
2720 N  N     . THR B 29  ? 0.3049 0.2508 0.2650 -0.0261 -0.0399 0.0241  9   THR B N     
2721 C  CA    . THR B 29  ? 0.2975 0.2423 0.2580 -0.0250 -0.0393 0.0253  9   THR B CA    
2722 C  C     . THR B 29  ? 0.3306 0.2740 0.2973 -0.0214 -0.0450 0.0257  9   THR B C     
2723 O  O     . THR B 29  ? 0.3736 0.3133 0.3391 -0.0217 -0.0514 0.0267  9   THR B O     
2724 C  CB    . THR B 29  ? 0.3377 0.2781 0.2876 -0.0300 -0.0400 0.0278  9   THR B CB    
2725 O  OG1   . THR B 29  ? 0.3513 0.2946 0.2963 -0.0328 -0.0345 0.0263  9   THR B OG1   
2726 C  CG2   . THR B 29  ? 0.3571 0.2964 0.3071 -0.0294 -0.0394 0.0292  9   THR B CG2   
2727 N  N     . VAL B 30  ? 0.2982 0.2445 0.2714 -0.0177 -0.0430 0.0247  10  VAL B N     
2728 C  CA    . VAL B 30  ? 0.3243 0.2697 0.3035 -0.0138 -0.0482 0.0243  10  VAL B CA    
2729 C  C     . VAL B 30  ? 0.3477 0.2904 0.3255 -0.0133 -0.0477 0.0255  10  VAL B C     
2730 O  O     . VAL B 30  ? 0.3079 0.2520 0.2827 -0.0151 -0.0421 0.0260  10  VAL B O     
2731 C  CB    . VAL B 30  ? 0.3315 0.2847 0.3219 -0.0093 -0.0470 0.0209  10  VAL B CB    
2732 C  CG1   . VAL B 30  ? 0.3371 0.2928 0.3288 -0.0102 -0.0483 0.0199  10  VAL B CG1   
2733 C  CG2   . VAL B 30  ? 0.3084 0.2673 0.3022 -0.0084 -0.0395 0.0195  10  VAL B CG2   
2734 N  N     . SER B 31  ? 0.3272 0.2660 0.3074 -0.0106 -0.0539 0.0257  11  SER B N     
2735 C  CA    . SER B 31  ? 0.3021 0.2374 0.2811 -0.0100 -0.0546 0.0268  11  SER B CA    
2736 C  C     . SER B 31  ? 0.3037 0.2457 0.2924 -0.0048 -0.0512 0.0236  11  SER B C     
2737 O  O     . SER B 31  ? 0.2957 0.2430 0.2930 -0.0007 -0.0525 0.0205  11  SER B O     
2738 C  CB    . SER B 31  ? 0.3833 0.3092 0.3589 -0.0098 -0.0640 0.0288  11  SER B CB    
2739 O  OG    . SER B 31  ? 0.3822 0.3046 0.3578 -0.0086 -0.0653 0.0294  11  SER B OG    
2740 N  N     . LEU B 32  ? 0.2954 0.2379 0.2829 -0.0053 -0.0470 0.0242  12  LEU B N     
2741 C  CA    . LEU B 32  ? 0.2633 0.2113 0.2589 -0.0009 -0.0443 0.0214  12  LEU B CA    
2742 C  C     . LEU B 32  ? 0.2979 0.2439 0.2989 0.0038  -0.0511 0.0195  12  LEU B C     
2743 O  O     . LEU B 32  ? 0.3157 0.2687 0.3254 0.0082  -0.0497 0.0158  12  LEU B O     
2744 C  CB    . LEU B 32  ? 0.2890 0.2361 0.2812 -0.0025 -0.0400 0.0229  12  LEU B CB    
2745 C  CG    . LEU B 32  ? 0.2990 0.2509 0.2981 0.0015  -0.0372 0.0204  12  LEU B CG    
2746 C  CD1   . LEU B 32  ? 0.2962 0.2572 0.3022 0.0035  -0.0322 0.0176  12  LEU B CD1   
2747 C  CD2   . LEU B 32  ? 0.3598 0.3103 0.3547 -0.0007 -0.0335 0.0222  12  LEU B CD2   
2748 N  N     . ASN B 33  ? 0.3416 0.2782 0.3375 0.0029  -0.0587 0.0216  13  ASN B N     
2749 C  CA    . ASN B 33  ? 0.3784 0.3122 0.3796 0.0080  -0.0663 0.0193  13  ASN B CA    
2750 C  C     . ASN B 33  ? 0.3647 0.3061 0.3751 0.0121  -0.0677 0.0152  13  ASN B C     
2751 O  O     . ASN B 33  ? 0.3572 0.3041 0.3766 0.0177  -0.0692 0.0107  13  ASN B O     
2752 C  CB    . ASN B 33  ? 0.3824 0.3033 0.3754 0.0055  -0.0753 0.0228  13  ASN B CB    
2753 C  CG    . ASN B 33  ? 0.5161 0.4299 0.4997 0.0006  -0.0743 0.0269  13  ASN B CG    
2754 O  OD1   . ASN B 33  ? 0.5953 0.5116 0.5811 0.0018  -0.0703 0.0261  13  ASN B OD1   
2755 N  ND2   . ASN B 33  ? 0.6786 0.5841 0.6516 -0.0054 -0.0778 0.0315  13  ASN B ND2   
2756 N  N     . ASP B 34  ? 0.3092 0.2521 0.3175 0.0093  -0.0670 0.0162  14  ASP B N     
2757 C  CA    . ASP B 34  ? 0.3271 0.2780 0.3439 0.0124  -0.0681 0.0125  14  ASP B CA    
2758 C  C     . ASP B 34  ? 0.2995 0.2629 0.3240 0.0140  -0.0602 0.0093  14  ASP B C     
2759 O  O     . ASP B 34  ? 0.3141 0.2862 0.3480 0.0179  -0.0611 0.0049  14  ASP B O     
2760 C  CB    . ASP B 34  ? 0.3871 0.3355 0.3986 0.0084  -0.0696 0.0149  14  ASP B CB    
2761 C  CG    . ASP B 34  ? 0.4826 0.4193 0.4873 0.0071  -0.0789 0.0177  14  ASP B CG    
2762 O  OD1   . ASP B 34  ? 0.6603 0.5942 0.6697 0.0118  -0.0864 0.0156  14  ASP B OD1   
2763 O  OD2   . ASP B 34  ? 0.4074 0.3376 0.4018 0.0014  -0.0788 0.0219  14  ASP B OD2   
2764 N  N     . LEU B 35  ? 0.2832 0.2480 0.3038 0.0107  -0.0527 0.0111  15  LEU B N     
2765 C  CA    . LEU B 35  ? 0.3007 0.2758 0.3276 0.0117  -0.0459 0.0085  15  LEU B CA    
2766 C  C     . LEU B 35  ? 0.3164 0.2956 0.3500 0.0164  -0.0464 0.0052  15  LEU B C     
2767 O  O     . LEU B 35  ? 0.3155 0.3050 0.3574 0.0190  -0.0445 0.0012  15  LEU B O     
2768 C  CB    . LEU B 35  ? 0.2647 0.2388 0.2857 0.0077  -0.0389 0.0112  15  LEU B CB    
2769 C  CG    . LEU B 35  ? 0.2626 0.2359 0.2789 0.0036  -0.0368 0.0130  15  LEU B CG    
2770 C  CD1   . LEU B 35  ? 0.2674 0.2381 0.2771 0.0002  -0.0312 0.0153  15  LEU B CD1   
2771 C  CD2   . LEU B 35  ? 0.2959 0.2780 0.3187 0.0039  -0.0348 0.0105  15  LEU B CD2   
2772 N  N     . LYS B 36  ? 0.3244 0.2958 0.3543 0.0173  -0.0492 0.0066  16  LYS B N     
2773 C  CA    . LYS B 36  ? 0.2920 0.2665 0.3278 0.0219  -0.0500 0.0032  16  LYS B CA    
2774 C  C     . LYS B 36  ? 0.3607 0.3388 0.4047 0.0273  -0.0565 -0.0016 16  LYS B C     
2775 O  O     . LYS B 36  ? 0.3851 0.3718 0.4370 0.0314  -0.0554 -0.0063 16  LYS B O     
2776 C  CB    . LYS B 36  ? 0.3791 0.3434 0.4084 0.0212  -0.0523 0.0059  16  LYS B CB    
2777 C  CG    . LYS B 36  ? 0.3504 0.3136 0.3736 0.0169  -0.0455 0.0093  16  LYS B CG    
2778 C  CD    . LYS B 36  ? 0.4716 0.4243 0.4871 0.0148  -0.0483 0.0128  16  LYS B CD    
2779 C  CE    . LYS B 36  ? 0.6344 0.5857 0.6536 0.0190  -0.0514 0.0104  16  LYS B CE    
2780 N  NZ    . LYS B 36  ? 0.8313 0.7726 0.8426 0.0161  -0.0537 0.0141  16  LYS B NZ    
2781 N  N     . ASN B 37  ? 0.3253 0.2974 0.3676 0.0275  -0.0635 -0.0007 17  ASN B N     
2782 C  CA    . ASN B 37  ? 0.3611 0.3359 0.4114 0.0332  -0.0709 -0.0055 17  ASN B CA    
2783 C  C     . ASN B 37  ? 0.3254 0.3130 0.3840 0.0342  -0.0691 -0.0092 17  ASN B C     
2784 O  O     . ASN B 37  ? 0.3903 0.3832 0.4574 0.0395  -0.0744 -0.0143 17  ASN B O     
2785 C  CB    . ASN B 37  ? 0.4931 0.4546 0.5376 0.0330  -0.0806 -0.0028 17  ASN B CB    
2786 C  CG    . ASN B 37  ? 0.4830 0.4319 0.5210 0.0331  -0.0852 -0.0002 17  ASN B CG    
2787 O  OD1   . ASN B 37  ? 0.4868 0.4367 0.5248 0.0336  -0.0812 -0.0007 17  ASN B OD1   
2788 N  ND2   . ASN B 37  ? 0.5139 0.4500 0.5454 0.0319  -0.0940 0.0028  17  ASN B ND2   
2789 N  N     . GLY B 38  ? 0.2984 0.2913 0.3550 0.0295  -0.0620 -0.0071 18  GLY B N     
2790 C  CA    . GLY B 38  ? 0.2786 0.2831 0.3421 0.0294  -0.0604 -0.0101 18  GLY B CA    
2791 C  C     . GLY B 38  ? 0.3399 0.3404 0.4026 0.0291  -0.0669 -0.0092 18  GLY B C     
2792 O  O     . GLY B 38  ? 0.3830 0.3933 0.4537 0.0309  -0.0685 -0.0130 18  GLY B O     
2793 N  N     . THR B 39  ? 0.3730 0.3596 0.4260 0.0266  -0.0711 -0.0044 19  THR B N     
2794 C  CA    . THR B 39  ? 0.3866 0.3675 0.4372 0.0259  -0.0782 -0.0030 19  THR B CA    
2795 C  C     . THR B 39  ? 0.4355 0.4116 0.4768 0.0192  -0.0749 0.0019  19  THR B C     
2796 O  O     . THR B 39  ? 0.3731 0.3420 0.4095 0.0176  -0.0808 0.0042  19  THR B O     
2797 C  CB    . THR B 39  ? 0.3604 0.3282 0.4069 0.0283  -0.0876 -0.0017 19  THR B CB    
2798 O  OG1   . THR B 39  ? 0.3744 0.3321 0.4104 0.0243  -0.0852 0.0032  19  THR B OG1   
2799 C  CG2   . THR B 39  ? 0.3834 0.3557 0.4400 0.0358  -0.0922 -0.0076 19  THR B CG2   
2800 N  N     . VAL B 40  ? 0.3643 0.3438 0.4025 0.0154  -0.0662 0.0036  20  VAL B N     
2801 C  CA    . VAL B 40  ? 0.3299 0.3055 0.3599 0.0097  -0.0634 0.0073  20  VAL B CA    
2802 C  C     . VAL B 40  ? 0.3792 0.3602 0.4132 0.0093  -0.0657 0.0057  20  VAL B C     
2803 O  O     . VAL B 40  ? 0.3712 0.3633 0.4152 0.0120  -0.0651 0.0016  20  VAL B O     
2804 C  CB    . VAL B 40  ? 0.4750 0.4537 0.5023 0.0066  -0.0542 0.0085  20  VAL B CB    
2805 C  CG1   . VAL B 40  ? 0.4964 0.4874 0.5324 0.0076  -0.0497 0.0051  20  VAL B CG1   
2806 C  CG2   . VAL B 40  ? 0.5157 0.4889 0.5337 0.0013  -0.0520 0.0120  20  VAL B CG2   
2807 N  N     . SER B 41  ? 0.3488 0.3226 0.3751 0.0055  -0.0684 0.0089  21  SER B N     
2808 C  CA    . SER B 41  ? 0.3595 0.3375 0.3887 0.0046  -0.0709 0.0077  21  SER B CA    
2809 C  C     . SER B 41  ? 0.3863 0.3732 0.4181 0.0019  -0.0633 0.0067  21  SER B C     
2810 O  O     . SER B 41  ? 0.3473 0.3310 0.3723 -0.0018 -0.0577 0.0091  21  SER B O     
2811 C  CB    . SER B 41  ? 0.4030 0.3705 0.4218 0.0006  -0.0752 0.0116  21  SER B CB    
2812 O  OG    . SER B 41  ? 0.4384 0.4099 0.4584 -0.0016 -0.0756 0.0110  21  SER B OG    
2813 N  N     . LEU B 42  ? 0.3248 0.3229 0.3664 0.0036  -0.0636 0.0030  22  LEU B N     
2814 C  CA    . LEU B 42  ? 0.3597 0.3655 0.4031 0.0002  -0.0575 0.0025  22  LEU B CA    
2815 C  C     . LEU B 42  ? 0.3467 0.3478 0.3834 -0.0044 -0.0582 0.0048  22  LEU B C     
2816 O  O     . LEU B 42  ? 0.3278 0.3303 0.3618 -0.0082 -0.0531 0.0057  22  LEU B O     
2817 C  CB    . LEU B 42  ? 0.3435 0.3639 0.3991 0.0026  -0.0575 -0.0022 22  LEU B CB    
2818 C  CG    . LEU B 42  ? 0.3438 0.3709 0.4066 0.0070  -0.0561 -0.0055 22  LEU B CG    
2819 C  CD1   . LEU B 42  ? 0.3545 0.3981 0.4290 0.0082  -0.0552 -0.0105 22  LEU B CD1   
2820 C  CD2   . LEU B 42  ? 0.3498 0.3738 0.4077 0.0055  -0.0493 -0.0034 22  LEU B CD2   
2821 N  N     . GLU B 43  ? 0.3244 0.3195 0.3581 -0.0042 -0.0650 0.0058  23  GLU B N     
2822 C  CA    A GLU B 43  ? 0.3361 0.3251 0.3616 -0.0088 -0.0657 0.0083  23  GLU B CA    
2823 C  CA    B GLU B 43  ? 0.3361 0.3250 0.3615 -0.0088 -0.0657 0.0084  23  GLU B CA    
2824 C  C     . GLU B 43  ? 0.3176 0.2979 0.3321 -0.0121 -0.0611 0.0115  23  GLU B C     
2825 O  O     . GLU B 43  ? 0.3398 0.3190 0.3496 -0.0159 -0.0573 0.0123  23  GLU B O     
2826 C  CB    A GLU B 43  ? 0.3261 0.3098 0.3499 -0.0079 -0.0745 0.0090  23  GLU B CB    
2827 C  CB    B GLU B 43  ? 0.3262 0.3095 0.3496 -0.0081 -0.0744 0.0091  23  GLU B CB    
2828 C  CG    A GLU B 43  ? 0.3684 0.3618 0.4036 -0.0048 -0.0795 0.0053  23  GLU B CG    
2829 C  CG    B GLU B 43  ? 0.4086 0.3867 0.4239 -0.0129 -0.0757 0.0113  23  GLU B CG    
2830 C  CD    A GLU B 43  ? 0.4472 0.4483 0.4932 0.0012  -0.0808 0.0014  23  GLU B CD    
2831 C  CD    B GLU B 43  ? 0.5238 0.4957 0.5364 -0.0126 -0.0848 0.0124  23  GLU B CD    
2832 O  OE1   A GLU B 43  ? 0.4002 0.3960 0.4441 0.0035  -0.0807 0.0022  23  GLU B OE1   
2833 O  OE1   B GLU B 43  ? 0.4946 0.4644 0.5104 -0.0086 -0.0906 0.0119  23  GLU B OE1   
2834 O  OE2   A GLU B 43  ? 0.4343 0.4475 0.4913 0.0036  -0.0821 -0.0027 23  GLU B OE2   
2835 O  OE2   B GLU B 43  ? 0.5214 0.4900 0.5282 -0.0164 -0.0866 0.0138  23  GLU B OE2   
2836 N  N     . ALA B 44  ? 0.3405 0.3148 0.3512 -0.0107 -0.0615 0.0130  24  ALA B N     
2837 C  CA    . ALA B 44  ? 0.3343 0.3023 0.3357 -0.0137 -0.0567 0.0154  24  ALA B CA    
2838 C  C     . ALA B 44  ? 0.3116 0.2848 0.3156 -0.0139 -0.0491 0.0143  24  ALA B C     
2839 O  O     . ALA B 44  ? 0.2958 0.2659 0.2934 -0.0169 -0.0450 0.0152  24  ALA B O     
2840 C  CB    . ALA B 44  ? 0.3833 0.3448 0.3807 -0.0124 -0.0590 0.0173  24  ALA B CB    
2841 N  N     . LEU B 45  ? 0.2732 0.2540 0.2861 -0.0109 -0.0475 0.0121  25  LEU B N     
2842 C  CA    . LEU B 45  ? 0.2797 0.2649 0.2946 -0.0116 -0.0409 0.0114  25  LEU B CA    
2843 C  C     . LEU B 45  ? 0.2889 0.2760 0.3027 -0.0151 -0.0389 0.0111  25  LEU B C     
2844 O  O     . LEU B 45  ? 0.2654 0.2499 0.2748 -0.0173 -0.0346 0.0118  25  LEU B O     
2845 C  CB    . LEU B 45  ? 0.2841 0.2781 0.3086 -0.0082 -0.0399 0.0089  25  LEU B CB    
2846 C  CG    . LEU B 45  ? 0.2945 0.2922 0.3203 -0.0089 -0.0335 0.0086  25  LEU B CG    
2847 C  CD1   . LEU B 45  ? 0.2666 0.2577 0.2867 -0.0083 -0.0308 0.0104  25  LEU B CD1   
2848 C  CD2   . LEU B 45  ? 0.2743 0.2829 0.3098 -0.0065 -0.0328 0.0057  25  LEU B CD2   
2849 N  N     . GLU B 46  ? 0.2478 0.2392 0.2657 -0.0157 -0.0426 0.0100  26  GLU B N     
2850 C  CA    . GLU B 46  ? 0.2641 0.2565 0.2804 -0.0195 -0.0414 0.0099  26  GLU B CA    
2851 C  C     . GLU B 46  ? 0.2648 0.2477 0.2708 -0.0223 -0.0417 0.0117  26  GLU B C     
2852 O  O     . GLU B 46  ? 0.2853 0.2661 0.2875 -0.0252 -0.0390 0.0118  26  GLU B O     
2853 C  CB    . GLU B 46  ? 0.2942 0.2942 0.3175 -0.0196 -0.0454 0.0082  26  GLU B CB    
2854 C  CG    . GLU B 46  ? 0.2899 0.2929 0.3132 -0.0240 -0.0438 0.0079  26  GLU B CG    
2855 C  CD    . GLU B 46  ? 0.3956 0.3906 0.4108 -0.0271 -0.0459 0.0093  26  GLU B CD    
2856 O  OE1   . GLU B 46  ? 0.4011 0.3906 0.4121 -0.0262 -0.0498 0.0102  26  GLU B OE1   
2857 O  OE2   . GLU B 46  ? 0.4335 0.4273 0.4458 -0.0308 -0.0438 0.0095  26  GLU B OE2   
2858 N  N     . GLU B 47  ? 0.2723 0.2491 0.2732 -0.0217 -0.0452 0.0130  27  GLU B N     
2859 C  CA    . GLU B 47  ? 0.2693 0.2383 0.2598 -0.0248 -0.0449 0.0144  27  GLU B CA    
2860 C  C     . GLU B 47  ? 0.2662 0.2324 0.2522 -0.0252 -0.0391 0.0145  27  GLU B C     
2861 O  O     . GLU B 47  ? 0.2758 0.2381 0.2553 -0.0276 -0.0372 0.0142  27  GLU B O     
2862 C  CB    . GLU B 47  ? 0.2851 0.2486 0.2706 -0.0247 -0.0499 0.0161  27  GLU B CB    
2863 C  CG    . GLU B 47  ? 0.4054 0.3620 0.3798 -0.0286 -0.0501 0.0174  27  GLU B CG    
2864 C  CD    . GLU B 47  ? 0.6970 0.6480 0.6658 -0.0295 -0.0559 0.0196  27  GLU B CD    
2865 O  OE1   . GLU B 47  ? 0.6619 0.6139 0.6363 -0.0268 -0.0609 0.0199  27  GLU B OE1   
2866 O  OE2   . GLU B 47  ? 0.7062 0.6519 0.6649 -0.0330 -0.0557 0.0209  27  GLU B OE2   
2867 N  N     . ALA B 48  ? 0.2524 0.2208 0.2422 -0.0226 -0.0365 0.0145  28  ALA B N     
2868 C  CA    . ALA B 48  ? 0.2615 0.2278 0.2479 -0.0225 -0.0313 0.0144  28  ALA B CA    
2869 C  C     . ALA B 48  ? 0.2618 0.2307 0.2511 -0.0230 -0.0277 0.0132  28  ALA B C     
2870 O  O     . ALA B 48  ? 0.2562 0.2218 0.2412 -0.0237 -0.0245 0.0127  28  ALA B O     
2871 C  CB    . ALA B 48  ? 0.2550 0.2223 0.2440 -0.0197 -0.0304 0.0151  28  ALA B CB    
2872 N  N     . PHE B 49  ? 0.2369 0.2118 0.2335 -0.0228 -0.0284 0.0126  29  PHE B N     
2873 C  CA    . PHE B 49  ? 0.2337 0.2112 0.2331 -0.0236 -0.0252 0.0120  29  PHE B CA    
2874 C  C     . PHE B 49  ? 0.2645 0.2443 0.2654 -0.0268 -0.0266 0.0116  29  PHE B C     
2875 O  O     . PHE B 49  ? 0.2573 0.2380 0.2592 -0.0286 -0.0244 0.0115  29  PHE B O     
2876 C  CB    . PHE B 49  ? 0.2273 0.2115 0.2339 -0.0213 -0.0237 0.0118  29  PHE B CB    
2877 C  CG    . PHE B 49  ? 0.2371 0.2191 0.2424 -0.0187 -0.0212 0.0123  29  PHE B CG    
2878 C  CD1   . PHE B 49  ? 0.2267 0.2021 0.2253 -0.0188 -0.0195 0.0128  29  PHE B CD1   
2879 C  CD2   . PHE B 49  ? 0.2471 0.2347 0.2585 -0.0162 -0.0205 0.0118  29  PHE B CD2   
2880 C  CE1   . PHE B 49  ? 0.2689 0.2434 0.2669 -0.0167 -0.0172 0.0132  29  PHE B CE1   
2881 C  CE2   . PHE B 49  ? 0.2466 0.2323 0.2570 -0.0140 -0.0183 0.0123  29  PHE B CE2   
2882 C  CZ    . PHE B 49  ? 0.2262 0.2053 0.2299 -0.0144 -0.0168 0.0132  29  PHE B CZ    
2883 N  N     . GLY B 50  ? 0.2663 0.2467 0.2672 -0.0280 -0.0304 0.0114  30  GLY B N     
2884 C  CA    . GLY B 50  ? 0.2699 0.2537 0.2731 -0.0312 -0.0321 0.0109  30  GLY B CA    
2885 C  C     . GLY B 50  ? 0.2933 0.2700 0.2896 -0.0344 -0.0316 0.0110  30  GLY B C     
2886 O  O     . GLY B 50  ? 0.2796 0.2493 0.2697 -0.0337 -0.0298 0.0109  30  GLY B O     
2887 N  N     . PRO B 51  ? 0.2929 0.2719 0.2907 -0.0378 -0.0336 0.0108  31  PRO B N     
2888 C  CA    . PRO B 51  ? 0.2947 0.2665 0.2862 -0.0411 -0.0337 0.0106  31  PRO B CA    
2889 C  C     . PRO B 51  ? 0.2662 0.2298 0.2496 -0.0407 -0.0349 0.0099  31  PRO B C     
2890 O  O     . PRO B 51  ? 0.3311 0.2877 0.3087 -0.0417 -0.0340 0.0090  31  PRO B O     
2891 C  CB    . PRO B 51  ? 0.3422 0.3194 0.3375 -0.0451 -0.0364 0.0107  31  PRO B CB    
2892 C  CG    . PRO B 51  ? 0.3914 0.3802 0.3960 -0.0439 -0.0360 0.0106  31  PRO B CG    
2893 C  CD    . PRO B 51  ? 0.3324 0.3211 0.3379 -0.0390 -0.0360 0.0103  31  PRO B CD    
2894 N  N     . ASP B 52  ? 0.3029 0.2671 0.2854 -0.0395 -0.0371 0.0101  32  ASP B N     
2895 C  CA    . ASP B 52  ? 0.3367 0.2942 0.3108 -0.0398 -0.0381 0.0094  32  ASP B CA    
2896 C  C     . ASP B 52  ? 0.2714 0.2268 0.2422 -0.0371 -0.0356 0.0095  32  ASP B C     
2897 O  O     . ASP B 52  ? 0.3224 0.2737 0.2862 -0.0377 -0.0362 0.0091  32  ASP B O     
2898 C  CB    . ASP B 52  ? 0.3320 0.2907 0.3057 -0.0412 -0.0428 0.0099  32  ASP B CB    
2899 C  CG    . ASP B 52  ? 0.4356 0.3965 0.4119 -0.0445 -0.0454 0.0096  32  ASP B CG    
2900 O  OD1   . ASP B 52  ? 0.5208 0.4775 0.4935 -0.0467 -0.0445 0.0088  32  ASP B OD1   
2901 O  OD2   . ASP B 52  ? 0.5278 0.4948 0.5099 -0.0447 -0.0486 0.0101  32  ASP B OD2   
2902 N  N     . SER B 53  ? 0.2947 0.2530 0.2700 -0.0346 -0.0328 0.0100  33  SER B N     
2903 C  CA    . SER B 53  ? 0.2817 0.2392 0.2550 -0.0322 -0.0309 0.0105  33  SER B CA    
2904 C  C     . SER B 53  ? 0.2971 0.2504 0.2654 -0.0316 -0.0272 0.0089  33  SER B C     
2905 O  O     . SER B 53  ? 0.2699 0.2202 0.2365 -0.0325 -0.0263 0.0074  33  SER B O     
2906 C  CB    . SER B 53  ? 0.2644 0.2272 0.2452 -0.0296 -0.0299 0.0115  33  SER B CB    
2907 O  OG    . SER B 53  ? 0.2481 0.2118 0.2315 -0.0291 -0.0265 0.0110  33  SER B OG    
2908 N  N     . LEU B 54  ? 0.2619 0.2151 0.2281 -0.0300 -0.0252 0.0092  34  LEU B N     
2909 C  CA    . LEU B 54  ? 0.2617 0.2131 0.2250 -0.0287 -0.0215 0.0074  34  LEU B CA    
2910 C  C     . LEU B 54  ? 0.2649 0.2183 0.2339 -0.0263 -0.0188 0.0078  34  LEU B C     
2911 O  O     . LEU B 54  ? 0.2674 0.2194 0.2350 -0.0248 -0.0160 0.0063  34  LEU B O     
2912 C  CB    . LEU B 54  ? 0.2675 0.2189 0.2256 -0.0289 -0.0206 0.0077  34  LEU B CB    
2913 C  CG    . LEU B 54  ? 0.2883 0.2375 0.2389 -0.0320 -0.0228 0.0073  34  LEU B CG    
2914 C  CD1   . LEU B 54  ? 0.2782 0.2281 0.2239 -0.0331 -0.0222 0.0084  34  LEU B CD1   
2915 C  CD2   . LEU B 54  ? 0.3026 0.2492 0.2486 -0.0328 -0.0217 0.0038  34  LEU B CD2   
2916 N  N     . GLY B 55  ? 0.2476 0.2047 0.2231 -0.0259 -0.0199 0.0095  35  GLY B N     
2917 C  CA    . GLY B 55  ? 0.2492 0.2087 0.2297 -0.0242 -0.0175 0.0100  35  GLY B CA    
2918 C  C     . GLY B 55  ? 0.2382 0.1986 0.2189 -0.0217 -0.0151 0.0103  35  GLY B C     
2919 O  O     . GLY B 55  ? 0.2457 0.2063 0.2282 -0.0203 -0.0126 0.0101  35  GLY B O     
2920 N  N     . ILE B 56  ? 0.2405 0.2013 0.2192 -0.0216 -0.0163 0.0112  36  ILE B N     
2921 C  CA    . ILE B 56  ? 0.2365 0.1979 0.2145 -0.0200 -0.0143 0.0117  36  ILE B CA    
2922 C  C     . ILE B 56  ? 0.2446 0.2067 0.2230 -0.0200 -0.0174 0.0136  36  ILE B C     
2923 O  O     . ILE B 56  ? 0.2481 0.2089 0.2240 -0.0217 -0.0208 0.0142  36  ILE B O     
2924 C  CB    . ILE B 56  ? 0.2402 0.1993 0.2119 -0.0206 -0.0120 0.0100  36  ILE B CB    
2925 C  CG1   . ILE B 56  ? 0.2386 0.1993 0.2105 -0.0191 -0.0096 0.0105  36  ILE B CG1   
2926 C  CG2   . ILE B 56  ? 0.2471 0.2043 0.2121 -0.0233 -0.0140 0.0098  36  ILE B CG2   
2927 C  CD1   . ILE B 56  ? 0.2440 0.2047 0.2116 -0.0192 -0.0065 0.0080  36  ILE B CD1   
2928 N  N     . LEU B 57  ? 0.2461 0.2098 0.2274 -0.0181 -0.0166 0.0145  37  LEU B N     
2929 C  CA    . LEU B 57  ? 0.2340 0.1973 0.2157 -0.0175 -0.0200 0.0162  37  LEU B CA    
2930 C  C     . LEU B 57  ? 0.2519 0.2138 0.2303 -0.0175 -0.0183 0.0171  37  LEU B C     
2931 O  O     . LEU B 57  ? 0.2597 0.2235 0.2405 -0.0159 -0.0147 0.0165  37  LEU B O     
2932 C  CB    . LEU B 57  ? 0.2412 0.2087 0.2314 -0.0148 -0.0214 0.0160  37  LEU B CB    
2933 C  CG    . LEU B 57  ? 0.2714 0.2384 0.2635 -0.0131 -0.0256 0.0169  37  LEU B CG    
2934 C  CD1   . LEU B 57  ? 0.2954 0.2601 0.2858 -0.0143 -0.0311 0.0175  37  LEU B CD1   
2935 C  CD2   . LEU B 57  ? 0.3226 0.2951 0.3234 -0.0098 -0.0254 0.0156  37  LEU B CD2   
2936 N  N     . VAL B 58  ? 0.2399 0.1985 0.2124 -0.0197 -0.0209 0.0187  38  VAL B N     
2937 C  CA    . VAL B 58  ? 0.2410 0.1985 0.2099 -0.0206 -0.0198 0.0200  38  VAL B CA    
2938 C  C     . VAL B 58  ? 0.2740 0.2298 0.2459 -0.0189 -0.0239 0.0218  38  VAL B C     
2939 O  O     . VAL B 58  ? 0.2903 0.2434 0.2622 -0.0189 -0.0292 0.0227  38  VAL B O     
2940 C  CB    . VAL B 58  ? 0.2737 0.2289 0.2331 -0.0251 -0.0201 0.0208  38  VAL B CB    
2941 C  CG1   . VAL B 58  ? 0.2861 0.2404 0.2415 -0.0269 -0.0198 0.0226  38  VAL B CG1   
2942 C  CG2   . VAL B 58  ? 0.2664 0.2240 0.2233 -0.0260 -0.0158 0.0180  38  VAL B CG2   
2943 N  N     . VAL B 59  ? 0.2464 0.2032 0.2207 -0.0172 -0.0220 0.0220  39  VAL B N     
2944 C  CA    . VAL B 59  ? 0.2684 0.2231 0.2454 -0.0152 -0.0257 0.0231  39  VAL B CA    
2945 C  C     . VAL B 59  ? 0.2589 0.2098 0.2289 -0.0183 -0.0264 0.0255  39  VAL B C     
2946 O  O     . VAL B 59  ? 0.2541 0.2075 0.2226 -0.0193 -0.0218 0.0252  39  VAL B O     
2947 C  CB    . VAL B 59  ? 0.2556 0.2148 0.2408 -0.0111 -0.0231 0.0214  39  VAL B CB    
2948 C  CG1   . VAL B 59  ? 0.2775 0.2345 0.2653 -0.0087 -0.0271 0.0220  39  VAL B CG1   
2949 C  CG2   . VAL B 59  ? 0.2506 0.2144 0.2420 -0.0092 -0.0223 0.0193  39  VAL B CG2   
2950 N  N     . LYS B 60  ? 0.2751 0.2201 0.2409 -0.0200 -0.0326 0.0278  40  LYS B N     
2951 C  CA    . LYS B 60  ? 0.2821 0.2222 0.2404 -0.0239 -0.0348 0.0307  40  LYS B CA    
2952 C  C     . LYS B 60  ? 0.3275 0.2639 0.2892 -0.0210 -0.0389 0.0315  40  LYS B C     
2953 O  O     . LYS B 60  ? 0.2944 0.2329 0.2645 -0.0158 -0.0399 0.0294  40  LYS B O     
2954 C  CB    . LYS B 60  ? 0.2882 0.2228 0.2374 -0.0289 -0.0395 0.0332  40  LYS B CB    
2955 C  CG    . LYS B 60  ? 0.3388 0.2680 0.2899 -0.0269 -0.0474 0.0340  40  LYS B CG    
2956 C  CD    . LYS B 60  ? 0.3867 0.3094 0.3275 -0.0326 -0.0526 0.0371  40  LYS B CD    
2957 C  CE    . LYS B 60  ? 0.5063 0.4226 0.4491 -0.0302 -0.0616 0.0378  40  LYS B CE    
2958 N  NZ    . LYS B 60  ? 0.5964 0.5054 0.5287 -0.0358 -0.0676 0.0412  40  LYS B NZ    
2959 N  N     . ASP B 61  ? 0.2866 0.2178 0.2416 -0.0247 -0.0415 0.0344  41  ASP B N     
2960 C  CA    . ASP B 61  ? 0.3652 0.2916 0.3222 -0.0225 -0.0459 0.0353  41  ASP B CA    
2961 C  C     . ASP B 61  ? 0.3355 0.2679 0.3007 -0.0179 -0.0408 0.0326  41  ASP B C     
2962 O  O     . ASP B 61  ? 0.3531 0.2846 0.3245 -0.0131 -0.0437 0.0311  41  ASP B O     
2963 C  CB    . ASP B 61  ? 0.3949 0.3154 0.3548 -0.0191 -0.0542 0.0351  41  ASP B CB    
2964 C  CG    . ASP B 61  ? 0.4313 0.3442 0.3823 -0.0239 -0.0605 0.0383  41  ASP B CG    
2965 O  OD1   . ASP B 61  ? 0.4488 0.3569 0.3899 -0.0301 -0.0617 0.0418  41  ASP B OD1   
2966 O  OD2   . ASP B 61  ? 0.4527 0.3649 0.4063 -0.0218 -0.0642 0.0372  41  ASP B OD2   
2967 N  N     . VAL B 62  ? 0.3197 0.2583 0.2848 -0.0192 -0.0336 0.0318  42  VAL B N     
2968 C  CA    . VAL B 62  ? 0.2902 0.2347 0.2626 -0.0152 -0.0286 0.0294  42  VAL B CA    
2969 C  C     . VAL B 62  ? 0.3477 0.2893 0.3190 -0.0155 -0.0298 0.0307  42  VAL B C     
2970 O  O     . VAL B 62  ? 0.3488 0.2847 0.3127 -0.0199 -0.0334 0.0337  42  VAL B O     
2971 C  CB    . VAL B 62  ? 0.3582 0.3094 0.3309 -0.0162 -0.0214 0.0279  42  VAL B CB    
2972 C  CG1   . VAL B 62  ? 0.3465 0.2994 0.3199 -0.0159 -0.0209 0.0265  42  VAL B CG1   
2973 C  CG2   . VAL B 62  ? 0.4233 0.3748 0.3886 -0.0213 -0.0192 0.0294  42  VAL B CG2   
2974 N  N     . PRO B 63  ? 0.3300 0.2751 0.3078 -0.0115 -0.0272 0.0288  43  PRO B N     
2975 C  CA    . PRO B 63  ? 0.3931 0.3351 0.3698 -0.0118 -0.0287 0.0300  43  PRO B CA    
2976 C  C     . PRO B 63  ? 0.4588 0.4009 0.4285 -0.0175 -0.0264 0.0324  43  PRO B C     
2977 O  O     . PRO B 63  ? 0.3482 0.2956 0.3162 -0.0197 -0.0213 0.0319  43  PRO B O     
2978 C  CB    . PRO B 63  ? 0.4276 0.3754 0.4123 -0.0070 -0.0247 0.0271  43  PRO B CB    
2979 C  CG    . PRO B 63  ? 0.4210 0.3730 0.4114 -0.0037 -0.0237 0.0246  43  PRO B CG    
2980 C  CD    . PRO B 63  ? 0.3556 0.3074 0.3413 -0.0071 -0.0230 0.0257  43  PRO B CD    
2981 N  N     . ALA B 64  ? 0.4394 0.3757 0.4049 -0.0198 -0.0303 0.0347  44  ALA B N     
2982 C  CA    . ALA B 64  ? 0.3850 0.3217 0.3431 -0.0263 -0.0287 0.0373  44  ALA B CA    
2983 C  C     . ALA B 64  ? 0.3838 0.3296 0.3453 -0.0258 -0.0212 0.0354  44  ALA B C     
2984 O  O     . ALA B 64  ? 0.4472 0.3974 0.4042 -0.0306 -0.0178 0.0361  44  ALA B O     
2985 C  CB    . ALA B 64  ? 0.5539 0.4822 0.5073 -0.0288 -0.0348 0.0403  44  ALA B CB    
2986 N  N     . GLU B 65  ? 0.3602 0.3092 0.3294 -0.0203 -0.0187 0.0329  45  GLU B N     
2987 C  CA    . GLU B 65  ? 0.3538 0.3103 0.3263 -0.0195 -0.0125 0.0312  45  GLU B CA    
2988 C  C     . GLU B 65  ? 0.3090 0.2719 0.2830 -0.0190 -0.0075 0.0290  45  GLU B C     
2989 O  O     . GLU B 65  ? 0.3194 0.2883 0.2953 -0.0188 -0.0028 0.0275  45  GLU B O     
2990 C  CB    . GLU B 65  ? 0.4058 0.3631 0.3853 -0.0142 -0.0118 0.0295  45  GLU B CB    
2991 C  CG    . GLU B 65  ? 0.5625 0.5204 0.5478 -0.0093 -0.0121 0.0272  45  GLU B CG    
2992 C  CD    . GLU B 65  ? 0.7961 0.7482 0.7826 -0.0069 -0.0181 0.0273  45  GLU B CD    
2993 O  OE1   . GLU B 65  ? 0.5581 0.5035 0.5394 -0.0096 -0.0232 0.0296  45  GLU B OE1   
2994 O  OE2   . GLU B 65  ? 0.7953 0.7496 0.7879 -0.0024 -0.0180 0.0248  45  GLU B OE2   
2995 N  N     . PHE B 66  ? 0.2991 0.2606 0.2726 -0.0186 -0.0088 0.0286  46  PHE B N     
2996 C  CA    . PHE B 66  ? 0.2884 0.2551 0.2635 -0.0177 -0.0046 0.0262  46  PHE B CA    
2997 C  C     . PHE B 66  ? 0.2661 0.2378 0.2369 -0.0217 -0.0011 0.0256  46  PHE B C     
2998 O  O     . PHE B 66  ? 0.2882 0.2655 0.2622 -0.0199 0.0033  0.0230  46  PHE B O     
2999 C  CB    . PHE B 66  ? 0.2601 0.2240 0.2345 -0.0174 -0.0071 0.0261  46  PHE B CB    
3000 C  CG    . PHE B 66  ? 0.2660 0.2340 0.2402 -0.0175 -0.0035 0.0239  46  PHE B CG    
3001 C  CD1   . PHE B 66  ? 0.2373 0.2085 0.2172 -0.0137 -0.0003 0.0215  46  PHE B CD1   
3002 C  CD2   . PHE B 66  ? 0.3052 0.2735 0.2730 -0.0217 -0.0035 0.0242  46  PHE B CD2   
3003 C  CE1   . PHE B 66  ? 0.2247 0.1985 0.2042 -0.0137 0.0023  0.0192  46  PHE B CE1   
3004 C  CE2   . PHE B 66  ? 0.2976 0.2695 0.2652 -0.0216 -0.0005 0.0216  46  PHE B CE2   
3005 C  CZ    . PHE B 66  ? 0.2401 0.2143 0.2137 -0.0173 0.0022  0.0191  46  PHE B CZ    
3006 N  N     . ALA B 67  ? 0.2807 0.2506 0.2441 -0.0273 -0.0031 0.0279  47  ALA B N     
3007 C  CA    . ALA B 67  ? 0.2454 0.2218 0.2044 -0.0316 0.0005  0.0267  47  ALA B CA    
3008 C  C     . ALA B 67  ? 0.2907 0.2741 0.2532 -0.0308 0.0047  0.0248  47  ALA B C     
3009 O  O     . ALA B 67  ? 0.2820 0.2724 0.2470 -0.0294 0.0090  0.0213  47  ALA B O     
3010 C  CB    . ALA B 67  ? 0.3322 0.3056 0.2818 -0.0389 -0.0028 0.0300  47  ALA B CB    
3011 N  N     . GLU B 68  ? 0.2831 0.2644 0.2465 -0.0310 0.0032  0.0268  48  GLU B N     
3012 C  CA    . GLU B 68  ? 0.2943 0.2824 0.2612 -0.0304 0.0068  0.0251  48  GLU B CA    
3013 C  C     . GLU B 68  ? 0.2663 0.2571 0.2411 -0.0239 0.0098  0.0218  48  GLU B C     
3014 O  O     . GLU B 68  ? 0.2837 0.2818 0.2612 -0.0228 0.0135  0.0187  48  GLU B O     
3015 C  CB    . GLU B 68  ? 0.3506 0.3350 0.3166 -0.0320 0.0042  0.0280  48  GLU B CB    
3016 C  CG    . GLU B 68  ? 0.4401 0.4319 0.4095 -0.0319 0.0077  0.0265  48  GLU B CG    
3017 C  CD    . GLU B 68  ? 0.7831 0.7707 0.7515 -0.0335 0.0048  0.0294  48  GLU B CD    
3018 O  OE1   . GLU B 68  ? 0.7210 0.7008 0.6840 -0.0367 0.0000  0.0328  48  GLU B OE1   
3019 O  OE2   . GLU B 68  ? 0.7760 0.7678 0.7490 -0.0314 0.0069  0.0281  48  GLU B OE2   
3020 N  N     . LEU B 69  ? 0.2432 0.2285 0.2216 -0.0196 0.0078  0.0223  49  LEU B N     
3021 C  CA    . LEU B 69  ? 0.2274 0.2146 0.2121 -0.0144 0.0101  0.0197  49  LEU B CA    
3022 C  C     . LEU B 69  ? 0.2109 0.2017 0.1958 -0.0137 0.0126  0.0167  49  LEU B C     
3023 O  O     . LEU B 69  ? 0.2240 0.2189 0.2126 -0.0110 0.0152  0.0139  49  LEU B O     
3024 C  CB    . LEU B 69  ? 0.2311 0.2130 0.2190 -0.0110 0.0076  0.0206  49  LEU B CB    
3025 C  CG    . LEU B 69  ? 0.2599 0.2391 0.2497 -0.0098 0.0057  0.0222  49  LEU B CG    
3026 C  CD1   . LEU B 69  ? 0.2603 0.2357 0.2530 -0.0067 0.0032  0.0223  49  LEU B CD1   
3027 C  CD2   . LEU B 69  ? 0.2935 0.2766 0.2872 -0.0077 0.0085  0.0209  49  LEU B CD2   
3028 N  N     . ARG B 70  ? 0.2299 0.2189 0.2106 -0.0159 0.0114  0.0170  50  ARG B N     
3029 C  CA    . ARG B 70  ? 0.2130 0.2051 0.1935 -0.0153 0.0135  0.0138  50  ARG B CA    
3030 C  C     . ARG B 70  ? 0.2457 0.2459 0.2257 -0.0167 0.0169  0.0109  50  ARG B C     
3031 O  O     . ARG B 70  ? 0.2213 0.2252 0.2052 -0.0133 0.0191  0.0071  50  ARG B O     
3032 C  CB    . ARG B 70  ? 0.2178 0.2069 0.1931 -0.0183 0.0115  0.0148  50  ARG B CB    
3033 C  CG    . ARG B 70  ? 0.2408 0.2336 0.2145 -0.0184 0.0137  0.0112  50  ARG B CG    
3034 C  CD    . ARG B 70  ? 0.2407 0.2316 0.2076 -0.0228 0.0119  0.0123  50  ARG B CD    
3035 N  NE    . ARG B 70  ? 0.2445 0.2405 0.2094 -0.0234 0.0145  0.0082  50  ARG B NE    
3036 C  CZ    . ARG B 70  ? 0.2523 0.2560 0.2146 -0.0262 0.0174  0.0058  50  ARG B CZ    
3037 N  NH1   . ARG B 70  ? 0.2598 0.2668 0.2206 -0.0294 0.0179  0.0077  50  ARG B NH1   
3038 N  NH2   . ARG B 70  ? 0.2388 0.2477 0.2002 -0.0259 0.0197  0.0011  50  ARG B NH2   
3039 N  N     . HIS B 71  ? 0.2160 0.2190 0.1915 -0.0217 0.0169  0.0125  51  HIS B N     
3040 C  CA    . HIS B 71  ? 0.2341 0.2467 0.2090 -0.0239 0.0203  0.0094  51  HIS B CA    
3041 C  C     . HIS B 71  ? 0.2434 0.2601 0.2251 -0.0197 0.0222  0.0071  51  HIS B C     
3042 O  O     . HIS B 71  ? 0.2470 0.2710 0.2318 -0.0176 0.0249  0.0024  51  HIS B O     
3043 C  CB    . HIS B 71  ? 0.2461 0.2607 0.2144 -0.0310 0.0196  0.0123  51  HIS B CB    
3044 C  CG    . HIS B 71  ? 0.2604 0.2866 0.2272 -0.0346 0.0233  0.0090  51  HIS B CG    
3045 N  ND1   . HIS B 71  ? 0.3449 0.3752 0.3063 -0.0416 0.0234  0.0112  51  HIS B ND1   
3046 C  CD2   . HIS B 71  ? 0.2578 0.2930 0.2279 -0.0322 0.0269  0.0031  51  HIS B CD2   
3047 C  CE1   . HIS B 71  ? 0.3378 0.3804 0.2995 -0.0437 0.0274  0.0068  51  HIS B CE1   
3048 N  NE2   . HIS B 71  ? 0.2894 0.3354 0.2567 -0.0376 0.0295  0.0016  51  HIS B NE2   
3049 N  N     . ARG B 72  ? 0.2147 0.2268 0.1991 -0.0180 0.0205  0.0099  52  ARG B N     
3050 C  CA    . ARG B 72  ? 0.2323 0.2479 0.2226 -0.0143 0.0220  0.0081  52  ARG B CA    
3051 C  C     . ARG B 72  ? 0.2256 0.2398 0.2209 -0.0085 0.0224  0.0050  52  ARG B C     
3052 O  O     . ARG B 72  ? 0.2325 0.2522 0.2317 -0.0058 0.0240  0.0011  52  ARG B O     
3053 C  CB    . ARG B 72  ? 0.2573 0.2683 0.2487 -0.0142 0.0200  0.0118  52  ARG B CB    
3054 C  CG    . ARG B 72  ? 0.3222 0.3349 0.3087 -0.0202 0.0193  0.0145  52  ARG B CG    
3055 C  CD    . ARG B 72  ? 0.4775 0.4880 0.4655 -0.0202 0.0178  0.0169  52  ARG B CD    
3056 N  NE    . ARG B 72  ? 0.6078 0.6099 0.5977 -0.0167 0.0152  0.0189  52  ARG B NE    
3057 C  CZ    . ARG B 72  ? 0.7497 0.7510 0.7447 -0.0124 0.0155  0.0182  52  ARG B CZ    
3058 N  NH1   . ARG B 72  ? 0.7735 0.7809 0.7725 -0.0106 0.0178  0.0158  52  ARG B NH1   
3059 N  NH2   . ARG B 72  ? 0.5659 0.5608 0.5621 -0.0099 0.0132  0.0197  52  ARG B NH2   
3060 N  N     . LEU B 73  ? 0.2125 0.2193 0.2075 -0.0068 0.0204  0.0065  53  LEU B N     
3061 C  CA    . LEU B 73  ? 0.1978 0.2020 0.1969 -0.0020 0.0202  0.0044  53  LEU B CA    
3062 C  C     . LEU B 73  ? 0.2075 0.2152 0.2066 -0.0008 0.0214  -0.0002 53  LEU B C     
3063 O  O     . LEU B 73  ? 0.2061 0.2148 0.2090 0.0031  0.0216  -0.0035 53  LEU B O     
3064 C  CB    . LEU B 73  ? 0.1978 0.1944 0.1967 -0.0011 0.0180  0.0071  53  LEU B CB    
3065 C  CG    . LEU B 73  ? 0.1947 0.1881 0.1974 0.0029  0.0173  0.0059  53  LEU B CG    
3066 C  CD1   . LEU B 73  ? 0.2398 0.2341 0.2461 0.0049  0.0175  0.0063  53  LEU B CD1   
3067 C  CD2   . LEU B 73  ? 0.2055 0.1931 0.2077 0.0029  0.0155  0.0081  53  LEU B CD2   
3068 N  N     . LEU B 74  ? 0.2127 0.2218 0.2072 -0.0040 0.0219  -0.0007 54  LEU B N     
3069 C  CA    . LEU B 74  ? 0.2079 0.2213 0.2022 -0.0029 0.0232  -0.0057 54  LEU B CA    
3070 C  C     . LEU B 74  ? 0.2306 0.2540 0.2277 -0.0022 0.0257  -0.0100 54  LEU B C     
3071 O  O     . LEU B 74  ? 0.2360 0.2623 0.2365 0.0017  0.0262  -0.0152 54  LEU B O     
3072 C  CB    . LEU B 74  ? 0.2125 0.2257 0.2006 -0.0071 0.0232  -0.0052 54  LEU B CB    
3073 C  CG    . LEU B 74  ? 0.2125 0.2166 0.1987 -0.0072 0.0205  -0.0018 54  LEU B CG    
3074 C  CD1   . LEU B 74  ? 0.2316 0.2355 0.2117 -0.0112 0.0200  -0.0015 54  LEU B CD1   
3075 C  CD2   . LEU B 74  ? 0.2723 0.2716 0.2622 -0.0025 0.0193  -0.0038 54  LEU B CD2   
3076 N  N     . SER B 75  ? 0.2072 0.2355 0.2036 -0.0056 0.0269  -0.0080 55  SER B N     
3077 C  CA    . SER B 75  ? 0.2417 0.2804 0.2418 -0.0048 0.0292  -0.0121 55  SER B CA    
3078 C  C     . SER B 75  ? 0.2214 0.2582 0.2283 0.0014  0.0280  -0.0139 55  SER B C     
3079 O  O     . SER B 75  ? 0.2042 0.2477 0.2157 0.0049  0.0289  -0.0195 55  SER B O     
3080 C  CB    . SER B 75  ? 0.2443 0.2878 0.2419 -0.0102 0.0302  -0.0090 55  SER B CB    
3081 O  OG    . SER B 75  ? 0.2548 0.3011 0.2455 -0.0165 0.0311  -0.0078 55  SER B OG    
3082 N  N     . TYR B 76  ? 0.2099 0.2378 0.2177 0.0028  0.0258  -0.0094 56  TYR B N     
3083 C  CA    . TYR B 76  ? 0.2130 0.2379 0.2262 0.0079  0.0242  -0.0104 56  TYR B CA    
3084 C  C     . TYR B 76  ? 0.2186 0.2407 0.2338 0.0124  0.0229  -0.0147 56  TYR B C     
3085 O  O     . TYR B 76  ? 0.2235 0.2463 0.2434 0.0168  0.0216  -0.0177 56  TYR B O     
3086 C  CB    . TYR B 76  ? 0.2192 0.2353 0.2319 0.0079  0.0222  -0.0051 56  TYR B CB    
3087 C  CG    . TYR B 76  ? 0.2160 0.2342 0.2289 0.0056  0.0227  -0.0020 56  TYR B CG    
3088 C  CD1   . TYR B 76  ? 0.2283 0.2518 0.2454 0.0074  0.0231  -0.0037 56  TYR B CD1   
3089 C  CD2   . TYR B 76  ? 0.2401 0.2547 0.2493 0.0020  0.0221  0.0025  56  TYR B CD2   
3090 C  CE1   . TYR B 76  ? 0.2372 0.2623 0.2542 0.0050  0.0233  -0.0008 56  TYR B CE1   
3091 C  CE2   . TYR B 76  ? 0.2429 0.2583 0.2519 0.0000  0.0219  0.0052  56  TYR B CE2   
3092 C  CZ    . TYR B 76  ? 0.2623 0.2830 0.2750 0.0013  0.0227  0.0036  56  TYR B CZ    
3093 O  OH    . TYR B 76  ? 0.2649 0.2861 0.2771 -0.0011 0.0223  0.0063  56  TYR B OH    
3094 N  N     . SER B 77  ? 0.2041 0.2227 0.2157 0.0114  0.0225  -0.0150 57  SER B N     
3095 C  CA    . SER B 77  ? 0.2290 0.2442 0.2421 0.0156  0.0208  -0.0193 57  SER B CA    
3096 C  C     . SER B 77  ? 0.2488 0.2734 0.2658 0.0187  0.0219  -0.0264 57  SER B C     
3097 O  O     . SER B 77  ? 0.2216 0.2439 0.2426 0.0240  0.0195  -0.0302 57  SER B O     
3098 C  CB    . SER B 77  ? 0.2250 0.2360 0.2333 0.0135  0.0205  -0.0188 57  SER B CB    
3099 O  OG    . SER B 77  ? 0.2297 0.2349 0.2390 0.0173  0.0179  -0.0219 57  SER B OG    
3100 N  N     . SER B 78  ? 0.2102 0.2458 0.2261 0.0154  0.0253  -0.0285 58  SER B N     
3101 C  CA    . SER B 78  ? 0.2122 0.2594 0.2325 0.0180  0.0269  -0.0358 58  SER B CA    
3102 C  C     . SER B 78  ? 0.2373 0.2877 0.2638 0.0211  0.0262  -0.0365 58  SER B C     
3103 O  O     . SER B 78  ? 0.2440 0.2972 0.2762 0.0269  0.0246  -0.0423 58  SER B O     
3104 C  CB    . SER B 78  ? 0.2208 0.2799 0.2375 0.0123  0.0310  -0.0373 58  SER B CB    
3105 O  OG    . SER B 78  ? 0.2357 0.2946 0.2480 0.0110  0.0316  -0.0397 58  SER B OG    
3106 N  N     . TYR B 79  ? 0.2427 0.2924 0.2682 0.0178  0.0268  -0.0307 59  TYR B N     
3107 C  CA    . TYR B 79  ? 0.2202 0.2733 0.2513 0.0203  0.0261  -0.0313 59  TYR B CA    
3108 C  C     . TYR B 79  ? 0.2503 0.2938 0.2850 0.0265  0.0218  -0.0318 59  TYR B C     
3109 O  O     . TYR B 79  ? 0.2531 0.3003 0.2938 0.0315  0.0201  -0.0368 59  TYR B O     
3110 C  CB    . TYR B 79  ? 0.2038 0.2555 0.2325 0.0156  0.0268  -0.0246 59  TYR B CB    
3111 C  CG    . TYR B 79  ? 0.2294 0.2908 0.2550 0.0092  0.0302  -0.0237 59  TYR B CG    
3112 C  CD1   . TYR B 79  ? 0.2570 0.3328 0.2859 0.0084  0.0328  -0.0289 59  TYR B CD1   
3113 C  CD2   . TYR B 79  ? 0.2732 0.3292 0.2925 0.0036  0.0303  -0.0174 59  TYR B CD2   
3114 C  CE1   . TYR B 79  ? 0.2691 0.3536 0.2941 0.0013  0.0356  -0.0275 59  TYR B CE1   
3115 C  CE2   . TYR B 79  ? 0.2689 0.3322 0.2843 -0.0030 0.0325  -0.0159 59  TYR B CE2   
3116 C  CZ    . TYR B 79  ? 0.2572 0.3346 0.2752 -0.0045 0.0353  -0.0206 59  TYR B CZ    
3117 O  OH    . TYR B 79  ? 0.2830 0.3675 0.2962 -0.0121 0.0372  -0.0186 59  TYR B OH    
3118 N  N     . LEU B 80  ? 0.2325 0.2634 0.2634 0.0259  0.0196  -0.0269 60  LEU B N     
3119 C  CA    . LEU B 80  ? 0.2326 0.2530 0.2651 0.0303  0.0153  -0.0264 60  LEU B CA    
3120 C  C     . LEU B 80  ? 0.2800 0.3007 0.3157 0.0357  0.0129  -0.0334 60  LEU B C     
3121 O  O     . LEU B 80  ? 0.2774 0.2955 0.3174 0.0406  0.0093  -0.0359 60  LEU B O     
3122 C  CB    . LEU B 80  ? 0.2090 0.2182 0.2363 0.0277  0.0140  -0.0207 60  LEU B CB    
3123 C  CG    . LEU B 80  ? 0.2559 0.2534 0.2831 0.0305  0.0095  -0.0192 60  LEU B CG    
3124 C  CD1   . LEU B 80  ? 0.3006 0.2962 0.3303 0.0316  0.0077  -0.0167 60  LEU B CD1   
3125 C  CD2   . LEU B 80  ? 0.2370 0.2262 0.2591 0.0271  0.0090  -0.0145 60  LEU B CD2   
3126 N  N     . GLY B 81  ? 0.2557 0.2795 0.2892 0.0349  0.0145  -0.0369 61  GLY B N     
3127 C  CA    . GLY B 81  ? 0.2452 0.2680 0.2812 0.0403  0.0118  -0.0439 61  GLY B CA    
3128 C  C     . GLY B 81  ? 0.2721 0.3060 0.3153 0.0450  0.0118  -0.0514 61  GLY B C     
3129 O  O     . GLY B 81  ? 0.2894 0.3215 0.3359 0.0509  0.0084  -0.0578 61  GLY B O     
3130 N  N     . ASN B 82  ? 0.2540 0.2992 0.2996 0.0427  0.0153  -0.0511 62  ASN B N     
3131 C  CA    . ASN B 82  ? 0.2681 0.3264 0.3211 0.0467  0.0158  -0.0585 62  ASN B CA    
