data_9QYH
# 
_entry.id   9QYH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9QYH         pdb_00009qyh 10.2210/pdb9qyh/pdb 
WWPDB D_1292147234 ?            ?                   
# 
_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       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9QYH 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-17 
_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                 3 
_pdbx_contact_author.email              G.A.Spyroulias@upatras.gr 
_pdbx_contact_author.name_first         Georgios 
_pdbx_contact_author.name_last          Spyroulias 
_pdbx_contact_author.name_mi            A. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1799-3312 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fourkiotis, K.N.' 1 0000-0002-5197-4142 
'Chikunova, A.'    2 0000-0002-2818-0539 
'Tsika, C.A.'      3 0000-0002-3723-0606 
'Kravvariti, P.K.' 4 0000-0001-7127-1666 
'Tsatsouli, A.S.'  5 ?                   
'Perrakis, A.'     6 0000-0002-1151-6227 
'Spyroulias, A.G.' 7 0000-0003-1799-3312 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Comparative analysis of hPARP9 macro domains' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_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 'Fourkiotis, K.N.' 1 0000-0002-5197-4142 
primary 'Chikunova, A.'    2 0000-0002-2818-0539 
primary 'Tsika, C.A.'      3 0000-0002-3723-0606 
primary 'Kravvariti, P.K.' 4 0000-0001-7127-1666 
primary 'Tsatsouli, A.S.'  5 ?                   
primary 'Perrakis, A.'     6 0000-0002-1151-6227 
primary 'Spyroulias, A.G.' 7 0000-0003-1799-3312 
# 
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 'Protein mono-ADP-ribosyltransferase PARP9' 22232.867 2  2.4.2.- ? ? ? 
2 non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE           663.425   2  ?       ? ? ? 
3 water       nat water                                       18.015    13 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'ADP-ribosyltransferase diphtheria toxin-like 9,ARTD9,B aggressive lymphoma protein,Poly [ADP-ribose] polymerase 9,PARP-9' 
# 
_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       
;GAMATTPSFNAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLV
TKGFNLFCKYIYHVLWHSEFPKPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKH
QLTVKFVIFPTDLEIYKAFSSEMAKRSKMLSLNNYSV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMATTPSFNAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLV
TKGFNLFCKYIYHVLWHSEFPKPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKH
QLTVKFVIFPTDLEIYKAFSSEMAKRSKMLSLNNYSV
;
_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 NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD 
3 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   ALA n 
1 5   THR n 
1 6   THR n 
1 7   PRO n 
1 8   SER n 
1 9   PHE n 
1 10  ASN n 
1 11  ALA n 
1 12  MET n 
1 13  VAL n 
1 14  VAL n 
1 15  ASN n 
1 16  ASN n 
1 17  LEU n 
1 18  THR n 
1 19  LEU n 
1 20  GLN n 
1 21  ILE n 
1 22  VAL n 
1 23  GLN n 
1 24  GLY n 
1 25  HIS n 
1 26  ILE n 
1 27  GLU n 
1 28  TRP n 
1 29  GLN n 
1 30  THR n 
1 31  ALA n 
1 32  ASP n 
1 33  VAL n 
1 34  ILE n 
1 35  VAL n 
1 36  ASN n 
1 37  SER n 
1 38  VAL n 
1 39  ASN n 
1 40  PRO n 
1 41  HIS n 
1 42  ASP n 
1 43  ILE n 
1 44  THR n 
1 45  VAL n 
1 46  GLY n 
1 47  PRO n 
1 48  VAL n 
1 49  ALA n 
1 50  LYS n 
1 51  SER n 
1 52  ILE n 
1 53  LEU n 
1 54  GLN n 
1 55  GLN n 
1 56  ALA n 
1 57  GLY n 
1 58  VAL n 
1 59  GLU n 
1 60  MET n 
1 61  LYS n 
1 62  SER n 
1 63  GLU n 
1 64  PHE n 
1 65  LEU n 
1 66  ALA n 
1 67  THR n 
1 68  LYS n 
1 69  ALA n 
1 70  LYS n 
1 71  GLN n 
1 72  PHE n 
1 73  GLN n 
1 74  ARG n 
1 75  SER n 
1 76  GLN n 
1 77  LEU n 
1 78  VAL n 
1 79  LEU n 
1 80  VAL n 
1 81  THR n 
1 82  LYS n 
1 83  GLY n 
1 84  PHE n 
1 85  ASN n 
1 86  LEU n 
1 87  PHE n 
1 88  CYS n 
1 89  LYS n 
1 90  TYR n 
1 91  ILE n 
1 92  TYR n 
1 93  HIS n 
1 94  VAL n 
1 95  LEU n 
1 96  TRP n 
1 97  HIS n 
1 98  SER n 
1 99  GLU n 
1 100 PHE n 
1 101 PRO n 
1 102 LYS n 
1 103 PRO n 
1 104 GLN n 
1 105 ILE n 
1 106 LEU n 
1 107 LYS n 
1 108 HIS n 
1 109 ALA n 
1 110 MET n 
1 111 LYS n 
1 112 GLU n 
1 113 CYS n 
1 114 LEU n 
1 115 GLU n 
1 116 LYS n 
1 117 CYS n 
1 118 ILE n 
1 119 GLU n 
1 120 GLN n 
1 121 ASN n 
1 122 ILE n 
1 123 THR n 
1 124 SER n 
1 125 ILE n 
1 126 SER n 
1 127 PHE n 
1 128 PRO n 
1 129 ALA n 
1 130 LEU n 
1 131 GLY n 
1 132 THR n 
1 133 GLY n 
1 134 ASN n 
1 135 MET n 
1 136 GLU n 
1 137 ILE n 
1 138 LYS n 
1 139 LYS n 
1 140 GLU n 
1 141 THR n 
1 142 ALA n 
1 143 ALA n 
1 144 GLU n 
1 145 ILE n 
1 146 LEU n 
1 147 PHE n 
1 148 ASP n 
1 149 GLU n 
1 150 VAL n 
1 151 LEU n 
1 152 THR n 
1 153 PHE n 
1 154 ALA n 
1 155 LYS n 
1 156 ASP n 
1 157 HIS n 
1 158 VAL n 
1 159 LYS n 
1 160 HIS n 
1 161 GLN n 
1 162 LEU n 
1 163 THR n 
1 164 VAL n 
1 165 LYS n 
1 166 PHE n 
1 167 VAL n 
1 168 ILE n 
1 169 PHE n 
1 170 PRO n 
1 171 THR n 
1 172 ASP n 
1 173 LEU n 
1 174 GLU n 
1 175 ILE n 
1 176 TYR n 
1 177 LYS n 
1 178 ALA n 
1 179 PHE n 
1 180 SER n 
1 181 SER n 
1 182 GLU n 
1 183 MET n 
1 184 ALA n 
1 185 LYS n 
1 186 ARG n 
1 187 SER n 
1 188 LYS n 
1 189 MET n 
1 190 LEU n 
1 191 SER n 
1 192 LEU n 
1 193 ASN n 
1 194 ASN n 
1 195 TYR n 
1 196 SER n 
1 197 VAL 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                   197 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PARP9, BAL, BAL1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                           ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                          ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                          ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                         ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                           ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                         ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                             ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                        ? 'C6 H13 N O2'       131.173 
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 
NAD non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE ? 'C21 H27 N7 O14 P2' 663.425 
PHE 'L-peptide linking' y PHENYLALANINE                     ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                           ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                            ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                         ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                          ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                            ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   301 ?   ?   ?   A . n 
A 1 2   ALA 2   302 ?   ?   ?   A . n 
A 1 3   MET 3   303 ?   ?   ?   A . n 
A 1 4   ALA 4   304 ?   ?   ?   A . n 
A 1 5   THR 5   305 ?   ?   ?   A . n 
A 1 6   THR 6   306 ?   ?   ?   A . n 
A 1 7   PRO 7   307 ?   ?   ?   A . n 
A 1 8   SER 8   308 ?   ?   ?   A . n 
A 1 9   PHE 9   309 ?   ?   ?   A . n 
A 1 10  ASN 10  310 310 ASN ASN A . n 
A 1 11  ALA 11  311 311 ALA ALA A . n 
A 1 12  MET 12  312 312 MET MET A . n 
A 1 13  VAL 13  313 313 VAL VAL A . n 
A 1 14  VAL 14  314 314 VAL VAL A . n 
A 1 15  ASN 15  315 315 ASN ASN A . n 
A 1 16  ASN 16  316 316 ASN ASN A . n 
A 1 17  LEU 17  317 317 LEU LEU A . n 
A 1 18  THR 18  318 318 THR THR A . n 
A 1 19  LEU 19  319 319 LEU LEU A . n 
A 1 20  GLN 20  320 320 GLN GLN A . n 
A 1 21  ILE 21  321 321 ILE ILE A . n 
A 1 22  VAL 22  322 322 VAL VAL A . n 
A 1 23  GLN 23  323 323 GLN GLN A . n 
A 1 24  GLY 24  324 324 GLY GLY A . n 
A 1 25  HIS 25  325 325 HIS HIS A . n 
A 1 26  ILE 26  326 326 ILE ILE A . n 
A 1 27  GLU 27  327 327 GLU GLU A . n 
A 1 28  TRP 28  328 328 TRP TRP A . n 
A 1 29  GLN 29  329 329 GLN GLN A . n 
A 1 30  THR 30  330 330 THR THR A . n 
A 1 31  ALA 31  331 331 ALA ALA A . n 
A 1 32  ASP 32  332 332 ASP ASP A . n 
A 1 33  VAL 33  333 333 VAL VAL A . n 
A 1 34  ILE 34  334 334 ILE ILE A . n 
A 1 35  VAL 35  335 335 VAL VAL A . n 
A 1 36  ASN 36  336 336 ASN ASN A . n 
A 1 37  SER 37  337 337 SER SER A . n 
A 1 38  VAL 38  338 338 VAL VAL A . n 
A 1 39  ASN 39  339 339 ASN ASN A . n 
A 1 40  PRO 40  340 340 PRO PRO A . n 
A 1 41  HIS 41  341 341 HIS HIS A . n 
A 1 42  ASP 42  342 342 ASP ASP A . n 
A 1 43  ILE 43  343 343 ILE ILE A . n 
A 1 44  THR 44  344 344 THR THR A . n 
A 1 45  VAL 45  345 345 VAL VAL A . n 
A 1 46  GLY 46  346 346 GLY GLY A . n 
A 1 47  PRO 47  347 347 PRO PRO A . n 
A 1 48  VAL 48  348 348 VAL VAL A . n 
A 1 49  ALA 49  349 349 ALA ALA A . n 
A 1 50  LYS 50  350 350 LYS LYS A . n 
A 1 51  SER 51  351 351 SER SER A . n 
A 1 52  ILE 52  352 352 ILE ILE A . n 
A 1 53  LEU 53  353 353 LEU LEU A . n 
A 1 54  GLN 54  354 354 GLN GLN A . n 
A 1 55  GLN 55  355 355 GLN GLN A . n 
A 1 56  ALA 56  356 356 ALA ALA A . n 
A 1 57  GLY 57  357 357 GLY GLY A . n 
A 1 58  VAL 58  358 358 VAL VAL A . n 
A 1 59  GLU 59  359 359 GLU GLU A . n 
A 1 60  MET 60  360 360 MET MET A . n 
A 1 61  LYS 61  361 361 LYS LYS A . n 
A 1 62  SER 62  362 362 SER SER A . n 
A 1 63  GLU 63  363 363 GLU GLU A . n 
A 1 64  PHE 64  364 364 PHE PHE A . n 
A 1 65  LEU 65  365 365 LEU LEU A . n 
A 1 66  ALA 66  366 366 ALA ALA A . n 
A 1 67  THR 67  367 367 THR THR A . n 
A 1 68  LYS 68  368 368 LYS LYS A . n 
A 1 69  ALA 69  369 369 ALA ALA A . n 
A 1 70  LYS 70  370 ?   ?   ?   A . n 
A 1 71  GLN 71  371 ?   ?   ?   A . n 
A 1 72  PHE 72  372 ?   ?   ?   A . n 
A 1 73  GLN 73  373 ?   ?   ?   A . n 
A 1 74  ARG 74  374 374 ARG ARG A . n 
A 1 75  SER 75  375 375 SER SER A . n 
A 1 76  GLN 76  376 376 GLN GLN A . n 
A 1 77  LEU 77  377 377 LEU LEU A . n 
A 1 78  VAL 78  378 378 VAL VAL A . n 
A 1 79  LEU 79  379 379 LEU LEU A . n 
A 1 80  VAL 80  380 380 VAL VAL A . n 
A 1 81  THR 81  381 381 THR THR A . n 
A 1 82  LYS 82  382 382 LYS LYS A . n 
A 1 83  GLY 83  383 383 GLY GLY A . n 
A 1 84  PHE 84  384 384 PHE PHE A . n 
A 1 85  ASN 85  385 385 ASN ASN A . n 
A 1 86  LEU 86  386 386 LEU LEU A . n 
A 1 87  PHE 87  387 387 PHE PHE A . n 
A 1 88  CYS 88  388 388 CYS CYS A . n 
A 1 89  LYS 89  389 389 LYS LYS A . n 
A 1 90  TYR 90  390 390 TYR TYR A . n 
A 1 91  ILE 91  391 391 ILE ILE A . n 
A 1 92  TYR 92  392 392 TYR TYR A . n 
A 1 93  HIS 93  393 393 HIS HIS A . n 
A 1 94  VAL 94  394 394 VAL VAL A . n 
A 1 95  LEU 95  395 395 LEU LEU A . n 
A 1 96  TRP 96  396 396 TRP TRP A . n 
A 1 97  HIS 97  397 397 HIS HIS A . n 
A 1 98  SER 98  398 398 SER SER A . n 
A 1 99  GLU 99  399 399 GLU GLU A . n 
A 1 100 PHE 100 400 400 PHE PHE A . n 
A 1 101 PRO 101 401 401 PRO PRO A . n 
A 1 102 LYS 102 402 402 LYS LYS A . n 
A 1 103 PRO 103 403 403 PRO PRO A . n 
A 1 104 GLN 104 404 404 GLN GLN A . n 
A 1 105 ILE 105 405 405 ILE ILE A . n 
A 1 106 LEU 106 406 406 LEU LEU A . n 
A 1 107 LYS 107 407 407 LYS LYS A . n 
A 1 108 HIS 108 408 408 HIS HIS A . n 
A 1 109 ALA 109 409 409 ALA ALA A . n 
A 1 110 MET 110 410 410 MET MET A . n 
A 1 111 LYS 111 411 411 LYS LYS A . n 
A 1 112 GLU 112 412 412 GLU GLU A . n 
A 1 113 CYS 113 413 413 CYS CYS A . n 
A 1 114 LEU 114 414 414 LEU LEU A . n 
A 1 115 GLU 115 415 415 GLU GLU A . n 
A 1 116 LYS 116 416 416 LYS LYS A . n 
A 1 117 CYS 117 417 417 CYS CYS A . n 
A 1 118 ILE 118 418 418 ILE ILE A . n 
A 1 119 GLU 119 419 419 GLU GLU A . n 
A 1 120 GLN 120 420 420 GLN GLN A . n 
A 1 121 ASN 121 421 421 ASN ASN A . n 
A 1 122 ILE 122 422 422 ILE ILE A . n 
A 1 123 THR 123 423 423 THR THR A . n 
A 1 124 SER 124 424 424 SER SER A . n 
A 1 125 ILE 125 425 425 ILE ILE A . n 
A 1 126 SER 126 426 426 SER SER A . n 
A 1 127 PHE 127 427 427 PHE PHE A . n 
A 1 128 PRO 128 428 428 PRO PRO A . n 
A 1 129 ALA 129 429 429 ALA ALA A . n 
A 1 130 LEU 130 430 430 LEU LEU A . n 
A 1 131 GLY 131 431 431 GLY GLY A . n 
A 1 132 THR 132 432 432 THR THR A . n 
A 1 133 GLY 133 433 433 GLY GLY A . n 
A 1 134 ASN 134 434 434 ASN ASN A . n 
A 1 135 MET 135 435 435 MET MET A . n 
A 1 136 GLU 136 436 436 GLU GLU A . n 
A 1 137 ILE 137 437 437 ILE ILE A . n 
A 1 138 LYS 138 438 438 LYS LYS A . n 
A 1 139 LYS 139 439 439 LYS LYS A . n 
A 1 140 GLU 140 440 440 GLU GLU A . n 
A 1 141 THR 141 441 441 THR THR A . n 
A 1 142 ALA 142 442 442 ALA ALA A . n 
A 1 143 ALA 143 443 443 ALA ALA A . n 
A 1 144 GLU 144 444 444 GLU GLU A . n 
A 1 145 ILE 145 445 445 ILE ILE A . n 
A 1 146 LEU 146 446 446 LEU LEU A . n 
A 1 147 PHE 147 447 447 PHE PHE A . n 
A 1 148 ASP 148 448 448 ASP ASP A . n 
A 1 149 GLU 149 449 449 GLU GLU A . n 
A 1 150 VAL 150 450 450 VAL VAL A . n 
A 1 151 LEU 151 451 451 LEU LEU A . n 
A 1 152 THR 152 452 452 THR THR A . n 
A 1 153 PHE 153 453 453 PHE PHE A . n 
A 1 154 ALA 154 454 454 ALA ALA A . n 
A 1 155 LYS 155 455 455 LYS LYS A . n 
A 1 156 ASP 156 456 456 ASP ASP A . n 
A 1 157 HIS 157 457 457 HIS HIS A . n 
A 1 158 VAL 158 458 458 VAL VAL A . n 
A 1 159 LYS 159 459 459 LYS LYS A . n 
A 1 160 HIS 160 460 460 HIS HIS A . n 
A 1 161 GLN 161 461 461 GLN GLN A . n 
A 1 162 LEU 162 462 462 LEU LEU A . n 
A 1 163 THR 163 463 463 THR THR A . n 
A 1 164 VAL 164 464 464 VAL VAL A . n 
A 1 165 LYS 165 465 465 LYS LYS A . n 
A 1 166 PHE 166 466 466 PHE PHE A . n 
A 1 167 VAL 167 467 467 VAL VAL A . n 
A 1 168 ILE 168 468 468 ILE ILE A . n 
A 1 169 PHE 169 469 469 PHE PHE A . n 
A 1 170 PRO 170 470 470 PRO PRO A . n 
A 1 171 THR 171 471 471 THR THR A . n 
A 1 172 ASP 172 472 472 ASP ASP A . n 
A 1 173 LEU 173 473 473 LEU LEU A . n 
A 1 174 GLU 174 474 474 GLU GLU A . n 
A 1 175 ILE 175 475 475 ILE ILE A . n 
A 1 176 TYR 176 476 476 TYR TYR A . n 
A 1 177 LYS 177 477 477 LYS LYS A . n 
A 1 178 ALA 178 478 478 ALA ALA A . n 
A 1 179 PHE 179 479 479 PHE PHE A . n 
A 1 180 SER 180 480 480 SER SER A . n 
A 1 181 SER 181 481 481 SER SER A . n 
A 1 182 GLU 182 482 482 GLU GLU A . n 
A 1 183 MET 183 483 483 MET MET A . n 
A 1 184 ALA 184 484 484 ALA ALA A . n 
A 1 185 LYS 185 485 485 LYS LYS A . n 
A 1 186 ARG 186 486 486 ARG ARG A . n 
A 1 187 SER 187 487 487 SER SER A . n 
A 1 188 LYS 188 488 488 LYS LYS A . n 
A 1 189 MET 189 489 489 MET MET A . n 
A 1 190 LEU 190 490 490 LEU LEU A . n 
A 1 191 SER 191 491 ?   ?   ?   A . n 
A 1 192 LEU 192 492 ?   ?   ?   A . n 
A 1 193 ASN 193 493 ?   ?   ?   A . n 
A 1 194 ASN 194 494 ?   ?   ?   A . n 
A 1 195 TYR 195 495 ?   ?   ?   A . n 
A 1 196 SER 196 496 ?   ?   ?   A . n 
A 1 197 VAL 197 497 ?   ?   ?   A . n 
B 1 1   GLY 1   301 ?   ?   ?   B . n 
B 1 2   ALA 2   302 ?   ?   ?   B . n 
B 1 3   MET 3   303 ?   ?   ?   B . n 
B 1 4   ALA 4   304 ?   ?   ?   B . n 
B 1 5   THR 5   305 ?   ?   ?   B . n 
B 1 6   THR 6   306 ?   ?   ?   B . n 
B 1 7   PRO 7   307 ?   ?   ?   B . n 
B 1 8   SER 8   308 ?   ?   ?   B . n 
B 1 9   PHE 9   309 ?   ?   ?   B . n 
B 1 10  ASN 10  310 310 ASN ASN B . n 
B 1 11  ALA 11  311 311 ALA ALA B . n 
B 1 12  MET 12  312 312 MET MET B . n 
B 1 13  VAL 13  313 313 VAL VAL B . n 
B 1 14  VAL 14  314 314 VAL VAL B . n 
B 1 15  ASN 15  315 315 ASN ASN B . n 
B 1 16  ASN 16  316 316 ASN ASN B . n 
B 1 17  LEU 17  317 317 LEU LEU B . n 
B 1 18  THR 18  318 318 THR THR B . n 
B 1 19  LEU 19  319 319 LEU LEU B . n 
B 1 20  GLN 20  320 320 GLN GLN B . n 
B 1 21  ILE 21  321 321 ILE ILE B . n 
B 1 22  VAL 22  322 322 VAL VAL B . n 
B 1 23  GLN 23  323 323 GLN GLN B . n 
B 1 24  GLY 24  324 324 GLY GLY B . n 
B 1 25  HIS 25  325 325 HIS HIS B . n 
B 1 26  ILE 26  326 326 ILE ILE B . n 
B 1 27  GLU 27  327 327 GLU GLU B . n 
B 1 28  TRP 28  328 328 TRP TRP B . n 
B 1 29  GLN 29  329 329 GLN GLN B . n 
B 1 30  THR 30  330 330 THR THR B . n 
B 1 31  ALA 31  331 331 ALA ALA B . n 
B 1 32  ASP 32  332 332 ASP ASP B . n 
B 1 33  VAL 33  333 333 VAL VAL B . n 
B 1 34  ILE 34  334 334 ILE ILE B . n 
B 1 35  VAL 35  335 335 VAL VAL B . n 
B 1 36  ASN 36  336 336 ASN ASN B . n 
B 1 37  SER 37  337 337 SER SER B . n 
B 1 38  VAL 38  338 338 VAL VAL B . n 
B 1 39  ASN 39  339 339 ASN ASN B . n 
B 1 40  PRO 40  340 340 PRO PRO B . n 
B 1 41  HIS 41  341 341 HIS HIS B . n 
B 1 42  ASP 42  342 342 ASP ASP B . n 
B 1 43  ILE 43  343 343 ILE ILE B . n 
B 1 44  THR 44  344 344 THR THR B . n 
B 1 45  VAL 45  345 345 VAL VAL B . n 
B 1 46  GLY 46  346 346 GLY GLY B . n 
B 1 47  PRO 47  347 347 PRO PRO B . n 
B 1 48  VAL 48  348 348 VAL VAL B . n 
B 1 49  ALA 49  349 349 ALA ALA B . n 
B 1 50  LYS 50  350 350 LYS LYS B . n 
B 1 51  SER 51  351 351 SER SER B . n 
B 1 52  ILE 52  352 352 ILE ILE B . n 
B 1 53  LEU 53  353 353 LEU LEU B . n 
B 1 54  GLN 54  354 354 GLN GLN B . n 
B 1 55  GLN 55  355 355 GLN GLN B . n 
B 1 56  ALA 56  356 356 ALA ALA B . n 
B 1 57  GLY 57  357 357 GLY GLY B . n 
B 1 58  VAL 58  358 358 VAL VAL B . n 
B 1 59  GLU 59  359 359 GLU GLU B . n 
B 1 60  MET 60  360 360 MET MET B . n 
B 1 61  LYS 61  361 361 LYS LYS B . n 
B 1 62  SER 62  362 362 SER SER B . n 
B 1 63  GLU 63  363 363 GLU GLU B . n 
B 1 64  PHE 64  364 364 PHE PHE B . n 
B 1 65  LEU 65  365 365 LEU LEU B . n 
B 1 66  ALA 66  366 366 ALA ALA B . n 
B 1 67  THR 67  367 367 THR THR B . n 
B 1 68  LYS 68  368 368 LYS LYS B . n 
B 1 69  ALA 69  369 369 ALA ALA B . n 
B 1 70  LYS 70  370 ?   ?   ?   B . n 
B 1 71  GLN 71  371 ?   ?   ?   B . n 
B 1 72  PHE 72  372 ?   ?   ?   B . n 
B 1 73  GLN 73  373 ?   ?   ?   B . n 
B 1 74  ARG 74  374 374 ARG ARG B . n 
B 1 75  SER 75  375 375 SER SER B . n 
B 1 76  GLN 76  376 376 GLN GLN B . n 
B 1 77  LEU 77  377 377 LEU LEU B . n 
B 1 78  VAL 78  378 378 VAL VAL B . n 
B 1 79  LEU 79  379 379 LEU LEU B . n 
B 1 80  VAL 80  380 380 VAL VAL B . n 
B 1 81  THR 81  381 381 THR THR B . n 
B 1 82  LYS 82  382 382 LYS LYS B . n 
B 1 83  GLY 83  383 383 GLY GLY B . n 
B 1 84  PHE 84  384 384 PHE PHE B . n 
B 1 85  ASN 85  385 385 ASN ASN B . n 
B 1 86  LEU 86  386 386 LEU LEU B . n 
B 1 87  PHE 87  387 387 PHE PHE B . n 
B 1 88  CYS 88  388 388 CYS CYS B . n 
B 1 89  LYS 89  389 389 LYS LYS B . n 
B 1 90  TYR 90  390 390 TYR TYR B . n 
B 1 91  ILE 91  391 391 ILE ILE B . n 
B 1 92  TYR 92  392 392 TYR TYR B . n 
B 1 93  HIS 93  393 393 HIS HIS B . n 
B 1 94  VAL 94  394 394 VAL VAL B . n 
B 1 95  LEU 95  395 395 LEU LEU B . n 
B 1 96  TRP 96  396 396 TRP TRP B . n 
B 1 97  HIS 97  397 397 HIS HIS B . n 
B 1 98  SER 98  398 398 SER SER B . n 
B 1 99  GLU 99  399 399 GLU GLU B . n 
B 1 100 PHE 100 400 400 PHE PHE B . n 
B 1 101 PRO 101 401 401 PRO PRO B . n 
B 1 102 LYS 102 402 402 LYS LYS B . n 
B 1 103 PRO 103 403 403 PRO PRO B . n 
B 1 104 GLN 104 404 404 GLN GLN B . n 
B 1 105 ILE 105 405 405 ILE ILE B . n 
B 1 106 LEU 106 406 406 LEU LEU B . n 
B 1 107 LYS 107 407 407 LYS LYS B . n 
B 1 108 HIS 108 408 408 HIS HIS B . n 
B 1 109 ALA 109 409 409 ALA ALA B . n 
B 1 110 MET 110 410 410 MET MET B . n 
B 1 111 LYS 111 411 411 LYS LYS B . n 
B 1 112 GLU 112 412 412 GLU GLU B . n 
B 1 113 CYS 113 413 413 CYS CYS B . n 
B 1 114 LEU 114 414 414 LEU LEU B . n 
B 1 115 GLU 115 415 415 GLU GLU B . n 
B 1 116 LYS 116 416 416 LYS LYS B . n 
B 1 117 CYS 117 417 417 CYS CYS B . n 
B 1 118 ILE 118 418 418 ILE ILE B . n 
B 1 119 GLU 119 419 419 GLU GLU B . n 
B 1 120 GLN 120 420 420 GLN GLN B . n 
B 1 121 ASN 121 421 421 ASN ASN B . n 
B 1 122 ILE 122 422 422 ILE ILE B . n 
B 1 123 THR 123 423 423 THR THR B . n 
B 1 124 SER 124 424 424 SER SER B . n 
B 1 125 ILE 125 425 425 ILE ILE B . n 
B 1 126 SER 126 426 426 SER SER B . n 
B 1 127 PHE 127 427 427 PHE PHE B . n 
B 1 128 PRO 128 428 428 PRO PRO B . n 
B 1 129 ALA 129 429 429 ALA ALA B . n 
B 1 130 LEU 130 430 430 LEU LEU B . n 
B 1 131 GLY 131 431 431 GLY GLY B . n 
B 1 132 THR 132 432 432 THR THR B . n 
B 1 133 GLY 133 433 433 GLY GLY B . n 
B 1 134 ASN 134 434 434 ASN ASN B . n 
B 1 135 MET 135 435 435 MET MET B . n 
B 1 136 GLU 136 436 436 GLU GLU B . n 
B 1 137 ILE 137 437 437 ILE ILE B . n 
B 1 138 LYS 138 438 438 LYS LYS B . n 
B 1 139 LYS 139 439 439 LYS LYS B . n 
B 1 140 GLU 140 440 440 GLU GLU B . n 
B 1 141 THR 141 441 441 THR THR B . n 
B 1 142 ALA 142 442 442 ALA ALA B . n 
B 1 143 ALA 143 443 443 ALA ALA B . n 
B 1 144 GLU 144 444 444 GLU GLU B . n 
B 1 145 ILE 145 445 445 ILE ILE B . n 
B 1 146 LEU 146 446 446 LEU LEU B . n 
B 1 147 PHE 147 447 447 PHE PHE B . n 
B 1 148 ASP 148 448 448 ASP ASP B . n 
B 1 149 GLU 149 449 449 GLU GLU B . n 
B 1 150 VAL 150 450 450 VAL VAL B . n 
B 1 151 LEU 151 451 451 LEU LEU B . n 
B 1 152 THR 152 452 452 THR THR B . n 
B 1 153 PHE 153 453 453 PHE PHE B . n 
B 1 154 ALA 154 454 454 ALA ALA B . n 
B 1 155 LYS 155 455 455 LYS LYS B . n 
B 1 156 ASP 156 456 456 ASP ASP B . n 
B 1 157 HIS 157 457 457 HIS HIS B . n 
B 1 158 VAL 158 458 458 VAL VAL B . n 
B 1 159 LYS 159 459 459 LYS LYS B . n 
B 1 160 HIS 160 460 460 HIS HIS B . n 
B 1 161 GLN 161 461 461 GLN GLN B . n 
B 1 162 LEU 162 462 462 LEU LEU B . n 
B 1 163 THR 163 463 463 THR THR B . n 
B 1 164 VAL 164 464 464 VAL VAL B . n 
B 1 165 LYS 165 465 465 LYS LYS B . n 
B 1 166 PHE 166 466 466 PHE PHE B . n 
B 1 167 VAL 167 467 467 VAL VAL B . n 
B 1 168 ILE 168 468 468 ILE ILE B . n 
B 1 169 PHE 169 469 469 PHE PHE B . n 
B 1 170 PRO 170 470 470 PRO PRO B . n 
B 1 171 THR 171 471 471 THR THR B . n 
B 1 172 ASP 172 472 472 ASP ASP B . n 
B 1 173 LEU 173 473 473 LEU LEU B . n 
B 1 174 GLU 174 474 474 GLU GLU B . n 
B 1 175 ILE 175 475 475 ILE ILE B . n 
B 1 176 TYR 176 476 476 TYR TYR B . n 
B 1 177 LYS 177 477 477 LYS LYS B . n 
B 1 178 ALA 178 478 478 ALA ALA B . n 
B 1 179 PHE 179 479 479 PHE PHE B . n 
B 1 180 SER 180 480 480 SER SER B . n 
B 1 181 SER 181 481 481 SER SER B . n 
B 1 182 GLU 182 482 482 GLU GLU B . n 
B 1 183 MET 183 483 483 MET MET B . n 
B 1 184 ALA 184 484 484 ALA ALA B . n 
B 1 185 LYS 185 485 485 LYS LYS B . n 
B 1 186 ARG 186 486 486 ARG ARG B . n 
B 1 187 SER 187 487 487 SER SER B . n 
B 1 188 LYS 188 488 488 LYS LYS B . n 
B 1 189 MET 189 489 489 MET MET B . n 
B 1 190 LEU 190 490 490 LEU LEU B . n 
B 1 191 SER 191 491 491 SER SER B . n 
B 1 192 LEU 192 492 492 LEU LEU B . n 
B 1 193 ASN 193 493 493 ASN ASN B . n 
B 1 194 ASN 194 494 494 ASN ASN B . n 
B 1 195 TYR 195 495 495 TYR TYR B . n 
B 1 196 SER 196 496 496 SER SER B . n 
B 1 197 VAL 197 497 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NAD 
_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 NAD 1 501 1  NAD NAD A . 
D 2 NAD 1 501 2  NAD NAD B . 
E 3 HOH 1 601 3  HOH HOH A . 
E 3 HOH 2 602 8  HOH HOH A . 
E 3 HOH 3 603 2  HOH HOH A . 
E 3 HOH 4 604 10 HOH HOH A . 
E 3 HOH 5 605 5  HOH HOH A . 
E 3 HOH 6 606 6  HOH HOH A . 
F 3 HOH 1 601 1  HOH HOH B . 
F 3 HOH 2 602 4  HOH HOH B . 
F 3 HOH 3 603 7  HOH HOH B . 
F 3 HOH 4 604 13 HOH HOH B . 
F 3 HOH 5 605 12 HOH HOH B . 
F 3 HOH 6 606 9  HOH HOH B . 
F 3 HOH 7 607 11 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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   116.90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9QYH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.428 
_cell.length_a_esd                 ? 
_cell.length_b                     73.827 
_cell.length_b_esd                 ? 
_cell.length_c                     58.465 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9QYH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   9QYH 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.09 
_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              6 
_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    '0.1 MES, 0.2M Ammonium chloride, 20% w/v PEG 6000' 
_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         2024-09-17 
_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   0.9655 
_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 MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9655 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9QYH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.5 
_reflns.d_resolution_low                               73.83 
_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                                     13136 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           92.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.5 
_reflns_shell.d_res_low                                     2.6 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1491 
_reflns_shell.percent_possible_obs                          ? 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.714 
_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                                  ? 
_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]                            2.90 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.96 
_refine.aniso_B[2][2]                            -3.01 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.57 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               77.358 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.935 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9QYH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.50 
_refine.ls_d_res_low                             52.19 
_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                     11763 
_refine.ls_number_reflns_R_free                  1356 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.70 
_refine.ls_percent_reflns_R_free                 10.3 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20227 
_refine.ls_R_factor_R_free                       0.24602 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19727 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.328 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_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                             35.336 
_refine.overall_SU_ML                            0.329 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        52.19 
_refine_hist.number_atoms_solvent             13 
_refine_hist.number_atoms_total               2964 
_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        2863 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         88 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  0.012  3016 ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  2919 ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 1.690  1.822  4091 ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.511  1.758  6741 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 6.628  5.000  356  ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 13.573 5.000  6    ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 16.450 10.000 549  ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.066  0.200  483  ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  3314 ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  640  ? r_gen_planes_other           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? ? 
'X-RAY DIFFRACTION' ? 3.334  3.937  1436 ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 3.333  3.938  1437 ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 5.357  7.063  1788 ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 5.357  7.064  1789 ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 4.009  4.565  1580 ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 4.008  4.569  1581 ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 6.351  8.260  2304 ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 9.824  40.21  3284 ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 9.822  40.22  3285 ? r_long_range_B_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          2.500 
_refine_ls_shell.d_res_low                           2.565 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                113 
_refine_ls_shell.number_reflns_R_work                869 
_refine_ls_shell.percent_reflns_obs                  91.01 
_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                     0.377 
_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.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      20 
_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                     0.405 
# 
_struct.entry_id                     9QYH 
_struct.title                        'PARP9 Macro Domain 2 in complex with NAD+' 
_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        9QYH 
_struct_keywords.text            'PARP9, MACRO DOMAIN, NAD+, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PARP9_HUMAN 
_struct_ref.pdbx_db_accession          Q8IXQ6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TTPSFNAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGF
NLFCKYIYHVLWHSEFPKPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQLTV
KFVIFPTDLEIYKAFSSEMAKRSKMLSLNNYSV
;
_struct_ref.pdbx_align_begin           305 
# 
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 9QYH A 5 ? 197 ? Q8IXQ6 305 ? 497 ? 305 497 
2 1 9QYH B 5 ? 197 ? Q8IXQ6 305 ? 497 ? 305 497 
# 
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 9QYH GLY A 1 ? UNP Q8IXQ6 ? ? 'expression tag' 301 1 
1 9QYH ALA A 2 ? UNP Q8IXQ6 ? ? 'expression tag' 302 2 
1 9QYH MET A 3 ? UNP Q8IXQ6 ? ? 'expression tag' 303 3 
1 9QYH ALA A 4 ? UNP Q8IXQ6 ? ? 'expression tag' 304 4 
2 9QYH GLY B 1 ? UNP Q8IXQ6 ? ? 'expression tag' 301 5 
2 9QYH ALA B 2 ? UNP Q8IXQ6 ? ? 'expression tag' 302 6 
2 9QYH MET B 3 ? UNP Q8IXQ6 ? ? 'expression tag' 303 7 
2 9QYH ALA B 4 ? UNP Q8IXQ6 ? ? 'expression tag' 304 8 
# 
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,E 
2 1 B,D,F 
# 
_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 HIS A 25  ? TRP A 28  ? HIS A 325 TRP A 328 5 ? 4  
HELX_P HELX_P2  AA2 GLY A 46  ? GLY A 57  ? GLY A 346 GLY A 357 1 ? 12 
HELX_P HELX_P3  AA3 VAL A 58  ? ALA A 66  ? VAL A 358 ALA A 366 1 ? 9  
HELX_P HELX_P4  AA4 PRO A 101 ? GLN A 120 ? PRO A 401 GLN A 420 1 ? 20 
HELX_P HELX_P5  AA5 LYS A 138 ? HIS A 157 ? LYS A 438 HIS A 457 1 ? 20 
HELX_P HELX_P6  AA6 ASP A 172 ? MET A 189 ? ASP A 472 MET A 489 1 ? 18 
HELX_P HELX_P7  AA7 HIS B 25  ? TRP B 28  ? HIS B 325 TRP B 328 5 ? 4  
HELX_P HELX_P8  AA8 GLY B 46  ? GLY B 57  ? GLY B 346 GLY B 357 1 ? 12 
HELX_P HELX_P9  AA9 VAL B 58  ? THR B 67  ? VAL B 358 THR B 367 1 ? 10 
HELX_P HELX_P10 AB1 PRO B 101 ? GLN B 120 ? PRO B 401 GLN B 420 1 ? 20 
HELX_P HELX_P11 AB2 THR B 132 ? GLU B 136 ? THR B 432 GLU B 436 5 ? 5  
HELX_P HELX_P12 AB3 LYS B 138 ? HIS B 157 ? LYS B 438 HIS B 457 1 ? 20 
HELX_P HELX_P13 AB4 ASP B 172 ? ASN B 193 ? ASP B 472 ASN B 493 1 ? 22 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? 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 ALA A 11  ? VAL A 14  ? ALA A 311 VAL A 314 
AA1 2 LEU A 17  ? GLN A 23  ? LEU A 317 GLN A 323 
AA1 3 LEU A 162 ? ILE A 168 ? LEU A 462 ILE A 468 
AA1 4 SER A 124 ? PRO A 128 ? SER A 424 PRO A 428 
AA1 5 THR A 30  ? VAL A 38  ? THR A 330 VAL A 338 
AA1 6 PHE A 87  ? LEU A 95  ? PHE A 387 LEU A 395 
AA1 7 VAL A 78  ? LYS A 82  ? VAL A 378 LYS A 382 
AA2 1 ALA B 11  ? VAL B 14  ? ALA B 311 VAL B 314 
AA2 2 LEU B 17  ? GLN B 23  ? LEU B 317 GLN B 323 
AA2 3 LEU B 162 ? ILE B 168 ? LEU B 462 ILE B 468 
AA2 4 SER B 124 ? PRO B 128 ? SER B 424 PRO B 428 
AA2 5 THR B 30  ? VAL B 38  ? THR B 330 VAL B 338 
AA2 6 PHE B 87  ? LEU B 95  ? PHE B 387 LEU B 395 
AA2 7 VAL B 78  ? LYS B 82  ? VAL B 378 LYS B 382 
# 
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 14  ? N VAL A 314 O LEU A 17  ? O LEU A 317 
AA1 2 3 N VAL A 22  ? N VAL A 322 O ILE A 168 ? O ILE A 468 
AA1 3 4 O VAL A 167 ? O VAL A 467 N PHE A 127 ? N PHE A 427 
AA1 4 5 O SER A 126 ? O SER A 426 N VAL A 35  ? N VAL A 335 
AA1 5 6 N ASN A 36  ? N ASN A 336 O VAL A 94  ? O VAL A 394 
AA1 6 7 O HIS A 93  ? O HIS A 393 N LEU A 79  ? N LEU A 379 
AA2 1 2 N VAL B 14  ? N VAL B 314 O LEU B 17  ? O LEU B 317 
AA2 2 3 N VAL B 22  ? N VAL B 322 O ILE B 168 ? O ILE B 468 
AA2 3 4 O THR B 163 ? O THR B 463 N ILE B 125 ? N ILE B 425 
AA2 4 5 O SER B 126 ? O SER B 426 N VAL B 35  ? N VAL B 335 
AA2 5 6 N ASN B 36  ? N ASN B 336 O VAL B 94  ? O VAL B 394 
AA2 6 7 O HIS B 93  ? O HIS B 393 N LEU B 79  ? N LEU B 379 
# 
_pdbx_entry_details.entry_id                   9QYH 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD1 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    448 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   NH2 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   ARG 
_pdbx_validate_close_contact.auth_seq_id_2    486 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.86 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 CG A GLN 404 ? ? 1_555 CD2 B LEU 492 ? ? 2_545 1.34 
2 1 NZ A LYS 407 ? ? 1_555 OD1 B ASN 493 ? ? 2_545 1.92 
# 
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 ASN A 315 ? ? 51.86   -115.94 
2  1 PHE A 384 ? ? 52.53   -129.68 
3  1 GLU A 399 ? ? -95.26  33.38   
4  1 ASN B 315 ? ? 49.96   -113.87 
5  1 GLN B 376 ? ? -160.07 102.93  
6  1 PHE B 384 ? ? 52.81   -129.08 
7  1 SER B 398 ? ? -95.58  43.87   
8  1 MET B 435 ? ? 39.23   61.32   
9  1 ASN B 493 ? ? -97.68  -105.99 
10 1 TYR B 495 ? ? 57.13   -165.73 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 374 ? ? 0.078 'SIDE CHAIN' 
2 1 ARG B 486 ? ? 0.076 'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 18.0565 -0.7121 5.3644  0.2960 ? -0.0266 ? 0.0069 ? 0.0192 ? -0.0444 ? 0.2268 ? 6.1215 ? -1.9468 ? 
-1.0698 ? 6.3395 ? 1.2720 ? 4.9011 ? 0.0857  ? 0.2841  ? -0.5621 ? -0.0380 ? -0.0212 ? 0.2027 ? 0.3280  ? -0.0942 ? -0.0645 ? 
2 'X-RAY DIFFRACTION' ? refined 11.9977 25.2770 15.3849 0.2785 ? 0.0628  ? 0.0507 ? 0.0329 ? -0.0302 ? 0.2895 ? 4.5659 ? 0.1540  ? 
0.3238  ? 5.7472 ? 1.9207 ? 5.3862 ? -0.0791 ? -0.1111 ? 0.5482  ? -0.0435 ? 0.0097  ? 0.2144 ? -0.4055 ? -0.3204 ? 0.0695  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 310 ? ? ? A 490 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 310 ? ? ? B 496 ? ? ? 
# 
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 GLY 301 ? A GLY 1   
2  1 Y 1 A ALA 302 ? A ALA 2   
3  1 Y 1 A MET 303 ? A MET 3   
4  1 Y 1 A ALA 304 ? A ALA 4   
5  1 Y 1 A THR 305 ? A THR 5   
6  1 Y 1 A THR 306 ? A THR 6   
7  1 Y 1 A PRO 307 ? A PRO 7   
8  1 Y 1 A SER 308 ? A SER 8   
9  1 Y 1 A PHE 309 ? A PHE 9   
10 1 Y 1 A LYS 370 ? A LYS 70  
11 1 Y 1 A GLN 371 ? A GLN 71  
12 1 Y 1 A PHE 372 ? A PHE 72  
13 1 Y 1 A GLN 373 ? A GLN 73  
14 1 Y 1 A SER 491 ? A SER 191 
15 1 Y 1 A LEU 492 ? A LEU 192 
16 1 Y 1 A ASN 493 ? A ASN 193 
17 1 Y 1 A ASN 494 ? A ASN 194 
18 1 Y 1 A TYR 495 ? A TYR 195 
19 1 Y 1 A SER 496 ? A SER 196 
20 1 Y 1 A VAL 497 ? A VAL 197 
21 1 Y 1 B GLY 301 ? B GLY 1   
22 1 Y 1 B ALA 302 ? B ALA 2   
23 1 Y 1 B MET 303 ? B MET 3   
24 1 Y 1 B ALA 304 ? B ALA 4   
25 1 Y 1 B THR 305 ? B THR 5   
26 1 Y 1 B THR 306 ? B THR 6   
27 1 Y 1 B PRO 307 ? B PRO 7   
28 1 Y 1 B SER 308 ? B SER 8   
29 1 Y 1 B PHE 309 ? B PHE 9   
30 1 Y 1 B LYS 370 ? B LYS 70  
31 1 Y 1 B GLN 371 ? B GLN 71  
32 1 Y 1 B PHE 372 ? B PHE 72  
33 1 Y 1 B GLN 373 ? B GLN 73  
34 1 Y 1 B VAL 497 ? B VAL 197 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
NAD PA   P N S 250 
NAD O1A  O N N 251 
NAD O2A  O N N 252 
NAD O5B  O N N 253 
NAD C5B  C N N 254 
NAD C4B  C N R 255 
NAD O4B  O N N 256 
NAD C3B  C N S 257 
NAD O3B  O N N 258 
NAD C2B  C N R 259 
NAD O2B  O N N 260 
NAD C1B  C N R 261 
NAD N9A  N Y N 262 
NAD C8A  C Y N 263 
NAD N7A  N Y N 264 
NAD C5A  C Y N 265 
NAD C6A  C Y N 266 
NAD N6A  N N N 267 
NAD N1A  N Y N 268 
NAD C2A  C Y N 269 
NAD N3A  N Y N 270 
NAD C4A  C Y N 271 
NAD O3   O N N 272 
NAD PN   P N N 273 
NAD O1N  O N N 274 
NAD O2N  O N N 275 
NAD O5D  O N N 276 
NAD C5D  C N N 277 
NAD C4D  C N R 278 
NAD O4D  O N N 279 
NAD C3D  C N S 280 
NAD O3D  O N N 281 
NAD C2D  C N R 282 
NAD O2D  O N N 283 
NAD C1D  C N R 284 
NAD N1N  N Y N 285 
NAD C2N  C Y N 286 
NAD C3N  C Y N 287 
NAD C7N  C N N 288 
NAD O7N  O N N 289 
NAD N7N  N N N 290 
NAD C4N  C Y N 291 
NAD C5N  C Y N 292 
NAD C6N  C Y N 293 
NAD HOA2 H N N 294 
NAD H51A H N N 295 
NAD H52A H N N 296 
NAD H4B  H N N 297 
NAD H3B  H N N 298 
NAD HO3A H N N 299 
NAD H2B  H N N 300 
NAD HO2A H N N 301 
NAD H1B  H N N 302 
NAD H8A  H N N 303 
NAD H61A H N N 304 
NAD H62A H N N 305 
NAD H2A  H N N 306 
NAD H51N H N N 307 
NAD H52N H N N 308 
NAD H4D  H N N 309 
NAD H3D  H N N 310 
NAD HO3N H N N 311 
NAD H2D  H N N 312 
NAD HO2N H N N 313 
NAD H1D  H N N 314 
NAD H2N  H N N 315 
NAD H71N H N N 316 
NAD H72N H N N 317 
NAD H4N  H N N 318 
NAD H5N  H N N 319 
NAD H6N  H N N 320 
PHE N    N N N 321 
PHE CA   C N S 322 
PHE C    C N N 323 
PHE O    O N N 324 
PHE CB   C N N 325 
PHE CG   C Y N 326 
PHE CD1  C Y N 327 
PHE CD2  C Y N 328 
PHE CE1  C Y N 329 
PHE CE2  C Y N 330 
PHE CZ   C Y N 331 
PHE OXT  O N N 332 
PHE H    H N N 333 
PHE H2   H N N 334 
PHE HA   H N N 335 
PHE HB2  H N N 336 
PHE HB3  H N N 337 
PHE HD1  H N N 338 
PHE HD2  H N N 339 
PHE HE1  H N N 340 
PHE HE2  H N N 341 
PHE HZ   H N N 342 
PHE HXT  H N N 343 
PRO N    N N N 344 
PRO CA   C N S 345 
PRO C    C N N 346 
PRO O    O N N 347 
PRO CB   C N N 348 
PRO CG   C N N 349 
PRO CD   C N N 350 
PRO OXT  O N N 351 
PRO H    H N N 352 
PRO HA   H N N 353 
PRO HB2  H N N 354 
PRO HB3  H N N 355 
PRO HG2  H N N 356 
PRO HG3  H N N 357 
PRO HD2  H N N 358 
PRO HD3  H N N 359 
PRO HXT  H N N 360 
SER N    N N N 361 
SER CA   C N S 362 
SER C    C N N 363 
SER O    O N N 364 
SER CB   C N N 365 
SER OG   O N N 366 
SER OXT  O N N 367 
SER H    H N N 368 
SER H2   H N N 369 
SER HA   H N N 370 
SER HB2  H N N 371 
SER HB3  H N N 372 
SER HG   H N N 373 
SER HXT  H N N 374 
THR N    N N N 375 
THR CA   C N S 376 
THR C    C N N 377 
THR O    O N N 378 
THR CB   C N R 379 
THR OG1  O N N 380 
THR CG2  C N N 381 
THR OXT  O N N 382 
THR H    H N N 383 
THR H2   H N N 384 
THR HA   H N N 385 
THR HB   H N N 386 
THR HG1  H N N 387 
THR HG21 H N N 388 
THR HG22 H N N 389 
THR HG23 H N N 390 
THR HXT  H N N 391 
TRP N    N N N 392 
TRP CA   C N S 393 
TRP C    C N N 394 
TRP O    O N N 395 
TRP CB   C N N 396 
TRP CG   C Y N 397 
TRP CD1  C Y N 398 
TRP CD2  C Y N 399 
TRP NE1  N Y N 400 
TRP CE2  C Y N 401 
TRP CE3  C Y N 402 
TRP CZ2  C Y N 403 
TRP CZ3  C Y N 404 
TRP CH2  C Y N 405 
TRP OXT  O N N 406 
TRP H    H N N 407 
TRP H2   H N N 408 
TRP HA   H N N 409 
TRP HB2  H N N 410 
TRP HB3  H N N 411 
TRP HD1  H N N 412 
TRP HE1  H N N 413 
TRP HE3  H N N 414 
TRP HZ2  H N N 415 
TRP HZ3  H N N 416 
TRP HH2  H N N 417 
TRP HXT  H N N 418 
TYR N    N N N 419 
TYR CA   C N S 420 
TYR C    C N N 421 
TYR O    O N N 422 
TYR CB   C N N 423 
TYR CG   C Y N 424 
TYR CD1  C Y N 425 
TYR CD2  C Y N 426 
TYR CE1  C Y N 427 
TYR CE2  C Y N 428 
TYR CZ   C Y N 429 
TYR OH   O N N 430 
TYR OXT  O N N 431 
TYR H    H N N 432 
TYR H2   H N N 433 
TYR HA   H N N 434 
TYR HB2  H N N 435 
TYR HB3  H N N 436 
TYR HD1  H N N 437 
TYR HD2  H N N 438 
TYR HE1  H N N 439 
TYR HE2  H N N 440 
TYR HH   H N N 441 
TYR HXT  H N N 442 
VAL N    N N N 443 
VAL CA   C N S 444 
VAL C    C N N 445 
VAL O    O N N 446 
VAL CB   C N N 447 
VAL CG1  C N N 448 
VAL CG2  C N N 449 
VAL OXT  O N N 450 
VAL H    H N N 451 
VAL H2   H N N 452 
VAL HA   H N N 453 
VAL HB   H N N 454 
VAL HG11 H N N 455 
VAL HG12 H N N 456 
VAL HG13 H N N 457 
VAL HG21 H N N 458 
VAL HG22 H N N 459 
VAL HG23 H N N 460 
VAL HXT  H N N 461 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NAD PA  O1A  doub N N 237 
NAD PA  O2A  sing N N 238 
NAD PA  O5B  sing N N 239 
NAD PA  O3   sing N N 240 
NAD O2A HOA2 sing N N 241 
NAD O5B C5B  sing N N 242 
NAD C5B C4B  sing N N 243 
NAD C5B H51A sing N N 244 
NAD C5B H52A sing N N 245 
NAD C4B O4B  sing N N 246 
NAD C4B C3B  sing N N 247 
NAD C4B H4B  sing N N 248 
NAD O4B C1B  sing N N 249 
NAD C3B O3B  sing N N 250 
NAD C3B C2B  sing N N 251 
NAD C3B H3B  sing N N 252 
NAD O3B HO3A sing N N 253 
NAD C2B O2B  sing N N 254 
NAD C2B C1B  sing N N 255 
NAD C2B H2B  sing N N 256 
NAD O2B HO2A sing N N 257 
NAD C1B N9A  sing N N 258 
NAD C1B H1B  sing N N 259 
NAD N9A C8A  sing Y N 260 
NAD N9A C4A  sing Y N 261 
NAD C8A N7A  doub Y N 262 
NAD C8A H8A  sing N N 263 
NAD N7A C5A  sing Y N 264 
NAD C5A C6A  sing Y N 265 
NAD C5A C4A  doub Y N 266 
NAD C6A N6A  sing N N 267 
NAD C6A N1A  doub Y N 268 
NAD N6A H61A sing N N 269 
NAD N6A H62A sing N N 270 
NAD N1A C2A  sing Y N 271 
NAD C2A N3A  doub Y N 272 
NAD C2A H2A  sing N N 273 
NAD N3A C4A  sing Y N 274 
NAD O3  PN   sing N N 275 
NAD PN  O1N  doub N N 276 
NAD PN  O2N  sing N N 277 
NAD PN  O5D  sing N N 278 
NAD O5D C5D  sing N N 279 
NAD C5D C4D  sing N N 280 
NAD C5D H51N sing N N 281 