3132 C  C     . ASN B 82  ? 0.2928 0.3504 0.3506 0.0489  0.0135  -0.0565 62  ASN B C     
3133 O  O     . ASN B 82  ? 0.3220 0.3916 0.3865 0.0517  0.0141  -0.0621 62  ASN B O     
3134 C  CB    . ASN B 82  ? 0.2659 0.3406 0.3182 0.0417  0.0218  -0.0611 62  ASN B CB    
3135 C  CG    . ASN B 82  ? 0.2824 0.3611 0.3322 0.0417  0.0234  -0.0667 62  ASN B CG    
3136 O  OD1   . ASN B 82  ? 0.3574 0.4446 0.4124 0.0467  0.0230  -0.0757 62  ASN B OD1   
3137 N  ND2   . ASN B 82  ? 0.2841 0.3564 0.3262 0.0365  0.0249  -0.0616 62  ASN B ND2   
3138 N  N     . LEU B 83  ? 0.2941 0.3387 0.3488 0.0477  0.0109  -0.0491 63  LEU B N     
3139 C  CA    . LEU B 83  ? 0.3179 0.3600 0.3765 0.0504  0.0078  -0.0475 63  LEU B CA    
3140 C  C     . LEU B 83  ? 0.3110 0.3508 0.3756 0.0583  0.0023  -0.0543 63  LEU B C     
3141 O  O     . LEU B 83  ? 0.2835 0.3179 0.3473 0.0615  -0.0002 -0.0581 63  LEU B O     
3142 C  CB    . LEU B 83  ? 0.3360 0.3641 0.3895 0.0476  0.0057  -0.0388 63  LEU B CB    
3143 C  CG    . LEU B 83  ? 0.2895 0.3188 0.3381 0.0407  0.0099  -0.0321 63  LEU B CG    
3144 C  CD1   . LEU B 83  ? 0.3511 0.3678 0.3957 0.0389  0.0075  -0.0250 63  LEU B CD1   
3145 C  CD2   . LEU B 83  ? 0.3447 0.3868 0.3968 0.0387  0.0130  -0.0329 63  LEU B CD2   
3146 N  N     . PRO B 84  ? 0.3701 0.4138 0.4408 0.0619  -0.0001 -0.0563 64  PRO B N     
3147 C  CA    . PRO B 84  ? 0.4021 0.4419 0.4785 0.0700  -0.0066 -0.0625 64  PRO B CA    
3148 C  C     . PRO B 84  ? 0.3642 0.3842 0.4354 0.0713  -0.0127 -0.0584 64  PRO B C     
3149 O  O     . PRO B 84  ? 0.3974 0.4075 0.4624 0.0665  -0.0126 -0.0500 64  PRO B O     
3150 C  CB    . PRO B 84  ? 0.4872 0.5330 0.5697 0.0720  -0.0081 -0.0629 64  PRO B CB    
3151 C  CG    . PRO B 84  ? 0.4526 0.5126 0.5348 0.0657  -0.0008 -0.0608 64  PRO B CG    
3152 C  CD    . PRO B 84  ? 0.4671 0.5197 0.5402 0.0590  0.0027  -0.0537 64  PRO B CD    
3153 N  N     . LYS B 85  ? 0.3761 0.3906 0.4499 0.0778  -0.0183 -0.0646 65  LYS B N     
3154 C  CA    . LYS B 85  ? 0.4778 0.4732 0.5460 0.0784  -0.0245 -0.0610 65  LYS B CA    
3155 C  C     . LYS B 85  ? 0.5114 0.4949 0.5768 0.0769  -0.0289 -0.0535 65  LYS B C     
3156 O  O     . LYS B 85  ? 0.4551 0.4244 0.5134 0.0735  -0.0315 -0.0471 65  LYS B O     
3157 C  CB    . LYS B 85  ? 0.6202 0.6110 0.6921 0.0862  -0.0310 -0.0694 65  LYS B CB    
3158 C  CG    . LYS B 85  ? 0.7290 0.6999 0.7939 0.0858  -0.0372 -0.0658 65  LYS B CG    
3159 C  CD    . LYS B 85  ? 0.8584 0.8238 0.9267 0.0937  -0.0441 -0.0746 65  LYS B CD    
3160 C  CE    . LYS B 85  ? 0.8191 0.7665 0.8793 0.0918  -0.0488 -0.0712 65  LYS B CE    
3161 N  NZ    . LYS B 85  ? 0.7523 0.6832 0.8057 0.0874  -0.0535 -0.0614 65  LYS B NZ    
3162 N  N     . SER B 86  ? 0.4527 0.4423 0.5235 0.0790  -0.0299 -0.0543 66  SER B N     
3163 C  CA    . SER B 86  ? 0.4287 0.4082 0.4964 0.0770  -0.0336 -0.0471 66  SER B CA    
3164 C  C     . SER B 86  ? 0.5285 0.5051 0.5886 0.0687  -0.0286 -0.0381 66  SER B C     
3165 O  O     . SER B 86  ? 0.5339 0.4978 0.5881 0.0657  -0.0319 -0.0315 66  SER B O     
3166 C  CB    . SER B 86  ? 0.6016 0.5904 0.6766 0.0802  -0.0345 -0.0497 66  SER B CB    
3167 O  OG    . SER B 86  ? 0.5721 0.5782 0.6504 0.0773  -0.0266 -0.0510 66  SER B OG    
3168 N  N     . GLU B 87  ? 0.4529 0.4415 0.5131 0.0648  -0.0208 -0.0379 67  GLU B N     
3169 C  CA    . GLU B 87  ? 0.4208 0.4070 0.4744 0.0577  -0.0165 -0.0301 67  GLU B CA    
3170 C  C     . GLU B 87  ? 0.3884 0.3642 0.4355 0.0551  -0.0172 -0.0274 67  GLU B C     
3171 O  O     . GLU B 87  ? 0.4165 0.3834 0.4579 0.0509  -0.0179 -0.0208 67  GLU B O     
3172 C  CB    . GLU B 87  ? 0.5341 0.5349 0.5894 0.0542  -0.0091 -0.0307 67  GLU B CB    
3173 C  CG    . GLU B 87  ? 0.4649 0.4752 0.5250 0.0546  -0.0078 -0.0312 67  GLU B CG    
3174 C  CD    . GLU B 87  ? 0.6275 0.6301 0.6845 0.0521  -0.0097 -0.0245 67  GLU B CD    
3175 O  OE1   . GLU B 87  ? 0.7066 0.7021 0.7572 0.0475  -0.0084 -0.0185 67  GLU B OE1   
3176 O  OE2   . GLU B 87  ? 0.7898 0.7939 0.8508 0.0548  -0.0127 -0.0254 67  GLU B OE2   
3177 N  N     . LEU B 88  ? 0.3453 0.3227 0.3934 0.0575  -0.0171 -0.0327 68  LEU B N     
3178 C  CA    . LEU B 88  ? 0.3375 0.3060 0.3796 0.0548  -0.0175 -0.0304 68  LEU B CA    
3179 C  C     . LEU B 88  ? 0.3809 0.3331 0.4191 0.0556  -0.0249 -0.0275 68  LEU B C     
3180 O  O     . LEU B 88  ? 0.3627 0.3064 0.3947 0.0511  -0.0252 -0.0224 68  LEU B O     
3181 C  CB    . LEU B 88  ? 0.3151 0.2895 0.3591 0.0574  -0.0159 -0.0373 68  LEU B CB    
3182 C  CG    . LEU B 88  ? 0.3511 0.3409 0.3966 0.0546  -0.0084 -0.0390 68  LEU B CG    
3183 C  CD1   . LEU B 88  ? 0.3412 0.3371 0.3882 0.0570  -0.0070 -0.0463 68  LEU B CD1   
3184 C  CD2   . LEU B 88  ? 0.3103 0.2989 0.3500 0.0475  -0.0041 -0.0316 68  LEU B CD2   
3185 N  N     . ASP B 89  ? 0.4114 0.3590 0.4531 0.0610  -0.0312 -0.0308 69  ASP B N     
3186 C  CA    . ASP B 89  ? 0.4127 0.3436 0.4500 0.0613  -0.0392 -0.0278 69  ASP B CA    
3187 C  C     . ASP B 89  ? 0.4209 0.3454 0.4520 0.0548  -0.0389 -0.0189 69  ASP B C     
3188 O  O     . ASP B 89  ? 0.5008 0.4127 0.5254 0.0515  -0.0429 -0.0144 69  ASP B O     
3189 C  CB    . ASP B 89  ? 0.4701 0.3976 0.5126 0.0684  -0.0464 -0.0328 69  ASP B CB    
3190 C  CG    . ASP B 89  ? 0.5142 0.4453 0.5623 0.0755  -0.0486 -0.0424 69  ASP B CG    
3191 O  OD1   . ASP B 89  ? 0.5950 0.5281 0.6414 0.0745  -0.0455 -0.0446 69  ASP B OD1   
3192 O  OD2   . ASP B 89  ? 0.6207 0.5530 0.6751 0.0823  -0.0536 -0.0482 69  ASP B OD2   
3193 N  N     . ARG B 90  ? 0.3953 0.3289 0.4282 0.0527  -0.0341 -0.0163 70  ARG B N     
3194 C  CA    . ARG B 90  ? 0.4525 0.3820 0.4801 0.0468  -0.0332 -0.0087 70  ARG B CA    
3195 C  C     . ARG B 90  ? 0.4021 0.3305 0.4241 0.0407  -0.0291 -0.0044 70  ARG B C     
3196 O  O     . ARG B 90  ? 0.4397 0.3633 0.4566 0.0357  -0.0292 0.0015  70  ARG B O     
3197 C  CB    . ARG B 90  ? 0.5362 0.4769 0.5673 0.0460  -0.0284 -0.0078 70  ARG B CB    
3198 C  CG    . ARG B 90  ? 0.6639 0.6097 0.7017 0.0516  -0.0309 -0.0124 70  ARG B CG    
3199 C  CD    . ARG B 90  ? 0.6680 0.6236 0.7079 0.0495  -0.0263 -0.0103 70  ARG B CD    
3200 N  NE    . ARG B 90  ? 0.9119 0.8749 0.9592 0.0545  -0.0279 -0.0151 70  ARG B NE    
3201 C  CZ    . ARG B 90  ? 0.9463 0.9043 0.9949 0.0571  -0.0337 -0.0147 70  ARG B CZ    
3202 N  NH1   . ARG B 90  ? 0.8773 0.8223 0.9197 0.0547  -0.0385 -0.0094 70  ARG B NH1   
3203 N  NH2   . ARG B 90  ? 1.0766 1.0433 1.1328 0.0619  -0.0347 -0.0198 70  ARG B NH2   
3204 N  N     . LEU B 91  ? 0.3526 0.2858 0.3757 0.0412  -0.0256 -0.0076 71  LEU B N     
3205 C  CA    . LEU B 91  ? 0.3575 0.2912 0.3763 0.0359  -0.0216 -0.0042 71  LEU B CA    
3206 C  C     . LEU B 91  ? 0.4249 0.3482 0.4393 0.0349  -0.0255 -0.0039 71  LEU B C     
3207 O  O     . LEU B 91  ? 0.3788 0.3027 0.3901 0.0309  -0.0225 -0.0018 71  LEU B O     
3208 C  CB    . LEU B 91  ? 0.3379 0.2838 0.3599 0.0362  -0.0152 -0.0072 71  LEU B CB    
3209 C  CG    . LEU B 91  ? 0.3324 0.2890 0.3583 0.0364  -0.0111 -0.0074 71  LEU B CG    
3210 C  CD1   . LEU B 91  ? 0.3325 0.2999 0.3602 0.0358  -0.0056 -0.0101 71  LEU B CD1   
3211 C  CD2   . LEU B 91  ? 0.3633 0.3188 0.3864 0.0322  -0.0098 -0.0013 71  LEU B CD2   
3212 N  N     . GLU B 92  ? 0.3685 0.2820 0.3825 0.0383  -0.0325 -0.0061 72  GLU B N     
3213 C  CA    . GLU B 92  ? 0.3619 0.2644 0.3714 0.0372  -0.0369 -0.0059 72  GLU B CA    
3214 C  C     . GLU B 92  ? 0.4696 0.3617 0.4719 0.0310  -0.0403 0.0012  72  GLU B C     
3215 O  O     . GLU B 92  ? 0.4984 0.3872 0.4995 0.0300  -0.0428 0.0044  72  GLU B O     
3216 C  CB    . GLU B 92  ? 0.4579 0.3535 0.4698 0.0438  -0.0437 -0.0120 72  GLU B CB    
3217 C  CG    . GLU B 92  ? 0.6565 0.5626 0.6747 0.0493  -0.0404 -0.0199 72  GLU B CG    
3218 C  CD    . GLU B 92  ? 0.8402 0.7386 0.8602 0.0557  -0.0474 -0.0265 72  GLU B CD    
3219 O  OE1   . GLU B 92  ? 0.7507 0.6339 0.7659 0.0550  -0.0550 -0.0243 72  GLU B OE1   
3220 O  OE2   . GLU B 92  ? 0.8170 0.7248 0.8429 0.0611  -0.0455 -0.0341 72  GLU B OE2   
3221 N  N     . ASN B 93  ? 0.4001 0.2876 0.3976 0.0265  -0.0403 0.0036  73  ASN B N     
3222 C  CA    . ASN B 93  ? 0.4156 0.2940 0.4058 0.0197  -0.0434 0.0101  73  ASN B CA    
3223 C  C     . ASN B 93  ? 0.3750 0.2427 0.3609 0.0183  -0.0483 0.0096  73  ASN B C     
3224 O  O     . ASN B 93  ? 0.3584 0.2293 0.3431 0.0153  -0.0448 0.0099  73  ASN B O     
3225 C  CB    . ASN B 93  ? 0.4094 0.2966 0.3983 0.0136  -0.0368 0.0146  73  ASN B CB    
3226 C  CG    . ASN B 93  ? 0.5087 0.3888 0.4903 0.0061  -0.0395 0.0210  73  ASN B CG    
3227 O  OD1   . ASN B 93  ? 0.4761 0.3440 0.4524 0.0039  -0.0460 0.0226  73  ASN B OD1   
3228 N  ND2   . ASN B 93  ? 0.4876 0.3757 0.4688 0.0019  -0.0348 0.0245  73  ASN B ND2   
3229 N  N     . GLU B 94  ? 0.4217 0.2761 0.4052 0.0207  -0.0568 0.0087  74  GLU B N     
3230 C  CA    . GLU B 94  ? 0.3994 0.2413 0.3780 0.0194  -0.0628 0.0082  74  GLU B CA    
3231 C  C     . GLU B 94  ? 0.4069 0.2431 0.3774 0.0098  -0.0636 0.0154  74  GLU B C     
3232 O  O     . GLU B 94  ? 0.4167 0.2492 0.3841 0.0068  -0.0644 0.0157  74  GLU B O     
3233 C  CB    . GLU B 94  ? 0.4702 0.2983 0.4483 0.0247  -0.0728 0.0054  74  GLU B CB    
3234 C  CG    . GLU B 94  ? 0.5916 0.4048 0.5646 0.0242  -0.0804 0.0043  74  GLU B CG    
3235 C  CD    . GLU B 94  ? 0.6908 0.4889 0.6629 0.0294  -0.0915 0.0018  74  GLU B CD    
3236 O  OE1   . GLU B 94  ? 0.6558 0.4555 0.6312 0.0332  -0.0930 0.0011  74  GLU B OE1   
3237 O  OE2   . GLU B 94  ? 0.7830 0.5670 0.7508 0.0298  -0.0991 0.0005  74  GLU B OE2   
3238 N  N     . LYS B 95  ? 0.4397 0.2763 0.4069 0.0046  -0.0633 0.0212  75  LYS B N     
3239 C  CA    . LYS B 95  ? 0.5309 0.3645 0.4906 -0.0052 -0.0635 0.0278  75  LYS B CA    
3240 C  C     . LYS B 95  ? 0.4617 0.3075 0.4233 -0.0086 -0.0555 0.0280  75  LYS B C     
3241 O  O     . LYS B 95  ? 0.4668 0.3096 0.4233 -0.0153 -0.0563 0.0311  75  LYS B O     
3242 C  CB    . LYS B 95  ? 0.6222 0.4564 0.5785 -0.0099 -0.0637 0.0331  75  LYS B CB    
3243 C  CG    . LYS B 95  ? 0.7374 0.5687 0.6852 -0.0207 -0.0644 0.0398  75  LYS B CG    
3244 C  CD    . LYS B 95  ? 0.9273 0.7558 0.8700 -0.0255 -0.0669 0.0448  75  LYS B CD    
3245 C  CE    . LYS B 95  ? 0.9027 0.7474 0.8483 -0.0280 -0.0581 0.0461  75  LYS B CE    
3246 N  NZ    . LYS B 95  ? 0.7834 0.6370 0.7275 -0.0349 -0.0526 0.0480  75  LYS B NZ    
3247 N  N     . ALA B 96  ? 0.4499 0.3092 0.4186 -0.0042 -0.0482 0.0246  76  ALA B N     
3248 C  CA    . ALA B 96  ? 0.4366 0.3071 0.4077 -0.0062 -0.0412 0.0241  76  ALA B CA    
3249 C  C     . ALA B 96  ? 0.4271 0.2956 0.3996 -0.0031 -0.0418 0.0198  76  ALA B C     
3250 O  O     . ALA B 96  ? 0.4150 0.2928 0.3901 -0.0037 -0.0363 0.0187  76  ALA B O     
3251 C  CB    . ALA B 96  ? 0.3656 0.2500 0.3430 -0.0031 -0.0341 0.0226  76  ALA B CB    
3252 N  N     . LYS B 97  ? 0.4212 0.2777 0.3919 0.0002  -0.0487 0.0172  77  LYS B N     
3253 C  CA    . LYS B 97  ? 0.4060 0.2601 0.3779 0.0038  -0.0497 0.0122  77  LYS B CA    
3254 C  C     . LYS B 97  ? 0.3461 0.2125 0.3251 0.0102  -0.0437 0.0066  77  LYS B C     
3255 O  O     . LYS B 97  ? 0.3711 0.2414 0.3514 0.0113  -0.0412 0.0034  77  LYS B O     
3256 C  CB    . LYS B 97  ? 0.4452 0.2986 0.4131 -0.0025 -0.0489 0.0147  77  LYS B CB    
3257 C  CG    . LYS B 97  ? 0.5908 0.4346 0.5511 -0.0107 -0.0538 0.0209  77  LYS B CG    
3258 C  CD    . LYS B 97  ? 0.6765 0.5034 0.6321 -0.0095 -0.0633 0.0211  77  LYS B CD    
3259 C  CE    . LYS B 97  ? 0.8934 0.7108 0.8403 -0.0191 -0.0682 0.0281  77  LYS B CE    
3260 N  NZ    . LYS B 97  ? 0.8247 0.6249 0.7662 -0.0187 -0.0782 0.0294  77  LYS B NZ    
3261 N  N     . TYR B 98  ? 0.3626 0.2355 0.3460 0.0137  -0.0414 0.0057  78  TYR B N     
3262 C  CA    . TYR B 98  ? 0.3356 0.2211 0.3255 0.0187  -0.0355 0.0011  78  TYR B CA    
3263 C  C     . TYR B 98  ? 0.3491 0.2455 0.3398 0.0151  -0.0283 0.0028  78  TYR B C     
3264 O  O     . TYR B 98  ? 0.3495 0.2550 0.3439 0.0180  -0.0239 -0.0009 78  TYR B O     
3265 C  CB    . TYR B 98  ? 0.3579 0.2417 0.3504 0.0251  -0.0378 -0.0063 78  TYR B CB    
3266 C  CG    . TYR B 98  ? 0.3576 0.2300 0.3498 0.0294  -0.0459 -0.0087 78  TYR B CG    
3267 C  CD1   . TYR B 98  ? 0.3753 0.2494 0.3713 0.0335  -0.0472 -0.0099 78  TYR B CD1   
3268 C  CD2   . TYR B 98  ? 0.4842 0.3431 0.4720 0.0294  -0.0529 -0.0097 78  TYR B CD2   
3269 C  CE1   . TYR B 98  ? 0.3734 0.2364 0.3693 0.0378  -0.0555 -0.0122 78  TYR B CE1   
3270 C  CE2   . TYR B 98  ? 0.4789 0.3258 0.4662 0.0337  -0.0613 -0.0120 78  TYR B CE2   
3271 C  CZ    . TYR B 98  ? 0.4637 0.3126 0.4551 0.0380  -0.0627 -0.0132 78  TYR B CZ    
3272 O  OH    . TYR B 98  ? 0.5140 0.3506 0.5052 0.0426  -0.0719 -0.0157 78  TYR B OH    
3273 N  N     . LEU B 99  ? 0.3180 0.2142 0.3053 0.0088  -0.0273 0.0082  79  LEU B N     
3274 C  CA    . LEU B 99  ? 0.3132 0.2194 0.3016 0.0057  -0.0213 0.0098  79  LEU B CA    
3275 C  C     . LEU B 99  ? 0.3031 0.2173 0.2940 0.0049  -0.0174 0.0123  79  LEU B C     
3276 O  O     . LEU B 99  ? 0.3017 0.2233 0.2933 0.0019  -0.0133 0.0144  79  LEU B O     
3277 C  CB    . LEU B 99  ? 0.3021 0.2050 0.2863 -0.0005 -0.0224 0.0132  79  LEU B CB    
3278 C  CG    . LEU B 99  ? 0.3199 0.2159 0.3019 0.0003  -0.0256 0.0104  79  LEU B CG    
3279 C  CD1   . LEU B 99  ? 0.3584 0.2510 0.3361 -0.0064 -0.0271 0.0141  79  LEU B CD1   
3280 C  CD2   . LEU B 99  ? 0.3346 0.2381 0.3199 0.0040  -0.0218 0.0059  79  LEU B CD2   
3281 N  N     . THR B 100 ? 0.3213 0.2338 0.3135 0.0077  -0.0191 0.0119  80  THR B N     
3282 C  CA    . THR B 100 ? 0.2998 0.2199 0.2949 0.0085  -0.0156 0.0130  80  THR B CA    
3283 C  C     . THR B 100 ? 0.2636 0.1847 0.2626 0.0146  -0.0165 0.0088  80  THR B C     
3284 O  O     . THR B 100 ? 0.3153 0.2285 0.3137 0.0173  -0.0216 0.0068  80  THR B O     
3285 C  CB    . THR B 100 ? 0.3610 0.2779 0.3530 0.0045  -0.0173 0.0176  80  THR B CB    
3286 O  OG1   . THR B 100 ? 0.3534 0.2729 0.3429 -0.0012 -0.0153 0.0209  80  THR B OG1   
3287 C  CG2   . THR B 100 ? 0.3699 0.2931 0.3650 0.0063  -0.0148 0.0179  80  THR B CG2   
3288 N  N     . GLY B 101 ? 0.2773 0.2083 0.2804 0.0166  -0.0119 0.0070  81  GLY B N     
3289 C  CA    . GLY B 101 ? 0.2822 0.2163 0.2894 0.0218  -0.0122 0.0029  81  GLY B CA    
3290 C  C     . GLY B 101 ? 0.2593 0.1952 0.2686 0.0255  -0.0122 -0.0028 81  GLY B C     
3291 O  O     . GLY B 101 ? 0.2705 0.2076 0.2782 0.0239  -0.0105 -0.0034 81  GLY B O     
3292 N  N     . TRP B 102 ? 0.2707 0.2072 0.2835 0.0306  -0.0144 -0.0072 82  TRP B N     
3293 C  CA    A TRP B 102 ? 0.2741 0.2154 0.2900 0.0348  -0.0138 -0.0138 82  TRP B CA    
3294 C  CA    B TRP B 102 ? 0.2748 0.2161 0.2907 0.0348  -0.0138 -0.0139 82  TRP B CA    
3295 C  C     . TRP B 102 ? 0.2821 0.2134 0.2971 0.0382  -0.0200 -0.0174 82  TRP B C     
3296 O  O     . TRP B 102 ? 0.3427 0.2641 0.3564 0.0391  -0.0256 -0.0158 82  TRP B O     
3297 C  CB    A TRP B 102 ? 0.3101 0.2614 0.3317 0.0385  -0.0117 -0.0177 82  TRP B CB    
3298 C  CB    B TRP B 102 ? 0.3087 0.2596 0.3303 0.0387  -0.0120 -0.0177 82  TRP B CB    
3299 C  CG    A TRP B 102 ? 0.2434 0.2048 0.2678 0.0405  -0.0082 -0.0237 82  TRP B CG    
3300 C  CG    B TRP B 102 ? 0.2759 0.2323 0.3013 0.0435  -0.0121 -0.0255 82  TRP B CG    
3301 C  CD1   A TRP B 102 ? 0.2728 0.2435 0.2965 0.0373  -0.0025 -0.0232 82  TRP B CD1   
3302 C  CD1   B TRP B 102 ? 0.2886 0.2412 0.3172 0.0494  -0.0172 -0.0310 82  TRP B CD1   
3303 C  CD2   A TRP B 102 ? 0.2700 0.2331 0.2977 0.0460  -0.0105 -0.0314 82  TRP B CD2   
3304 C  CD2   B TRP B 102 ? 0.2358 0.2029 0.2622 0.0429  -0.0071 -0.0291 82  TRP B CD2   
3305 N  NE1   A TRP B 102 ? 0.2859 0.2646 0.3119 0.0397  -0.0007 -0.0297 82  TRP B NE1   
3306 N  NE1   B TRP B 102 ? 0.2762 0.2377 0.3083 0.0528  -0.0153 -0.0384 82  TRP B NE1   
3307 C  CE2   A TRP B 102 ? 0.2375 0.2124 0.2663 0.0453  -0.0053 -0.0352 82  TRP B CE2   
3308 C  CE2   B TRP B 102 ? 0.2631 0.2338 0.2935 0.0485  -0.0089 -0.0372 82  TRP B CE2   
3309 C  CE3   A TRP B 102 ? 0.2838 0.2396 0.3136 0.0515  -0.0168 -0.0356 82  TRP B CE3   
3310 C  CE3   B TRP B 102 ? 0.2766 0.2505 0.3007 0.0382  -0.0016 -0.0265 82  TRP B CE3   
3311 C  CZ2   A TRP B 102 ? 0.2652 0.2462 0.2974 0.0498  -0.0056 -0.0435 82  TRP B CZ2   
3312 C  CZ2   B TRP B 102 ? 0.2653 0.2471 0.2971 0.0488  -0.0047 -0.0426 82  TRP B CZ2   
3313 C  CZ3   A TRP B 102 ? 0.2803 0.2414 0.3140 0.0567  -0.0175 -0.0441 82  TRP B CZ3   
3314 C  CZ3   B TRP B 102 ? 0.3038 0.2874 0.3287 0.0382  0.0019  -0.0312 82  TRP B CZ3   
3315 C  CH2   A TRP B 102 ? 0.3058 0.2801 0.3408 0.0558  -0.0115 -0.0482 82  TRP B CH2   
3316 C  CH2   B TRP B 102 ? 0.2696 0.2576 0.2981 0.0433  0.0007  -0.0392 82  TRP B CH2   
3317 N  N     . SER B 103 ? 0.2839 0.2172 0.2991 0.0399  -0.0193 -0.0222 83  SER B N     
3318 C  CA    . SER B 103 ? 0.2902 0.2150 0.3053 0.0443  -0.0253 -0.0272 83  SER B CA    
3319 C  C     . SER B 103 ? 0.3316 0.2644 0.3492 0.0476  -0.0228 -0.0346 83  SER B C     
3320 O  O     . SER B 103 ? 0.3020 0.2445 0.3192 0.0447  -0.0168 -0.0345 83  SER B O     
3321 C  CB    . SER B 103 ? 0.3549 0.2659 0.3637 0.0407  -0.0298 -0.0231 83  SER B CB    
3322 O  OG    . SER B 103 ? 0.3650 0.2790 0.3707 0.0364  -0.0258 -0.0215 83  SER B OG    
3323 N  N     . LEU B 104 ? 0.3327 0.2611 0.3525 0.0535  -0.0278 -0.0413 84  LEU B N     
3324 C  CA    . LEU B 104 ? 0.3223 0.2577 0.3442 0.0570  -0.0263 -0.0494 84  LEU B CA    
3325 C  C     . LEU B 104 ? 0.4058 0.3292 0.4225 0.0562  -0.0305 -0.0498 84  LEU B C     
3326 O  O     . LEU B 104 ? 0.4506 0.3597 0.4651 0.0575  -0.0378 -0.0486 84  LEU B O     
3327 C  CB    . LEU B 104 ? 0.3307 0.2712 0.3596 0.0648  -0.0290 -0.0579 84  LEU B CB    
3328 C  CG    . LEU B 104 ? 0.5048 0.4579 0.5376 0.0689  -0.0259 -0.0676 84  LEU B CG    
3329 C  CD1   . LEU B 104 ? 0.3870 0.3562 0.4201 0.0642  -0.0169 -0.0663 84  LEU B CD1   
3330 C  CD2   . LEU B 104 ? 0.4485 0.4055 0.4891 0.0772  -0.0298 -0.0759 84  LEU B CD2   
3331 N  N     . GLY B 105 ? 0.3436 0.2724 0.3579 0.0537  -0.0264 -0.0513 85  GLY B N     
3332 C  CA    . GLY B 105 ? 0.3951 0.3140 0.4044 0.0524  -0.0298 -0.0518 85  GLY B CA    
3333 C  C     . GLY B 105 ? 0.3844 0.3115 0.3944 0.0548  -0.0270 -0.0597 85  GLY B C     
3334 O  O     . GLY B 105 ? 0.4456 0.3872 0.4597 0.0567  -0.0221 -0.0644 85  GLY B O     
3335 N  N     . LYS B 106 ? 0.4570 0.3751 0.4625 0.0541  -0.0304 -0.0610 86  LYS B N     
3336 C  CA    . LYS B 106 ? 0.4912 0.4150 0.4964 0.0565  -0.0290 -0.0690 86  LYS B CA    
3337 C  C     . LYS B 106 ? 0.6519 0.5711 0.6505 0.0507  -0.0281 -0.0653 86  LYS B C     
3338 O  O     . LYS B 106 ? 0.6110 0.5184 0.6054 0.0466  -0.0313 -0.0584 86  LYS B O     
3339 C  CB    . LYS B 106 ? 0.5010 0.4175 0.5087 0.0643  -0.0361 -0.0778 86  LYS B CB    
3340 C  CG    . LYS B 106 ? 0.5970 0.5222 0.6059 0.0681  -0.0343 -0.0879 86  LYS B CG    
3341 C  CD    . LYS B 106 ? 0.5486 0.4637 0.5594 0.0759  -0.0426 -0.0963 86  LYS B CD    
3342 C  CE    . LYS B 106 ? 0.5337 0.4618 0.5483 0.0815  -0.0402 -0.1085 86  LYS B CE    
3343 N  NZ    . LYS B 106 ? 0.5703 0.4885 0.5874 0.0900  -0.0489 -0.1176 86  LYS B NZ    
3344 N  N     . GLU B 107 ? 0.6798 0.6090 0.6774 0.0500  -0.0235 -0.0698 87  GLU B N     
3345 C  CA    . GLU B 107 ? 0.7171 0.6431 0.7086 0.0454  -0.0228 -0.0681 87  GLU B CA    
3346 C  C     . GLU B 107 ? 0.8025 0.7291 0.7936 0.0500  -0.0248 -0.0780 87  GLU B C     
3347 O  O     . GLU B 107 ? 0.7103 0.6490 0.7053 0.0541  -0.0219 -0.0858 87  GLU B O     
3348 C  CB    . GLU B 107 ? 0.6485 0.5859 0.6380 0.0393  -0.0156 -0.0635 87  GLU B CB    
3349 C  CG    . GLU B 107 ? 0.6593 0.5938 0.6479 0.0340  -0.0144 -0.0534 87  GLU B CG    
3350 C  CD    . GLU B 107 ? 0.6398 0.5856 0.6273 0.0290  -0.0080 -0.0497 87  GLU B CD    
3351 O  OE1   . GLU B 107 ? 0.6543 0.6082 0.6398 0.0282  -0.0048 -0.0538 87  GLU B OE1   
3352 O  OE2   . GLU B 107 ? 0.5604 0.5065 0.5485 0.0258  -0.0065 -0.0428 87  GLU B OE2   
3353 N  N     . THR B 108 ? 0.8326 0.7469 0.8189 0.0491  -0.0297 -0.0781 88  THR B N     
3354 C  CA    . THR B 108 ? 0.9468 0.8599 0.9323 0.0538  -0.0325 -0.0879 88  THR B CA    
3355 C  C     . THR B 108 ? 0.8722 0.7858 0.8514 0.0489  -0.0304 -0.0874 88  THR B C     
3356 O  O     . THR B 108 ? 0.9140 0.8255 0.8894 0.0420  -0.0285 -0.0790 88  THR B O     
3357 C  CB    . THR B 108 ? 1.0459 0.9416 1.0313 0.0586  -0.0421 -0.0904 88  THR B CB    
3358 O  OG1   . THR B 108 ? 1.0607 0.9424 1.0412 0.0528  -0.0458 -0.0808 88  THR B OG1   
3359 C  CG2   . THR B 108 ? 0.7818 0.6781 0.7739 0.0653  -0.0449 -0.0939 88  THR B CG2   
3360 N  N     . ASN B 116 ? 0.6064 0.5836 0.6111 0.0567  -0.0090 -0.0955 96  ASN B N     
3361 C  CA    . ASN B 116 ? 0.6055 0.5904 0.6115 0.0524  -0.0042 -0.0887 96  ASN B CA    
3362 C  C     . ASN B 116 ? 0.5389 0.5166 0.5496 0.0556  -0.0080 -0.0852 96  ASN B C     
3363 O  O     . ASN B 116 ? 0.5931 0.5554 0.6022 0.0563  -0.0138 -0.0813 96  ASN B O     
3364 C  CB    . ASN B 116 ? 0.6405 0.6218 0.6400 0.0443  -0.0016 -0.0790 96  ASN B CB    
3365 C  CG    . ASN B 116 ? 0.8620 0.8542 0.8570 0.0396  0.0037  -0.0808 96  ASN B CG    
3366 O  OD1   . ASN B 116 ? 0.8917 0.8971 0.8885 0.0412  0.0070  -0.0884 96  ASN B OD1   
3367 N  ND2   . ASN B 116 ? 0.8284 0.8152 0.8173 0.0335  0.0042  -0.0740 96  ASN B ND2   
3368 N  N     . LEU B 117 ? 0.4594 0.4482 0.4755 0.0570  -0.0050 -0.0862 97  LEU B N     
3369 C  CA    . LEU B 117 ? 0.4161 0.3994 0.4362 0.0589  -0.0078 -0.0818 97  LEU B CA    
3370 C  C     . LEU B 117 ? 0.3836 0.3686 0.4010 0.0518  -0.0036 -0.0718 97  LEU B C     
3371 O  O     . LEU B 117 ? 0.3859 0.3832 0.4023 0.0478  0.0024  -0.0712 97  LEU B O     
3372 C  CB    . LEU B 117 ? 0.4522 0.4464 0.4804 0.0651  -0.0077 -0.0894 97  LEU B CB    
3373 C  CG    . LEU B 117 ? 0.5422 0.5291 0.5744 0.0681  -0.0120 -0.0860 97  LEU B CG    
3374 C  CD1   . LEU B 117 ? 0.6035 0.5720 0.6344 0.0722  -0.0207 -0.0864 97  LEU B CD1   
3375 C  CD2   . LEU B 117 ? 0.5950 0.5956 0.6357 0.0733  -0.0109 -0.0931 97  LEU B CD2   
3376 N  N     . LYS B 118 ? 0.3588 0.3317 0.3748 0.0503  -0.0069 -0.0643 98  LYS B N     
3377 C  CA    . LYS B 118 ? 0.3645 0.3373 0.3774 0.0438  -0.0036 -0.0551 98  LYS B CA    
3378 C  C     . LYS B 118 ? 0.3979 0.3659 0.4136 0.0446  -0.0058 -0.0503 98  LYS B C     
3379 O  O     . LYS B 118 ? 0.4095 0.3655 0.4249 0.0468  -0.0115 -0.0491 98  LYS B O     
3380 C  CB    . LYS B 118 ? 0.4517 0.4145 0.4584 0.0394  -0.0050 -0.0500 98  LYS B CB    
3381 C  CG    . LYS B 118 ? 0.5203 0.4817 0.5243 0.0334  -0.0028 -0.0410 98  LYS B CG    
3382 C  CD    . LYS B 118 ? 0.5228 0.4709 0.5233 0.0311  -0.0070 -0.0357 98  LYS B CD    
3383 C  CE    . LYS B 118 ? 0.5760 0.5166 0.5733 0.0321  -0.0105 -0.0393 98  LYS B CE    
3384 N  NZ    . LYS B 118 ? 0.6142 0.5439 0.6074 0.0279  -0.0137 -0.0334 98  LYS B NZ    
3385 N  N     . GLY B 119 ? 0.3118 0.2886 0.3295 0.0424  -0.0016 -0.0472 99  GLY B N     
3386 C  CA    . GLY B 119 ? 0.3106 0.2828 0.3295 0.0417  -0.0031 -0.0413 99  GLY B CA    
3387 C  C     . GLY B 119 ? 0.3417 0.3093 0.3558 0.0355  -0.0016 -0.0332 99  GLY B C     
3388 O  O     . GLY B 119 ? 0.2911 0.2648 0.3028 0.0316  0.0026  -0.0316 99  GLY B O     
3389 N  N     . SER B 120 ? 0.2623 0.2192 0.2747 0.0346  -0.0053 -0.0284 100 SER B N     
3390 C  CA    . SER B 120 ? 0.2460 0.1995 0.2547 0.0292  -0.0041 -0.0213 100 SER B CA    
3391 C  C     . SER B 120 ? 0.2687 0.2222 0.2789 0.0281  -0.0038 -0.0166 100 SER B C     
3392 O  O     . SER B 120 ? 0.2591 0.2083 0.2712 0.0309  -0.0072 -0.0171 100 SER B O     
3393 C  CB    . SER B 120 ? 0.2818 0.2236 0.2865 0.0276  -0.0083 -0.0192 100 SER B CB    
3394 O  OG    . SER B 120 ? 0.3336 0.2744 0.3367 0.0286  -0.0091 -0.0236 100 SER B OG    
3395 N  N     . TYR B 121 ? 0.2266 0.1844 0.2358 0.0240  -0.0002 -0.0121 101 TYR B N     
3396 C  CA    . TYR B 121 ? 0.2303 0.1878 0.2402 0.0225  0.0001  -0.0074 101 TYR B CA    
3397 C  C     . TYR B 121 ? 0.2587 0.2134 0.2655 0.0179  0.0006  -0.0023 101 TYR B C     
3398 O  O     . TYR B 121 ? 0.2375 0.1963 0.2432 0.0156  0.0033  -0.0015 101 TYR B O     
3399 C  CB    . TYR B 121 ? 0.2495 0.2166 0.2623 0.0228  0.0038  -0.0078 101 TYR B CB    
3400 C  CG    . TYR B 121 ? 0.2279 0.1941 0.2413 0.0215  0.0038  -0.0034 101 TYR B CG    
3401 C  CD1   . TYR B 121 ? 0.2463 0.2092 0.2616 0.0239  0.0010  -0.0035 101 TYR B CD1   
3402 C  CD2   . TYR B 121 ? 0.2196 0.1877 0.2314 0.0178  0.0061  0.0007  101 TYR B CD2   
3403 C  CE1   . TYR B 121 ? 0.2374 0.1994 0.2525 0.0223  0.0009  0.0005  101 TYR B CE1   
3404 C  CE2   . TYR B 121 ? 0.2611 0.2287 0.2734 0.0167  0.0060  0.0042  101 TYR B CE2   
3405 C  CZ    . TYR B 121 ? 0.2620 0.2266 0.2755 0.0187  0.0037  0.0041  101 TYR B CZ    
3406 O  OH    . TYR B 121 ? 0.2885 0.2527 0.3019 0.0173  0.0037  0.0076  101 TYR B OH    
3407 N  N     . TYR B 122 ? 0.2293 0.1773 0.2346 0.0165  -0.0021 0.0010  102 TYR B N     
3408 C  CA    . TYR B 122 ? 0.2457 0.1921 0.2485 0.0120  -0.0017 0.0053  102 TYR B CA    
3409 C  C     . TYR B 122 ? 0.2434 0.1920 0.2469 0.0104  -0.0007 0.0089  102 TYR B C     
3410 O  O     . TYR B 122 ? 0.2561 0.2023 0.2603 0.0118  -0.0024 0.0093  102 TYR B O     
3411 C  CB    . TYR B 122 ? 0.2518 0.1891 0.2512 0.0102  -0.0058 0.0064  102 TYR B CB    
3412 C  CG    . TYR B 122 ? 0.2588 0.1929 0.2566 0.0109  -0.0073 0.0034  102 TYR B CG    
3413 C  CD1   . TYR B 122 ? 0.2789 0.2088 0.2772 0.0150  -0.0101 -0.0010 102 TYR B CD1   
3414 C  CD2   . TYR B 122 ? 0.2678 0.2026 0.2637 0.0075  -0.0062 0.0047  102 TYR B CD2   
3415 C  CE1   . TYR B 122 ? 0.2546 0.1812 0.2512 0.0158  -0.0117 -0.0042 102 TYR B CE1   
3416 C  CE2   . TYR B 122 ? 0.2396 0.1709 0.2335 0.0079  -0.0079 0.0020  102 TYR B CE2   
3417 C  CZ    . TYR B 122 ? 0.2904 0.2176 0.2845 0.0120  -0.0105 -0.0025 102 TYR B CZ    
3418 O  OH    . TYR B 122 ? 0.3046 0.2282 0.2967 0.0127  -0.0122 -0.0058 102 TYR B OH    
3419 N  N     . ALA B 123 ? 0.2340 0.1867 0.2373 0.0074  0.0017  0.0114  103 ALA B N     
3420 C  CA    . ALA B 123 ? 0.2236 0.1785 0.2273 0.0055  0.0026  0.0144  103 ALA B CA    
3421 C  C     . ALA B 123 ? 0.2884 0.2449 0.2910 0.0017  0.0033  0.0166  103 ALA B C     
3422 O  O     . ALA B 123 ? 0.2691 0.2281 0.2719 0.0011  0.0044  0.0159  103 ALA B O     
3423 C  CB    . ALA B 123 ? 0.2463 0.2077 0.2526 0.0070  0.0055  0.0141  103 ALA B CB    
3424 N  N     . ASN B 124 ? 0.2459 0.2017 0.2472 -0.0012 0.0026  0.0192  104 ASN B N     
3425 C  CA    . ASN B 124 ? 0.2539 0.2145 0.2554 -0.0045 0.0039  0.0206  104 ASN B CA    
3426 C  C     . ASN B 124 ? 0.2309 0.1988 0.2356 -0.0031 0.0068  0.0200  104 ASN B C     
3427 O  O     . ASN B 124 ? 0.2465 0.2153 0.2524 -0.0007 0.0076  0.0196  104 ASN B O     
3428 C  CB    . ASN B 124 ? 0.2891 0.2484 0.2880 -0.0087 0.0027  0.0232  104 ASN B CB    
3429 C  CG    . ASN B 124 ? 0.2648 0.2262 0.2640 -0.0086 0.0035  0.0242  104 ASN B CG    
3430 O  OD1   . ASN B 124 ? 0.2702 0.2387 0.2719 -0.0083 0.0061  0.0239  104 ASN B OD1   
3431 N  ND2   . ASN B 124 ? 0.2900 0.2451 0.2866 -0.0085 0.0009  0.0254  104 ASN B ND2   
3432 N  N     . CYS B 125 ? 0.2364 0.2091 0.2425 -0.0046 0.0078  0.0199  105 CYS B N     
3433 C  CA    . CYS B 125 ? 0.2119 0.1905 0.2210 -0.0031 0.0095  0.0191  105 CYS B CA    
3434 C  C     . CYS B 125 ? 0.2111 0.1953 0.2215 -0.0050 0.0104  0.0196  105 CYS B C     
3435 O  O     . CYS B 125 ? 0.2302 0.2199 0.2435 -0.0044 0.0111  0.0184  105 CYS B O     
3436 C  CB    . CYS B 125 ? 0.2066 0.1866 0.2167 -0.0024 0.0095  0.0180  105 CYS B CB    
3437 S  SG    . CYS B 125 ? 0.2392 0.2145 0.2475 -0.0004 0.0091  0.0169  105 CYS B SG    
3438 N  N     . ALA B 126 ? 0.2233 0.2065 0.2317 -0.0074 0.0101  0.0211  106 ALA B N     
3439 C  CA    . ALA B 126 ? 0.2165 0.2062 0.2258 -0.0095 0.0114  0.0211  106 ALA B CA    
3440 C  C     . ALA B 126 ? 0.2264 0.2201 0.2385 -0.0063 0.0127  0.0196  106 ALA B C     
3441 O  O     . ALA B 126 ? 0.2518 0.2526 0.2663 -0.0067 0.0138  0.0182  106 ALA B O     
3442 C  CB    . ALA B 126 ? 0.2570 0.2438 0.2623 -0.0129 0.0105  0.0234  106 ALA B CB    
3443 N  N     . PHE B 127 ? 0.2528 0.2425 0.2648 -0.0033 0.0124  0.0197  107 PHE B N     
3444 C  CA    . PHE B 127 ? 0.2578 0.2501 0.2720 -0.0006 0.0131  0.0185  107 PHE B CA    
3445 C  C     . PHE B 127 ? 0.2766 0.2729 0.2938 0.0008  0.0130  0.0167  107 PHE B C     
3446 O  O     . PHE B 127 ? 0.2567 0.2558 0.2758 0.0026  0.0131  0.0154  107 PHE B O     
3447 C  CB    . PHE B 127 ? 0.2385 0.2262 0.2520 0.0018  0.0128  0.0189  107 PHE B CB    
3448 C  CG    . PHE B 127 ? 0.2371 0.2221 0.2504 0.0027  0.0122  0.0185  107 PHE B CG    
3449 C  CD1   . PHE B 127 ? 0.2776 0.2640 0.2921 0.0038  0.0120  0.0176  107 PHE B CD1   
3450 C  CD2   . PHE B 127 ? 0.2672 0.2478 0.2786 0.0024  0.0115  0.0188  107 PHE B CD2   
3451 C  CE1   . PHE B 127 ? 0.2260 0.2101 0.2394 0.0039  0.0116  0.0173  107 PHE B CE1   
3452 C  CE2   . PHE B 127 ? 0.2804 0.2593 0.2913 0.0032  0.0113  0.0179  107 PHE B CE2   
3453 C  CZ    . PHE B 127 ? 0.2476 0.2286 0.2593 0.0036  0.0115  0.0173  107 PHE B CZ    
3454 N  N     . TYR B 128 ? 0.2315 0.2276 0.2491 0.0001  0.0123  0.0164  108 TYR B N     
3455 C  CA    . TYR B 128 ? 0.2431 0.2428 0.2637 0.0015  0.0115  0.0146  108 TYR B CA    
3456 C  C     . TYR B 128 ? 0.2474 0.2548 0.2712 0.0012  0.0121  0.0126  108 TYR B C     
3457 O  O     . TYR B 128 ? 0.2522 0.2625 0.2789 0.0038  0.0111  0.0104  108 TYR B O     
3458 C  CB    . TYR B 128 ? 0.2083 0.2068 0.2286 0.0004  0.0105  0.0147  108 TYR B CB    
3459 C  CG    . TYR B 128 ? 0.2111 0.2125 0.2344 0.0019  0.0089  0.0129  108 TYR B CG    
3460 C  CD1   . TYR B 128 ? 0.2441 0.2416 0.2667 0.0040  0.0073  0.0130  108 TYR B CD1   
3461 C  CD2   . TYR B 128 ? 0.2224 0.2307 0.2492 0.0012  0.0087  0.0111  108 TYR B CD2   
3462 C  CE1   . TYR B 128 ? 0.2167 0.2155 0.2415 0.0054  0.0048  0.0116  108 TYR B CE1   
3463 C  CE2   . TYR B 128 ? 0.2507 0.2614 0.2808 0.0032  0.0065  0.0091  108 TYR B CE2   
3464 C  CZ    . TYR B 128 ? 0.2314 0.2366 0.2603 0.0055  0.0042  0.0095  108 TYR B CZ    
3465 O  OH    . TYR B 128 ? 0.2493 0.2557 0.2810 0.0075  0.0011  0.0078  108 TYR B OH    
3466 N  N     . VAL B 129 ? 0.2321 0.2429 0.2550 -0.0021 0.0133  0.0130  109 VAL B N     
3467 C  CA    . VAL B 129 ? 0.2524 0.2725 0.2781 -0.0032 0.0144  0.0108  109 VAL B CA    
3468 C  C     . VAL B 129 ? 0.2748 0.2968 0.3004 -0.0021 0.0154  0.0100  109 VAL B C     
3469 O  O     . VAL B 129 ? 0.3178 0.3469 0.3469 -0.0005 0.0157  0.0067  109 VAL B O     
3470 C  CB    . VAL B 129 ? 0.2731 0.2962 0.2968 -0.0084 0.0153  0.0121  109 VAL B CB    
3471 C  CG1   . VAL B 129 ? 0.3693 0.4040 0.3958 -0.0104 0.0170  0.0094  109 VAL B CG1   
3472 C  CG2   . VAL B 129 ? 0.2345 0.2554 0.2583 -0.0096 0.0141  0.0127  109 VAL B CG2   
3473 N  N     . ASP B 130 ? 0.2818 0.2978 0.3035 -0.0029 0.0157  0.0126  110 ASP B N     
3474 C  CA    . ASP B 130 ? 0.3141 0.3311 0.3349 -0.0023 0.0165  0.0123  110 ASP B CA    
3475 C  C     . ASP B 130 ? 0.2798 0.2883 0.2979 -0.0010 0.0157  0.0148  110 ASP B C     
3476 O  O     . ASP B 130 ? 0.2850 0.2886 0.2998 -0.0030 0.0154  0.0172  110 ASP B O     
3477 C  CB    . ASP B 130 ? 0.3412 0.3634 0.3598 -0.0068 0.0180  0.0128  110 ASP B CB    
3478 C  CG    . ASP B 130 ? 0.4363 0.4585 0.4528 -0.0069 0.0186  0.0130  110 ASP B CG    
3479 O  OD1   . ASP B 130 ? 0.3590 0.3767 0.3757 -0.0035 0.0179  0.0131  110 ASP B OD1   
3480 O  OD2   . ASP B 130 ? 0.4075 0.4347 0.4217 -0.0108 0.0198  0.0133  110 ASP B OD2   
3481 N  N     . PRO B 131 ? 0.3056 0.3122 0.3249 0.0023  0.0151  0.0139  111 PRO B N     
3482 C  CA    . PRO B 131 ? 0.3176 0.3174 0.3351 0.0035  0.0144  0.0158  111 PRO B CA    
3483 C  C     . PRO B 131 ? 0.3071 0.3043 0.3217 0.0020  0.0147  0.0178  111 PRO B C     
3484 O  O     . PRO B 131 ? 0.3644 0.3566 0.3778 0.0028  0.0140  0.0191  111 PRO B O     
3485 C  CB    . PRO B 131 ? 0.3115 0.3113 0.3306 0.0064  0.0136  0.0145  111 PRO B CB    
3486 C  CG    . PRO B 131 ? 0.3376 0.3422 0.3597 0.0075  0.0130  0.0117  111 PRO B CG    
3487 C  CD    . PRO B 131 ? 0.3737 0.3843 0.3962 0.0050  0.0146  0.0110  111 PRO B CD    
3488 N  N     . SER B 132 ? 0.3040 0.3047 0.3173 -0.0002 0.0154  0.0178  112 SER B N     
3489 C  CA    . SER B 132 ? 0.3250 0.3224 0.3349 -0.0020 0.0149  0.0200  112 SER B CA    
3490 C  C     . SER B 132 ? 0.3858 0.3791 0.3927 -0.0050 0.0139  0.0222  112 SER B C     
3491 O  O     . SER B 132 ? 0.3689 0.3576 0.3727 -0.0062 0.0124  0.0243  112 SER B O     
3492 C  CB    . SER B 132 ? 0.3567 0.3591 0.3654 -0.0039 0.0159  0.0193  112 SER B CB    
3493 O  OG    . SER B 132 ? 0.3881 0.3925 0.3990 -0.0008 0.0162  0.0173  112 SER B OG    
3494 N  N     . LEU B 133 ? 0.2863 0.2806 0.2938 -0.0063 0.0140  0.0219  113 LEU B N     
3495 C  CA    . LEU B 133 ? 0.2970 0.2870 0.3011 -0.0096 0.0125  0.0241  113 LEU B CA    
3496 C  C     . LEU B 133 ? 0.3426 0.3248 0.3462 -0.0072 0.0106  0.0248  113 LEU B C     
3497 O  O     . LEU B 133 ? 0.3183 0.3004 0.3246 -0.0043 0.0110  0.0233  113 LEU B O     
3498 C  CB    . LEU B 133 ? 0.2840 0.2787 0.2889 -0.0123 0.0133  0.0234  113 LEU B CB    
3499 C  CG    . LEU B 133 ? 0.3691 0.3733 0.3746 -0.0154 0.0152  0.0221  113 LEU B CG    
3500 C  CD1   . LEU B 133 ? 0.3531 0.3623 0.3605 -0.0175 0.0157  0.0211  113 LEU B CD1   
3501 C  CD2   . LEU B 133 ? 0.3633 0.3667 0.3636 -0.0203 0.0147  0.0246  113 LEU B CD2   
3502 N  N     . SER B 134 ? 0.3213 0.2970 0.3214 -0.0087 0.0082  0.0268  114 SER B N     
3503 C  CA    . SER B 134 ? 0.3252 0.2936 0.3250 -0.0064 0.0058  0.0267  114 SER B CA    
3504 C  C     . SER B 134 ? 0.2842 0.2489 0.2817 -0.0091 0.0042  0.0275  114 SER B C     
3505 O  O     . SER B 134 ? 0.2985 0.2571 0.2956 -0.0072 0.0020  0.0269  114 SER B O     
3506 C  CB    . SER B 134 ? 0.3634 0.3258 0.3610 -0.0056 0.0031  0.0280  114 SER B CB    
3507 O  OG    . SER B 134 ? 0.4630 0.4220 0.4556 -0.0103 0.0009  0.0308  114 SER B OG    
3508 N  N     . CYS B 135 ? 0.2709 0.2397 0.2670 -0.0136 0.0051  0.0285  115 CYS B N     
3509 C  CA    . CYS B 135 ? 0.2778 0.2440 0.2711 -0.0176 0.0036  0.0297  115 CYS B CA    
3510 C  C     . CYS B 135 ? 0.2821 0.2566 0.2748 -0.0225 0.0056  0.0303  115 CYS B C     
3511 O  O     . CYS B 135 ? 0.3164 0.2971 0.3101 -0.0226 0.0077  0.0297  115 CYS B O     
3512 C  CB    . CYS B 135 ? 0.2708 0.2263 0.2590 -0.0195 -0.0009 0.0320  115 CYS B CB    
3513 S  SG    . CYS B 135 ? 0.3481 0.3011 0.3316 -0.0227 -0.0028 0.0350  115 CYS B SG    
3514 N  N     . ALA B 136 ? 0.2700 0.2450 0.2610 -0.0268 0.0050  0.0311  116 ALA B N     
3515 C  CA    . ALA B 136 ? 0.3096 0.2937 0.2999 -0.0324 0.0068  0.0314  116 ALA B CA    
3516 C  C     . ALA B 136 ? 0.3400 0.3238 0.3254 -0.0367 0.0062  0.0339  116 ALA B C     
3517 O  O     . ALA B 136 ? 0.3398 0.3134 0.3203 -0.0376 0.0028  0.0365  116 ALA B O     
3518 C  CB    . ALA B 136 ? 0.2986 0.2819 0.2868 -0.0372 0.0055  0.0326  116 ALA B CB    
3519 N  N     . LYS B 137 ? 0.3633 0.3583 0.3498 -0.0394 0.0093  0.0327  117 LYS B N     
3520 C  CA    . LYS B 137 ? 0.3937 0.3897 0.3746 -0.0451 0.0089  0.0351  117 LYS B CA    
3521 C  C     . LYS B 137 ? 0.4020 0.3931 0.3761 -0.0530 0.0060  0.0388  117 LYS B C     
3522 O  O     . LYS B 137 ? 0.4038 0.4005 0.3790 -0.0563 0.0070  0.0382  117 LYS B O     
3523 C  CB    . LYS B 137 ? 0.4916 0.5023 0.4752 -0.0466 0.0131  0.0322  117 LYS B CB    
3524 C  CG    . LYS B 137 ? 0.6184 0.6330 0.6081 -0.0391 0.0153  0.0286  117 LYS B CG    
3525 C  CD    . LYS B 137 ? 0.7604 0.7898 0.7539 -0.0397 0.0190  0.0246  117 LYS B CD    
3526 C  CE    . LYS B 137 ? 0.6667 0.6978 0.6652 -0.0325 0.0202  0.0213  117 LYS B CE    
3527 N  NZ    . LYS B 137 ? 0.6092 0.6335 0.6038 -0.0317 0.0190  0.0234  117 LYS B NZ    
3528 N  N     . PRO B 138 ? 0.4464 0.4266 0.4134 -0.0561 0.0019  0.0428  118 PRO B N     
3529 C  CA    . PRO B 138 ? 0.3720 0.3448 0.3318 -0.0636 -0.0021 0.0467  118 PRO B CA    
3530 C  C     . PRO B 138 ? 0.4240 0.4069 0.3794 -0.0733 -0.0002 0.0482  118 PRO B C     
3531 O  O     . PRO B 138 ? 0.4850 0.4777 0.4404 -0.0750 0.0030  0.0472  118 PRO B O     
3532 C  CB    . PRO B 138 ? 0.4611 0.4189 0.4148 -0.0632 -0.0076 0.0501  118 PRO B CB    
3533 C  CG    . PRO B 138 ? 0.5050 0.4670 0.4609 -0.0592 -0.0053 0.0487  118 PRO B CG    
3534 C  CD    . PRO B 138 ? 0.4309 0.4041 0.3961 -0.0527 0.0000  0.0438  118 PRO B CD    
3535 N  N     . THR B 139 ? 0.4228 0.4040 0.3746 -0.0798 -0.0021 0.0503  119 THR B N     
3536 C  CA    . THR B 139 ? 0.4636 0.4533 0.4099 -0.0907 -0.0012 0.0525  119 THR B CA    
3537 C  C     . THR B 139 ? 0.5280 0.5029 0.4642 -0.0982 -0.0077 0.0582  119 THR B C     
3538 O  O     . THR B 139 ? 0.5083 0.4680 0.4435 -0.0940 -0.0126 0.0594  119 THR B O     
3539 C  CB    . THR B 139 ? 0.4783 0.4836 0.4309 -0.0922 0.0033  0.0489  119 THR B CB    
3540 O  OG1   . THR B 139 ? 0.4914 0.4890 0.4447 -0.0915 0.0005  0.0496  119 THR B OG1   
3541 C  CG2   . THR B 139 ? 0.4843 0.5016 0.4473 -0.0834 0.0085  0.0429  119 THR B CG2   
3542 N  N     . GLU B 140 ? 0.5366 0.5160 0.4651 -0.1097 -0.0082 0.0617  120 GLU B N     
3543 C  CA    . GLU B 140 ? 0.5411 0.5062 0.4592 -0.1181 -0.0150 0.0674  120 GLU B CA    