NAD C5D H52N sing N N 282 
NAD C4D O4D  sing N N 283 
NAD C4D C3D  sing N N 284 
NAD C4D H4D  sing N N 285 
NAD O4D C1D  sing N N 286 
NAD C3D O3D  sing N N 287 
NAD C3D C2D  sing N N 288 
NAD C3D H3D  sing N N 289 
NAD O3D HO3N sing N N 290 
NAD C2D O2D  sing N N 291 
NAD C2D C1D  sing N N 292 
NAD C2D H2D  sing N N 293 
NAD O2D HO2N sing N N 294 
NAD C1D N1N  sing N N 295 
NAD C1D H1D  sing N N 296 
NAD N1N C2N  sing Y N 297 
NAD N1N C6N  doub Y N 298 
NAD C2N C3N  doub Y N 299 
NAD C2N H2N  sing N N 300 
NAD C3N C7N  sing N N 301 
NAD C3N C4N  sing Y N 302 
NAD C7N O7N  doub N N 303 
NAD C7N N7N  sing N N 304 
NAD N7N H71N sing N N 305 
NAD N7N H72N sing N N 306 
NAD C4N C5N  doub Y N 307 
NAD C4N H4N  sing N N 308 
NAD C5N C6N  sing Y N 309 
NAD C5N H5N  sing N N 310 
NAD C6N H6N  sing N N 311 
PHE N   CA   sing N N 312 
PHE N   H    sing N N 313 
PHE N   H2   sing N N 314 
PHE CA  C    sing N N 315 
PHE CA  CB   sing N N 316 
PHE CA  HA   sing N N 317 
PHE C   O    doub N N 318 
PHE C   OXT  sing N N 319 
PHE CB  CG   sing N N 320 
PHE CB  HB2  sing N N 321 
PHE CB  HB3  sing N N 322 
PHE CG  CD1  doub Y N 323 
PHE CG  CD2  sing Y N 324 
PHE CD1 CE1  sing Y N 325 
PHE CD1 HD1  sing N N 326 
PHE CD2 CE2  doub Y N 327 
PHE CD2 HD2  sing N N 328 
PHE CE1 CZ   doub Y N 329 
PHE CE1 HE1  sing N N 330 
PHE CE2 CZ   sing Y N 331 
PHE CE2 HE2  sing N N 332 
PHE CZ  HZ   sing N N 333 
PHE OXT HXT  sing N N 334 
PRO N   CA   sing N N 335 
PRO N   CD   sing N N 336 
PRO N   H    sing N N 337 
PRO CA  C    sing N N 338 
PRO CA  CB   sing N N 339 
PRO CA  HA   sing N N 340 
PRO C   O    doub N N 341 
PRO C   OXT  sing N N 342 
PRO CB  CG   sing N N 343 
PRO CB  HB2  sing N N 344 
PRO CB  HB3  sing N N 345 
PRO CG  CD   sing N N 346 
PRO CG  HG2  sing N N 347 
PRO CG  HG3  sing N N 348 
PRO CD  HD2  sing N N 349 
PRO CD  HD3  sing N N 350 
PRO OXT HXT  sing N N 351 
SER N   CA   sing N N 352 
SER N   H    sing N N 353 
SER N   H2   sing N N 354 
SER CA  C    sing N N 355 
SER CA  CB   sing N N 356 
SER CA  HA   sing N N 357 
SER C   O    doub N N 358 
SER C   OXT  sing N N 359 
SER CB  OG   sing N N 360 
SER CB  HB2  sing N N 361 
SER CB  HB3  sing N N 362 
SER OG  HG   sing N N 363 
SER OXT HXT  sing N N 364 
THR N   CA   sing N N 365 
THR N   H    sing N N 366 
THR N   H2   sing N N 367 
THR CA  C    sing N N 368 
THR CA  CB   sing N N 369 
THR CA  HA   sing N N 370 
THR C   O    doub N N 371 
THR C   OXT  sing N N 372 
THR CB  OG1  sing N N 373 
THR CB  CG2  sing N N 374 
THR CB  HB   sing N N 375 
THR OG1 HG1  sing N N 376 
THR CG2 HG21 sing N N 377 
THR CG2 HG22 sing N N 378 
THR CG2 HG23 sing N N 379 
THR OXT HXT  sing N N 380 
TRP N   CA   sing N N 381 
TRP N   H    sing N N 382 
TRP N   H2   sing N N 383 
TRP CA  C    sing N N 384 
TRP CA  CB   sing N N 385 
TRP CA  HA   sing N N 386 
TRP C   O    doub N N 387 
TRP C   OXT  sing N N 388 
TRP CB  CG   sing N N 389 
TRP CB  HB2  sing N N 390 
TRP CB  HB3  sing N N 391 
TRP CG  CD1  doub Y N 392 
TRP CG  CD2  sing Y N 393 
TRP CD1 NE1  sing Y N 394 
TRP CD1 HD1  sing N N 395 
TRP CD2 CE2  doub Y N 396 
TRP CD2 CE3  sing Y N 397 
TRP NE1 CE2  sing Y N 398 
TRP NE1 HE1  sing N N 399 
TRP CE2 CZ2  sing Y N 400 
TRP CE3 CZ3  doub Y N 401 
TRP CE3 HE3  sing N N 402 
TRP CZ2 CH2  doub Y N 403 
TRP CZ2 HZ2  sing N N 404 
TRP CZ3 CH2  sing Y N 405 
TRP CZ3 HZ3  sing N N 406 
TRP CH2 HH2  sing N N 407 
TRP OXT HXT  sing N N 408 
TYR N   CA   sing N N 409 
TYR N   H    sing N N 410 
TYR N   H2   sing N N 411 
TYR CA  C    sing N N 412 
TYR CA  CB   sing N N 413 
TYR CA  HA   sing N N 414 
TYR C   O    doub N N 415 
TYR C   OXT  sing N N 416 
TYR CB  CG   sing N N 417 
TYR CB  HB2  sing N N 418 
TYR CB  HB3  sing N N 419 
TYR CG  CD1  doub Y N 420 
TYR CG  CD2  sing Y N 421 
TYR CD1 CE1  sing Y N 422 
TYR CD1 HD1  sing N N 423 
TYR CD2 CE2  doub Y N 424 
TYR CD2 HD2  sing N N 425 
TYR CE1 CZ   doub Y N 426 
TYR CE1 HE1  sing N N 427 
TYR CE2 CZ   sing Y N 428 
TYR CE2 HE2  sing N N 429 
TYR CZ  OH   sing N N 430 
TYR OH  HH   sing N N 431 
TYR OXT HXT  sing N N 432 
VAL N   CA   sing N N 433 
VAL N   H    sing N N 434 
VAL N   H2   sing N N 435 
VAL CA  C    sing N N 436 
VAL CA  CB   sing N N 437 
VAL CA  HA   sing N N 438 
VAL C   O    doub N N 439 
VAL C   OXT  sing N N 440 
VAL CB  CG1  sing N N 441 
VAL CB  CG2  sing N N 442 
VAL CB  HB   sing N N 443 
VAL CG1 HG11 sing N N 444 
VAL CG1 HG12 sing N N 445 
VAL CG1 HG13 sing N N 446 
VAL CG2 HG21 sing N N 447 
VAL CG2 HG22 sing N N 448 
VAL CG2 HG23 sing N N 449 
VAL OXT HXT  sing N N 450 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'European Regional Development Fund' 'European Union' 5002550-INSPIRED         1 
'European Union (EU)'                'European Union' 101087215-ESPERANCE      2 
'European Union (EU)'                'European Union' 101159708-MILESTONE      3 
'European Union (EU)'                'European Union' '871037-iNEXT Discovery' 4 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9QYF 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9QYH 
_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]   0.018717 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.009496 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013545 
_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]   0.019180 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
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   . ASN A 1 10  ? 7.550   11.962  -4.062  1.00 95.15  ? 310 ASN A N   1 
ATOM   2    C CA  . ASN A 1 10  ? 8.284   10.750  -3.592  1.00 89.59  ? 310 ASN A CA  1 
ATOM   3    C C   . ASN A 1 10  ? 8.424   10.788  -2.069  1.00 74.04  ? 310 ASN A C   1 
ATOM   4    O O   . ASN A 1 10  ? 9.515   10.626  -1.527  1.00 66.50  ? 310 ASN A O   1 
ATOM   5    C CB  . ASN A 1 10  ? 9.620   10.584  -4.313  1.00 96.04  ? 310 ASN A CB  1 
ATOM   6    C CG  . ASN A 1 10  ? 10.609  11.666  -3.937  1.00 105.16 ? 310 ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 10  ? 10.248  12.669  -3.307  1.00 106.42 ? 310 ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 10  ? 11.866  11.482  -4.318  1.00 110.09 ? 310 ASN A ND2 1 
ATOM   9    N N   . ALA A 1 11  ? 7.285   10.962  -1.393  1.00 68.42  ? 311 ALA A N   1 
ATOM   10   C CA  . ALA A 1 11  ? 7.162   10.696  0.028   1.00 64.15  ? 311 ALA A CA  1 
ATOM   11   C C   . ALA A 1 11  ? 5.685   10.505  0.337   1.00 64.37  ? 311 ALA A C   1 
ATOM   12   O O   . ALA A 1 11  ? 4.852   11.067  -0.357  1.00 67.25  ? 311 ALA A O   1 
ATOM   13   C CB  . ALA A 1 11  ? 7.760   11.826  0.844   1.00 63.38  ? 311 ALA A CB  1 
ATOM   14   N N   . MET A 1 12  ? 5.371   9.713   1.362   1.00 64.60  ? 312 MET A N   1 
ATOM   15   C CA  . MET A 1 12  ? 3.987   9.452   1.706   1.00 71.38  ? 312 MET A CA  1 
ATOM   16   C C   . MET A 1 12  ? 3.875   9.116   3.184   1.00 67.76  ? 312 MET A C   1 
ATOM   17   O O   . MET A 1 12  ? 4.832   8.679   3.802   1.00 69.47  ? 312 MET A O   1 
ATOM   18   C CB  . MET A 1 12  ? 3.409   8.308   0.864   1.00 79.24  ? 312 MET A CB  1 
ATOM   19   C CG  . MET A 1 12  ? 4.095   6.959   1.022   1.00 82.41  ? 312 MET A CG  1 
ATOM   20   S SD  . MET A 1 12  ? 3.419   5.714   -0.105  1.00 91.59  ? 312 MET A SD  1 
ATOM   21   C CE  . MET A 1 12  ? 4.401   4.334   0.504   1.00 90.62  ? 312 MET A CE  1 
ATOM   22   N N   . VAL A 1 13  ? 2.703   9.366   3.751   1.00 68.06  ? 313 VAL A N   1 
ATOM   23   C CA  . VAL A 1 13  ? 2.509   9.091   5.201   1.00 68.81  ? 313 VAL A CA  1 
ATOM   24   C C   . VAL A 1 13  ? 1.433   8.009   5.326   1.00 71.94  ? 313 VAL A C   1 
ATOM   25   O O   . VAL A 1 13  ? 0.343   8.194   4.765   1.00 78.39  ? 313 VAL A O   1 
ATOM   26   C CB  . VAL A 1 13  ? 2.148   10.332  6.042   1.00 68.34  ? 313 VAL A CB  1 
ATOM   27   C CG1 . VAL A 1 13  ? 1.782   9.960   7.472   1.00 67.14  ? 313 VAL A CG1 1 
ATOM   28   C CG2 . VAL A 1 13  ? 3.262   11.368  6.038   1.00 65.90  ? 313 VAL A CG2 1 
ATOM   29   N N   . VAL A 1 14  ? 1.757   6.912   5.998   1.00 67.30  ? 314 VAL A N   1 
ATOM   30   C CA  . VAL A 1 14  ? 0.739   5.861   6.249   1.00 72.53  ? 314 VAL A CA  1 
ATOM   31   C C   . VAL A 1 14  ? 0.541   5.817   7.765   1.00 73.68  ? 314 VAL A C   1 
ATOM   32   O O   . VAL A 1 14  ? 1.486   5.433   8.468   1.00 71.75  ? 314 VAL A O   1 
ATOM   33   C CB  . VAL A 1 14  ? 1.161   4.495   5.683   1.00 74.87  ? 314 VAL A CB  1 
ATOM   34   C CG1 . VAL A 1 14  ? 0.068   3.449   5.858   1.00 78.85  ? 314 VAL A CG1 1 
ATOM   35   C CG2 . VAL A 1 14  ? 1.590   4.592   4.225   1.00 73.17  ? 314 VAL A CG2 1 
ATOM   36   N N   . ASN A 1 15  ? -0.630  6.234   8.234   1.00 78.77  ? 315 ASN A N   1 
ATOM   37   C CA  . ASN A 1 15  ? -0.890  6.295   9.695   1.00 83.98  ? 315 ASN A CA  1 
ATOM   38   C C   . ASN A 1 15  ? 0.235   7.078   10.375  1.00 80.46  ? 315 ASN A C   1 
ATOM   39   O O   . ASN A 1 15  ? 0.362   8.283   10.095  1.00 77.57  ? 315 ASN A O   1 
ATOM   40   C CB  . ASN A 1 15  ? -1.078  4.908   10.293  1.00 89.03  ? 315 ASN A CB  1 
ATOM   41   C CG  . ASN A 1 15  ? -1.880  3.998   9.396   1.00 95.24  ? 315 ASN A CG  1 
ATOM   42   O OD1 . ASN A 1 15  ? -2.721  4.469   8.624   1.00 99.49  ? 315 ASN A OD1 1 
ATOM   43   N ND2 . ASN A 1 15  ? -1.633  2.699   9.480   1.00 96.96  ? 315 ASN A ND2 1 
ATOM   44   N N   . ASN A 1 16  ? 1.004   6.421   11.241  1.00 80.36  ? 316 ASN A N   1 
ATOM   45   C CA  . ASN A 1 16  ? 2.070   7.128   12.000  1.00 83.14  ? 316 ASN A CA  1 
ATOM   46   C C   . ASN A 1 16  ? 3.429   6.819   11.375  1.00 76.50  ? 316 ASN A C   1 
ATOM   47   O O   . ASN A 1 16  ? 4.446   6.945   12.078  1.00 77.83  ? 316 ASN A O   1 
ATOM   48   C CB  . ASN A 1 16  ? 2.038   6.770   13.479  1.00 90.68  ? 316 ASN A CB  1 
ATOM   49   C CG  . ASN A 1 16  ? 1.455   7.879   14.321  1.00 97.39  ? 316 ASN A CG  1 
ATOM   50   O OD1 . ASN A 1 16  ? 0.862   8.820   13.784  1.00 101.49 ? 316 ASN A OD1 1 
ATOM   51   N ND2 . ASN A 1 16  ? 1.610   7.786   15.633  1.00 99.89  ? 316 ASN A ND2 1 
ATOM   52   N N   . LEU A 1 17  ? 3.436   6.432   10.102  1.00 73.78  ? 317 LEU A N   1 
ATOM   53   C CA  . LEU A 1 17  ? 4.685   6.144   9.423   1.00 66.90  ? 317 LEU A CA  1 
ATOM   54   C C   . LEU A 1 17  ? 4.845   7.126   8.272   1.00 67.73  ? 317 LEU A C   1 
ATOM   55   O O   . LEU A 1 17  ? 3.952   7.270   7.435   1.00 72.64  ? 317 LEU A O   1 
ATOM   56   C CB  . LEU A 1 17  ? 4.748   4.699   8.941   1.00 67.02  ? 317 LEU A CB  1 
ATOM   57   C CG  . LEU A 1 17  ? 6.042   4.278   8.226   1.00 62.16  ? 317 LEU A CG  1 
ATOM   58   C CD1 . LEU A 1 17  ? 6.545   2.974   8.787   1.00 64.24  ? 317 LEU A CD1 1 
ATOM   59   C CD2 . LEU A 1 17  ? 5.850   4.120   6.734   1.00 62.33  ? 317 LEU A CD2 1 
ATOM   60   N N   . THR A 1 18  ? 5.988   7.815   8.287   1.00 62.44  ? 318 THR A N   1 
ATOM   61   C CA  . THR A 1 18  ? 6.442   8.622   7.177   1.00 58.48  ? 318 THR A CA  1 
ATOM   62   C C   . THR A 1 18  ? 7.482   7.821   6.405   1.00 56.25  ? 318 THR A C   1 
ATOM   63   O O   . THR A 1 18  ? 8.426   7.321   7.011   1.00 56.06  ? 318 THR A O   1 
ATOM   64   C CB  . THR A 1 18  ? 7.037   9.886   7.790   1.00 56.68  ? 318 THR A CB  1 
ATOM   65   O OG1 . THR A 1 18  ? 5.905   10.661  8.175   1.00 55.95  ? 318 THR A OG1 1 
ATOM   66   C CG2 . THR A 1 18  ? 7.941   10.604  6.808   1.00 55.30  ? 318 THR A CG2 1 
ATOM   67   N N   . LEU A 1 19  ? 7.338   7.745   5.082   1.00 57.78  ? 319 LEU A N   1 
ATOM   68   C CA  . LEU A 1 19  ? 8.324   7.096   4.224   1.00 58.00  ? 319 LEU A CA  1 
ATOM   69   C C   . LEU A 1 19  ? 8.705   7.998   3.047   1.00 55.23  ? 319 LEU A C   1 
ATOM   70   O O   . LEU A 1 19  ? 7.842   8.448   2.306   1.00 52.87  ? 319 LEU A O   1 
ATOM   71   C CB  . LEU A 1 19  ? 7.720   5.787   3.731   1.00 62.25  ? 319 LEU A CB  1 
ATOM   72   C CG  . LEU A 1 19  ? 8.486   5.082   2.615   1.00 65.12  ? 319 LEU A CG  1 
ATOM   73   C CD1 . LEU A 1 19  ? 9.878   4.720   3.073   1.00 63.97  ? 319 LEU A CD1 1 
ATOM   74   C CD2 . LEU A 1 19  ? 7.702   3.856   2.188   1.00 73.17  ? 319 LEU A CD2 1 
ATOM   75   N N   . GLN A 1 20  ? 10.011  8.191   2.860   1.00 55.42  ? 320 GLN A N   1 
ATOM   76   C CA  . GLN A 1 20  ? 10.566  9.132   1.904   1.00 60.02  ? 320 GLN A CA  1 
ATOM   77   C C   . GLN A 1 20  ? 11.670  8.455   1.093   1.00 59.04  ? 320 GLN A C   1 
ATOM   78   O O   . GLN A 1 20  ? 12.500  7.733   1.622   1.00 58.42  ? 320 GLN A O   1 
ATOM   79   C CB  . GLN A 1 20  ? 11.225  10.338  2.584   1.00 62.54  ? 320 GLN A CB  1 
ATOM   80   C CG  . GLN A 1 20  ? 10.382  10.988  3.677   1.00 67.58  ? 320 GLN A CG  1 
ATOM   81   C CD  . GLN A 1 20  ? 11.029  12.196  4.331   1.00 70.63  ? 320 GLN A CD  1 
ATOM   82   O OE1 . GLN A 1 20  ? 11.566  13.086  3.663   1.00 88.36  ? 320 GLN A OE1 1 
ATOM   83   N NE2 . GLN A 1 20  ? 10.985  12.262  5.652   1.00 68.80  ? 320 GLN A NE2 1 
ATOM   84   N N   . ILE A 1 21  ? 11.708  8.739   -0.205  1.00 60.33  ? 321 ILE A N   1 
ATOM   85   C CA  . ILE A 1 21  ? 12.821  8.317   -1.026  1.00 59.42  ? 321 ILE A CA  1 
ATOM   86   C C   . ILE A 1 21  ? 13.755  9.510   -1.156  1.00 61.09  ? 321 ILE A C   1 
ATOM   87   O O   . ILE A 1 21  ? 13.343  10.595  -1.546  1.00 62.47  ? 321 ILE A O   1 
ATOM   88   C CB  . ILE A 1 21  ? 12.344  7.814   -2.399  1.00 64.58  ? 321 ILE A CB  1 
ATOM   89   C CG1 . ILE A 1 21  ? 11.439  6.605   -2.283  1.00 65.90  ? 321 ILE A CG1 1 
ATOM   90   C CG2 . ILE A 1 21  ? 13.529  7.501   -3.301  1.00 64.68  ? 321 ILE A CG2 1 
ATOM   91   C CD1 . ILE A 1 21  ? 10.484  6.461   -3.449  1.00 70.19  ? 321 ILE A CD1 1 
ATOM   92   N N   . VAL A 1 22  ? 15.029  9.266   -0.879  1.00 59.76  ? 322 VAL A N   1 
ATOM   93   C CA  . VAL A 1 22  ? 16.027  10.304  -0.855  1.00 55.93  ? 322 VAL A CA  1 
ATOM   94   C C   . VAL A 1 22  ? 17.232  9.874   -1.681  1.00 61.57  ? 322 VAL A C   1 
ATOM   95   O O   . VAL A 1 22  ? 17.659  8.730   -1.550  1.00 56.99  ? 322 VAL A O   1 
ATOM   96   C CB  . VAL A 1 22  ? 16.336  10.466  0.631   1.00 52.36  ? 322 VAL A CB  1 
ATOM   97   C CG1 . VAL A 1 22  ? 17.780  10.849  0.896   1.00 53.20  ? 322 VAL A CG1 1 
ATOM   98   C CG2 . VAL A 1 22  ? 15.364  11.460  1.250   1.00 56.18  ? 322 VAL A CG2 1 
ATOM   99   N N   . GLN A 1 23  ? 17.741  10.811  -2.512  1.00 63.19  ? 323 GLN A N   1 
ATOM   100  C CA  . GLN A 1 23  ? 19.006  10.677  -3.207  1.00 60.91  ? 323 GLN A CA  1 
ATOM   101  C C   . GLN A 1 23  ? 20.105  11.287  -2.351  1.00 57.35  ? 323 GLN A C   1 
ATOM   102  O O   . GLN A 1 23  ? 20.146  12.491  -2.224  1.00 66.41  ? 323 GLN A O   1 
ATOM   103  C CB  . GLN A 1 23  ? 18.953  11.408  -4.545  1.00 68.61  ? 323 GLN A CB  1 
ATOM   104  C CG  . GLN A 1 23  ? 17.871  10.873  -5.478  1.00 77.78  ? 323 GLN A CG  1 
ATOM   105  C CD  . GLN A 1 23  ? 17.913  11.434  -6.886  1.00 86.74  ? 323 GLN A CD  1 
ATOM   106  O OE1 . GLN A 1 23  ? 18.768  11.068  -7.708  1.00 96.31  ? 323 GLN A OE1 1 
ATOM   107  N NE2 . GLN A 1 23  ? 16.958  12.303  -7.190  1.00 89.16  ? 323 GLN A NE2 1 
ATOM   108  N N   . GLY A 1 24  ? 20.984  10.471  -1.766  1.00 50.49  ? 324 GLY A N   1 
ATOM   109  C CA  . GLY A 1 24  ? 22.135  10.968  -1.037  1.00 48.86  ? 324 GLY A CA  1 
ATOM   110  C C   . GLY A 1 24  ? 23.066  9.821   -0.684  1.00 49.08  ? 324 GLY A C   1 
ATOM   111  O O   . GLY A 1 24  ? 22.935  8.734   -1.247  1.00 52.89  ? 324 GLY A O   1 
ATOM   112  N N   . HIS A 1 25  ? 23.982  10.057  0.262   1.00 49.05  ? 325 HIS A N   1 
ATOM   113  C CA  . HIS A 1 25  ? 24.829  9.004   0.799   1.00 49.10  ? 325 HIS A CA  1 
ATOM   114  C C   . HIS A 1 25  ? 24.286  8.540   2.148   1.00 48.86  ? 325 HIS A C   1 
ATOM   115  O O   . HIS A 1 25  ? 23.865  9.337   2.991   1.00 53.45  ? 325 HIS A O   1 
ATOM   116  C CB  . HIS A 1 25  ? 26.273  9.482   0.983   1.00 55.34  ? 325 HIS A CB  1 
ATOM   117  C CG  . HIS A 1 25  ? 26.981  9.953   -0.252  1.00 62.32  ? 325 HIS A CG  1 
ATOM   118  N ND1 . HIS A 1 25  ? 28.349  9.837   -0.368  1.00 65.45  ? 325 HIS A ND1 1 
ATOM   119  C CD2 . HIS A 1 25  ? 26.560  10.543  -1.397  1.00 66.06  ? 325 HIS A CD2 1 
ATOM   120  C CE1 . HIS A 1 25  ? 28.726  10.337  -1.543  1.00 71.60  ? 325 HIS A CE1 1 
ATOM   121  N NE2 . HIS A 1 25  ? 27.658  10.770  -2.186  1.00 69.43  ? 325 HIS A NE2 1 
ATOM   122  N N   . ILE A 1 26  ? 24.316  7.230   2.358   1.00 45.86  ? 326 ILE A N   1 
ATOM   123  C CA  . ILE A 1 26  ? 23.810  6.602   3.567   1.00 45.10  ? 326 ILE A CA  1 
ATOM   124  C C   . ILE A 1 26  ? 24.697  6.935   4.756   1.00 45.80  ? 326 ILE A C   1 
ATOM   125  O O   . ILE A 1 26  ? 24.183  7.074   5.863   1.00 47.78  ? 326 ILE A O   1 
ATOM   126  C CB  . ILE A 1 26  ? 23.688  5.069   3.382   1.00 45.73  ? 326 ILE A CB  1 
ATOM   127  C CG1 . ILE A 1 26  ? 23.043  4.419   4.583   1.00 41.48  ? 326 ILE A CG1 1 
ATOM   128  C CG2 . ILE A 1 26  ? 25.016  4.405   3.006   1.00 46.54  ? 326 ILE A CG2 1 
ATOM   129  C CD1 . ILE A 1 26  ? 21.545  4.636   4.595   1.00 43.01  ? 326 ILE A CD1 1 
ATOM   130  N N   . GLU A 1 27  ? 26.016  7.008   4.542   1.00 46.79  ? 327 GLU A N   1 
ATOM   131  C CA  . GLU A 1 27  ? 26.937  7.287   5.638   1.00 51.13  ? 327 GLU A CA  1 
ATOM   132  C C   . GLU A 1 27  ? 26.918  8.768   6.060   1.00 56.94  ? 327 GLU A C   1 
ATOM   133  O O   . GLU A 1 27  ? 27.540  9.136   7.059   1.00 58.59  ? 327 GLU A O   1 
ATOM   134  C CB  . GLU A 1 27  ? 28.357  6.844   5.285   1.00 54.02  ? 327 GLU A CB  1 
ATOM   135  C CG  . GLU A 1 27  ? 29.129  7.713   4.287   1.00 57.88  ? 327 GLU A CG  1 
ATOM   136  C CD  . GLU A 1 27  ? 28.604  7.728   2.853   1.00 58.89  ? 327 GLU A CD  1 
ATOM   137  O OE1 . GLU A 1 27  ? 27.520  7.124   2.719   1.00 51.53  ? 327 GLU A OE1 1 
ATOM   138  O OE2 . GLU A 1 27  ? 29.223  8.327   1.912   1.00 61.99  ? 327 GLU A OE2 1 
ATOM   139  N N   . TRP A 1 28  ? 26.232  9.633   5.297   1.00 55.96  ? 328 TRP A N   1 
ATOM   140  C CA  . TRP A 1 28  ? 26.149  11.043  5.644   1.00 59.32  ? 328 TRP A CA  1 
ATOM   141  C C   . TRP A 1 28  ? 24.753  11.357  6.196   1.00 59.38  ? 328 TRP A C   1 
ATOM   142  O O   . TRP A 1 28  ? 24.318  12.507  6.166   1.00 55.53  ? 328 TRP A O   1 
ATOM   143  C CB  . TRP A 1 28  ? 26.472  11.933  4.431   1.00 60.10  ? 328 TRP A CB  1 
ATOM   144  C CG  . TRP A 1 28  ? 27.890  11.882  3.926   1.00 61.82  ? 328 TRP A CG  1 
ATOM   145  C CD1 . TRP A 1 28  ? 29.010  11.427  4.560   1.00 64.62  ? 328 TRP A CD1 1 
ATOM   146  C CD2 . TRP A 1 28  ? 28.349  12.391  2.661   1.00 62.69  ? 328 TRP A CD2 1 
ATOM   147  N NE1 . TRP A 1 28  ? 30.129  11.600  3.777   1.00 63.60  ? 328 TRP A NE1 1 
ATOM   148  C CE2 . TRP A 1 28  ? 29.750  12.199  2.612   1.00 64.89  ? 328 TRP A CE2 1 
ATOM   149  C CE3 . TRP A 1 28  ? 27.707  12.994  1.577   1.00 65.15  ? 328 TRP A CE3 1 
ATOM   150  C CZ2 . TRP A 1 28  ? 30.512  12.586  1.519   1.00 70.62  ? 328 TRP A CZ2 1 
ATOM   151  C CZ3 . TRP A 1 28  ? 28.466  13.395  0.500   1.00 69.97  ? 328 TRP A CZ3 1 
ATOM   152  C CH2 . TRP A 1 28  ? 29.847  13.196  0.477   1.00 73.30  ? 328 TRP A CH2 1 
ATOM   153  N N   . GLN A 1 29  ? 24.044  10.342  6.716   1.00 55.23  ? 329 GLN A N   1 
ATOM   154  C CA  . GLN A 1 29  ? 22.679  10.566  7.159   1.00 49.38  ? 329 GLN A CA  1 
ATOM   155  C C   . GLN A 1 29  ? 22.642  10.802  8.656   1.00 48.04  ? 329 GLN A C   1 
ATOM   156  O O   . GLN A 1 29  ? 23.556  10.439  9.402   1.00 47.37  ? 329 GLN A O   1 
ATOM   157  C CB  . GLN A 1 29  ? 21.661  9.446   6.989   1.00 47.09  ? 329 GLN A CB  1 
ATOM   158  C CG  . GLN A 1 29  ? 21.397  9.069   5.542   1.00 48.85  ? 329 GLN A CG  1 
ATOM   159  C CD  . GLN A 1 29  ? 20.582  10.082  4.781   1.00 46.05  ? 329 GLN A CD  1 
ATOM   160  O OE1 . GLN A 1 29  ? 19.427  10.327  5.088   1.00 49.23  ? 329 GLN A OE1 1 
ATOM   161  N NE2 . GLN A 1 29  ? 21.134  10.609  3.710   1.00 49.49  ? 329 GLN A NE2 1 
ATOM   162  N N   . THR A 1 30  ? 21.523  11.422  9.020   1.00 45.82  ? 330 THR A N   1 
ATOM   163  C CA  . THR A 1 30  ? 21.103  11.623  10.379  1.00 46.55  ? 330 THR A CA  1 
ATOM   164  C C   . THR A 1 30  ? 19.856  10.784  10.620  1.00 46.00  ? 330 THR A C   1 
ATOM   165  O O   . THR A 1 30  ? 18.820  11.001  10.010  1.00 52.58  ? 330 THR A O   1 
ATOM   166  C CB  . THR A 1 30  ? 20.802  13.100  10.569  1.00 48.21  ? 330 THR A CB  1 
ATOM   167  O OG1 . THR A 1 30  ? 22.005  13.850  10.520  1.00 52.29  ? 330 THR A OG1 1 
ATOM   168  C CG2 . THR A 1 30  ? 20.328  13.348  11.973  1.00 51.21  ? 330 THR A CG2 1 
ATOM   169  N N   . ALA A 1 31  ? 19.953  9.788   11.487  1.00 42.44  ? 331 ALA A N   1 
ATOM   170  C CA  . ALA A 1 31  ? 18.754  9.101   11.905  1.00 40.32  ? 331 ALA A CA  1 
ATOM   171  C C   . ALA A 1 31  ? 19.088  8.369   13.193  1.00 41.59  ? 331 ALA A C   1 
ATOM   172  O O   . ALA A 1 31  ? 20.271  8.216   13.501  1.00 42.26  ? 331 ALA A O   1 
ATOM   173  C CB  . ALA A 1 31  ? 18.295  8.199   10.805  1.00 39.88  ? 331 ALA A CB  1 
ATOM   174  N N   . ASP A 1 32  ? 18.070  8.025   13.987  1.00 41.09  ? 332 ASP A N   1 
ATOM   175  C CA  . ASP A 1 32  ? 18.318  7.137   15.101  1.00 45.54  ? 332 ASP A CA  1 
ATOM   176  C C   . ASP A 1 32  ? 19.144  5.925   14.634  1.00 44.18  ? 332 ASP A C   1 
ATOM   177  O O   . ASP A 1 32  ? 20.134  5.555   15.280  1.00 43.52  ? 332 ASP A O   1 
ATOM   178  C CB  . ASP A 1 32  ? 17.008  6.669   15.696  1.00 51.11  ? 332 ASP A CB  1 
ATOM   179  C CG  . ASP A 1 32  ? 16.147  7.754   16.307  1.00 53.34  ? 332 ASP A CG  1 
ATOM   180  O OD1 . ASP A 1 32  ? 16.733  8.781   16.690  1.00 56.11  ? 332 ASP A OD1 1 
ATOM   181  O OD2 . ASP A 1 32  ? 14.914  7.541   16.383  1.00 54.57  ? 332 ASP A OD2 1 
ATOM   182  N N   . VAL A 1 33  ? 18.738  5.325   13.502  1.00 39.10  ? 333 VAL A N   1 
ATOM   183  C CA  . VAL A 1 33  ? 19.377  4.119   13.023  1.00 40.47  ? 333 VAL A CA  1 
ATOM   184  C C   . VAL A 1 33  ? 19.701  4.278   11.551  1.00 39.85  ? 333 VAL A C   1 
ATOM   185  O O   . VAL A 1 33  ? 18.838  4.697   10.793  1.00 37.49  ? 333 VAL A O   1 
ATOM   186  C CB  . VAL A 1 33  ? 18.443  2.916   13.217  1.00 43.25  ? 333 VAL A CB  1 
ATOM   187  C CG1 . VAL A 1 33  ? 18.894  1.714   12.385  1.00 42.36  ? 333 VAL A CG1 1 
ATOM   188  C CG2 . VAL A 1 33  ? 18.260  2.567   14.695  1.00 44.80  ? 333 VAL A CG2 1 
ATOM   189  N N   . ILE A 1 34  ? 20.926  3.902   11.176  1.00 42.97  ? 334 ILE A N   1 
ATOM   190  C CA  . ILE A 1 34  ? 21.344  3.815   9.782   1.00 44.88  ? 334 ILE A CA  1 
ATOM   191  C C   . ILE A 1 34  ? 21.638  2.342   9.511   1.00 45.39  ? 334 ILE A C   1 
ATOM   192  O O   . ILE A 1 34  ? 22.279  1.680   10.321  1.00 43.66  ? 334 ILE A O   1 
ATOM   193  C CB  . ILE A 1 34  ? 22.572  4.709   9.516   1.00 47.12  ? 334 ILE A CB  1 
ATOM   194  C CG1 . ILE A 1 34  ? 22.236  6.180   9.657   1.00 49.52  ? 334 ILE A CG1 1 
ATOM   195  C CG2 . ILE A 1 34  ? 23.218  4.444   8.158   1.00 47.56  ? 334 ILE A CG2 1 
ATOM   196  C CD1 . ILE A 1 34  ? 23.461  7.073   9.727   1.00 50.16  ? 334 ILE A CD1 1 
ATOM   197  N N   . VAL A 1 35  ? 21.167  1.838   8.367   1.00 45.18  ? 335 VAL A N   1 
ATOM   198  C CA  . VAL A 1 35  ? 21.349  0.439   8.027   1.00 49.11  ? 335 VAL A CA  1 
ATOM   199  C C   . VAL A 1 35  ? 22.585  0.246   7.147   1.00 48.65  ? 335 VAL A C   1 
ATOM   200  O O   . VAL A 1 35  ? 22.699  0.827   6.069   1.00 48.96  ? 335 VAL A O   1 
ATOM   201  C CB  . VAL A 1 35  ? 20.113  -0.188  7.365   1.00 49.82  ? 335 VAL A CB  1 
ATOM   202  C CG1 . VAL A 1 35  ? 20.299  -1.687  7.186   1.00 53.82  ? 335 VAL A CG1 1 
ATOM   203  C CG2 . VAL A 1 35  ? 18.863  0.055   8.189   1.00 52.38  ? 335 VAL A CG2 1 
ATOM   204  N N   . ASN A 1 36  ? 23.474  -0.640  7.623   1.00 50.37  ? 336 ASN A N   1 
ATOM   205  C CA  . ASN A 1 36  ? 24.622  -1.120  6.873   1.00 48.92  ? 336 ASN A CA  1 
ATOM   206  C C   . ASN A 1 36  ? 24.243  -2.424  6.166   1.00 48.81  ? 336 ASN A C   1 
ATOM   207  O O   . ASN A 1 36  ? 23.271  -3.109  6.517   1.00 44.62  ? 336 ASN A O   1 
ATOM   208  C CB  . ASN A 1 36  ? 25.828  -1.287  7.793   1.00 51.11  ? 336 ASN A CB  1 
ATOM   209  C CG  . ASN A 1 36  ? 27.142  -1.319  7.049   1.00 54.73  ? 336 ASN A CG  1 
ATOM   210  O OD1 . ASN A 1 36  ? 27.174  -1.107  5.834   1.00 57.53  ? 336 ASN A OD1 1 
ATOM   211  N ND2 . ASN A 1 36  ? 28.245  -1.543  7.757   1.00 61.67  ? 336 ASN A ND2 1 
ATOM   212  N N   . SER A 1 37  ? 25.024  -2.743  5.138   1.00 49.94  ? 337 SER A N   1 
ATOM   213  C CA  . SER A 1 37  ? 24.832  -3.959  4.365   1.00 52.74  ? 337 SER A CA  1 
ATOM   214  C C   . SER A 1 37  ? 26.192  -4.604  4.096   1.00 53.73  ? 337 SER A C   1 
ATOM   215  O O   . SER A 1 37  ? 27.009  -4.019  3.365   1.00 51.51  ? 337 SER A O   1 
ATOM   216  C CB  . SER A 1 37  ? 24.107  -3.631  3.103   1.00 52.32  ? 337 SER A CB  1 
ATOM   217  O OG  . SER A 1 37  ? 23.583  -4.810  2.532   1.00 53.55  ? 337 SER A OG  1 
ATOM   218  N N   . VAL A 1 38  ? 26.443  -5.752  4.753   1.00 54.32  ? 338 VAL A N   1 
ATOM   219  C CA  . VAL A 1 38  ? 27.778  -6.332  4.803   1.00 59.03  ? 338 VAL A CA  1 
ATOM   220  C C   . VAL A 1 38  ? 27.756  -7.810  4.434   1.00 63.53  ? 338 VAL A C   1 
ATOM   221  O O   . VAL A 1 38  ? 26.762  -8.509  4.610   1.00 64.12  ? 338 VAL A O   1 
ATOM   222  C CB  . VAL A 1 38  ? 28.483  -6.230  6.162   1.00 57.80  ? 338 VAL A CB  1 
ATOM   223  C CG1 . VAL A 1 38  ? 28.646  -4.793  6.591   1.00 55.62  ? 338 VAL A CG1 1 
ATOM   224  C CG2 . VAL A 1 38  ? 27.774  -7.056  7.221   1.00 57.09  ? 338 VAL A CG2 1 
ATOM   225  N N   . ASN A 1 39  ? 28.923  -8.260  3.973   1.00 64.90  ? 339 ASN A N   1 
ATOM   226  C CA  . ASN A 1 39  ? 29.288  -9.658  4.014   1.00 67.12  ? 339 ASN A CA  1 
ATOM   227  C C   . ASN A 1 39  ? 29.947  -9.894  5.372   1.00 71.27  ? 339 ASN A C   1 
ATOM   228  O O   . ASN A 1 39  ? 30.930  -9.240  5.707   1.00 70.33  ? 339 ASN A O   1 
ATOM   229  C CB  . ASN A 1 39  ? 30.148  -9.997  2.805   1.00 68.09  ? 339 ASN A CB  1 
ATOM   230  C CG  . ASN A 1 39  ? 30.794  -11.353 2.883   1.00 71.72  ? 339 ASN A CG  1 
ATOM   231  O OD1 . ASN A 1 39  ? 30.724  -12.057 3.894   1.00 70.91  ? 339 ASN A OD1 1 
ATOM   232  N ND2 . ASN A 1 39  ? 31.436  -11.740 1.802   1.00 77.73  ? 339 ASN A ND2 1 
ATOM   233  N N   . PRO A 1 40  ? 29.421  -10.821 6.208   1.00 75.08  ? 340 PRO A N   1 
ATOM   234  C CA  . PRO A 1 40  ? 29.883  -10.951 7.593   1.00 75.31  ? 340 PRO A CA  1 
ATOM   235  C C   . PRO A 1 40  ? 31.347  -11.354 7.733   1.00 75.16  ? 340 PRO A C   1 
ATOM   236  O O   . PRO A 1 40  ? 31.968  -11.022 8.744   1.00 72.66  ? 340 PRO A O   1 
ATOM   237  C CB  . PRO A 1 40  ? 28.923  -11.971 8.236   1.00 80.18  ? 340 PRO A CB  1 
ATOM   238  C CG  . PRO A 1 40  ? 28.177  -12.645 7.077   1.00 79.20  ? 340 PRO A CG  1 
ATOM   239  C CD  . PRO A 1 40  ? 28.323  -11.744 5.873   1.00 76.69  ? 340 PRO A CD  1 
ATOM   240  N N   . HIS A 1 41  ? 31.877  -12.025 6.703   1.00 75.98  ? 341 HIS A N   1 
ATOM   241  C CA  . HIS A 1 41  ? 33.270  -12.434 6.681   1.00 81.59  ? 341 HIS A CA  1 
ATOM   242  C C   . HIS A 1 41  ? 34.168  -11.208 6.467   1.00 79.48  ? 341 HIS A C   1 
ATOM   243  O O   . HIS A 1 41  ? 35.312  -11.189 6.918   1.00 77.78  ? 341 HIS A O   1 
ATOM   244  C CB  . HIS A 1 41  ? 33.531  -13.536 5.639   1.00 89.19  ? 341 HIS A CB  1 
ATOM   245  C CG  . HIS A 1 41  ? 32.535  -14.655 5.549   1.00 94.74  ? 341 HIS A CG  1 
ATOM   246  N ND1 . HIS A 1 41  ? 32.638  -15.588 4.536   1.00 100.80 ? 341 HIS A ND1 1 
ATOM   247  C CD2 . HIS A 1 41  ? 31.475  -15.028 6.280   1.00 97.28  ? 341 HIS A CD2 1 
ATOM   248  C CE1 . HIS A 1 41  ? 31.665  -16.481 4.644   1.00 101.58 ? 341 HIS A CE1 1 
ATOM   249  N NE2 . HIS A 1 41  ? 30.937  -16.152 5.688   1.00 101.68 ? 341 HIS A NE2 1 
ATOM   250  N N   . ASP A 1 42  ? 33.651  -10.156 5.805   1.00 81.29  ? 342 ASP A N   1 
ATOM   251  C CA  . ASP A 1 42  ? 34.445  -8.965  5.515   1.00 77.80  ? 342 ASP A CA  1 
ATOM   252  C C   . ASP A 1 42  ? 33.544  -7.742  5.333   1.00 71.41  ? 342 ASP A C   1 
ATOM   253  O O   . ASP A 1 42  ? 32.886  -7.563  4.307   1.00 67.39  ? 342 ASP A O   1 
ATOM   254  C CB  . ASP A 1 42  ? 35.370  -9.218  4.332   1.00 81.27  ? 342 ASP A CB  1 
ATOM   255  C CG  . ASP A 1 42  ? 36.638  -8.381  4.301   1.00 84.45  ? 342 ASP A CG  1 
ATOM   256  O OD1 . ASP A 1 42  ? 36.620  -7.312  4.922   1.00 88.64  ? 342 ASP A OD1 1 
ATOM   257  O OD2 . ASP A 1 42  ? 37.640  -8.823  3.688   1.00 88.88  ? 342 ASP A OD2 1 
ATOM   258  N N   . ILE A 1 43  ? 33.552  -6.863  6.340   1.00 71.46  ? 343 ILE A N   1 
ATOM   259  C CA  . ILE A 1 43  ? 32.717  -5.670  6.317   1.00 67.37  ? 343 ILE A CA  1 
ATOM   260  C C   . ILE A 1 43  ? 33.463  -4.520  5.645   1.00 69.35  ? 343 ILE A C   1 
ATOM   261  O O   . ILE A 1 43  ? 32.978  -3.391  5.662   1.00 66.89  ? 343 ILE A O   1 
ATOM   262  C CB  . ILE A 1 43  ? 32.326  -5.272  7.742   1.00 66.20  ? 343 ILE A CB  1 
ATOM   263  C CG1 . ILE A 1 43  ? 33.560  -4.840  8.554   1.00 72.20  ? 343 ILE A CG1 1 
ATOM   264  C CG2 . ILE A 1 43  ? 31.571  -6.400  8.437   1.00 65.67  ? 343 ILE A CG2 1 
ATOM   265  C CD1 . ILE A 1 43  ? 33.280  -3.747  9.570   1.00 72.60  ? 343 ILE A CD1 1 
ATOM   266  N N   . THR A 1 44  ? 34.659  -4.799  5.106   1.00 71.84  ? 344 THR A N   1 
ATOM   267  C CA  . THR A 1 44  ? 35.470  -3.777  4.473   1.00 73.24  ? 344 THR A CA  1 
ATOM   268  C C   . THR A 1 44  ? 35.236  -3.799  2.967   1.00 73.80  ? 344 THR A C   1 
ATOM   269  O O   . THR A 1 44  ? 35.898  -3.077  2.230   1.00 79.66  ? 344 THR A O   1 
ATOM   270  C CB  . THR A 1 44  ? 36.943  -4.029  4.777   1.00 77.11  ? 344 THR A CB  1 
ATOM   271  O OG1 . THR A 1 44  ? 37.284  -5.053  3.842   1.00 79.88  ? 344 THR A OG1 1 
ATOM   272  C CG2 . THR A 1 44  ? 37.183  -4.384  6.233   1.00 77.01  ? 344 THR A CG2 1 
ATOM   273  N N   . VAL A 1 45  ? 34.310  -4.641  2.517   1.00 69.13  ? 345 VAL A N   1 
ATOM   274  C CA  . VAL A 1 45  ? 34.068  -4.821  1.103   1.00 69.90  ? 345 VAL A CA  1 
ATOM   275  C C   . VAL A 1 45  ? 32.626  -4.444  0.815   1.00 65.23  ? 345 VAL A C   1 
ATOM   276  O O   . VAL A 1 45  ? 31.759  -4.648  1.666   1.00 60.77  ? 345 VAL A O   1 
ATOM   277  C CB  . VAL A 1 45  ? 34.364  -6.293  0.758   1.00 77.23  ? 345 VAL A CB  1 
ATOM   278  C CG1 . VAL A 1 45  ? 34.158  -6.611  -0.717  1.00 77.62  ? 345 VAL A CG1 1 
ATOM   279  C CG2 . VAL A 1 45  ? 35.773  -6.679  1.197   1.00 84.36  ? 345 VAL A CG2 1 
ATOM   280  N N   . GLY A 1 46  ? 32.417  -3.919  -0.400  1.00 67.85  ? 346 GLY A N   1 
ATOM   281  C CA  . GLY A 1 46  ? 31.114  -3.465  -0.857  1.00 67.79  ? 346 GLY A CA  1 
ATOM   282  C C   . GLY A 1 46  ? 30.958  -1.945  -0.744  1.00 65.74  ? 346 GLY A C   1 
ATOM   283  O O   . GLY A 1 46  ? 31.433  -1.337  0.212   1.00 65.29  ? 346 GLY A O   1 
ATOM   284  N N   . PRO A 1 47  ? 30.282  -1.292  -1.719  1.00 67.81  ? 347 PRO A N   1 
ATOM   285  C CA  . PRO A 1 47  ? 30.018  0.156   -1.670  1.00 68.14  ? 347 PRO A CA  1 
ATOM   286  C C   . PRO A 1 47  ? 29.588  0.733   -0.311  1.00 64.81  ? 347 PRO A C   1 
ATOM   287  O O   . PRO A 1 47  ? 30.308  1.541   0.275   1.00 65.05  ? 347 PRO A O   1 
ATOM   288  C CB  . PRO A 1 47  ? 28.932  0.337   -2.759  1.00 67.37  ? 347 PRO A CB  1 
ATOM   289  C CG  . PRO A 1 47  ? 29.221  -0.760  -3.754  1.00 74.32  ? 347 PRO A CG  1 
ATOM   290  C CD  . PRO A 1 47  ? 29.793  -1.920  -2.955  1.00 71.97  ? 347 PRO A CD  1 
ATOM   291  N N   . VAL A 1 48  ? 28.433  0.292   0.203   1.00 60.03  ? 348 VAL A N   1 
ATOM   292  C CA  . VAL A 1 48  ? 27.857  0.771   1.454   1.00 55.51  ? 348 VAL A CA  1 
ATOM   293  C C   . VAL A 1 48  ? 28.784  0.455   2.631   1.00 56.77  ? 348 VAL A C   1 
ATOM   294  O O   . VAL A 1 48  ? 29.109  1.314   3.435   1.00 61.52  ? 348 VAL A O   1 
ATOM   295  C CB  . VAL A 1 48  ? 26.466  0.115   1.604   1.00 53.49  ? 348 VAL A CB  1 
ATOM   296  C CG1 . VAL A 1 48  ? 25.840  0.322   2.978   1.00 54.37  ? 348 VAL A CG1 1 
ATOM   297  C CG2 . VAL A 1 48  ? 25.500  0.569   0.511   1.00 51.86  ? 348 VAL A CG2 1 
ATOM   298  N N   . ALA A 1 49  ? 29.263  -0.777  2.722   1.00 59.03  ? 349 ALA A N   1 
ATOM   299  C CA  . ALA A 1 49  ? 30.083  -1.175  3.854   1.00 61.49  ? 349 ALA A CA  1 
ATOM   300  C C   . ALA A 1 49  ? 31.301  -0.264  3.995   1.00 64.75  ? 349 ALA A C   1 
ATOM   301  O O   . ALA A 1 49  ? 31.745  0.014   5.103   1.00 65.47  ? 349 ALA A O   1 
ATOM   302  C CB  . ALA A 1 49  ? 30.500  -2.615  3.690   1.00 60.75  ? 349 ALA A CB  1 
ATOM   303  N N   . LYS A 1 50  ? 31.871  0.148   2.861   1.00 69.99  ? 350 LYS A N   1 
ATOM   304  C CA  . LYS A 1 50  ? 33.083  0.952   2.841   1.00 75.57  ? 350 LYS A CA  1 
ATOM   305  C C   . LYS A 1 50  ? 32.769  2.386   3.259   1.00 72.70  ? 350 LYS A C   1 
ATOM   306  O O   . LYS A 1 50  ? 33.381  2.901   4.203   1.00 79.67  ? 350 LYS A O   1 
ATOM   307  C CB  . LYS A 1 50  ? 33.713  0.924   1.447   1.00 79.55  ? 350 LYS A CB  1 
ATOM   308  C CG  . LYS A 1 50  ? 34.663  -0.235  1.210   1.00 90.73  ? 350 LYS A CG  1 
ATOM   309  C CD  . LYS A 1 50  ? 34.671  -0.829  -0.202  1.00 98.57  ? 350 LYS A CD  1 
ATOM   310  C CE  . LYS A 1 50  ? 34.470  0.161   -1.317  1.00 100.64 ? 350 LYS A CE  1 
ATOM   311  N NZ  . LYS A 1 50  ? 35.034  -0.315  -2.582  1.00 101.38 ? 350 LYS A NZ  1 
ATOM   312  N N   . SER A 1 51  ? 31.828  3.013   2.535   1.00 61.92  ? 351 SER A N   1 
ATOM   313  C CA  . SER A 1 51  ? 31.336  4.341   2.866   1.00 59.40  ? 351 SER A CA  1 
ATOM   314  C C   . SER A 1 51  ? 31.138  4.485   4.377   1.00 57.62  ? 351 SER A C   1 
ATOM   315  O O   . SER A 1 51  ? 31.585  5.453   4.989   1.00 62.54  ? 351 SER A O   1 
ATOM   316  C CB  . SER A 1 51  ? 30.052  4.614   2.135   1.00 57.09  ? 351 SER A CB  1 
ATOM   317  O OG  . SER A 1 51  ? 30.229  4.445   0.738   1.00 59.11  ? 351 SER A OG  1 
ATOM   318  N N   . ILE A 1 52  ? 30.475  3.483   4.961   1.00 54.61  ? 352 ILE A N   1 
ATOM   319  C CA  . ILE A 1 52  ? 30.095  3.472   6.357   1.00 51.93  ? 352 ILE A CA  1 
ATOM   320  C C   . ILE A 1 52  ? 31.327  3.322   7.226   1.00 57.46  ? 352 ILE A C   1 
ATOM   321  O O   . ILE A 1 52  ? 31.454  4.024   8.218   1.00 65.54  ? 352 ILE A O   1 
ATOM   322  C CB  . ILE A 1 52  ? 29.025  2.391   6.588   1.00 46.74  ? 352 ILE A CB  1 
ATOM   323  C CG1 . ILE A 1 52  ? 27.675  2.922   6.056   1.00 44.59  ? 352 ILE A CG1 1 
ATOM   324  C CG2 . ILE A 1 52  ? 28.973  1.950   8.042   1.00 46.60  ? 352 ILE A CG2 1 
ATOM   325  C CD1 . ILE A 1 52  ? 26.432  2.286   6.634   1.00 43.89  ? 352 ILE A CD1 1 
ATOM   326  N N   . LEU A 1 53  ? 32.235  2.436   6.828   1.00 65.08  ? 353 LEU A N   1 
ATOM   327  C CA  . LEU A 1 53  ? 33.422  2.137   7.612   1.00 72.26  ? 353 LEU A CA  1 
ATOM   328  C C   . LEU A 1 53  ? 34.311  3.371   7.675   1.00 72.31  ? 353 LEU A C   1 
ATOM   329  O O   . LEU A 1 53  ? 34.859  3.658   8.735   1.00 75.30  ? 353 LEU A O   1 
ATOM   330  C CB  . LEU A 1 53  ? 34.186  0.931   7.052   1.00 78.96  ? 353 LEU A CB  1 
ATOM   331  C CG  . LEU A 1 53  ? 35.469  0.532   7.799   1.00 86.23  ? 353 LEU A CG  1 
ATOM   332  C CD1 . LEU A 1 53  ? 35.255  0.241   9.297   1.00 87.57  ? 353 LEU A CD1 1 
ATOM   333  C CD2 . LEU A 1 53  ? 36.117  -0.666  7.114   1.00 85.03  ? 353 LEU A CD2 1 
ATOM   334  N N   . GLN A 1 54  ? 34.475  4.058   6.536   1.00 75.21  ? 354 GLN A N   1 
ATOM   335  C CA  . GLN A 1 54  ? 35.268  5.280   6.484   1.00 82.21  ? 354 GLN A CA  1 
ATOM   336  C C   . GLN A 1 54  ? 34.646  6.331   7.388   1.00 79.38  ? 354 GLN A C   1 
ATOM   337  O O   . GLN A 1 54  ? 35.318  6.863   8.262   1.00 83.80  ? 354 GLN A O   1 
ATOM   338  C CB  . GLN A 1 54  ? 35.307  6.023   5.153   1.00 85.70  ? 354 GLN A CB  1 
ATOM   339  C CG  . GLN A 1 54  ? 36.426  5.585   4.227   1.00 94.67  ? 354 GLN A CG  1 
ATOM   340  C CD  . GLN A 1 54  ? 36.357  6.350   2.928   1.00 100.93 ? 354 GLN A CD  1 
ATOM   341  O OE1 . GLN A 1 54  ? 35.320  6.375   2.249   1.00 97.88  ? 354 GLN A OE1 1 
ATOM   342  N NE2 . GLN A 1 54  ? 37.446  7.034   2.614   1.00 109.32 ? 354 GLN A NE2 1 
ATOM   343  N N   . GLN A 1 55  ? 33.359  6.603   7.175   1.00 71.72  ? 355 GLN A N   1 
ATOM   344  C CA  . GLN A 1 55  ? 32.703  7.676   7.893   1.00 72.59  ? 355 GLN A CA  1 
ATOM   345  C C   . GLN A 1 55  ? 32.645  7.384   9.389   1.00 69.74  ? 355 GLN A C   1 
ATOM   346  O O   . GLN A 1 55  ? 32.737  8.311   10.188  1.00 75.43  ? 355 GLN A O   1 