3544 C  C     . GLU B 140 ? 0.5068 0.4678 0.4277 -0.1170 -0.0166 0.0667  120 GLU B C     
3545 O  O     . GLU B 140 ? 0.5770 0.5206 0.4923 -0.1179 -0.0234 0.0700  120 GLU B O     
3546 C  CB    . GLU B 140 ? 0.6311 0.6040 0.5402 -0.1318 -0.0145 0.0711  120 GLU B CB    
3547 C  CG    . GLU B 140 ? 0.8552 0.8139 0.7527 -0.1422 -0.0218 0.0776  120 GLU B CG    
3548 C  CD    . GLU B 140 ? 1.1547 1.1220 1.0424 -0.1569 -0.0212 0.0816  120 GLU B CD    
3549 O  OE1   . GLU B 140 ? 1.0791 1.0664 0.9705 -0.1589 -0.0142 0.0783  120 GLU B OE1   
3550 O  OE2   . GLU B 140 ? 1.2351 1.1893 1.1113 -0.1667 -0.0280 0.0878  120 GLU B OE2   
3551 N  N     . GLU B 141 ? 0.4783 0.4548 0.4079 -0.1148 -0.0110 0.0622  121 GLU B N     
3552 C  CA    . GLU B 141 ? 0.4626 0.4366 0.3950 -0.1142 -0.0123 0.0614  121 GLU B CA    
3553 C  C     . GLU B 141 ? 0.4463 0.4084 0.3839 -0.1026 -0.0143 0.0590  121 GLU B C     
3554 O  O     . GLU B 141 ? 0.4515 0.4017 0.3868 -0.1024 -0.0189 0.0602  121 GLU B O     
3555 C  CB    . GLU B 141 ? 0.4762 0.4709 0.4166 -0.1152 -0.0059 0.0571  121 GLU B CB    
3556 C  CG    . GLU B 141 ? 0.4705 0.4645 0.4135 -0.1158 -0.0071 0.0563  121 GLU B CG    
3557 C  CD    . GLU B 141 ? 0.6259 0.6412 0.5775 -0.1165 -0.0012 0.0517  121 GLU B CD    
3558 O  OE1   . GLU B 141 ? 0.5607 0.5897 0.5187 -0.1124 0.0039  0.0477  121 GLU B OE1   
3559 O  OE2   . GLU B 141 ? 0.5649 0.5832 0.5170 -0.1211 -0.0020 0.0520  121 GLU B OE2   
3560 N  N     . PHE B 142 ? 0.3962 0.3620 0.3406 -0.0932 -0.0110 0.0554  122 PHE B N     
3561 C  CA    . PHE B 142 ? 0.3999 0.3582 0.3501 -0.0824 -0.0118 0.0524  122 PHE B CA    
3562 C  C     . PHE B 142 ? 0.3745 0.3268 0.3250 -0.0761 -0.0124 0.0521  122 PHE B C     
3563 O  O     . PHE B 142 ? 0.3679 0.3306 0.3228 -0.0731 -0.0079 0.0498  122 PHE B O     
3564 C  CB    . PHE B 142 ? 0.3325 0.3039 0.2925 -0.0769 -0.0064 0.0475  122 PHE B CB    
3565 C  CG    . PHE B 142 ? 0.3721 0.3501 0.3330 -0.0823 -0.0058 0.0472  122 PHE B CG    
3566 C  CD1   . PHE B 142 ? 0.4059 0.3724 0.3630 -0.0843 -0.0104 0.0491  122 PHE B CD1   
3567 C  CD2   . PHE B 142 ? 0.4137 0.4098 0.3799 -0.0846 -0.0009 0.0445  122 PHE B CD2   
3568 C  CE1   . PHE B 142 ? 0.4331 0.4057 0.3910 -0.0894 -0.0100 0.0489  122 PHE B CE1   
3569 C  CE2   . PHE B 142 ? 0.3906 0.3937 0.3584 -0.0894 -0.0004 0.0440  122 PHE B CE2   
3570 C  CZ    . PHE B 142 ? 0.3997 0.3911 0.3632 -0.0920 -0.0050 0.0464  122 PHE B CZ    
3571 N  N     . ASN B 143 ? 0.3577 0.2936 0.3041 -0.0736 -0.0182 0.0540  123 ASN B N     
3572 C  CA    . ASN B 143 ? 0.4060 0.3359 0.3524 -0.0680 -0.0196 0.0538  123 ASN B CA    
3573 C  C     . ASN B 143 ? 0.3954 0.3113 0.3428 -0.0610 -0.0243 0.0526  123 ASN B C     
3574 O  O     . ASN B 143 ? 0.3947 0.3044 0.3412 -0.0613 -0.0269 0.0523  123 ASN B O     
3575 C  CB    . ASN B 143 ? 0.4333 0.3586 0.3710 -0.0755 -0.0228 0.0585  123 ASN B CB    
3576 C  CG    . ASN B 143 ? 0.5270 0.4401 0.4553 -0.0837 -0.0294 0.0631  123 ASN B CG    
3577 O  OD1   . ASN B 143 ? 0.5315 0.4293 0.4574 -0.0807 -0.0356 0.0638  123 ASN B OD1   
3578 N  ND2   . ASN B 143 ? 0.5103 0.4303 0.4331 -0.0943 -0.0283 0.0661  123 ASN B ND2   
3579 N  N     . PRO B 144 ? 0.3727 0.2840 0.3220 -0.0544 -0.0254 0.0514  124 PRO B N     
3580 C  CA    . PRO B 144 ? 0.4312 0.3305 0.3819 -0.0474 -0.0299 0.0494  124 PRO B CA    
3581 C  C     . PRO B 144 ? 0.5030 0.3862 0.4460 -0.0513 -0.0381 0.0525  124 PRO B C     
3582 O  O     . PRO B 144 ? 0.5299 0.4040 0.4743 -0.0461 -0.0419 0.0501  124 PRO B O     
3583 C  CB    . PRO B 144 ? 0.4322 0.3313 0.3859 -0.0413 -0.0297 0.0481  124 PRO B CB    
3584 C  CG    . PRO B 144 ? 0.4312 0.3450 0.3885 -0.0422 -0.0229 0.0475  124 PRO B CG    
3585 C  CD    . PRO B 144 ? 0.3480 0.2670 0.3002 -0.0518 -0.0218 0.0506  124 PRO B CD    
3586 N  N     . ASP B 145 ? 0.5017 0.3810 0.4363 -0.0606 -0.0413 0.0575  125 ASP B N     
3587 C  CA    . ASP B 145 ? 0.5347 0.3967 0.4610 -0.0646 -0.0501 0.0607  125 ASP B CA    
3588 C  C     . ASP B 145 ? 0.5155 0.3754 0.4404 -0.0682 -0.0511 0.0607  125 ASP B C     
3589 O  O     . ASP B 145 ? 0.6379 0.4835 0.5600 -0.0664 -0.0578 0.0604  125 ASP B O     
3590 C  CB    . ASP B 145 ? 0.5435 0.4006 0.4599 -0.0742 -0.0540 0.0667  125 ASP B CB    
3591 C  CG    . ASP B 145 ? 0.7738 0.6291 0.6903 -0.0705 -0.0551 0.0671  125 ASP B CG    
3592 O  OD1   . ASP B 145 ? 0.7692 0.6189 0.6908 -0.0610 -0.0572 0.0636  125 ASP B OD1   
3593 O  OD2   . ASP B 145 ? 0.9175 0.7776 0.8290 -0.0773 -0.0539 0.0706  125 ASP B OD2   
3594 N  N     . ASN B 146 ? 0.4396 0.3134 0.3666 -0.0730 -0.0450 0.0607  126 ASN B N     
3595 C  CA    . ASN B 146 ? 0.4764 0.3486 0.4021 -0.0767 -0.0461 0.0607  126 ASN B CA    
3596 C  C     . ASN B 146 ? 0.4065 0.2863 0.3413 -0.0690 -0.0413 0.0553  126 ASN B C     
3597 O  O     . ASN B 146 ? 0.4431 0.3185 0.3772 -0.0700 -0.0434 0.0546  126 ASN B O     
3598 C  CB    . ASN B 146 ? 0.5172 0.3987 0.4383 -0.0885 -0.0438 0.0645  126 ASN B CB    
3599 C  CG    . ASN B 146 ? 0.5308 0.4328 0.4584 -0.0885 -0.0349 0.0624  126 ASN B CG    
3600 O  OD1   . ASN B 146 ? 0.4846 0.3929 0.4192 -0.0804 -0.0308 0.0589  126 ASN B OD1   
3601 N  ND2   . ASN B 146 ? 0.6244 0.5372 0.5497 -0.0978 -0.0322 0.0643  126 ASN B ND2   
3602 N  N     . PHE B 147 ? 0.4452 0.3357 0.3879 -0.0619 -0.0354 0.0517  127 PHE B N     
3603 C  CA    . PHE B 147 ? 0.3878 0.2843 0.3384 -0.0545 -0.0315 0.0469  127 PHE B CA    
3604 C  C     . PHE B 147 ? 0.3446 0.2406 0.3004 -0.0451 -0.0303 0.0434  127 PHE B C     
3605 O  O     . PHE B 147 ? 0.3232 0.2307 0.2854 -0.0410 -0.0245 0.0409  127 PHE B O     
3606 C  CB    . PHE B 147 ? 0.3525 0.2657 0.3080 -0.0568 -0.0246 0.0458  127 PHE B CB    
3607 C  CG    . PHE B 147 ? 0.3731 0.2881 0.3255 -0.0647 -0.0255 0.0476  127 PHE B CG    
3608 C  CD1   . PHE B 147 ? 0.3753 0.2882 0.3296 -0.0628 -0.0262 0.0455  127 PHE B CD1   
3609 C  CD2   . PHE B 147 ? 0.4066 0.3258 0.3538 -0.0744 -0.0257 0.0515  127 PHE B CD2   
3610 C  CE1   . PHE B 147 ? 0.4220 0.3367 0.3736 -0.0703 -0.0272 0.0473  127 PHE B CE1   
3611 C  CE2   . PHE B 147 ? 0.4104 0.3322 0.3549 -0.0823 -0.0264 0.0532  127 PHE B CE2   
3612 C  CZ    . PHE B 147 ? 0.4223 0.3418 0.3692 -0.0800 -0.0273 0.0511  127 PHE B CZ    
3613 N  N     . PRO B 148 ? 0.4149 0.2978 0.3682 -0.0414 -0.0361 0.0431  128 PRO B N     
3614 C  CA    . PRO B 148 ? 0.3941 0.2778 0.3528 -0.0327 -0.0350 0.0396  128 PRO B CA    
3615 C  C     . PRO B 148 ? 0.3831 0.2734 0.3486 -0.0260 -0.0308 0.0346  128 PRO B C     
3616 O  O     . PRO B 148 ? 0.3903 0.2871 0.3612 -0.0205 -0.0273 0.0321  128 PRO B O     
3617 C  CB    . PRO B 148 ? 0.4123 0.2799 0.3667 -0.0306 -0.0432 0.0399  128 PRO B CB    
3618 C  CG    . PRO B 148 ? 0.4530 0.3108 0.4015 -0.0357 -0.0481 0.0417  128 PRO B CG    
3619 C  CD    . PRO B 148 ? 0.5354 0.4020 0.4813 -0.0447 -0.0444 0.0454  128 PRO B CD    
3620 N  N     . GLU B 149 ? 0.4027 0.2922 0.3681 -0.0271 -0.0310 0.0335  129 GLU B N     
3621 C  CA    . GLU B 149 ? 0.3924 0.2875 0.3632 -0.0215 -0.0275 0.0289  129 GLU B CA    
3622 C  C     . GLU B 149 ? 0.3610 0.2706 0.3367 -0.0218 -0.0205 0.0285  129 GLU B C     
3623 O  O     . GLU B 149 ? 0.3555 0.2703 0.3354 -0.0174 -0.0175 0.0252  129 GLU B O     
3624 C  CB    . GLU B 149 ? 0.4250 0.3137 0.3934 -0.0227 -0.0305 0.0278  129 GLU B CB    
3625 C  CG    . GLU B 149 ? 0.4233 0.3155 0.3891 -0.0304 -0.0295 0.0309  129 GLU B CG    
3626 C  CD    . GLU B 149 ? 0.4619 0.3462 0.4206 -0.0381 -0.0343 0.0357  129 GLU B CD    
3627 O  OE1   . GLU B 149 ? 0.4742 0.3517 0.4298 -0.0382 -0.0377 0.0376  129 GLU B OE1   
3628 O  OE2   . GLU B 149 ? 0.6381 0.5229 0.5938 -0.0446 -0.0350 0.0379  129 GLU B OE2   
3629 N  N     . TYR B 150 ? 0.3100 0.2261 0.2849 -0.0268 -0.0183 0.0316  130 TYR B N     
3630 C  CA    . TYR B 150 ? 0.2694 0.1988 0.2491 -0.0266 -0.0125 0.0308  130 TYR B CA    
3631 C  C     . TYR B 150 ? 0.2944 0.2294 0.2754 -0.0263 -0.0101 0.0318  130 TYR B C     
3632 O  O     . TYR B 150 ? 0.2685 0.2125 0.2543 -0.0234 -0.0059 0.0301  130 TYR B O     
3633 C  CB    . TYR B 150 ? 0.3014 0.2369 0.2804 -0.0328 -0.0112 0.0323  130 TYR B CB    
3634 C  CG    . TYR B 150 ? 0.2957 0.2284 0.2743 -0.0333 -0.0126 0.0311  130 TYR B CG    
3635 C  CD1   . TYR B 150 ? 0.2776 0.2151 0.2607 -0.0288 -0.0100 0.0280  130 TYR B CD1   
3636 C  CD2   . TYR B 150 ? 0.2893 0.2141 0.2625 -0.0386 -0.0169 0.0333  130 TYR B CD2   
3637 C  CE1   . TYR B 150 ? 0.2907 0.2256 0.2731 -0.0295 -0.0114 0.0268  130 TYR B CE1   
3638 C  CE2   . TYR B 150 ? 0.3448 0.2668 0.3175 -0.0392 -0.0183 0.0321  130 TYR B CE2   
3639 C  CZ    . TYR B 150 ? 0.3341 0.2614 0.3115 -0.0345 -0.0155 0.0288  130 TYR B CZ    
3640 O  OH    . TYR B 150 ? 0.3096 0.2341 0.2861 -0.0353 -0.0170 0.0276  130 TYR B OH    
3641 N  N     . LEU B 151 ? 0.3268 0.2562 0.3032 -0.0295 -0.0130 0.0347  131 LEU B N     
3642 C  CA    . LEU B 151 ? 0.3188 0.2547 0.2955 -0.0310 -0.0106 0.0361  131 LEU B CA    
3643 C  C     . LEU B 151 ? 0.3542 0.2843 0.3304 -0.0271 -0.0127 0.0362  131 LEU B C     
3644 O  O     . LEU B 151 ? 0.3159 0.2496 0.2912 -0.0287 -0.0115 0.0376  131 LEU B O     
3645 C  CB    . LEU B 151 ? 0.3034 0.2406 0.2747 -0.0397 -0.0116 0.0398  131 LEU B CB    
3646 C  CG    . LEU B 151 ? 0.3200 0.2635 0.2916 -0.0445 -0.0100 0.0399  131 LEU B CG    
3647 C  CD1   . LEU B 151 ? 0.3659 0.3109 0.3313 -0.0539 -0.0111 0.0436  131 LEU B CD1   
3648 C  CD2   . LEU B 151 ? 0.3042 0.2612 0.2829 -0.0415 -0.0045 0.0366  131 LEU B CD2   
3649 N  N     . SER B 152 ? 0.3185 0.2405 0.2955 -0.0220 -0.0158 0.0343  132 SER B N     
3650 C  CA    . SER B 152 ? 0.3376 0.2552 0.3150 -0.0179 -0.0179 0.0338  132 SER B CA    
3651 C  C     . SER B 152 ? 0.3362 0.2635 0.3195 -0.0133 -0.0129 0.0314  132 SER B C     
3652 O  O     . SER B 152 ? 0.3456 0.2797 0.3331 -0.0110 -0.0092 0.0290  132 SER B O     
3653 C  CB    . SER B 152 ? 0.3173 0.2246 0.2946 -0.0133 -0.0227 0.0315  132 SER B CB    
3654 O  OG    . SER B 152 ? 0.3799 0.2764 0.3511 -0.0176 -0.0283 0.0339  132 SER B OG    
3655 N  N     . PRO B 153 ? 0.3166 0.2441 0.3000 -0.0121 -0.0133 0.0322  133 PRO B N     
3656 C  CA    A PRO B 153 ? 0.2964 0.2324 0.2849 -0.0083 -0.0091 0.0302  133 PRO B CA    
3657 C  CA    B PRO B 153 ? 0.2958 0.2319 0.2844 -0.0083 -0.0091 0.0302  133 PRO B CA    
3658 C  C     . PRO B 153 ? 0.2870 0.2233 0.2802 -0.0021 -0.0086 0.0264  133 PRO B C     
3659 O  O     . PRO B 153 ? 0.3345 0.2638 0.3274 0.0007  -0.0124 0.0249  133 PRO B O     
3660 C  CB    A PRO B 153 ? 0.3301 0.2640 0.3166 -0.0088 -0.0109 0.0321  133 PRO B CB    
3661 C  CB    B PRO B 153 ? 0.3304 0.2645 0.3170 -0.0089 -0.0108 0.0321  133 PRO B CB    
3662 C  CG    A PRO B 153 ? 0.2911 0.2184 0.2708 -0.0149 -0.0146 0.0359  133 PRO B CG    
3663 C  CG    B PRO B 153 ? 0.2999 0.2224 0.2815 -0.0104 -0.0170 0.0340  133 PRO B CG    
3664 C  CD    A PRO B 153 ? 0.3469 0.2673 0.3249 -0.0156 -0.0176 0.0356  133 PRO B CD    
3665 C  CD    B PRO B 153 ? 0.3511 0.2707 0.3293 -0.0149 -0.0179 0.0353  133 PRO B CD    
3666 N  N     . ASN B 154 ? 0.2950 0.2397 0.2922 -0.0001 -0.0042 0.0246  134 ASN B N     
3667 C  CA    . ASN B 154 ? 0.2573 0.2043 0.2586 0.0047  -0.0030 0.0211  134 ASN B CA    
3668 C  C     . ASN B 154 ? 0.3311 0.2764 0.3342 0.0084  -0.0049 0.0198  134 ASN B C     
3669 O  O     . ASN B 154 ? 0.3271 0.2724 0.3294 0.0076  -0.0055 0.0217  134 ASN B O     
3670 C  CB    . ASN B 154 ? 0.2540 0.2096 0.2582 0.0051  0.0015  0.0202  134 ASN B CB    
3671 C  CG    . ASN B 154 ? 0.2311 0.1884 0.2347 0.0029  0.0028  0.0202  134 ASN B CG    
3672 O  OD1   . ASN B 154 ? 0.2774 0.2301 0.2791 0.0020  0.0009  0.0200  134 ASN B OD1   
3673 N  ND2   . ASN B 154 ? 0.2393 0.2030 0.2445 0.0022  0.0057  0.0204  134 ASN B ND2   
3674 N  N     . LEU B 155 ? 0.2722 0.2166 0.2778 0.0125  -0.0060 0.0163  135 LEU B N     
3675 C  CA    . LEU B 155 ? 0.2671 0.2112 0.2756 0.0167  -0.0080 0.0140  135 LEU B CA    
3676 C  C     . LEU B 155 ? 0.3175 0.2705 0.3304 0.0194  -0.0042 0.0107  135 LEU B C     
3677 O  O     . LEU B 155 ? 0.3383 0.2932 0.3524 0.0208  -0.0031 0.0077  135 LEU B O     
3678 C  CB    . LEU B 155 ? 0.2699 0.2056 0.2777 0.0194  -0.0133 0.0119  135 LEU B CB    
3679 C  CG    . LEU B 155 ? 0.3609 0.2858 0.3632 0.0162  -0.0183 0.0154  135 LEU B CG    
3680 C  CD1   . LEU B 155 ? 0.4568 0.3728 0.4588 0.0196  -0.0241 0.0125  135 LEU B CD1   
3681 C  CD2   . LEU B 155 ? 0.3995 0.3227 0.3999 0.0143  -0.0199 0.0188  135 LEU B CD2   
3682 N  N     . TRP B 156 ? 0.3003 0.2587 0.3153 0.0198  -0.0022 0.0112  136 TRP B N     
3683 C  CA    . TRP B 156 ? 0.2948 0.2619 0.3133 0.0210  0.0013  0.0089  136 TRP B CA    
3684 C  C     . TRP B 156 ? 0.3254 0.2956 0.3479 0.0248  0.0001  0.0059  136 TRP B C     
3685 O  O     . TRP B 156 ? 0.3100 0.2769 0.3328 0.0257  -0.0027 0.0070  136 TRP B O     
3686 C  CB    . TRP B 156 ? 0.3203 0.2918 0.3382 0.0182  0.0044  0.0116  136 TRP B CB    
3687 C  CG    . TRP B 156 ? 0.3079 0.2781 0.3229 0.0151  0.0058  0.0138  136 TRP B CG    
3688 C  CD1   . TRP B 156 ? 0.3160 0.2833 0.3284 0.0124  0.0051  0.0167  136 TRP B CD1   
3689 C  CD2   . TRP B 156 ? 0.2885 0.2613 0.3031 0.0141  0.0079  0.0130  136 TRP B CD2   
3690 N  NE1   . TRP B 156 ? 0.2983 0.2668 0.3095 0.0102  0.0067  0.0175  136 TRP B NE1   
3691 C  CE2   . TRP B 156 ? 0.2978 0.2690 0.3103 0.0113  0.0082  0.0154  136 TRP B CE2   
3692 C  CE3   . TRP B 156 ? 0.2946 0.2713 0.3105 0.0150  0.0094  0.0105  136 TRP B CE3   
3693 C  CZ2   . TRP B 156 ? 0.3172 0.2900 0.3290 0.0099  0.0095  0.0153  136 TRP B CZ2   
3694 C  CZ3   . TRP B 156 ? 0.2606 0.2382 0.2749 0.0131  0.0108  0.0108  136 TRP B CZ3   
3695 C  CH2   . TRP B 156 ? 0.3167 0.2921 0.3292 0.0109  0.0106  0.0132  136 TRP B CH2   
3696 N  N     . PRO B 157 ? 0.3313 0.3086 0.3572 0.0266  0.0021  0.0020  137 PRO B N     
3697 C  CA    . PRO B 157 ? 0.3141 0.2973 0.3445 0.0295  0.0019  -0.0008 137 PRO B CA    
3698 C  C     . PRO B 157 ? 0.3147 0.3013 0.3451 0.0271  0.0037  0.0023  137 PRO B C     
3699 O  O     . PRO B 157 ? 0.3417 0.3283 0.3692 0.0237  0.0060  0.0055  137 PRO B O     
3700 C  CB    . PRO B 157 ? 0.3478 0.3396 0.3808 0.0304  0.0047  -0.0054 137 PRO B CB    
3701 C  CG    . PRO B 157 ? 0.3900 0.3811 0.4190 0.0269  0.0073  -0.0033 137 PRO B CG    
3702 C  CD    . PRO B 157 ? 0.3419 0.3231 0.3672 0.0256  0.0050  0.0002  137 PRO B CD    
3703 N  N     . GLN B 158 ? 0.4044 0.3938 0.4381 0.0293  0.0022  0.0011  138 GLN B N     
3704 C  CA    . GLN B 158 ? 0.3945 0.3872 0.4283 0.0272  0.0037  0.0037  138 GLN B CA    
3705 C  C     . GLN B 158 ? 0.3391 0.3396 0.3730 0.0245  0.0078  0.0034  138 GLN B C     
3706 O  O     . GLN B 158 ? 0.3682 0.3750 0.4043 0.0252  0.0095  -0.0001 138 GLN B O     
3707 C  CB    . GLN B 158 ? 0.5141 0.5093 0.5519 0.0300  0.0012  0.0020  138 GLN B CB    
3708 C  CG    . GLN B 158 ? 0.5364 0.5227 0.5730 0.0319  -0.0037 0.0034  138 GLN B CG    
3709 C  CD    . GLN B 158 ? 0.5514 0.5338 0.5843 0.0289  -0.0041 0.0081  138 GLN B CD    
3710 O  OE1   . GLN B 158 ? 0.6466 0.6342 0.6799 0.0269  -0.0015 0.0092  138 GLN B OE1   
3711 N  NE2   . GLN B 158 ? 0.7232 0.6966 0.7522 0.0282  -0.0075 0.0107  138 GLN B NE2   
3712 N  N     . GLU B 159 ? 0.3565 0.3564 0.3878 0.0213  0.0093  0.0069  139 GLU B N     
3713 C  CA    . GLU B 159 ? 0.3748 0.3800 0.4052 0.0183  0.0122  0.0073  139 GLU B CA    
3714 C  C     . GLU B 159 ? 0.3726 0.3869 0.4067 0.0186  0.0133  0.0043  139 GLU B C     
3715 O  O     . GLU B 159 ? 0.4102 0.4301 0.4440 0.0167  0.0156  0.0029  139 GLU B O     
3716 C  CB    . GLU B 159 ? 0.3693 0.3721 0.3971 0.0158  0.0124  0.0110  139 GLU B CB    
3717 C  CG    . GLU B 159 ? 0.3901 0.3979 0.4174 0.0128  0.0141  0.0116  139 GLU B CG    
3718 C  CD    . GLU B 159 ? 0.3996 0.4086 0.4244 0.0103  0.0157  0.0116  139 GLU B CD    
3719 O  OE1   . GLU B 159 ? 0.3971 0.4027 0.4205 0.0108  0.0158  0.0115  139 GLU B OE1   
3720 O  OE2   . GLU B 159 ? 0.5144 0.5274 0.5382 0.0073  0.0167  0.0120  139 GLU B OE2   
3721 N  N     . SER B 160 ? 0.3179 0.3345 0.3556 0.0208  0.0117  0.0032  140 SER B N     
3722 C  CA    . SER B 160 ? 0.3272 0.3541 0.3691 0.0209  0.0129  0.0000  140 SER B CA    
3723 C  C     . SER B 160 ? 0.3318 0.3645 0.3773 0.0236  0.0133  -0.0053 140 SER B C     
3724 O  O     . SER B 160 ? 0.3624 0.4058 0.4108 0.0226  0.0154  -0.0085 140 SER B O     
3725 C  CB    . SER B 160 ? 0.4843 0.5124 0.5293 0.0224  0.0108  0.0002  140 SER B CB    
3726 O  OG    . SER B 160 ? 0.3819 0.4078 0.4237 0.0188  0.0113  0.0042  140 SER B OG    
3727 N  N     . THR B 161 ? 0.3199 0.3463 0.3651 0.0268  0.0114  -0.0066 141 THR B N     
3728 C  CA    . THR B 161 ? 0.2885 0.3200 0.3370 0.0299  0.0115  -0.0122 141 THR B CA    
3729 C  C     . THR B 161 ? 0.3556 0.3896 0.4007 0.0268  0.0147  -0.0127 141 THR B C     
3730 O  O     . THR B 161 ? 0.3138 0.3570 0.3613 0.0272  0.0166  -0.0175 141 THR B O     
3731 C  CB    . THR B 161 ? 0.4466 0.4689 0.4956 0.0345  0.0072  -0.0135 141 THR B CB    
3732 O  OG1   . THR B 161 ? 0.4222 0.4419 0.4741 0.0372  0.0036  -0.0131 141 THR B OG1   
3733 C  CG2   . THR B 161 ? 0.4646 0.4911 0.5170 0.0383  0.0067  -0.0199 141 THR B CG2   
3734 N  N     . LEU B 162 ? 0.3244 0.3513 0.3640 0.0235  0.0154  -0.0080 142 LEU B N     
3735 C  CA    . LEU B 162 ? 0.3058 0.3338 0.3414 0.0202  0.0179  -0.0076 142 LEU B CA    
3736 C  C     . LEU B 162 ? 0.2445 0.2692 0.2757 0.0157  0.0188  -0.0023 142 LEU B C     
3737 O  O     . LEU B 162 ? 0.2658 0.2824 0.2937 0.0150  0.0179  0.0009  142 LEU B O     
3738 C  CB    . LEU B 162 ? 0.2996 0.3206 0.3335 0.0222  0.0165  -0.0086 142 LEU B CB    
3739 C  CG    . LEU B 162 ? 0.2743 0.2981 0.3050 0.0197  0.0188  -0.0098 142 LEU B CG    
3740 C  CD1   . LEU B 162 ? 0.2926 0.3284 0.3261 0.0196  0.0211  -0.0150 142 LEU B CD1   
3741 C  CD2   . LEU B 162 ? 0.2502 0.2664 0.2793 0.0218  0.0170  -0.0106 142 LEU B CD2   
3742 N  N     . PRO B 163 ? 0.2224 0.2532 0.2536 0.0124  0.0203  -0.0014 143 PRO B N     
3743 C  CA    . PRO B 163 ? 0.2722 0.2988 0.2996 0.0088  0.0201  0.0034  143 PRO B CA    
3744 C  C     . PRO B 163 ? 0.2341 0.2565 0.2564 0.0059  0.0206  0.0056  143 PRO B C     
3745 O  O     . PRO B 163 ? 0.2584 0.2852 0.2790 0.0036  0.0221  0.0041  143 PRO B O     
3746 C  CB    . PRO B 163 ? 0.3138 0.3486 0.3420 0.0056  0.0214  0.0031  143 PRO B CB    
3747 C  CG    . PRO B 163 ? 0.3473 0.3909 0.3811 0.0085  0.0220  -0.0018 143 PRO B CG    
3748 C  CD    . PRO B 163 ? 0.2901 0.3325 0.3251 0.0120  0.0218  -0.0051 143 PRO B CD    
3749 N  N     . GLY B 164 ? 0.2345 0.2490 0.2547 0.0059  0.0191  0.0089  144 GLY B N     
3750 C  CA    . GLY B 164 ? 0.2386 0.2485 0.2546 0.0036  0.0188  0.0111  144 GLY B CA    
3751 C  C     . GLY B 164 ? 0.2265 0.2328 0.2419 0.0053  0.0186  0.0101  144 GLY B C     
3752 O  O     . GLY B 164 ? 0.2333 0.2359 0.2457 0.0037  0.0180  0.0118  144 GLY B O     
3753 N  N     . PHE B 165 ? 0.2509 0.2577 0.2691 0.0086  0.0185  0.0074  145 PHE B N     
3754 C  CA    . PHE B 165 ? 0.2218 0.2250 0.2391 0.0098  0.0180  0.0064  145 PHE B CA    
3755 C  C     . PHE B 165 ? 0.2378 0.2341 0.2536 0.0098  0.0166  0.0093  145 PHE B C     
3756 O  O     . PHE B 165 ? 0.2328 0.2267 0.2462 0.0084  0.0165  0.0101  145 PHE B O     
3757 C  CB    . PHE B 165 ? 0.2376 0.2417 0.2580 0.0136  0.0174  0.0027  145 PHE B CB    
3758 C  CG    . PHE B 165 ? 0.2309 0.2296 0.2501 0.0149  0.0161  0.0019  145 PHE B CG    
3759 C  CD1   . PHE B 165 ? 0.2567 0.2561 0.2734 0.0133  0.0171  0.0009  145 PHE B CD1   
3760 C  CD2   . PHE B 165 ? 0.3010 0.2939 0.3213 0.0175  0.0136  0.0020  145 PHE B CD2   
3761 C  CE1   . PHE B 165 ? 0.2662 0.2604 0.2818 0.0145  0.0157  -0.0001 145 PHE B CE1   
3762 C  CE2   . PHE B 165 ? 0.2765 0.2638 0.2953 0.0183  0.0120  0.0013  145 PHE B CE2   
3763 C  CZ    . PHE B 165 ? 0.2420 0.2302 0.2587 0.0169  0.0131  0.0001  145 PHE B CZ    
3764 N  N     . LYS B 166 ? 0.2423 0.2359 0.2594 0.0111  0.0155  0.0106  146 LYS B N     
3765 C  CA    . LYS B 166 ? 0.2291 0.2178 0.2450 0.0108  0.0145  0.0128  146 LYS B CA    
3766 C  C     . LYS B 166 ? 0.2342 0.2227 0.2483 0.0086  0.0147  0.0147  146 LYS B C     
3767 O  O     . LYS B 166 ? 0.2192 0.2055 0.2322 0.0079  0.0143  0.0153  146 LYS B O     
3768 C  CB    . LYS B 166 ? 0.2154 0.2020 0.2324 0.0120  0.0134  0.0139  146 LYS B CB    
3769 C  CG    . LYS B 166 ? 0.2636 0.2467 0.2792 0.0109  0.0126  0.0159  146 LYS B CG    
3770 C  CD    . LYS B 166 ? 0.2837 0.2645 0.2993 0.0115  0.0113  0.0168  146 LYS B CD    
3771 C  CE    . LYS B 166 ? 0.2868 0.2655 0.3006 0.0097  0.0108  0.0187  146 LYS B CE    
3772 N  NZ    . LYS B 166 ? 0.3473 0.3288 0.3611 0.0086  0.0120  0.0194  146 LYS B NZ    
3773 N  N     . PRO B 167 ? 0.1993 0.1896 0.2132 0.0075  0.0149  0.0157  147 PRO B N     
3774 C  CA    . PRO B 167 ? 0.2523 0.2411 0.2645 0.0059  0.0141  0.0172  147 PRO B CA    
3775 C  C     . PRO B 167 ? 0.2410 0.2295 0.2508 0.0043  0.0139  0.0170  147 PRO B C     
3776 O  O     . PRO B 167 ? 0.2220 0.2082 0.2310 0.0038  0.0127  0.0178  147 PRO B O     
3777 C  CB    . PRO B 167 ? 0.2492 0.2393 0.2612 0.0049  0.0137  0.0180  147 PRO B CB    
3778 C  CG    . PRO B 167 ? 0.2725 0.2646 0.2868 0.0065  0.0144  0.0173  147 PRO B CG    
3779 C  CD    . PRO B 167 ? 0.2182 0.2115 0.2335 0.0078  0.0152  0.0154  147 PRO B CD    
3780 N  N     . THR B 168 ? 0.2183 0.2098 0.2273 0.0033  0.0151  0.0157  148 THR B N     
3781 C  CA    . THR B 168 ? 0.2166 0.2080 0.2227 0.0013  0.0150  0.0155  148 THR B CA    
3782 C  C     . THR B 168 ? 0.2326 0.2213 0.2390 0.0026  0.0146  0.0149  148 THR B C     
3783 O  O     . THR B 168 ? 0.2270 0.2134 0.2314 0.0014  0.0134  0.0158  148 THR B O     
3784 C  CB    . THR B 168 ? 0.2505 0.2470 0.2557 -0.0002 0.0167  0.0136  148 THR B CB    
3785 O  OG1   . THR B 168 ? 0.2710 0.2706 0.2757 -0.0021 0.0171  0.0144  148 THR B OG1   
3786 C  CG2   . THR B 168 ? 0.2603 0.2568 0.2615 -0.0029 0.0166  0.0135  148 THR B CG2   
3787 N  N     . PHE B 169 ? 0.2287 0.2171 0.2372 0.0048  0.0152  0.0134  149 PHE B N     
3788 C  CA    . PHE B 169 ? 0.1914 0.1768 0.1999 0.0056  0.0145  0.0131  149 PHE B CA    
3789 C  C     . PHE B 169 ? 0.2302 0.2134 0.2390 0.0052  0.0133  0.0150  149 PHE B C     
3790 O  O     . PHE B 169 ? 0.2355 0.2175 0.2434 0.0043  0.0126  0.0152  149 PHE B O     
3791 C  CB    . PHE B 169 ? 0.2057 0.1899 0.2161 0.0079  0.0143  0.0117  149 PHE B CB    
3792 C  CG    . PHE B 169 ? 0.2378 0.2185 0.2475 0.0083  0.0133  0.0108  149 PHE B CG    
3793 C  CD1   . PHE B 169 ? 0.2204 0.1982 0.2296 0.0073  0.0123  0.0126  149 PHE B CD1   
3794 C  CD2   . PHE B 169 ? 0.2472 0.2280 0.2568 0.0097  0.0132  0.0079  149 PHE B CD2   
3795 C  CE1   . PHE B 169 ? 0.2349 0.2090 0.2429 0.0070  0.0110  0.0120  149 PHE B CE1   
3796 C  CE2   . PHE B 169 ? 0.2389 0.2153 0.2474 0.0100  0.0117  0.0070  149 PHE B CE2   
3797 C  CZ    . PHE B 169 ? 0.2338 0.2065 0.2413 0.0084  0.0105  0.0094  149 PHE B CZ    
3798 N  N     . GLU B 170 ? 0.2221 0.2056 0.2325 0.0058  0.0132  0.0160  150 GLU B N     
3799 C  CA    . GLU B 170 ? 0.2162 0.1992 0.2274 0.0057  0.0123  0.0170  150 GLU B CA    
3800 C  C     . GLU B 170 ? 0.2353 0.2182 0.2457 0.0049  0.0110  0.0174  150 GLU B C     
3801 O  O     . GLU B 170 ? 0.2450 0.2278 0.2561 0.0047  0.0100  0.0173  150 GLU B O     
3802 C  CB    . GLU B 170 ? 0.2491 0.2330 0.2618 0.0065  0.0126  0.0175  150 GLU B CB    
3803 C  CG    . GLU B 170 ? 0.2266 0.2096 0.2397 0.0069  0.0129  0.0175  150 GLU B CG    
3804 C  CD    . GLU B 170 ? 0.4367 0.4205 0.4506 0.0076  0.0131  0.0181  150 GLU B CD    
3805 O  OE1   . GLU B 170 ? 0.3889 0.3738 0.4030 0.0079  0.0132  0.0181  150 GLU B OE1   
3806 O  OE2   . GLU B 170 ? 0.4761 0.4590 0.4897 0.0073  0.0128  0.0187  150 GLU B OE2   
3807 N  N     . ASP B 171 ? 0.2323 0.2150 0.2412 0.0041  0.0106  0.0179  151 ASP B N     
3808 C  CA    . ASP B 171 ? 0.2230 0.2040 0.2303 0.0031  0.0083  0.0187  151 ASP B CA    
3809 C  C     . ASP B 171 ? 0.2407 0.2207 0.2461 0.0018  0.0076  0.0186  151 ASP B C     
3810 O  O     . ASP B 171 ? 0.2455 0.2240 0.2511 0.0019  0.0053  0.0187  151 ASP B O     
3811 C  CB    . ASP B 171 ? 0.2270 0.2074 0.2320 0.0015  0.0076  0.0197  151 ASP B CB    
3812 C  CG    . ASP B 171 ? 0.3110 0.2913 0.3177 0.0027  0.0071  0.0200  151 ASP B CG    
3813 O  OD1   . ASP B 171 ? 0.3155 0.2963 0.3250 0.0048  0.0070  0.0192  151 ASP B OD1   
3814 O  OD2   . ASP B 171 ? 0.3302 0.3103 0.3352 0.0012  0.0069  0.0209  151 ASP B OD2   
3815 N  N     . LEU B 172 ? 0.2135 0.1945 0.2172 0.0008  0.0093  0.0179  152 LEU B N     
3816 C  CA    . LEU B 172 ? 0.1987 0.1786 0.1999 -0.0006 0.0086  0.0176  152 LEU B CA    
3817 C  C     . LEU B 172 ? 0.2193 0.1987 0.2227 0.0006  0.0082  0.0170  152 LEU B C     
3818 O  O     . LEU B 172 ? 0.2292 0.2074 0.2319 -0.0001 0.0063  0.0173  152 LEU B O     
3819 C  CB    . LEU B 172 ? 0.2136 0.1956 0.2126 -0.0017 0.0106  0.0162  152 LEU B CB    
3820 C  CG    . LEU B 172 ? 0.2165 0.1976 0.2124 -0.0034 0.0100  0.0156  152 LEU B CG    
3821 C  CD1   . LEU B 172 ? 0.2151 0.1936 0.2079 -0.0057 0.0072  0.0176  152 LEU B CD1   
3822 C  CD2   . LEU B 172 ? 0.2377 0.2221 0.2313 -0.0046 0.0122  0.0136  152 LEU B CD2   
3823 N  N     . CYS B 173 ? 0.2060 0.1861 0.2117 0.0019  0.0096  0.0163  153 CYS B N     
3824 C  CA    . CYS B 173 ? 0.1961 0.1760 0.2034 0.0020  0.0091  0.0161  153 CYS B CA    
3825 C  C     . CYS B 173 ? 0.2386 0.2200 0.2483 0.0024  0.0076  0.0165  153 CYS B C     
3826 O  O     . CYS B 173 ? 0.2217 0.2036 0.2322 0.0019  0.0064  0.0162  153 CYS B O     
3827 C  CB    . CYS B 173 ? 0.2445 0.2241 0.2529 0.0027  0.0103  0.0158  153 CYS B CB    
3828 S  SG    . CYS B 173 ? 0.2613 0.2388 0.2678 0.0031  0.0109  0.0142  153 CYS B SG    
3829 N  N     . ARG B 174 ? 0.1952 0.1776 0.2063 0.0035  0.0074  0.0167  154 ARG B N     
3830 C  CA    . ARG B 174 ? 0.2089 0.1931 0.2228 0.0046  0.0057  0.0161  154 ARG B CA    
3831 C  C     . ARG B 174 ? 0.2505 0.2329 0.2635 0.0043  0.0027  0.0162  154 ARG B C     
3832 O  O     . ARG B 174 ? 0.2389 0.2232 0.2544 0.0050  0.0010  0.0151  154 ARG B O     
3833 C  CB    . ARG B 174 ? 0.2261 0.2112 0.2414 0.0060  0.0056  0.0160  154 ARG B CB    
3834 C  CG    . ARG B 174 ? 0.2351 0.2225 0.2537 0.0078  0.0035  0.0144  154 ARG B CG    
3835 C  CD    . ARG B 174 ? 0.2444 0.2330 0.2645 0.0094  0.0035  0.0137  154 ARG B CD    
3836 N  NE    . ARG B 174 ? 0.2661 0.2571 0.2864 0.0088  0.0065  0.0139  154 ARG B NE    
3837 C  CZ    . ARG B 174 ? 0.2645 0.2601 0.2869 0.0084  0.0079  0.0128  154 ARG B CZ    
3838 N  NH1   . ARG B 174 ? 0.2798 0.2796 0.3051 0.0087  0.0070  0.0110  154 ARG B NH1   
3839 N  NH2   . ARG B 174 ? 0.3278 0.3243 0.3493 0.0073  0.0100  0.0136  154 ARG B NH2   
3840 N  N     . LEU B 175 ? 0.2144 0.1934 0.2235 0.0031  0.0018  0.0174  155 LEU B N     
3841 C  CA    . LEU B 175 ? 0.2270 0.2032 0.2339 0.0022  -0.0015 0.0180  155 LEU B CA    
3842 C  C     . LEU B 175 ? 0.2664 0.2431 0.2731 0.0013  -0.0017 0.0175  155 LEU B C     
3843 O  O     . LEU B 175 ? 0.2316 0.2083 0.2398 0.0018  -0.0046 0.0170  155 LEU B O     
3844 C  CB    . LEU B 175 ? 0.2439 0.2170 0.2455 -0.0002 -0.0018 0.0196  155 LEU B CB    
3845 C  CG    . LEU B 175 ? 0.2411 0.2099 0.2385 -0.0023 -0.0058 0.0211  155 LEU B CG    
3846 C  CD1   . LEU B 175 ? 0.3050 0.2718 0.2976 -0.0051 -0.0058 0.0228  155 LEU B CD1   
3847 C  CD2   . LEU B 175 ? 0.2858 0.2543 0.2807 -0.0041 -0.0060 0.0210  155 LEU B CD2   
3848 N  N     . ILE B 176 ? 0.2240 0.2013 0.2291 0.0001  0.0011  0.0173  156 ILE B N     
3849 C  CA    . ILE B 176 ? 0.1967 0.1738 0.2011 -0.0010 0.0008  0.0168  156 ILE B CA    
3850 C  C     . ILE B 176 ? 0.2504 0.2306 0.2593 -0.0001 0.0004  0.0159  156 ILE B C     
3851 O  O     . ILE B 176 ? 0.2134 0.1941 0.2230 -0.0006 -0.0017 0.0155  156 ILE B O     
3852 C  CB    . ILE B 176 ? 0.1962 0.1728 0.1981 -0.0020 0.0034  0.0162  156 ILE B CB    
3853 C  CG1   . ILE B 176 ? 0.2034 0.1787 0.2007 -0.0035 0.0038  0.0166  156 ILE B CG1   
3854 C  CG2   . ILE B 176 ? 0.2383 0.2143 0.2398 -0.0029 0.0029  0.0155  156 ILE B CG2   
3855 C  CD1   . ILE B 176 ? 0.2424 0.2185 0.2381 -0.0036 0.0065  0.0150  156 ILE B CD1   
3856 N  N     . ILE B 177 ? 0.2055 0.1886 0.2175 0.0009  0.0022  0.0154  157 ILE B N     
3857 C  CA    . ILE B 177 ? 0.1885 0.1760 0.2044 0.0009  0.0022  0.0144  157 ILE B CA    
3858 C  C     . ILE B 177 ? 0.1949 0.1854 0.2145 0.0026  -0.0004 0.0132  157 ILE B C     
3859 O  O     . ILE B 177 ? 0.2121 0.2065 0.2347 0.0024  -0.0016 0.0120  157 ILE B O     
3860 C  CB    . ILE B 177 ? 0.1861 0.1758 0.2033 0.0008  0.0047  0.0145  157 ILE B CB    
3861 C  CG1   . ILE B 177 ? 0.2015 0.1875 0.2154 -0.0006 0.0063  0.0153  157 ILE B CG1   
3862 C  CG2   . ILE B 177 ? 0.1973 0.1931 0.2183 0.0000  0.0049  0.0134  157 ILE B CG2   
3863 C  CD1   . ILE B 177 ? 0.2427 0.2288 0.2566 -0.0006 0.0080  0.0159  157 ILE B CD1   
3864 N  N     . ASP B 178 ? 0.2058 0.1946 0.2254 0.0045  -0.0019 0.0132  158 ASP B N     
3865 C  CA    . ASP B 178 ? 0.2142 0.2045 0.2372 0.0067  -0.0056 0.0116  158 ASP B CA    
3866 C  C     . ASP B 178 ? 0.2021 0.1907 0.2244 0.0060  -0.0087 0.0117  158 ASP B C     
3867 O  O     . ASP B 178 ? 0.2123 0.2051 0.2391 0.0074  -0.0110 0.0097  158 ASP B O     
3868 C  CB    . ASP B 178 ? 0.2099 0.1958 0.2313 0.0083  -0.0078 0.0122  158 ASP B CB    
3869 C  CG    . ASP B 178 ? 0.2820 0.2705 0.3056 0.0099  -0.0059 0.0112  158 ASP B CG    
3870 O  OD1   . ASP B 178 ? 0.2648 0.2595 0.2919 0.0102  -0.0034 0.0096  158 ASP B OD1   
3871 O  OD2   . ASP B 178 ? 0.2931 0.2774 0.3145 0.0104  -0.0071 0.0121  158 ASP B OD2   
3872 N  N     . VAL B 179 ? 0.1990 0.1821 0.2156 0.0038  -0.0090 0.0138  159 VAL B N     
3873 C  CA    . VAL B 179 ? 0.2127 0.1938 0.2277 0.0028  -0.0120 0.0141  159 VAL B CA    
3874 C  C     . VAL B 179 ? 0.2212 0.2069 0.2388 0.0017  -0.0106 0.0131  159 VAL B C     
3875 O  O     . VAL B 179 ? 0.2264 0.2140 0.2465 0.0020  -0.0135 0.0121  159 VAL B O     
3876 C  CB    . VAL B 179 ? 0.2154 0.1905 0.2232 0.0001  -0.0123 0.0164  159 VAL B CB    
3877 C  CG1   . VAL B 179 ? 0.2288 0.2016 0.2343 -0.0014 -0.0159 0.0168  159 VAL B CG1   
3878 C  CG2   . VAL B 179 ? 0.2543 0.2252 0.2591 0.0002  -0.0140 0.0178  159 VAL B CG2   
3879 N  N     . ALA B 180 ? 0.2141 0.2011 0.2310 0.0002  -0.0066 0.0133  160 ALA B N     
3880 C  CA    . ALA B 180 ? 0.2155 0.2059 0.2341 -0.0015 -0.0056 0.0127  160 ALA B CA    
3881 C  C     . ALA B 180 ? 0.2176 0.2157 0.2428 -0.0004 -0.0065 0.0106  160 ALA B C     
3882 O  O     . ALA B 180 ? 0.2073 0.2088 0.2345 -0.0017 -0.0075 0.0098  160 ALA B O     
3883 C  CB    . ALA B 180 ? 0.2031 0.1925 0.2196 -0.0030 -0.0020 0.0134  160 ALA B CB    
3884 N  N     . VAL B 181 ? 0.2176 0.2192 0.2461 0.0018  -0.0059 0.0094  161 VAL B N     
3885 C  CA    . VAL B 181 ? 0.2110 0.2216 0.2463 0.0031  -0.0065 0.0065  161 VAL B CA    
3886 C  C     . VAL B 181 ? 0.1915 0.2031 0.2299 0.0051  -0.0111 0.0048  161 VAL B C     
3887 O  O     . VAL B 181 ? 0.2130 0.2322 0.2565 0.0050  -0.0120 0.0025  161 VAL B O     
3888 C  CB    . VAL B 181 ? 0.2133 0.2270 0.2512 0.0055  -0.0053 0.0051  161 VAL B CB    
3889 C  CG1   . VAL B 181 ? 0.2278 0.2517 0.2732 0.0076  -0.0064 0.0010  161 VAL B CG1   
3890 C  CG2   . VAL B 181 ? 0.2242 0.2379 0.2594 0.0031  -0.0010 0.0066  161 VAL B CG2   
3891 N  N     . LEU B 182 ? 0.2197 0.2238 0.2550 0.0067  -0.0145 0.0060  162 LEU B N     
3892 C  CA    . LEU B 182 ? 0.2375 0.2410 0.2750 0.0085  -0.0199 0.0048  162 LEU B CA    
3893 C  C     . LEU B 182 ? 0.2072 0.2103 0.2430 0.0057  -0.0207 0.0057  162 LEU B C     
3894 O  O     . LEU B 182 ? 0.2269 0.2341 0.2670 0.0067  -0.0241 0.0037  162 LEU B O     
3895 C  CB    . LEU B 182 ? 0.2308 0.2249 0.2637 0.0099  -0.0239 0.0065  162 LEU B CB    
3896 C  CG    . LEU B 182 ? 0.2373 0.2313 0.2723 0.0130  -0.0244 0.0052  162 LEU B CG    
3897 C  CD1   . LEU B 182 ? 0.3181 0.3018 0.3471 0.0129  -0.0281 0.0078  162 LEU B CD1   
3898 C  CD2   . LEU B 182 ? 0.2794 0.2809 0.3230 0.0172  -0.0273 0.0006  162 LEU B CD2   
3899 N  N     . VAL B 183 ? 0.2177 0.2159 0.2472 0.0023  -0.0179 0.0084  163 VAL B N     
3900 C  CA    . VAL B 183 ? 0.2040 0.2015 0.2314 -0.0005 -0.0184 0.0091  163 VAL B CA    
3901 C  C     . VAL B 183 ? 0.2299 0.2363 0.2628 -0.0017 -0.0168 0.0072  163 VAL B C     
3902 O  O     . VAL B 183 ? 0.2177 0.2275 0.2532 -0.0025 -0.0192 0.0062  163 VAL B O     
3903 C  CB    . VAL B 183 ? 0.2173 0.2081 0.2372 -0.0034 -0.0157 0.0115  163 VAL B CB    
3904 C  CG1   . VAL B 183 ? 0.2365 0.2266 0.2543 -0.0063 -0.0160 0.0118  163 VAL B CG1   
3905 C  CG2   . VAL B 183 ? 0.2283 0.2116 0.2424 -0.0031 -0.0176 0.0132  163 VAL B CG2   
3906 N  N     . ALA B 184 ? 0.2249 0.2357 0.2596 -0.0024 -0.0129 0.0068  164 ALA B N     
3907 C  CA    . ALA B 184 ? 0.2135 0.2338 0.2530 -0.0044 -0.0111 0.0052  164 ALA B CA    
3908 C  C     . ALA B 184 ? 0.2413 0.2711 0.2889 -0.0019 -0.0139 0.0015  164 ALA B C     
3909 O  O     . ALA B 184 ? 0.2258 0.2632 0.2772 -0.0039 -0.0143 0.0000  164 ALA B O     
3910 C  CB    . ALA B 184 ? 0.1920 0.2147 0.2312 -0.0055 -0.0070 0.0055  164 ALA B CB    
3911 N  N     . ARG B 185 ? 0.1937 0.2234 0.2441 0.0026  -0.0160 -0.0002 165 ARG B N     
3912 C  CA    . ARG B 185 ? 0.1948 0.2331 0.2534 0.0061  -0.0195 -0.0045 165 ARG B CA    
3913 C  C     . ARG B 185 ? 0.2364 0.2734 0.2958 0.0062  -0.0241 -0.0047 165 ARG B C     
3914 O  O     . ARG B 185 ? 0.2185 0.2656 0.2849 0.0065  -0.0256 -0.0079 165 ARG B O     
3915 C  CB    . ARG B 185 ? 0.2176 0.2532 0.2778 0.0112  -0.0219 -0.0061 165 ARG B CB    
3916 C  CG    . ARG B 185 ? 0.2945 0.3376 0.3634 0.0160  -0.0266 -0.0112 165 ARG B CG    
3917 C  CD    . ARG B 185 ? 0.3554 0.3930 0.4246 0.0209  -0.0299 -0.0124 165 ARG B CD    
3918 N  NE    . ARG B 185 ? 0.4196 0.4598 0.4884 0.0209  -0.0253 -0.0129 165 ARG B NE    
3919 C  CZ    . ARG B 185 ? 0.5482 0.5829 0.6159 0.0241  -0.0268 -0.0132 165 ARG B CZ    
3920 N  NH1   . ARG B 185 ? 0.4705 0.4963 0.5369 0.0274  -0.0331 -0.0130 165 ARG B NH1   
3921 N  NH2   . ARG B 185 ? 0.5215 0.5591 0.5887 0.0236  -0.0224 -0.0135 165 ARG B NH2   
3922 N  N     . ALA B 186 ? 0.2047 0.2301 0.2571 0.0054  -0.0264 -0.0013 166 ALA B N     
3923 C  CA    . ALA B 186 ? 0.2056 0.2290 0.2577 0.0048  -0.0309 -0.0011 166 ALA B CA    
3924 C  C     . ALA B 186 ? 0.2268 0.2556 0.2794 0.0004  -0.0286 -0.0008 166 ALA B C     
3925 O  O     . ALA B 186 ? 0.2285 0.2632 0.2859 0.0004  -0.0316 -0.0028 166 ALA B O     
3926 C  CB    . ALA B 186 ? 0.2581 0.2683 0.3012 0.0040  -0.0332 0.0027  166 ALA B CB    
3927 N  N     . CYS B 187 ? 0.2309 0.2574 0.2786 -0.0034 -0.0237 0.0015  167 CYS B N     
3928 C  CA    . CYS B 187 ? 0.2032 0.2341 0.2510 -0.0080 -0.0218 0.0019  167 CYS B CA    
3929 C  C     . CYS B 187 ? 0.2377 0.2830 0.2943 -0.0083 -0.0212 -0.0017 167 CYS B C     
3930 O  O     . CYS B 187 ? 0.2487 0.2998 0.3079 -0.0112 -0.0222 -0.0025 167 CYS B O     
3931 C  CB    . CYS B 187 ? 0.2299 0.2554 0.2713 -0.0115 -0.0173 0.0046  167 CYS B CB    
3932 S  SG    . CYS B 187 ? 0.2360 0.2468 0.2672 -0.0119 -0.0173 0.0079  167 CYS B SG    
3933 N  N     . ASP B 188 ? 0.1971 0.2491 0.2583 -0.0059 -0.0193 -0.0040 168 ASP B N     
3934 C  CA    . ASP B 188 ? 0.1963 0.2640 0.2664 -0.0060 -0.0185 -0.0082 168 ASP B CA    
3935 C  C     . ASP B 188 ? 0.2207 0.2948 0.2984 -0.0025 -0.0237 -0.0119 168 ASP B C     
3936 O  O     . ASP B 188 ? 0.2132 0.2998 0.2973 -0.0044 -0.0237 -0.0147 168 ASP B O     
3937 C  CB    . ASP B 188 ? 0.2133 0.2867 0.2868 -0.0033 -0.0160 -0.0106 168 ASP B CB    
3938 C  CG    . ASP B 188 ? 0.2274 0.2995 0.2958 -0.0076 -0.0106 -0.0079 168 ASP B CG    
3939 O  OD1   . ASP B 188 ? 0.2352 0.3070 0.2999 -0.0134 -0.0088 -0.0054 168 ASP B OD1   
3940 O  OD2   . ASP B 188 ? 0.2218 0.2927 0.2896 -0.0053 -0.0089 -0.0082 168 ASP B OD2   
3941 N  N     . ARG B 189 ? 0.2081 0.2742 0.2852 0.0025  -0.0284 -0.0121 169 ARG B N     
3942 C  CA    . ARG B 189 ? 0.2080 0.2789 0.2920 0.0062  -0.0345 -0.0156 169 ARG B CA    
3943 C  C     . ARG B 189 ? 0.2443 0.3158 0.3273 0.0021  -0.0360 -0.0141 169 ARG B C     
3944 O  O     . ARG B 189 ? 0.2384 0.3217 0.3294 0.0023  -0.0380 -0.0178 169 ARG B O     
3945 C  CB    . ARG B 189 ? 0.2756 0.3346 0.3569 0.0112  -0.0401 -0.0148 169 ARG B CB    
3946 C  CG    . ARG B 189 ? 0.3055 0.3646 0.3896 0.0162  -0.0406 -0.0172 169 ARG B CG    
3947 C  CD    . ARG B 189 ? 0.4806 0.5251 0.5594 0.0195  -0.0465 -0.0150 169 ARG B CD    
3948 N  NE    . ARG B 189 ? 0.5744 0.6155 0.6541 0.0208  -0.0535 -0.0152 169 ARG B NE    
3949 C  CZ    . ARG B 189 ? 0.5796 0.6067 0.6513 0.0203  -0.0581 -0.0113 169 ARG B CZ    
3950 N  NH1   . ARG B 189 ? 0.4360 0.4519 0.4984 0.0183  -0.0560 -0.0070 169 ARG B NH1   
3951 N  NH2   . ARG B 189 ? 0.5611 0.5859 0.6340 0.0214  -0.0649 -0.0117 169 ARG B NH2   
3952 N  N     . PHE B 190 ? 0.2232 0.2826 0.2964 -0.0017 -0.0349 -0.0092 170 PHE B N     
3953 C  CA    . PHE B 190 ? 0.2269 0.2855 0.2978 -0.0061 -0.0361 -0.0076 170 PHE B CA    
3954 C  C     . PHE B 190 ? 0.2420 0.3131 0.3171 -0.0109 -0.0324 -0.0090 170 PHE B C     
3955 O  O     . PHE B 190 ? 0.2312 0.3105 0.3113 -0.0125 -0.0347 -0.0109 170 PHE B O     
3956 C  CB    . PHE B 190 ? 0.2546 0.2984 0.3139 -0.0091 -0.0349 -0.0027 170 PHE B CB    