ATOM   347  C CB  . GLN A 1 55  ? 31.292  7.915   7.356   1.00 73.18  ? 355 GLN A CB  1 
ATOM   348  C CG  . GLN A 1 55  ? 30.662  9.217   7.841   1.00 71.60  ? 355 GLN A CG  1 
ATOM   349  C CD  . GLN A 1 55  ? 31.506  10.433  7.526   1.00 72.58  ? 355 GLN A CD  1 
ATOM   350  O OE1 . GLN A 1 55  ? 31.957  10.643  6.394   1.00 65.76  ? 355 GLN A OE1 1 
ATOM   351  N NE2 . GLN A 1 55  ? 31.742  11.237  8.550   1.00 76.41  ? 355 GLN A NE2 1 
ATOM   352  N N   . ALA A 1 56  ? 32.453  6.118   9.774   1.00 66.73  ? 356 ALA A N   1 
ATOM   353  C CA  . ALA A 1 56  ? 32.145  5.803   11.162  1.00 69.92  ? 356 ALA A CA  1 
ATOM   354  C C   . ALA A 1 56  ? 33.420  5.653   11.993  1.00 75.87  ? 356 ALA A C   1 
ATOM   355  O O   . ALA A 1 56  ? 33.399  5.808   13.225  1.00 73.38  ? 356 ALA A O   1 
ATOM   356  C CB  . ALA A 1 56  ? 31.294  4.564   11.230  1.00 65.14  ? 356 ALA A CB  1 
ATOM   357  N N   . GLY A 1 57  ? 34.511  5.316   11.292  1.00 81.27  ? 357 GLY A N   1 
ATOM   358  C CA  . GLY A 1 57  ? 35.839  5.269   11.881  1.00 89.90  ? 357 GLY A CA  1 
ATOM   359  C C   . GLY A 1 57  ? 36.231  3.848   12.264  1.00 90.16  ? 357 GLY A C   1 
ATOM   360  O O   . GLY A 1 57  ? 35.382  2.961   12.310  1.00 84.75  ? 357 GLY A O   1 
ATOM   361  N N   . VAL A 1 58  ? 37.516  3.681   12.594  1.00 96.94  ? 358 VAL A N   1 
ATOM   362  C CA  . VAL A 1 58  ? 38.117  2.377   12.844  1.00 100.03 ? 358 VAL A CA  1 
ATOM   363  C C   . VAL A 1 58  ? 37.438  1.670   14.026  1.00 101.24 ? 358 VAL A C   1 
ATOM   364  O O   . VAL A 1 58  ? 37.409  0.437   14.052  1.00 99.65  ? 358 VAL A O   1 
ATOM   365  C CB  . VAL A 1 58  ? 39.645  2.500   13.066  1.00 102.11 ? 358 VAL A CB  1 
ATOM   366  C CG1 . VAL A 1 58  ? 39.995  3.137   14.412  1.00 104.88 ? 358 VAL A CG1 1 
ATOM   367  C CG2 . VAL A 1 58  ? 40.362  1.160   12.921  1.00 102.22 ? 358 VAL A CG2 1 
ATOM   368  N N   . GLU A 1 59  ? 36.906  2.438   14.999  1.00 96.16  ? 359 GLU A N   1 
ATOM   369  C CA  . GLU A 1 59  ? 36.387  1.876   16.240  1.00 94.34  ? 359 GLU A CA  1 
ATOM   370  C C   . GLU A 1 59  ? 35.072  1.133   16.003  1.00 89.18  ? 359 GLU A C   1 
ATOM   371  O O   . GLU A 1 59  ? 34.629  0.382   16.865  1.00 89.78  ? 359 GLU A O   1 
ATOM   372  C CB  . GLU A 1 59  ? 36.159  2.949   17.305  1.00 95.97  ? 359 GLU A CB  1 
ATOM   373  C CG  . GLU A 1 59  ? 37.430  3.710   17.670  1.00 102.58 ? 359 GLU A CG  1 
ATOM   374  C CD  . GLU A 1 59  ? 37.259  4.687   18.817  1.00 107.36 ? 359 GLU A CD  1 
ATOM   375  O OE1 . GLU A 1 59  ? 36.975  4.192   19.923  1.00 114.58 ? 359 GLU A OE1 1 
ATOM   376  O OE2 . GLU A 1 59  ? 37.396  5.917   18.626  1.00 105.86 ? 359 GLU A OE2 1 
ATOM   377  N N   . MET A 1 60  ? 34.445  1.371   14.845  1.00 85.07  ? 360 MET A N   1 
ATOM   378  C CA  . MET A 1 60  ? 33.189  0.736   14.477  1.00 81.13  ? 360 MET A CA  1 
ATOM   379  C C   . MET A 1 60  ? 33.413  -0.735  14.112  1.00 79.03  ? 360 MET A C   1 
ATOM   380  O O   . MET A 1 60  ? 32.568  -1.586  14.378  1.00 73.67  ? 360 MET A O   1 
ATOM   381  C CB  . MET A 1 60  ? 32.588  1.494   13.291  1.00 79.01  ? 360 MET A CB  1 
ATOM   382  C CG  . MET A 1 60  ? 31.149  1.144   12.968  1.00 77.14  ? 360 MET A CG  1 
ATOM   383  S SD  . MET A 1 60  ? 30.968  -0.137  11.718  1.00 82.71  ? 360 MET A SD  1 
ATOM   384  C CE  . MET A 1 60  ? 31.702  0.456   10.186  1.00 79.55  ? 360 MET A CE  1 
ATOM   385  N N   . LYS A 1 61  ? 34.566  -1.013  13.493  1.00 80.70  ? 361 LYS A N   1 
ATOM   386  C CA  . LYS A 1 61  ? 34.958  -2.352  13.084  1.00 82.07  ? 361 LYS A CA  1 
ATOM   387  C C   . LYS A 1 61  ? 35.388  -3.192  14.290  1.00 88.87  ? 361 LYS A C   1 
ATOM   388  O O   . LYS A 1 61  ? 35.377  -4.417  14.193  1.00 93.15  ? 361 LYS A O   1 
ATOM   389  C CB  . LYS A 1 61  ? 36.078  -2.226  12.044  1.00 83.94  ? 361 LYS A CB  1 
ATOM   390  C CG  . LYS A 1 61  ? 36.648  -3.525  11.493  1.00 85.13  ? 361 LYS A CG  1 
ATOM   391  C CD  . LYS A 1 61  ? 37.863  -3.361  10.589  1.00 87.21  ? 361 LYS A CD  1 
ATOM   392  C CE  . LYS A 1 61  ? 38.303  -4.722  10.157  1.00 90.20  ? 361 LYS A CE  1 
ATOM   393  N NZ  . LYS A 1 61  ? 39.509  -4.668  9.340   1.00 94.30  ? 361 LYS A NZ  1 
ATOM   394  N N   . SER A 1 62  ? 35.777  -2.553  15.410  1.00 90.46  ? 362 SER A N   1 
ATOM   395  C CA  . SER A 1 62  ? 36.128  -3.278  16.626  1.00 92.72  ? 362 SER A CA  1 
ATOM   396  C C   . SER A 1 62  ? 34.884  -3.848  17.302  1.00 96.34  ? 362 SER A C   1 
ATOM   397  O O   . SER A 1 62  ? 34.825  -5.045  17.578  1.00 105.29 ? 362 SER A O   1 
ATOM   398  C CB  . SER A 1 62  ? 36.893  -2.434  17.590  1.00 92.80  ? 362 SER A CB  1 
ATOM   399  O OG  . SER A 1 62  ? 38.195  -2.216  17.091  1.00 94.16  ? 362 SER A OG  1 
ATOM   400  N N   . GLU A 1 63  ? 33.894  -2.994  17.583  1.00 94.61  ? 363 GLU A N   1 
ATOM   401  C CA  . GLU A 1 63  ? 32.705  -3.459  18.275  1.00 95.47  ? 363 GLU A CA  1 
ATOM   402  C C   . GLU A 1 63  ? 31.979  -4.474  17.390  1.00 89.45  ? 363 GLU A C   1 
ATOM   403  O O   . GLU A 1 63  ? 31.287  -5.342  17.911  1.00 90.57  ? 363 GLU A O   1 
ATOM   404  C CB  . GLU A 1 63  ? 31.779  -2.318  18.694  1.00 97.84  ? 363 GLU A CB  1 
ATOM   405  C CG  . GLU A 1 63  ? 30.761  -2.721  19.762  1.00 105.49 ? 363 GLU A CG  1 
ATOM   406  C CD  . GLU A 1 63  ? 29.550  -1.804  19.900  1.00 110.72 ? 363 GLU A CD  1 
ATOM   407  O OE1 . GLU A 1 63  ? 29.386  -0.887  19.068  1.00 109.08 ? 363 GLU A OE1 1 
ATOM   408  O OE2 . GLU A 1 63  ? 28.755  -1.988  20.847  1.00 114.64 ? 363 GLU A OE2 1 
ATOM   409  N N   . PHE A 1 64  ? 32.157  -4.380  16.062  1.00 82.09  ? 364 PHE A N   1 
ATOM   410  C CA  . PHE A 1 64  ? 31.526  -5.297  15.120  1.00 78.02  ? 364 PHE A CA  1 
ATOM   411  C C   . PHE A 1 64  ? 32.165  -6.692  15.140  1.00 79.44  ? 364 PHE A C   1 
ATOM   412  O O   . PHE A 1 64  ? 31.457  -7.695  15.038  1.00 76.76  ? 364 PHE A O   1 
ATOM   413  C CB  . PHE A 1 64  ? 31.601  -4.809  13.675  1.00 71.19  ? 364 PHE A CB  1 
ATOM   414  C CG  . PHE A 1 64  ? 30.916  -5.762  12.705  1.00 70.90  ? 364 PHE A CG  1 
ATOM   415  C CD1 . PHE A 1 64  ? 31.554  -6.915  12.253  1.00 72.55  ? 364 PHE A CD1 1 
ATOM   416  C CD2 . PHE A 1 64  ? 29.634  -5.497  12.228  1.00 68.94  ? 364 PHE A CD2 1 
ATOM   417  C CE1 . PHE A 1 64  ? 30.930  -7.770  11.350  1.00 70.80  ? 364 PHE A CE1 1 
ATOM   418  C CE2 . PHE A 1 64  ? 29.016  -6.358  11.322  1.00 68.30  ? 364 PHE A CE2 1 
ATOM   419  C CZ  . PHE A 1 64  ? 29.664  -7.499  10.889  1.00 67.02  ? 364 PHE A CZ  1 
ATOM   420  N N   . LEU A 1 65  ? 33.503  -6.755  15.208  1.00 81.83  ? 365 LEU A N   1 
ATOM   421  C CA  . LEU A 1 65  ? 34.223  -8.026  15.251  1.00 85.43  ? 365 LEU A CA  1 
ATOM   422  C C   . LEU A 1 65  ? 34.102  -8.653  16.638  1.00 90.66  ? 365 LEU A C   1 
ATOM   423  O O   . LEU A 1 65  ? 34.288  -9.851  16.766  1.00 95.10  ? 365 LEU A O   1 
ATOM   424  C CB  . LEU A 1 65  ? 35.696  -7.908  14.851  1.00 85.24  ? 365 LEU A CB  1 
ATOM   425  C CG  . LEU A 1 65  ? 35.972  -7.527  13.391  1.00 82.27  ? 365 LEU A CG  1 
ATOM   426  C CD1 . LEU A 1 65  ? 37.437  -7.146  13.232  1.00 84.98  ? 365 LEU A CD1 1 
ATOM   427  C CD2 . LEU A 1 65  ? 35.573  -8.595  12.377  1.00 81.08  ? 365 LEU A CD2 1 
ATOM   428  N N   . ALA A 1 66  ? 33.778  -7.860  17.667  1.00 93.90  ? 366 ALA A N   1 
ATOM   429  C CA  . ALA A 1 66  ? 33.746  -8.350  19.038  1.00 98.38  ? 366 ALA A CA  1 
ATOM   430  C C   . ALA A 1 66  ? 32.357  -8.853  19.440  1.00 99.04  ? 366 ALA A C   1 
ATOM   431  O O   . ALA A 1 66  ? 32.203  -9.435  20.513  1.00 102.21 ? 366 ALA A O   1 
ATOM   432  C CB  . ALA A 1 66  ? 34.217  -7.257  19.972  1.00 99.88  ? 366 ALA A CB  1 
ATOM   433  N N   . THR A 1 67  ? 31.349  -8.618  18.592  1.00 98.95  ? 367 THR A N   1 
ATOM   434  C CA  . THR A 1 67  ? 29.966  -8.938  18.916  1.00 103.30 ? 367 THR A CA  1 
ATOM   435  C C   . THR A 1 67  ? 29.383  -10.007 17.988  1.00 110.82 ? 367 THR A C   1 
ATOM   436  O O   . THR A 1 67  ? 28.257  -10.455 18.210  1.00 110.84 ? 367 THR A O   1 
ATOM   437  C CB  . THR A 1 67  ? 29.140  -7.659  18.854  1.00 99.79  ? 367 THR A CB  1 
ATOM   438  O OG1 . THR A 1 67  ? 29.395  -7.171  17.541  1.00 94.09  ? 367 THR A OG1 1 
ATOM   439  C CG2 . THR A 1 67  ? 29.505  -6.679  19.957  1.00 101.97 ? 367 THR A CG2 1 
ATOM   440  N N   . LYS A 1 68  ? 30.115  -10.379 16.928  1.00 119.38 ? 368 LYS A N   1 
ATOM   441  C CA  . LYS A 1 68  ? 29.844  -11.617 16.208  1.00 123.52 ? 368 LYS A CA  1 
ATOM   442  C C   . LYS A 1 68  ? 30.472  -12.751 17.033  1.00 132.10 ? 368 LYS A C   1 
ATOM   443  O O   . LYS A 1 68  ? 31.617  -12.615 17.478  1.00 140.83 ? 368 LYS A O   1 
ATOM   444  C CB  . LYS A 1 68  ? 30.350  -11.386 14.773  1.00 125.21 ? 368 LYS A CB  1 
ATOM   445  C CG  . LYS A 1 68  ? 29.967  -12.459 13.767  1.00 136.68 ? 368 LYS A CG  1 
ATOM   446  C CD  . LYS A 1 68  ? 30.750  -12.450 12.456  1.00 138.23 ? 368 LYS A CD  1 
ATOM   447  C CE  . LYS A 1 68  ? 30.524  -13.716 11.667  1.00 143.00 ? 368 LYS A CE  1 
ATOM   448  N NZ  . LYS A 1 68  ? 29.106  -13.916 11.337  1.00 145.82 ? 368 LYS A NZ  1 
ATOM   449  N N   . ALA A 1 69  ? 29.715  -13.830 17.323  1.00 128.28 ? 369 ALA A N   1 
ATOM   450  C CA  . ALA A 1 69  ? 30.174  -14.876 18.235  1.00 121.62 ? 369 ALA A CA  1 
ATOM   451  C C   . ALA A 1 69  ? 29.281  -16.112 18.118  1.00 122.27 ? 369 ALA A C   1 
ATOM   452  O O   . ALA A 1 69  ? 29.841  -17.231 18.157  1.00 128.05 ? 369 ALA A O   1 
ATOM   453  C CB  . ALA A 1 69  ? 30.210  -14.361 19.660  1.00 118.98 ? 369 ALA A CB  1 
ATOM   454  N N   . ARG A 1 74  ? 26.560  -18.283 12.700  1.00 140.85 ? 374 ARG A N   1 
ATOM   455  C CA  . ARG A 1 74  ? 25.496  -17.842 13.640  1.00 145.01 ? 374 ARG A CA  1 
ATOM   456  C C   . ARG A 1 74  ? 24.314  -17.266 12.858  1.00 142.95 ? 374 ARG A C   1 
ATOM   457  O O   . ARG A 1 74  ? 24.496  -16.631 11.820  1.00 141.79 ? 374 ARG A O   1 
ATOM   458  C CB  . ARG A 1 74  ? 26.053  -16.810 14.627  1.00 150.73 ? 374 ARG A CB  1 
ATOM   459  C CG  . ARG A 1 74  ? 25.060  -16.297 15.661  1.00 161.71 ? 374 ARG A CG  1 
ATOM   460  C CD  . ARG A 1 74  ? 25.680  -15.330 16.663  1.00 169.48 ? 374 ARG A CD  1 
ATOM   461  N NE  . ARG A 1 74  ? 24.793  -14.804 17.711  1.00 170.31 ? 374 ARG A NE  1 
ATOM   462  C CZ  . ARG A 1 74  ? 25.147  -14.104 18.786  1.00 166.39 ? 374 ARG A CZ  1 
ATOM   463  N NH1 . ARG A 1 74  ? 26.314  -13.491 18.838  1.00 171.66 ? 374 ARG A NH1 1 
ATOM   464  N NH2 . ARG A 1 74  ? 24.297  -13.970 19.793  1.00 157.75 ? 374 ARG A NH2 1 
ATOM   465  N N   . SER A 1 75  ? 23.106  -17.460 13.403  1.00 138.73 ? 375 SER A N   1 
ATOM   466  C CA  . SER A 1 75  ? 21.867  -17.091 12.724  1.00 127.74 ? 375 SER A CA  1 
ATOM   467  C C   . SER A 1 75  ? 21.569  -15.581 12.771  1.00 123.24 ? 375 SER A C   1 
ATOM   468  O O   . SER A 1 75  ? 20.692  -15.132 12.039  1.00 130.65 ? 375 SER A O   1 
ATOM   469  C CB  . SER A 1 75  ? 20.705  -17.914 13.253  1.00 122.31 ? 375 SER A CB  1 
ATOM   470  O OG  . SER A 1 75  ? 20.831  -18.183 14.641  1.00 123.38 ? 375 SER A OG  1 
ATOM   471  N N   . GLN A 1 76  ? 22.279  -14.798 13.608  1.00 110.33 ? 376 GLN A N   1 
ATOM   472  C CA  . GLN A 1 76  ? 22.130  -13.351 13.664  1.00 95.54  ? 376 GLN A CA  1 
ATOM   473  C C   . GLN A 1 76  ? 22.125  -12.799 12.239  1.00 92.46  ? 376 GLN A C   1 
ATOM   474  O O   . GLN A 1 76  ? 23.115  -12.901 11.533  1.00 95.23  ? 376 GLN A O   1 
ATOM   475  C CB  . GLN A 1 76  ? 23.234  -12.701 14.507  1.00 98.80  ? 376 GLN A CB  1 
ATOM   476  C CG  . GLN A 1 76  ? 24.656  -13.159 14.173  1.00 109.92 ? 376 GLN A CG  1 
ATOM   477  C CD  . GLN A 1 76  ? 25.765  -12.429 14.911  1.00 115.31 ? 376 GLN A CD  1 
ATOM   478  O OE1 . GLN A 1 76  ? 26.933  -12.839 14.890  1.00 118.97 ? 376 GLN A OE1 1 
ATOM   479  N NE2 . GLN A 1 76  ? 25.425  -11.342 15.587  1.00 114.86 ? 376 GLN A NE2 1 
ATOM   480  N N   . LEU A 1 77  ? 20.991  -12.247 11.793  1.00 88.55  ? 377 LEU A N   1 
ATOM   481  C CA  . LEU A 1 77  ? 20.887  -11.641 10.472  1.00 83.04  ? 377 LEU A CA  1 
ATOM   482  C C   . LEU A 1 77  ? 21.207  -10.138 10.515  1.00 74.97  ? 377 LEU A C   1 
ATOM   483  O O   . LEU A 1 77  ? 21.725  -9.567  9.554   1.00 71.39  ? 377 LEU A O   1 
ATOM   484  C CB  . LEU A 1 77  ? 19.459  -11.928 10.011  1.00 87.87  ? 377 LEU A CB  1 
ATOM   485  C CG  . LEU A 1 77  ? 19.097  -11.519 8.582   1.00 91.19  ? 377 LEU A CG  1 
ATOM   486  C CD1 . LEU A 1 77  ? 19.925  -12.226 7.529   1.00 94.36  ? 377 LEU A CD1 1 
ATOM   487  C CD2 . LEU A 1 77  ? 17.628  -11.795 8.358   1.00 94.43  ? 377 LEU A CD2 1 
ATOM   488  N N   . VAL A 1 78  ? 20.903  -9.494  11.651  1.00 69.39  ? 378 VAL A N   1 
ATOM   489  C CA  . VAL A 1 78  ? 21.160  -8.085  11.881  1.00 58.62  ? 378 VAL A CA  1 
ATOM   490  C C   . VAL A 1 78  ? 21.990  -7.937  13.148  1.00 58.64  ? 378 VAL A C   1 
ATOM   491  O O   . VAL A 1 78  ? 21.502  -8.209  14.241  1.00 63.72  ? 378 VAL A O   1 
ATOM   492  C CB  . VAL A 1 78  ? 19.824  -7.354  12.044  1.00 59.82  ? 378 VAL A CB  1 
ATOM   493  C CG1 . VAL A 1 78  ? 20.032  -5.884  12.410  1.00 69.41  ? 378 VAL A CG1 1 
ATOM   494  C CG2 . VAL A 1 78  ? 18.954  -7.457  10.809  1.00 57.70  ? 378 VAL A CG2 1 
ATOM   495  N N   . LEU A 1 79  ? 23.240  -7.503  12.988  1.00 57.57  ? 379 LEU A N   1 
ATOM   496  C CA  . LEU A 1 79  ? 24.111  -7.143  14.098  1.00 61.13  ? 379 LEU A CA  1 
ATOM   497  C C   . LEU A 1 79  ? 23.909  -5.655  14.430  1.00 64.13  ? 379 LEU A C   1 
ATOM   498  O O   . LEU A 1 79  ? 23.803  -4.806  13.542  1.00 61.81  ? 379 LEU A O   1 
ATOM   499  C CB  . LEU A 1 79  ? 25.539  -7.462  13.651  1.00 61.98  ? 379 LEU A CB  1 
ATOM   500  C CG  . LEU A 1 79  ? 26.623  -7.574  14.729  1.00 67.21  ? 379 LEU A CG  1 
ATOM   501  C CD1 . LEU A 1 79  ? 27.881  -8.261  14.228  1.00 68.06  ? 379 LEU A CD1 1 
ATOM   502  C CD2 . LEU A 1 79  ? 27.006  -6.207  15.251  1.00 71.28  ? 379 LEU A CD2 1 
ATOM   503  N N   . VAL A 1 80  ? 23.843  -5.327  15.722  1.00 66.18  ? 380 VAL A N   1 
ATOM   504  C CA  . VAL A 1 80  ? 23.590  -3.964  16.140  1.00 65.58  ? 380 VAL A CA  1 
ATOM   505  C C   . VAL A 1 80  ? 24.815  -3.383  16.830  1.00 70.43  ? 380 VAL A C   1 
ATOM   506  O O   . VAL A 1 80  ? 25.364  -3.981  17.745  1.00 71.28  ? 380 VAL A O   1 
ATOM   507  C CB  . VAL A 1 80  ? 22.364  -3.974  17.056  1.00 69.59  ? 380 VAL A CB  1 
ATOM   508  C CG1 . VAL A 1 80  ? 22.191  -2.642  17.768  1.00 75.39  ? 380 VAL A CG1 1 
ATOM   509  C CG2 . VAL A 1 80  ? 21.112  -4.334  16.265  1.00 68.89  ? 380 VAL A CG2 1 
ATOM   510  N N   . THR A 1 81  ? 25.238  -2.197  16.385  1.00 72.66  ? 381 THR A N   1 
ATOM   511  C CA  . THR A 1 81  ? 26.289  -1.467  17.081  1.00 79.32  ? 381 THR A CA  1 
ATOM   512  C C   . THR A 1 81  ? 25.840  -0.025  17.317  1.00 78.92  ? 381 THR A C   1 
ATOM   513  O O   . THR A 1 81  ? 24.762  0.386   16.895  1.00 75.61  ? 381 THR A O   1 
ATOM   514  C CB  . THR A 1 81  ? 27.603  -1.546  16.302  1.00 79.93  ? 381 THR A CB  1 
ATOM   515  O OG1 . THR A 1 81  ? 27.420  -0.921  15.032  1.00 75.70  ? 381 THR A OG1 1 
ATOM   516  C CG2 . THR A 1 81  ? 28.065  -2.984  16.124  1.00 81.59  ? 381 THR A CG2 1 
ATOM   517  N N   . LYS A 1 82  ? 26.660  0.720   18.055  1.00 80.68  ? 382 LYS A N   1 
ATOM   518  C CA  . LYS A 1 82  ? 26.486  2.153   18.188  1.00 74.59  ? 382 LYS A CA  1 
ATOM   519  C C   . LYS A 1 82  ? 26.857  2.765   16.843  1.00 66.06  ? 382 LYS A C   1 
ATOM   520  O O   . LYS A 1 82  ? 27.274  2.027   15.943  1.00 63.10  ? 382 LYS A O   1 
ATOM   521  C CB  . LYS A 1 82  ? 27.363  2.691   19.324  1.00 80.35  ? 382 LYS A CB  1 
ATOM   522  C CG  . LYS A 1 82  ? 26.727  2.849   20.686  1.00 87.52  ? 382 LYS A CG  1 
ATOM   523  C CD  . LYS A 1 82  ? 27.399  3.980   21.469  1.00 98.27  ? 382 LYS A CD  1 
ATOM   524  C CE  . LYS A 1 82  ? 27.249  5.364   20.856  1.00 97.65  ? 382 LYS A CE  1 
ATOM   525  N NZ  . LYS A 1 82  ? 28.281  6.281   21.355  1.00 102.72 ? 382 LYS A NZ  1 
ATOM   526  N N   . GLY A 1 83  ? 26.711  4.095   16.745  1.00 58.20  ? 383 GLY A N   1 
ATOM   527  C CA  . GLY A 1 83  ? 26.946  4.834   15.514  1.00 55.46  ? 383 GLY A CA  1 
ATOM   528  C C   . GLY A 1 83  ? 28.353  5.425   15.404  1.00 58.89  ? 383 GLY A C   1 
ATOM   529  O O   . GLY A 1 83  ? 28.746  5.813   14.300  1.00 59.57  ? 383 GLY A O   1 
ATOM   530  N N   . PHE A 1 84  ? 29.099  5.525   16.521  1.00 61.00  ? 384 PHE A N   1 
ATOM   531  C CA  . PHE A 1 84  ? 30.411  6.157   16.487  1.00 67.64  ? 384 PHE A CA  1 
ATOM   532  C C   . PHE A 1 84  ? 30.289  7.542   15.846  1.00 68.22  ? 384 PHE A C   1 
ATOM   533  O O   . PHE A 1 84  ? 29.395  8.290   16.210  1.00 70.11  ? 384 PHE A O   1 
ATOM   534  C CB  . PHE A 1 84  ? 31.361  5.174   15.791  1.00 71.10  ? 384 PHE A CB  1 
ATOM   535  C CG  . PHE A 1 84  ? 31.315  3.851   16.536  1.00 79.67  ? 384 PHE A CG  1 
ATOM   536  C CD1 . PHE A 1 84  ? 32.111  3.653   17.664  1.00 86.86  ? 384 PHE A CD1 1 
ATOM   537  C CD2 . PHE A 1 84  ? 30.402  2.856   16.176  1.00 77.77  ? 384 PHE A CD2 1 
ATOM   538  C CE1 . PHE A 1 84  ? 32.022  2.474   18.385  1.00 89.13  ? 384 PHE A CE1 1 
ATOM   539  C CE2 . PHE A 1 84  ? 30.327  1.675   16.896  1.00 79.25  ? 384 PHE A CE2 1 
ATOM   540  C CZ  . PHE A 1 84  ? 31.139  1.487   17.994  1.00 85.68  ? 384 PHE A CZ  1 
ATOM   541  N N   . ASN A 1 85  ? 31.137  7.848   14.857  1.00 70.98  ? 385 ASN A N   1 
ATOM   542  C CA  . ASN A 1 85  ? 31.166  9.139   14.180  1.00 72.17  ? 385 ASN A CA  1 
ATOM   543  C C   . ASN A 1 85  ? 30.089  9.277   13.098  1.00 70.89  ? 385 ASN A C   1 
ATOM   544  O O   . ASN A 1 85  ? 30.189  10.179  12.261  1.00 72.00  ? 385 ASN A O   1 
ATOM   545  C CB  . ASN A 1 85  ? 32.474  9.370   13.428  1.00 75.30  ? 385 ASN A CB  1 
ATOM   546  C CG  . ASN A 1 85  ? 33.691  9.297   14.309  1.00 83.16  ? 385 ASN A CG  1 
ATOM   547  O OD1 . ASN A 1 85  ? 33.571  9.185   15.533  1.00 87.35  ? 385 ASN A OD1 1 
ATOM   548  N ND2 . ASN A 1 85  ? 34.868  9.351   13.702  1.00 88.79  ? 385 ASN A ND2 1 
ATOM   549  N N   . LEU A 1 86  ? 29.102  8.372   13.057  1.00 65.66  ? 386 LEU A N   1 