3957 C  CG    . PHE B 190 ? 0.2426 0.2847 0.2984 -0.0140 -0.0354 -0.0011 170 PHE B CG    
3958 C  CD1   . PHE B 190 ? 0.2602 0.3046 0.3139 -0.0193 -0.0312 0.0001  170 PHE B CD1   
3959 C  CD2   . PHE B 190 ? 0.2781 0.3153 0.3320 -0.0137 -0.0405 -0.0006 170 PHE B CD2   
3960 C  CE1   . PHE B 190 ? 0.3218 0.3638 0.3720 -0.0238 -0.0321 0.0015  170 PHE B CE1   
3961 C  CE2   . PHE B 190 ? 0.3432 0.3787 0.3937 -0.0183 -0.0411 0.0007  170 PHE B CE2   
3962 C  CZ    . PHE B 190 ? 0.3062 0.3440 0.3550 -0.0232 -0.0369 0.0017  170 PHE B CZ    
3963 N  N     . ALA B 191 ? 0.2116 0.2841 0.2843 -0.0137 -0.0270 -0.0078 171 ALA B N     
3964 C  CA    . ALA B 191 ? 0.2556 0.3383 0.3303 -0.0197 -0.0236 -0.0081 171 ALA B CA    
3965 C  C     . ALA B 191 ? 0.2275 0.3290 0.3137 -0.0186 -0.0239 -0.0136 171 ALA B C     
3966 O  O     . ALA B 191 ? 0.2407 0.3525 0.3304 -0.0233 -0.0235 -0.0147 171 ALA B O     
3967 C  CB    . ALA B 191 ? 0.2305 0.3094 0.2994 -0.0228 -0.0184 -0.0055 171 ALA B CB    
3968 N  N     . GLU B 192 ? 0.2062 0.3127 0.2984 -0.0125 -0.0247 -0.0173 172 GLU B N     
3969 C  CA    . GLU B 192 ? 0.2365 0.3618 0.3405 -0.0103 -0.0253 -0.0237 172 GLU B CA    
3970 C  C     . GLU B 192 ? 0.2312 0.3615 0.3415 -0.0085 -0.0308 -0.0263 172 GLU B C     
3971 O  O     . GLU B 192 ? 0.2306 0.3781 0.3500 -0.0097 -0.0308 -0.0309 172 GLU B O     
3972 C  CB    . GLU B 192 ? 0.2144 0.3416 0.3229 -0.0031 -0.0259 -0.0274 172 GLU B CB    
3973 C  CG    . GLU B 192 ? 0.2394 0.3663 0.3440 -0.0050 -0.0201 -0.0261 172 GLU B CG    
3974 C  CD    . GLU B 192 ? 0.3095 0.4310 0.4148 0.0020  -0.0214 -0.0279 172 GLU B CD    
3975 O  OE1   . GLU B 192 ? 0.3259 0.4475 0.4368 0.0085  -0.0268 -0.0315 172 GLU B OE1   
3976 O  OE2   . GLU B 192 ? 0.2479 0.3642 0.3477 0.0008  -0.0175 -0.0255 172 GLU B OE2   
3977 N  N     . LYS B 193 ? 0.2281 0.3441 0.3334 -0.0061 -0.0356 -0.0235 173 LYS B N     
3978 C  CA    . LYS B 193 ? 0.2384 0.3583 0.3490 -0.0050 -0.0413 -0.0256 173 LYS B CA    
3979 C  C     . LYS B 193 ? 0.2413 0.3617 0.3482 -0.0124 -0.0403 -0.0227 173 LYS B C     
3980 O  O     . LYS B 193 ? 0.3005 0.4304 0.4141 -0.0129 -0.0436 -0.0254 173 LYS B O     
3981 C  CB    . LYS B 193 ? 0.3043 0.4092 0.4109 0.0002  -0.0477 -0.0239 173 LYS B CB    
3982 C  CG    . LYS B 193 ? 0.3523 0.4579 0.4647 0.0083  -0.0514 -0.0279 173 LYS B CG    
3983 C  CD    . LYS B 193 ? 0.6446 0.7340 0.7516 0.0120  -0.0583 -0.0254 173 LYS B CD    
3984 C  CE    . LYS B 193 ? 0.6975 0.7869 0.8105 0.0201  -0.0636 -0.0296 173 LYS B CE    
3985 N  NZ    . LYS B 193 ? 0.8139 0.8876 0.9215 0.0230  -0.0715 -0.0270 173 LYS B NZ    
3986 N  N     . GLN B 194 ? 0.2637 0.3741 0.3604 -0.0181 -0.0362 -0.0174 174 GLN B N     
3987 C  CA    . GLN B 194 ? 0.2504 0.3567 0.3417 -0.0245 -0.0364 -0.0142 174 GLN B CA    
3988 C  C     . GLN B 194 ? 0.2639 0.3784 0.3544 -0.0324 -0.0316 -0.0132 174 GLN B C     
3989 O  O     . GLN B 194 ? 0.2694 0.3843 0.3578 -0.0380 -0.0326 -0.0117 174 GLN B O     
3990 C  CB    . GLN B 194 ? 0.2694 0.3556 0.3484 -0.0251 -0.0369 -0.0090 174 GLN B CB    
3991 C  CG    . GLN B 194 ? 0.2718 0.3486 0.3495 -0.0192 -0.0422 -0.0090 174 GLN B CG    
3992 C  CD    . GLN B 194 ? 0.3204 0.3985 0.4004 -0.0196 -0.0478 -0.0098 174 GLN B CD    
3993 O  OE1   . GLN B 194 ? 0.4096 0.4920 0.4896 -0.0249 -0.0474 -0.0093 174 GLN B OE1   
3994 N  NE2   . GLN B 194 ? 0.3437 0.4185 0.4260 -0.0141 -0.0536 -0.0111 174 GLN B NE2   
3995 N  N     . ILE B 195 ? 0.2499 0.3708 0.3415 -0.0335 -0.0269 -0.0139 175 ILE B N     
3996 C  CA    . ILE B 195 ? 0.2761 0.4016 0.3643 -0.0418 -0.0225 -0.0118 175 ILE B CA    
3997 C  C     . ILE B 195 ? 0.2058 0.3530 0.3039 -0.0435 -0.0200 -0.0166 175 ILE B C     
3998 O  O     . ILE B 195 ? 0.2583 0.4113 0.3602 -0.0395 -0.0178 -0.0194 175 ILE B O     
3999 C  CB    . ILE B 195 ? 0.2886 0.4006 0.3671 -0.0431 -0.0191 -0.0075 175 ILE B CB    
4000 C  CG1   . ILE B 195 ? 0.2368 0.3291 0.3060 -0.0414 -0.0214 -0.0036 175 ILE B CG1   
4001 C  CG2   . ILE B 195 ? 0.2706 0.3866 0.3451 -0.0519 -0.0155 -0.0052 175 ILE B CG2   
4002 C  CD1   . ILE B 195 ? 0.3005 0.3798 0.3611 -0.0415 -0.0184 -0.0001 175 ILE B CD1   
4003 N  N     . ALA B 196 ? 0.2835 0.4433 0.3854 -0.0498 -0.0201 -0.0178 176 ALA B N     
4004 C  CA    . ALA B 196 ? 0.2556 0.4380 0.3668 -0.0524 -0.0172 -0.0226 176 ALA B CA    
4005 C  C     . ALA B 196 ? 0.2436 0.4273 0.3493 -0.0578 -0.0117 -0.0204 176 ALA B C     
4006 O  O     . ALA B 196 ? 0.3728 0.5450 0.4682 -0.0645 -0.0104 -0.0147 176 ALA B O     
4007 C  CB    . ALA B 196 ? 0.3298 0.5254 0.4455 -0.0592 -0.0185 -0.0238 176 ALA B CB    
4008 N  N     . GLY B 197 ? 0.2532 0.4506 0.3658 -0.0547 -0.0089 -0.0252 177 GLY B N     
4009 C  CA    . GLY B 197 ? 0.3165 0.5169 0.4244 -0.0597 -0.0038 -0.0237 177 GLY B CA    
4010 C  C     . GLY B 197 ? 0.2834 0.4661 0.3833 -0.0555 -0.0027 -0.0201 177 GLY B C     
4011 O  O     . GLY B 197 ? 0.2958 0.4796 0.3914 -0.0593 0.0011  -0.0186 177 GLY B O     
4012 N  N     . TYR B 198 ? 0.2738 0.4408 0.3716 -0.0481 -0.0062 -0.0189 178 TYR B N     
4013 C  CA    . TYR B 198 ? 0.2629 0.4135 0.3534 -0.0443 -0.0053 -0.0156 178 TYR B CA    
4014 C  C     . TYR B 198 ? 0.2740 0.4338 0.3693 -0.0400 -0.0025 -0.0196 178 TYR B C     
4015 O  O     . TYR B 198 ? 0.2800 0.4543 0.3857 -0.0353 -0.0035 -0.0260 178 TYR B O     
4016 C  CB    . TYR B 198 ? 0.2348 0.3701 0.3233 -0.0374 -0.0096 -0.0144 178 TYR B CB    
4017 C  CG    . TYR B 198 ? 0.2516 0.3694 0.3319 -0.0342 -0.0089 -0.0107 178 TYR B CG    
4018 C  CD1   . TYR B 198 ? 0.2756 0.3792 0.3457 -0.0386 -0.0081 -0.0052 178 TYR B CD1   
4019 C  CD2   . TYR B 198 ? 0.1944 0.3101 0.2774 -0.0267 -0.0095 -0.0129 178 TYR B CD2   
4020 C  CE1   . TYR B 198 ? 0.2411 0.3300 0.3044 -0.0355 -0.0075 -0.0023 178 TYR B CE1   
4021 C  CE2   . TYR B 198 ? 0.2314 0.3321 0.3071 -0.0242 -0.0089 -0.0095 178 TYR B CE2   
4022 C  CZ    . TYR B 198 ? 0.2697 0.3578 0.3359 -0.0286 -0.0077 -0.0044 178 TYR B CZ    
4023 O  OH    . TYR B 198 ? 0.2428 0.3176 0.3026 -0.0259 -0.0070 -0.0017 178 TYR B OH    
4024 N  N     . PRO B 199 ? 0.2610 0.4135 0.3495 -0.0416 0.0006  -0.0166 179 PRO B N     
4025 C  CA    . PRO B 199 ? 0.2826 0.4428 0.3750 -0.0374 0.0031  -0.0204 179 PRO B CA    
4026 C  C     . PRO B 199 ? 0.2789 0.4291 0.3731 -0.0276 0.0000  -0.0218 179 PRO B C     
4027 O  O     . PRO B 199 ? 0.2540 0.3864 0.3406 -0.0259 -0.0011 -0.0172 179 PRO B O     
4028 C  CB    . PRO B 199 ? 0.3130 0.4655 0.3957 -0.0431 0.0067  -0.0154 179 PRO B CB    
4029 C  CG    . PRO B 199 ? 0.3606 0.5020 0.4349 -0.0500 0.0057  -0.0095 179 PRO B CG    
4030 C  CD    . PRO B 199 ? 0.3679 0.5042 0.4447 -0.0467 0.0016  -0.0098 179 PRO B CD    
4031 N  N     . ALA B 200 ? 0.2906 0.4523 0.3947 -0.0212 -0.0016 -0.0283 180 ALA B N     
4032 C  CA    . ALA B 200 ? 0.3361 0.4881 0.4418 -0.0121 -0.0055 -0.0297 180 ALA B CA    
4033 C  C     . ALA B 200 ? 0.2721 0.4108 0.3702 -0.0107 -0.0036 -0.0262 180 ALA B C     
4034 O  O     . ALA B 200 ? 0.2530 0.3972 0.3497 -0.0134 0.0006  -0.0265 180 ALA B O     
4035 C  CB    . ALA B 200 ? 0.3941 0.5613 0.5117 -0.0055 -0.0076 -0.0380 180 ALA B CB    
4036 N  N     . GLY B 201 ? 0.2314 0.3530 0.3242 -0.0071 -0.0066 -0.0227 181 GLY B N     
4037 C  CA    . GLY B 201 ? 0.2745 0.3840 0.3609 -0.0051 -0.0053 -0.0198 181 GLY B CA    
4038 C  C     . GLY B 201 ? 0.2241 0.3258 0.3014 -0.0112 -0.0015 -0.0142 181 GLY B C     
4039 O  O     . GLY B 201 ? 0.2183 0.3132 0.2913 -0.0101 0.0003  -0.0125 181 GLY B O     
4040 N  N     . TYR B 202 ? 0.2386 0.3401 0.3126 -0.0175 -0.0007 -0.0114 182 TYR B N     
4041 C  CA    . TYR B 202 ? 0.2087 0.3042 0.2746 -0.0237 0.0024  -0.0068 182 TYR B CA    
4042 C  C     . TYR B 202 ? 0.2190 0.2969 0.2770 -0.0218 0.0019  -0.0025 182 TYR B C     
4043 O  O     . TYR B 202 ? 0.2283 0.3020 0.2821 -0.0225 0.0043  -0.0006 182 TYR B O     
4044 C  CB    . TYR B 202 ? 0.2409 0.3389 0.3049 -0.0308 0.0023  -0.0048 182 TYR B CB    
4045 C  CG    . TYR B 202 ? 0.2442 0.3371 0.3003 -0.0377 0.0048  -0.0005 182 TYR B CG    
4046 C  CD1   . TYR B 202 ? 0.2977 0.4002 0.3541 -0.0415 0.0081  -0.0012 182 TYR B CD1   
4047 C  CD2   . TYR B 202 ? 0.2510 0.3294 0.2992 -0.0403 0.0034  0.0041  182 TYR B CD2   
4048 C  CE1   . TYR B 202 ? 0.3238 0.4203 0.3720 -0.0482 0.0095  0.0032  182 TYR B CE1   
4049 C  CE2   . TYR B 202 ? 0.2449 0.3173 0.2856 -0.0463 0.0047  0.0080  182 TYR B CE2   
4050 C  CZ    . TYR B 202 ? 0.2959 0.3769 0.3365 -0.0503 0.0075  0.0078  182 TYR B CZ    
4051 O  OH    . TYR B 202 ? 0.3071 0.3812 0.3398 -0.0566 0.0079  0.0120  182 TYR B OH    
4052 N  N     . LEU B 203 ? 0.2016 0.2695 0.2573 -0.0196 -0.0011 -0.0010 183 LEU B N     
4053 C  CA    . LEU B 203 ? 0.2302 0.2830 0.2783 -0.0185 -0.0012 0.0027  183 LEU B CA    
4054 C  C     . LEU B 203 ? 0.2185 0.2679 0.2668 -0.0134 -0.0008 0.0020  183 LEU B C     
4055 O  O     . LEU B 203 ? 0.2118 0.2531 0.2547 -0.0136 0.0008  0.0046  183 LEU B O     
4056 C  CB    . LEU B 203 ? 0.2574 0.3021 0.3031 -0.0175 -0.0044 0.0038  183 LEU B CB    
4057 C  CG    . LEU B 203 ? 0.2498 0.2928 0.2924 -0.0229 -0.0049 0.0057  183 LEU B CG    
4058 C  CD1   . LEU B 203 ? 0.2657 0.3047 0.3082 -0.0214 -0.0085 0.0054  183 LEU B CD1   
4059 C  CD2   . LEU B 203 ? 0.2686 0.3009 0.3032 -0.0260 -0.0034 0.0092  183 LEU B CD2   
4060 N  N     . GLU B 204 ? 0.2284 0.2839 0.2830 -0.0087 -0.0026 -0.0015 184 GLU B N     
4061 C  CA    . GLU B 204 ? 0.2182 0.2702 0.2728 -0.0042 -0.0026 -0.0023 184 GLU B CA    
4062 C  C     . GLU B 204 ? 0.2284 0.2841 0.2819 -0.0060 0.0013  -0.0021 184 GLU B C     
4063 O  O     . GLU B 204 ? 0.2242 0.2721 0.2733 -0.0051 0.0025  0.0001  184 GLU B O     
4064 C  CB    . GLU B 204 ? 0.2082 0.2667 0.2702 0.0011  -0.0059 -0.0068 184 GLU B CB    
4065 C  CG    . GLU B 204 ? 0.2579 0.3118 0.3197 0.0058  -0.0067 -0.0076 184 GLU B CG    
4066 C  CD    . GLU B 204 ? 0.2967 0.3565 0.3660 0.0114  -0.0107 -0.0126 184 GLU B CD    
4067 O  OE1   . GLU B 204 ? 0.3366 0.4031 0.4114 0.0122  -0.0133 -0.0154 184 GLU B OE1   
4068 O  OE2   . GLU B 204 ? 0.3695 0.4272 0.4394 0.0151  -0.0115 -0.0140 184 GLU B OE2   
4069 N  N     . GLY B 205 ? 0.2423 0.3102 0.2995 -0.0092 0.0034  -0.0042 185 GLY B N     
4070 C  CA    . GLY B 205 ? 0.2419 0.3137 0.2974 -0.0117 0.0069  -0.0039 185 GLY B CA    
4071 C  C     . GLY B 205 ? 0.2632 0.3252 0.3105 -0.0162 0.0085  0.0012  185 GLY B C     
4072 O  O     . GLY B 205 ? 0.2676 0.3255 0.3113 -0.0163 0.0102  0.0027  185 GLY B O     
4073 N  N     . VAL B 206 ? 0.2670 0.3245 0.3112 -0.0199 0.0075  0.0036  186 VAL B N     
4074 C  CA    . VAL B 206 ? 0.2485 0.2958 0.2850 -0.0238 0.0080  0.0080  186 VAL B CA    
4075 C  C     . VAL B 206 ? 0.2722 0.3073 0.3048 -0.0197 0.0075  0.0098  186 VAL B C     
4076 O  O     . VAL B 206 ? 0.2570 0.2868 0.2853 -0.0207 0.0087  0.0119  186 VAL B O     
4077 C  CB    . VAL B 206 ? 0.2653 0.3097 0.2996 -0.0278 0.0064  0.0096  186 VAL B CB    
4078 C  CG1   . VAL B 206 ? 0.3065 0.3370 0.3333 -0.0292 0.0055  0.0133  186 VAL B CG1   
4079 C  CG2   . VAL B 206 ? 0.2807 0.3363 0.3167 -0.0342 0.0074  0.0091  186 VAL B CG2   
4080 N  N     . VAL B 207 ? 0.2267 0.2579 0.2606 -0.0153 0.0056  0.0089  187 VAL B N     
4081 C  CA    . VAL B 207 ? 0.1929 0.2137 0.2230 -0.0122 0.0052  0.0105  187 VAL B CA    
4082 C  C     . VAL B 207 ? 0.2308 0.2532 0.2623 -0.0092 0.0065  0.0096  187 VAL B C     
4083 O  O     . VAL B 207 ? 0.2448 0.2610 0.2725 -0.0089 0.0075  0.0114  187 VAL B O     
4084 C  CB    . VAL B 207 ? 0.2348 0.2512 0.2650 -0.0095 0.0026  0.0101  187 VAL B CB    
4085 C  CG1   . VAL B 207 ? 0.2442 0.2524 0.2709 -0.0067 0.0026  0.0113  187 VAL B CG1   
4086 C  CG2   . VAL B 207 ? 0.2907 0.3040 0.3183 -0.0126 0.0014  0.0112  187 VAL B CG2   
4087 N  N     . LYS B 208 ? 0.1935 0.2242 0.2305 -0.0069 0.0062  0.0065  188 LYS B N     
4088 C  CA    . LYS B 208 ? 0.2197 0.2508 0.2577 -0.0036 0.0068  0.0054  188 LYS B CA    
4089 C  C     . LYS B 208 ? 0.2308 0.2644 0.2669 -0.0063 0.0097  0.0063  188 LYS B C     
4090 O  O     . LYS B 208 ? 0.2269 0.2578 0.2619 -0.0042 0.0104  0.0065  188 LYS B O     
4091 C  CB    . LYS B 208 ? 0.2583 0.2972 0.3029 0.0001  0.0051  0.0012  188 LYS B CB    
4092 C  CG    . LYS B 208 ? 0.3187 0.3706 0.3681 -0.0014 0.0069  -0.0020 188 LYS B CG    
4093 C  CD    . LYS B 208 ? 0.4815 0.5415 0.5382 0.0024  0.0044  -0.0068 188 LYS B CD    
4094 C  CE    . LYS B 208 ? 0.4384 0.4927 0.4963 0.0082  0.0012  -0.0082 188 LYS B CE    
4095 N  NZ    . LYS B 208 ? 0.6522 0.7147 0.7180 0.0124  -0.0020 -0.0135 188 LYS B NZ    
4096 N  N     . THR B 209 ? 0.2281 0.2666 0.2634 -0.0112 0.0111  0.0069  189 THR B N     
4097 C  CA    . THR B 209 ? 0.2204 0.2613 0.2530 -0.0146 0.0134  0.0080  189 THR B CA    
4098 C  C     . THR B 209 ? 0.2500 0.2814 0.2758 -0.0183 0.0133  0.0123  189 THR B C     
4099 O  O     . THR B 209 ? 0.2335 0.2656 0.2561 -0.0220 0.0144  0.0138  189 THR B O     
4100 C  CB    . THR B 209 ? 0.2439 0.2982 0.2798 -0.0184 0.0150  0.0056  189 THR B CB    
4101 O  OG1   . THR B 209 ? 0.2707 0.3265 0.3059 -0.0228 0.0143  0.0068  189 THR B OG1   
4102 C  CG2   . THR B 209 ? 0.2860 0.3505 0.3294 -0.0139 0.0147  0.0005  189 THR B CG2   
4103 N  N     . SER B 210 ? 0.2344 0.2569 0.2579 -0.0175 0.0116  0.0139  190 SER B N     
4104 C  CA    . SER B 210 ? 0.2092 0.2228 0.2268 -0.0207 0.0107  0.0172  190 SER B CA    
4105 C  C     . SER B 210 ? 0.2095 0.2163 0.2239 -0.0189 0.0110  0.0187  190 SER B C     
4106 O  O     . SER B 210 ? 0.2518 0.2564 0.2675 -0.0144 0.0112  0.0178  190 SER B O     
4107 C  CB    . SER B 210 ? 0.2592 0.2657 0.2754 -0.0198 0.0088  0.0177  190 SER B CB    
4108 O  OG    . SER B 210 ? 0.2329 0.2298 0.2436 -0.0216 0.0076  0.0201  190 SER B OG    
4109 N  N     . THR B 211 ? 0.2381 0.2414 0.2481 -0.0228 0.0106  0.0211  191 THR B N     
4110 C  CA    . THR B 211 ? 0.2442 0.2394 0.2508 -0.0214 0.0098  0.0228  191 THR B CA    
4111 C  C     . THR B 211 ? 0.2814 0.2659 0.2839 -0.0218 0.0072  0.0244  191 THR B C     
4112 O  O     . THR B 211 ? 0.2718 0.2491 0.2716 -0.0205 0.0059  0.0255  191 THR B O     
4113 C  CB    . THR B 211 ? 0.2843 0.2818 0.2882 -0.0251 0.0104  0.0243  191 THR B CB    
4114 O  OG1   . THR B 211 ? 0.3161 0.3142 0.3165 -0.0316 0.0094  0.0262  191 THR B OG1   
4115 C  CG2   . THR B 211 ? 0.2928 0.3010 0.3007 -0.0240 0.0131  0.0219  191 THR B CG2   
4116 N  N     . THR B 212 ? 0.2456 0.2288 0.2478 -0.0234 0.0060  0.0242  192 THR B N     
4117 C  CA    . THR B 212 ? 0.2532 0.2262 0.2516 -0.0236 0.0032  0.0251  192 THR B CA    
4118 C  C     . THR B 212 ? 0.2317 0.2021 0.2319 -0.0189 0.0032  0.0230  192 THR B C     
4119 O  O     . THR B 212 ? 0.2446 0.2068 0.2421 -0.0176 0.0011  0.0228  192 THR B O     
4120 C  CB    . THR B 212 ? 0.2360 0.2082 0.2318 -0.0292 0.0014  0.0265  192 THR B CB    
4121 O  OG1   . THR B 212 ? 0.2567 0.2356 0.2563 -0.0289 0.0026  0.0247  192 THR B OG1   
4122 C  CG2   . THR B 212 ? 0.2820 0.2582 0.2755 -0.0353 0.0016  0.0288  192 THR B CG2   
4123 N  N     . THR B 213 ? 0.2303 0.2072 0.2345 -0.0164 0.0051  0.0213  193 THR B N     
4124 C  CA    . THR B 213 ? 0.2278 0.2026 0.2328 -0.0126 0.0051  0.0196  193 THR B CA    
4125 C  C     . THR B 213 ? 0.2380 0.2066 0.2412 -0.0096 0.0047  0.0192  193 THR B C     
4126 O  O     . THR B 213 ? 0.2445 0.2134 0.2481 -0.0085 0.0054  0.0197  193 THR B O     
4127 C  CB    . THR B 213 ? 0.1990 0.1807 0.2080 -0.0104 0.0066  0.0184  193 THR B CB    
4128 O  OG1   . THR B 213 ? 0.2027 0.1899 0.2139 -0.0125 0.0063  0.0179  193 THR B OG1   
4129 C  CG2   . THR B 213 ? 0.2084 0.1874 0.2171 -0.0071 0.0066  0.0172  193 THR B CG2   
4130 N  N     . LYS B 214 ? 0.2121 0.1758 0.2135 -0.0083 0.0035  0.0180  194 LYS B N     
4131 C  CA    . LYS B 214 ? 0.2292 0.1875 0.2292 -0.0056 0.0027  0.0168  194 LYS B CA    
4132 C  C     . LYS B 214 ? 0.2544 0.2141 0.2551 -0.0026 0.0039  0.0145  194 LYS B C     
4133 O  O     . LYS B 214 ? 0.2366 0.1963 0.2364 -0.0031 0.0036  0.0135  194 LYS B O     
4134 C  CB    . LYS B 214 ? 0.2297 0.1800 0.2263 -0.0069 -0.0005 0.0169  194 LYS B CB    
4135 C  CG    . LYS B 214 ? 0.3520 0.2968 0.3479 -0.0032 -0.0020 0.0146  194 LYS B CG    
4136 C  CD    . LYS B 214 ? 0.3726 0.3131 0.3675 -0.0033 -0.0040 0.0162  194 LYS B CD    
4137 C  CE    . LYS B 214 ? 0.3572 0.2907 0.3481 -0.0076 -0.0076 0.0186  194 LYS B CE    
4138 N  NZ    . LYS B 214 ? 0.3364 0.2666 0.3259 -0.0083 -0.0094 0.0208  194 LYS B NZ    
4139 N  N     . ALA B 215 ? 0.2152 0.1764 0.2171 0.0001  0.0051  0.0136  195 ALA B N     
4140 C  CA    . ALA B 215 ? 0.2259 0.1892 0.2280 0.0022  0.0064  0.0114  195 ALA B CA    
4141 C  C     . ALA B 215 ? 0.2270 0.1869 0.2283 0.0046  0.0054  0.0086  195 ALA B C     
4142 O  O     . ALA B 215 ? 0.2479 0.2047 0.2497 0.0060  0.0041  0.0086  195 ALA B O     
4143 C  CB    . ALA B 215 ? 0.1992 0.1675 0.2033 0.0031  0.0084  0.0120  195 ALA B CB    
4144 N  N     . ARG B 216 ? 0.2107 0.1714 0.2108 0.0053  0.0058  0.0060  196 ARG B N     
4145 C  CA    . ARG B 216 ? 0.2153 0.1739 0.2151 0.0081  0.0048  0.0021  196 ARG B CA    
4146 C  C     . ARG B 216 ? 0.2375 0.2025 0.2377 0.0092  0.0074  -0.0006 196 ARG B C     
4147 O  O     . ARG B 216 ? 0.2335 0.2012 0.2317 0.0072  0.0086  -0.0007 196 ARG B O     
4148 C  CB    . ARG B 216 ? 0.2514 0.2045 0.2486 0.0074  0.0025  0.0008  196 ARG B CB    
4149 C  CG    . ARG B 216 ? 0.2684 0.2190 0.2654 0.0108  0.0009  -0.0041 196 ARG B CG    
4150 C  CD    . ARG B 216 ? 0.2657 0.2113 0.2596 0.0099  -0.0013 -0.0057 196 ARG B CD    
4151 N  NE    . ARG B 216 ? 0.2576 0.2082 0.2498 0.0083  0.0011  -0.0067 196 ARG B NE    
4152 C  CZ    . ARG B 216 ? 0.2697 0.2174 0.2590 0.0067  -0.0002 -0.0077 196 ARG B CZ    
4153 N  NH1   . ARG B 216 ? 0.2914 0.2311 0.2791 0.0063  -0.0038 -0.0076 196 ARG B NH1   
4154 N  NH2   . ARG B 216 ? 0.2816 0.2341 0.2690 0.0053  0.0018  -0.0088 196 ARG B NH2   
4155 N  N     . LEU B 217 ? 0.2129 0.1808 0.2155 0.0119  0.0081  -0.0028 197 LEU B N     
4156 C  CA    . LEU B 217 ? 0.2122 0.1875 0.2153 0.0125  0.0106  -0.0058 197 LEU B CA    
4157 C  C     . LEU B 217 ? 0.2182 0.1936 0.2222 0.0159  0.0096  -0.0115 197 LEU B C     
4158 O  O     . LEU B 217 ? 0.2482 0.2205 0.2547 0.0192  0.0074  -0.0131 197 LEU B O     
4159 C  CB    . LEU B 217 ? 0.2243 0.2042 0.2300 0.0129  0.0122  -0.0045 197 LEU B CB    
4160 C  CG    . LEU B 217 ? 0.2506 0.2391 0.2566 0.0121  0.0150  -0.0065 197 LEU B CG    
4161 C  CD1   . LEU B 217 ? 0.2527 0.2434 0.2550 0.0079  0.0164  -0.0041 197 LEU B CD1   
4162 C  CD2   . LEU B 217 ? 0.2451 0.2366 0.2542 0.0130  0.0156  -0.0052 197 LEU B CD2   
4163 N  N     . LEU B 218 ? 0.2201 0.1989 0.2219 0.0153  0.0108  -0.0148 198 LEU B N     
4164 C  CA    . LEU B 218 ? 0.2260 0.2052 0.2286 0.0188  0.0097  -0.0210 198 LEU B CA    
4165 C  C     . LEU B 218 ? 0.2374 0.2278 0.2415 0.0194  0.0130  -0.0256 198 LEU B C     
4166 O  O     . LEU B 218 ? 0.2523 0.2489 0.2541 0.0156  0.0160  -0.0238 198 LEU B O     
4167 C  CB    . LEU B 218 ? 0.2504 0.2253 0.2492 0.0177  0.0084  -0.0224 198 LEU B CB    
4168 C  CG    . LEU B 218 ? 0.2652 0.2295 0.2625 0.0168  0.0048  -0.0188 198 LEU B CG    
4169 C  CD1   . LEU B 218 ? 0.2636 0.2243 0.2572 0.0159  0.0034  -0.0210 198 LEU B CD1   
4170 C  CD2   . LEU B 218 ? 0.2850 0.2426 0.2848 0.0203  0.0012  -0.0195 198 LEU B CD2   
4171 N  N     . HIS B 219 ? 0.2361 0.2291 0.2440 0.0242  0.0120  -0.0314 199 HIS B N     
4172 C  CA    . HIS B 219 ? 0.2353 0.2405 0.2455 0.0253  0.0150  -0.0373 199 HIS B CA    
4173 C  C     . HIS B 219 ? 0.2818 0.2871 0.2927 0.0293  0.0133  -0.0449 199 HIS B C     
4174 O  O     . HIS B 219 ? 0.2830 0.2827 0.2973 0.0346  0.0094  -0.0481 199 HIS B O     
4175 C  CB    . HIS B 219 ? 0.2339 0.2443 0.2496 0.0279  0.0153  -0.0382 199 HIS B CB    
4176 C  CG    . HIS B 219 ? 0.2270 0.2512 0.2459 0.0293  0.0182  -0.0451 199 HIS B CG    
4177 N  ND1   . HIS B 219 ? 0.2421 0.2771 0.2586 0.0243  0.0227  -0.0447 199 HIS B ND1   
4178 C  CD2   . HIS B 219 ? 0.2471 0.2766 0.2716 0.0350  0.0171  -0.0527 199 HIS B CD2   
4179 C  CE1   . HIS B 219 ? 0.2266 0.2741 0.2469 0.0263  0.0247  -0.0518 199 HIS B CE1   
4180 N  NE2   . HIS B 219 ? 0.2533 0.2981 0.2790 0.0332  0.0214  -0.0571 199 HIS B NE2   
4181 N  N     . TYR B 220 ? 0.2635 0.2745 0.2707 0.0269  0.0157  -0.0479 200 TYR B N     
4182 C  CA    . TYR B 220 ? 0.2994 0.3131 0.3073 0.0306  0.0149  -0.0563 200 TYR B CA    
4183 C  C     . TYR B 220 ? 0.3168 0.3455 0.3292 0.0328  0.0180  -0.0634 200 TYR B C     
4184 O  O     . TYR B 220 ? 0.2918 0.3318 0.3022 0.0280  0.0226  -0.0630 200 TYR B O     
4185 C  CB    . TYR B 220 ? 0.3038 0.3167 0.3052 0.0267  0.0160  -0.0563 200 TYR B CB    
4186 C  CG    . TYR B 220 ? 0.3168 0.3153 0.3148 0.0255  0.0123  -0.0509 200 TYR B CG    
4187 C  CD1   . TYR B 220 ? 0.3719 0.3611 0.3698 0.0294  0.0078  -0.0544 200 TYR B CD1   
4188 C  CD2   . TYR B 220 ? 0.2950 0.2894 0.2900 0.0205  0.0129  -0.0426 200 TYR B CD2   
4189 C  CE1   . TYR B 220 ? 0.3791 0.3559 0.3738 0.0276  0.0045  -0.0493 200 TYR B CE1   
4190 C  CE2   . TYR B 220 ? 0.3605 0.3435 0.3529 0.0193  0.0097  -0.0381 200 TYR B CE2   
4191 C  CZ    . TYR B 220 ? 0.3653 0.3399 0.3575 0.0224  0.0057  -0.0413 200 TYR B CZ    
4192 O  OH    . TYR B 220 ? 0.4116 0.3756 0.4011 0.0204  0.0026  -0.0367 200 TYR B OH    
4193 N  N     . PHE B 221 ? 0.2796 0.3084 0.2980 0.0398  0.0150  -0.0700 201 PHE B N     
4194 C  CA    . PHE B 221 ? 0.2894 0.3330 0.3139 0.0430  0.0173  -0.0776 201 PHE B CA    
4195 C  C     . PHE B 221 ? 0.3579 0.4135 0.3805 0.0421  0.0207  -0.0853 201 PHE B C     
4196 O  O     . PHE B 221 ? 0.3905 0.4400 0.4091 0.0425  0.0191  -0.0874 201 PHE B O     
4197 C  CB    . PHE B 221 ? 0.2936 0.3325 0.3252 0.0516  0.0121  -0.0829 201 PHE B CB    
4198 C  CG    . PHE B 221 ? 0.2646 0.2955 0.2987 0.0524  0.0093  -0.0764 201 PHE B CG    
4199 C  CD1   . PHE B 221 ? 0.2501 0.2912 0.2894 0.0527  0.0115  -0.0766 201 PHE B CD1   
4200 C  CD2   . PHE B 221 ? 0.2671 0.2807 0.2983 0.0525  0.0045  -0.0702 201 PHE B CD2   
4201 C  CE1   . PHE B 221 ? 0.2546 0.2885 0.2959 0.0534  0.0089  -0.0708 201 PHE B CE1   
4202 C  CE2   . PHE B 221 ? 0.2808 0.2878 0.3138 0.0528  0.0021  -0.0644 201 PHE B CE2   
4203 C  CZ    . PHE B 221 ? 0.3215 0.3383 0.3595 0.0534  0.0043  -0.0647 201 PHE B CZ    
4204 N  N     . PRO B 222 ? 0.3215 0.3946 0.3464 0.0401  0.0256  -0.0895 202 PRO B N     
4205 C  CA    . PRO B 222 ? 0.3738 0.4603 0.3971 0.0391  0.0291  -0.0977 202 PRO B CA    
4206 C  C     . PRO B 222 ? 0.4532 0.5387 0.4814 0.0478  0.0254  -0.1083 202 PRO B C     
4207 O  O     . PRO B 222 ? 0.4618 0.5423 0.4970 0.0551  0.0209  -0.1111 202 PRO B O     
4208 C  CB    . PRO B 222 ? 0.4071 0.5129 0.4336 0.0360  0.0343  -0.1003 202 PRO B CB    
4209 C  CG    . PRO B 222 ? 0.3103 0.4106 0.3364 0.0323  0.0343  -0.0903 202 PRO B CG    
4210 C  CD    . PRO B 222 ? 0.3308 0.4126 0.3590 0.0376  0.0283  -0.0862 202 PRO B CD    
4211 N  N     . GLU B 223 ? 0.5464 0.6360 0.5707 0.0471  0.0267  -0.1141 203 GLU B N     
4212 C  CA    . GLU B 223 ? 0.6935 0.7834 0.7220 0.0553  0.0233  -0.1253 203 GLU B CA    
4213 C  C     . GLU B 223 ? 0.8129 0.9125 0.8522 0.0634  0.0219  -0.1341 203 GLU B C     
4214 O  O     . GLU B 223 ? 0.7592 0.8790 0.8024 0.0629  0.0267  -0.1413 203 GLU B O     
4215 C  CB    . GLU B 223 ? 0.6795 0.7812 0.7034 0.0525  0.0273  -0.1325 203 GLU B CB    
4216 C  CG    . GLU B 223 ? 0.8729 0.9745 0.9009 0.0613  0.0236  -0.1447 203 GLU B CG    
4217 C  CD    . GLU B 223 ? 0.9840 1.1037 1.0098 0.0594  0.0286  -0.1545 203 GLU B CD    
4218 O  OE1   . GLU B 223 ? 0.9398 1.0752 0.9626 0.0516  0.0353  -0.1527 203 GLU B OE1   
4219 O  OE2   . GLU B 223 ? 1.1738 1.2921 1.2006 0.0653  0.0258  -0.1640 203 GLU B OE2   
4220 N  N     . CYS B 246 ? 0.8690 0.7813 0.8100 0.0085  -0.0219 -0.0639 226 CYS B N     
4221 C  CA    . CYS B 246 ? 0.9666 0.8810 0.9129 0.0092  -0.0202 -0.0589 226 CYS B CA    
4222 C  C     . CYS B 246 ? 0.7797 0.6860 0.7265 0.0051  -0.0230 -0.0502 226 CYS B C     
4223 O  O     . CYS B 246 ? 0.7705 0.6774 0.7146 0.0000  -0.0226 -0.0456 226 CYS B O     
4224 C  CB    . CYS B 246 ? 0.9219 0.8499 0.8693 0.0074  -0.0140 -0.0573 226 CYS B CB    
4225 S  SG    . CYS B 246 ? 1.3092 1.2413 1.2635 0.0099  -0.0117 -0.0540 226 CYS B SG    
4226 N  N     . ALA B 247 ? 0.6304 0.5297 0.5805 0.0072  -0.0260 -0.0483 227 ALA B N     
4227 C  CA    . ALA B 247 ? 0.5879 0.4797 0.5379 0.0030  -0.0290 -0.0409 227 ALA B CA    
4228 C  C     . ALA B 247 ? 0.4283 0.3278 0.3812 -0.0004 -0.0249 -0.0340 227 ALA B C     
4229 O  O     . ALA B 247 ? 0.4191 0.3259 0.3756 0.0019  -0.0213 -0.0340 227 ALA B O     
4230 C  CB    . ALA B 247 ? 0.5341 0.4149 0.4855 0.0056  -0.0341 -0.0411 227 ALA B CB    
4231 N  N     . THR B 248 ? 0.3996 0.2978 0.3513 -0.0056 -0.0257 -0.0284 228 THR B N     
4232 C  CA    . THR B 248 ? 0.3547 0.2599 0.3094 -0.0086 -0.0226 -0.0223 228 THR B CA    
4233 C  C     . THR B 248 ? 0.3715 0.2725 0.3292 -0.0095 -0.0243 -0.0178 228 THR B C     
4234 O  O     . THR B 248 ? 0.3792 0.2707 0.3355 -0.0092 -0.0286 -0.0184 228 THR B O     
4235 C  CB    . THR B 248 ? 0.3514 0.2583 0.3040 -0.0136 -0.0230 -0.0190 228 THR B CB    
4236 O  OG1   . THR B 248 ? 0.3740 0.2720 0.3245 -0.0164 -0.0277 -0.0178 228 THR B OG1   
4237 C  CG2   . THR B 248 ? 0.3891 0.3003 0.3380 -0.0135 -0.0214 -0.0228 228 THR B CG2   
4238 N  N     . HIS B 249 ? 0.3190 0.2270 0.2803 -0.0107 -0.0212 -0.0135 229 HIS B N     
4239 C  CA    . HIS B 249 ? 0.3280 0.2342 0.2918 -0.0127 -0.0221 -0.0087 229 HIS B CA    
4240 C  C     . HIS B 249 ? 0.3126 0.2266 0.2789 -0.0163 -0.0198 -0.0041 229 HIS B C     
4241 O  O     . HIS B 249 ? 0.2788 0.1990 0.2452 -0.0165 -0.0175 -0.0044 229 HIS B O     
4242 C  CB    . HIS B 249 ? 0.3155 0.2222 0.2823 -0.0089 -0.0209 -0.0092 229 HIS B CB    
4243 C  CG    . HIS B 249 ? 0.3119 0.2286 0.2819 -0.0072 -0.0161 -0.0090 229 HIS B CG    
4244 N  ND1   . HIS B 249 ? 0.2899 0.2111 0.2594 -0.0039 -0.0136 -0.0134 229 HIS B ND1   
4245 C  CD2   . HIS B 249 ? 0.2911 0.2140 0.2643 -0.0084 -0.0134 -0.0050 229 HIS B CD2   
4246 C  CE1   . HIS B 249 ? 0.2726 0.2018 0.2447 -0.0037 -0.0099 -0.0116 229 HIS B CE1   
4247 N  NE2   . HIS B 249 ? 0.3155 0.2454 0.2900 -0.0060 -0.0098 -0.0067 229 HIS B NE2   
4248 N  N     . LEU B 250 ? 0.2965 0.2100 0.2647 -0.0193 -0.0207 0.0000  230 LEU B N     
4249 C  CA    . LEU B 250 ? 0.2832 0.2050 0.2551 -0.0219 -0.0185 0.0039  230 LEU B CA    
4250 C  C     . LEU B 250 ? 0.3329 0.2577 0.3081 -0.0203 -0.0163 0.0057  230 LEU B C     
4251 O  O     . LEU B 250 ? 0.3155 0.2345 0.2898 -0.0199 -0.0180 0.0060  230 LEU B O     
4252 C  CB    . LEU B 250 ? 0.2776 0.1984 0.2491 -0.0273 -0.0210 0.0068  230 LEU B CB    
4253 C  CG    . LEU B 250 ? 0.3130 0.2304 0.2812 -0.0297 -0.0237 0.0055  230 LEU B CG    
4254 C  CD1   . LEU B 250 ? 0.3702 0.2866 0.3381 -0.0356 -0.0264 0.0086  230 LEU B CD1   
4255 C  CD2   . LEU B 250 ? 0.3278 0.2522 0.2970 -0.0290 -0.0218 0.0047  230 LEU B CD2   
4256 N  N     . ASP B 251 ? 0.2631 0.1964 0.2419 -0.0195 -0.0131 0.0068  231 ASP B N     
4257 C  CA    . ASP B 251 ? 0.2461 0.1827 0.2281 -0.0186 -0.0113 0.0088  231 ASP B CA    
4258 C  C     . ASP B 251 ? 0.2670 0.2049 0.2503 -0.0230 -0.0124 0.0120  231 ASP B C     
4259 O  O     . ASP B 251 ? 0.2543 0.1951 0.2381 -0.0264 -0.0133 0.0130  231 ASP B O     
4260 C  CB    . ASP B 251 ? 0.2378 0.1824 0.2231 -0.0167 -0.0081 0.0091  231 ASP B CB    
4261 C  CG    . ASP B 251 ? 0.2571 0.2018 0.2411 -0.0130 -0.0065 0.0064  231 ASP B CG    
4262 O  OD1   . ASP B 251 ? 0.2511 0.1908 0.2321 -0.0116 -0.0075 0.0035  231 ASP B OD1   
4263 O  OD2   . ASP B 251 ? 0.2756 0.2257 0.2616 -0.0118 -0.0043 0.0070  231 ASP B OD2   
4264 N  N     . HIS B 252 ? 0.2547 0.1911 0.2384 -0.0234 -0.0123 0.0136  232 HIS B N     
4265 C  CA    A HIS B 252 ? 0.2781 0.2151 0.2616 -0.0284 -0.0136 0.0167  232 HIS B CA    
4266 C  CA    B HIS B 252 ? 0.2749 0.2123 0.2586 -0.0286 -0.0136 0.0166  232 HIS B CA    
4267 C  C     . HIS B 252 ? 0.3267 0.2747 0.3150 -0.0298 -0.0107 0.0183  232 HIS B C     
4268 O  O     . HIS B 252 ? 0.2583 0.2104 0.2473 -0.0347 -0.0112 0.0202  232 HIS B O     
4269 C  CB    A HIS B 252 ? 0.3023 0.2312 0.2829 -0.0286 -0.0157 0.0177  232 HIS B CB    
4270 C  CB    B HIS B 252 ? 0.3316 0.2595 0.3112 -0.0301 -0.0167 0.0178  232 HIS B CB    
4271 C  CG    A HIS B 252 ? 0.3081 0.2358 0.2866 -0.0349 -0.0177 0.0211  232 HIS B CG    
4272 C  CG    B HIS B 252 ? 0.3336 0.2625 0.3144 -0.0287 -0.0153 0.0191  232 HIS B CG    
4273 N  ND1   A HIS B 252 ? 0.3270 0.2590 0.3067 -0.0368 -0.0162 0.0235  232 HIS B ND1   
4274 N  ND1   B HIS B 252 ? 0.3346 0.2574 0.3144 -0.0242 -0.0161 0.0174  232 HIS B ND1   
4275 C  CD2   A HIS B 252 ? 0.3910 0.3140 0.3659 -0.0403 -0.0211 0.0226  232 HIS B CD2   
4276 C  CD2   B HIS B 252 ? 0.3142 0.2494 0.2970 -0.0314 -0.0135 0.0216  232 HIS B CD2   
4277 C  CE1   A HIS B 252 ? 0.3043 0.2348 0.2810 -0.0434 -0.0184 0.0264  232 HIS B CE1   
4278 C  CE1   B HIS B 252 ? 0.3355 0.2604 0.3165 -0.0241 -0.0149 0.0192  232 HIS B CE1   
4279 N  NE2   A HIS B 252 ? 0.3349 0.2597 0.3086 -0.0458 -0.0215 0.0260  232 HIS B NE2   
4280 N  NE2   B HIS B 252 ? 0.3340 0.2663 0.3165 -0.0285 -0.0133 0.0217  232 HIS B NE2   
4281 N  N     . GLY B 253 ? 0.2478 0.2009 0.2393 -0.0258 -0.0079 0.0174  233 GLY B N     
4282 C  CA    . GLY B 253 ? 0.2270 0.1896 0.2231 -0.0261 -0.0055 0.0183  233 GLY B CA    
4283 C  C     . GLY B 253 ? 0.2230 0.1935 0.2229 -0.0264 -0.0051 0.0175  233 GLY B C     
4284 O  O     . GLY B 253 ? 0.2262 0.1962 0.2253 -0.0286 -0.0069 0.0172  233 GLY B O     
4285 N  N     . CYS B 254 ? 0.2164 0.1940 0.2206 -0.0238 -0.0031 0.0170  234 CYS B N     
4286 C  CA    . CYS B 254 ? 0.2282 0.2134 0.2368 -0.0233 -0.0034 0.0159  234 CYS B CA    
4287 C  C     . CYS B 254 ? 0.2118 0.1942 0.2194 -0.0198 -0.0040 0.0148  234 CYS B C     
4288 O  O     . CYS B 254 ? 0.2217 0.2028 0.2282 -0.0205 -0.0058 0.0143  234 CYS B O     
4289 C  CB    . CYS B 254 ? 0.2076 0.2021 0.2215 -0.0226 -0.0018 0.0154  234 CYS B CB    
4290 S  SG    . CYS B 254 ? 0.2639 0.2653 0.2792 -0.0282 -0.0011 0.0163  234 CYS B SG    
4291 N  N     . LEU B 255 ? 0.2086 0.1902 0.2163 -0.0164 -0.0025 0.0147  235 LEU B N     
4292 C  CA    . LEU B 255 ? 0.2081 0.1877 0.2145 -0.0139 -0.0031 0.0140  235 LEU B CA    
4293 C  C     . LEU B 255 ? 0.2081 0.1831 0.2115 -0.0119 -0.0014 0.0139  235 LEU B C     
4294 O  O     . LEU B 255 ? 0.2364 0.2126 0.2413 -0.0107 0.0002  0.0144  235 LEU B O     
4295 C  CB    . LEU B 255 ? 0.2044 0.1894 0.2150 -0.0119 -0.0038 0.0137  235 LEU B CB    
4296 C  CG    . LEU B 255 ? 0.2079 0.1985 0.2225 -0.0129 -0.0060 0.0129  235 LEU B CG    
4297 C  CD1   . LEU B 255 ? 0.2432 0.2398 0.2631 -0.0102 -0.0066 0.0119  235 LEU B CD1   
4298 C  CD2   . LEU B 255 ? 0.2432 0.2302 0.2547 -0.0135 -0.0086 0.0129  235 LEU B CD2   
4299 N  N     . THR B 256 ? 0.2115 0.1819 0.2108 -0.0116 -0.0017 0.0131  236 THR B N     
4300 C  CA    . THR B 256 ? 0.2194 0.1868 0.2162 -0.0097 -0.0001 0.0123  236 THR B CA    
4301 C  C     . THR B 256 ? 0.2469 0.2158 0.2426 -0.0086 0.0002  0.0122  236 THR B C     
4302 O  O     . THR B 256 ? 0.2277 0.1956 0.2205 -0.0097 -0.0010 0.0118  236 THR B O     
4303 C  CB    . THR B 256 ? 0.2174 0.1797 0.2103 -0.0101 -0.0007 0.0106  236 THR B CB    
4304 O  OG1   . THR B 256 ? 0.2201 0.1797 0.2132 -0.0118 -0.0019 0.0111  236 THR B OG1   
4305 C  CG2   . THR B 256 ? 0.2201 0.1810 0.2117 -0.0076 0.0010  0.0089  236 THR B CG2   
4306 N  N     . GLY B 257 ? 0.2071 0.1778 0.2045 -0.0070 0.0016  0.0128  237 GLY B N     
4307 C  CA    . GLY B 257 ? 0.2069 0.1782 0.2025 -0.0066 0.0018  0.0131  237 GLY B CA    
4308 C  C     . GLY B 257 ? 0.2427 0.2128 0.2346 -0.0065 0.0035  0.0115  237 GLY B C     
4309 O  O     . GLY B 257 ? 0.2390 0.2083 0.2315 -0.0052 0.0048  0.0101  237 GLY B O     
4310 N  N     . LEU B 258 ? 0.2177 0.1879 0.2057 -0.0079 0.0030  0.0114  238 LEU B N     
4311 C  CA    . LEU B 258 ? 0.2300 0.2008 0.2143 -0.0084 0.0047  0.0092  238 LEU B CA    
4312 C  C     . LEU B 258 ? 0.2307 0.2034 0.2119 -0.0102 0.0051  0.0102  238 LEU B C     
4313 O  O     . LEU B 258 ? 0.2396 0.2112 0.2193 -0.0119 0.0027  0.0125  238 LEU B O     
4314 C  CB    . LEU B 258 ? 0.2445 0.2134 0.2250 -0.0100 0.0037  0.0076  238 LEU B CB    
4315 C  CG    . LEU B 258 ? 0.2470 0.2130 0.2294 -0.0093 0.0025  0.0069  238 LEU B CG    
4316 C  CD1   . LEU B 258 ? 0.3377 0.3018 0.3161 -0.0115 0.0008  0.0061  238 LEU B CD1   
4317 C  CD2   . LEU B 258 ? 0.2640 0.2287 0.2475 -0.0071 0.0038  0.0044  238 LEU B CD2   
4318 N  N     . THR B 259 ? 0.2432 0.2190 0.2233 -0.0100 0.0076  0.0084  239 THR B N     
4319 C  CA    . THR B 259 ? 0.2372 0.2158 0.2128 -0.0130 0.0083  0.0087  239 THR B CA    
4320 C  C     . THR B 259 ? 0.2418 0.2228 0.2131 -0.0146 0.0097  0.0054  239 THR B C     
4321 O  O     . THR B 259 ? 0.2577 0.2385 0.2304 -0.0124 0.0105  0.0022  239 THR B O     
4322 C  CB    . THR B 259 ? 0.2668 0.2490 0.2443 -0.0123 0.0104  0.0087  239 THR B CB    
4323 O  OG1   . THR B 259 ? 0.3008 0.2863 0.2805 -0.0099 0.0130  0.0049  239 THR B OG1   
4324 C  CG2   . THR B 259 ? 0.2877 0.2676 0.2698 -0.0101 0.0092  0.0112  239 THR B CG2   
4325 N  N     . SER B 260 ? 0.2304 0.2139 0.1960 -0.0187 0.0098  0.0061  240 SER B N     
4326 C  CA    . SER B 260 ? 0.2575 0.2457 0.2191 -0.0204 0.0121  0.0022  240 SER B CA    
4327 C  C     . SER B 260 ? 0.2425 0.2368 0.2078 -0.0178 0.0155  -0.0017 240 SER B C     
4328 O  O     . SER B 260 ? 0.2506 0.2462 0.2195 -0.0165 0.0162  -0.0004 240 SER B O     
4329 C  CB    . SER B 260 ? 0.2970 0.2873 0.2508 -0.0264 0.0117  0.0039  240 SER B CB    
4330 O  OG    . SER B 260 ? 0.2737 0.2676 0.2272 -0.0285 0.0128  0.0056  240 SER B OG    
4331 N  N     . ALA B 261 ? 0.2356 0.2336 0.2002 -0.0166 0.0173  -0.0069 241 ALA B N     
4332 C  CA    . ALA B 261 ? 0.2514 0.2555 0.2203 -0.0133 0.0200  -0.0116 241 ALA B CA    
4333 C  C     . ALA B 261 ? 0.2567 0.2698 0.2236 -0.0167 0.0227  -0.0122 241 ALA B C     
4334 O  O     . ALA B 261 ? 0.2695 0.2847 0.2301 -0.0224 0.0228  -0.0101 241 ALA B O     
4335 C  CB    . ALA B 261 ? 0.2769 0.2825 0.2458 -0.0106 0.0206  -0.0178 241 ALA B CB    
4336 N  N     . MET B 262 ? 0.2317 0.2500 0.2039 -0.0137 0.0246  -0.0148 242 MET B N     
4337 C  CA    . MET B 262 ? 0.2326 0.2613 0.2040 -0.0167 0.0276  -0.0163 242 MET B CA    
4338 C  C     . MET B 262 ? 0.2391 0.2774 0.2128 -0.0142 0.0304  -0.0243 242 MET B C     
4339 O  O     . MET B 262 ? 0.2459 0.2832 0.2256 -0.0080 0.0299  -0.0283 242 MET B O     
4340 C  CB    . MET B 262 ? 0.2327 0.2614 0.2088 -0.0153 0.0276  -0.0136 242 MET B CB    
4341 C  CG    . MET B 262 ? 0.2609 0.3011 0.2370 -0.0184 0.0306  -0.0155 242 MET B CG    
4342 S  SD    . MET B 262 ? 0.2746 0.3151 0.2577 -0.0151 0.0305  -0.0138 242 MET B SD    
4343 C  CE    . MET B 262 ? 0.2615 0.3149 0.2419 -0.0216 0.0336  -0.0144 242 MET B CE    
4344 N  N     . PHE B 263 ? 0.2406 0.2883 0.2092 -0.0192 0.0329  -0.0269 243 PHE B N     
4345 C  CA    . PHE B 263 ? 0.2433 0.3032 0.2146 -0.0172 0.0361  -0.0352 243 PHE B CA    
4346 C  C     . PHE B 263 ? 0.2860 0.3574 0.2595 -0.0197 0.0390  -0.0359 243 PHE B C     
4347 O  O     . PHE B 263 ? 0.2681 0.3406 0.2365 -0.0264 0.0394  -0.0307 243 PHE B O     
4348 C  CB    . PHE B 263 ? 0.2508 0.3158 0.2152 -0.0213 0.0376  -0.0387 243 PHE B CB    
4349 C  CG    . PHE B 263 ? 0.3123 0.3673 0.2754 -0.0181 0.0348  -0.0394 243 PHE B CG    
4350 C  CD1   . PHE B 263 ? 0.2957 0.3512 0.2635 -0.0115 0.0345  -0.0467 243 PHE B CD1   
4351 C  CD2   . PHE B 263 ? 0.3286 0.3732 0.2859 -0.0217 0.0320  -0.0329 243 PHE B CD2   
4352 C  CE1   . PHE B 263 ? 0.3450 0.3906 0.3111 -0.0092 0.0316  -0.0471 243 PHE B CE1   
4353 C  CE2   . PHE B 263 ? 0.3494 0.3853 0.3057 -0.0192 0.0294  -0.0334 243 PHE B CE2   
4354 C  CZ    . PHE B 263 ? 0.3301 0.3664 0.2905 -0.0132 0.0293  -0.0404 243 PHE B CZ    
4355 N  N     . VAL B 264 ? 0.2396 0.3188 0.2208 -0.0141 0.0405  -0.0424 244 VAL B N     
4356 C  CA    . VAL B 264 ? 0.2531 0.3437 0.2380 -0.0155 0.0430  -0.0437 244 VAL B CA    
4357 C  C     . VAL B 264 ? 0.2559 0.3622 0.2447 -0.0132 0.0463  -0.0538 244 VAL B C     
4358 O  O     . VAL B 264 ? 0.2654 0.3704 0.2594 -0.0058 0.0451  -0.0600 244 VAL B O     
4359 C  CB    . VAL B 264 ? 0.2687 0.3530 0.2609 -0.0102 0.0409  -0.0411 244 VAL B CB    
4360 C  CG1   . VAL B 264 ? 0.2311 0.3269 0.2263 -0.0128 0.0433  -0.0414 244 VAL B CG1   
4361 C  CG2   . VAL B 264 ? 0.3645 0.4337 0.3539 -0.0110 0.0375  -0.0328 244 VAL B CG2   
4362 N  N     . ASP B 265 ? 0.2433 0.3647 0.2299 -0.0194 0.0501  -0.0557 245 ASP B N     
4363 C  CA    . ASP B 265 ? 0.2457 0.3852 0.2376 -0.0172 0.0537  -0.0659 245 ASP B CA    
4364 C  C     . ASP B 265 ? 0.2920 0.4364 0.2932 -0.0128 0.0536  -0.0672 245 ASP B C     
4365 O  O     . ASP B 265 ? 0.2418 0.3927 0.2422 -0.0184 0.0552  -0.0636 245 ASP B O     
4366 C  CB    . ASP B 265 ? 0.2667 0.4212 0.2512 -0.0270 0.0580  -0.0673 245 ASP B CB    
4367 C  CG    . ASP B 265 ? 0.3375 0.5134 0.3279 -0.0250 0.0622  -0.0787 245 ASP B CG    
4368 O  OD1   . ASP B 265 ? 0.2725 0.4512 0.2734 -0.0159 0.0613  -0.0851 245 ASP B OD1   
4369 O  OD2   . ASP B 265 ? 0.3818 0.5718 0.3662 -0.0327 0.0661  -0.0814 245 ASP B OD2   
4370 N  N     . GLU B 266 ? 0.2568 0.3973 0.2666 -0.0029 0.0511  -0.0723 246 GLU B N     
4371 C  CA    . GLU B 266 ? 0.2327 0.3748 0.2513 0.0019  0.0499  -0.0728 246 GLU B CA    
4372 C  C     . GLU B 266 ? 0.2646 0.4279 0.2897 0.0025  0.0535  -0.0813 246 GLU B C     
4373 O  O     . GLU B 266 ? 0.2862 0.4532 0.3181 0.0051  0.0529  -0.0815 246 GLU B O     
4374 C  CB    . GLU B 266 ? 0.2325 0.3608 0.2569 0.0118  0.0450  -0.0741 246 GLU B CB    
4375 C  CG    . GLU B 266 ? 0.2490 0.3576 0.2682 0.0107  0.0416  -0.0645 246 GLU B CG    
4376 C  CD    . GLU B 266 ? 0.2303 0.3249 0.2542 0.0189  0.0367  -0.0647 246 GLU B CD    
4377 O  OE1   . GLU B 266 ? 0.2733 0.3709 0.3031 0.0259  0.0351  -0.0727 246 GLU B OE1   
4378 O  OE2   . GLU B 266 ? 0.2277 0.3085 0.2489 0.0180  0.0342  -0.0569 246 GLU B OE2   
4379 N  N     . ALA B 267 ? 0.2917 0.4699 0.3149 -0.0002 0.0572  -0.0886 247 ALA B N     
4380 C  CA    . ALA B 267 ? 0.3047 0.5057 0.3329 -0.0022 0.0615  -0.0959 247 ALA B CA    
4381 C  C     . ALA B 267 ? 0.3347 0.5424 0.3563 -0.0137 0.0645  -0.0887 247 ALA B C     
4382 O  O     . ALA B 267 ? 0.3434 0.5624 0.3701 -0.0151 0.0661  -0.0896 247 ALA B O     
4383 C  CB    . ALA B 267 ? 0.3237 0.5397 0.3519 -0.0015 0.0646  -0.1067 247 ALA B CB    
4384 N  N     . ALA B 268 ? 0.2637 0.4635 0.2737 -0.0221 0.0648  -0.0813 248 ALA B N     
4385 C  CA    . ALA B 268 ? 0.3005 0.5039 0.3027 -0.0336 0.0666  -0.0738 248 ALA B CA    
4386 C  C     . ALA B 268 ? 0.2878 0.4784 0.2915 -0.0332 0.0633  -0.0650 248 ALA B C     
4387 O  O     . ALA B 268 ? 0.3100 0.5081 0.3130 -0.0394 0.0647  -0.0620 248 ALA B O     
4388 C  CB    . ALA B 268 ? 0.3537 0.5498 0.3429 -0.0419 0.0666  -0.0681 248 ALA B CB    
4389 N  N     . THR B 269 ? 0.2612 0.4326 0.2664 -0.0266 0.0589  -0.0608 249 THR B N     
4390 C  CA    . THR B 269 ? 0.2788 0.4374 0.2854 -0.0256 0.0557  -0.0529 249 THR B CA    
4391 C  C     . THR B 269 ? 0.3027 0.4544 0.3191 -0.0143 0.0528  -0.0562 249 THR B C     
4392 O  O     . THR B 269 ? 0.2529 0.3894 0.2685 -0.0096 0.0496  -0.0539 249 THR B O     
4393 C  CB    . THR B 269 ? 0.3066 0.4479 0.3039 -0.0302 0.0528  -0.0432 249 THR B CB    
4394 O  OG1   . THR B 269 ? 0.2970 0.4271 0.2932 -0.0251 0.0508  -0.0440 249 THR B OG1   
4395 C  CG2   . THR B 269 ? 0.3653 0.5122 0.3520 -0.0417 0.0548  -0.0396 249 THR B CG2   
4396 N  N     . PRO B 270 ? 0.2498 0.4123 0.2752 -0.0101 0.0535  -0.0615 250 PRO B N     
4397 C  CA    . PRO B 270 ? 0.2381 0.3945 0.2726 0.0007  0.0502  -0.0655 250 PRO B CA    
4398 C  C     . PRO B 270 ? 0.2430 0.3800 0.2765 0.0031  0.0459  -0.0572 250 PRO B C     
4399 O  O     . PRO B 270 ? 0.2353 0.3680 0.2656 -0.0018 0.0457  -0.0499 250 PRO B O     
4400 C  CB    . PRO B 270 ? 0.2517 0.4248 0.2953 0.0028  0.0518  -0.0714 250 PRO B CB    
4401 C  CG    . PRO B 270 ? 0.3279 0.5196 0.3676 -0.0060 0.0570  -0.0741 250 PRO B CG    
4402 C  CD    . PRO B 270 ? 0.2978 0.4799 0.3255 -0.0153 0.0573  -0.0649 250 PRO B CD    
4403 N  N     . PRO B 271 ? 0.2589 0.3835 0.2947 0.0105  0.0423  -0.0583 251 PRO B N     
4404 C  CA    . PRO B 271 ? 0.2732 0.3799 0.3077 0.0125  0.0385  -0.0508 251 PRO B CA    
4405 C  C     . PRO B 271 ? 0.2891 0.3953 0.3308 0.0170  0.0363  -0.0507 251 PRO B C     
4406 O  O     . PRO B 271 ? 0.2871 0.3843 0.3328 0.0238  0.0324  -0.0517 251 PRO B O     
4407 C  CB    . PRO B 271 ? 0.2765 0.3725 0.3102 0.0176  0.0357  -0.0528 251 PRO B CB    
4408 C  CG    . PRO B 271 ? 0.2634 0.3708 0.3027 0.0225  0.0365  -0.0631 251 PRO B CG    
4409 C  CD    . PRO B 271 ? 0.2449 0.3712 0.2838 0.0167  0.0415  -0.0664 251 PRO B CD    
4410 N  N     . VAL B 272 ? 0.2471 0.3625 0.2898 0.0128  0.0383  -0.0491 252 VAL B N     
4411 C  CA    . VAL B 272 ? 0.2356 0.3546 0.2857 0.0165  0.0369  -0.0503 252 VAL B CA    
4412 C  C     . VAL B 272 ? 0.2568 0.3681 0.3034 0.0121  0.0361  -0.0416 252 VAL B C     
4413 O  O     . VAL B 272 ? 0.3854 0.4989 0.4259 0.0045  0.0383  -0.0372 252 VAL B O     
4414 C  CB    . VAL B 272 ? 0.2697 0.4094 0.3255 0.0157  0.0401  -0.0576 252 VAL B CB    
4415 C  CG1   . VAL B 272 ? 0.3058 0.4494 0.3682 0.0177  0.0387  -0.0574 252 VAL B CG1   
4416 C  CG2   . VAL B 272 ? 0.2966 0.4439 0.3577 0.0220  0.0401  -0.0676 252 VAL B CG2   
4417 N  N     . VAL B 273 ? 0.2349 0.3370 0.2849 0.0167  0.0326  -0.0393 253 VAL B N     
4418 C  CA    . VAL B 273 ? 0.2738 0.3684 0.3209 0.0134  0.0315  -0.0318 253 VAL B CA    
4419 C  C     . VAL B 273 ? 0.3926 0.5002 0.4429 0.0101  0.0334  -0.0328 253 VAL B C     
4420 O  O     . VAL B 273 ? 0.3576 0.4701 0.4150 0.0144  0.0321  -0.0360 253 VAL B O     
4421 C  CB    . VAL B 273 ? 0.3293 0.4107 0.3784 0.0189  0.0273  -0.0292 253 VAL B CB    
4422 C  CG1   . VAL B 273 ? 0.4093 0.4846 0.4558 0.0155  0.0265  -0.0223 253 VAL B CG1   
4423 C  CG2   . VAL B 273 ? 0.3468 0.4159 0.3922 0.0211  0.0255  -0.0279 253 VAL B CG2   
4424 N  N     . ASN B 274 ? 0.3202 0.4331 0.3650 0.0021  0.0362  -0.0299 254 ASN B N     
4425 C  CA    . ASN B 274 ? 0.4020 0.5275 0.4485 -0.0028 0.0381  -0.0302 254 ASN B CA    
4426 C  C     . ASN B 274 ? 0.5566 0.6745 0.5947 -0.0105 0.0378  -0.0221 254 ASN B C     
4427 O  O     . ASN B 274 ? 0.5494 0.6692 0.5807 -0.0171 0.0396  -0.0202 254 ASN B O     
4428 C  CB    . ASN B 274 ? 0.3476 0.4915 0.3959 -0.0056 0.0420  -0.0369 254 ASN B CB    
4429 C  CG    . ASN B 274 ? 0.4318 0.5905 0.4827 -0.0108 0.0440  -0.0379 254 ASN B CG    
4430 O  OD1   . ASN B 274 ? 0.4790 0.6368 0.5343 -0.0089 0.0422  -0.0364 254 ASN B OD1   
4431 N  ND2   . ASN B 274 ? 0.3802 0.5528 0.4280 -0.0179 0.0478  -0.0401 254 ASN B ND2   
4432 N  N     . PRO B 275 ? 0.5065 0.6149 0.5446 -0.0096 0.0352  -0.0172 255 PRO B N     
4433 C  CA    . PRO B 275 ? 0.6568 0.7562 0.6872 -0.0158 0.0340  -0.0099 255 PRO B CA    
4434 C  C     . PRO B 275 ? 0.7243 0.8340 0.7510 -0.0246 0.0359  -0.0088 255 PRO B C     
4435 O  O     . PRO B 275 ? 0.7499 0.8739 0.7815 -0.0258 0.0379  -0.0128 255 PRO B O     
4436 C  CB    . PRO B 275 ? 0.6945 0.7848 0.7273 -0.0122 0.0311  -0.0068 255 PRO B CB    
4437 C  CG    . PRO B 275 ? 0.6703 0.7595 0.7099 -0.0038 0.0300  -0.0110 255 PRO B CG    
4438 C  CD    . PRO B 275 ? 0.5086 0.6124 0.5531 -0.0025 0.0325  -0.0181 255 PRO B CD    
4439 N  N     . SER B 276 ? 0.8272 0.9295 0.8452 -0.0312 0.0350  -0.0033 256 SER B N     
4440 C  CA    . SER B 276 ? 0.8733 0.9826 0.8856 -0.0409 0.0359  -0.0009 256 SER B CA    
4441 C  C     . SER B 276 ? 0.8901 1.0018 0.9046 -0.0431 0.0348  0.0010  256 SER B C     
4442 O  O     . SER B 276 ? 0.8422 0.9503 0.8627 -0.0367 0.0333  0.0004  256 SER B O     
4443 C  CB    . SER B 276 ? 0.8191 0.9166 0.8212 -0.0467 0.0337  0.0051  256 SER B CB    
4444 O  OG    . SER B 276 ? 0.7876 0.8836 0.7872 -0.0454 0.0348  0.0034  256 SER B OG    
4445 N  N     . VAL B 277 ? 0.9367 1.0543 0.9459 -0.0525 0.0351  0.0036  257 VAL B N     
4446 C  CA    . VAL B 277 ? 0.9644 1.0849 0.9752 -0.0556 0.0339  0.0055  257 VAL B CA    
4447 C  C     . VAL B 277 ? 0.9092 1.0126 0.9185 -0.0523 0.0295  0.0105  257 VAL B C     
4448 O  O     . VAL B 277 ? 0.8465 0.9504 0.8604 -0.0500 0.0284  0.0105  257 VAL B O     
4449 C  CB    . VAL B 277 ? 0.9749 1.1028 0.9782 -0.0676 0.0345  0.0083  257 VAL B CB    
4450 C  CG1   . VAL B 277 ? 0.8548 1.0043 0.8620 -0.0707 0.0395  0.0020  257 VAL B CG1   
4451 C  CG2   . VAL B 277 ? 0.9114 1.0266 0.9035 -0.0734 0.0320  0.0140  257 VAL B CG2   
4452 N  N     . ASN B 278 ? 0.8176 0.9061 0.8207 -0.0520 0.0269  0.0145  258 ASN B N     
4453 C  CA    . ASN B 278 ? 0.7248 0.7979 0.7268 -0.0484 0.0230  0.0184  258 ASN B CA    
4454 C  C     . ASN B 278 ? 0.8098 0.8787 0.8186 -0.0384 0.0231  0.0157  258 ASN B C     
4455 O  O     . ASN B 278 ? 0.6376 0.6970 0.6471 -0.0349 0.0205  0.0178  258 ASN B O     
4456 C  CB    . ASN B 278 ? 0.7402 0.7998 0.7332 -0.0520 0.0196  0.0233  258 ASN B CB    
4457 C  CG    . ASN B 278 ? 0.8949 0.9522 0.8867 -0.0493 0.0208  0.0219  258 ASN B CG    
4458 O  OD1   . ASN B 278 ? 0.9585 1.0249 0.9553 -0.0457 0.0243  0.0171  258 ASN B OD1   
4459 N  ND2   . ASN B 278 ? 0.7594 0.8043 0.7446 -0.0508 0.0175  0.0257  258 ASN B ND2   
4460 N  N     . GLY B 279 ? 0.8774 0.9529 0.8907 -0.0340 0.0259  0.0111  259 GLY B N     
4461 C  CA    . GLY B 279 ? 0.8138 0.8851 0.8328 -0.0252 0.0257  0.0086  259 GLY B CA    
4462 C  C     . GLY B 279 ? 0.7297 0.7920 0.7462 -0.0221 0.0252  0.0091  259 GLY B C     
4463 O  O     . GLY B 279 ? 0.7839 0.8413 0.8042 -0.0156 0.0245  0.0078  259 GLY B O     
4464 N  N     . SER B 280 ? 0.7610 0.8206 0.7710 -0.0269 0.0251  0.0112  260 SER B N     
4465 C  CA    . SER B 280 ? 0.8867 0.9385 0.8944 -0.0243 0.0246  0.0116  260 SER B CA    
4466 C  C     . SER B 280 ? 0.8181 0.8782 0.8282 -0.0224 0.0276  0.0066  260 SER B C     
4467 O  O     . SER B 280 ? 0.7554 0.8281 0.7674 -0.0248 0.0302  0.0032  260 SER B O     
4468 C  CB    . SER B 280 ? 0.8607 0.9048 0.8600 -0.0300 0.0224  0.0161  260 SER B CB    
4469 O  OG    . SER B 280 ? 0.9397 0.9919 0.9347 -0.0376 0.0237  0.0164  260 SER B OG    
4470 N  N     . LEU B 281 ? 0.4966 0.5501 0.5068 -0.0182 0.0271  0.0060  261 LEU B N     
4471 C  CA    . LEU B 281 ? 0.6029 0.6623 0.6149 -0.0159 0.0293  0.0012  261 LEU B CA    
4472 C  C     . LEU B 281 ? 0.5233 0.5801 0.5285 -0.0203 0.0294  0.0028  261 LEU B C     
4473 O  O     . LEU B 281 ? 0.4730 0.5191 0.4754 -0.0189 0.0273  0.0055  261 LEU B O     
4474 C  CB    . LEU B 281 ? 0.5402 0.5942 0.5572 -0.0083 0.0283  -0.0010 261 LEU B CB    
4475 C  CG    . LEU B 281 ? 0.4708 0.5305 0.4906 -0.0049 0.0298  -0.0067 261 LEU B CG    
4476 C  CD1   . LEU B 281 ? 0.4155 0.4903 0.4393 -0.0059 0.0324  -0.0117 261 LEU B CD1   
4477 C  CD2   . LEU B 281 ? 0.3762 0.4295 0.4006 0.0022  0.0279  -0.0083 261 LEU B CD2   
4478 N  N     . PRO B 282 ? 0.4473 0.5138 0.4494 -0.0255 0.0317  0.0009  262 PRO B N     
4479 C  CA    . PRO B 282 ? 0.3729 0.4365 0.3671 -0.0308 0.0314  0.0030  262 PRO B CA    
4480 C  C     . PRO B 282 ? 0.3317 0.3938 0.3266 -0.0268 0.0322  -0.0003 262 PRO B C     
4481 O  O     . PRO B 282 ? 0.3603 0.4278 0.3614 -0.0213 0.0338  -0.0056 262 PRO B O     
4482 C  CB    . PRO B 282 ? 0.4326 0.5091 0.4236 -0.0383 0.0340  0.0017  262 PRO B CB    
4483 C  CG    . PRO B 282 ? 0.4486 0.5378 0.4482 -0.0342 0.0369  -0.0043 262 PRO B CG    
4484 C  CD    . PRO B 282 ? 0.3893 0.4708 0.3948 -0.0276 0.0346  -0.0032 262 PRO B CD    
4485 N  N     . PRO B 283 ? 0.3220 0.3765 0.3106 -0.0293 0.0306  0.0026  263 PRO B N     
4486 C  CA    . PRO B 283 ? 0.2782 0.3326 0.2666 -0.0268 0.0314  -0.0007 263 PRO B CA    
4487 C  C     . PRO B 283 ? 0.3356 0.4037 0.3231 -0.0298 0.0350  -0.0059 263 PRO B C     
4488 O  O     . PRO B 283 ? 0.3072 0.3839 0.2917 -0.0361 0.0366  -0.0055 263 PRO B O     
4489 C  CB    . PRO B 283 ? 0.3697 0.4137 0.3509 -0.0301 0.0285  0.0042  263 PRO B CB    
4490 C  CG    . PRO B 283 ? 0.3924 0.4348 0.3685 -0.0366 0.0268  0.0091  263 PRO B CG    
4491 C  CD    . PRO B 283 ? 0.3330 0.3784 0.3147 -0.0345 0.0273  0.0089  263 PRO B CD    
4492 N  N     . LEU B 284 ? 0.2687 0.3389 0.2586 -0.0255 0.0362  -0.0109 264 LEU B N     
4493 C  CA    . LEU B 284 ? 0.2486 0.3321 0.2381 -0.0274 0.0397  -0.0170 264 LEU B CA    
4494 C  C     . LEU B 284 ? 0.3145 0.3972 0.2945 -0.0342 0.0398  -0.0150 264 LEU B C     
4495 O  O     . LEU B 284 ? 0.3562 0.4269 0.3317 -0.0350 0.0369  -0.0103 264 LEU B O     
4496 C  CB    . LEU B 284 ? 0.2609 0.3462 0.2571 -0.0192 0.0402  -0.0238 264 LEU B CB    
4497 C  CG    . LEU B 284 ? 0.2653 0.3516 0.2706 -0.0123 0.0395  -0.0264 264 LEU B CG    
4498 C  CD1   . LEU B 284 ? 0.3103 0.3926 0.3203 -0.0044 0.0382  -0.0314 264 LEU B CD1   
4499 C  CD2   . LEU B 284 ? 0.2252 0.3284 0.2344 -0.0141 0.0427  -0.0313 264 LEU B CD2   
4500 N  N     . GLY B 285 ? 0.2840 0.3805 0.2615 -0.0390 0.0432  -0.0192 265 GLY B N     
4501 C  CA    . GLY B 285 ? 0.2830 0.3799 0.2505 -0.0467 0.0435  -0.0173 265 GLY B CA    
4502 C  C     . GLY B 285 ? 0.2818 0.3721 0.2482 -0.0428 0.0425  -0.0193 265 GLY B C     
4503 O  O     . GLY B 285 ? 0.3352 0.4311 0.3069 -0.0370 0.0443  -0.0264 265 GLY B O     
4504 N  N     . GLU B 286 ? 0.3233 0.4012 0.2830 -0.0456 0.0391  -0.0134 266 GLU B N     
4505 C  CA    . GLU B 286 ? 0.2865 0.3579 0.2442 -0.0429 0.0379  -0.0147 266 GLU B CA    
4506 C  C     . GLU B 286 ? 0.2967 0.3757 0.2461 -0.0497 0.0398  -0.0169 266 GLU B C     
4507 O  O     . GLU B 286 ? 0.2979 0.3802 0.2395 -0.0585 0.0399  -0.0133 266 GLU B O     
4508 C  CB    . GLU B 286 ? 0.3196 0.3747 0.2748 -0.0423 0.0331  -0.0077 266 GLU B CB    
4509 C  CG    . GLU B 286 ? 0.3218 0.3703 0.2749 -0.0402 0.0315  -0.0086 266 GLU B CG    
4510 C  CD    . GLU B 286 ? 0.3083 0.3427 0.2628 -0.0368 0.0273  -0.0036 266 GLU B CD    
4511 O  OE1   . GLU B 286 ? 0.2807 0.3101 0.2368 -0.0368 0.0253  0.0009  266 GLU B OE1   
4512 O  OE2   . GLU B 286 ? 0.2839 0.3129 0.2381 -0.0343 0.0259  -0.0046 266 GLU B OE2   
4513 N  N     . LEU B 287 ? 0.2611 0.3433 0.2119 -0.0460 0.0413  -0.0230 267 LEU B N     
4514 C  CA    . LEU B 287 ? 0.2820 0.3708 0.2246 -0.0521 0.0430  -0.0254 267 LEU B CA    
4515 C  C     . LEU B 287 ? 0.3326 0.4089 0.2660 -0.0572 0.0389  -0.0182 267 LEU B C     
4516 O  O     . LEU B 287 ? 0.3637 0.4266 0.2992 -0.0528 0.0352  -0.0146 267 LEU B O     
4517 C  CB    . LEU B 287 ? 0.3193 0.4131 0.2657 -0.0461 0.0449  -0.0340 267 LEU B CB    
4518 C  CG    . LEU B 287 ? 0.4149 0.5215 0.3707 -0.0400 0.0483  -0.0428 267 LEU B CG    
4519 C  CD1   . LEU B 287 ? 0.3816 0.4924 0.3390 -0.0353 0.0495  -0.0514 267 LEU B CD1   
4520 C  CD2   . LEU B 287 ? 0.4341 0.5570 0.3888 -0.0463 0.0522  -0.0446 267 LEU B CD2   
4521 N  N     . PRO B 288 ? 0.3648 0.4453 0.2878 -0.0668 0.0393  -0.0159 268 PRO B N     
4522 C  CA    . PRO B 288 ? 0.4317 0.4996 0.3457 -0.0717 0.0346  -0.0089 268 PRO B CA    
4523 C  C     . PRO B 288 ? 0.4730 0.5335 0.3872 -0.0672 0.0328  -0.0108 268 PRO B C     
4524 O  O     . PRO B 288 ? 0.5200 0.5671 0.4323 -0.0665 0.0280  -0.0053 268 PRO B O     
4525 C  CB    . PRO B 288 ? 0.4187 0.4953 0.3214 -0.0832 0.0360  -0.0078 268 PRO B CB    
4526 C  CG    . PRO B 288 ? 0.4238 0.5188 0.3299 -0.0826 0.0423  -0.0168 268 PRO B CG    
4527 C  CD    . PRO B 288 ? 0.3543 0.4520 0.2733 -0.0736 0.0439  -0.0204 268 PRO B CD    
4528 N  N     . THR B 289 ? 0.4225 0.4916 0.3388 -0.0642 0.0363  -0.0186 269 THR B N     
4529 C  CA    . THR B 289 ? 0.5659 0.6286 0.4815 -0.0605 0.0346  -0.0208 269 THR B CA    
4530 C  C     . THR B 289 ? 0.5618 0.6291 0.4868 -0.0515 0.0371  -0.0290 269 THR B C     
4531 O  O     . THR B 289 ? 0.4402 0.5193 0.3703 -0.0496 0.0409  -0.0346 269 THR B O     
4532 C  CB    . THR B 289 ? 0.5039 0.5707 0.4084 -0.0682 0.0352  -0.0217 269 THR B CB    
4533 O  OG1   . THR B 289 ? 0.7977 0.8584 0.7024 -0.0639 0.0336  -0.0245 269 THR B OG1   
4534 C  CG2   . THR B 289 ? 0.5779 0.6628 0.4806 -0.0720 0.0408  -0.0286 269 THR B CG2   
4535 N  N     . SER B 290 ? 0.5368 0.5942 0.4643 -0.0460 0.0345  -0.0296 270 SER B N     
4536 C  CA    . SER B 290 ? 0.4060 0.4660 0.3408 -0.0380 0.0358  -0.0374 270 SER B CA    
4537 C  C     . SER B 290 ? 0.3855 0.4599 0.3177 -0.0399 0.0399  -0.0459 270 SER B C     
4538 O  O     . SER B 290 ? 0.4221 0.4998 0.3451 -0.0467 0.0406  -0.0456 270 SER B O     
4539 C  CB    . SER B 290 ? 0.5072 0.5547 0.4426 -0.0339 0.0321  -0.0365 270 SER B CB    
4540 O  OG    . SER B 290 ? 0.4851 0.5351 0.4249 -0.0277 0.0329  -0.0447 270 SER B OG    
4541 N  N     . PRO B 291 ? 0.4272 0.5107 0.3672 -0.0339 0.0425  -0.0539 271 PRO B N     
4542 C  CA    . PRO B 291 ? 0.3786 0.4767 0.3170 -0.0346 0.0463  -0.0634 271 PRO B CA    
4543 C  C     . PRO B 291 ? 0.4712 0.5645 0.4067 -0.0320 0.0448  -0.0679 271 PRO B C     
4544 O  O     . PRO B 291 ? 0.4567 0.5615 0.3891 -0.0336 0.0477  -0.0755 271 PRO B O     
4545 C  CB    . PRO B 291 ? 0.4724 0.5795 0.4216 -0.0273 0.0483  -0.0705 271 PRO B CB    
4546 C  CG    . PRO B 291 ? 0.4285 0.5208 0.3845 -0.0204 0.0442  -0.0663 271 PRO B CG    
4547 C  CD    . PRO B 291 ? 0.4234 0.5043 0.3739 -0.0259 0.0417  -0.0551 271 PRO B CD    
4548 N  N     . ASP B 292 ? 0.4110 0.4883 0.3472 -0.0286 0.0403  -0.0636 272 ASP B N     
4549 C  CA    . ASP B 292 ? 0.3991 0.4701 0.3330 -0.0259 0.0382  -0.0674 272 ASP B CA    
4550 C  C     . ASP B 292 ? 0.4023 0.4593 0.3302 -0.0298 0.0342  -0.0586 272 ASP B C     
4551 O  O     . ASP B 292 ? 0.3655 0.4112 0.2975 -0.0269 0.0310  -0.0526 272 ASP B O     
4552 C  CB    . ASP B 292 ? 0.4031 0.4687 0.3462 -0.0158 0.0360  -0.0730 272 ASP B CB    
4553 C  CG    . ASP B 292 ? 0.3914 0.4496 0.3321 -0.0128 0.0332  -0.0773 272 ASP B CG    
4554 O  OD1   . ASP B 292 ? 0.3800 0.4367 0.3122 -0.0184 0.0330  -0.0755 272 ASP B OD1   
4555 O  OD2   . ASP B 292 ? 0.4300 0.4833 0.3772 -0.0050 0.0309  -0.0824 272 ASP B OD2   
4556 N  N     . PRO B 293 ? 0.3759 0.4340 0.2941 -0.0364 0.0343  -0.0575 273 PRO B N     
4557 C  CA    . PRO B 293 ? 0.3650 0.4103 0.2777 -0.0401 0.0300  -0.0491 273 PRO B CA    
4558 C  C     . PRO B 293 ? 0.3956 0.4283 0.3123 -0.0342 0.0260  -0.0490 273 PRO B C     
4559 O  O     . PRO B 293 ? 0.4305 0.4526 0.3458 -0.0357 0.0223  -0.0419 273 PRO B O     
4560 C  CB    . PRO B 293 ? 0.5012 0.5518 0.4026 -0.0481 0.0310  -0.0499 273 PRO B CB    
4561 C  CG    . PRO B 293 ? 0.4805 0.5442 0.3826 -0.0460 0.0352  -0.0607 273 PRO B CG    
4562 C  CD    . PRO B 293 ? 0.4359 0.5072 0.3475 -0.0409 0.0379  -0.0642 273 PRO B CD    
4563 N  N     . LYS B 294 ? 0.3689 0.4024 0.2907 -0.0275 0.0263  -0.0567 274 LYS B N     
4564 C  CA    . LYS B 294 ? 0.3635 0.3844 0.2888 -0.0224 0.0222  -0.0563 274 LYS B CA    
4565 C  C     . LYS B 294 ? 0.3849 0.3988 0.3187 -0.0175 0.0203  -0.0524 274 LYS B C     
4566 O  O     . LYS B 294 ? 0.3768 0.3798 0.3131 -0.0146 0.0167  -0.0504 274 LYS B O     
4567 C  CB    . LYS B 294 ? 0.4154 0.4382 0.3417 -0.0175 0.0222  -0.0661 274 LYS B CB    
4568 C  CG    . LYS B 294 ? 0.4586 0.4849 0.3758 -0.0222 0.0228  -0.0695 274 LYS B CG    
4569 C  CD    . LYS B 294 ? 0.5489 0.5747 0.4672 -0.0169 0.0218  -0.0790 274 LYS B CD    
4570 C  CE    . LYS B 294 ? 0.9106 0.9215 0.8275 -0.0157 0.0166  -0.0762 274 LYS B CE    
4571 N  NZ    . LYS B 294 ? 1.0217 1.0315 0.9371 -0.0119 0.0151  -0.0853 274 LYS B NZ    
4572 N  N     . ALA B 295 ? 0.3124 0.3324 0.2503 -0.0170 0.0228  -0.0513 275 ALA B N     
4573 C  CA    . ALA B 295 ? 0.3225 0.3358 0.2676 -0.0131 0.0210  -0.0470 275 ALA B CA    
4574 C  C     . ALA B 295 ? 0.2756 0.2802 0.2188 -0.0166 0.0183  -0.0379 275 ALA B C     
4575 O  O     . ALA B 295 ? 0.3698 0.3758 0.3069 -0.0225 0.0184  -0.0339 275 ALA B O     
4576 C  CB    . ALA B 295 ? 0.3512 0.3735 0.3009 -0.0120 0.0241  -0.0480 275 ALA B CB    
4577 N  N     . GLY B 296 ? 0.2999 0.2958 0.2484 -0.0130 0.0156  -0.0348 276 GLY B N     
4578 C  CA    . GLY B 296 ? 0.3429 0.3324 0.2915 -0.0154 0.0133  -0.0269 276 GLY B CA    
4579 C  C     . GLY B 296 ? 0.3112 0.2907 0.2617 -0.0134 0.0096  -0.0252 276 GLY B C     
4580 O  O     . GLY B 296 ? 0.2857 0.2618 0.2384 -0.0096 0.0084  -0.0293 276 GLY B O     
4581 N  N     . LEU B 297 ? 0.2908 0.2660 0.2406 -0.0161 0.0074  -0.0190 277 LEU B N     
4582 C  CA    . LEU B 297 ? 0.2619 0.2292 0.2140 -0.0152 0.0041  -0.0164 277 LEU B CA    
4583 C  C     . LEU B 297 ? 0.2866 0.2508 0.2336 -0.0177 0.0019  -0.0172 277 LEU B C     
4584 O  O     . LEU B 297 ? 0.2830 0.2494 0.2245 -0.0217 0.0018  -0.0160 277 LEU B O     
4585 C  CB    . LEU B 297 ? 0.2611 0.2270 0.2161 -0.0165 0.0029  -0.0101 277 LEU B CB    
4586 C  CG    . LEU B 297 ? 0.2542 0.2144 0.2116 -0.0166 -0.0003 -0.0069 277 LEU B CG    
4587 C  CD1   . LEU B 297 ? 0.2533 0.2095 0.2150 -0.0134 -0.0010 -0.0084 277 LEU B CD1   
4588 C  CD2   . LEU B 297 ? 0.2738 0.2347 0.2339 -0.0177 -0.0012 -0.0018 277 LEU B CD2   
4589 N  N     . TYR B 298 ? 0.2711 0.2293 0.2193 -0.0158 -0.0004 -0.0191 278 TYR B N     
4590 C  CA    . TYR B 298 ? 0.2775 0.2318 0.2213 -0.0180 -0.0029 -0.0201 278 TYR B CA    
4591 C  C     . TYR B 298 ? 0.3191 0.2669 0.2660 -0.0183 -0.0063 -0.0163 278 TYR B C     
4592 O  O     . TYR B 298 ? 0.2730 0.2177 0.2246 -0.0157 -0.0069 -0.0159 278 TYR B O     
4593 C  CB    . TYR B 298 ? 0.2848 0.2382 0.2263 -0.0156 -0.0028 -0.0271 278 TYR B CB    
4594 C  CG    . TYR B 298 ? 0.3124 0.2739 0.2501 -0.0159 0.0006  -0.0319 278 TYR B CG    
4595 C  CD1   . TYR B 298 ? 0.3042 0.2719 0.2453 -0.0133 0.0038  -0.0343 278 TYR B CD1   
4596 C  CD2   . TYR B 298 ? 0.3264 0.2900 0.2571 -0.0193 0.0007  -0.0342 278 TYR B CD2   
4597 C  CE1   . TYR B 298 ? 0.3074 0.2843 0.2452 -0.0143 0.0072  -0.0390 278 TYR B CE1   
4598 C  CE2   . TYR B 298 ? 0.3618 0.3341 0.2886 -0.0204 0.0041  -0.0388 278 TYR B CE2   
4599 C  CZ    . TYR B 298 ? 0.3544 0.3338 0.2849 -0.0180 0.0075  -0.0412 278 TYR B CZ    
4600 O  OH    . TYR B 298 ? 0.3597 0.3494 0.2865 -0.0197 0.0111  -0.0461 278 TYR B OH    
4601 N  N     . ILE B 299 ? 0.2772 0.2236 0.2217 -0.0217 -0.0086 -0.0134 279 ILE B N     
4602 C  CA    . ILE B 299 ? 0.2751 0.2176 0.2230 -0.0227 -0.0116 -0.0098 279 ILE B CA    
4603 C  C     . ILE B 299 ? 0.3377 0.2760 0.2813 -0.0250 -0.0146 -0.0112 279 ILE B C     
4604 O  O     . ILE B 299 ? 0.3256 0.2653 0.2637 -0.0272 -0.0148 -0.0123 279 ILE B O     
4605 C  CB    . ILE B 299 ? 0.2692 0.2149 0.2197 -0.0243 -0.0121 -0.0047 279 ILE B CB    
4606 C  CG1   . ILE B 299 ? 0.3023 0.2517 0.2565 -0.0221 -0.0092 -0.0036 279 ILE B CG1   
4607 C  CG2   . ILE B 299 ? 0.2672 0.2110 0.2218 -0.0255 -0.0150 -0.0017 279 ILE B CG2   
4608 C  CD1   . ILE B 299 ? 0.2967 0.2489 0.2532 -0.0231 -0.0099 0.0007  279 ILE B CD1   
4609 N  N     . LYS B 300 ? 0.3153 0.2485 0.2610 -0.0250 -0.0170 -0.0109 280 LYS B N     
4610 C  CA    . LYS B 300 ? 0.2989 0.2277 0.2410 -0.0275 -0.0203 -0.0119 280 LYS B CA    
4611 C  C     . LYS B 300 ? 0.3350 0.2641 0.2809 -0.0302 -0.0228 -0.0072 280 LYS B C     
4612 O  O     . LYS B 300 ? 0.3514 0.2781 0.3011 -0.0304 -0.0240 -0.0058 280 LYS B O     
4613 C  CB    . LYS B 300 ? 0.3331 0.2552 0.2737 -0.0257 -0.0218 -0.0161 280 LYS B CB    
4614 C  CG    . LYS B 300 ? 0.4847 0.4015 0.4208 -0.0283 -0.0254 -0.0175 280 LYS B CG    
4615 C  CD    . LYS B 300 ? 0.6596 0.5679 0.5949 -0.0268 -0.0280 -0.0208 280 LYS B CD    
4616 C  CE    . LYS B 300 ? 0.6702 0.5774 0.6017 -0.0231 -0.0270 -0.0277 280 LYS B CE    
4617 N  NZ    . LYS B 300 ? 0.7235 0.6330 0.6489 -0.0251 -0.0268 -0.0304 280 LYS B NZ    
4618 N  N     . SER B 301 ? 0.3090 0.2414 0.2540 -0.0325 -0.0239 -0.0050 281 SER B N     
4619 C  CA    . SER B 301 ? 0.2967 0.2310 0.2459 -0.0348 -0.0265 -0.0013 281 SER B CA    
4620 C  C     . SER B 301 ? 0.3629 0.2929 0.3101 -0.0376 -0.0299 -0.0021 281 SER B C     
4621 O  O     . SER B 301 ? 0.3363 0.2608 0.2786 -0.0375 -0.0305 -0.0054 281 SER B O     
4622 C  CB    . SER B 301 ? 0.3506 0.2890 0.2993 -0.0359 -0.0275 0.0010  281 SER B CB    
4623 O  OG    . SER B 301 ? 0.3783 0.3145 0.3205 -0.0383 -0.0297 -0.0003 281 SER B OG    
4624 N  N     . ARG B 302 ? 0.3390 0.2719 0.2902 -0.0399 -0.0324 0.0007  282 ARG B N     
4625 C  CA    . ARG B 302 ? 0.4178 0.3477 0.3677 -0.0433 -0.0359 0.0006  282 ARG B CA    
4626 C  C     . ARG B 302 ? 0.4328 0.3597 0.3757 -0.0449 -0.0380 -0.0013 282 ARG B C     
4627 O  O     . ARG B 302 ? 0.4174 0.3407 0.3581 -0.0477 -0.0410 -0.0020 282 ARG B O     
4628 C  CB    . ARG B 302 ? 0.4580 0.3939 0.4146 -0.0455 -0.0378 0.0037  282 ARG B CB    
4629 C  CG    . ARG B 302 ? 0.6290 0.5660 0.5905 -0.0465 -0.0372 0.0050  282 ARG B CG    
4630 C  CD    . ARG B 302 ? 0.7096 0.6546 0.6779 -0.0491 -0.0390 0.0072  282 ARG B CD    
4631 N  NE    . ARG B 302 ? 0.7118 0.6566 0.6784 -0.0522 -0.0428 0.0071  282 ARG B NE    
4632 C  CZ    . ARG B 302 ? 0.9427 0.8951 0.9151 -0.0545 -0.0450 0.0083  282 ARG B CZ    
4633 N  NH1   . ARG B 302 ? 0.7442 0.7053 0.7245 -0.0540 -0.0437 0.0095  282 ARG B NH1   
4634 N  NH2   . ARG B 302 ? 0.9685 0.9203 0.9390 -0.0571 -0.0487 0.0080  282 ARG B NH2   
4635 N  N     . THR B 303 ? 0.3788 0.3072 0.3177 -0.0439 -0.0367 -0.0021 283 THR B N     
4636 C  CA    . THR B 303 ? 0.4179 0.3431 0.3488 -0.0457 -0.0382 -0.0045 283 THR B CA    
4637 C  C     . THR B 303 ? 0.4758 0.3953 0.4018 -0.0446 -0.0372 -0.0092 283 THR B C     
4638 O  O     . THR B 303 ? 0.5203 0.4365 0.4399 -0.0463 -0.0390 -0.0119 283 THR B O     
4639 C  CB    . THR B 303 ? 0.3891 0.3172 0.3156 -0.0456 -0.0369 -0.0042 283 THR B CB    
4640 O  OG1   . THR B 303 ? 0.4442 0.3733 0.3701 -0.0427 -0.0325 -0.0063 283 THR B OG1   
4641 C  CG2   . THR B 303 ? 0.4518 0.3843 0.3829 -0.0460 -0.0386 0.0001  283 THR B CG2   
4642 N  N     . GLY B 304 ? 0.3951 0.3131 0.3239 -0.0416 -0.0349 -0.0105 284 GLY B N     
4643 C  CA    . GLY B 304 ? 0.4276 0.3401 0.3527 -0.0396 -0.0345 -0.0155 284 GLY B CA    
4644 C  C     . GLY B 304 ? 0.4279 0.3431 0.3489 -0.0371 -0.0310 -0.0195 284 GLY B C     
4645 O  O     . GLY B 304 ? 0.4488 0.3607 0.3678 -0.0344 -0.0304 -0.0246 284 GLY B O     
4646 N  N     . GLN B 305 ? 0.4073 0.3287 0.3275 -0.0379 -0.0290 -0.0176 285 GLN B N     
4647 C  CA    . GLN B 305 ? 0.3568 0.2823 0.2726 -0.0369 -0.0256 -0.0210 285 GLN B CA    
4648 C  C     . GLN B 305 ? 0.4041 0.3338 0.3248 -0.0339 -0.0220 -0.0199 285 GLN B C     
4649 O  O     . GLN B 305 ? 0.4022 0.3337 0.3281 -0.0340 -0.0221 -0.0151 285 GLN B O     
4650 C  CB    . GLN B 305 ? 0.4647 0.3935 0.3747 -0.0408 -0.0262 -0.0191 285 GLN B CB    
4651 C  CG    . GLN B 305 ? 0.3971 0.3314 0.3019 -0.0411 -0.0225 -0.0216 285 GLN B CG    
4652 C  CD    . GLN B 305 ? 0.4510 0.3877 0.3496 -0.0459 -0.0239 -0.0185 285 GLN B CD    
4653 O  OE1   . GLN B 305 ? 0.6015 0.5397 0.4919 -0.0485 -0.0233 -0.0216 285 GLN B OE1   
4654 N  NE2   . GLN B 305 ? 0.3817 0.3186 0.2838 -0.0470 -0.0259 -0.0126 285 GLN B NE2   
4655 N  N     . THR B 306 ? 0.3787 0.3108 0.2980 -0.0312 -0.0189 -0.0248 286 THR B N     
4656 C  CA    . THR B 306 ? 0.3460 0.2824 0.2697 -0.0284 -0.0155 -0.0243 286 THR B CA    
4657 C  C     . THR B 306 ? 0.3618 0.3052 0.2818 -0.0309 -0.0130 -0.0230 286 THR B C     
4658 O  O     . THR B 306 ? 0.3916 0.3377 0.3048 -0.0329 -0.0121 -0.0264 286 THR B O     
4659 C  CB    . THR B 306 ? 0.3745 0.3102 0.2994 -0.0239 -0.0139 -0.0305 286 THR B CB    
4660 O  OG1   . THR B 306 ? 0.4185 0.3461 0.3459 -0.0222 -0.0172 -0.0312 286 THR B OG1   
4661 C  CG2   . THR B 306 ? 0.3725 0.3134 0.3022 -0.0211 -0.0104 -0.0301 286 THR B CG2   
4662 N  N     . VAL B 307 ? 0.3230 0.2690 0.2469 -0.0310 -0.0121 -0.0183 287 VAL B N     
4663 C  CA    . VAL B 307 ? 0.3420 0.2934 0.2623 -0.0338 -0.0104 -0.0162 287 VAL B CA    
4664 C  C     . VAL B 307 ? 0.3548 0.3105 0.2796 -0.0311 -0.0069 -0.0162 287 VAL B C     
4665 O  O     . VAL B 307 ? 0.3197 0.2737 0.2513 -0.0277 -0.0068 -0.0154 287 VAL B O     
4666 C  CB    . VAL B 307 ? 0.3514 0.3011 0.2712 -0.0370 -0.0138 -0.0101 287 VAL B CB    
4667 C  CG1   . VAL B 307 ? 0.3769 0.3227 0.2921 -0.0399 -0.0174 -0.0103 287 VAL B CG1   
4668 C  CG2   . VAL B 307 ? 0.3280 0.2762 0.2563 -0.0346 -0.0149 -0.0063 287 VAL B CG2   
4669 N  N     . GLN B 308 ? 0.2993 0.2610 0.2198 -0.0333 -0.0043 -0.0170 288 GLN B N     
4670 C  CA    . GLN B 308 ? 0.3043 0.2708 0.2285 -0.0317 -0.0012 -0.0163 288 GLN B CA    
4671 C  C     . GLN B 308 ? 0.3303 0.2957 0.2554 -0.0339 -0.0030 -0.0097 288 GLN B C     
4672 O  O     . GLN B 308 ? 0.3465 0.3102 0.2664 -0.0380 -0.0056 -0.0065 288 GLN B O     
4673 C  CB    . GLN B 308 ? 0.2926 0.2670 0.2117 -0.0334 0.0026  -0.0209 288 GLN B CB    
4674 C  CG    . GLN B 308 ? 0.3152 0.2959 0.2383 -0.0315 0.0062  -0.0218 288 GLN B CG    
4675 C  CD    . GLN B 308 ? 0.4226 0.4129 0.3408 -0.0337 0.0101  -0.0272 288 GLN B CD    
4676 O  OE1   . GLN B 308 ? 0.5328 0.5253 0.4431 -0.0383 0.0100  -0.0283 288 GLN B OE1   
4677 N  NE2   . GLN B 308 ? 0.4089 0.4056 0.3317 -0.0305 0.0134  -0.0307 288 GLN B NE2   
4678 N  N     . VAL B 309 ? 0.2762 0.2421 0.2079 -0.0310 -0.0020 -0.0077 289 VAL B N     
4679 C  CA    . VAL B 309 ? 0.2721 0.2367 0.2058 -0.0321 -0.0039 -0.0021 289 VAL B CA    
4680 C  C     . VAL B 309 ? 0.3374 0.3064 0.2732 -0.0313 -0.0009 -0.0018 289 VAL B C     
4681 O  O     . VAL B 309 ? 0.3441 0.3152 0.2847 -0.0275 0.0018  -0.0046 289 VAL B O     
4682 C  CB    . VAL B 309 ? 0.2938 0.2540 0.2344 -0.0294 -0.0065 0.0004  289 VAL B CB    
4683 C  CG1   . VAL B 309 ? 0.3357 0.2956 0.2791 -0.0297 -0.0084 0.0052  289 VAL B CG1   
4684 C  CG2   . VAL B 309 ? 0.3046 0.2610 0.2433 -0.0308 -0.0098 0.0003  289 VAL B CG2   
4685 N  N     . LYS B 310 ? 0.3113 0.2813 0.2431 -0.0349 -0.0017 0.0016  290 LYS B N     
4686 C  CA    . LYS B 310 ? 0.3154 0.2898 0.2482 -0.0351 0.0009  0.0022  290 LYS B CA    
4687 C  C     . LYS B 310 ? 0.3348 0.3057 0.2718 -0.0340 -0.0016 0.0070  290 LYS B C     
4688 O  O     . LYS B 310 ? 0.3861 0.3522 0.3226 -0.0350 -0.0058 0.0104  290 LYS B O     
4689 C  CB    . LYS B 310 ? 0.3835 0.3623 0.3074 -0.0410 0.0020  0.0022  290 LYS B CB    
4690 C  CG    . LYS B 310 ? 0.3964 0.3810 0.3167 -0.0417 0.0054  -0.0038 290 LYS B CG    
4691 C  CD    . LYS B 310 ? 0.5238 0.5140 0.4347 -0.0485 0.0067  -0.0039 290 LYS B CD    
4692 C  CE    . LYS B 310 ? 0.5898 0.5874 0.4974 -0.0490 0.0104  -0.0109 290 LYS B CE    
4693 N  NZ    . LYS B 310 ? 0.6702 0.6749 0.5845 -0.0442 0.0148  -0.0164 290 LYS B NZ    
4694 N  N     . ILE B 311 ? 0.2835 0.2572 0.2253 -0.0316 0.0009  0.0069  291 ILE B N     
4695 C  CA    . ILE B 311 ? 0.2616 0.2329 0.2071 -0.0305 -0.0010 0.0108  291 ILE B CA    
4696 C  C     . ILE B 311 ? 0.2836 0.2574 0.2241 -0.0346 -0.0005 0.0126  291 ILE B C     
4697 O  O     . ILE B 311 ? 0.2991 0.2789 0.2390 -0.0351 0.0035  0.0100  291 ILE B O     
4698 C  CB    . ILE B 311 ? 0.2548 0.2270 0.2087 -0.0254 0.0010  0.0096  291 ILE B CB    
4699 C  CG1   . ILE B 311 ? 0.3259 0.2957 0.2840 -0.0223 0.0004  0.0080  291 ILE B CG1   
4700 C  CG2   . ILE B 311 ? 0.3075 0.2778 0.2649 -0.0244 -0.0009 0.0132  291 ILE B CG2   
4701 C  CD1   . ILE B 311 ? 0.3749 0.3453 0.3399 -0.0181 0.0023  0.0068  291 ILE B CD1   
4702 N  N     . PRO B 312 ? 0.3007 0.2700 0.2372 -0.0378 -0.0047 0.0170  292 PRO B N     
4703 C  CA    . PRO B 312 ? 0.2988 0.2695 0.2302 -0.0423 -0.0047 0.0193  292 PRO B CA    
4704 C  C     . PRO B 312 ? 0.2690 0.2429 0.2064 -0.0392 -0.0018 0.0187  292 PRO B C     
4705 O  O     . PRO B 312 ? 0.3011 0.2732 0.2461 -0.0341 -0.0021 0.0186  292 PRO B O     
4706 C  CB    . PRO B 312 ? 0.3260 0.2886 0.2539 -0.0446 -0.0112 0.0242  292 PRO B CB    
4707 C  CG    . PRO B 312 ? 0.3276 0.2867 0.2563 -0.0430 -0.0141 0.0237  292 PRO B CG    
4708 C  CD    . PRO B 312 ? 0.3162 0.2789 0.2529 -0.0375 -0.0101 0.0198  292 PRO B CD    
4709 N  N     . ARG B 313 ? 0.2772 0.2567 0.2111 -0.0428 0.0010  0.0182  293 ARG B N     
4710 C  CA    . ARG B 313 ? 0.2755 0.2591 0.2150 -0.0401 0.0041  0.0171  293 ARG B CA    
4711 C  C     . ARG B 313 ? 0.2824 0.2601 0.2256 -0.0380 0.0007  0.0208  293 ARG B C     
4712 O  O     . ARG B 313 ? 0.2926 0.2717 0.2427 -0.0336 0.0025  0.0198  293 ARG B O     
4713 C  CB    . ARG B 313 ? 0.2995 0.2908 0.2340 -0.0453 0.0072  0.0163  293 ARG B CB    
4714 C  CG    . ARG B 313 ? 0.3533 0.3502 0.2941 -0.0424 0.0107  0.0144  293 ARG B CG    
4715 C  CD    . ARG B 313 ? 0.3389 0.3460 0.2758 -0.0473 0.0146  0.0123  293 ARG B CD    
4716 N  NE    . ARG B 313 ? 0.3781 0.3930 0.3136 -0.0477 0.0181  0.0069  293 ARG B NE    
4717 C  CZ    . ARG B 313 ? 0.4593 0.4850 0.3913 -0.0521 0.0218  0.0039  293 ARG B CZ    
4718 N  NH1   . ARG B 313 ? 0.5491 0.5793 0.4785 -0.0571 0.0225  0.0060  293 ARG B NH1   
4719 N  NH2   . ARG B 313 ? 0.4315 0.4640 0.3625 -0.0517 0.0247  -0.0017 293 ARG B NH2   
4720 N  N     . ASP B 314 ? 0.2916 0.2622 0.2301 -0.0409 -0.0046 0.0249  294 ASP B N     
4721 C  CA    . ASP B 314 ? 0.3327 0.2976 0.2744 -0.0389 -0.0085 0.0279  294 ASP B CA    
4722 C  C     . ASP B 314 ? 0.3181 0.2787 0.2663 -0.0334 -0.0112 0.0276  294 ASP B C     
4723 O  O     . ASP B 314 ? 0.3338 0.2897 0.2848 -0.0313 -0.0150 0.0295  294 ASP B O     
4724 C  CB    . ASP B 314 ? 0.3541 0.3130 0.2874 -0.0449 -0.0137 0.0324  294 ASP B CB    
4725 C  CG    . ASP B 314 ? 0.4458 0.3995 0.3726 -0.0481 -0.0182 0.0341  294 ASP B CG    
4726 O  OD1   . ASP B 314 ? 0.4372 0.3935 0.3644 -0.0471 -0.0163 0.0317  294 ASP B OD1   
4727 O  OD2   . ASP B 314 ? 0.6214 0.5677 0.5420 -0.0520 -0.0242 0.0382  294 ASP B OD2   
4728 N  N     . CYS B 315 ? 0.2847 0.2474 0.2357 -0.0310 -0.0094 0.0249  295 CYS B N     
4729 C  CA    . CYS B 315 ? 0.2568 0.2168 0.2136 -0.0267 -0.0117 0.0245  295 CYS B CA    
4730 C  C     . CYS B 315 ? 0.2626 0.2267 0.2268 -0.0222 -0.0075 0.0215  295 CYS B C     
4731 O  O     . CYS B 315 ? 0.2525 0.2209 0.2169 -0.0220 -0.0032 0.0194  295 CYS B O     
4732 C  CB    . CYS B 315 ? 0.2622 0.2198 0.2152 -0.0287 -0.0144 0.0247  295 CYS B CB    
4733 S  SG    . CYS B 315 ? 0.3436 0.2940 0.2882 -0.0336 -0.0213 0.0288  295 CYS B SG    
4734 N  N     . ILE B 316 ? 0.2375 0.2006 0.2077 -0.0186 -0.0092 0.0212  296 ILE B N     
4735 C  CA    . ILE B 316 ? 0.2237 0.1898 0.1999 -0.0152 -0.0061 0.0189  296 ILE B CA    
4736 C  C     . ILE B 316 ? 0.2924 0.2576 0.2693 -0.0151 -0.0076 0.0181  296 ILE B C     
4737 O  O     . ILE B 316 ? 0.3333 0.2963 0.3101 -0.0155 -0.0116 0.0193  296 ILE B O     
4738 C  CB    . ILE B 316 ? 0.2543 0.2212 0.2370 -0.0118 -0.0063 0.0192  296 ILE B CB    
4739 C  CG1   . ILE B 316 ? 0.2316 0.1986 0.2133 -0.0121 -0.0054 0.0203  296 ILE B CG1   
4740 C  CG2   . ILE B 316 ? 0.3056 0.2753 0.2933 -0.0094 -0.0033 0.0173  296 ILE B CG2   
4741 C  CD1   . ILE B 316 ? 0.3163 0.2832 0.3033 -0.0091 -0.0068 0.0207  296 ILE B CD1   
4742 N  N     . ALA B 317 ? 0.2386 0.2053 0.2164 -0.0145 -0.0049 0.0159  297 ALA B N     
4743 C  CA    . ALA B 317 ? 0.2281 0.1940 0.2068 -0.0146 -0.0065 0.0152  297 ALA B CA    
4744 C  C     . ALA B 317 ? 0.2414 0.2089 0.2262 -0.0123 -0.0053 0.0143  297 ALA B C     
4745 O  O     . ALA B 317 ? 0.2235 0.1922 0.2107 -0.0106 -0.0028 0.0138  297 ALA B O     
4746 C  CB    . ALA B 317 ? 0.2602 0.2253 0.2335 -0.0167 -0.0054 0.0134  297 ALA B CB    
4747 N  N     . PHE B 318 ? 0.2225 0.1900 0.2094 -0.0126 -0.0074 0.0143  298 PHE B N     
4748 C  CA    . PHE B 318 ? 0.2222 0.1916 0.2139 -0.0117 -0.0065 0.0137  298 PHE B CA    
4749 C  C     . PHE B 318 ? 0.2438 0.2116 0.2338 -0.0135 -0.0074 0.0127  298 PHE B C     
4750 O  O     . PHE B 318 ? 0.2382 0.2055 0.2269 -0.0149 -0.0102 0.0130  298 PHE B O     
4751 C  CB    . PHE B 318 ? 0.2531 0.2262 0.2507 -0.0105 -0.0082 0.0143  298 PHE B CB    
4752 C  CG    . PHE B 318 ? 0.2132 0.1875 0.2127 -0.0084 -0.0073 0.0149  298 PHE B CG    
4753 C  CD1   . PHE B 318 ? 0.2151 0.1912 0.2172 -0.0073 -0.0045 0.0146  298 PHE B CD1   
4754 C  CD2   . PHE B 318 ? 0.2595 0.2322 0.2573 -0.0081 -0.0096 0.0159  298 PHE B CD2   
4755 C  CE1   . PHE B 318 ? 0.2406 0.2176 0.2442 -0.0055 -0.0038 0.0151  298 PHE B CE1   
4756 C  CE2   . PHE B 318 ? 0.2379 0.2108 0.2369 -0.0065 -0.0091 0.0164  298 PHE B CE2   
4757 C  CZ    . PHE B 318 ? 0.2523 0.2278 0.2546 -0.0050 -0.0060 0.0159  298 PHE B CZ    
4758 N  N     . GLN B 319 ? 0.2213 0.1875 0.2109 -0.0136 -0.0057 0.0117  299 GLN B N     
4759 C  CA    . GLN B 319 ? 0.2250 0.1889 0.2133 -0.0154 -0.0070 0.0109  299 GLN B CA    
4760 C  C     . GLN B 319 ? 0.2679 0.2342 0.2607 -0.0164 -0.0075 0.0117  299 GLN B C     
4761 O  O     . GLN B 319 ? 0.2237 0.1917 0.2193 -0.0155 -0.0059 0.0123  299 GLN B O     
4762 C  CB    . GLN B 319 ? 0.2408 0.2003 0.2251 -0.0151 -0.0058 0.0088  299 GLN B CB    
4763 C  CG    . GLN B 319 ? 0.2886 0.2468 0.2677 -0.0155 -0.0058 0.0072  299 GLN B CG    
4764 C  CD    . GLN B 319 ? 0.3244 0.2795 0.3005 -0.0144 -0.0046 0.0041  299 GLN B CD    
4765 O  OE1   . GLN B 319 ? 0.2848 0.2406 0.2621 -0.0122 -0.0026 0.0031  299 GLN B OE1   
4766 N  NE2   . GLN B 319 ? 0.2633 0.2153 0.2359 -0.0156 -0.0060 0.0021  299 GLN B NE2   
4767 N  N     . THR B 320 ? 0.2255 0.1922 0.2186 -0.0187 -0.0097 0.0118  300 THR B N     
4768 C  CA    . THR B 320 ? 0.2416 0.2111 0.2381 -0.0208 -0.0101 0.0125  300 THR B CA    
4769 C  C     . THR B 320 ? 0.2436 0.2078 0.2374 -0.0220 -0.0096 0.0124  300 THR B C     
4770 O  O     . THR B 320 ? 0.2988 0.2569 0.2881 -0.0215 -0.0099 0.0111  300 THR B O     
4771 C  CB    . THR B 320 ? 0.2436 0.2152 0.2410 -0.0233 -0.0128 0.0124  300 THR B CB    
4772 O  OG1   . THR B 320 ? 0.3072 0.2727 0.2990 -0.0242 -0.0141 0.0115  300 THR B OG1   
4773 C  CG2   . THR B 320 ? 0.3047 0.2820 0.3062 -0.0220 -0.0142 0.0125  300 THR B CG2   
4774 N  N     . GLY B 321 ? 0.2271 0.1937 0.2234 -0.0239 -0.0091 0.0136  301 GLY B N     
4775 C  CA    . GLY B 321 ? 0.2320 0.1927 0.2254 -0.0258 -0.0098 0.0141  301 GLY B CA    
4776 C  C     . GLY B 321 ? 0.2585 0.2213 0.2526 -0.0308 -0.0114 0.0154  301 GLY B C     
4777 O  O     . GLY B 321 ? 0.2321 0.2030 0.2304 -0.0324 -0.0115 0.0156  301 GLY B O     
4778 N  N     . GLU B 322 ? 0.2416 0.1974 0.2319 -0.0334 -0.0130 0.0163  302 GLU B N     
4779 C  CA    . GLU B 322 ? 0.2465 0.2030 0.2361 -0.0393 -0.0151 0.0178  302 GLU B CA    
4780 C  C     . GLU B 322 ? 0.2621 0.2288 0.2562 -0.0424 -0.0134 0.0194  302 GLU B C     