ATOM   550  C CA  . LEU A 1 86  ? 27.928  8.617   12.238  1.00 65.72  ? 386 LEU A CA  1 
ATOM   551  C C   . LEU A 1 86  ? 26.919  9.406   13.062  1.00 66.20  ? 386 LEU A C   1 
ATOM   552  O O   . LEU A 1 86  ? 26.828  9.249   14.285  1.00 66.79  ? 386 LEU A O   1 
ATOM   553  C CB  . LEU A 1 86  ? 27.268  7.342   11.719  1.00 66.81  ? 386 LEU A CB  1 
ATOM   554  C CG  . LEU A 1 86  ? 28.098  6.479   10.768  1.00 67.45  ? 386 LEU A CG  1 
ATOM   555  C CD1 . LEU A 1 86  ? 27.159  5.538   10.028  1.00 63.52  ? 386 LEU A CD1 1 
ATOM   556  C CD2 . LEU A 1 86  ? 28.940  7.314   9.812   1.00 69.15  ? 386 LEU A CD2 1 
ATOM   557  N N   . PHE A 1 87  ? 26.123  10.216  12.359  1.00 63.76  ? 387 PHE A N   1 
ATOM   558  C CA  . PHE A 1 87  ? 25.092  11.005  13.001  1.00 59.54  ? 387 PHE A CA  1 
ATOM   559  C C   . PHE A 1 87  ? 23.907  10.088  13.220  1.00 55.55  ? 387 PHE A C   1 
ATOM   560  O O   . PHE A 1 87  ? 22.868  10.277  12.597  1.00 56.27  ? 387 PHE A O   1 
ATOM   561  C CB  . PHE A 1 87  ? 24.795  12.235  12.134  1.00 59.67  ? 387 PHE A CB  1 
ATOM   562  C CG  . PHE A 1 87  ? 25.904  13.278  12.156  1.00 62.03  ? 387 PHE A CG  1 
ATOM   563  C CD1 . PHE A 1 87  ? 26.232  13.938  13.342  1.00 63.28  ? 387 PHE A CD1 1 
ATOM   564  C CD2 . PHE A 1 87  ? 26.596  13.609  10.997  1.00 62.21  ? 387 PHE A CD2 1 
ATOM   565  C CE1 . PHE A 1 87  ? 27.231  14.891  13.369  1.00 68.34  ? 387 PHE A CE1 1 
ATOM   566  C CE2 . PHE A 1 87  ? 27.598  14.577  11.031  1.00 69.86  ? 387 PHE A CE2 1 
ATOM   567  C CZ  . PHE A 1 87  ? 27.914  15.215  12.215  1.00 70.76  ? 387 PHE A CZ  1 
ATOM   568  N N   . CYS A 1 88  ? 24.117  9.063   14.049  1.00 53.32  ? 388 CYS A N   1 
ATOM   569  C CA  . CYS A 1 88  ? 23.094  8.073   14.329  1.00 51.33  ? 388 CYS A CA  1 
ATOM   570  C C   . CYS A 1 88  ? 23.325  7.494   15.717  1.00 52.76  ? 388 CYS A C   1 
ATOM   571  O O   . CYS A 1 88  ? 24.426  7.573   16.261  1.00 54.27  ? 388 CYS A O   1 
ATOM   572  C CB  . CYS A 1 88  ? 23.040  7.010   13.226  1.00 56.44  ? 388 CYS A CB  1 
ATOM   573  S SG  . CYS A 1 88  ? 24.423  5.828   13.145  1.00 54.23  ? 388 CYS A SG  1 
ATOM   574  N N   . LYS A 1 89  ? 22.273  6.912   16.286  1.00 57.03  ? 389 LYS A N   1 
ATOM   575  C CA  . LYS A 1 89  ? 22.356  6.319   17.611  1.00 65.03  ? 389 LYS A CA  1 
ATOM   576  C C   . LYS A 1 89  ? 22.889  4.893   17.518  1.00 67.89  ? 389 LYS A C   1 
ATOM   577  O O   . LYS A 1 89  ? 23.621  4.434   18.394  1.00 72.40  ? 389 LYS A O   1 
ATOM   578  C CB  . LYS A 1 89  ? 20.992  6.365   18.303  1.00 69.09  ? 389 LYS A CB  1 
ATOM   579  C CG  . LYS A 1 89  ? 20.650  7.728   18.891  1.00 73.24  ? 389 LYS A CG  1 
ATOM   580  C CD  . LYS A 1 89  ? 19.251  7.843   19.490  1.00 76.99  ? 389 LYS A CD  1 
ATOM   581  C CE  . LYS A 1 89  ? 18.946  9.215   20.015  1.00 80.19  ? 389 LYS A CE  1 
ATOM   582  N NZ  . LYS A 1 89  ? 17.635  9.241   20.673  1.00 82.71  ? 389 LYS A NZ  1 
ATOM   583  N N   . TYR A 1 90  ? 22.521  4.206   16.438  1.00 64.38  ? 390 TYR A N   1 
ATOM   584  C CA  . TYR A 1 90  ? 22.848  2.804   16.281  1.00 65.28  ? 390 TYR A CA  1 
ATOM   585  C C   . TYR A 1 90  ? 23.101  2.563   14.798  1.00 61.84  ? 390 TYR A C   1 
ATOM   586  O O   . TYR A 1 90  ? 22.613  3.325   13.966  1.00 66.70  ? 390 TYR A O   1 
ATOM   587  C CB  . TYR A 1 90  ? 21.715  1.898   16.790  1.00 64.56  ? 390 TYR A CB  1 
ATOM   588  C CG  . TYR A 1 90  ? 21.358  1.944   18.276  1.00 67.15  ? 390 TYR A CG  1 
ATOM   589  C CD1 . TYR A 1 90  ? 22.314  1.750   19.268  1.00 69.95  ? 390 TYR A CD1 1 
ATOM   590  C CD2 . TYR A 1 90  ? 20.049  2.191   18.691  1.00 68.01  ? 390 TYR A CD2 1 
ATOM   591  C CE1 . TYR A 1 90  ? 21.982  1.815   20.613  1.00 71.32  ? 390 TYR A CE1 1 
ATOM   592  C CE2 . TYR A 1 90  ? 19.703  2.265   20.032  1.00 67.42  ? 390 TYR A CE2 1 
ATOM   593  C CZ  . TYR A 1 90  ? 20.680  2.083   20.997  1.00 71.05  ? 390 TYR A CZ  1 
ATOM   594  O OH  . TYR A 1 90  ? 20.378  2.131   22.331  1.00 75.23  ? 390 TYR A OH  1 
ATOM   595  N N   . ILE A 1 91  ? 23.886  1.525   14.492  1.00 56.69  ? 391 ILE A N   1 
ATOM   596  C CA  . ILE A 1 91  ? 23.955  0.967   13.149  1.00 55.03  ? 391 ILE A CA  1 
ATOM   597  C C   . ILE A 1 91  ? 23.415  -0.463  13.176  1.00 54.86  ? 391 ILE A C   1 
ATOM   598  O O   . ILE A 1 91  ? 23.858  -1.302  13.966  1.00 62.39  ? 391 ILE A O   1 
ATOM   599  C CB  . ILE A 1 91  ? 25.385  0.982   12.592  1.00 56.01  ? 391 ILE A CB  1 
ATOM   600  C CG1 . ILE A 1 91  ? 25.943  2.369   12.500  1.00 58.37  ? 391 ILE A CG1 1 
ATOM   601  C CG2 . ILE A 1 91  ? 25.440  0.282   11.238  1.00 56.74  ? 391 ILE A CG2 1 
ATOM   602  C CD1 . ILE A 1 91  ? 27.459  2.405   12.472  1.00 63.09  ? 391 ILE A CD1 1 
ATOM   603  N N   . TYR A 1 92  ? 22.444  -0.734  12.305  1.00 49.17  ? 392 TYR A N   1 
ATOM   604  C CA  . TYR A 1 92  ? 21.963  -2.082  12.104  1.00 48.56  ? 392 TYR A CA  1 
ATOM   605  C C   . TYR A 1 92  ? 22.662  -2.680  10.880  1.00 50.15  ? 392 TYR A C   1 
ATOM   606  O O   . TYR A 1 92  ? 22.373  -2.307  9.737   1.00 49.99  ? 392 TYR A O   1 
ATOM   607  C CB  . TYR A 1 92  ? 20.454  -1.981  11.918  1.00 44.76  ? 392 TYR A CB  1 
ATOM   608  C CG  . TYR A 1 92  ? 19.561  -1.703  13.114  1.00 41.63  ? 392 TYR A CG  1 
ATOM   609  C CD1 . TYR A 1 92  ? 20.039  -1.342  14.366  1.00 41.49  ? 392 TYR A CD1 1 
ATOM   610  C CD2 . TYR A 1 92  ? 18.184  -1.784  12.940  1.00 40.74  ? 392 TYR A CD2 1 
ATOM   611  C CE1 . TYR A 1 92  ? 19.161  -1.036  15.399  1.00 41.90  ? 392 TYR A CE1 1 
ATOM   612  C CE2 . TYR A 1 92  ? 17.301  -1.505  13.963  1.00 40.82  ? 392 TYR A CE2 1 
ATOM   613  C CZ  . TYR A 1 92  ? 17.787  -1.098  15.184  1.00 42.46  ? 392 TYR A CZ  1 
ATOM   614  O OH  . TYR A 1 92  ? 16.789  -0.859  16.099  1.00 45.92  ? 392 TYR A OH  1 
ATOM   615  N N   . HIS A 1 93  ? 23.601  -3.600  11.116  1.00 50.74  ? 393 HIS A N   1 
ATOM   616  C CA  . HIS A 1 93  ? 24.324  -4.238  10.019  1.00 52.71  ? 393 HIS A CA  1 
ATOM   617  C C   . HIS A 1 93  ? 23.544  -5.454  9.542   1.00 49.74  ? 393 HIS A C   1 
ATOM   618  O O   . HIS A 1 93  ? 23.391  -6.420  10.282  1.00 52.59  ? 393 HIS A O   1 
ATOM   619  C CB  . HIS A 1 93  ? 25.727  -4.693  10.446  1.00 54.51  ? 393 HIS A CB  1 
ATOM   620  C CG  . HIS A 1 93  ? 26.475  -3.630  11.165  1.00 54.98  ? 393 HIS A CG  1 
ATOM   621  N ND1 . HIS A 1 93  ? 27.398  -2.809  10.558  1.00 53.88  ? 393 HIS A ND1 1 
ATOM   622  C CD2 . HIS A 1 93  ? 26.416  -3.256  12.450  1.00 56.43  ? 393 HIS A CD2 1 
ATOM   623  C CE1 . HIS A 1 93  ? 27.895  -1.986  11.466  1.00 56.30  ? 393 HIS A CE1 1 
ATOM   624  N NE2 . HIS A 1 93  ? 27.317  -2.242  12.628  1.00 57.05  ? 393 HIS A NE2 1 
ATOM   625  N N   . VAL A 1 94  ? 23.048  -5.402  8.308   1.00 48.85  ? 394 VAL A N   1 
ATOM   626  C CA  . VAL A 1 94  ? 22.424  -6.574  7.715   1.00 54.27  ? 394 VAL A CA  1 
ATOM   627  C C   . VAL A 1 94  ? 23.521  -7.543  7.279   1.00 52.65  ? 394 VAL A C   1 
ATOM   628  O O   . VAL A 1 94  ? 24.385  -7.164  6.495   1.00 50.58  ? 394 VAL A O   1 
ATOM   629  C CB  . VAL A 1 94  ? 21.523  -6.167  6.538   1.00 55.14  ? 394 VAL A CB  1 
ATOM   630  C CG1 . VAL A 1 94  ? 21.151  -7.359  5.667   1.00 56.58  ? 394 VAL A CG1 1 
ATOM   631  C CG2 . VAL A 1 94  ? 20.288  -5.419  7.035   1.00 54.59  ? 394 VAL A CG2 1 
ATOM   632  N N   . LEU A 1 95  ? 23.505  -8.763  7.826   1.00 53.84  ? 395 LEU A N   1 
ATOM   633  C CA  . LEU A 1 95  ? 24.514  -9.755  7.483   1.00 58.13  ? 395 LEU A CA  1 
ATOM   634  C C   . LEU A 1 95  ? 23.943  -10.681 6.423   1.00 60.19  ? 395 LEU A C   1 
ATOM   635  O O   . LEU A 1 95  ? 23.081  -11.505 6.732   1.00 61.68  ? 395 LEU A O   1 
ATOM   636  C CB  . LEU A 1 95  ? 24.966  -10.543 8.707   1.00 58.69  ? 395 LEU A CB  1 
ATOM   637  C CG  . LEU A 1 95  ? 25.164  -9.717  9.977   1.00 57.88  ? 395 LEU A CG  1 
ATOM   638  C CD1 . LEU A 1 95  ? 25.653  -10.589 11.115  1.00 61.95  ? 395 LEU A CD1 1 
ATOM   639  C CD2 . LEU A 1 95  ? 26.150  -8.641  9.709   1.00 57.12  ? 395 LEU A CD2 1 
ATOM   640  N N   . TRP A 1 96  ? 24.443  -10.548 5.188   1.00 61.29  ? 396 TRP A N   1 
ATOM   641  C CA  . TRP A 1 96  ? 24.158  -11.532 4.155   1.00 66.77  ? 396 TRP A CA  1 
ATOM   642  C C   . TRP A 1 96  ? 25.004  -12.791 4.340   1.00 71.32  ? 396 TRP A C   1 
ATOM   643  O O   . TRP A 1 96  ? 26.165  -12.819 3.941   1.00 72.86  ? 396 TRP A O   1 
ATOM   644  C CB  . TRP A 1 96  ? 24.427  -10.938 2.773   1.00 65.65  ? 396 TRP A CB  1 
ATOM   645  C CG  . TRP A 1 96  ? 23.673  -9.665  2.522   1.00 62.11  ? 396 TRP A CG  1 
ATOM   646  C CD1 . TRP A 1 96  ? 24.061  -8.406  2.859   1.00 55.16  ? 396 TRP A CD1 1 
ATOM   647  C CD2 . TRP A 1 96  ? 22.421  -9.543  1.812   1.00 61.43  ? 396 TRP A CD2 1 
ATOM   648  N NE1 . TRP A 1 96  ? 23.116  -7.514  2.445   1.00 54.53  ? 396 TRP A NE1 1 
ATOM   649  C CE2 . TRP A 1 96  ? 22.110  -8.172  1.794   1.00 56.16  ? 396 TRP A CE2 1 
ATOM   650  C CE3 . TRP A 1 96  ? 21.549  -10.451 1.197   1.00 64.38  ? 396 TRP A CE3 1 
ATOM   651  C CZ2 . TRP A 1 96  ? 20.956  -7.685  1.191   1.00 57.88  ? 396 TRP A CZ2 1 
ATOM   652  C CZ3 . TRP A 1 96  ? 20.413  -9.968  0.589   1.00 63.18  ? 396 TRP A CZ3 1 
ATOM   653  C CH2 . TRP A 1 96  ? 20.127  -8.603  0.587   1.00 61.77  ? 396 TRP A CH2 1 
ATOM   654  N N   . HIS A 1 97  ? 24.402  -13.837 4.914   1.00 76.99  ? 397 HIS A N   1 
ATOM   655  C CA  . HIS A 1 97  ? 25.003  -15.159 4.905   1.00 84.87  ? 397 HIS A CA  1 
ATOM   656  C C   . HIS A 1 97  ? 24.737  -15.813 3.554   1.00 90.44  ? 397 HIS A C   1 
ATOM   657  O O   . HIS A 1 97  ? 23.664  -15.647 2.975   1.00 91.73  ? 397 HIS A O   1 
ATOM   658  C CB  . HIS A 1 97  ? 24.479  -16.003 6.069   1.00 86.45  ? 397 HIS A CB  1 
ATOM   659  C CG  . HIS A 1 97  ? 24.665  -15.345 7.398   1.00 83.98  ? 397 HIS A CG  1 
ATOM   660  N ND1 . HIS A 1 97  ? 25.830  -15.410 8.136   1.00 82.94  ? 397 HIS A ND1 1 
ATOM   661  C CD2 . HIS A 1 97  ? 23.809  -14.606 8.113   1.00 79.51  ? 397 HIS A CD2 1 
ATOM   662  C CE1 . HIS A 1 97  ? 25.664  -14.746 9.272   1.00 79.70  ? 397 HIS A CE1 1 
ATOM   663  N NE2 . HIS A 1 97  ? 24.447  -14.247 9.275   1.00 78.92  ? 397 HIS A NE2 1 
ATOM   664  N N   . SER A 1 98  ? 25.720  -16.600 3.107   1.00 100.19 ? 398 SER A N   1 
ATOM   665  C CA  . SER A 1 98  ? 25.799  -17.097 1.743   1.00 103.83 ? 398 SER A CA  1 
ATOM   666  C C   . SER A 1 98  ? 24.898  -18.308 1.474   1.00 104.72 ? 398 SER A C   1 
ATOM   667  O O   . SER A 1 98  ? 24.567  -18.517 0.314   1.00 104.59 ? 398 SER A O   1 
ATOM   668  C CB  . SER A 1 98  ? 27.239  -17.384 1.368   1.00 107.60 ? 398 SER A CB  1 
ATOM   669  O OG  . SER A 1 98  ? 27.846  -18.318 2.252   1.00 115.46 ? 398 SER A OG  1 
ATOM   670  N N   . GLU A 1 99  ? 24.436  -19.042 2.508   1.00 106.62 ? 399 GLU A N   1 
ATOM   671  C CA  . GLU A 1 99  ? 23.725  -20.306 2.306   1.00 113.93 ? 399 GLU A CA  1 
ATOM   672  C C   . GLU A 1 99  ? 22.195  -20.123 2.302   1.00 115.39 ? 399 GLU A C   1 
ATOM   673  O O   . GLU A 1 99  ? 21.471  -21.040 2.682   1.00 116.44 ? 399 GLU A O   1 
ATOM   674  C CB  . GLU A 1 99  ? 24.148  -21.341 3.361   1.00 116.72 ? 399 GLU A CB  1 
ATOM   675  C CG  . GLU A 1 99  ? 25.499  -22.026 3.128   1.00 118.99 ? 399 GLU A CG  1 
ATOM   676  C CD  . GLU A 1 99  ? 25.850  -23.263 3.978   1.00 126.11 ? 399 GLU A CD  1 
ATOM   677  O OE1 . GLU A 1 99  ? 25.110  -24.291 4.015   1.00 128.91 ? 399 GLU A OE1 1 
ATOM   678  O OE2 . GLU A 1 99  ? 26.935  -23.224 4.609   1.00 122.90 ? 399 GLU A OE2 1 
ATOM   679  N N   . PHE A 1 100 ? 21.693  -18.980 1.802   1.00 118.20 ? 400 PHE A N   1 
ATOM   680  C CA  . PHE A 1 100 ? 20.272  -18.646 1.863   1.00 118.19 ? 400 PHE A CA  1 
ATOM   681  C C   . PHE A 1 100 ? 19.801  -17.980 0.573   1.00 109.59 ? 400 PHE A C   1 
ATOM   682  O O   . PHE A 1 100 ? 20.592  -17.303 -0.068  1.00 108.21 ? 400 PHE A O   1 
ATOM   683  C CB  . PHE A 1 100 ? 20.013  -17.689 3.032   1.00 119.44 ? 400 PHE A CB  1 
ATOM   684  C CG  . PHE A 1 100 ? 20.273  -18.326 4.389   1.00 129.22 ? 400 PHE A CG  1 
ATOM   685  C CD1 . PHE A 1 100 ? 19.343  -19.198 4.951   1.00 134.65 ? 400 PHE A CD1 1 
ATOM   686  C CD2 . PHE A 1 100 ? 21.452  -18.077 5.086   1.00 129.64 ? 400 PHE A CD2 1 
ATOM   687  C CE1 . PHE A 1 100 ? 19.586  -19.796 6.179   1.00 137.19 ? 400 PHE A CE1 1 
ATOM   688  C CE2 . PHE A 1 100 ? 21.694  -18.687 6.310   1.00 131.99 ? 400 PHE A CE2 1 
ATOM   689  C CZ  . PHE A 1 100 ? 20.760  -19.540 6.857   1.00 132.56 ? 400 PHE A CZ  1 
ATOM   690  N N   . PRO A 1 101 ? 18.498  -18.075 0.194   1.00 105.38 ? 401 PRO A N   1 
ATOM   691  C CA  . PRO A 1 101 ? 17.975  -17.345 -0.961  1.00 103.87 ? 401 PRO A CA  1 
ATOM   692  C C   . PRO A 1 101 ? 17.982  -15.858 -0.603  1.00 98.73  ? 401 PRO A C   1 
ATOM   693  O O   . PRO A 1 101 ? 17.583  -15.490 0.497   1.00 92.69  ? 401 PRO A O   1 
ATOM   694  C CB  . PRO A 1 101 ? 16.560  -17.886 -1.213  1.00 105.80 ? 401 PRO A CB  1 
ATOM   695  C CG  . PRO A 1 101 ? 16.293  -18.881 -0.098  1.00 107.20 ? 401 PRO A CG  1 
ATOM   696  C CD  . PRO A 1 101 ? 17.436  -18.801 0.905   1.00 105.30 ? 401 PRO A CD  1 
ATOM   697  N N   . LYS A 1 102 ? 18.434  -15.019 -1.546  1.00 96.46  ? 402 LYS A N   1 
ATOM   698  C CA  . LYS A 1 102 ? 18.692  -13.612 -1.284  1.00 90.25  ? 402 LYS A CA  1 
ATOM   699  C C   . LYS A 1 102 ? 17.379  -12.871 -1.034  1.00 85.72  ? 402 LYS A C   1 
ATOM   700  O O   . LYS A 1 102 ? 17.226  -12.238 0.008   1.00 80.71  ? 402 LYS A O   1 
ATOM   701  C CB  . LYS A 1 102 ? 19.554  -13.021 -2.403  1.00 92.24  ? 402 LYS A CB  1 
ATOM   702  C CG  . LYS A 1 102 ? 20.975  -13.558 -2.426  1.00 98.20  ? 402 LYS A CG  1 
ATOM   703  C CD  . LYS A 1 102 ? 21.793  -13.264 -1.169  1.00 104.62 ? 402 LYS A CD  1 
ATOM   704  C CE  . LYS A 1 102 ? 22.842  -14.318 -0.915  1.00 113.87 ? 402 LYS A CE  1 
ATOM   705  N NZ  . LYS A 1 102 ? 23.383  -14.288 0.449   1.00 112.05 ? 402 LYS A NZ  1 
ATOM   706  N N   . PRO A 1 103 ? 16.362  -12.965 -1.918  1.00 84.23  ? 403 PRO A N   1 
ATOM   707  C CA  . PRO A 1 103 ? 15.068  -12.338 -1.635  1.00 83.67  ? 403 PRO A CA  1 
ATOM   708  C C   . PRO A 1 103 ? 14.522  -12.646 -0.237  1.00 86.96  ? 403 PRO A C   1 
ATOM   709  O O   . PRO A 1 103 ? 13.797  -11.838 0.330   1.00 98.05  ? 403 PRO A O   1 
ATOM   710  C CB  . PRO A 1 103 ? 14.151  -12.872 -2.754  1.00 87.27  ? 403 PRO A CB  1 
ATOM   711  C CG  . PRO A 1 103 ? 15.103  -13.281 -3.866  1.00 87.54  ? 403 PRO A CG  1 
ATOM   712  C CD  . PRO A 1 103 ? 16.377  -13.722 -3.179  1.00 86.10  ? 403 PRO A CD  1 
ATOM   713  N N   . GLN A 1 104 ? 14.868  -13.809 0.325   1.00 93.46  ? 404 GLN A N   1 
ATOM   714  C CA  . GLN A 1 104 ? 14.414  -14.193 1.654   1.00 94.93  ? 404 GLN A CA  1 
ATOM   715  C C   . GLN A 1 104 ? 15.233  -13.505 2.739   1.00 85.77  ? 404 GLN A C   1 
ATOM   716  O O   . GLN A 1 104 ? 14.707  -13.280 3.826   1.00 86.16  ? 404 GLN A O   1 
ATOM   717  C CB  . GLN A 1 104 ? 14.478  -15.695 1.944   1.00 102.92 ? 404 GLN A CB  1 
ATOM   718  C CG  . GLN A 1 104 ? 13.276  -16.458 1.406   1.00 113.90 ? 404 GLN A CG  1 
ATOM   719  C CD  . GLN A 1 104 ? 13.161  -17.876 1.914   1.00 122.52 ? 404 GLN A CD  1 
ATOM   720  O OE1 . GLN A 1 104 ? 13.996  -18.362 2.686   1.00 123.34 ? 404 GLN A OE1 1 
ATOM   721  N NE2 . GLN A 1 104 ? 12.104  -18.545 1.474   1.00 126.22 ? 404 GLN A NE2 1 
ATOM   722  N N   . ILE A 1 105 ? 16.520  -13.252 2.470   1.00 81.31  ? 405 ILE A N   1 
ATOM   723  C CA  . ILE A 1 105 ? 17.426  -12.621 3.420   1.00 79.77  ? 405 ILE A CA  1 
ATOM   724  C C   . ILE A 1 105 ? 17.001  -11.170 3.604   1.00 75.19  ? 405 ILE A C   1 
ATOM   725  O O   . ILE A 1 105 ? 17.009  -10.641 4.713   1.00 68.72  ? 405 ILE A O   1 
ATOM   726  C CB  . ILE A 1 105 ? 18.881  -12.686 2.918   1.00 83.86  ? 405 ILE A CB  1 
ATOM   727  C CG1 . ILE A 1 105 ? 19.460  -14.095 3.034   1.00 97.72  ? 405 ILE A CG1 1 
ATOM   728  C CG2 . ILE A 1 105 ? 19.774  -11.662 3.621   1.00 80.95  ? 405 ILE A CG2 1 
ATOM   729  C CD1 . ILE A 1 105 ? 19.967  -14.461 4.423   1.00 103.61 ? 405 ILE A CD1 1 
ATOM   730  N N   . LEU A 1 106 ? 16.685  -10.534 2.473   1.00 72.17  ? 406 LEU A N   1 
ATOM   731  C CA  . LEU A 1 106 ? 16.184  -9.179  2.482   1.00 69.53  ? 406 LEU A CA  1 
ATOM   732  C C   . LEU A 1 106 ? 14.891  -9.132  3.295   1.00 68.63  ? 406 LEU A C   1 
ATOM   733  O O   . LEU A 1 106 ? 14.749  -8.335  4.233   1.00 61.55  ? 406 LEU A O   1 
ATOM   734  C CB  . LEU A 1 106 ? 15.985  -8.720  1.037   1.00 70.52  ? 406 LEU A CB  1 
ATOM   735  C CG  . LEU A 1 106 ? 15.537  -7.266  0.848   1.00 69.32  ? 406 LEU A CG  1 
ATOM   736  C CD1 . LEU A 1 106 ? 16.583  -6.345  1.393   1.00 63.89  ? 406 LEU A CD1 1 
ATOM   737  C CD2 . LEU A 1 106 ? 15.242  -6.939  -0.609  1.00 72.58  ? 406 LEU A CD2 1 
ATOM   738  N N   . LYS A 1 107 ? 13.952  -10.010 2.936   1.00 68.91  ? 407 LYS A N   1 
ATOM   739  C CA  . LYS A 1 107 ? 12.629  -9.897  3.509   1.00 71.13  ? 407 LYS A CA  1 
ATOM   740  C C   . LYS A 1 107 ? 12.758  -10.076 5.017   1.00 71.63  ? 407 LYS A C   1 
ATOM   741  O O   . LYS A 1 107 ? 12.095  -9.383  5.785   1.00 71.47  ? 407 LYS A O   1 
ATOM   742  C CB  . LYS A 1 107 ? 11.638  -10.859 2.853   1.00 76.79  ? 407 LYS A CB  1 
ATOM   743  C CG  . LYS A 1 107 ? 10.202  -10.595 3.327   1.00 83.14  ? 407 LYS A CG  1 
ATOM   744  C CD  . LYS A 1 107 ? 9.388   -11.839 3.667   1.00 90.80  ? 407 LYS A CD  1 
ATOM   745  C CE  . LYS A 1 107 ? 8.321   -11.617 4.703   1.00 92.97  ? 407 LYS A CE  1 
ATOM   746  N NZ  . LYS A 1 107 ? 7.182   -10.869 4.170   1.00 95.96  ? 407 LYS A NZ  1 
ATOM   747  N N   . HIS A 1 108 ? 13.650  -10.984 5.436   1.00 73.24  ? 408 HIS A N   1 
ATOM   748  C CA  . HIS A 1 108 ? 13.782  -11.323 6.846   1.00 73.54  ? 408 HIS A CA  1 
ATOM   749  C C   . HIS A 1 108 ? 14.595  -10.219 7.532   1.00 65.74  ? 408 HIS A C   1 
ATOM   750  O O   . HIS A 1 108 ? 14.278  -9.796  8.641   1.00 63.21  ? 408 HIS A O   1 
ATOM   751  C CB  . HIS A 1 108 ? 14.282  -12.767 7.037   1.00 76.96  ? 408 HIS A CB  1 
ATOM   752  C CG  . HIS A 1 108 ? 13.320  -13.879 6.668   1.00 86.57  ? 408 HIS A CG  1 
ATOM   753  N ND1 . HIS A 1 108 ? 11.946  -13.827 6.824   1.00 93.91  ? 408 HIS A ND1 1 
ATOM   754  C CD2 . HIS A 1 108 ? 13.557  -15.106 6.151   1.00 89.19  ? 408 HIS A CD2 1 
ATOM   755  C CE1 . HIS A 1 108 ? 11.385  -14.962 6.408   1.00 90.89  ? 408 HIS A CE1 1 
ATOM   756  N NE2 . HIS A 1 108 ? 12.347  -15.742 5.983   1.00 92.13  ? 408 HIS A NE2 1 
ATOM   757  N N   . ALA A 1 109 ? 15.632  -9.726  6.859   1.00 61.81  ? 409 ALA A N   1 
ATOM   758  C CA  . ALA A 1 109 ? 16.485  -8.685  7.478   1.00 59.85  ? 409 ALA A CA  1 
ATOM   759  C C   . ALA A 1 109 ? 15.653  -7.429  7.717   1.00 60.24  ? 409 ALA A C   1 
ATOM   760  O O   . ALA A 1 109 ? 15.831  -6.770  8.751   1.00 53.89  ? 409 ALA A O   1 
ATOM   761  C CB  . ALA A 1 109 ? 17.674  -8.394  6.609   1.00 57.45  ? 409 ALA A CB  1 
ATOM   762  N N   . MET A 1 110 ? 14.755  -7.131  6.786   1.00 60.41  ? 410 MET A N   1 
ATOM   763  C CA  . MET A 1 110 ? 13.878  -5.952  6.931   1.00 58.45  ? 410 MET A CA  1 
ATOM   764  C C   . MET A 1 110 ? 13.043  -6.104  8.200   1.00 61.35  ? 410 MET A C   1 
ATOM   765  O O   . MET A 1 110 ? 13.177  -5.261  9.100   1.00 68.06  ? 410 MET A O   1 
ATOM   766  C CB  . MET A 1 110 ? 12.947  -5.841  5.728   1.00 60.12  ? 410 MET A CB  1 
ATOM   767  C CG  . MET A 1 110 ? 13.576  -5.183  4.520   1.00 58.39  ? 410 MET A CG  1 
ATOM   768  S SD  . MET A 1 110 ? 14.245  -3.549  4.881   1.00 58.28  ? 410 MET A SD  1 
ATOM   769  C CE  . MET A 1 110 ? 12.734  -2.589  5.034   1.00 54.73  ? 410 MET A CE  1 
ATOM   770  N N   . LYS A 1 111 ? 12.221  -7.143  8.267   1.00 68.03  ? 411 LYS A N   1 
ATOM   771  C CA  . LYS A 1 111 ? 11.324  -7.337  9.432   1.00 68.73  ? 411 LYS A CA  1 
ATOM   772  C C   . LYS A 1 111 ? 12.122  -7.194  10.731  1.00 61.10  ? 411 LYS A C   1 
ATOM   773  O O   . LYS A 1 111 ? 11.657  -6.491  11.622  1.00 55.35  ? 411 LYS A O   1 
ATOM   774  C CB  . LYS A 1 111 ? 10.648  -8.704  9.313   1.00 78.97  ? 411 LYS A CB  1 
ATOM   775  C CG  . LYS A 1 111 ? 10.123  -9.303  10.610  1.00 86.82  ? 411 LYS A CG  1 
ATOM   776  C CD  . LYS A 1 111 ? 8.888   -10.174 10.419  1.00 91.56  ? 411 LYS A CD  1 
ATOM   777  C CE  . LYS A 1 111 ? 8.272   -10.594 11.715  1.00 96.92  ? 411 LYS A CE  1 
ATOM   778  N NZ  . LYS A 1 111 ? 9.283   -10.803 12.755  1.00 101.00 ? 411 LYS A NZ  1 
ATOM   779  N N   . GLU A 1 112 ? 13.283  -7.832  10.813  1.00 59.82  ? 412 GLU A N   1 
ATOM   780  C CA  . GLU A 1 112 ? 14.101  -7.774  12.045  1.00 61.37  ? 412 GLU A CA  1 
ATOM   781  C C   . GLU A 1 112 ? 14.474  -6.318  12.322  1.00 58.53  ? 412 GLU A C   1 
ATOM   782  O O   . GLU A 1 112 ? 14.251  -5.864  13.452  1.00 57.68  ? 412 GLU A O   1 
ATOM   783  C CB  . GLU A 1 112 ? 15.348  -8.636  11.868  1.00 30.00  ? 412 GLU A CB  1 
ATOM   784  C CG  . GLU A 1 112 ? 16.206  -8.733  13.125  1.00 30.00  ? 412 GLU A CG  1 
ATOM   785  C CD  . GLU A 1 112 ? 17.278  -9.801  13.025  1.00 30.00  ? 412 GLU A CD  1 
ATOM   786  O OE1 . GLU A 1 112 ? 17.140  -10.684 12.157  1.00 30.00  ? 412 GLU A OE1 1 
ATOM   787  O OE2 . GLU A 1 112 ? 18.249  -9.750  13.808  1.00 30.00  ? 412 GLU A OE2 1 
ATOM   788  N N   . CYS A 1 113 ? 15.007  -5.624  11.316  1.00 56.31  ? 413 CYS A N   1 
ATOM   789  C CA  . CYS A 1 113 ? 15.425  -4.209  11.474  1.00 55.09  ? 413 CYS A CA  1 
ATOM   790  C C   . CYS A 1 113 ? 14.224  -3.397  11.975  1.00 56.53  ? 413 CYS A C   1 
ATOM   791  O O   . CYS A 1 113 ? 14.397  -2.614  12.916  1.00 58.45  ? 413 CYS A O   1 
ATOM   792  C CB  . CYS A 1 113 ? 15.965  -3.662  10.158  1.00 53.80  ? 413 CYS A CB  1 
ATOM   793  S SG  . CYS A 1 113 ? 17.689  -4.092  9.812   1.00 54.88  ? 413 CYS A SG  1 
ATOM   794  N N   . LEU A 1 114 ? 13.051  -3.616  11.393  1.00 53.81  ? 414 LEU A N   1 
ATOM   795  C CA  . LEU A 1 114 ? 11.845  -2.843  11.770  1.00 53.56  ? 414 LEU A CA  1 
ATOM   796  C C   . LEU A 1 114 ? 11.298  -3.290  13.135  1.00 57.40  ? 414 LEU A C   1 
ATOM   797  O O   . LEU A 1 114 ? 10.659  -2.468  13.803  1.00 60.88  ? 414 LEU A O   1 
ATOM   798  C CB  . LEU A 1 114 ? 10.841  -3.027  10.638  1.00 54.52  ? 414 LEU A CB  1 
ATOM   799  C CG  . LEU A 1 114 ? 11.214  -2.368  9.308   1.00 54.68  ? 414 LEU A CG  1 
ATOM   800  C CD1 . LEU A 1 114 ? 10.234  -2.768  8.225   1.00 60.26  ? 414 LEU A CD1 1 
ATOM   801  C CD2 . LEU A 1 114 ? 11.249  -0.862  9.468   1.00 52.44  ? 414 LEU A CD2 1 
ATOM   802  N N   . GLU A 1 115 ? 11.526  -4.538  13.537  1.00 61.86  ? 415 GLU A N   1 
ATOM   803  C CA  . GLU A 1 115 ? 11.081  -4.992  14.836  1.00 66.08  ? 415 GLU A CA  1 
ATOM   804  C C   . GLU A 1 115 ? 11.996  -4.377  15.872  1.00 63.52  ? 415 GLU A C   1 
ATOM   805  O O   . GLU A 1 115 ? 11.555  -4.001  16.955  1.00 65.14  ? 415 GLU A O   1 
ATOM   806  C CB  . GLU A 1 115 ? 11.246  -6.498  14.971  1.00 76.28  ? 415 GLU A CB  1 
ATOM   807  C CG  . GLU A 1 115 ? 10.251  -7.297  14.139  1.00 80.91  ? 415 GLU A CG  1 
ATOM   808  C CD  . GLU A 1 115 ? 9.389   -8.052  15.102  1.00 84.31  ? 415 GLU A CD  1 
ATOM   809  O OE1 . GLU A 1 115 ? 8.598   -7.340  15.759  1.00 90.35  ? 415 GLU A OE1 1 
ATOM   810  O OE2 . GLU A 1 115 ? 9.578   -9.287  15.234  1.00 86.34  ? 415 GLU A OE2 1 
ATOM   811  N N   . LYS A 1 116 ? 13.282  -4.299  15.527  1.00 58.83  ? 416 LYS A N   1 
ATOM   812  C CA  . LYS A 1 116 ? 14.212  -3.680  16.441  1.00 62.90  ? 416 LYS A CA  1 
ATOM   813  C C   . LYS A 1 116 ? 13.807  -2.219  16.655  1.00 64.39  ? 416 LYS A C   1 
ATOM   814  O O   . LYS A 1 116 ? 14.069  -1.664  17.718  1.00 66.58  ? 416 LYS A O   1 
ATOM   815  C CB  . LYS A 1 116 ? 15.654  -3.815  15.949  1.00 61.74  ? 416 LYS A CB  1 
ATOM   816  C CG  . LYS A 1 116 ? 16.204  -5.204  15.933  1.00 64.86  ? 416 LYS A CG  1 
ATOM   817  C CD  . LYS A 1 116 ? 17.687  -5.280  16.252  1.00 69.00  ? 416 LYS A CD  1 
ATOM   818  C CE  . LYS A 1 116 ? 18.165  -6.713  16.260  1.00 76.69  ? 416 LYS A CE  1 
ATOM   819  N NZ  . LYS A 1 116 ? 17.376  -7.616  17.111  1.00 82.93  ? 416 LYS A NZ  1 
ATOM   820  N N   . CYS A 1 117 ? 13.172  -1.587  15.658  1.00 62.29  ? 417 CYS A N   1 
ATOM   821  C CA  . CYS A 1 117 ? 12.719  -0.211  15.842  1.00 61.31  ? 417 CYS A CA  1 
ATOM   822  C C   . CYS A 1 117 ? 11.722  -0.123  16.996  1.00 62.99  ? 417 CYS A C   1 
ATOM   823  O O   . CYS A 1 117 ? 11.711  0.866   17.720  1.00 72.08  ? 417 CYS A O   1 
ATOM   824  C CB  . CYS A 1 117 ? 12.112  0.421   14.592  1.00 55.68  ? 417 CYS A CB  1 
ATOM   825  S SG  . CYS A 1 117 ? 13.303  0.622   13.249  1.00 50.32  ? 417 CYS A SG  1 
ATOM   826  N N   . ILE A 1 118 ? 10.895  -1.147  17.203  1.00 61.16  ? 418 ILE A N   1 
ATOM   827  C CA  . ILE A 1 118 ? 10.026  -1.109  18.370  1.00 60.82  ? 418 ILE A CA  1 
ATOM   828  C C   . ILE A 1 118 ? 10.840  -1.422  19.619  1.00 62.31  ? 418 ILE A C   1 
ATOM   829  O O   . ILE A 1 118 ? 10.592  -0.842  20.654  1.00 62.77  ? 418 ILE A O   1 
ATOM   830  C CB  . ILE A 1 118 ? 8.810   -2.026  18.230  1.00 60.23  ? 418 ILE A CB  1 
ATOM   831  C CG1 . ILE A 1 118 ? 8.075   -1.741  16.948  1.00 58.92  ? 418 ILE A CG1 1 
ATOM   832  C CG2 . ILE A 1 118 ? 7.907   -1.853  19.439  1.00 64.47  ? 418 ILE A CG2 1 
ATOM   833  C CD1 . ILE A 1 118 ? 6.884   -2.638  16.680  1.00 62.77  ? 418 ILE A CD1 1 
ATOM   834  N N   . GLU A 1 119 ? 11.835  -2.301  19.506  1.00 66.33  ? 419 GLU A N   1 
ATOM   835  C CA  . GLU A 1 119 ? 12.617  -2.731  20.657  1.00 72.28  ? 419 GLU A CA  1 
ATOM   836  C C   . GLU A 1 119 ? 13.352  -1.535  21.252  1.00 70.56  ? 419 GLU A C   1 
ATOM   837  O O   . GLU A 1 119 ? 13.319  -1.309  22.453  1.00 77.16  ? 419 GLU A O   1 
ATOM   838  C CB  . GLU A 1 119 ? 13.599  -3.861  20.322  1.00 75.01  ? 419 GLU A CB  1 
ATOM   839  C CG  . GLU A 1 119 ? 12.917  -5.161  19.899  1.00 80.46  ? 419 GLU A CG  1 
ATOM   840  C CD  . GLU A 1 119 ? 13.829  -6.289  19.446  1.00 85.38  ? 419 GLU A CD  1 
ATOM   841  O OE1 . GLU A 1 119 ? 15.048  -6.143  19.632  1.00 91.75  ? 419 GLU A OE1 1 
ATOM   842  O OE2 . GLU A 1 119 ? 13.340  -7.293  18.883  1.00 91.91  ? 419 GLU A OE2 1 
ATOM   843  N N   . GLN A 1 120 ? 13.984  -0.739  20.400  1.00 69.98  ? 420 GLN A N   1 
ATOM   844  C CA  . GLN A 1 120 ? 14.861  0.316   20.877  1.00 74.00  ? 420 GLN A CA  1 
ATOM   845  C C   . GLN A 1 120 ? 14.197  1.699   20.860  1.00 70.43  ? 420 GLN A C   1 
ATOM   846  O O   . GLN A 1 120 ? 14.899  2.694   21.026  1.00 68.15  ? 420 GLN A O   1 
ATOM   847  C CB  . GLN A 1 120 ? 16.145  0.253   20.053  1.00 73.28  ? 420 GLN A CB  1 
ATOM   848  C CG  . GLN A 1 120 ? 17.079  -0.857  20.517  1.00 76.64  ? 420 GLN A CG  1 
ATOM   849  C CD  . GLN A 1 120 ? 18.325  -0.955  19.671  1.00 78.45  ? 420 GLN A CD  1 
ATOM   850  O OE1 . GLN A 1 120 ? 19.445  -1.113  20.167  1.00 79.69  ? 420 GLN A OE1 1 
ATOM   851  N NE2 . GLN A 1 120 ? 18.135  -0.833  18.369  1.00 80.20  ? 420 GLN A NE2 1 
ATOM   852  N N   . ASN A 1 121 ? 12.863  1.759   20.714  1.00 69.41  ? 421 ASN A N   1 
ATOM   853  C CA  . ASN A 1 121 ? 12.158  3.028   20.657  1.00 71.13  ? 421 ASN A CA  1 
ATOM   854  C C   . ASN A 1 121 ? 12.877  3.962   19.682  1.00 70.93  ? 421 ASN A C   1 
ATOM   855  O O   . ASN A 1 121 ? 13.312  5.046   20.062  1.00 77.14  ? 421 ASN A O   1 
ATOM   856  C CB  . ASN A 1 121 ? 12.051  3.674   22.032  1.00 74.37  ? 421 ASN A CB  1 
ATOM   857  C CG  . ASN A 1 121 ? 11.290  2.820   23.012  1.00 79.56  ? 421 ASN A CG  1 
ATOM   858  O OD1 . ASN A 1 121 ? 11.853  2.390   24.027  1.00 86.65  ? 421 ASN A OD1 1 
ATOM   859  N ND2 . ASN A 1 121 ? 10.014  2.580   22.739  1.00 79.34  ? 421 ASN A ND2 1 
ATOM   860  N N   . ILE A 1 122 ? 13.020  3.475   18.447  1.00 62.78  ? 422 ILE A N   1 
ATOM   861  C CA  . ILE A 1 122 ? 13.614  4.160   17.316  1.00 58.14  ? 422 ILE A CA  1 
ATOM   862  C C   . ILE A 1 122 ? 12.505  4.999   16.682  1.00 59.23  ? 422 ILE A C   1 
ATOM   863  O O   . ILE A 1 122 ? 11.389  4.501   16.508  1.00 54.48  ? 422 ILE A O   1 
ATOM   864  C CB  . ILE A 1 122 ? 14.183  3.089   16.348  1.00 54.03  ? 422 ILE A CB  1 
ATOM   865  C CG1 . ILE A 1 122 ? 15.349  2.313   16.960  1.00 55.16  ? 422 ILE A CG1 1 
ATOM   866  C CG2 . ILE A 1 122 ? 14.562  3.620   14.970  1.00 49.74  ? 422 ILE A CG2 1 
ATOM   867  C CD1 . ILE A 1 122 ? 16.421  3.147   17.633  1.00 55.32  ? 422 ILE A CD1 1 
ATOM   868  N N   . THR A 1 123 ? 12.815  6.259   16.346  1.00 59.58  ? 423 THR A N   1 
ATOM   869  C CA  . THR A 1 123 ? 11.858  7.120   15.657  1.00 64.31  ? 423 THR A CA  1 
ATOM   870  C C   . THR A 1 123 ? 12.225  7.293   14.185  1.00 57.96  ? 423 THR A C   1 
ATOM   871  O O   . THR A 1 123 ? 11.379  7.662   13.382  1.00 60.44  ? 423 THR A O   1 
ATOM   872  C CB  . THR A 1 123 ? 11.721  8.489   16.325  1.00 66.06  ? 423 THR A CB  1 
ATOM   873  O OG1 . THR A 1 123 ? 13.007  9.092   16.233  1.00 68.95  ? 423 THR A OG1 1 
ATOM   874  C CG2 . THR A 1 123 ? 11.270  8.384   17.767  1.00 66.00  ? 423 THR A CG2 1 
ATOM   875  N N   . SER A 1 124 ? 13.469  7.039   13.804  1.00 52.43  ? 424 SER A N   1 
ATOM   876  C CA  . SER A 1 124 ? 13.812  7.212   12.406  1.00 46.18  ? 424 SER A CA  1 
ATOM   877  C C   . SER A 1 124 ? 14.871  6.188   12.017  1.00 43.46  ? 424 SER A C   1 
ATOM   878  O O   . SER A 1 124 ? 15.791  5.890   12.784  1.00 45.73  ? 424 SER A O   1 
ATOM   879  C CB  . SER A 1 124 ? 14.271  8.604   12.149  1.00 43.97  ? 424 SER A CB  1 
ATOM   880  O OG  . SER A 1 124 ? 15.449  8.884   12.896  1.00 44.69  ? 424 SER A OG  1 
ATOM   881  N N   . ILE A 1 125 ? 14.716  5.651   10.811  1.00 41.17  ? 425 ILE A N   1 
ATOM   882  C CA  . ILE A 1 125 ? 15.608  4.622   10.306  1.00 40.07  ? 425 ILE A CA  1 
ATOM   883  C C   . ILE A 1 125 ? 15.793  4.878   8.813   1.00 38.44  ? 425 ILE A C   1 
ATOM   884  O O   . ILE A 1 125 ? 14.813  5.070   8.100   1.00 37.42  ? 425 ILE A O   1 
ATOM   885  C CB  . ILE A 1 125 ? 15.076  3.192   10.597  1.00 40.32  ? 425 ILE A CB  1 
ATOM   886  C CG1 . ILE A 1 125 ? 16.045  2.136   10.099  1.00 41.52  ? 425 ILE A CG1 1 
ATOM   887  C CG2 . ILE A 1 125 ? 13.688  2.949   10.001  1.00 39.11  ? 425 ILE A CG2 1 
ATOM   888  C CD1 . ILE A 1 125 ? 15.820  0.765   10.691  1.00 45.81  ? 425 ILE A CD1 1 
ATOM   889  N N   . SER A 1 126 ? 17.046  4.827   8.356   1.00 38.02  ? 426 SER A N   1 
ATOM   890  C CA  . SER A 1 126 ? 17.362  5.035   6.960   1.00 40.08  ? 426 SER A CA  1 
ATOM   891  C C   . SER A 1 126 ? 18.103  3.816   6.443   1.00 39.11  ? 426 SER A C   1 
ATOM   892  O O   . SER A 1 126 ? 19.075  3.375   7.045   1.00 40.03  ? 426 SER A O   1 
ATOM   893  C CB  . SER A 1 126 ? 18.167  6.319   6.748   1.00 45.04  ? 426 SER A CB  1 
ATOM   894  O OG  . SER A 1 126 ? 17.472  7.437   7.299   1.00 52.21  ? 426 SER A OG  1 
ATOM   895  N N   . PHE A 1 127 ? 17.645  3.349   5.282   1.00 40.88  ? 427 PHE A N   1 
ATOM   896  C CA  . PHE A 1 127 ? 18.113  2.148   4.630   1.00 43.06  ? 427 PHE A CA  1 
ATOM   897  C C   . PHE A 1 127 ? 18.664  2.517   3.262   1.00 46.21  ? 427 PHE A C   1 
ATOM   898  O O   . PHE A 1 127 ? 18.057  3.338   2.573   1.00 49.45  ? 427 PHE A O   1 
ATOM   899  C CB  . PHE A 1 127 ? 16.977  1.152   4.348   1.00 44.46  ? 427 PHE A CB  1 
ATOM   900  C CG  . PHE A 1 127 ? 16.151  0.619   5.519   1.00 43.34  ? 427 PHE A CG  1 
ATOM   901  C CD1 . PHE A 1 127 ? 15.090  1.358   6.030   1.00 42.90  ? 427 PHE A CD1 1 
ATOM   902  C CD2 . PHE A 1 127 ? 16.374  -0.657  6.031   1.00 44.01  ? 427 PHE A CD2 1 
ATOM   903  C CE1 . PHE A 1 127 ? 14.342  0.895   7.089   1.00 44.35  ? 427 PHE A CE1 1 
ATOM   904  C CE2 . PHE A 1 127 ? 15.602  -1.141  7.062   1.00 45.31  ? 427 PHE A CE2 1 
ATOM   905  C CZ  . PHE A 1 127 ? 14.604  -0.353  7.601   1.00 48.64  ? 427 PHE A CZ  1 
ATOM   906  N N   . PRO A 1 128 ? 19.754  1.856   2.790   1.00 46.62  ? 428 PRO A N   1 
ATOM   907  C CA  . PRO A 1 128 ? 20.184  1.951   1.398   1.00 46.04  ? 428 PRO A CA  1 
ATOM   908  C C   . PRO A 1 128 ? 19.297  1.024   0.593   1.00 47.50  ? 428 PRO A C   1 
ATOM   909  O O   . PRO A 1 128 ? 18.398  0.425   1.161   1.00 46.08  ? 428 PRO A O   1 
ATOM   910  C CB  . PRO A 1 128 ? 21.628  1.502   1.472   1.00 49.03  ? 428 PRO A CB  1 
ATOM   911  C CG  . PRO A 1 128 ? 21.639  0.465   2.579   1.00 47.50  ? 428 PRO A CG  1 
ATOM   912  C CD  . PRO A 1 128 ? 20.645  0.994   3.580   1.00 47.11  ? 428 PRO A CD  1 
ATOM   913  N N   . ALA A 1 129 ? 19.502  0.958   -0.727  1.00 53.51  ? 429 ALA A N   1 
ATOM   914  C CA  . ALA A 1 129 ? 18.717  0.048   -1.549  1.00 57.14  ? 429 ALA A CA  1 
ATOM   915  C C   . ALA A 1 129 ? 19.301  -1.357  -1.411  1.00 60.32  ? 429 ALA A C   1 
ATOM   916  O O   . ALA A 1 129 ? 20.085  -1.802  -2.257  1.00 61.42  ? 429 ALA A O   1 
ATOM   917  C CB  . ALA A 1 129 ? 18.716  0.500   -2.975  1.00 61.77  ? 429 ALA A CB  1 
ATOM   918  N N   . LEU A 1 130 ? 18.919  -2.024  -0.313  1.00 57.95  ? 430 LEU A N   1 
ATOM   919  C CA  . LEU A 1 130 ? 19.511  -3.280  0.116   1.00 58.17  ? 430 LEU A CA  1 
ATOM   920  C C   . LEU A 1 130 ? 19.406  -4.351  -0.961  1.00 59.14  ? 430 LEU A C   1 
ATOM   921  O O   . LEU A 1 130 ? 18.328  -4.616  -1.484  1.00 59.31  ? 430 LEU A O   1 
ATOM   922  C CB  . LEU A 1 130 ? 18.775  -3.742  1.365   1.00 56.31  ? 430 LEU A CB  1 
ATOM   923  C CG  . LEU A 1 130 ? 19.148  -3.072  2.680   1.00 52.20  ? 430 LEU A CG  1 
ATOM   924  C CD1 . LEU A 1 130 ? 18.096  -3.502  3.661   1.00 54.55  ? 430 LEU A CD1 1 
ATOM   925  C CD2 . LEU A 1 130 ? 20.526  -3.470  3.169   1.00 53.86  ? 430 LEU A CD2 1 
ATOM   926  N N   . GLY A 1 131 ? 20.551  -4.947  -1.286  1.00 61.95  ? 431 GLY A N   1 
ATOM   927  C CA  . GLY A 1 131 ? 20.584  -6.129  -2.125  1.00 67.91  ? 431 GLY A CA  1 
ATOM   928  C C   . GLY A 1 131 ? 20.616  -5.802  -3.613  1.00 71.78  ? 431 GLY A C   1 
ATOM   929  O O   . GLY A 1 131 ? 20.540  -6.717  -4.447  1.00 80.71  ? 431 GLY A O   1 
ATOM   930  N N   . THR A 1 132 ? 20.765  -4.512  -3.954  1.00 63.97  ? 432 THR A N   1 
ATOM   931  C CA  . THR A 1 132 ? 20.845  -4.143  -5.361  1.00 64.28  ? 432 THR A CA  1 
ATOM   932  C C   . THR A 1 132 ? 22.289  -4.245  -5.847  1.00 62.91  ? 432 THR A C   1 
ATOM   933  O O   . THR A 1 132 ? 22.548  -4.276  -7.052  1.00 65.27  ? 432 THR A O   1 
ATOM   934  C CB  . THR A 1 132 ? 20.194  -2.779  -5.559  1.00 62.83  ? 432 THR A CB  1 
ATOM   935  O OG1 . THR A 1 132 ? 20.694  -1.852  -4.593  1.00 57.61  ? 432 THR A OG1 1 
ATOM   936  C CG2 . THR A 1 132 ? 18.687  -2.889  -5.400  1.00 62.63  ? 432 THR A CG2 1 
ATOM   937  N N   . GLY A 1 133 ? 23.218  -4.390  -4.892  1.00 63.14  ? 433 GLY A N   1 
ATOM   938  C CA  . GLY A 1 133 ? 24.641  -4.395  -5.176  1.00 66.84  ? 433 GLY A CA  1 
ATOM   939  C C   . GLY A 1 133 ? 25.000  -5.557  -6.083  1.00 75.28  ? 433 GLY A C   1 
ATOM   940  O O   . GLY A 1 133 ? 24.601  -6.692  -5.814  1.00 79.76  ? 433 GLY A O   1 
ATOM   941  N N   . ASN A 1 134 ? 25.691  -5.217  -7.177  1.00 83.43  ? 434 ASN A N   1 
ATOM   942  C CA  . ASN A 1 134 ? 26.244  -6.160  -8.142  1.00 95.14  ? 434 ASN A CA  1 
ATOM   943  C C   . ASN A 1 134 ? 25.169  -6.726  -9.064  1.00 103.82 ? 434 ASN A C   1 
ATOM   944  O O   . ASN A 1 134 ? 25.495  -7.561  -9.909  1.00 109.60 ? 434 ASN A O   1 
ATOM   945  C CB  . ASN A 1 134 ? 27.024  -7.299  -7.490  1.00 94.74  ? 434 ASN A CB  1 
ATOM   946  C CG  . ASN A 1 134 ? 28.365  -6.853  -6.952  1.00 94.12  ? 434 ASN A CG  1 
ATOM   947  O OD1 . ASN A 1 134 ? 28.641  -6.998  -5.749  1.00 86.99  ? 434 ASN A OD1 1 
ATOM   948  N ND2 . ASN A 1 134 ? 29.211  -6.326  -7.829  1.00 96.67  ? 434 ASN A ND2 1 
ATOM   949  N N   . MET A 1 135 ? 23.924  -6.236  -8.942  1.00 108.75 ? 435 MET A N   1 
ATOM   950  C CA  . MET A 1 135 ? 22.771  -6.903  -9.529  1.00 124.90 ? 435 MET A CA  1 
ATOM   951  C C   . MET A 1 135 ? 22.671  -8.311  -8.922  1.00 128.02 ? 435 MET A C   1 
ATOM   952  O O   . MET A 1 135 ? 22.946  -9.300  -9.602  1.00 154.59 ? 435 MET A O   1 
ATOM   953  C CB  . MET A 1 135 ? 22.894  -6.895  -11.063 1.00 141.64 ? 435 MET A CB  1 
ATOM   954  C CG  . MET A 1 135 ? 21.837  -7.664  -11.846 1.00 164.05 ? 435 MET A CG  1 
ATOM   955  S SD  . MET A 1 135 ? 20.222  -6.871  -11.987 1.00 190.62 ? 435 MET A SD  1 
ATOM   956  C CE  . MET A 1 135 ? 19.544  -7.864  -13.327 1.00 192.56 ? 435 MET A CE  1 