4781 O  O     . GLU B 322 ? 0.2746 0.2473 0.2705 -0.0469 -0.0143 0.0200  302 GLU B O     
4782 C  CB    . GLU B 322 ? 0.2631 0.2082 0.2468 -0.0416 -0.0179 0.0187  302 GLU B CB    
4783 C  CG    . GLU B 322 ? 0.2812 0.2165 0.2604 -0.0388 -0.0201 0.0163  302 GLU B CG    
4784 C  CD    . GLU B 322 ? 0.3309 0.2547 0.3045 -0.0417 -0.0242 0.0169  302 GLU B CD    
4785 O  OE1   . GLU B 322 ? 0.4697 0.3918 0.4413 -0.0469 -0.0269 0.0181  302 GLU B OE1   
4786 O  OE2   . GLU B 322 ? 0.4473 0.3635 0.4185 -0.0390 -0.0252 0.0162  302 GLU B OE2   
4787 N  N     . ALA B 323 ? 0.2659 0.2355 0.2619 -0.0402 -0.0110 0.0198  303 ALA B N     
4788 C  CA    . ALA B 323 ? 0.2380 0.2184 0.2382 -0.0431 -0.0091 0.0206  303 ALA B CA    
4789 C  C     . ALA B 323 ? 0.2631 0.2548 0.2699 -0.0415 -0.0082 0.0187  303 ALA B C     
4790 O  O     . ALA B 323 ? 0.2511 0.2528 0.2616 -0.0452 -0.0078 0.0185  303 ALA B O     
4791 C  CB    . ALA B 323 ? 0.2653 0.2460 0.2659 -0.0408 -0.0069 0.0212  303 ALA B CB    
4792 N  N     . LEU B 324 ? 0.2377 0.2281 0.2458 -0.0363 -0.0081 0.0171  304 LEU B N     
4793 C  CA    A LEU B 324 ? 0.2197 0.2190 0.2335 -0.0346 -0.0085 0.0153  304 LEU B CA    
4794 C  CA    B LEU B 324 ? 0.2198 0.2187 0.2335 -0.0344 -0.0085 0.0153  304 LEU B CA    
4795 C  C     . LEU B 324 ? 0.2544 0.2549 0.2682 -0.0380 -0.0110 0.0151  304 LEU B C     
4796 O  O     . LEU B 324 ? 0.2352 0.2460 0.2546 -0.0393 -0.0115 0.0139  304 LEU B O     
4797 C  CB    A LEU B 324 ? 0.2461 0.2423 0.2600 -0.0289 -0.0085 0.0142  304 LEU B CB    
4798 C  CB    B LEU B 324 ? 0.2441 0.2391 0.2573 -0.0289 -0.0087 0.0143  304 LEU B CB    
4799 C  CG    A LEU B 324 ? 0.2590 0.2634 0.2789 -0.0264 -0.0096 0.0125  304 LEU B CG    
4800 C  CG    B LEU B 324 ? 0.2296 0.2300 0.2470 -0.0268 -0.0105 0.0127  304 LEU B CG    
4801 C  CD1   A LEU B 324 ? 0.2838 0.2879 0.3051 -0.0215 -0.0087 0.0118  304 LEU B CD1   
4802 C  CD1   B LEU B 324 ? 0.2102 0.2222 0.2350 -0.0262 -0.0097 0.0113  304 LEU B CD1   
4803 C  CD2   A LEU B 324 ? 0.2159 0.2177 0.2344 -0.0269 -0.0126 0.0121  304 LEU B CD2   
4804 C  CD2   B LEU B 324 ? 0.2489 0.2438 0.2640 -0.0226 -0.0110 0.0125  304 LEU B CD2   
4805 N  N     . GLU B 325 ? 0.2454 0.2360 0.2533 -0.0396 -0.0128 0.0159  305 GLU B N     
4806 C  CA    . GLU B 325 ? 0.2344 0.2255 0.2416 -0.0435 -0.0155 0.0159  305 GLU B CA    
4807 C  C     . GLU B 325 ? 0.2799 0.2788 0.2895 -0.0496 -0.0154 0.0169  305 GLU B C     
4808 O  O     . GLU B 325 ? 0.2610 0.2687 0.2749 -0.0520 -0.0165 0.0160  305 GLU B O     
4809 C  CB    . GLU B 325 ? 0.2609 0.2392 0.2608 -0.0442 -0.0175 0.0163  305 GLU B CB    
4810 C  CG    . GLU B 325 ? 0.2476 0.2249 0.2458 -0.0486 -0.0205 0.0164  305 GLU B CG    
4811 C  CD    . GLU B 325 ? 0.3978 0.3621 0.3886 -0.0489 -0.0228 0.0162  305 GLU B CD    
4812 O  OE1   . GLU B 325 ? 0.3219 0.2801 0.3099 -0.0444 -0.0220 0.0149  305 GLU B OE1   
4813 O  OE2   . GLU B 325 ? 0.3771 0.3377 0.3649 -0.0537 -0.0255 0.0169  305 GLU B OE2   
4814 N  N     . ARG B 326 ? 0.2523 0.2488 0.2591 -0.0525 -0.0143 0.0187  306 ARG B N     
4815 C  CA    . ARG B 326 ? 0.2656 0.2698 0.2735 -0.0595 -0.0141 0.0200  306 ARG B CA    
4816 C  C     . ARG B 326 ? 0.2733 0.2941 0.2897 -0.0589 -0.0117 0.0179  306 ARG B C     
4817 O  O     . ARG B 326 ? 0.2392 0.2707 0.2595 -0.0634 -0.0121 0.0172  306 ARG B O     
4818 C  CB    . ARG B 326 ? 0.2725 0.2693 0.2745 -0.0629 -0.0140 0.0227  306 ARG B CB    
4819 C  CG    . ARG B 326 ? 0.3904 0.3918 0.3907 -0.0719 -0.0148 0.0249  306 ARG B CG    
4820 C  CD    . ARG B 326 ? 0.5007 0.4976 0.4979 -0.0766 -0.0184 0.0257  306 ARG B CD    
4821 N  NE    . ARG B 326 ? 0.6473 0.6455 0.6407 -0.0862 -0.0197 0.0286  306 ARG B NE    
4822 C  CZ    . ARG B 326 ? 0.6818 0.6659 0.6666 -0.0904 -0.0232 0.0316  306 ARG B CZ    
4823 N  NH1   . ARG B 326 ? 0.6869 0.6553 0.6668 -0.0855 -0.0255 0.0314  306 ARG B NH1   
4824 N  NH2   . ARG B 326 ? 0.7885 0.7744 0.7695 -0.1000 -0.0246 0.0346  306 ARG B NH2   
4825 N  N     . ILE B 327 ? 0.2467 0.2702 0.2663 -0.0533 -0.0094 0.0166  307 ILE B N     
4826 C  CA    . ILE B 327 ? 0.2786 0.3174 0.3064 -0.0517 -0.0074 0.0139  307 ILE B CA    
4827 C  C     . ILE B 327 ? 0.2320 0.2787 0.2662 -0.0497 -0.0093 0.0111  307 ILE B C     
4828 O  O     . ILE B 327 ? 0.2677 0.3291 0.3091 -0.0509 -0.0086 0.0086  307 ILE B O     
4829 C  CB    . ILE B 327 ? 0.2490 0.2863 0.2779 -0.0456 -0.0053 0.0131  307 ILE B CB    
4830 C  CG1   . ILE B 327 ? 0.2428 0.2765 0.2671 -0.0486 -0.0033 0.0154  307 ILE B CG1   
4831 C  CG2   . ILE B 327 ? 0.2363 0.2876 0.2742 -0.0419 -0.0043 0.0093  307 ILE B CG2   
4832 C  CD1   . ILE B 327 ? 0.2164 0.2455 0.2401 -0.0428 -0.0017 0.0152  307 ILE B CD1   
4833 N  N     . THR B 328 ? 0.2399 0.2776 0.2716 -0.0466 -0.0118 0.0113  308 THR B N     
4834 C  CA    . THR B 328 ? 0.2429 0.2864 0.2799 -0.0448 -0.0144 0.0090  308 THR B CA    
4835 C  C     . THR B 328 ? 0.2441 0.2876 0.2793 -0.0505 -0.0167 0.0099  308 THR B C     
4836 O  O     . THR B 328 ? 0.2521 0.2980 0.2902 -0.0493 -0.0195 0.0084  308 THR B O     
4837 C  CB    . THR B 328 ? 0.2932 0.3277 0.3282 -0.0386 -0.0162 0.0087  308 THR B CB    
4838 O  OG1   . THR B 328 ? 0.2590 0.2798 0.2855 -0.0398 -0.0170 0.0110  308 THR B OG1   
4839 C  CG2   . THR B 328 ? 0.2805 0.3147 0.3170 -0.0333 -0.0144 0.0080  308 THR B CG2   
4840 N  N     . GLY B 329 ? 0.2598 0.3001 0.2900 -0.0569 -0.0161 0.0123  309 GLY B N     
4841 C  CA    . GLY B 329 ? 0.2633 0.3029 0.2913 -0.0631 -0.0186 0.0134  309 GLY B CA    
4842 C  C     . GLY B 329 ? 0.3521 0.3804 0.3756 -0.0612 -0.0218 0.0137  309 GLY B C     
4843 O  O     . GLY B 329 ? 0.3471 0.3785 0.3719 -0.0641 -0.0244 0.0132  309 GLY B O     
4844 N  N     . GLY B 330 ? 0.2707 0.2868 0.2890 -0.0565 -0.0217 0.0142  310 GLY B N     
4845 C  CA    . GLY B 330 ? 0.2741 0.2798 0.2874 -0.0547 -0.0243 0.0142  310 GLY B CA    
4846 C  C     . GLY B 330 ? 0.2608 0.2699 0.2779 -0.0501 -0.0259 0.0123  310 GLY B C     
4847 O  O     . GLY B 330 ? 0.3120 0.3129 0.3245 -0.0489 -0.0280 0.0122  310 GLY B O     
4848 N  N     . LYS B 331 ? 0.2598 0.2803 0.2849 -0.0473 -0.0252 0.0106  311 LYS B N     
4849 C  CA    . LYS B 331 ? 0.2537 0.2761 0.2821 -0.0428 -0.0278 0.0089  311 LYS B CA    
4850 C  C     . LYS B 331 ? 0.3043 0.3167 0.3277 -0.0380 -0.0273 0.0095  311 LYS B C     
4851 O  O     . LYS B 331 ? 0.3127 0.3205 0.3338 -0.0359 -0.0300 0.0093  311 LYS B O     
4852 C  CB    . LYS B 331 ? 0.2905 0.3274 0.3291 -0.0406 -0.0279 0.0063  311 LYS B CB    
4853 C  CG    . LYS B 331 ? 0.3494 0.3982 0.3936 -0.0454 -0.0289 0.0051  311 LYS B CG    
4854 C  CD    . LYS B 331 ? 0.4184 0.4816 0.4734 -0.0421 -0.0305 0.0014  311 LYS B CD    
4855 C  CE    . LYS B 331 ? 0.4494 0.5269 0.5107 -0.0475 -0.0307 -0.0002 311 LYS B CE    
4856 N  NZ    . LYS B 331 ? 0.6212 0.6937 0.6783 -0.0523 -0.0336 0.0014  311 LYS B NZ    
4857 N  N     . PHE B 332 ? 0.2489 0.2581 0.2703 -0.0366 -0.0240 0.0103  312 PHE B N     
4858 C  CA    . PHE B 332 ? 0.2402 0.2391 0.2554 -0.0336 -0.0229 0.0111  312 PHE B CA    
4859 C  C     . PHE B 332 ? 0.2671 0.2575 0.2756 -0.0364 -0.0216 0.0123  312 PHE B C     
4860 O  O     . PHE B 332 ? 0.2570 0.2495 0.2662 -0.0402 -0.0208 0.0130  312 PHE B O     
4861 C  CB    . PHE B 332 ? 0.2400 0.2413 0.2580 -0.0295 -0.0206 0.0108  312 PHE B CB    
4862 C  CG    . PHE B 332 ? 0.2482 0.2545 0.2713 -0.0256 -0.0229 0.0095  312 PHE B CG    
4863 C  CD1   . PHE B 332 ? 0.2799 0.2870 0.3040 -0.0256 -0.0269 0.0088  312 PHE B CD1   
4864 C  CD2   . PHE B 332 ? 0.2780 0.2876 0.3047 -0.0220 -0.0215 0.0088  312 PHE B CD2   
4865 C  CE1   . PHE B 332 ? 0.2962 0.3066 0.3247 -0.0218 -0.0300 0.0076  312 PHE B CE1   
4866 C  CE2   . PHE B 332 ? 0.3110 0.3240 0.3422 -0.0182 -0.0245 0.0074  312 PHE B CE2   
4867 C  CZ    . PHE B 332 ? 0.2491 0.2621 0.2811 -0.0180 -0.0289 0.0068  312 PHE B CZ    
4868 N  N     . LYS B 333 ? 0.2671 0.2480 0.2692 -0.0349 -0.0217 0.0123  313 LYS B N     
4869 C  CA    . LYS B 333 ? 0.2681 0.2401 0.2639 -0.0369 -0.0216 0.0125  313 LYS B CA    
4870 C  C     . LYS B 333 ? 0.2743 0.2400 0.2663 -0.0335 -0.0194 0.0121  313 LYS B C     
4871 O  O     . LYS B 333 ? 0.2863 0.2522 0.2779 -0.0303 -0.0186 0.0116  313 LYS B O     
4872 C  CB    . LYS B 333 ? 0.2977 0.2645 0.2889 -0.0388 -0.0245 0.0118  313 LYS B CB    
4873 C  CG    . LYS B 333 ? 0.3710 0.3424 0.3648 -0.0433 -0.0271 0.0122  313 LYS B CG    
4874 C  CD    . LYS B 333 ? 0.5413 0.5125 0.5351 -0.0476 -0.0268 0.0135  313 LYS B CD    
4875 C  CE    . LYS B 333 ? 0.6264 0.5977 0.6192 -0.0529 -0.0299 0.0138  313 LYS B CE    
4876 N  NZ    . LYS B 333 ? 0.6448 0.6234 0.6418 -0.0526 -0.0318 0.0129  313 LYS B NZ    
4877 N  N     . ALA B 334 ? 0.2636 0.2238 0.2528 -0.0344 -0.0187 0.0124  314 ALA B N     
4878 C  CA    . ALA B 334 ? 0.2545 0.2077 0.2395 -0.0313 -0.0174 0.0111  314 ALA B CA    
4879 C  C     . ALA B 334 ? 0.2960 0.2426 0.2755 -0.0314 -0.0192 0.0091  314 ALA B C     
4880 O  O     . ALA B 334 ? 0.3146 0.2576 0.2918 -0.0346 -0.0218 0.0091  314 ALA B O     
4881 C  CB    . ALA B 334 ? 0.2669 0.2161 0.2512 -0.0320 -0.0169 0.0119  314 ALA B CB    
4882 N  N     . VAL B 335 ? 0.2559 0.2013 0.2328 -0.0284 -0.0180 0.0074  315 VAL B N     
4883 C  CA    . VAL B 335 ? 0.2818 0.2228 0.2532 -0.0286 -0.0193 0.0051  315 VAL B CA    
4884 C  C     . VAL B 335 ? 0.2952 0.2308 0.2630 -0.0259 -0.0182 0.0021  315 VAL B C     
4885 O  O     . VAL B 335 ? 0.3035 0.2412 0.2725 -0.0230 -0.0156 0.0017  315 VAL B O     
4886 C  CB    . VAL B 335 ? 0.2905 0.2355 0.2611 -0.0282 -0.0192 0.0053  315 VAL B CB    
4887 C  CG1   . VAL B 335 ? 0.2909 0.2320 0.2551 -0.0290 -0.0205 0.0028  315 VAL B CG1   
4888 C  CG2   . VAL B 335 ? 0.2798 0.2305 0.2551 -0.0302 -0.0211 0.0076  315 VAL B CG2   
4889 N  N     . PRO B 336 ? 0.2715 0.2004 0.2350 -0.0265 -0.0203 -0.0003 316 PRO B N     
4890 C  CA    . PRO B 336 ? 0.2959 0.2197 0.2568 -0.0232 -0.0198 -0.0040 316 PRO B CA    
4891 C  C     . PRO B 336 ? 0.2961 0.2240 0.2553 -0.0204 -0.0168 -0.0068 316 PRO B C     
4892 O  O     . PRO B 336 ? 0.2912 0.2224 0.2481 -0.0218 -0.0164 -0.0069 316 PRO B O     
4893 C  CB    . PRO B 336 ? 0.3381 0.2544 0.2946 -0.0247 -0.0234 -0.0065 316 PRO B CB    
4894 C  CG    . PRO B 336 ? 0.3699 0.2863 0.3276 -0.0294 -0.0258 -0.0028 316 PRO B CG    
4895 C  CD    . PRO B 336 ? 0.2890 0.2145 0.2505 -0.0301 -0.0237 0.0000  316 PRO B CD    
4896 N  N     . HIS B 337 ? 0.2822 0.2101 0.2426 -0.0169 -0.0150 -0.0089 317 HIS B N     
4897 C  CA    . HIS B 337 ? 0.2777 0.2109 0.2370 -0.0147 -0.0118 -0.0115 317 HIS B CA    
4898 C  C     . HIS B 337 ? 0.2784 0.2099 0.2384 -0.0105 -0.0110 -0.0156 317 HIS B C     
4899 O  O     . HIS B 337 ? 0.2977 0.2233 0.2593 -0.0092 -0.0132 -0.0157 317 HIS B O     
4900 C  CB    . HIS B 337 ? 0.2834 0.2232 0.2456 -0.0154 -0.0094 -0.0076 317 HIS B CB    
4901 C  CG    . HIS B 337 ? 0.3039 0.2439 0.2712 -0.0140 -0.0088 -0.0050 317 HIS B CG    
4902 N  ND1   . HIS B 337 ? 0.2559 0.1946 0.2260 -0.0160 -0.0105 -0.0016 317 HIS B ND1   
4903 C  CD2   . HIS B 337 ? 0.2824 0.2245 0.2522 -0.0113 -0.0066 -0.0055 317 HIS B CD2   
4904 C  CE1   . HIS B 337 ? 0.2506 0.1903 0.2244 -0.0146 -0.0093 0.0000  317 HIS B CE1   
4905 N  NE2   . HIS B 337 ? 0.2547 0.1959 0.2284 -0.0116 -0.0072 -0.0022 317 HIS B NE2   
4906 N  N     . PHE B 338 ? 0.2729 0.2100 0.2318 -0.0088 -0.0081 -0.0189 318 PHE B N     
4907 C  CA    . PHE B 338 ? 0.3026 0.2406 0.2635 -0.0044 -0.0069 -0.0232 318 PHE B CA    
4908 C  C     . PHE B 338 ? 0.3185 0.2659 0.2792 -0.0041 -0.0027 -0.0245 318 PHE B C     
4909 O  O     . PHE B 338 ? 0.2780 0.2296 0.2355 -0.0074 -0.0014 -0.0231 318 PHE B O     
4910 C  CB    . PHE B 338 ? 0.3421 0.2749 0.3006 -0.0017 -0.0093 -0.0295 318 PHE B CB    
4911 C  CG    . PHE B 338 ? 0.3159 0.2521 0.2694 -0.0029 -0.0084 -0.0337 318 PHE B CG    
4912 C  CD1   . PHE B 338 ? 0.3601 0.3048 0.3127 -0.0014 -0.0049 -0.0386 318 PHE B CD1   
4913 C  CD2   . PHE B 338 ? 0.3665 0.2979 0.3160 -0.0060 -0.0110 -0.0329 318 PHE B CD2   
4914 C  CE1   . PHE B 338 ? 0.3812 0.3295 0.3284 -0.0031 -0.0039 -0.0425 318 PHE B CE1   
4915 C  CE2   . PHE B 338 ? 0.4125 0.3467 0.3567 -0.0074 -0.0103 -0.0367 318 PHE B CE2   
4916 C  CZ    . PHE B 338 ? 0.3901 0.3329 0.3330 -0.0061 -0.0067 -0.0415 318 PHE B CZ    
4917 N  N     . VAL B 339 ? 0.3197 0.2702 0.2838 -0.0005 -0.0011 -0.0271 319 VAL B N     
4918 C  CA    . VAL B 339 ? 0.2935 0.2535 0.2578 -0.0006 0.0029  -0.0285 319 VAL B CA    
4919 C  C     . VAL B 339 ? 0.3327 0.2966 0.2971 0.0031  0.0039  -0.0364 319 VAL B C     
4920 O  O     . VAL B 339 ? 0.3446 0.3042 0.3123 0.0076  0.0018  -0.0397 319 VAL B O     
4921 C  CB    . VAL B 339 ? 0.2948 0.2573 0.2637 0.0002  0.0044  -0.0246 319 VAL B CB    
4922 C  CG1   . VAL B 339 ? 0.3053 0.2775 0.2744 0.0002  0.0082  -0.0267 319 VAL B CG1   
4923 C  CG2   . VAL B 339 ? 0.2805 0.2409 0.2496 -0.0033 0.0036  -0.0177 319 VAL B CG2   
4924 N  N     . ARG B 340 ? 0.2964 0.2686 0.2572 0.0012  0.0068  -0.0396 320 ARG B N     
4925 C  CA    . ARG B 340 ? 0.2923 0.2714 0.2533 0.0043  0.0086  -0.0479 320 ARG B CA    
4926 C  C     . ARG B 340 ? 0.3562 0.3464 0.3198 0.0042  0.0127  -0.0488 320 ARG B C     
4927 O  O     . ARG B 340 ? 0.3175 0.3121 0.2786 -0.0005 0.0150  -0.0440 320 ARG B O     
4928 C  CB    . ARG B 340 ? 0.3888 0.3712 0.3432 0.0014  0.0095  -0.0517 320 ARG B CB    
4929 C  CG    . ARG B 340 ? 0.6115 0.5857 0.5641 0.0036  0.0057  -0.0557 320 ARG B CG    
4930 C  CD    . ARG B 340 ? 0.5598 0.5386 0.5055 0.0001  0.0070  -0.0592 320 ARG B CD    
4931 N  NE    . ARG B 340 ? 0.5531 0.5446 0.4983 0.0009  0.0111  -0.0663 320 ARG B NE    
4932 C  CZ    . ARG B 340 ? 0.7338 0.7285 0.6788 0.0046  0.0110  -0.0756 320 ARG B CZ    
4933 N  NH1   . ARG B 340 ? 0.7630 0.7476 0.7078 0.0081  0.0066  -0.0788 320 ARG B NH1   
4934 N  NH2   . ARG B 340 ? 0.6578 0.6663 0.6028 0.0048  0.0152  -0.0821 320 ARG B NH2   
4935 N  N     . GLY B 341 ? 0.3666 0.3610 0.3349 0.0094  0.0133  -0.0552 321 GLY B N     
4936 C  CA    . GLY B 341 ? 0.4086 0.4154 0.3796 0.0095  0.0173  -0.0576 321 GLY B CA    
4937 C  C     . GLY B 341 ? 0.3953 0.4140 0.3623 0.0072  0.0208  -0.0639 321 GLY B C     
4938 O  O     . GLY B 341 ? 0.3976 0.4147 0.3592 0.0053  0.0202  -0.0660 321 GLY B O     
4939 N  N     . ALA B 342 ? 0.3776 0.4090 0.3469 0.0066  0.0247  -0.0666 322 ALA B N     
4940 C  CA    . ALA B 342 ? 0.4242 0.4695 0.3902 0.0041  0.0286  -0.0733 322 ALA B CA    
4941 C  C     . ALA B 342 ? 0.5096 0.5594 0.4804 0.0113  0.0280  -0.0843 322 ALA B C     
4942 O  O     . ALA B 342 ? 0.5245 0.5723 0.5029 0.0179  0.0261  -0.0871 322 ALA B O     
4943 C  CB    . ALA B 342 ? 0.4679 0.5259 0.4343 -0.0001 0.0329  -0.0716 322 ALA B CB    
4944 N  N     . ARG B 343 ? 0.4948 0.5508 0.4611 0.0101  0.0294  -0.0909 323 ARG B N     
4945 C  CA    . ARG B 343 ? 0.5670 0.6282 0.5378 0.0172  0.0288  -0.1026 323 ARG B CA    
4946 C  C     . ARG B 343 ? 0.6532 0.7309 0.6307 0.0197  0.0325  -0.1090 323 ARG B C     
4947 O  O     . ARG B 343 ? 0.5298 0.6196 0.5051 0.0135  0.0372  -0.1065 323 ARG B O     
4948 C  CB    . ARG B 343 ? 0.5199 0.5849 0.4838 0.0149  0.0298  -0.1083 323 ARG B CB    
4949 C  CG    . ARG B 343 ? 0.6241 0.6719 0.5835 0.0151  0.0248  -0.1048 323 ARG B CG    
4950 C  CD    . ARG B 343 ? 0.5661 0.6173 0.5169 0.0105  0.0262  -0.1079 323 ARG B CD    
4951 N  NE    . ARG B 343 ? 0.5223 0.5787 0.4656 0.0009  0.0295  -0.1005 323 ARG B NE    
4952 C  CZ    . ARG B 343 ? 0.6081 0.6687 0.5425 -0.0051 0.0312  -0.1015 323 ARG B CZ    
4953 N  NH1   . ARG B 343 ? 0.6630 0.7243 0.5949 -0.0027 0.0303  -0.1097 323 ARG B NH1   
4954 N  NH2   . ARG B 343 ? 0.5428 0.6066 0.4703 -0.0139 0.0334  -0.0940 323 ARG B NH2   
4955 N  N     . ALA B 344 ? 0.7311 0.8091 0.7166 0.0287  0.0299  -0.1173 324 ALA B N     
4956 C  CA    . ALA B 344 ? 0.7933 0.8862 0.7869 0.0324  0.0325  -0.1236 324 ALA B CA    
4957 C  C     . ALA B 344 ? 0.7902 0.9047 0.7812 0.0275  0.0390  -0.1302 324 ALA B C     
4958 O  O     . ALA B 344 ? 0.7284 0.8571 0.7228 0.0253  0.0430  -0.1309 324 ALA B O     
4959 C  CB    . ALA B 344 ? 0.7810 0.8699 0.7830 0.0434  0.0277  -0.1328 324 ALA B CB    
4960 N  N     . GLU B 345 ? 0.6172 0.7348 0.6019 0.0254  0.0401  -0.1353 325 GLU B N     
4961 C  CA    . GLU B 345 ? 0.6823 0.8204 0.6627 0.0192  0.0464  -0.1408 325 GLU B CA    
4962 C  C     . GLU B 345 ? 0.7739 0.9178 0.7488 0.0088  0.0505  -0.1310 325 GLU B C     
4963 O  O     . GLU B 345 ? 0.8637 1.0268 0.8384 0.0041  0.0558  -0.1348 325 GLU B O     
4964 C  CB    . GLU B 345 ? 0.7492 0.8857 0.7212 0.0168  0.0464  -0.1447 325 GLU B CB    
4965 C  CG    . GLU B 345 ? 0.9202 1.0758 0.8847 0.0080  0.0528  -0.1482 325 GLU B CG    
4966 C  CD    . GLU B 345 ? 1.1592 1.3115 1.1145 0.0052  0.0522  -0.1509 325 GLU B CD    
4967 O  OE1   . GLU B 345 ? 1.1610 1.2988 1.1175 0.0117  0.0471  -0.1532 325 GLU B OE1   
4968 O  OE2   . GLU B 345 ? 1.1517 1.3155 1.0981 -0.0040 0.0567  -0.1506 325 GLU B OE2   
4969 N  N     . MET B 346 ? 0.6702 0.7980 0.6408 0.0049  0.0479  -0.1187 326 MET B N     
4970 C  CA    . MET B 346 ? 0.7923 0.9227 0.7579 -0.0042 0.0504  -0.1090 326 MET B CA    
4971 C  C     . MET B 346 ? 0.7342 0.8637 0.7078 -0.0013 0.0499  -0.1050 326 MET B C     
4972 O  O     . MET B 346 ? 0.5407 0.6791 0.5128 -0.0077 0.0531  -0.1009 326 MET B O     
4973 C  CB    . MET B 346 ? 0.7172 0.8313 0.6741 -0.0097 0.0476  -0.0983 326 MET B CB    
4974 C  CG    . MET B 346 ? 0.7519 0.8695 0.6980 -0.0168 0.0491  -0.0991 326 MET B CG    
4975 S  SD    . MET B 346 ? 0.9168 1.0283 0.8625 -0.0102 0.0463  -0.1080 326 MET B SD    
4976 C  CE    . MET B 346 ? 0.6043 0.7105 0.5359 -0.0202 0.0460  -0.1017 326 MET B CE    
4977 N  N     . SER B 347 ? 0.6605 0.7789 0.6420 0.0076  0.0455  -0.1059 327 SER B N     
4978 C  CA    . SER B 347 ? 0.5455 0.6632 0.5348 0.0110  0.0447  -0.1030 327 SER B CA    
4979 C  C     . SER B 347 ? 0.6101 0.7478 0.6065 0.0133  0.0484  -0.1121 327 SER B C     
4980 O  O     . SER B 347 ? 0.5446 0.6885 0.5443 0.0112  0.0502  -0.1088 327 SER B O     
4981 C  CB    . SER B 347 ? 0.6018 0.7025 0.5968 0.0195  0.0387  -0.1021 327 SER B CB    
4982 O  OG    . SER B 347 ? 0.5890 0.6898 0.5919 0.0236  0.0376  -0.1008 327 SER B OG    
4983 N  N     . ALA B 348 ? 0.7276 0.8758 0.7269 0.0179  0.0494  -0.1240 328 ALA B N     
4984 C  CA    . ALA B 348 ? 0.6831 0.8537 0.6889 0.0196  0.0535  -0.1344 328 ALA B CA    
4985 C  C     . ALA B 348 ? 0.6681 0.8407 0.6847 0.0257  0.0520  -0.1352 328 ALA B C     
4986 O  O     . ALA B 348 ? 0.7396 0.9303 0.7605 0.0237  0.0560  -0.1388 328 ALA B O     
4987 C  CB    . ALA B 348 ? 0.6825 0.8700 0.6810 0.0082  0.0600  -0.1327 328 ALA B CB    
4988 N  N     . GLY B 349 ? 0.6241 0.7784 0.6449 0.0327  0.0460  -0.1317 329 GLY B N     
4989 C  CA    . GLY B 349 ? 0.4998 0.6542 0.5303 0.0386  0.0437  -0.1319 329 GLY B CA    
4990 C  C     . GLY B 349 ? 0.5755 0.7328 0.6050 0.0319  0.0463  -0.1228 329 GLY B C     
4991 O  O     . GLY B 349 ? 0.5736 0.7332 0.6110 0.0360  0.0450  -0.1231 329 GLY B O     
4992 N  N     . ARG B 350 ? 0.5183 0.6748 0.5382 0.0218  0.0494  -0.1145 330 ARG B N     
4993 C  CA    . ARG B 350 ? 0.3924 0.5511 0.4105 0.0149  0.0515  -0.1057 330 ARG B CA    
4994 C  C     . ARG B 350 ? 0.2808 0.4207 0.2915 0.0103  0.0491  -0.0932 330 ARG B C     
4995 O  O     . ARG B 350 ? 0.2695 0.4057 0.2807 0.0078  0.0487  -0.0859 330 ARG B O     
4996 C  CB    . ARG B 350 ? 0.4230 0.6015 0.4364 0.0056  0.0577  -0.1076 330 ARG B CB    
4997 C  CG    . ARG B 350 ? 0.5162 0.6953 0.5190 -0.0011 0.0597  -0.1071 330 ARG B CG    
4998 C  CD    . ARG B 350 ? 0.6859 0.8842 0.6831 -0.0115 0.0655  -0.1080 330 ARG B CD    
4999 N  NE    . ARG B 350 ? 0.7197 0.9173 0.7056 -0.0187 0.0670  -0.1066 330 ARG B NE    
5000 C  CZ    . ARG B 350 ? 0.8773 1.0879 0.8615 -0.0190 0.0699  -0.1162 330 ARG B CZ    
5001 N  NH1   . ARG B 350 ? 0.8491 1.0753 0.8427 -0.0121 0.0717  -0.1284 330 ARG B NH1   
5002 N  NH2   . ARG B 350 ? 1.0254 1.2335 0.9984 -0.0260 0.0707  -0.1137 330 ARG B NH2   
5003 N  N     . ILE B 351 ? 0.3009 0.4294 0.3049 0.0092  0.0473  -0.0909 331 ILE B N     
5004 C  CA    . ILE B 351 ? 0.2910 0.4046 0.2877 0.0040  0.0454  -0.0797 331 ILE B CA    
5005 C  C     . ILE B 351 ? 0.2686 0.3641 0.2687 0.0105  0.0401  -0.0762 331 ILE B C     
5006 O  O     . ILE B 351 ? 0.3581 0.4471 0.3597 0.0162  0.0373  -0.0808 331 ILE B O     
5007 C  CB    . ILE B 351 ? 0.2945 0.4069 0.2813 -0.0022 0.0465  -0.0785 331 ILE B CB    
5008 C  CG1   . ILE B 351 ? 0.3885 0.5196 0.3710 -0.0093 0.0517  -0.0825 331 ILE B CG1   
5009 C  CG2   . ILE B 351 ? 0.3418 0.4396 0.3220 -0.0073 0.0441  -0.0671 331 ILE B CG2   
5010 C  CD1   . ILE B 351 ? 0.3988 0.5361 0.3798 -0.0162 0.0539  -0.0766 331 ILE B CD1   
5011 N  N     . ALA B 352 ? 0.2446 0.3320 0.2455 0.0094  0.0386  -0.0681 332 ALA B N     
5012 C  CA    . ALA B 352 ? 0.2529 0.3237 0.2557 0.0137  0.0340  -0.0633 332 ALA B CA    
5013 C  C     . ALA B 352 ? 0.2628 0.3228 0.2582 0.0081  0.0330  -0.0545 332 ALA B C     
5014 O  O     . ALA B 352 ? 0.2409 0.3054 0.2304 0.0010  0.0353  -0.0509 332 ALA B O     
5015 C  CB    . ALA B 352 ? 0.2404 0.3100 0.2497 0.0167  0.0328  -0.0607 332 ALA B CB    
5016 N  N     . ARG B 353 ? 0.2398 0.2856 0.2356 0.0111  0.0290  -0.0511 333 ARG B N     
5017 C  CA    . ARG B 353 ? 0.2421 0.2776 0.2322 0.0068  0.0275  -0.0435 333 ARG B CA    
5018 C  C     . ARG B 353 ? 0.2387 0.2639 0.2320 0.0089  0.0247  -0.0376 333 ARG B C     
5019 O  O     . ARG B 353 ? 0.2592 0.2784 0.2566 0.0142  0.0219  -0.0395 333 ARG B O     
5020 C  CB    . ARG B 353 ? 0.2608 0.2901 0.2469 0.0071  0.0256  -0.0455 333 ARG B CB    
5021 C  CG    . ARG B 353 ? 0.2892 0.3077 0.2706 0.0035  0.0234  -0.0378 333 ARG B CG    
5022 C  CD    . ARG B 353 ? 0.3107 0.3234 0.2880 0.0035  0.0215  -0.0399 333 ARG B CD    
5023 N  NE    . ARG B 353 ? 0.3189 0.3274 0.2996 0.0095  0.0191  -0.0457 333 ARG B NE    
5024 C  CZ    . ARG B 353 ? 0.3061 0.3029 0.2871 0.0115  0.0152  -0.0438 333 ARG B CZ    
5025 N  NH1   . ARG B 353 ? 0.3303 0.3197 0.3090 0.0083  0.0136  -0.0368 333 ARG B NH1   
5026 N  NH2   . ARG B 353 ? 0.3651 0.3576 0.3487 0.0168  0.0124  -0.0493 333 ARG B NH2   
5027 N  N     . ASN B 354 ? 0.2291 0.2521 0.2200 0.0046  0.0250  -0.0306 334 ASN B N     
5028 C  CA    . ASN B 354 ? 0.2246 0.2393 0.2181 0.0060  0.0228  -0.0252 334 ASN B CA    
5029 C  C     . ASN B 354 ? 0.2456 0.2520 0.2351 0.0029  0.0209  -0.0195 334 ASN B C     
5030 O  O     . ASN B 354 ? 0.2286 0.2367 0.2130 -0.0018 0.0217  -0.0173 334 ASN B O     
5031 C  CB    . ASN B 354 ? 0.2196 0.2396 0.2152 0.0045  0.0244  -0.0226 334 ASN B CB    
5032 C  CG    . ASN B 354 ? 0.2441 0.2731 0.2447 0.0078  0.0260  -0.0283 334 ASN B CG    
5033 O  OD1   . ASN B 354 ? 0.2295 0.2562 0.2346 0.0133  0.0242  -0.0321 334 ASN B OD1   
5034 N  ND2   . ASN B 354 ? 0.2478 0.2874 0.2478 0.0043  0.0290  -0.0291 334 ASN B ND2   
5035 N  N     . THR B 355 ? 0.2222 0.2196 0.2136 0.0053  0.0182  -0.0171 335 THR B N     
5036 C  CA    . THR B 355 ? 0.2490 0.2397 0.2375 0.0027  0.0164  -0.0124 335 THR B CA    
5037 C  C     . THR B 355 ? 0.2257 0.2113 0.2173 0.0036  0.0148  -0.0080 335 THR B C     
5038 O  O     . THR B 355 ? 0.2154 0.1999 0.2108 0.0067  0.0143  -0.0088 335 THR B O     
5039 C  CB    . THR B 355 ? 0.2354 0.2206 0.2220 0.0034  0.0143  -0.0144 335 THR B CB    
5040 O  OG1   . THR B 355 ? 0.2743 0.2537 0.2641 0.0073  0.0121  -0.0157 335 THR B OG1   
5041 C  CG2   . THR B 355 ? 0.3266 0.3170 0.3103 0.0032  0.0158  -0.0199 335 THR B CG2   
5042 N  N     . LEU B 356 ? 0.2602 0.2426 0.2501 0.0010  0.0138  -0.0036 336 LEU B N     
5043 C  CA    . LEU B 356 ? 0.2239 0.2024 0.2165 0.0015  0.0124  0.0001  336 LEU B CA    
5044 C  C     . LEU B 356 ? 0.2259 0.1997 0.2173 0.0001  0.0104  0.0021  336 LEU B C     
5045 O  O     . LEU B 356 ? 0.2600 0.2340 0.2483 -0.0023 0.0099  0.0027  336 LEU B O     
5046 C  CB    . LEU B 356 ? 0.2472 0.2283 0.2404 0.0001  0.0132  0.0033  336 LEU B CB    
5047 C  CG    . LEU B 356 ? 0.2493 0.2276 0.2452 0.0005  0.0120  0.0066  336 LEU B CG    
5048 C  CD1   . LEU B 356 ? 0.2707 0.2477 0.2698 0.0032  0.0120  0.0061  336 LEU B CD1   
5049 C  CD2   . LEU B 356 ? 0.2616 0.2418 0.2572 -0.0010 0.0121  0.0092  336 LEU B CD2   
5050 N  N     . ALA B 357 ? 0.2117 0.1814 0.2053 0.0012  0.0089  0.0031  337 ALA B N     
5051 C  CA    . ALA B 357 ? 0.2359 0.2025 0.2291 -0.0006 0.0071  0.0053  337 ALA B CA    
5052 C  C     . ALA B 357 ? 0.2275 0.1939 0.2239 -0.0006 0.0068  0.0080  337 ALA B C     
5053 O  O     . ALA B 357 ? 0.2302 0.1955 0.2281 0.0011  0.0070  0.0078  337 ALA B O     
5054 C  CB    . ALA B 357 ? 0.2621 0.2239 0.2537 -0.0005 0.0053  0.0034  337 ALA B CB    
5055 N  N     . VAL B 358 ? 0.2062 0.1738 0.2035 -0.0023 0.0061  0.0102  338 VAL B N     
5056 C  CA    . VAL B 358 ? 0.2050 0.1738 0.2052 -0.0025 0.0060  0.0122  338 VAL B CA    
5057 C  C     . VAL B 358 ? 0.2123 0.1801 0.2127 -0.0048 0.0044  0.0129  338 VAL B C     
5058 O  O     . VAL B 358 ? 0.2342 0.2041 0.2350 -0.0059 0.0036  0.0133  338 VAL B O     
5059 C  CB    . VAL B 358 ? 0.1988 0.1715 0.2010 -0.0022 0.0066  0.0135  338 VAL B CB    
5060 C  CG1   . VAL B 358 ? 0.2233 0.1983 0.2287 -0.0023 0.0067  0.0147  338 VAL B CG1   
5061 C  CG2   . VAL B 358 ? 0.2127 0.1864 0.2143 -0.0008 0.0079  0.0130  338 VAL B CG2   
5062 N  N     . PHE B 359 ? 0.2079 0.1724 0.2077 -0.0056 0.0035  0.0132  339 PHE B N     
5063 C  CA    . PHE B 359 ? 0.2108 0.1743 0.2101 -0.0087 0.0019  0.0141  339 PHE B CA    
5064 C  C     . PHE B 359 ? 0.2075 0.1762 0.2098 -0.0104 0.0025  0.0158  339 PHE B C     
5065 O  O     . PHE B 359 ? 0.2253 0.1932 0.2274 -0.0116 0.0025  0.0170  339 PHE B O     
5066 C  CB    . PHE B 359 ? 0.2368 0.1934 0.2332 -0.0095 0.0000  0.0139  339 PHE B CB    
5067 C  CG    . PHE B 359 ? 0.2485 0.2007 0.2425 -0.0071 -0.0006 0.0111  339 PHE B CG    
5068 C  CD1   . PHE B 359 ? 0.2236 0.1748 0.2157 -0.0078 -0.0014 0.0097  339 PHE B CD1   
5069 C  CD2   . PHE B 359 ? 0.2669 0.2163 0.2607 -0.0042 -0.0005 0.0096  339 PHE B CD2   
5070 C  CE1   . PHE B 359 ? 0.2402 0.1885 0.2300 -0.0056 -0.0017 0.0065  339 PHE B CE1   
5071 C  CE2   . PHE B 359 ? 0.2472 0.1941 0.2394 -0.0017 -0.0010 0.0062  339 PHE B CE2   
5072 C  CZ    . PHE B 359 ? 0.2712 0.2178 0.2613 -0.0024 -0.0014 0.0045  339 PHE B CZ    
5073 N  N     . THR B 360 ? 0.2107 0.1851 0.2158 -0.0106 0.0027  0.0157  340 THR B N     
5074 C  CA    . THR B 360 ? 0.2015 0.1823 0.2100 -0.0121 0.0032  0.0164  340 THR B CA    
5075 C  C     . THR B 360 ? 0.2153 0.1967 0.2232 -0.0162 0.0020  0.0171  340 THR B C     
5076 O  O     . THR B 360 ? 0.2522 0.2314 0.2587 -0.0174 0.0005  0.0167  340 THR B O     
5077 C  CB    . THR B 360 ? 0.2125 0.1993 0.2249 -0.0104 0.0031  0.0154  340 THR B CB    
5078 O  OG1   . THR B 360 ? 0.2134 0.2011 0.2262 -0.0114 0.0013  0.0148  340 THR B OG1   
5079 C  CG2   . THR B 360 ? 0.2197 0.2047 0.2316 -0.0071 0.0036  0.0151  340 THR B CG2   
5080 N  N     . GLN B 361 ? 0.2057 0.1901 0.2142 -0.0189 0.0027  0.0181  341 GLN B N     
5081 C  CA    . GLN B 361 ? 0.2269 0.2113 0.2336 -0.0240 0.0015  0.0194  341 GLN B CA    
5082 C  C     . GLN B 361 ? 0.2515 0.2439 0.2603 -0.0269 0.0030  0.0200  341 GLN B C     
5083 O  O     . GLN B 361 ? 0.2528 0.2482 0.2633 -0.0246 0.0047  0.0196  341 GLN B O     
5084 C  CB    . GLN B 361 ? 0.2318 0.2054 0.2329 -0.0252 -0.0005 0.0207  341 GLN B CB    
5085 C  CG    . GLN B 361 ? 0.2415 0.2105 0.2410 -0.0229 -0.0001 0.0213  341 GLN B CG    
5086 C  CD    . GLN B 361 ? 0.2574 0.2156 0.2527 -0.0215 -0.0024 0.0210  341 GLN B CD    
5087 O  OE1   . GLN B 361 ? 0.2702 0.2241 0.2635 -0.0223 -0.0043 0.0203  341 GLN B OE1   
5088 N  NE2   . GLN B 361 ? 0.2608 0.2150 0.2551 -0.0190 -0.0025 0.0211  341 GLN B NE2   
5089 N  N     . PRO B 362 ? 0.2289 0.2251 0.2372 -0.0323 0.0024  0.0209  342 PRO B N     
5090 C  CA    . PRO B 362 ? 0.2225 0.2289 0.2331 -0.0357 0.0043  0.0209  342 PRO B CA    
5091 C  C     . PRO B 362 ? 0.2456 0.2477 0.2517 -0.0381 0.0045  0.0232  342 PRO B C     
5092 O  O     . PRO B 362 ? 0.2746 0.2655 0.2756 -0.0384 0.0025  0.0252  342 PRO B O     
5093 C  CB    . PRO B 362 ? 0.2414 0.2531 0.2521 -0.0417 0.0034  0.0212  342 PRO B CB    
5094 C  CG    . PRO B 362 ? 0.2390 0.2443 0.2489 -0.0402 0.0011  0.0209  342 PRO B CG    
5095 C  CD    . PRO B 362 ? 0.2354 0.2285 0.2415 -0.0360 0.0002  0.0216  342 PRO B CD    
5096 N  N     . ASN B 363 ? 0.2709 0.2826 0.2791 -0.0399 0.0068  0.0227  343 ASN B N     
5097 C  CA    . ASN B 363 ? 0.2611 0.2702 0.2642 -0.0444 0.0067  0.0254  343 ASN B CA    
5098 C  C     . ASN B 363 ? 0.2457 0.2510 0.2434 -0.0520 0.0043  0.0283  343 ASN B C     
5099 O  O     . ASN B 363 ? 0.2708 0.2803 0.2701 -0.0548 0.0038  0.0277  343 ASN B O     
5100 C  CB    . ASN B 363 ? 0.2749 0.2966 0.2810 -0.0456 0.0098  0.0238  343 ASN B CB    
5101 C  CG    . ASN B 363 ? 0.2777 0.3001 0.2872 -0.0387 0.0114  0.0218  343 ASN B CG    
5102 O  OD1   . ASN B 363 ? 0.2749 0.2873 0.2817 -0.0355 0.0103  0.0231  343 ASN B OD1   
5103 N  ND2   . ASN B 363 ? 0.3051 0.3393 0.3207 -0.0364 0.0135  0.0182  343 ASN B ND2   
5104 N  N     . LEU B 364 ? 0.2955 0.2919 0.2864 -0.0555 0.0022  0.0317  344 LEU B N     
5105 C  CA    . LEU B 364 ? 0.2877 0.2765 0.2721 -0.0625 -0.0014 0.0350  344 LEU B CA    
5106 C  C     . LEU B 364 ? 0.2731 0.2738 0.2577 -0.0708 -0.0001 0.0355  344 LEU B C     
5107 O  O     . LEU B 364 ? 0.2922 0.2897 0.2737 -0.0761 -0.0026 0.0372  344 LEU B O     
5108 C  CB    . LEU B 364 ? 0.2892 0.2661 0.2662 -0.0647 -0.0044 0.0385  344 LEU B CB    
5109 C  CG    . LEU B 364 ? 0.3164 0.2816 0.2934 -0.0568 -0.0062 0.0376  344 LEU B CG    
5110 C  CD1   . LEU B 364 ? 0.3773 0.3323 0.3481 -0.0583 -0.0093 0.0406  344 LEU B CD1   
5111 C  CD2   . LEU B 364 ? 0.3836 0.3396 0.3600 -0.0543 -0.0091 0.0367  344 LEU B CD2   
5112 N  N     . GLY B 365 ? 0.2980 0.3132 0.2864 -0.0719 0.0038  0.0337  345 GLY B N     
5113 C  CA    . GLY B 365 ? 0.2985 0.3279 0.2881 -0.0796 0.0056  0.0333  345 GLY B CA    
5114 C  C     . GLY B 365 ? 0.2978 0.3399 0.2959 -0.0772 0.0076  0.0290  345 GLY B C     
5115 O  O     . GLY B 365 ? 0.3374 0.3926 0.3373 -0.0835 0.0090  0.0282  345 GLY B O     
5116 N  N     . ASP B 366 ? 0.2786 0.3177 0.2819 -0.0685 0.0075  0.0263  346 ASP B N     
5117 C  CA    . ASP B 366 ? 0.2497 0.2993 0.2609 -0.0657 0.0084  0.0225  346 ASP B CA    
5118 C  C     . ASP B 366 ? 0.2801 0.3253 0.2891 -0.0700 0.0056  0.0241  346 ASP B C     
5119 O  O     . ASP B 366 ? 0.3011 0.3311 0.3040 -0.0703 0.0025  0.0271  346 ASP B O     
5120 C  CB    . ASP B 366 ? 0.2641 0.3104 0.2803 -0.0558 0.0086  0.0197  346 ASP B CB    
5121 C  CG    . ASP B 366 ? 0.3035 0.3557 0.3232 -0.0511 0.0112  0.0173  346 ASP B CG    
5122 O  OD1   . ASP B 366 ? 0.3964 0.4596 0.4171 -0.0548 0.0135  0.0163  346 ASP B OD1   
5123 O  OD2   . ASP B 366 ? 0.4168 0.4629 0.4381 -0.0440 0.0109  0.0163  346 ASP B OD2   
5124 N  N     . GLU B 367 ? 0.2575 0.3162 0.2720 -0.0727 0.0065  0.0217  347 GLU B N     
5125 C  CA    . GLU B 367 ? 0.2637 0.3196 0.2764 -0.0772 0.0038  0.0230  347 GLU B CA    
5126 C  C     . GLU B 367 ? 0.3271 0.3742 0.3418 -0.0701 0.0016  0.0218  347 GLU B C     
5127 O  O     . GLU B 367 ? 0.3265 0.3773 0.3472 -0.0627 0.0027  0.0185  347 GLU B O     
5128 C  CB    . GLU B 367 ? 0.3012 0.3760 0.3199 -0.0824 0.0054  0.0204  347 GLU B CB    
5129 C  CG    . GLU B 367 ? 0.3562 0.4403 0.3715 -0.0917 0.0074  0.0220  347 GLU B CG    
5130 C  CD    . GLU B 367 ? 0.5671 0.6705 0.5877 -0.0982 0.0089  0.0195  347 GLU B CD    
5131 O  OE1   . GLU B 367 ? 0.5207 0.6312 0.5489 -0.0946 0.0084  0.0160  347 GLU B OE1   
5132 O  OE2   . GLU B 367 ? 0.5405 0.6521 0.5574 -0.1075 0.0103  0.0211  347 GLU B OE2   
5133 N  N     . VAL B 368 ? 0.2998 0.3345 0.3086 -0.0728 -0.0017 0.0245  348 VAL B N     
5134 C  CA    . VAL B 368 ? 0.3343 0.3621 0.3443 -0.0678 -0.0038 0.0232  348 VAL B CA    
5135 C  C     . VAL B 368 ? 0.3169 0.3498 0.3283 -0.0728 -0.0056 0.0230  348 VAL B C     
5136 O  O     . VAL B 368 ? 0.3116 0.3462 0.3272 -0.0687 -0.0066 0.0207  348 VAL B O     
5137 C  CB    . VAL B 368 ? 0.3405 0.3497 0.3434 -0.0651 -0.0064 0.0254  348 VAL B CB    
5138 C  CG1   . VAL B 368 ? 0.3405 0.3456 0.3431 -0.0594 -0.0046 0.0252  348 VAL B CG1   
5139 C  CG2   . VAL B 368 ? 0.4170 0.4165 0.4118 -0.0726 -0.0095 0.0291  348 VAL B CG2   
5140 N  N     . ASP B 369 ? 0.3631 0.3981 0.3707 -0.0819 -0.0065 0.0255  349 ASP B N     
5141 C  CA    . ASP B 369 ? 0.4586 0.5014 0.4681 -0.0879 -0.0079 0.0252  349 ASP B CA    
5142 C  C     . ASP B 369 ? 0.3870 0.4497 0.4020 -0.0927 -0.0046 0.0235  349 ASP B C     
5143 O  O     . ASP B 369 ? 0.4160 0.4805 0.4263 -0.1001 -0.0038 0.0261  349 ASP B O     
5144 C  CB    . ASP B 369 ? 0.3843 0.4140 0.3846 -0.0953 -0.0119 0.0293  349 ASP B CB    
5145 C  CG    . ASP B 369 ? 0.5602 0.5965 0.5621 -0.1013 -0.0137 0.0291  349 ASP B CG    
5146 O  OD1   . ASP B 369 ? 0.5131 0.5677 0.5220 -0.1043 -0.0114 0.0268  349 ASP B OD1   
5147 O  OD2   . ASP B 369 ? 0.5055 0.5289 0.5019 -0.1029 -0.0177 0.0308  349 ASP B OD2   
5148 N  N     . MET B 370 ? 0.4152 0.4929 0.4402 -0.0885 -0.0029 0.0188  350 MET B N     
5149 C  CA    A MET B 370 ? 0.4124 0.5108 0.4440 -0.0916 0.0005  0.0158  350 MET B CA    
5150 C  CA    B MET B 370 ? 0.4128 0.5113 0.4446 -0.0915 0.0005  0.0157  350 MET B CA    
5151 C  C     . MET B 370 ? 0.4620 0.5723 0.4943 -0.1017 0.0001  0.0162  350 MET B C     
5152 O  O     . MET B 370 ? 0.6072 0.7351 0.6434 -0.1065 0.0032  0.0141  350 MET B O     
5153 C  CB    A MET B 370 ? 0.4874 0.5972 0.5299 -0.0826 0.0018  0.0100  350 MET B CB    
5154 C  CB    B MET B 370 ? 0.4869 0.5968 0.5296 -0.0824 0.0018  0.0099  350 MET B CB    
5155 C  CG    A MET B 370 ? 0.4812 0.5874 0.5244 -0.0751 0.0038  0.0089  350 MET B CG    
5156 C  CG    B MET B 370 ? 0.4818 0.5904 0.5261 -0.0752 0.0041  0.0083  350 MET B CG    
5157 S  SD    A MET B 370 ? 0.4627 0.5713 0.5151 -0.0635 0.0026  0.0039  350 MET B SD    
5158 S  SD    B MET B 370 ? 0.4770 0.5624 0.5149 -0.0675 0.0021  0.0112  350 MET B SD    
5159 C  CE    A MET B 370 ? 0.4156 0.5016 0.4606 -0.0600 -0.0010 0.0077  350 MET B CE    
5160 C  CE    B MET B 370 ? 0.4104 0.4965 0.4553 -0.0596 -0.0005 0.0076  350 MET B CE    
5161 N  N     . GLU B 371 ? 0.4504 0.5520 0.4788 -0.1052 -0.0034 0.0186  351 GLU B N     
5162 C  CA    . GLU B 371 ? 0.5525 0.6645 0.5806 -0.1159 -0.0041 0.0195  351 GLU B CA    
5163 C  C     . GLU B 371 ? 0.6841 0.7885 0.7012 -0.1263 -0.0047 0.0251  351 GLU B C     
5164 O  O     . GLU B 371 ? 0.6372 0.7559 0.6543 -0.1356 -0.0028 0.0254  351 GLU B O     
5165 C  CB    . GLU B 371 ? 0.7131 0.8192 0.7414 -0.1160 -0.0080 0.0198  351 GLU B CB    
5166 C  CG    . GLU B 371 ? 0.8814 0.9963 0.9084 -0.1277 -0.0093 0.0213  351 GLU B CG    
5167 C  CD    . GLU B 371 ? 1.1028 1.2031 1.1244 -0.1297 -0.0143 0.0240  351 GLU B CD    
5168 O  OE1   . GLU B 371 ? 1.0937 1.1775 1.1125 -0.1220 -0.0164 0.0243  351 GLU B OE1   
5169 O  OE2   . GLU B 371 ? 1.0951 1.2013 1.1153 -0.1392 -0.0159 0.0254  351 GLU B OE2   
5170 N  N     . GLN B 372 ? 0.5543 0.6365 0.5619 -0.1249 -0.0077 0.0293  352 GLN B N     
5171 C  CA    . GLN B 372 ? 0.5393 0.6105 0.5356 -0.1339 -0.0098 0.0348  352 GLN B CA    
5172 C  C     . GLN B 372 ? 0.6061 0.6762 0.5998 -0.1323 -0.0072 0.0357  352 GLN B C     
5173 O  O     . GLN B 372 ? 0.5270 0.5897 0.5114 -0.1403 -0.0088 0.0403  352 GLN B O     
5174 C  CB    . GLN B 372 ? 0.6062 0.6532 0.5938 -0.1330 -0.0153 0.0384  352 GLN B CB    
5175 C  CG    . GLN B 372 ? 0.7608 0.8076 0.7509 -0.1332 -0.0179 0.0371  352 GLN B CG    
5176 C  CD    . GLN B 372 ? 0.9281 0.9525 0.9085 -0.1351 -0.0238 0.0407  352 GLN B CD    
5177 O  OE1   . GLN B 372 ? 0.8690 0.8818 0.8397 -0.1421 -0.0269 0.0452  352 GLN B OE1   
5178 N  NE2   . GLN B 372 ? 0.9170 0.9349 0.8996 -0.1288 -0.0257 0.0385  352 GLN B NE2   
5179 N  N     . HIS B 373 ? 0.4400 0.5168 0.4413 -0.1225 -0.0037 0.0315  353 HIS B N     
5180 C  CA    . HIS B 373 ? 0.4534 0.5311 0.4534 -0.1204 -0.0009 0.0316  353 HIS B CA    
5181 C  C     . HIS B 373 ? 0.4798 0.5348 0.4702 -0.1187 -0.0042 0.0360  353 HIS B C     
5182 O  O     . HIS B 373 ? 0.4965 0.5484 0.4811 -0.1223 -0.0038 0.0387  353 HIS B O     
5183 C  CB    . HIS B 373 ? 0.5217 0.6159 0.5208 -0.1306 0.0020  0.0321  353 HIS B CB    
5184 C  CG    . HIS B 373 ? 0.5973 0.7158 0.6068 -0.1321 0.0053  0.0269  353 HIS B CG    
5185 N  ND1   . HIS B 373 ? 0.6074 0.7409 0.6276 -0.1238 0.0091  0.0207  353 HIS B ND1   
5186 C  CD2   . HIS B 373 ? 0.6376 0.7677 0.6488 -0.1404 0.0049  0.0266  353 HIS B CD2   
5187 C  CE1   . HIS B 373 ? 0.6113 0.7652 0.6399 -0.1267 0.0108  0.0164  353 HIS B CE1   
5188 N  NE2   . HIS B 373 ? 0.5918 0.7447 0.6153 -0.1368 0.0086  0.0200  353 HIS B NE2   
5189 N  N     . ILE B 374 ? 0.3806 0.4203 0.3695 -0.1128 -0.0074 0.0363  354 ILE B N     
5190 C  CA    . ILE B 374 ? 0.3271 0.3462 0.3086 -0.1092 -0.0106 0.0391  354 ILE B CA    
5191 C  C     . ILE B 374 ? 0.3431 0.3625 0.3295 -0.0986 -0.0076 0.0363  354 ILE B C     
5192 O  O     . ILE B 374 ? 0.3475 0.3729 0.3415 -0.0912 -0.0058 0.0324  354 ILE B O     
5193 C  CB    . ILE B 374 ? 0.4044 0.4080 0.3822 -0.1076 -0.0153 0.0400  354 ILE B CB    
5194 C  CG1   . ILE B 374 ? 0.4165 0.4186 0.3885 -0.1188 -0.0188 0.0433  354 ILE B CG1   
5195 C  CG2   . ILE B 374 ? 0.3633 0.3474 0.3353 -0.1019 -0.0183 0.0414  354 ILE B CG2   
5196 C  CD1   . ILE B 374 ? 0.4342 0.4239 0.4037 -0.1176 -0.0232 0.0433  354 ILE B CD1   
5197 N  N     . THR B 375 ? 0.2952 0.3077 0.2769 -0.0983 -0.0076 0.0383  355 THR B N     
5198 C  CA    . THR B 375 ? 0.2912 0.3037 0.2768 -0.0892 -0.0050 0.0360  355 THR B CA    
5199 C  C     . THR B 375 ? 0.2828 0.2787 0.2663 -0.0815 -0.0077 0.0359  355 THR B C     
5200 O  O     . THR B 375 ? 0.3243 0.3074 0.3026 -0.0832 -0.0119 0.0377  355 THR B O     
5201 C  CB    . THR B 375 ? 0.3426 0.3555 0.3242 -0.0921 -0.0039 0.0381  355 THR B CB    
5202 O  OG1   . THR B 375 ? 0.3648 0.3602 0.3366 -0.0958 -0.0086 0.0426  355 THR B OG1   
5203 C  CG2   . THR B 375 ? 0.3560 0.3864 0.3388 -0.1005 -0.0009 0.0380  355 THR B CG2   
5204 N  N     . PHE B 376 ? 0.2843 0.2811 0.2721 -0.0732 -0.0053 0.0335  356 PHE B N     
5205 C  CA    . PHE B 376 ? 0.3175 0.3008 0.3038 -0.0660 -0.0072 0.0329  356 PHE B CA    
5206 C  C     . PHE B 376 ? 0.3137 0.2818 0.2921 -0.0678 -0.0110 0.0361  356 PHE B C     
5207 O  O     . PHE B 376 ? 0.3259 0.2814 0.3011 -0.0652 -0.0145 0.0360  356 PHE B O     
5208 C  CB    . PHE B 376 ? 0.2532 0.2411 0.2453 -0.0577 -0.0040 0.0300  356 PHE B CB    
5209 C  CG    . PHE B 376 ? 0.2741 0.2504 0.2650 -0.0508 -0.0054 0.0290  356 PHE B CG    
5210 C  CD1   . PHE B 376 ? 0.2783 0.2499 0.2692 -0.0488 -0.0072 0.0277  356 PHE B CD1   
5211 C  CD2   . PHE B 376 ? 0.2687 0.2398 0.2586 -0.0465 -0.0050 0.0291  356 PHE B CD2   
5212 C  CE1   . PHE B 376 ? 0.2720 0.2344 0.2617 -0.0429 -0.0082 0.0263  356 PHE B CE1   
5213 C  CE2   . PHE B 376 ? 0.3036 0.2659 0.2929 -0.0405 -0.0061 0.0277  356 PHE B CE2   
5214 C  CZ    . PHE B 376 ? 0.2785 0.2370 0.2677 -0.0388 -0.0075 0.0261  356 PHE B CZ    
5215 N  N     . GLY B 377 ? 0.3127 0.2817 0.2876 -0.0722 -0.0109 0.0386  357 GLY B N     
5216 C  CA    . GLY B 377 ? 0.3398 0.2935 0.3067 -0.0743 -0.0155 0.0419  357 GLY B CA    
5217 C  C     . GLY B 377 ? 0.3723 0.3159 0.3327 -0.0807 -0.0207 0.0444  357 GLY B C     
5218 O  O     . GLY B 377 ? 0.3941 0.3221 0.3500 -0.0784 -0.0255 0.0450  357 GLY B O     
5219 N  N     . GLU B 378 ? 0.3500 0.3027 0.3101 -0.0887 -0.0200 0.0457  358 GLU B N     
5220 C  CA    . GLU B 378 ? 0.3655 0.3096 0.3196 -0.0956 -0.0249 0.0482  358 GLU B CA    
5221 C  C     . GLU B 378 ? 0.3703 0.3072 0.3265 -0.0896 -0.0267 0.0453  358 GLU B C     
5222 O  O     . GLU B 378 ? 0.3779 0.2992 0.3281 -0.0902 -0.0323 0.0465  358 GLU B O     
5223 C  CB    . GLU B 378 ? 0.3705 0.3293 0.3255 -0.1052 -0.0227 0.0494  358 GLU B CB    
5224 C  CG    . GLU B 378 ? 0.3802 0.3451 0.3310 -0.1130 -0.0215 0.0525  358 GLU B CG    
5225 C  CD    . GLU B 378 ? 0.3957 0.3816 0.3507 -0.1199 -0.0170 0.0516  358 GLU B CD    
5226 O  OE1   . GLU B 378 ? 0.3752 0.3714 0.3373 -0.1180 -0.0148 0.0484  358 GLU B OE1   
5227 O  OE2   . GLU B 378 ? 0.5489 0.5417 0.5003 -0.1272 -0.0157 0.0539  358 GLU B OE2   
5228 N  N     . PHE B 379 ? 0.3526 0.3004 0.3170 -0.0837 -0.0223 0.0414  359 PHE B N     
5229 C  CA    . PHE B 379 ? 0.3928 0.3356 0.3592 -0.0781 -0.0235 0.0386  359 PHE B CA    
5230 C  C     . PHE B 379 ? 0.4402 0.3680 0.4037 -0.0712 -0.0263 0.0375  359 PHE B C     
5231 O  O     . PHE B 379 ? 0.3960 0.3124 0.3559 -0.0702 -0.0304 0.0367  359 PHE B O     
5232 C  CB    . PHE B 379 ? 0.3438 0.3009 0.3191 -0.0728 -0.0184 0.0350  359 PHE B CB    
5233 C  CG    . PHE B 379 ? 0.3883 0.3420 0.3657 -0.0672 -0.0190 0.0320  359 PHE B CG    
5234 C  CD1   . PHE B 379 ? 0.4575 0.4107 0.4340 -0.0709 -0.0213 0.0319  359 PHE B CD1   
5235 C  CD2   . PHE B 379 ? 0.4104 0.3626 0.3908 -0.0587 -0.0172 0.0293  359 PHE B CD2   
5236 C  CE1   . PHE B 379 ? 0.5309 0.4813 0.5089 -0.0661 -0.0218 0.0292  359 PHE B CE1   
5237 C  CE2   . PHE B 379 ? 0.4196 0.3696 0.4014 -0.0543 -0.0176 0.0267  359 PHE B CE2   
5238 C  CZ    . PHE B 379 ? 0.4200 0.3690 0.4005 -0.0579 -0.0199 0.0266  359 PHE B CZ    
5239 N  N     . ALA B 380 ? 0.3719 0.2997 0.3366 -0.0666 -0.0244 0.0371  360 ALA B N     
5240 C  CA    . ALA B 380 ? 0.4345 0.3500 0.3974 -0.0599 -0.0269 0.0355  360 ALA B CA    
5241 C  C     . ALA B 380 ? 0.4196 0.3191 0.3744 -0.0636 -0.0337 0.0381  360 ALA B C     
5242 O  O     . ALA B 380 ? 0.4886 0.3763 0.4416 -0.0585 -0.0372 0.0359  360 ALA B O     
5243 C  CB    . ALA B 380 ? 0.3716 0.2914 0.3376 -0.0551 -0.0236 0.0350  360 ALA B CB    
5244 N  N     . ARG B 381 ? 0.4366 0.3353 0.3864 -0.0725 -0.0358 0.0424  361 ARG B N     
5245 C  CA    . ARG B 381 ? 0.4492 0.3314 0.3902 -0.0772 -0.0432 0.0455  361 ARG B CA    
5246 C  C     . ARG B 381 ? 0.4819 0.3579 0.4190 -0.0824 -0.0473 0.0461  361 ARG B C     
5247 O  O     . ARG B 381 ? 0.4847 0.3465 0.4137 -0.0877 -0.0542 0.0491  361 ARG B O     
5248 C  CB    . ARG B 381 ? 0.4820 0.3651 0.4179 -0.0854 -0.0442 0.0504  361 ARG B CB    
5249 C  CG    . ARG B 381 ? 0.5509 0.4361 0.4887 -0.0808 -0.0420 0.0503  361 ARG B CG    
5250 C  CD    . ARG B 381 ? 0.6881 0.5552 0.6211 -0.0767 -0.0486 0.0505  361 ARG B CD    
5251 N  NE    . ARG B 381 ? 0.6711 0.5397 0.6055 -0.0729 -0.0471 0.0507  361 ARG B NE    
5252 C  CZ    . ARG B 381 ? 0.5735 0.4434 0.5138 -0.0631 -0.0447 0.0466  361 ARG B CZ    
5253 N  NH1   . ARG B 381 ? 0.6773 0.5478 0.6224 -0.0561 -0.0434 0.0420  361 ARG B NH1   
5254 N  NH2   . ARG B 381 ? 0.5046 0.3755 0.4456 -0.0606 -0.0439 0.0473  361 ARG B NH2   
5255 N  N     . GLY B 382 ? 0.4465 0.3317 0.3885 -0.0813 -0.0439 0.0436  362 GLY B N     
5256 C  CA    . GLY B 382 ? 0.4281 0.3072 0.3666 -0.0855 -0.0479 0.0438  362 GLY B CA    
5257 C  C     . GLY B 382 ? 0.5121 0.3979 0.4479 -0.0970 -0.0482 0.0478  362 GLY B C     
5258 O  O     . GLY B 382 ? 0.4706 0.3493 0.4019 -0.1021 -0.0527 0.0489  362 GLY B O     
5259 N  N     . ILE B 383 ? 0.4369 0.3365 0.3751 -0.1014 -0.0438 0.0497  363 ILE B N     
5260 C  CA    . ILE B 383 ? 0.3911 0.2998 0.3271 -0.1128 -0.0435 0.0532  363 ILE B CA    
5261 C  C     . ILE B 383 ? 0.4277 0.3504 0.3707 -0.1128 -0.0398 0.0504  363 ILE B C     
5262 O  O     . ILE B 383 ? 0.4684 0.4025 0.4199 -0.1055 -0.0346 0.0465  363 ILE B O     
5263 C  CB    . ILE B 383 ? 0.4199 0.3401 0.3565 -0.1169 -0.0396 0.0553  363 ILE B CB    
5264 C  CG1   . ILE B 383 ? 0.4804 0.3851 0.4086 -0.1185 -0.0445 0.0589  363 ILE B CG1   
5265 C  CG2   . ILE B 383 ? 0.4397 0.3743 0.3759 -0.1284 -0.0377 0.0576  363 ILE B CG2   
5266 C  CD1   . ILE B 383 ? 0.6359 0.5503 0.5640 -0.1215 -0.0409 0.0607  363 ILE B CD1   
5267 N  N     . VAL B 384 ? 0.4274 0.3488 0.3666 -0.1212 -0.0431 0.0523  364 VAL B N     
5268 C  CA    . VAL B 384 ? 0.4227 0.3564 0.3680 -0.1220 -0.0407 0.0499  364 VAL B CA    
5269 C  C     . VAL B 384 ? 0.4205 0.3686 0.3659 -0.1336 -0.0393 0.0524  364 VAL B C     
5270 O  O     . VAL B 384 ? 0.5072 0.4675 0.4584 -0.1350 -0.0374 0.0503  364 VAL B O     
5271 C  CB    . VAL B 384 ? 0.4771 0.3974 0.4194 -0.1199 -0.0456 0.0487  364 VAL B CB    
5272 C  CG1   . VAL B 384 ? 0.5002 0.4098 0.4437 -0.1080 -0.0458 0.0451  364 VAL B CG1   
5273 C  CG2   . VAL B 384 ? 0.5326 0.4372 0.4642 -0.1290 -0.0529 0.0530  364 VAL B CG2   
5274 N  N     . ALA B 385 ? 0.4652 0.4132 0.4045 -0.1422 -0.0403 0.0566  365 ALA B N     
5275 C  CA    . ALA B 385 ? 0.4290 0.3925 0.3681 -0.1542 -0.0387 0.0588  365 ALA B CA    
5276 C  C     . ALA B 385 ? 0.5007 0.4706 0.4373 -0.1589 -0.0362 0.0612  365 ALA B C     
5277 O  O     . ALA B 385 ? 0.5383 0.4940 0.4688 -0.1566 -0.0388 0.0634  365 ALA B O     
5278 C  CB    . ALA B 385 ? 0.4692 0.4219 0.3992 -0.1651 -0.0452 0.0630  365 ALA B CB    
5279 N  N     . LYS B 386 ? 0.5225 0.5143 0.4637 -0.1653 -0.0312 0.0605  366 LYS B N     
5280 C  CA    . LYS B 386 ? 0.5023 0.5035 0.4421 -0.1691 -0.0277 0.0617  366 LYS B CA    
5281 C  C     . LYS B 386 ? 0.4683 0.4904 0.4089 -0.1817 -0.0248 0.0625  366 LYS B C     
5282 O  O     . LYS B 386 ? 0.5046 0.5417 0.4530 -0.1823 -0.0223 0.0591  366 LYS B O     
5283 C  CB    . LYS B 386 ? 0.5548 0.5649 0.5043 -0.1568 -0.0220 0.0567  366 LYS B CB    
5284 C  CG    . LYS B 386 ? 0.6543 0.6720 0.6024 -0.1588 -0.0186 0.0575  366 LYS B CG    
5285 C  CD    . LYS B 386 ? 0.4940 0.5165 0.4509 -0.1457 -0.0141 0.0527  366 LYS B CD    
5286 C  CE    . LYS B 386 ? 0.5754 0.6083 0.5321 -0.1476 -0.0101 0.0527  366 LYS B CE    
5287 N  NZ    . LYS B 386 ? 0.5953 0.6304 0.5597 -0.1350 -0.0066 0.0483  366 LYS B NZ    
5288 N  N     . ASN B 387 ? 0.5470 0.5703 0.4794 -0.1918 -0.0252 0.0667  367 ASN B N     
5289 C  CA    . ASN B 387 ? 0.4768 0.5226 0.4101 -0.2040 -0.0214 0.0669  367 ASN B CA    
5290 C  C     . ASN B 387 ? 0.5863 0.6365 0.5140 -0.2094 -0.0193 0.0693  367 ASN B C     
5291 O  O     . ASN B 387 ? 0.5959 0.6275 0.5158 -0.2070 -0.0228 0.0727  367 ASN B O     
5292 C  CB    . ASN B 387 ? 0.5297 0.5716 0.4548 -0.2181 -0.0264 0.0717  367 ASN B CB    
5293 C  CG    . ASN B 387 ? 0.6054 0.6234 0.5141 -0.2271 -0.0341 0.0796  367 ASN B CG    
5294 O  OD1   . ASN B 387 ? 0.5381 0.5317 0.4417 -0.2206 -0.0399 0.0814  367 ASN B OD1   
5295 N  ND2   . ASN B 387 ? 0.5211 0.5466 0.4213 -0.2420 -0.0344 0.0839  367 ASN B ND2   
5296 N  N     . THR B 388 ? 0.6153 0.6912 0.5474 -0.2163 -0.0133 0.0668  368 THR B N     
5297 C  CA    . THR B 388 ? 0.7317 0.8163 0.6591 -0.2225 -0.0103 0.0683  368 THR B CA    
5298 C  C     . THR B 388 ? 0.7296 0.8209 0.6468 -0.2403 -0.0119 0.0730  368 THR B C     
5299 O  O     . THR B 388 ? 0.7551 0.8595 0.6755 -0.2449 -0.0112 0.0710  368 THR B O     
5300 C  CB    . THR B 388 ? 0.8704 0.9808 0.8110 -0.2153 -0.0018 0.0605  368 THR B CB    
5301 O  OG1   . THR B 388 ? 0.9824 1.1166 0.9326 -0.2186 0.0020  0.0558  368 THR B OG1   
5302 C  CG2   . THR B 388 ? 0.8008 0.9035 0.7503 -0.1974 -0.0006 0.0560  368 THR B CG2   
5303 N  N     . VAL B 389 ? 0.6075 0.6879 0.5119 -0.2449 -0.0152 0.0775  369 VAL B N     
5304 C  CA    . VAL B 389 ? 0.6507 0.7340 0.5433 -0.2564 -0.0181 0.0806  369 VAL B CA    
5305 C  C     . VAL B 389 ? 0.6776 0.7776 0.5685 -0.2592 -0.0131 0.0785  369 VAL B C     
5306 O  O     . VAL B 389 ? 0.6801 0.7850 0.5775 -0.2521 -0.0085 0.0756  369 VAL B O     
5307 C  CB    . VAL B 389 ? 0.6390 0.6923 0.5154 -0.2609 -0.0285 0.0882  369 VAL B CB    
5308 C  CG1   . VAL B 389 ? 0.5905 0.6281 0.4681 -0.2584 -0.0336 0.0895  369 VAL B CG1   
5309 C  CG2   . VAL B 389 ? 0.6127 0.6473 0.4833 -0.2559 -0.0315 0.0913  369 VAL B CG2   
5310 N  N     . SER B 390 ? 0.5478 0.6564 0.4295 -0.2700 -0.0142 0.0799  370 SER B N     
5311 C  CA    . SER B 390 ? 0.6211 0.7458 0.4998 -0.2741 -0.0100 0.0779  370 SER B CA    
5312 C  C     . SER B 390 ? 0.6575 0.7616 0.5194 -0.2798 -0.0170 0.0848  370 SER B C     
5313 O  O     . SER B 390 ? 0.5326 0.6131 0.3840 -0.2831 -0.0255 0.0910  370 SER B O     
5314 C  CB    . SER B 390 ? 0.6217 0.7724 0.5015 -0.2826 -0.0061 0.0741  370 SER B CB    
5315 O  OG    . SER B 390 ? 0.7134 0.8794 0.5894 -0.2871 -0.0024 0.0718  370 SER B OG    
5316 O  OXT   . SER B 390 ? 0.7731 0.8835 0.6318 -0.2811 -0.0146 0.0841  370 SER B OXT   
5317 MN MN    . MN  C .   ? 0.2439 0.2135 0.2414 -0.0135 -0.0178 0.0267  401 MN  A MN    
5318 O  "O5'" . THM D .   ? 0.3943 0.3415 0.3775 -0.0099 -0.0334 0.0174  402 THM A "O5'" 
5319 C  "C5'" . THM D .   ? 0.3996 0.3464 0.3834 -0.0138 -0.0342 0.0207  402 THM A "C5'" 
5320 C  "C4'" . THM D .   ? 0.3013 0.2547 0.2891 -0.0128 -0.0296 0.0219  402 THM A "C4'" 
5321 O  "O4'" . THM D .   ? 0.2832 0.2450 0.2744 -0.0120 -0.0261 0.0224  402 THM A "O4'" 
5322 C  "C3'" . THM D .   ? 0.2636 0.2153 0.2517 -0.0081 -0.0280 0.0192  402 THM A "C3'" 
5323 O  "O3'" . THM D .   ? 0.3419 0.2881 0.3286 -0.0090 -0.0303 0.0198  402 THM A "O3'" 
5324 C  "C2'" . THM D .   ? 0.2247 0.1849 0.2169 -0.0067 -0.0229 0.0201  402 THM A "C2'" 
5325 C  "C1'" . THM D .   ? 0.2476 0.2128 0.2410 -0.0083 -0.0223 0.0213  402 THM A "C1'" 
5326 N  N1    . THM D .   ? 0.2558 0.2221 0.2483 -0.0057 -0.0216 0.0193  402 THM A N1    
5327 C  C2    . THM D .   ? 0.2622 0.2333 0.2562 -0.0067 -0.0209 0.0206  402 THM A C2    
5328 O  O2    . THM D .   ? 0.2632 0.2385 0.2601 -0.0090 -0.0207 0.0228  402 THM A O2    
5329 N  N3    . THM D .   ? 0.2371 0.2084 0.2291 -0.0050 -0.0207 0.0190  402 THM A N3    
5330 C  C4    . THM D .   ? 0.2732 0.2417 0.2620 -0.0026 -0.0206 0.0159  402 THM A C4    
5331 O  O4    . THM D .   ? 0.2857 0.2553 0.2722 -0.0021 -0.0204 0.0147  402 THM A O4    
5332 C  C5    . THM D .   ? 0.3154 0.2799 0.3038 -0.0011 -0.0211 0.0140  402 THM A C5    
5333 C  C5M   . THM D .   ? 0.3320 0.2950 0.3182 0.0020  -0.0210 0.0096  402 THM A C5M   
5334 C  C6    . THM D .   ? 0.2662 0.2292 0.2563 -0.0026 -0.0218 0.0159  402 THM A C6    
5335 C  C1    . EDO E .   ? 0.5053 0.4889 0.5124 -0.0047 -0.0010 0.0254  403 EDO A C1    
5336 O  O1    . EDO E .   ? 0.5334 0.5144 0.5398 -0.0034 -0.0008 0.0250  403 EDO A O1    
5337 C  C2    . EDO E .   ? 0.4985 0.4799 0.5061 -0.0017 -0.0017 0.0241  403 EDO A C2    
5338 O  O2    . EDO E .   ? 0.4413 0.4161 0.4461 -0.0012 -0.0049 0.0235  403 EDO A O2    
5339 MN MN    . MN  F .   ? 0.2607 0.2020 0.2387 -0.0075 -0.0054 -0.0022 401 MN  B MN    
5340 CL CL    . CL  G .   ? 0.3267 0.2492 0.3132 0.0041  -0.0117 -0.0017 402 CL  B CL    
5341 O  "O5'" . THM H .   ? 0.4569 0.3642 0.4329 -0.0151 -0.0207 0.0096  403 THM B "O5'" 
5342 C  "C5'" . THM H .   ? 0.4149 0.3232 0.3899 -0.0152 -0.0204 0.0073  403 THM B "C5'" 
5343 C  "C4'" . THM H .   ? 0.3056 0.2235 0.2839 -0.0122 -0.0158 0.0055  403 THM B "C4'" 
5344 O  "O4'" . THM H .   ? 0.2731 0.1993 0.2546 -0.0144 -0.0128 0.0088  403 THM B "O4'" 
5345 C  "C3'" . THM H .   ? 0.2930 0.2121 0.2730 -0.0068 -0.0142 0.0023  403 THM B "C3'" 
5346 O  "O3'" . THM H .   ? 0.3408 0.2577 0.3190 -0.0039 -0.0149 -0.0025 403 THM B "O3'" 
5347 C  "C2'" . THM H .   ? 0.2782 0.2075 0.2615 -0.0065 -0.0096 0.0036  403 THM B "C2'" 
5348 C  "C1'" . THM H .   ? 0.2757 0.2077 0.2601 -0.0108 -0.0094 0.0080  403 THM B "C1'" 
5349 N  N1    . THM H .   ? 0.2531 0.1860 0.2392 -0.0112 -0.0089 0.0105  403 THM B N1    
5350 C  C2    . THM H .   ? 0.2851 0.2237 0.2732 -0.0145 -0.0076 0.0135  403 THM B C2    
5351 O  O2    . THM H .   ? 0.2661 0.2092 0.2551 -0.0167 -0.0070 0.0141  403 THM B O2    
5352 N  N3    . THM H .   ? 0.2733 0.2128 0.2623 -0.0151 -0.0071 0.0156  403 THM B N3    
5353 C  C4    . THM H .   ? 0.2977 0.2322 0.2859 -0.0127 -0.0083 0.0153  403 THM B C4    
5354 O  O4    . THM H .   ? 0.3117 0.2472 0.3003 -0.0140 -0.0080 0.0175  403 THM B O4    
5355 C  C5    . THM H .   ? 0.2944 0.2230 0.2813 -0.0089 -0.0100 0.0119  403 THM B C5    
5356 C  C5M   . THM H .   ? 0.3202 0.2434 0.3068 -0.0056 -0.0119 0.0108  403 THM B C5M   
5357 C  C6    . THM H .   ? 0.2741 0.2026 0.2600 -0.0083 -0.0100 0.0095  403 THM B C6    
5358 O  O6    . BU3 I .   ? 0.4799 0.4476 0.4545 -0.0065 0.0064  -0.0059 404 BU3 B O6    
5359 C  C3    . BU3 I .   ? 0.5376 0.5102 0.5086 -0.0091 0.0079  -0.0056 404 BU3 B C3    
5360 C  C4    . BU3 I .   ? 0.5754 0.5460 0.5421 -0.0126 0.0059  -0.0036 404 BU3 B C4    
5361 C  C2    . BU3 I .   ? 0.4502 0.4280 0.4194 -0.0083 0.0105  -0.0108 404 BU3 B C2    
5362 O  O5    . BU3 I .   ? 0.4951 0.4747 0.4691 -0.0046 0.0117  -0.0127 404 BU3 B O5    
5363 C  C1    . BU3 I .   ? 0.4394 0.4231 0.4038 -0.0123 0.0122  -0.0103 404 BU3 B C1    
5364 O  O     . HOH J .   ? 0.3493 0.4997 0.3671 0.0005  0.0384  -0.0610 501 HOH A O     
5365 O  O     . HOH J .   ? 0.6139 0.5650 0.5220 -0.0396 -0.0488 0.0515  502 HOH A O     
5366 O  O     . HOH J .   ? 0.5469 0.7480 0.6243 -0.0586 0.0188  -0.0029 503 HOH A O     
5367 O  O     . HOH J .   ? 0.5525 0.7292 0.5703 0.0054  0.0411  -0.0827 504 HOH A O     
5368 O  O     C HOH J .   ? 0.2856 0.2516 0.2720 -0.0103 -0.0288 0.0191  505 HOH A O     
5369 O  O     . HOH J .   ? 0.5565 0.5957 0.5707 -0.0072 0.0223  0.0065  506 HOH A O     
5370 O  O     . HOH J .   ? 0.5578 0.5582 0.5031 0.0041  -0.0137 -0.0350 507 HOH A O     
5371 O  O     . HOH J .   ? 0.6223 0.5559 0.5974 0.0164  -0.0414 -0.0172 508 HOH A O     
5372 O  O     . HOH J .   ? 0.5274 0.4991 0.4921 -0.0274 -0.0593 0.0249  509 HOH A O     
5373 O  O     . HOH J .   ? 0.5176 0.4395 0.5227 0.0268  -0.0474 0.0011  510 HOH A O     
5374 O  O     . HOH J .   ? 0.4522 0.5996 0.5548 -0.0306 -0.0471 0.0109  511 HOH A O     
5375 O  O     . HOH J .   ? 0.6207 0.5556 0.5650 -0.0120 -0.0535 -0.0052 512 HOH A O     
5376 O  O     . HOH J .   ? 0.4906 0.4312 0.4852 0.0030  -0.0265 0.0237  513 HOH A O     
5377 O  O     . HOH J .   ? 0.3230 0.3054 0.3144 0.0231  -0.0139 -0.0226 514 HOH A O     
5378 O  O     . HOH J .   ? 0.5458 0.5430 0.4813 -0.0305 -0.0041 0.0264  515 HOH A O     
5379 O  O     . HOH J .   ? 0.2953 0.3922 0.3943 0.0402  -0.0038 -0.0251 516 HOH A O     
5380 O  O     . HOH J .   ? 0.6029 0.6184 0.5985 0.0500  -0.0213 -0.0831 517 HOH A O     
5381 O  O     . HOH J .   ? 0.5682 0.5988 0.5480 -0.0817 -0.0087 0.0451  518 HOH A O     
5382 O  O     . HOH J .   ? 0.6451 0.5880 0.6304 0.0042  -0.0421 0.0428  519 HOH A O     
5383 O  O     . HOH J .   ? 0.5578 0.6046 0.4926 -0.0210 0.0115  -0.0197 520 HOH A O     
5384 O  O     . HOH J .   ? 0.6123 0.5711 0.6247 0.0168  -0.0102 0.0236  521 HOH A O     
5385 O  O     . HOH J .   ? 0.5294 0.5040 0.4902 -0.0247 -0.0037 0.0399  522 HOH A O     
5386 O  O     . HOH J .   ? 0.5246 0.4660 0.5359 0.0326  -0.0368 -0.0092 523 HOH A O     
5387 O  O     . HOH J .   ? 0.4403 0.4119 0.4063 -0.0503 -0.0134 0.0437  524 HOH A O     
5388 O  O     . HOH J .   ? 0.2634 0.2757 0.2968 0.0383  -0.0073 -0.0284 525 HOH A O     
5389 O  O     . HOH J .   ? 0.5846 0.5625 0.5812 -0.0120 -0.0003 0.0284  526 HOH A O     
5390 O  O     . HOH J .   ? 0.4631 0.5939 0.5536 0.0138  0.0135  -0.0210 527 HOH A O     
5391 O  O     . HOH J .   ? 0.4159 0.3988 0.3790 0.0011  -0.0148 -0.0059 528 HOH A O     
5392 O  O     . HOH J .   ? 0.5701 0.5345 0.5000 -0.0299 -0.0589 0.0249  529 HOH A O     
5393 O  O     . HOH J .   ? 0.5060 0.4876 0.5072 -0.0018 0.0091  0.0265  530 HOH A O     
5394 O  O     . HOH J .   ? 0.4933 0.4629 0.5008 0.0065  -0.0041 0.0198  531 HOH A O     
5395 O  O     . HOH J .   ? 0.4803 0.4679 0.4934 0.0078  0.0123  0.0206  532 HOH A O     
5396 O  O     . HOH J .   ? 0.3812 0.6422 0.5272 -0.0383 -0.0117 -0.0192 533 HOH A O     
5397 O  O     . HOH J .   ? 0.4124 0.3670 0.3969 -0.0284 -0.0373 0.0287  534 HOH A O     
5398 O  O     . HOH J .   ? 0.4087 0.6252 0.5148 -0.0294 0.0177  -0.0202 535 HOH A O     
5399 O  O     . HOH J .   ? 0.4765 0.5502 0.5808 0.0372  -0.0596 0.0003  536 HOH A O     
5400 O  O     . HOH J .   ? 0.4937 0.4529 0.4750 -0.0016 -0.0499 0.0430  537 HOH A O     
5401 O  O     . HOH J .   ? 0.5525 0.5316 0.5822 0.0258  -0.0087 0.0153  538 HOH A O     
5402 O  O     . HOH J .   ? 0.6420 0.6279 0.6339 -0.0530 -0.0524 0.0344  539 HOH A O     
5403 O  O     . HOH J .   ? 0.5067 0.4954 0.5043 -0.0053 -0.0407 0.0323  540 HOH A O     
5404 O  O     . HOH J .   ? 0.2541 0.2354 0.2584 -0.0097 -0.0114 0.0260  541 HOH A O     
5405 O  O     . HOH J .   ? 0.5505 0.5366 0.6021 0.0428  -0.0296 0.0054  542 HOH A O     
5406 O  O     . HOH J .   ? 0.4117 0.4876 0.4219 -0.0790 -0.0054 0.0362  543 HOH A O     
5407 O  O     . HOH J .   ? 0.3458 0.4164 0.3769 0.0027  0.0238  -0.0134 544 HOH A O     
5408 O  O     . HOH J .   ? 0.4626 0.4245 0.4197 -0.0185 -0.0191 0.0433  545 HOH A O     
5409 O  O     . HOH J .   ? 0.3671 0.3888 0.3189 0.0002  -0.0006 -0.0297 546 HOH A O     
5410 O  O     . HOH J .   ? 0.5693 0.5361 0.5023 -0.0270 -0.0520 0.0248  547 HOH A O     
5411 O  O     . HOH J .   ? 0.4027 0.3879 0.4127 0.0006  0.0038  0.0234  548 HOH A O     
5412 O  O     . HOH J .   ? 0.4321 0.4926 0.4901 0.0389  0.0014  -0.0400 549 HOH A O     
5413 O  O     . HOH J .   ? 0.3629 0.3622 0.4010 0.0256  -0.0014 0.0106  550 HOH A O     
5414 O  O     . HOH J .   ? 0.4815 0.4950 0.4803 -0.0646 -0.0295 0.0406  551 HOH A O     
5415 O  O     . HOH J .   ? 0.4200 0.3743 0.4193 0.0265  -0.0268 -0.0142 552 HOH A O     
5416 O  O     . HOH J .   ? 0.2374 0.4173 0.3833 0.0084  -0.0481 -0.0131 553 HOH A O     
5417 O  O     . HOH J .   ? 0.4147 0.6098 0.5348 -0.0442 -0.0397 0.0041  554 HOH A O     
5418 O  O     . HOH J .   ? 0.4849 0.4133 0.4632 -0.0140 -0.0415 0.0206  555 HOH A O     
5419 O  O     . HOH J .   ? 0.4605 0.5058 0.5259 0.0119  -0.0648 0.0209  556 HOH A O     
5420 O  O     . HOH J .   ? 0.2844 0.2924 0.3114 0.0157  0.0086  0.0037  557 HOH A O     
5421 O  O     . HOH J .   ? 0.4592 0.4319 0.4108 -0.0179 -0.0376 0.0302  558 HOH A O     
5422 O  O     . HOH J .   ? 0.2920 0.3448 0.3752 0.0296  -0.0508 0.0088  559 HOH A O     
5423 O  O     . HOH J .   ? 0.4275 0.4161 0.4428 0.0080  0.0130  0.0185  560 HOH A O     
5424 O  O     . HOH J .   ? 0.3958 0.5747 0.4818 -0.0531 -0.0019 0.0058  561 HOH A O     
5425 O  O     . HOH J .   ? 0.5250 0.4783 0.5206 0.0294  -0.0303 -0.0223 562 HOH A O     
5426 O  O     . HOH J .   ? 0.2653 0.3022 0.2786 -0.0247 0.0136  0.0220  563 HOH A O     
5427 O  O     . HOH J .   ? 0.4638 0.5253 0.4809 -0.0076 0.0259  -0.0033 564 HOH A O     
5428 O  O     . HOH J .   ? 0.2669 0.2498 0.2222 -0.0112 -0.0176 0.0149  565 HOH A O     
5429 O  O     . HOH J .   ? 0.5210 0.4668 0.4932 -0.0085 -0.0390 0.0094  566 HOH A O     
5430 O  O     . HOH J .   ? 0.6436 0.5047 0.6065 -0.0043 -0.0816 0.0312  567 HOH A O     
5431 O  O     . HOH J .   ? 0.3737 0.3514 0.3552 -0.0310 -0.0049 0.0354  568 HOH A O     
5432 O  O     . HOH J .   ? 0.5715 0.4771 0.5793 0.0311  -0.0694 0.0040  569 HOH A O     
5433 O  O     . HOH J .   ? 0.4087 0.5192 0.4377 -0.0146 0.0333  -0.0187 570 HOH A O     
5434 O  O     . HOH J .   ? 0.4044 0.3635 0.4035 0.0049  -0.0066 0.0310  571 HOH A O     
5435 O  O     . HOH J .   ? 0.3027 0.4076 0.3761 -0.0320 -0.0381 0.0192  572 HOH A O     
5436 O  O     . HOH J .   ? 0.3716 0.3682 0.3341 -0.0025 -0.0057 -0.0022 573 HOH A O     
5437 O  O     . HOH J .   ? 0.4432 0.4899 0.4812 0.0490  -0.0051 -0.0604 574 HOH A O     
5438 O  O     . HOH J .   ? 0.5004 0.6498 0.6546 0.0464  -0.0544 -0.0267 575 HOH A O     
5439 O  O     . HOH J .   ? 0.3311 0.3757 0.3565 -0.0152 0.0146  0.0172  576 HOH A O     
5440 O  O     . HOH J .   ? 0.5887 0.4595 0.5251 -0.0477 -0.0704 0.0517  577 HOH A O     
5441 O  O     . HOH J .   ? 0.3940 0.4118 0.4493 0.0225  -0.0640 0.0226  578 HOH A O     
5442 O  O     . HOH J .   ? 0.3463 0.2668 0.3206 -0.0222 -0.0433 0.0295  579 HOH A O     
5443 O  O     . HOH J .   ? 0.3229 0.3461 0.3686 0.0434  -0.0095 -0.0342 580 HOH A O     
5444 O  O     . HOH J .   ? 0.4919 0.5558 0.5443 -0.0267 -0.0640 0.0264  581 HOH A O     
5445 O  O     . HOH J .   ? 0.5015 0.5166 0.4795 -0.0900 -0.0250 0.0501  582 HOH A O     
5446 O  O     . HOH J .   ? 0.5289 0.4802 0.4667 -0.0224 -0.0543 0.0063  583 HOH A O     
5447 O  O     . HOH J .   ? 0.3885 0.2950 0.2842 -0.0988 -0.0541 0.0730  584 HOH A O     
5448 O  O     . HOH J .   ? 0.6467 0.6451 0.6456 -0.0182 -0.0610 0.0324  585 HOH A O     
5449 O  O     . HOH J .   ? 0.2576 0.2431 0.2568 0.0008  -0.0226 0.0302  586 HOH A O     
5450 O  O     . HOH J .   ? 0.2641 0.2433 0.2481 -0.0036 -0.0219 0.0313  587 HOH A O     
5451 O  O     . HOH J .   ? 0.4279 0.4017 0.3632 -0.0212 -0.0344 0.0176  588 HOH A O     
5452 O  O     . HOH J .   ? 0.2998 0.2890 0.3147 0.0069  0.0094  0.0209  589 HOH A O     
5453 O  O     . HOH J .   ? 0.6239 0.5309 0.5765 -0.0552 -0.0766 0.0308  590 HOH A O     
5454 O  O     . HOH J .   ? 0.4378 0.4289 0.4490 0.0023  0.0116  0.0205  591 HOH A O     
5455 O  O     . HOH J .   ? 0.4580 0.4021 0.4524 0.0048  -0.0248 0.0149  592 HOH A O     
5456 O  O     . HOH J .   ? 0.5302 0.4956 0.5365 0.0122  -0.0479 0.0365  593 HOH A O     
5457 O  O     . HOH J .   ? 0.2430 0.3444 0.2831 -0.0414 0.0121  0.0158  594 HOH A O     
5458 O  O     . HOH J .   ? 0.6278 0.4525 0.5219 -0.0720 -0.1010 0.0718  595 HOH A O     
5459 O  O     . HOH J .   ? 0.4548 0.4526 0.4844 0.0184  0.0001  0.0044  596 HOH A O     
5460 O  O     . HOH J .   ? 0.4613 0.4139 0.4374 -0.0451 -0.0554 0.0305  597 HOH A O     
5461 O  O     . HOH J .   ? 0.2500 0.2342 0.2640 0.0094  0.0073  0.0184  598 HOH A O     
5462 O  O     . HOH J .   ? 0.3244 0.4691 0.4589 0.0188  -0.0574 -0.0077 599 HOH A O     
5463 O  O     . HOH J .   ? 0.2833 0.2820 0.2691 0.0259  -0.0117 -0.0388 600 HOH A O     
5464 O  O     . HOH J .   ? 0.3784 0.3354 0.3592 -0.0033 -0.0209 0.0400  601 HOH A O     
5465 O  O     . HOH J .   ? 0.5744 0.6575 0.6289 -0.0516 -0.0773 0.0287  602 HOH A O     
5466 O  O     . HOH J .   ? 0.3776 0.3317 0.3894 0.0222  -0.0228 0.0045  603 HOH A O     
5467 O  O     . HOH J .   ? 0.4896 0.4724 0.4668 -0.0248 -0.0607 0.0298  604 HOH A O     
5468 O  O     . HOH J .   ? 0.7486 0.7551 0.7440 -0.0686 -0.0371 0.0417  605 HOH A O     
5469 O  O     . HOH J .   ? 0.5478 0.5020 0.5387 0.0047  -0.0285 0.0386  606 HOH A O     
5470 O  O     . HOH J .   ? 0.2979 0.3526 0.3853 0.0385  -0.0330 -0.0014 607 HOH A O     
5471 O  O     . HOH J .   ? 0.3696 0.4292 0.3364 -0.0236 0.0247  -0.0041 608 HOH A O     
5472 O  O     . HOH J .   ? 0.3291 0.3144 0.3309 -0.0138 -0.0013 0.0286  609 HOH A O     
5473 O  O     . HOH J .   ? 0.4364 0.4031 0.3986 -0.0136 -0.0468 0.0402  610 HOH A O     
5474 O  O     . HOH J .   ? 0.2279 0.3099 0.2690 -0.0263 0.0116  0.0147  611 HOH A O     
5475 O  O     . HOH J .   ? 0.4851 0.4691 0.4124 -0.0384 -0.0103 0.0384  612 HOH A O     
5476 O  O     . HOH J .   ? 0.3224 0.2381 0.2989 -0.0118 -0.0404 0.0313  613 HOH A O     
5477 O  O     . HOH J .   ? 0.2649 0.2494 0.2773 0.0091  0.0088  0.0228  614 HOH A O     
5478 O  O     . HOH J .   ? 0.5169 0.4829 0.4822 -0.0280 -0.0572 0.0219  615 HOH A O     
5479 O  O     . HOH J .   ? 0.2950 0.2795 0.3048 0.0041  -0.0001 0.0215  616 HOH A O     
5480 O  O     . HOH J .   ? 0.2594 0.3424 0.2855 0.0155  0.0223  -0.0366 617 HOH A O     
5481 O  O     . HOH J .   ? 0.4394 0.5409 0.4278 -0.0026 0.0296  -0.0443 618 HOH A O     
5482 O  O     . HOH J .   ? 0.4654 0.5011 0.4665 -0.0738 -0.0208 0.0414  619 HOH A O     
5483 O  O     . HOH J .   ? 0.3606 0.4137 0.4032 0.0036  0.0162  0.0058  620 HOH A O     
5484 O  O     . HOH J .   ? 0.4987 0.5935 0.5524 0.0467  0.0070  -0.0722 621 HOH A O     
5485 O  O     . HOH J .   ? 0.2916 0.3120 0.3072 -0.0312 -0.0103 0.0304  622 HOH A O     
5486 O  O     . HOH J .   ? 0.2548 0.2697 0.2643 -0.0338 -0.0080 0.0319  623 HOH A O     
5487 O  O     . HOH J .   ? 0.3039 0.4570 0.4411 0.0109  -0.0675 -0.0046 624 HOH A O     
5488 O  O     . HOH J .   ? 0.6408 0.5833 0.5319 -0.0542 -0.0451 0.0613  625 HOH A O     
5489 O  O     . HOH J .   ? 0.4883 0.4720 0.4941 -0.0017 0.0061  0.0236  626 HOH A O     
5490 O  O     . HOH J .   ? 0.3556 0.3515 0.3696 0.0051  0.0143  0.0176  627 HOH A O     
5491 O  O     . HOH J .   ? 0.3410 0.3307 0.2676 -0.0203 -0.0192 0.0032  628 HOH A O     
5492 O  O     . HOH J .   ? 0.2322 0.2265 0.2520 0.0099  0.0074  0.0213  629 HOH A O     
5493 O  O     . HOH J .   ? 0.2694 0.2483 0.2426 -0.0030 -0.0162 0.0120  630 HOH A O     
5494 O  O     . HOH J .   ? 0.3719 0.3227 0.3630 -0.0029 -0.0245 0.0178  631 HOH A O     
5495 O  O     . HOH J .   ? 0.4402 0.5426 0.4642 -0.0525 0.0191  0.0170  632 HOH A O     
5496 O  O     . HOH J .   ? 0.5118 0.6991 0.5945 -0.0782 -0.0150 0.0150  633 HOH A O     
5497 O  O     . HOH J .   ? 0.3266 0.4537 0.3392 -0.0057 0.0365  -0.0425 634 HOH A O     
5498 O  O     . HOH J .   ? 0.2738 0.2711 0.2789 -0.0304 -0.0177 0.0321  635 HOH A O     
5499 O  O     . HOH J .   ? 0.3614 0.5121 0.4153 -0.0568 0.0151  0.0097  636 HOH A O     
5500 O  O     . HOH J .   ? 0.4609 0.3937 0.3738 -0.0922 -0.0394 0.0659  637 HOH A O     
5501 O  O     . HOH J .   ? 0.3300 0.3157 0.3475 0.0124  0.0071  0.0215  638 HOH A O     
5502 O  O     . HOH J .   ? 0.3543 0.2999 0.3115 -0.0514 -0.0270 0.0479  639 HOH A O     
5503 O  O     . HOH J .   ? 0.4493 0.4577 0.4944 0.0311  -0.0111 -0.0109 640 HOH A O     
5504 O  O     . HOH J .   ? 0.3543 0.3203 0.3510 -0.0074 -0.0070 0.0276  641 HOH A O     
5505 O  O     . HOH J .   ? 0.2913 0.2399 0.2965 0.0159  -0.0228 0.0100  642 HOH A O     
5506 O  O     . HOH J .   ? 0.3356 0.5068 0.4930 0.0397  -0.0412 -0.0311 643 HOH A O     
5507 O  O     . HOH J .   ? 0.5089 0.5446 0.6011 0.0529  -0.0521 -0.0045 644 HOH A O     
5508 O  O     . HOH J .   ? 0.5033 0.4545 0.4752 -0.0051 -0.0474 0.0458  645 HOH A O     
5509 O  O     . HOH J .   ? 0.2535 0.2664 0.2236 -0.0006 0.0042  -0.0070 646 HOH A O     
5510 O  O     . HOH J .   ? 0.4843 0.4501 0.4753 -0.0113 -0.0060 0.0293  647 HOH A O     
5511 O  O     . HOH J .   ? 0.2589 0.3714 0.2854 0.0071  0.0301  -0.0428 648 HOH A O     
5512 O  O     . HOH J .   ? 0.3292 0.3457 0.3649 0.0049  -0.0546 0.0284  649 HOH A O     
5513 O  O     . HOH J .   ? 0.4641 0.4017 0.4294 -0.0585 -0.0477 0.0444  650 HOH A O     
5514 O  O     . HOH J .   ? 0.6282 0.5968 0.6699 0.0447  -0.0422 -0.0160 651 HOH A O     
5515 O  O     . HOH J .   ? 0.4100 0.4178 0.3519 -0.0239 0.0009  0.0148  652 HOH A O     
5516 O  O     . HOH J .   ? 0.3989 0.3625 0.3773 0.0003  -0.0238 0.0067  653 HOH A O     
5517 O  O     . HOH J .   ? 0.5453 0.6417 0.6251 0.0241  0.0116  -0.0191 654 HOH A O     
5518 O  O     . HOH J .   ? 0.2716 0.2616 0.2212 -0.0180 -0.0090 0.0225  655 HOH A O     
5519 O  O     . HOH J .   ? 0.5123 0.4714 0.4969 -0.0058 -0.0081 0.0370  656 HOH A O     
5520 O  O     . HOH J .   ? 0.2684 0.2232 0.2582 0.0038  -0.0229 0.0100  657 HOH A O     
5521 O  O     . HOH J .   ? 0.6488 0.5307 0.6350 0.0178  -0.0708 0.0102  658 HOH A O     
5522 O  O     . HOH J .   ? 0.4693 0.5289 0.4130 -0.0233 0.0188  -0.0176 659 HOH A O     
5523 O  O     . HOH J .   ? 0.3798 0.4568 0.4842 0.0379  -0.0491 -0.0029 660 HOH A O     
5524 O  O     . HOH J .   ? 0.5763 0.5190 0.5060 -0.1043 -0.0470 0.0666  661 HOH A O     
5525 O  O     . HOH J .   ? 0.3089 0.4616 0.3396 -0.0026 0.0390  -0.0524 662 HOH A O     
5526 O  O     C HOH J .   ? 0.2844 0.2406 0.2680 -0.0081 -0.0303 0.0160  663 HOH A O     
5527 O  O     . HOH J .   ? 0.5627 0.5454 0.5490 -0.0099 -0.0511 0.0351  664 HOH A O     
5528 O  O     . HOH J .   ? 0.6438 0.7909 0.6590 0.0382  0.0211  -0.1157 665 HOH A O     
5529 O  O     . HOH J .   ? 0.3785 0.3537 0.3427 -0.0138 -0.0346 0.0238  666 HOH A O     
5530 O  O     . HOH J .   ? 0.3818 0.3962 0.3996 -0.0149 -0.0573 0.0308  667 HOH A O     
5531 O  O     . HOH J .   ? 0.4286 0.3535 0.4136 -0.0025 -0.0371 0.0191  668 HOH A O     
5532 O  O     . HOH J .   ? 0.5228 0.5810 0.5420 -0.0756 -0.0317 0.0381  669 HOH A O     
5533 O  O     . HOH J .   ? 0.5955 0.5322 0.6126 0.0431  -0.0471 -0.0201 670 HOH A O     
5534 O  O     . HOH J .   ? 0.5754 0.6078 0.5067 -0.0284 0.0084  -0.0014 671 HOH A O     
5535 O  O     . HOH J .   ? 0.3816 0.3331 0.3643 0.0009  -0.0397 0.0427  672 HOH A O     
5536 O  O     . HOH J .   ? 0.2990 0.2757 0.3020 0.0082  -0.0048 0.0143  673 HOH A O     
5537 O  O     . HOH J .   ? 0.5933 0.5323 0.5639 0.0340  -0.0481 -0.0513 674 HOH A O     
5538 O  O     . HOH J .   ? 0.4642 0.3986 0.4379 -0.0368 -0.0459 0.0329  675 HOH A O     
5539 O  O     . HOH J .   ? 0.3490 0.3292 0.3533 -0.0090 -0.0085 0.0264  676 HOH A O     
5540 O  O     . HOH J .   ? 0.3489 0.3502 0.3543 0.0178  0.0027  -0.0072 677 HOH A O     
5541 O  O     . HOH J .   ? 0.5549 0.5862 0.4896 -0.0532 0.0153  0.0270  678 HOH A O     
5542 O  O     . HOH J .   ? 0.3788 0.3575 0.4083 0.0242  -0.0421 0.0266  679 HOH A O     
5543 O  O     . HOH J .   ? 0.4987 0.4414 0.5104 0.0284  -0.0341 -0.0022 680 HOH A O     
5544 O  O     . HOH J .   ? 0.3344 0.3056 0.3417 0.0125  -0.0064 0.0117  681 HOH A O     
5545 O  O     . HOH J .   ? 0.2812 0.5874 0.4548 -0.0154 0.0022  -0.0477 682 HOH A O     
5546 O  O     . HOH J .   ? 0.5311 0.3978 0.5087 0.0116  -0.0818 0.0186  683 HOH A O     
5547 O  O     . HOH J .   ? 0.3540 0.4178 0.2686 -0.0808 0.0237  0.0259  684 HOH A O     
5548 O  O     . HOH J .   ? 0.4851 0.4649 0.4831 -0.0141 -0.0020 0.0293  685 HOH A O     
5549 O  O     . HOH J .   ? 0.4024 0.3951 0.3123 -0.0354 -0.0176 0.0186  686 HOH A O     
5550 O  O     . HOH J .   ? 0.3951 0.3661 0.4119 0.0171  -0.0059 0.0229  687 HOH A O     
5551 O  O     . HOH J .   ? 0.2966 0.3712 0.3479 -0.0389 -0.0411 0.0261  688 HOH A O     
5552 O  O     . HOH J .   ? 0.5714 0.5191 0.5566 -0.0043 -0.0127 0.0377  689 HOH A O     
5553 O  O     . HOH J .   ? 0.3543 0.4744 0.4243 -0.0011 0.0208  -0.0118 690 HOH A O     
5554 O  O     . HOH J .   ? 0.6365 0.5755 0.6510 0.0263  -0.0369 0.0251  691 HOH A O     
5555 O  O     . HOH J .   ? 0.5196 0.5071 0.4836 -0.0020 -0.0110 0.0009  692 HOH A O     
5556 O  O     . HOH J .   ? 0.3254 0.3179 0.3341 -0.0072 -0.0156 0.0254  693 HOH A O     
5557 O  O     . HOH J .   ? 0.4741 0.4638 0.5153 0.0548  -0.0305 -0.0409 694 HOH A O     
5558 O  O     . HOH J .   ? 0.5456 0.6414 0.5158 -0.0077 0.0274  -0.0452 695 HOH A O     
5559 O  O     . HOH J .   ? 0.3284 0.6256 0.4822 -0.0403 0.0032  -0.0319 696 HOH A O     
5560 O  O     . HOH J .   ? 0.3101 0.2439 0.2940 -0.0120 -0.0330 0.0253  697 HOH A O     
5561 O  O     . HOH J .   ? 0.3909 0.5942 0.5488 0.0382  -0.0109 -0.0493 698 HOH A O     
5562 O  O     . HOH J .   ? 0.5309 0.6319 0.4682 -0.0481 0.0339  -0.0149 699 HOH A O     
5563 O  O     . HOH J .   ? 0.3415 0.3447 0.3612 0.0053  0.0139  0.0177  700 HOH A O     
5564 O  O     . HOH J .   ? 0.2667 0.2347 0.2697 0.0038  -0.0089 0.0190  701 HOH A O     
5565 O  O     . HOH J .   ? 0.3676 0.5802 0.4953 -0.0102 0.0025  -0.0240 702 HOH A O     
5566 O  O     . HOH J .   ? 0.3607 0.5852 0.5065 0.0009  -0.0058 -0.0312 703 HOH A O     
5567 O  O     . HOH J .   ? 0.4839 0.6061 0.5445 0.0611  0.0043  -0.1054 704 HOH A O     
5568 O  O     . HOH J .   ? 0.4062 0.4974 0.3458 -0.0694 0.0337  0.0107  705 HOH A O     
5569 O  O     . HOH J .   ? 0.4532 0.5364 0.4664 -0.0149 0.0308  -0.0090 706 HOH A O     
5570 O  O     . HOH J .   ? 0.5513 0.5430 0.5089 -0.0651 -0.0063 0.0449  707 HOH A O     
5571 O  O     . HOH J .   ? 0.4249 0.4255 0.3313 -0.0403 -0.0116 0.0192  708 HOH A O     
5572 O  O     . HOH J .   ? 0.6442 0.5502 0.5586 -0.0757 -0.0506 0.0640  709 HOH A O     
5573 O  O     . HOH J .   ? 0.6099 0.6884 0.6642 0.0451  0.0040  -0.0604 710 HOH A O     
5574 O  O     . HOH J .   ? 0.5010 0.3700 0.4454 -0.0340 -0.0709 0.0459  711 HOH A O     
5575 O  O     . HOH J .   ? 0.3088 0.3554 0.2638 -0.0330 0.0211  0.0083  712 HOH A O     
5576 O  O     . HOH J .   ? 0.6308 0.5675 0.6211 0.0073  -0.0313 0.0090  713 HOH A O     
5577 O  O     . HOH J .   ? 0.3755 0.4760 0.4104 -0.0005 0.0289  -0.0246 714 HOH A O     
5578 O  O     . HOH J .   ? 0.6949 0.5944 0.6567 -0.0317 -0.0598 0.0304  715 HOH A O     
5579 O  O     . HOH J .   ? 0.4303 0.4570 0.3967 -0.0697 0.0060  0.0385  716 HOH A O     
5580 O  O     . HOH J .   ? 0.4437 0.4105 0.3883 -0.0260 -0.0184 0.0433  717 HOH A O     
5581 O  O     . HOH J .   ? 0.3675 0.3424 0.3702 -0.0021 -0.0101 0.0222  718 HOH A O     
5582 O  O     . HOH J .   ? 0.5197 0.6254 0.5068 0.0027  0.0279  -0.0554 719 HOH A O     
5583 O  O     . HOH J .   ? 0.3835 0.4041 0.3808 -0.0071 0.0185  0.0127  720 HOH A O     
5584 O  O     . HOH J .   ? 0.3993 0.3717 0.4172 0.0183  -0.0239 0.0279  721 HOH A O     
5585 O  O     . HOH J .   ? 0.5666 0.5092 0.5405 -0.0461 -0.0483 0.0357  722 HOH A O     
5586 O  O     . HOH J .   ? 0.6094 0.6435 0.6965 0.0443  -0.0677 0.0062  723 HOH A O     
5587 O  O     . HOH J .   ? 0.3609 0.5196 0.4194 -0.0626 0.0105  0.0114  724 HOH A O     
5588 O  O     . HOH J .   ? 0.5376 0.5425 0.5507 -0.0083 -0.0573 0.0323  725 HOH A O     
5589 O  O     . HOH J .   ? 0.7209 0.5724 0.6653 -0.0245 -0.0837 0.0430  726 HOH A O     
5590 O  O     . HOH J .   ? 0.4830 0.4976 0.4911 -0.0511 -0.0338 0.0354  727 HOH A O     
5591 O  O     . HOH J .   ? 0.3623 0.5994 0.5019 -0.0424 -0.0281 -0.0082 728 HOH A O     
5592 O  O     . HOH J .   ? 0.5136 0.4866 0.4556 -0.0324 -0.0107 0.0431  729 HOH A O     
5593 O  O     . HOH J .   ? 0.6006 0.5942 0.6368 0.0202  -0.0651 0.0291  730 HOH A O     
5594 O  O     . HOH J .   ? 0.3736 0.4538 0.4807 0.0444  -0.0360 -0.0116 731 HOH A O     
5595 O  O     . HOH J .   ? 0.4260 0.4202 0.4368 -0.0042 0.0063  0.0242  732 HOH A O     
5596 O  O     . HOH J .   ? 0.4516 0.4722 0.4752 0.0524  -0.0160 -0.0649 733 HOH A O     
5597 O  O     . HOH J .   ? 0.5365 0.3759 0.4160 -0.1043 -0.0944 0.0824  734 HOH A O     
5598 O  O     . HOH J .   ? 0.3602 0.4642 0.4774 0.0235  -0.0787 0.0031  735 HOH A O     
5599 O  O     . HOH J .   ? 0.4448 0.6157 0.6063 0.0497  -0.0377 -0.0395 736 HOH A O     
5600 O  O     . HOH J .   ? 0.3724 0.3423 0.3065 -0.0250 -0.0373 0.0337  737 HOH A O     
5601 O  O     . HOH J .   ? 0.5421 0.5000 0.5473 0.0136  -0.0299 0.0336  738 HOH A O     
5602 O  O     . HOH J .   ? 0.4241 0.5795 0.4787 0.0543  0.0154  -0.1178 739 HOH A O     
5603 O  O     . HOH J .   ? 0.5740 0.6165 0.5157 -0.0575 0.0203  0.0260  740 HOH A O     
5604 O  O     . HOH J .   ? 0.4390 0.5756 0.3824 -0.0546 0.0436  -0.0255 741 HOH A O     
5605 O  O     . HOH J .   ? 0.4092 0.4306 0.4527 0.0484  -0.0129 -0.0429 742 HOH A O     
5606 O  O     . HOH J .   ? 0.4798 0.4902 0.5256 0.0295  0.0006  0.0029  743 HOH A O     
5607 O  O     . HOH J .   ? 0.4347 0.4098 0.3992 -0.0176 -0.0461 0.0287  744 HOH A O     
5608 O  O     . HOH J .   ? 0.2572 0.2235 0.2543 -0.0112 -0.0165 0.0262  745 HOH A O     
5609 O  O     . HOH J .   ? 0.4423 0.3995 0.4400 0.0022  -0.0168 0.0179  746 HOH A O     
5610 O  O     . HOH J .   ? 0.5556 0.5608 0.4708 -0.0457 -0.0025 0.0284  747 HOH A O     
5611 O  O     . HOH J .   ? 0.5114 0.5111 0.5955 0.0674  -0.0545 -0.0134 748 HOH A O     
5612 O  O     . HOH J .   ? 0.6742 0.6509 0.7261 0.0429  -0.0680 0.0178  749 HOH A O     
5613 O  O     . HOH J .   ? 0.2105 0.1813 0.2135 -0.0014 -0.0043 0.0243  750 HOH A O     
5614 O  O     . HOH J .   ? 0.5449 0.5622 0.5118 0.0307  -0.0153 -0.0739 751 HOH A O     
5615 O  O     . HOH J .   ? 0.5945 0.6324 0.5109 -0.0341 0.0071  -0.0068 752 HOH A O     
5616 O  O     . HOH J .   ? 0.5877 0.5900 0.5154 -0.0454 0.0014  0.0341  753 HOH A O     
5617 O  O     . HOH J .   ? 0.6021 0.4086 0.4693 -0.0963 -0.1136 0.0852  754 HOH A O     
5618 O  O     . HOH J .   ? 0.7043 0.7425 0.6664 -0.0429 0.0213  0.0223  755 HOH A O     
5619 O  O     . HOH J .   ? 0.2637 0.2293 0.2607 -0.0063 -0.0174 0.0225  756 HOH A O     
5620 O  O     . HOH J .   ? 0.3013 0.4308 0.4124 0.0346  -0.0008 -0.0301 757 HOH A O     
5621 O  O     . HOH J .   ? 0.5511 0.4962 0.5401 0.0186  -0.0309 -0.0092 758 HOH A O     
5622 O  O     . HOH J .   ? 0.3869 0.3691 0.3978 0.0052  0.0057  0.0212  759 HOH A O     
5623 O  O     . HOH J .   ? 0.4529 0.6034 0.4607 -0.0213 0.0437  -0.0407 760 HOH A O     
5624 O  O     . HOH J .   ? 0.5075 0.5282 0.4371 -0.0326 0.0049  0.0108  761 HOH A O     
5625 O  O     . HOH J .   ? 0.6138 0.6436 0.7158 0.0647  -0.0681 -0.0100 762 HOH A O     
5626 O  O     . HOH J .   ? 0.5879 0.6523 0.6167 -0.0662 -0.0328 0.0344  763 HOH A O     
5627 O  O     . HOH J .   ? 0.6251 0.5832 0.5334 -0.0356 -0.0629 0.0148  764 HOH A O     
5628 O  O     . HOH J .   ? 0.5411 0.4821 0.5305 -0.0005 -0.0287 0.0162  765 HOH A O     
5629 O  O     . HOH J .   ? 0.7256 0.5630 0.6538 -0.0368 -0.0933 0.0525  766 HOH A O     
5630 O  O     . HOH J .   ? 0.5096 0.5739 0.5668 0.0186  0.0156  -0.0087 767 HOH A O     
5631 O  O     . HOH J .   ? 0.5072 0.7509 0.6736 0.0185  -0.0075 -0.0476 768 HOH A O     
5632 O  O     . HOH J .   ? 0.5249 0.5381 0.5796 0.0398  -0.0192 -0.0207 769 HOH A O     
5633 O  O     . HOH J .   ? 0.4540 0.4959 0.4505 -0.0814 -0.0172 0.0432  770 HOH A O     
5634 O  O     . HOH J .   ? 0.5831 0.5469 0.5818 -0.0005 -0.0070 0.0241  771 HOH A O     
5635 O  O     . HOH J .   ? 0.5570 0.5533 0.5741 0.0065  0.0137  0.0183  772 HOH A O     
5636 O  O     . HOH J .   ? 0.5160 0.4922 0.5211 0.0006  -0.0061 0.0218  773 HOH A O     
5637 O  O     . HOH J .   ? 0.3849 0.5378 0.5190 0.0033  -0.0749 -0.0003 774 HOH A O     
5638 O  O     . HOH J .   ? 0.6016 0.5908 0.6182 0.0069  -0.0644 0.0351  775 HOH A O     
5639 O  O     . HOH J .   ? 0.4419 0.4232 0.4503 0.0014  0.0034  0.0230  776 HOH A O     
5640 O  O     . HOH J .   ? 0.4405 0.3908 0.4177 -0.0024 -0.0322 0.0074  777 HOH A O     
5641 O  O     . HOH J .   ? 0.6107 0.5581 0.5945 0.0029  -0.0500 0.0442  778 HOH A O     
5642 O  O     . HOH J .   ? 0.6508 0.5720 0.6137 -0.0504 -0.0551 0.0395  779 HOH A O     
5643 O  O     . HOH J .   ? 0.5269 0.6282 0.6215 0.0372  0.0037  -0.0279 780 HOH A O     
5644 O  O     . HOH J .   ? 0.5617 0.4663 0.5090 -0.0710 -0.0843 0.0373  781 HOH A O     
5645 O  O     . HOH J .   ? 0.3269 0.4412 0.4129 -0.0236 -0.0461 0.0155  782 HOH A O     
5646 O  O     . HOH J .   ? 0.6341 0.6194 0.5195 -0.0369 -0.0334 -0.0018 783 HOH A O     
5647 O  O     . HOH J .   ? 0.4923 0.6267 0.5898 -0.0308 -0.0594 0.0146  784 HOH A O     
5648 O  O     . HOH J .   ? 0.4031 0.5335 0.4828 -0.0460 -0.0349 0.0181  785 HOH A O     
5649 O  O     . HOH J .   ? 0.5002 0.4377 0.4933 0.0193  -0.0339 -0.0050 786 HOH A O     
5650 O  O     . HOH J .   ? 0.5687 0.5226 0.5249 -0.0248 -0.0552 0.0150  787 HOH A O     
5651 O  O     . HOH J .   ? 0.5753 0.5927 0.5943 -0.0032 0.0153  0.0174  788 HOH A O     
5652 O  O     . HOH J .   ? 0.5712 0.5073 0.5473 -0.0246 -0.0450 0.0240  789 HOH A O     
5653 O  O     . HOH J .   ? 0.7303 0.6901 0.6927 0.0409  -0.0455 -0.0775 790 HOH A O     
5654 O  O     . HOH J .   ? 0.5400 0.5773 0.5631 -0.0090 0.0177  0.0145  791 HOH A O     
5655 O  O     . HOH J .   ? 0.3926 0.3440 0.3854 -0.0051 -0.0223 0.0217  792 HOH A O     
5656 O  O     . HOH J .   ? 0.4513 0.4367 0.4714 0.0145  0.0076  0.0189  793 HOH A O     
5657 O  O     . HOH J .   ? 0.5099 0.7507 0.6325 -0.0402 0.0051  -0.0171 794 HOH A O     
5658 O  O     . HOH J .   ? 0.7015 0.6748 0.5542 -0.0815 -0.0307 0.0545  795 HOH A O     
5659 O  O     . HOH J .   ? 0.4667 0.5229 0.4965 0.0013  0.0217  -0.0054 796 HOH A O     
5660 O  O     . HOH J .   ? 0.6030 0.6136 0.6486 0.0173  -0.0715 0.0274  797 HOH A O     
5661 O  O     . HOH J .   ? 0.6669 0.6082 0.6501 0.0032  -0.0325 0.0063  798 HOH A O     
5662 O  O     . HOH J .   ? 0.4163 0.3994 0.4283 0.0082  0.0100  0.0224  799 HOH A O     
5663 O  O     . HOH J .   ? 0.5727 0.5545 0.5900 0.0116  -0.0653 0.0354  800 HOH A O     
5664 O  O     . HOH J .   ? 0.4396 0.6012 0.3672 -0.0748 0.0500  -0.0258 801 HOH A O     
5665 O  O     . HOH J .   ? 0.4435 0.4200 0.4737 0.0263  -0.0319 0.0233  802 HOH A O     
5666 O  O     . HOH J .   ? 0.4134 0.4163 0.3263 -0.0263 -0.0135 -0.0035 803 HOH A O     
5667 O  O     . HOH J .   ? 0.6682 0.6256 0.6466 -0.0511 -0.0527 0.0346  804 HOH A O     
5668 O  O     . HOH J .   ? 0.4752 0.4803 0.3782 -0.0362 -0.0125 0.0061  805 HOH A O     
5669 O  O     . HOH J .   ? 0.3664 0.4815 0.4000 -0.0535 0.0170  0.0156  806 HOH A O     
5670 O  O     . HOH J .   ? 0.5211 0.5911 0.6347 0.0550  -0.0525 -0.0136 807 HOH A O     
5671 O  O     . HOH J .   ? 0.5275 0.5259 0.5377 -0.0007 0.0143  0.0188  808 HOH A O     
5672 O  O     . HOH J .   ? 0.4370 0.4099 0.3867 -0.0182 -0.0373 0.0233  809 HOH A O     
5673 O  O     . HOH J .   ? 0.6793 0.7486 0.7948 0.0510  -0.0738 -0.0056 810 HOH A O     
5674 O  O     . HOH J .   ? 0.5189 0.4766 0.4836 -0.0109 -0.0577 0.0458  811 HOH A O     
5675 O  O     . HOH J .   ? 0.4507 0.4541 0.4778 0.0144  0.0073  0.0066  812 HOH A O     
5676 O  O     . HOH J .   ? 0.5486 0.6221 0.6619 0.0499  -0.0579 -0.0089 813 HOH A O     
5677 O  O     . HOH J .   ? 0.6365 0.6567 0.5571 -0.0161 -0.0057 -0.0260 814 HOH A O     
5678 O  O     . HOH J .   ? 0.6574 0.6105 0.6239 -0.0710 -0.0468 0.0480  815 HOH A O     
5679 O  O     . HOH J .   ? 0.6221 0.7796 0.7786 0.0351  -0.0692 -0.0185 816 HOH A O     
5680 O  O     . HOH J .   ? 0.6579 0.6630 0.5419 -0.0469 -0.0163 0.0091  817 HOH A O     
5681 O  O     . HOH J .   ? 0.5169 0.5248 0.4191 -0.0272 -0.0146 -0.0149 818 HOH A O     
5682 O  O     . HOH J .   ? 0.5646 0.5721 0.5434 -0.0897 -0.0318 0.0504  819 HOH A O     
5683 O  O     . HOH J .   ? 0.5337 0.5768 0.5853 -0.0031 -0.0672 0.0260  820 HOH A O     
5684 O  O     . HOH J .   ? 0.6234 0.6841 0.5872 -0.1044 0.0030  0.0454  821 HOH A O     
5685 O  O     . HOH K .   ? 0.5480 0.4727 0.5286 -0.0046 -0.0568 0.0283  501 HOH B O     
5686 O  O     . HOH K .   ? 0.6772 0.6341 0.6430 -0.1062 -0.0335 0.0390  502 HOH B O     
5687 O  O     . HOH K .   ? 0.5454 0.5118 0.5273 -0.0014 0.0070  -0.0062 503 HOH B O     
5688 O  O     . HOH K .   ? 0.4202 0.4533 0.4421 -0.0324 0.0103  0.0156  504 HOH B O     
5689 O  O     . HOH K .   ? 0.5616 0.5661 0.6258 0.0229  -0.0785 -0.0079 505 HOH B O     
5690 O  O     C HOH K .   ? 0.3061 0.2383 0.2886 -0.0283 -0.0131 0.0223  506 HOH B O     
5691 O  O     . HOH K .   ? 0.5422 0.5350 0.5858 0.0390  -0.0043 -0.0080 507 HOH B O     
5692 O  O     . HOH K .   ? 0.5240 0.5358 0.5854 0.0273  -0.0433 -0.0096 508 HOH B O     
5693 O  O     . HOH K .   ? 0.3919 0.3287 0.3795 -0.0061 -0.0679 0.0236  509 HOH B O     
5694 O  O     . HOH K .   ? 0.4954 0.4743 0.5067 0.0050  0.0115  0.0199  510 HOH B O     
5695 O  O     . HOH K .   ? 0.4036 0.6181 0.5277 -0.0387 -0.0023 -0.0366 511 HOH B O     
5696 O  O     . HOH K .   ? 0.5562 0.5787 0.5417 -0.0569 0.0137  0.0317  512 HOH B O     
5697 O  O     . HOH K .   ? 0.6328 0.6056 0.6323 -0.0019 0.0006  0.0234  513 HOH B O     
5698 O  O     . HOH K .   ? 0.5030 0.4778 0.4839 -0.0052 0.0097  -0.0011 514 HOH B O     
5699 O  O     . HOH K .   ? 0.5643 0.5568 0.4943 -0.0417 0.0093  0.0043  515 HOH B O     
5700 O  O     . HOH K .   ? 0.2903 0.4157 0.2691 -0.0348 0.0514  -0.0421 516 HOH B O     
5701 O  O     . HOH K .   ? 0.4707 0.5070 0.5102 0.0018  0.0105  0.0022  517 HOH B O     
5702 O  O     . HOH K .   ? 0.4521 0.3889 0.3836 -0.0366 -0.0240 -0.0058 518 HOH B O     
5703 O  O     . HOH K .   ? 0.4167 0.4345 0.4329 -0.0001 0.0180  0.0115  519 HOH B O     
5704 O  O     . HOH K .   ? 0.4296 0.3718 0.3778 -0.0315 -0.0277 0.0339  520 HOH B O     
5705 O  O     . HOH K .   ? 0.6928 0.7207 0.5635 -0.0440 0.0195  -0.0824 521 HOH B O     
5706 O  O     . HOH K .   ? 0.4906 0.3430 0.4094 -0.1095 -0.0654 0.0507  522 HOH B O     
5707 O  O     . HOH K .   ? 0.5864 0.4618 0.5495 -0.0182 -0.0405 0.0375  523 HOH B O     
5708 O  O     . HOH K .   ? 0.3915 0.3096 0.3742 -0.0126 -0.0161 0.0267  524 HOH B O     
5709 O  O     . HOH K .   ? 0.4631 0.4885 0.4085 -0.0486 0.0214  0.0105  525 HOH B O     
5710 O  O     . HOH K .   ? 0.3805 0.3185 0.3748 -0.0029 -0.0063 0.0227  526 HOH B O     
5711 O  O     . HOH K .   ? 0.4332 0.3978 0.3885 -0.0360 -0.0083 0.0345  527 HOH B O     
5712 O  O     . HOH K .   ? 0.2642 0.3421 0.3438 0.0070  -0.0145 -0.0164 528 HOH B O     
5713 O  O     . HOH K .   ? 0.3455 0.3085 0.2639 -0.0442 -0.0101 0.0084  529 HOH B O     
5714 O  O     . HOH K .   ? 0.4757 0.4399 0.4579 0.0109  0.0048  -0.0282 530 HOH B O     
5715 O  O     . HOH K .   ? 0.4109 0.5125 0.4259 -0.0540 0.0244  0.0150  531 HOH B O     
5716 O  O     . HOH K .   ? 0.2659 0.4331 0.3829 -0.0250 -0.0192 -0.0293 532 HOH B O     
5717 O  O     . HOH K .   ? 0.5011 0.6501 0.5760 -0.0745 -0.0062 -0.0045 533 HOH B O     
5718 O  O     . HOH K .   ? 0.2695 0.2205 0.2508 -0.0084 -0.0020 0.0017  534 HOH B O     
5719 O  O     . HOH K .   ? 0.4115 0.3405 0.4176 0.0383  -0.0186 -0.0327 535 HOH B O     
5720 O  O     . HOH K .   ? 0.2858 0.2082 0.2894 0.0267  -0.0180 -0.0096 536 HOH B O     
5721 O  O     . HOH K .   ? 0.5728 0.5582 0.5970 0.0140  -0.0074 0.0101  537 HOH B O     
5722 O  O     . HOH K .   ? 0.5814 0.5328 0.5586 -0.0452 -0.0323 0.0094  538 HOH B O     
5723 O  O     . HOH K .   ? 0.4309 0.4173 0.4460 0.0087  0.0130  0.0188  539 HOH B O     
5724 O  O     . HOH K .   ? 0.2741 0.3469 0.3109 0.0388  0.0251  -0.0726 540 HOH B O     
5725 O  O     . HOH K .   ? 0.3613 0.3437 0.3043 -0.0245 0.0088  -0.0115 541 HOH B O     
5726 O  O     . HOH K .   ? 0.5919 0.5125 0.5904 0.0115  -0.0706 0.0199  542 HOH B O     
5727 O  O     . HOH K .   ? 0.6370 0.5994 0.5989 -0.0324 -0.0093 0.0354  543 HOH B O     
5728 O  O     . HOH K .   ? 0.5163 0.5390 0.4659 0.0006  0.0214  -0.0744 544 HOH B O     
5729 O  O     . HOH K .   ? 0.4687 0.4419 0.4612 -0.0311 -0.0520 0.0127  545 HOH B O     
5730 O  O     . HOH K .   ? 0.4460 0.5482 0.5256 -0.0011 0.0010  -0.0191 546 HOH B O     
5731 O  O     . HOH K .   ? 0.6805 0.7041 0.6401 -0.1625 -0.0250 0.0525  547 HOH B O     
5732 O  O     . HOH K .   ? 0.5631 0.5873 0.5283 -0.1130 -0.0010 0.0461  548 HOH B O     
5733 O  O     . HOH K .   ? 0.5842 0.6113 0.5764 -0.0234 0.0219  0.0142  549 HOH B O     
5734 O  O     . HOH K .   ? 0.3828 0.2951 0.3553 -0.0279 -0.0225 0.0121  550 HOH B O     
5735 O  O     . HOH K .   ? 0.4609 0.5253 0.5210 0.0329  0.0167  -0.0288 551 HOH B O     
5736 O  O     . HOH K .   ? 0.6123 0.5586 0.5161 -0.0320 -0.0114 -0.0392 552 HOH B O     
5737 O  O     . HOH K .   ? 0.5492 0.5988 0.5890 0.0679  0.0069  -0.1121 553 HOH B O     
5738 O  O     . HOH K .   ? 0.6324 0.5821 0.5984 -0.0924 -0.0284 0.0387  554 HOH B O     
5739 O  O     . HOH K .   ? 0.4297 0.5312 0.5274 0.0115  -0.0206 -0.0265 555 HOH B O     
5740 O  O     . HOH K .   ? 0.4649 0.4620 0.3960 -0.0311 0.0141  -0.0191 556 HOH B O     
5741 O  O     . HOH K .   ? 0.4103 0.6487 0.4607 0.0010  0.0650  -0.1055 557 HOH B O     
5742 O  O     . HOH K .   ? 0.6084 0.6730 0.5170 -0.0524 0.0359  -0.0425 558 HOH B O     
5743 O  O     . HOH K .   ? 0.6631 0.5752 0.6283 -0.0556 -0.0293 0.0281  559 HOH B O     
5744 O  O     . HOH K .   ? 0.3545 0.3036 0.3253 -0.0402 -0.0070 0.0415  560 HOH B O     
5745 O  O     . HOH K .   ? 0.5232 0.5005 0.5176 -0.0644 -0.0274 0.0187  561 HOH B O     
5746 O  O     . HOH K .   ? 0.5724 0.5129 0.5692 0.0033  -0.0091 0.0270  562 HOH B O     
5747 O  O     . HOH K .   ? 0.4734 0.5665 0.5742 0.0166  -0.0320 -0.0271 563 HOH B O     
5748 O  O     . HOH K .   ? 0.2695 0.4132 0.2901 -0.0189 0.0494  -0.0411 564 HOH B O     
5749 O  O     . HOH K .   ? 0.3843 0.4701 0.4329 -0.0629 -0.0087 0.0067  565 HOH B O     
5750 O  O     . HOH K .   ? 0.3504 0.4561 0.3421 -0.0394 0.0427  -0.0136 566 HOH B O     
5751 O  O     . HOH K .   ? 0.4071 0.3917 0.4187 -0.0208 -0.0602 0.0110  567 HOH B O     
5752 O  O     . HOH K .   ? 0.5744 0.7261 0.6210 -0.0966 0.0120  0.0061  568 HOH B O     
5753 O  O     . HOH K .   ? 0.5672 0.5949 0.5309 -0.0965 0.0077  0.0436  569 HOH B O     
5754 O  O     . HOH K .   ? 0.3887 0.5076 0.4607 0.0295  0.0279  -0.0497 570 HOH B O     
5755 O  O     . HOH K .   ? 0.3861 0.2940 0.3720 0.0005  -0.0245 0.0267  571 HOH B O     
5756 O  O     . HOH K .   ? 0.5724 0.6139 0.5863 -0.0198 0.0220  0.0123  572 HOH B O     
5757 O  O     . HOH K .   ? 0.4558 0.4721 0.4841 -0.0352 -0.0382 0.0071  573 HOH B O     
5758 O  O     . HOH K .   ? 0.3044 0.2850 0.2537 -0.0370 0.0024  0.0235  574 HOH B O     
5759 O  O     . HOH K .   ? 0.5271 0.7117 0.5592 -0.1515 0.0088  0.0167  575 HOH B O     
5760 O  O     . HOH K .   ? 0.4435 0.3645 0.3955 -0.0363 -0.0300 -0.0026 576 HOH B O     
5761 O  O     . HOH K .   ? 0.4907 0.5745 0.5682 0.0650  0.0102  -0.0816 577 HOH B O     
5762 O  O     . HOH K .   ? 0.3553 0.3124 0.2871 -0.0384 -0.0151 0.0148  578 HOH B O     
5763 O  O     . HOH K .   ? 0.4073 0.5312 0.4518 0.0363  0.0364  -0.0928 579 HOH B O     
5764 O  O     . HOH K .   ? 0.2767 0.2729 0.2335 -0.0345 0.0114  0.0178  580 HOH B O     
5765 O  O     . HOH K .   ? 0.2774 0.2403 0.2692 -0.0226 0.0014  0.0295  581 HOH B O     
5766 O  O     . HOH K .   ? 0.5092 0.5228 0.4560 -0.0304 0.0212  -0.0100 582 HOH B O     
5767 O  O     . HOH K .   ? 0.2373 0.2356 0.2560 -0.0077 0.0074  0.0151  583 HOH B O     
5768 O  O     . HOH K .   ? 0.4389 0.5687 0.5647 0.0178  -0.0394 -0.0394 584 HOH B O     
5769 O  O     . HOH K .   ? 0.4400 0.4470 0.3810 -0.0382 0.0169  0.0017  585 HOH B O     
5770 O  O     . HOH K .   ? 0.3488 0.3939 0.3702 -0.0267 0.0182  0.0128  586 HOH B O     
5771 O  O     . HOH K .   ? 0.4809 0.5199 0.4929 -0.0228 0.0172  0.0191  587 HOH B O     
5772 O  O     . HOH K .   ? 0.4215 0.6562 0.4176 -0.0329 0.0747  -0.0998 588 HOH B O     
5773 O  O     . HOH K .   ? 0.2563 0.2004 0.2367 -0.0215 -0.0121 0.0075  589 HOH B O     
5774 O  O     . HOH K .   ? 0.2382 0.2340 0.2545 -0.0069 0.0099  0.0168  590 HOH B O     
5775 O  O     . HOH K .   ? 0.4018 0.5025 0.4852 -0.0380 -0.0421 -0.0094 591 HOH B O     
5776 O  O     . HOH K .   ? 0.5005 0.5233 0.4291 -0.0330 0.0237  -0.0316 592 HOH B O     
5777 O  O     . HOH K .   ? 0.3225 0.2802 0.2961 -0.0083 0.0013  -0.0042 593 HOH B O     
5778 O  O     . HOH K .   ? 0.6460 0.5630 0.6076 0.0119  -0.0175 -0.0451 594 HOH B O     
5779 O  O     . HOH K .   ? 0.3356 0.2400 0.3379 0.0282  -0.0297 -0.0034 595 HOH B O     
5780 O  O     . HOH K .   ? 0.5207 0.4171 0.4592 -0.0292 -0.0787 0.0429  596 HOH B O     
5781 O  O     . HOH K .   ? 0.6406 0.5117 0.5886 -0.0126 -0.0390 -0.0208 597 HOH B O     
5782 O  O     . HOH K .   ? 0.3460 0.5146 0.4630 -0.0184 -0.0133 -0.0323 598 HOH B O     
5783 O  O     . HOH K .   ? 0.4133 0.3426 0.4080 0.0210  -0.0115 -0.0181 599 HOH B O     
5784 O  O     . HOH K .   ? 0.2868 0.2358 0.2571 -0.0210 -0.0117 0.0037  600 HOH B O     
5785 O  O     . HOH K .   ? 0.4928 0.4661 0.5300 0.0416  -0.0102 -0.0104 601 HOH B O     
5786 O  O     . HOH K .   ? 0.2727 0.2222 0.2792 0.0124  -0.0018 0.0125  602 HOH B O     
5787 O  O     . HOH K .   ? 0.3620 0.2921 0.3428 0.0022  -0.0084 -0.0090 603 HOH B O     
5788 O  O     . HOH K .   ? 0.6030 0.5894 0.5873 -0.0184 0.0074  0.0248  604 HOH B O     
5789 O  O     . HOH K .   ? 0.3310 0.3749 0.2816 -0.0349 0.0310  -0.0164 605 HOH B O     
5790 O  O     . HOH K .   ? 0.5256 0.5115 0.5268 -0.0035 0.0101  0.0209  606 HOH B O     
5791 O  O     . HOH K .   ? 0.4115 0.3966 0.3912 -0.0056 0.0140  -0.0045 607 HOH B O     
5792 O  O     . HOH K .   ? 0.7317 0.5458 0.6713 -0.0273 -0.0716 0.0389  608 HOH B O     
5793 O  O     . HOH K .   ? 0.3131 0.2590 0.2792 -0.0374 -0.0300 0.0062  609 HOH B O     
5794 O  O     . HOH K .   ? 0.5545 0.4943 0.5933 0.0656  -0.0342 -0.0420 610 HOH B O     
5795 O  O     . HOH K .   ? 0.4124 0.5268 0.4246 -0.0227 0.0435  -0.0243 611 HOH B O     
5796 O  O     . HOH K .   ? 0.4690 0.6498 0.4316 -0.0543 0.0656  -0.0629 612 HOH B O     
5797 O  O     . HOH K .   ? 0.2962 0.2445 0.2886 -0.0156 -0.0029 0.0243  613 HOH B O     
5798 O  O     . HOH K .   ? 0.5949 0.5291 0.6222 0.0272  -0.0992 0.0061  614 HOH B O     
5799 O  O     . HOH K .   ? 0.5029 0.4006 0.4695 -0.0353 -0.0280 0.0275  615 HOH B O     
5800 O  O     C HOH K .   ? 0.3448 0.2598 0.3229 -0.0214 -0.0182 0.0172  616 HOH B O     
5801 O  O     . HOH K .   ? 0.6129 0.5737 0.5960 -0.0702 -0.0250 0.0256  617 HOH B O     
5802 O  O     . HOH K .   ? 0.4047 0.3802 0.4126 0.0043  -0.0003 0.0189  618 HOH B O     
5803 O  O     . HOH K .   ? 0.4807 0.4340 0.4052 -0.0439 -0.0200 0.0222  619 HOH B O     
5804 O  O     . HOH K .   ? 0.3904 0.4133 0.4336 0.0110  -0.0006 0.0006  620 HOH B O     
5805 O  O     . HOH K .   ? 0.4337 0.4177 0.4062 -0.0598 0.0017  0.0406  621 HOH B O     
5806 O  O     . HOH K .   ? 0.2463 0.2254 0.2087 -0.0233 0.0053  0.0143  622 HOH B O     
5807 O  O     . HOH K .   ? 0.2803 0.2566 0.2869 -0.0030 0.0096  0.0222  623 HOH B O     
5808 O  O     . HOH K .   ? 0.3187 0.3265 0.3675 0.0147  -0.0359 -0.0010 624 HOH B O     
5809 O  O     . HOH K .   ? 0.2748 0.2294 0.2399 -0.0299 -0.0306 0.0131  625 HOH B O     
5810 O  O     . HOH K .   ? 0.4516 0.4684 0.4503 -0.0429 0.0126  0.0266  626 HOH B O     
5811 O  O     . HOH K .   ? 0.4279 0.3647 0.4034 -0.0433 -0.0262 0.0118  627 HOH B O     
5812 O  O     . HOH K .   ? 0.5113 0.4802 0.4909 0.0169  0.0042  -0.0452 628 HOH B O     
5813 O  O     . HOH K .   ? 0.3731 0.5542 0.4272 0.0221  0.0499  -0.0969 629 HOH B O     
5814 O  O     . HOH K .   ? 0.5416 0.6369 0.5764 -0.0575 0.0158  0.0084  630 HOH B O     
5815 O  O     . HOH K .   ? 0.3954 0.4402 0.4423 0.0144  0.0139  0.0017  631 HOH B O     
5816 O  O     . HOH K .   ? 0.2750 0.2298 0.2381 -0.0274 -0.0260 0.0145  632 HOH B O     
5817 O  O     . HOH K .   ? 0.4517 0.4330 0.4625 0.0053  0.0114  0.0217  633 HOH B O     
5818 O  O     . HOH K .   ? 0.4258 0.3223 0.3815 -0.0228 -0.0297 -0.0072 634 HOH B O     
5819 O  O     . HOH K .   ? 0.3093 0.4040 0.3660 -0.0281 0.0105  -0.0037 635 HOH B O     
5820 O  O     . HOH K .   ? 0.4683 0.4605 0.4265 -0.1091 -0.0102 0.0498  636 HOH B O     
5821 O  O     . HOH K .   ? 0.5719 0.5822 0.5877 -0.0001 0.0168  0.0158  637 HOH B O     
5822 O  O     . HOH K .   ? 0.3865 0.3010 0.3516 0.0028  -0.0169 -0.0263 638 HOH B O     
5823 O  O     . HOH K .   ? 0.4356 0.3746 0.4075 -0.0399 -0.0274 0.0078  639 HOH B O     
5824 O  O     . HOH K .   ? 0.3489 0.3625 0.2999 -0.0501 0.0147  0.0228  640 HOH B O     
5825 O  O     . HOH K .   ? 0.3343 0.3093 0.3274 -0.0340 -0.0405 0.0112  641 HOH B O     
5826 O  O     . HOH K .   ? 0.4804 0.5531 0.4492 -0.0532 0.0334  0.0055  642 HOH B O     
5827 O  O     . HOH K .   ? 0.6181 0.4701 0.6082 0.0305  -0.0637 0.0052  643 HOH B O     
5828 O  O     . HOH K .   ? 0.5441 0.5263 0.5538 0.0020  0.0118  0.0218  644 HOH B O     
5829 O  O     . HOH K .   ? 0.5936 0.4743 0.5529 -0.0018 -0.0329 -0.0212 645 HOH B O     
5830 O  O     . HOH K .   ? 0.4308 0.5676 0.5112 -0.0274 0.0084  -0.0172 646 HOH B O     
5831 O  O     . HOH K .   ? 0.3000 0.2999 0.3296 0.0120  0.0004  0.0079  647 HOH B O     
5832 O  O     . HOH K .   ? 0.5716 0.6674 0.5864 -0.0875 0.0152  0.0196  648 HOH B O     
5833 O  O     . HOH K .   ? 0.5852 0.5648 0.5587 0.0209  0.0053  -0.0657 649 HOH B O     
5834 O  O     . HOH K .   ? 0.4872 0.6124 0.5080 -0.0237 0.0435  -0.0232 650 HOH B O     
5835 O  O     . HOH K .   ? 0.2492 0.2162 0.2420 0.0068  0.0080  -0.0070 651 HOH B O     
5836 O  O     . HOH K .   ? 0.4243 0.5238 0.5347 0.0156  -0.0464 -0.0294 652 HOH B O     
5837 O  O     . HOH K .   ? 0.3992 0.3846 0.4144 0.0074  0.0085  0.0168  653 HOH B O     
5838 O  O     . HOH K .   ? 0.6515 0.5739 0.6212 -0.0130 -0.0438 0.0343  654 HOH B O     
5839 O  O     . HOH K .   ? 0.4898 0.4353 0.4208 -0.0405 -0.0280 0.0274  655 HOH B O     
5840 O  O     . HOH K .   ? 0.6448 0.4765 0.5605 -0.0888 -0.0668 0.0542  656 HOH B O     
5841 O  O     . HOH K .   ? 0.4385 0.4386 0.4653 0.0192  0.0131  0.0037  657 HOH B O     
5842 O  O     . HOH K .   ? 0.4479 0.4423 0.3565 -0.0306 0.0111  -0.0479 658 HOH B O     
5843 O  O     . HOH K .   ? 0.3320 0.3314 0.3548 0.0141  0.0149  0.0090  659 HOH B O     
5844 O  O     . HOH K .   ? 0.5629 0.4596 0.5343 -0.0031 -0.0245 -0.0074 660 HOH B O     
5845 O  O     . HOH K .   ? 0.4371 0.4597 0.4732 0.0076  0.0083  0.0038  661 HOH B O     
5846 O  O     . HOH K .   ? 0.3125 0.4514 0.4439 0.0019  -0.0571 -0.0350 662 HOH B O     
5847 O  O     . HOH K .   ? 0.6459 0.5489 0.6099 -0.0485 -0.0316 0.0222  663 HOH B O     
5848 O  O     . HOH K .   ? 0.4256 0.4174 0.3971 -0.0026 0.0157  -0.0250 664 HOH B O     
5849 O  O     . HOH K .   ? 0.3820 0.3521 0.3898 0.0040  0.0079  0.0213  665 HOH B O     
5850 O  O     . HOH K .   ? 0.3342 0.2973 0.3318 -0.0159 -0.0023 0.0147  666 HOH B O     
5851 O  O     . HOH K .   ? 0.5247 0.5873 0.5111 -0.1036 0.0096  0.0344  667 HOH B O     
5852 O  O     . HOH K .   ? 0.4751 0.5185 0.5664 0.0349  -0.0600 -0.0243 668 HOH B O     
5853 O  O     . HOH K .   ? 0.3543 0.3859 0.3377 0.0136  0.0241  -0.0630 669 HOH B O     
5854 O  O     . HOH K .   ? 0.5315 0.4931 0.5599 0.0340  -0.0116 0.0018  670 HOH B O     
5855 O  O     . HOH K .   ? 0.5618 0.5014 0.5344 -0.0191 -0.0630 0.0253  671 HOH B O     
5856 O  O     . HOH K .   ? 0.4494 0.4080 0.3198 -0.0672 -0.0183 -0.0009 672 HOH B O     
5857 O  O     . HOH K .   ? 0.6858 0.6313 0.5984 -0.0550 -0.0261 0.0361  673 HOH B O     
5858 O  O     . HOH K .   ? 0.3968 0.3507 0.3507 -0.0318 -0.0156 0.0339  674 HOH B O     
5859 O  O     . HOH K .   ? 0.3766 0.3667 0.3941 0.0076  0.0112  0.0163  675 HOH B O     
5860 O  O     . HOH K .   ? 0.5972 0.6171 0.6876 0.0907  -0.0293 -0.0726 676 HOH B O     
5861 O  O     . HOH K .   ? 0.3410 0.3200 0.3521 0.0069  0.0041  0.0189  677 HOH B O     
5862 O  O     . HOH K .   ? 0.4716 0.4427 0.4495 -0.0195 -0.0018 0.0287  678 HOH B O     
5863 O  O     . HOH K .   ? 0.4734 0.4440 0.4845 0.0072  -0.0132 0.0166  679 HOH B O     
5864 O  O     . HOH K .   ? 0.3763 0.3391 0.3551 -0.0327 -0.0418 0.0128  680 HOH B O     
5865 O  O     . HOH K .   ? 0.6496 0.6656 0.5496 -0.0504 0.0181  -0.0272 681 HOH B O     
5866 O  O     . HOH K .   ? 0.5406 0.6194 0.6318 0.0230  -0.0237 -0.0261 682 HOH B O     
5867 O  O     . HOH K .   ? 0.6343 0.4984 0.6082 0.0052  -0.0426 0.0030  683 HOH B O     
5868 O  O     . HOH K .   ? 0.5536 0.5503 0.6072 0.0309  -0.0426 -0.0078 684 HOH B O     
5869 O  O     . HOH K .   ? 0.3585 0.3597 0.3958 0.0144  -0.0141 0.0038  685 HOH B O     
5870 O  O     . HOH K .   ? 0.4829 0.4374 0.4948 0.0167  -0.0049 0.0173  686 HOH B O     
5871 O  O     . HOH K .   ? 0.6716 0.6100 0.6467 -0.0609 -0.0311 0.0192  687 HOH B O     
5872 O  O     . HOH K .   ? 0.3931 0.3699 0.3849 -0.0175 0.0070  0.0309  688 HOH B O     
5873 O  O     . HOH K .   ? 0.4232 0.3841 0.4108 -0.0563 -0.0211 0.0214  689 HOH B O     
5874 O  O     . HOH K .   ? 0.3305 0.2795 0.3104 0.0028  -0.0002 -0.0135 690 HOH B O     
5875 O  O     . HOH K .   ? 0.4218 0.3398 0.4037 -0.0160 -0.0156 0.0205  691 HOH B O     
5876 O  O     . HOH K .   ? 0.2770 0.2296 0.2578 -0.0223 -0.0126 0.0080  692 HOH B O     
5877 O  O     . HOH K .   ? 0.6551 0.5683 0.6108 -0.0804 -0.0357 0.0375  693 HOH B O     
5878 O  O     . HOH K .   ? 0.6263 0.6912 0.6506 -0.0436 0.0170  0.0126  694 HOH B O     
5879 O  O     . HOH K .   ? 0.5666 0.5082 0.5203 -0.0477 -0.0443 0.0057  695 HOH B O     
5880 O  O     . HOH K .   ? 0.5817 0.6098 0.6095 0.0037  0.0180  0.0101  696 HOH B O     
5881 O  O     . HOH K .   ? 0.4213 0.6653 0.4491 -0.0297 0.0710  -0.0845 697 HOH B O     
5882 O  O     . HOH K .   ? 0.3982 0.4052 0.4576 0.0140  -0.0785 -0.0045 698 HOH B O     
5883 O  O     . HOH K .   ? 0.3019 0.2903 0.3160 0.0241  0.0107  -0.0197 699 HOH B O     
5884 O  O     . HOH K .   ? 0.4109 0.3897 0.3958 -0.0291 0.0060  0.0340  700 HOH B O     
5885 O  O     . HOH K .   ? 0.5294 0.4826 0.4777 -0.0345 -0.0167 0.0334  701 HOH B O     
5886 O  O     . HOH K .   ? 0.3687 0.5319 0.4001 -0.0250 0.0501  -0.0373 702 HOH B O     
5887 O  O     . HOH K .   ? 0.5324 0.5100 0.6046 0.0512  -0.0957 -0.0197 703 HOH B O     
5888 O  O     . HOH K .   ? 0.5361 0.5794 0.6286 0.0911  -0.0190 -0.0869 704 HOH B O     
5889 O  O     . HOH K .   ? 0.5541 0.5877 0.6155 0.0659  -0.0010 -0.0699 705 HOH B O     
5890 O  O     . HOH K .   ? 0.4040 0.2967 0.3670 -0.0215 -0.0295 0.0010  706 HOH B O     
5891 O  O     . HOH K .   ? 0.6115 0.5867 0.6238 0.0073  -0.0062 0.0165  707 HOH B O     
5892 O  O     . HOH K .   ? 0.4012 0.4318 0.3950 -0.0662 0.0103  0.0300  708 HOH B O     
5893 O  O     . HOH K .   ? 0.4391 0.3746 0.3876 -0.0318 -0.0530 0.0279  709 HOH B O     
5894 O  O     . HOH K .   ? 0.4187 0.4172 0.3711 -0.0224 0.0165  -0.0107 710 HOH B O     
5895 O  O     . HOH K .   ? 0.4846 0.4131 0.4176 -0.0397 -0.0401 0.0397  711 HOH B O     
5896 O  O     . HOH K .   ? 0.3268 0.3216 0.3179 -0.0482 0.0049  0.0314  712 HOH B O     
5897 O  O     . HOH K .   ? 0.4023 0.3880 0.3155 -0.0577 0.0015  0.0186  713 HOH B O     
5898 O  O     . HOH K .   ? 0.4915 0.4184 0.4004 -0.0292 -0.0202 -0.0387 714 HOH B O     
5899 O  O     . HOH K .   ? 0.4327 0.4329 0.3955 -0.0066 0.0180  -0.0317 715 HOH B O     
5900 O  O     . HOH K .   ? 0.5707 0.5060 0.5053 -0.0389 -0.0467 0.0280  716 HOH B O     
5901 O  O     . HOH K .   ? 0.3345 0.2698 0.3050 0.0057  -0.0074 -0.0275 717 HOH B O     
5902 O  O     . HOH K .   ? 0.5526 0.4448 0.5155 -0.0399 -0.0316 0.0262  718 HOH B O     
5903 O  O     . HOH K .   ? 0.4778 0.4487 0.3456 -0.0658 -0.0090 -0.0127 719 HOH B O     
5904 O  O     . HOH K .   ? 0.5311 0.5582 0.5851 0.0334  0.0045  -0.0083 720 HOH B O     
5905 O  O     . HOH K .   ? 0.4875 0.5471 0.4764 0.0126  0.0315  -0.0707 721 HOH B O     
5906 O  O     . HOH K .   ? 0.3379 0.3224 0.2857 -0.0256 0.0094  -0.0032 722 HOH B O     
5907 O  O     . HOH K .   ? 0.5685 0.4608 0.5300 -0.0346 -0.0331 0.0099  723 HOH B O     
5908 O  O     . HOH K .   ? 0.6475 0.6284 0.5103 -0.0599 -0.0016 -0.0371 724 HOH B O     
5909 O  O     . HOH K .   ? 0.4466 0.4324 0.4711 0.0190  0.0061  0.0139  725 HOH B O     
5910 O  O     . HOH K .   ? 0.3757 0.3957 0.3752 -0.0366 0.0156  0.0248  726 HOH B O     
5911 O  O     . HOH K .   ? 0.3750 0.4398 0.4051 -0.0747 -0.0078 0.0154  727 HOH B O     
5912 O  O     . HOH K .   ? 0.3647 0.3535 0.3802 0.0065  0.0130  0.0180  728 HOH B O     
5913 O  O     . HOH K .   ? 0.4657 0.4789 0.4561 0.0258  0.0155  -0.0691 729 HOH B O     
5914 O  O     . HOH K .   ? 0.4630 0.4872 0.5131 -0.0101 -0.0561 0.0003  730 HOH B O     
5915 O  O     . HOH K .   ? 0.6777 0.6198 0.5640 -0.0429 -0.0173 -0.0379 731 HOH B O     
5916 O  O     . HOH K .   ? 0.2951 0.3319 0.2975 -0.0098 0.0274  -0.0007 732 HOH B O     
5917 O  O     . HOH K .   ? 0.3788 0.4766 0.4090 -0.0709 0.0137  0.0122  733 HOH B O     
5918 O  O     . HOH K .   ? 0.3808 0.3802 0.4288 0.0162  -0.0493 -0.0007 734 HOH B O     
5919 O  O     . HOH K .   ? 0.5279 0.5950 0.4741 -0.0606 0.0336  0.0018  735 HOH B O     
5920 O  O     . HOH K .   ? 0.6178 0.6403 0.5562 -0.1217 0.0031  0.0551  736 HOH B O     
5921 O  O     . HOH K .   ? 0.3975 0.3472 0.3991 -0.0022 -0.0704 0.0182  737 HOH B O     
5922 O  O     . HOH K .   ? 0.4832 0.5521 0.5853 0.0254  -0.0604 -0.0262 738 HOH B O     
5923 O  O     . HOH K .   ? 0.6699 0.5085 0.6434 0.0131  -0.0667 0.0199  739 HOH B O     
5924 O  O     . HOH K .   ? 0.6242 0.5026 0.5666 -0.0105 -0.0361 -0.0306 740 HOH B O     
5925 O  O     . HOH K .   ? 0.5032 0.4818 0.5259 0.0195  0.0000  0.0175  741 HOH B O     
5926 O  O     . HOH K .   ? 0.6275 0.6415 0.7034 0.0412  -0.0584 -0.0204 742 HOH B O     
5927 O  O     . HOH K .   ? 0.6603 0.6883 0.6693 -0.0110 0.0216  0.0121  743 HOH B O     
5928 O  O     . HOH K .   ? 0.2734 0.2148 0.2554 -0.0033 -0.0040 -0.0027 744 HOH B O     
5929 O  O     . HOH K .   ? 0.4426 0.5161 0.5300 0.0157  -0.0281 -0.0204 745 HOH B O     
5930 O  O     . HOH K .   ? 0.4353 0.4874 0.5087 -0.0041 -0.0563 -0.0086 746 HOH B O     
5931 O  O     . HOH K .   ? 0.5343 0.4410 0.5151 -0.0007 -0.0912 0.0279  747 HOH B O     
5932 O  O     . HOH K .   ? 0.3890 0.3578 0.3962 0.0039  -0.0149 0.0178  748 HOH B O     
5933 O  O     . HOH K .   ? 0.2806 0.2275 0.2561 -0.0044 -0.0021 -0.0079 749 HOH B O     
5934 O  O     . HOH K .   ? 0.5408 0.5348 0.5601 0.0104  0.0137  0.0166  750 HOH B O     
5935 O  O     . HOH K .   ? 0.2555 0.2233 0.2380 0.0041  0.0076  -0.0159 751 HOH B O     
5936 O  O     . HOH K .   ? 0.4951 0.5836 0.5676 0.0030  0.0029  -0.0166 752 HOH B O     
5937 O  O     . HOH K .   ? 0.6051 0.6489 0.6158 -0.0422 0.0174  0.0191  753 HOH B O     
5938 O  O     . HOH K .   ? 0.6899 0.5838 0.6322 -0.0245 -0.0326 -0.0177 754 HOH B O     
5939 O  O     . HOH K .   ? 0.6161 0.6486 0.5553 -0.0393 0.0268  -0.0138 755 HOH B O     
5940 O  O     . HOH K .   ? 0.6873 0.6599 0.5998 -0.0600 -0.0071 0.0289  756 HOH B O     
5941 O  O     . HOH K .   ? 0.3661 0.4899 0.3526 -0.0435 0.0482  -0.0233 757 HOH B O     
5942 O  O     . HOH K .   ? 0.3995 0.4213 0.4615 0.0179  -0.0424 -0.0073 758 HOH B O     
5943 O  O     . HOH K .   ? 0.6172 0.5420 0.6264 0.0183  -0.0791 0.0145  759 HOH B O     
5944 O  O     . HOH K .   ? 0.3109 0.2662 0.2949 -0.0027 0.0020  -0.0016 760 HOH B O     
5945 O  O     . HOH K .   ? 0.5131 0.4594 0.4510 -0.0443 -0.0220 0.0406  761 HOH B O     
5946 O  O     . HOH K .   ? 0.5664 0.6136 0.6472 0.0073  -0.0711 -0.0125 762 HOH B O     
5947 O  O     . HOH K .   ? 0.6293 0.5679 0.5648 -0.0399 -0.0459 0.0236  763 HOH B O     
5948 O  O     . HOH K .   ? 0.4654 0.5550 0.5176 0.0525  0.0224  -0.0916 764 HOH B O     
5949 O  O     . HOH K .   ? 0.4777 0.6037 0.4186 -0.0676 0.0517  -0.0284 765 HOH B O     
5950 O  O     . HOH K .   ? 0.4978 0.4817 0.5188 0.0166  0.0089  0.0138  766 HOH B O     
5951 O  O     . HOH K .   ? 0.5818 0.5472 0.4973 -0.0493 -0.0099 0.0167  767 HOH B O     
5952 O  O     . HOH K .   ? 0.5747 0.5686 0.5575 -0.0343 0.0102  0.0333  768 HOH B O     
5953 O  O     . HOH K .   ? 0.5980 0.6055 0.5078 -0.0680 0.0105  0.0180  769 HOH B O     
5954 O  O     . HOH K .   ? 0.2904 0.5298 0.4333 -0.0473 -0.0160 -0.0408 770 HOH B O     
5955 O  O     . HOH K .   ? 0.5778 0.7032 0.6252 -0.0706 0.0126  0.0039  771 HOH B O     
5956 O  O     . HOH K .   ? 0.5535 0.5294 0.5643 0.0070  -0.0010 0.0180  772 HOH B O     
5957 O  O     . HOH K .   ? 0.4053 0.3413 0.3693 -0.0377 -0.0284 0.0042  773 HOH B O     
5958 O  O     . HOH K .   ? 0.5293 0.5270 0.5316 -0.0715 -0.0232 0.0208  774 HOH B O     
5959 O  O     . HOH K .   ? 0.6789 0.8449 0.7240 0.0296  0.0470  -0.1081 775 HOH B O     
5960 O  O     . HOH K .   ? 0.6185 0.5198 0.5979 -0.0016 -0.0221 0.0026  776 HOH B O     
5961 O  O     . HOH K .   ? 0.6267 0.6663 0.6116 -0.0375 0.0226  0.0172  777 HOH B O     
5962 O  O     . HOH K .   ? 0.4488 0.4368 0.4618 0.0063  0.0130  0.0202  778 HOH B O     
5963 O  O     . HOH K .   ? 0.4664 0.4584 0.4867 0.0106  0.0083  0.0136  779 HOH B O     
5964 O  O     . HOH K .   ? 0.6726 0.5799 0.6464 0.0057  -0.0196 -0.0179 780 HOH B O     
5965 O  O     . HOH K .   ? 0.3561 0.3629 0.3088 -0.0177 0.0200  -0.0245 781 HOH B O     
5966 O  O     . HOH K .   ? 0.5295 0.4137 0.4855 -0.0237 -0.0344 -0.0036 782 HOH B O     
5967 O  O     . HOH K .   ? 0.4838 0.3841 0.4576 -0.0206 -0.0244 0.0201  783 HOH B O     
5968 O  O     . HOH K .   ? 0.5706 0.4646 0.5371 -0.0285 -0.0295 0.0133  784 HOH B O     
5969 O  O     . HOH K .   ? 0.5819 0.5588 0.4936 -0.0534 -0.0027 0.0145  785 HOH B O     
5970 O  O     . HOH K .   ? 0.5911 0.7175 0.6665 -0.0208 0.0112  -0.0168 786 HOH B O     
5971 O  O     . HOH K .   ? 0.6443 0.5590 0.6284 0.0121  -0.0164 -0.0147 787 HOH B O     
5972 O  O     . HOH K .   ? 0.6663 0.5692 0.6579 0.0245  -0.0256 -0.0187 788 HOH B O     
5973 O  O     . HOH K .   ? 0.4055 0.4916 0.4539 -0.0703 -0.0146 0.0075  789 HOH B O     
5974 O  O     . HOH K .   ? 0.4539 0.4378 0.4710 0.0105  0.0037  0.0152  790 HOH B O     
5975 O  O     . HOH K .   ? 0.5195 0.5357 0.5579 0.0134  0.0021  0.0019  791 HOH B O     
5976 O  O     . HOH K .   ? 0.6880 0.6839 0.6216 -0.0357 0.0126  -0.0054 792 HOH B O     
5977 O  O     . HOH K .   ? 0.4023 0.5251 0.4669 -0.0641 -0.0036 -0.0008 793 HOH B O     
5978 O  O     . HOH K .   ? 0.6483 0.5360 0.6133 -0.0155 -0.0301 0.0002  794 HOH B O     
5979 O  O     . HOH K .   ? 0.4581 0.4236 0.3600 -0.0558 -0.0112 0.0133  795 HOH B O     
5980 O  O     . HOH K .   ? 0.3748 0.5278 0.3783 -0.0367 0.0535  -0.0371 796 HOH B O     
5981 O  O     . HOH K .   ? 0.5653 0.5178 0.5093 -0.1061 -0.0214 0.0557  797 HOH B O     
5982 O  O     . HOH K .   ? 0.7125 0.6293 0.6448 -0.1073 -0.0349 0.0593  798 HOH B O     
5983 O  O     . HOH K .   ? 0.4577 0.4171 0.4307 -0.0343 -0.0024 0.0407  799 HOH B O     
5984 O  O     . HOH K .   ? 0.5109 0.5050 0.5404 0.0163  -0.0041 0.0066  800 HOH B O     
5985 O  O     . HOH K .   ? 0.4485 0.3878 0.4131 -0.0397 -0.0115 0.0450  801 HOH B O     
5986 O  O     . HOH K .   ? 0.6146 0.5515 0.5927 0.0072  -0.0059 -0.0207 802 HOH B O     
5987 O  O     . HOH K .   ? 0.4559 0.4999 0.5388 0.0286  -0.0456 -0.0198 803 HOH B O     
5988 O  O     . HOH K .   ? 0.3917 0.5405 0.3540 -0.0552 0.0573  -0.0419 804 HOH B O     
5989 O  O     . HOH K .   ? 0.5602 0.5801 0.5869 -0.0468 -0.0398 0.0078  805 HOH B O     
5990 O  O     . HOH K .   ? 0.4391 0.4090 0.4538 0.0088  -0.0229 0.0144  806 HOH B O     
5991 O  O     . HOH K .   ? 0.4254 0.4264 0.4097 -0.0569 0.0063  0.0347  807 HOH B O     
5992 O  O     . HOH K .   ? 0.4689 0.4518 0.4982 0.0162  -0.0233 0.0070  808 HOH B O     
5993 O  O     . HOH K .   ? 0.3686 0.3725 0.3098 -0.0494 0.0118  0.0206  809 HOH B O     
5994 O  O     . HOH K .   ? 0.5702 0.5451 0.5853 0.0129  0.0065  0.0190  810 HOH B O     
5995 O  O     . HOH K .   ? 0.5184 0.5654 0.5385 -0.0193 0.0214  0.0099  811 HOH B O     
5996 O  O     . HOH K .   ? 0.5038 0.4879 0.4344 -0.0530 0.0011  0.0276  812 HOH B O     
5997 O  O     . HOH K .   ? 0.6421 0.5617 0.6089 -0.0504 -0.0327 0.0131  813 HOH B O     
5998 O  O     . HOH K .   ? 0.5708 0.5230 0.5011 -0.0493 -0.0186 0.0389  814 HOH B O     
5999 O  O     . HOH K .   ? 0.5270 0.5937 0.5608 -0.0196 0.0205  0.0030  815 HOH B O     
6000 O  O     . HOH K .   ? 0.6341 0.5610 0.5679 -0.0427 -0.0368 0.0446  816 HOH B O     
6001 O  O     . HOH K .   ? 0.5354 0.5048 0.5235 -0.0109 -0.0021 0.0268  817 HOH B O     
6002 O  O     . HOH K .   ? 0.4095 0.4865 0.4778 0.0411  0.0163  -0.0433 818 HOH B O     
6003 O  O     . HOH K .   ? 0.5363 0.7927 0.5509 -0.0157 0.0763  -0.1233 819 HOH B O     
6004 O  O     . HOH K .   ? 0.5083 0.7053 0.6483 -0.0064 -0.0179 -0.0471 820 HOH B O     
6005 O  O     . HOH K .   ? 0.6485 0.5710 0.5951 -0.0542 -0.0214 0.0542  821 HOH B O     
6006 O  O     . HOH K .   ? 0.5179 0.5026 0.5581 0.0247  -0.0362 0.0000  822 HOH B O     
6007 O  O     . HOH K .   ? 0.5430 0.6024 0.6153 0.0496  0.0068  -0.0414 823 HOH B O     
6008 O  O     . HOH K .   ? 0.6134 0.5106 0.5683 -0.0344 -0.0338 -0.0003 824 HOH B O     
6009 O  O     . HOH K .   ? 0.5335 0.5702 0.5472 -0.0271 0.0190  0.0162  825 HOH B O     
6010 O  O     . HOH K .   ? 0.7193 0.6921 0.6855 -0.0444 0.0010  0.0428  826 HOH B O     
6011 O  O     . HOH K .   ? 0.4778 0.6462 0.4363 -0.0705 0.0607  -0.0372 827 HOH B O     
6012 O  O     . HOH K .   ? 0.4200 0.4217 0.5090 0.0500  -0.1047 -0.0247 828 HOH B O     
6013 O  O     . HOH K .   ? 0.6387 0.8493 0.6635 -0.0370 0.0627  -0.0567 829 HOH B O     
6014 O  O     . HOH K .   ? 0.4573 0.6058 0.5379 0.0490  0.0310  -0.0934 830 HOH B O     
6015 O  O     . HOH K .   ? 0.2043 0.4603 0.3560 -0.0548 -0.0214 -0.0428 831 HOH B O     
6016 O  O     . HOH K .   ? 0.6615 0.6392 0.5482 -0.0656 -0.0050 0.0088  832 HOH B O     
6017 O  O     . HOH K .   ? 0.7562 0.8276 0.6340 -0.0372 0.0335  -0.1103 833 HOH B O     
# 