ATOM   957  N N   . GLU A 1 136 ? 22.323  -8.379  -7.626  1.00 109.23 ? 436 GLU A N   1 
ATOM   958  C CA  . GLU A 1 136 ? 22.117  -9.628  -6.900  1.00 97.29  ? 436 GLU A CA  1 
ATOM   959  C C   . GLU A 1 136 ? 20.619  -9.890  -6.786  1.00 91.14  ? 436 GLU A C   1 
ATOM   960  O O   . GLU A 1 136 ? 20.148  -10.992 -7.045  1.00 88.39  ? 436 GLU A O   1 
ATOM   961  C CB  . GLU A 1 136 ? 22.777  -9.532  -5.522  1.00 97.47  ? 436 GLU A CB  1 
ATOM   962  C CG  . GLU A 1 136 ? 24.277  -9.793  -5.574  1.00 103.36 ? 436 GLU A CG  1 
ATOM   963  C CD  . GLU A 1 136 ? 24.683  -11.258 -5.645  1.00 106.07 ? 436 GLU A CD  1 
ATOM   964  O OE1 . GLU A 1 136 ? 24.328  -12.057 -6.552  1.00 98.76  ? 436 GLU A OE1 1 
ATOM   965  O OE2 . GLU A 1 136 ? 25.432  -11.580 -4.707  1.00 114.23 ? 436 GLU A OE2 1 
ATOM   966  N N   . ILE A 1 137 ? 19.890  -8.856  -6.347  1.00 91.07  ? 437 ILE A N   1 
ATOM   967  C CA  . ILE A 1 137 ? 18.441  -8.810  -6.412  1.00 86.02  ? 437 ILE A CA  1 
ATOM   968  C C   . ILE A 1 137 ? 18.056  -7.712  -7.397  1.00 84.86  ? 437 ILE A C   1 
ATOM   969  O O   . ILE A 1 137 ? 18.656  -6.638  -7.374  1.00 78.30  ? 437 ILE A O   1 
ATOM   970  C CB  . ILE A 1 137 ? 17.840  -8.546  -5.023  1.00 83.27  ? 437 ILE A CB  1 
ATOM   971  C CG1 . ILE A 1 137 ? 18.362  -9.540  -3.983  1.00 81.05  ? 437 ILE A CG1 1 
ATOM   972  C CG2 . ILE A 1 137 ? 16.310  -8.528  -5.094  1.00 86.82  ? 437 ILE A CG2 1 
ATOM   973  C CD1 . ILE A 1 137 ? 17.888  -9.247  -2.568  1.00 78.96  ? 437 ILE A CD1 1 
ATOM   974  N N   . LYS A 1 138 ? 17.063  -8.012  -8.248  1.00 87.96  ? 438 LYS A N   1 
ATOM   975  C CA  . LYS A 1 138 ? 16.612  -7.106  -9.291  1.00 91.95  ? 438 LYS A CA  1 
ATOM   976  C C   . LYS A 1 138 ? 15.988  -5.871  -8.641  1.00 87.14  ? 438 LYS A C   1 
ATOM   977  O O   . LYS A 1 138 ? 15.395  -5.962  -7.566  1.00 87.18  ? 438 LYS A O   1 
ATOM   978  C CB  . LYS A 1 138 ? 15.636  -7.891  -10.173 1.00 101.82 ? 438 LYS A CB  1 
ATOM   979  C CG  . LYS A 1 138 ? 15.150  -7.185  -11.433 1.00 112.86 ? 438 LYS A CG  1 
ATOM   980  C CD  . LYS A 1 138 ? 16.126  -7.175  -12.609 1.00 119.86 ? 438 LYS A CD  1 
ATOM   981  C CE  . LYS A 1 138 ? 15.760  -6.180  -13.692 1.00 122.32 ? 438 LYS A CE  1 
ATOM   982  N NZ  . LYS A 1 138 ? 15.861  -4.779  -13.256 1.00 114.16 ? 438 LYS A NZ  1 
ATOM   983  N N   . LYS A 1 139 ? 16.126  -4.713  -9.298  1.00 84.60  ? 439 LYS A N   1 
ATOM   984  C CA  . LYS A 1 139 ? 15.810  -3.430  -8.681  1.00 80.68  ? 439 LYS A CA  1 
ATOM   985  C C   . LYS A 1 139 ? 14.359  -3.406  -8.210  1.00 78.52  ? 439 LYS A C   1 
ATOM   986  O O   . LYS A 1 139 ? 14.110  -3.099  -7.057  1.00 71.54  ? 439 LYS A O   1 
ATOM   987  C CB  . LYS A 1 139 ? 16.163  -2.268  -9.616  1.00 83.85  ? 439 LYS A CB  1 
ATOM   988  C CG  . LYS A 1 139 ? 15.432  -2.236  -10.942 1.00 93.00  ? 439 LYS A CG  1 
ATOM   989  C CD  . LYS A 1 139 ? 16.192  -1.609  -12.108 1.00 98.39  ? 439 LYS A CD  1 
ATOM   990  C CE  . LYS A 1 139 ? 15.365  -1.605  -13.363 1.00 103.53 ? 439 LYS A CE  1 
ATOM   991  N NZ  . LYS A 1 139 ? 16.173  -1.604  -14.585 1.00 108.37 ? 439 LYS A NZ  1 
ATOM   992  N N   . GLU A 1 140 ? 13.418  -3.777  -9.084  1.00 85.12  ? 440 GLU A N   1 
ATOM   993  C CA  . GLU A 1 140 ? 11.995  -3.722  -8.769  1.00 89.48  ? 440 GLU A CA  1 
ATOM   994  C C   . GLU A 1 140 ? 11.623  -4.676  -7.633  1.00 88.53  ? 440 GLU A C   1 
ATOM   995  O O   . GLU A 1 140 ? 10.658  -4.417  -6.913  1.00 92.76  ? 440 GLU A O   1 
ATOM   996  C CB  . GLU A 1 140 ? 11.107  -4.101  -9.953  1.00 95.96  ? 440 GLU A CB  1 
ATOM   997  C CG  . GLU A 1 140 ? 11.150  -3.088  -11.093 1.00 100.67 ? 440 GLU A CG  1 
ATOM   998  C CD  . GLU A 1 140 ? 12.313  -3.203  -12.066 1.00 103.94 ? 440 GLU A CD  1 
ATOM   999  O OE1 . GLU A 1 140 ? 13.261  -3.986  -11.826 1.00 102.02 ? 440 GLU A OE1 1 
ATOM   1000 O OE2 . GLU A 1 140 ? 12.242  -2.513  -13.113 1.00 109.78 ? 440 GLU A OE2 1 
ATOM   1001 N N   . THR A 1 141 ? 12.371  -5.780  -7.493  1.00 83.14  ? 441 THR A N   1 
ATOM   1002 C CA  . THR A 1 141 ? 12.085  -6.789  -6.484  1.00 80.66  ? 441 THR A CA  1 
ATOM   1003 C C   . THR A 1 141 ? 12.544  -6.280  -5.115  1.00 76.50  ? 441 THR A C   1 
ATOM   1004 O O   . THR A 1 141 ? 11.813  -6.397  -4.127  1.00 72.76  ? 441 THR A O   1 
ATOM   1005 C CB  . THR A 1 141 ? 12.750  -8.118  -6.872  1.00 82.34  ? 441 THR A CB  1 
ATOM   1006 O OG1 . THR A 1 141 ? 12.097  -8.653  -8.020  1.00 86.06  ? 441 THR A OG1 1 
ATOM   1007 C CG2 . THR A 1 141 ? 12.634  -9.191  -5.803  1.00 81.35  ? 441 THR A CG2 1 
ATOM   1008 N N   . ALA A 1 142 ? 13.766  -5.730  -5.055  1.00 75.53  ? 442 ALA A N   1 
ATOM   1009 C CA  . ALA A 1 142 ? 14.236  -5.103  -3.830  1.00 72.98  ? 442 ALA A CA  1 
ATOM   1010 C C   . ALA A 1 142 ? 13.194  -4.090  -3.374  1.00 72.07  ? 442 ALA A C   1 
ATOM   1011 O O   . ALA A 1 142 ? 12.663  -4.208  -2.274  1.00 73.76  ? 442 ALA A O   1 
ATOM   1012 C CB  . ALA A 1 142 ? 15.584  -4.449  -4.030  1.00 71.42  ? 442 ALA A CB  1 
ATOM   1013 N N   . ALA A 1 143 ? 12.863  -3.144  -4.264  1.00 71.52  ? 443 ALA A N   1 
ATOM   1014 C CA  . ALA A 1 143 ? 11.853  -2.134  -3.989  1.00 72.55  ? 443 ALA A CA  1 
ATOM   1015 C C   . ALA A 1 143 ? 10.544  -2.798  -3.567  1.00 74.07  ? 443 ALA A C   1 
ATOM   1016 O O   . ALA A 1 143 ? 9.990   -2.444  -2.537  1.00 74.38  ? 443 ALA A O   1 
ATOM   1017 C CB  . ALA A 1 143 ? 11.664  -1.233  -5.187  1.00 73.48  ? 443 ALA A CB  1 
ATOM   1018 N N   . GLU A 1 144 ? 10.070  -3.783  -4.330  1.00 79.70  ? 444 GLU A N   1 
ATOM   1019 C CA  . GLU A 1 144 ? 8.853   -4.490  -3.954  1.00 84.49  ? 444 GLU A CA  1 
ATOM   1020 C C   . GLU A 1 144 ? 8.936   -4.931  -2.490  1.00 81.96  ? 444 GLU A C   1 
ATOM   1021 O O   . GLU A 1 144 ? 8.031   -4.632  -1.708  1.00 82.05  ? 444 GLU A O   1 
ATOM   1022 C CB  . GLU A 1 144 ? 8.576   -5.666  -4.887  1.00 89.19  ? 444 GLU A CB  1 
ATOM   1023 C CG  . GLU A 1 144 ? 7.927   -5.238  -6.202  1.00 98.58  ? 444 GLU A CG  1 
ATOM   1024 C CD  . GLU A 1 144 ? 7.839   -6.325  -7.265  1.00 110.08 ? 444 GLU A CD  1 
ATOM   1025 O OE1 . GLU A 1 144 ? 7.180   -7.341  -6.937  1.00 111.92 ? 444 GLU A OE1 1 
ATOM   1026 O OE2 . GLU A 1 144 ? 8.394   -6.184  -8.389  1.00 110.92 ? 444 GLU A OE2 1 
ATOM   1027 N N   . ILE A 1 145 ? 10.045  -5.593  -2.128  1.00 75.90  ? 445 ILE A N   1 
ATOM   1028 C CA  . ILE A 1 145 ? 10.217  -6.178  -0.808  1.00 71.01  ? 445 ILE A CA  1 
ATOM   1029 C C   . ILE A 1 145 ? 10.361  -5.094  0.257   1.00 65.22  ? 445 ILE A C   1 
ATOM   1030 O O   . ILE A 1 145 ? 9.766   -5.193  1.328   1.00 62.73  ? 445 ILE A O   1 
ATOM   1031 C CB  . ILE A 1 145 ? 11.420  -7.135  -0.799  1.00 74.56  ? 445 ILE A CB  1 
ATOM   1032 C CG1 . ILE A 1 145 ? 11.135  -8.368  -1.657  1.00 81.36  ? 445 ILE A CG1 1 
ATOM   1033 C CG2 . ILE A 1 145 ? 11.811  -7.530  0.629   1.00 72.49  ? 445 ILE A CG2 1 
ATOM   1034 C CD1 . ILE A 1 145 ? 12.297  -9.339  -1.762  1.00 81.44  ? 445 ILE A CD1 1 
ATOM   1035 N N   . LEU A 1 146 ? 11.181  -4.080  -0.034  1.00 64.03  ? 446 LEU A N   1 
ATOM   1036 C CA  . LEU A 1 146 ? 11.447  -3.008  0.909   1.00 61.00  ? 446 LEU A CA  1 
ATOM   1037 C C   . LEU A 1 146 ? 10.146  -2.318  1.306   1.00 61.88  ? 446 LEU A C   1 
ATOM   1038 O O   . LEU A 1 146 ? 9.853   -2.217  2.497   1.00 64.95  ? 446 LEU A O   1 
ATOM   1039 C CB  . LEU A 1 146 ? 12.455  -2.017  0.333   1.00 64.71  ? 446 LEU A CB  1 
ATOM   1040 C CG  . LEU A 1 146 ? 13.947  -2.390  0.394   1.00 64.92  ? 446 LEU A CG  1 
ATOM   1041 C CD1 . LEU A 1 146 ? 14.745  -1.110  0.570   1.00 67.91  ? 446 LEU A CD1 1 
ATOM   1042 C CD2 . LEU A 1 146 ? 14.343  -3.352  1.476   1.00 63.51  ? 446 LEU A CD2 1 
ATOM   1043 N N   . PHE A 1 147 ? 9.348   -1.876  0.324   1.00 64.92  ? 447 PHE A N   1 
ATOM   1044 C CA  . PHE A 1 147 ? 8.047   -1.275  0.616   1.00 67.85  ? 447 PHE A CA  1 
ATOM   1045 C C   . PHE A 1 147 ? 7.144   -2.280  1.337   1.00 73.35  ? 447 PHE A C   1 
ATOM   1046 O O   . PHE A 1 147 ? 6.513   -1.924  2.334   1.00 71.12  ? 447 PHE A O   1 
ATOM   1047 C CB  . PHE A 1 147 ? 7.348   -0.706  -0.624  1.00 68.41  ? 447 PHE A CB  1 
ATOM   1048 C CG  . PHE A 1 147 ? 7.977   0.595   -1.083  1.00 69.32  ? 447 PHE A CG  1 
ATOM   1049 C CD1 . PHE A 1 147 ? 9.039   0.601   -1.974  1.00 70.78  ? 447 PHE A CD1 1 
ATOM   1050 C CD2 . PHE A 1 147 ? 7.553   1.816   -0.571  1.00 75.70  ? 447 PHE A CD2 1 
ATOM   1051 C CE1 . PHE A 1 147 ? 9.635   1.797   -2.371  1.00 71.71  ? 447 PHE A CE1 1 
ATOM   1052 C CE2 . PHE A 1 147 ? 8.156   3.008   -0.976  1.00 74.16  ? 447 PHE A CE2 1 
ATOM   1053 C CZ  . PHE A 1 147 ? 9.197   2.994   -1.870  1.00 70.05  ? 447 PHE A CZ  1 
ATOM   1054 N N   . ASP A 1 148 ? 7.079   -3.520  0.820   1.00 80.76  ? 448 ASP A N   1 
ATOM   1055 C CA  . ASP A 1 148 ? 6.264   -4.589  1.389   1.00 87.55  ? 448 ASP A CA  1 
ATOM   1056 C C   . ASP A 1 148 ? 6.415   -4.588  2.910   1.00 79.67  ? 448 ASP A C   1 
ATOM   1057 O O   . ASP A 1 148 ? 5.428   -4.484  3.631   1.00 82.28  ? 448 ASP A O   1 
ATOM   1058 C CB  . ASP A 1 148 ? 6.650   -5.939  0.793   1.00 100.17 ? 448 ASP A CB  1 
ATOM   1059 C CG  . ASP A 1 148 ? 5.583   -7.027  0.618   1.00 110.45 ? 448 ASP A CG  1 
ATOM   1060 O OD1 . ASP A 1 148 ? 4.377   -6.718  0.765   1.00 118.12 ? 448 ASP A OD1 1 
ATOM   1061 O OD2 . ASP A 1 148 ? 5.971   -8.188  0.310   1.00 108.85 ? 448 ASP A OD2 1 
ATOM   1062 N N   . GLU A 1 149 ? 7.651   -4.715  3.395   1.00 70.66  ? 449 GLU A N   1 
ATOM   1063 C CA  . GLU A 1 149 ? 7.873   -4.870  4.822   1.00 71.69  ? 449 GLU A CA  1 
ATOM   1064 C C   . GLU A 1 149 ? 7.557   -3.579  5.579   1.00 69.67  ? 449 GLU A C   1 
ATOM   1065 O O   . GLU A 1 149 ? 6.938   -3.615  6.647   1.00 71.24  ? 449 GLU A O   1 
ATOM   1066 C CB  . GLU A 1 149 ? 9.310   -5.326  5.046   1.00 69.67  ? 449 GLU A CB  1 
ATOM   1067 C CG  . GLU A 1 149 ? 9.520   -6.760  4.596   1.00 75.70  ? 449 GLU A CG  1 
ATOM   1068 C CD  . GLU A 1 149 ? 8.607   -7.723  5.335   1.00 82.41  ? 449 GLU A CD  1 
ATOM   1069 O OE1 . GLU A 1 149 ? 8.726   -7.767  6.578   1.00 80.87  ? 449 GLU A OE1 1 
ATOM   1070 O OE2 . GLU A 1 149 ? 7.760   -8.390  4.690   1.00 85.21  ? 449 GLU A OE2 1 
ATOM   1071 N N   . VAL A 1 150 ? 7.999   -2.446  5.023   1.00 64.14  ? 450 VAL A N   1 
ATOM   1072 C CA  . VAL A 1 150 ? 7.753   -1.161  5.647   1.00 62.65  ? 450 VAL A CA  1 
ATOM   1073 C C   . VAL A 1 150 ? 6.250   -1.005  5.831   1.00 65.60  ? 450 VAL A C   1 
ATOM   1074 O O   . VAL A 1 150 ? 5.799   -0.769  6.944   1.00 66.32  ? 450 VAL A O   1 
ATOM   1075 C CB  . VAL A 1 150 ? 8.372   0.032   4.888   1.00 60.90  ? 450 VAL A CB  1 
ATOM   1076 C CG1 . VAL A 1 150 ? 7.877   1.376   5.418   1.00 61.64  ? 450 VAL A CG1 1 
ATOM   1077 C CG2 . VAL A 1 150 ? 9.890   0.005   4.971   1.00 57.11  ? 450 VAL A CG2 1 
ATOM   1078 N N   . LEU A 1 151 ? 5.482   -1.173  4.751   1.00 71.27  ? 451 LEU A N   1 
ATOM   1079 C CA  . LEU A 1 151 ? 4.040   -0.980  4.819   1.00 76.66  ? 451 LEU A CA  1 
ATOM   1080 C C   . LEU A 1 151 ? 3.422   -1.949  5.822   1.00 82.90  ? 451 LEU A C   1 
ATOM   1081 O O   . LEU A 1 151 ? 2.495   -1.575  6.525   1.00 87.63  ? 451 LEU A O   1 
ATOM   1082 C CB  . LEU A 1 151 ? 3.374   -1.116  3.452   1.00 78.04  ? 451 LEU A CB  1 
ATOM   1083 C CG  . LEU A 1 151 ? 3.741   -0.050  2.416   1.00 78.26  ? 451 LEU A CG  1 
ATOM   1084 C CD1 . LEU A 1 151 ? 2.571   0.168   1.482   1.00 82.22  ? 451 LEU A CD1 1 
ATOM   1085 C CD2 . LEU A 1 151 ? 4.181   1.281   3.009   1.00 76.83  ? 451 LEU A CD2 1 
ATOM   1086 N N   . THR A 1 152 ? 3.932   -3.184  5.873   1.00 88.70  ? 452 THR A N   1 
ATOM   1087 C CA  . THR A 1 152 ? 3.429   -4.196  6.790   1.00 95.22  ? 452 THR A CA  1 
ATOM   1088 C C   . THR A 1 152 ? 3.483   -3.656  8.217   1.00 92.87  ? 452 THR A C   1 
ATOM   1089 O O   . THR A 1 152 ? 2.485   -3.687  8.935   1.00 91.73  ? 452 THR A O   1 
ATOM   1090 C CB  . THR A 1 152 ? 4.248   -5.482  6.638   1.00 98.12  ? 452 THR A CB  1 
ATOM   1091 O OG1 . THR A 1 152 ? 3.807   -6.061  5.412   1.00 100.12 ? 452 THR A OG1 1 
ATOM   1092 C CG2 . THR A 1 152 ? 4.005   -6.479  7.762   1.00 101.37 ? 452 THR A CG2 1 
ATOM   1093 N N   . PHE A 1 153 ? 4.673   -3.174  8.593   1.00 92.69  ? 453 PHE A N   1 
ATOM   1094 C CA  . PHE A 1 153 ? 4.938   -2.603  9.903   1.00 89.29  ? 453 PHE A CA  1 
ATOM   1095 C C   . PHE A 1 153 ? 3.968   -1.462  10.216  1.00 92.57  ? 453 PHE A C   1 
ATOM   1096 O O   . PHE A 1 153 ? 3.443   -1.359  11.323  1.00 93.42  ? 453 PHE A O   1 
ATOM   1097 C CB  . PHE A 1 153 ? 6.382   -2.095  9.887   1.00 82.92  ? 453 PHE A CB  1 
ATOM   1098 C CG  . PHE A 1 153 ? 6.749   -1.362  11.163  1.00 80.83  ? 453 PHE A CG  1 
ATOM   1099 C CD1 . PHE A 1 153 ? 6.389   -0.027  11.346  1.00 81.80  ? 453 PHE A CD1 1 
ATOM   1100 C CD2 . PHE A 1 153 ? 7.428   -2.018  12.180  1.00 78.83  ? 453 PHE A CD2 1 
ATOM   1101 C CE1 . PHE A 1 153 ? 6.699   0.633   12.523  1.00 81.26  ? 453 PHE A CE1 1 
ATOM   1102 C CE2 . PHE A 1 153 ? 7.740   -1.354  13.356  1.00 80.89  ? 453 PHE A CE2 1 
ATOM   1103 C CZ  . PHE A 1 153 ? 7.382   -0.028  13.523  1.00 82.03  ? 453 PHE A CZ  1 
ATOM   1104 N N   . ALA A 1 154 ? 3.751   -0.593  9.226   1.00 94.29  ? 454 ALA A N   1 
ATOM   1105 C CA  . ALA A 1 154 ? 2.864   0.547   9.382   1.00 105.43 ? 454 ALA A CA  1 
ATOM   1106 C C   . ALA A 1 154 ? 1.459   0.101   9.793   1.00 116.43 ? 454 ALA A C   1 
ATOM   1107 O O   . ALA A 1 154 ? 0.800   0.814   10.547  1.00 133.52 ? 454 ALA A O   1 
ATOM   1108 C CB  . ALA A 1 154 ? 2.836   1.355   8.102   1.00 107.17 ? 454 ALA A CB  1 
ATOM   1109 N N   . LYS A 1 155 ? 1.006   -1.059  9.282   1.00 112.53 ? 455 LYS A N   1 
ATOM   1110 C CA  . LYS A 1 155 ? -0.322  -1.584  9.568   1.00 109.44 ? 455 LYS A CA  1 
ATOM   1111 C C   . LYS A 1 155 ? -0.305  -2.332  10.901  1.00 103.51 ? 455 LYS A C   1 
ATOM   1112 O O   . LYS A 1 155 ? -1.240  -2.224  11.683  1.00 101.18 ? 455 LYS A O   1 
ATOM   1113 C CB  . LYS A 1 155 ? -0.806  -2.485  8.424   1.00 113.69 ? 455 LYS A CB  1 
ATOM   1114 C CG  . LYS A 1 155 ? -2.259  -2.934  8.505   1.00 127.11 ? 455 LYS A CG  1 
ATOM   1115 C CD  . LYS A 1 155 ? -2.513  -4.363  8.029   1.00 134.30 ? 455 LYS A CD  1 
ATOM   1116 C CE  . LYS A 1 155 ? -1.886  -4.678  6.701   1.00 135.00 ? 455 LYS A CE  1 
ATOM   1117 N NZ  . LYS A 1 155 ? -2.298  -5.993  6.202   1.00 139.17 ? 455 LYS A NZ  1 
ATOM   1118 N N   . ASP A 1 156 ? 0.776   -3.060  11.176  1.00 102.01 ? 456 ASP A N   1 
ATOM   1119 C CA  . ASP A 1 156 ? 0.802   -3.993  12.289  1.00 106.22 ? 456 ASP A CA  1 
ATOM   1120 C C   . ASP A 1 156 ? 1.305   -3.324  13.571  1.00 105.35 ? 456 ASP A C   1 
ATOM   1121 O O   . ASP A 1 156 ? 1.232   -3.919  14.643  1.00 104.05 ? 456 ASP A O   1 
ATOM   1122 C CB  . ASP A 1 156 ? 1.590   -5.240  11.912  1.00 110.24 ? 456 ASP A CB  1 
ATOM   1123 C CG  . ASP A 1 156 ? 0.977   -6.115  10.825  1.00 114.99 ? 456 ASP A CG  1 
ATOM   1124 O OD1 . ASP A 1 156 ? -0.108  -5.759  10.312  1.00 114.11 ? 456 ASP A OD1 1 
ATOM   1125 O OD2 . ASP A 1 156 ? 1.594   -7.153  10.502  1.00 120.80 ? 456 ASP A OD2 1 
ATOM   1126 N N   . HIS A 1 157 ? 1.838   -2.099  13.482  1.00 103.46 ? 457 HIS A N   1 
ATOM   1127 C CA  . HIS A 1 157 ? 2.255   -1.402  14.688  1.00 99.63  ? 457 HIS A CA  1 
ATOM   1128 C C   . HIS A 1 157 ? 2.086   0.099   14.469  1.00 101.68 ? 457 HIS A C   1 
ATOM   1129 O O   . HIS A 1 157 ? 3.059   0.842   14.322  1.00 105.71 ? 457 HIS A O   1 
ATOM   1130 C CB  . HIS A 1 157 ? 3.680   -1.788  15.100  1.00 95.00  ? 457 HIS A CB  1 
ATOM   1131 C CG  . HIS A 1 157 ? 4.079   -3.229  14.966  1.00 91.61  ? 457 HIS A CG  1 
ATOM   1132 N ND1 . HIS A 1 157 ? 4.599   -3.749  13.796  1.00 85.32  ? 457 HIS A ND1 1 
ATOM   1133 C CD2 . HIS A 1 157 ? 4.112   -4.220  15.860  1.00 93.47  ? 457 HIS A CD2 1 
ATOM   1134 C CE1 . HIS A 1 157 ? 4.911   -5.019  13.985  1.00 87.70  ? 457 HIS A CE1 1 
ATOM   1135 N NE2 . HIS A 1 157 ? 4.627   -5.322  15.230  1.00 92.57  ? 457 HIS A NE2 1 
ATOM   1136 N N   . VAL A 1 158 ? 0.815   0.518   14.483  1.00 106.87 ? 458 VAL A N   1 
ATOM   1137 C CA  . VAL A 1 158 ? 0.388   1.870   14.147  1.00 104.11 ? 458 VAL A CA  1 
ATOM   1138 C C   . VAL A 1 158 ? 0.578   2.802   15.349  1.00 97.78  ? 458 VAL A C   1 
ATOM   1139 O O   . VAL A 1 158 ? 0.493   4.023   15.225  1.00 88.22  ? 458 VAL A O   1 
ATOM   1140 C CB  . VAL A 1 158 ? -1.078  1.802   13.660  1.00 107.29 ? 458 VAL A CB  1 
ATOM   1141 C CG1 . VAL A 1 158 ? -2.026  1.217   14.705  1.00 110.50 ? 458 VAL A CG1 1 
ATOM   1142 C CG2 . VAL A 1 158 ? -1.576  3.148   13.147  1.00 108.19 ? 458 VAL A CG2 1 
ATOM   1143 N N   . LYS A 1 159 ? 0.849   2.215   16.520  1.00 97.11  ? 459 LYS A N   1 
ATOM   1144 C CA  . LYS A 1 159 ? 1.110   2.983   17.726  1.00 96.98  ? 459 LYS A CA  1 
ATOM   1145 C C   . LYS A 1 159 ? 2.524   3.562   17.727  1.00 89.42  ? 459 LYS A C   1 
ATOM   1146 O O   . LYS A 1 159 ? 2.815   4.411   18.559  1.00 91.76  ? 459 LYS A O   1 
ATOM   1147 C CB  . LYS A 1 159 ? 0.915   2.097   18.960  1.00 101.37 ? 459 LYS A CB  1 
ATOM   1148 C CG  . LYS A 1 159 ? -0.496  1.529   19.108  1.00 110.32 ? 459 LYS A CG  1 
ATOM   1149 C CD  . LYS A 1 159 ? -0.553  0.178   19.821  1.00 117.48 ? 459 LYS A CD  1 
ATOM   1150 C CE  . LYS A 1 159 ? -1.630  -0.750  19.330  1.00 118.87 ? 459 LYS A CE  1 
ATOM   1151 N NZ  . LYS A 1 159 ? -1.386  -2.113  19.804  1.00 122.09 ? 459 LYS A NZ  1 
ATOM   1152 N N   . HIS A 1 160 ? 3.399   3.103   16.814  1.00 83.40  ? 460 HIS A N   1 
ATOM   1153 C CA  . HIS A 1 160 ? 4.800   3.512   16.791  1.00 77.85  ? 460 HIS A CA  1 
ATOM   1154 C C   . HIS A 1 160 ? 5.051   4.489   15.642  1.00 79.04  ? 460 HIS A C   1 
ATOM   1155 O O   . HIS A 1 160 ? 4.837   4.133   14.475  1.00 80.17  ? 460 HIS A O   1 
ATOM   1156 C CB  . HIS A 1 160 ? 5.734   2.308   16.635  1.00 71.21  ? 460 HIS A CB  1 
ATOM   1157 C CG  . HIS A 1 160 ? 7.184   2.587   16.898  1.00 63.53  ? 460 HIS A CG  1 
ATOM   1158 N ND1 . HIS A 1 160 ? 7.752   2.551   18.155  1.00 63.14  ? 460 HIS A ND1 1 
ATOM   1159 C CD2 . HIS A 1 160 ? 8.187   2.859   16.065  1.00 58.88  ? 460 HIS A CD2 1 
ATOM   1160 C CE1 . HIS A 1 160 ? 9.057   2.795   18.072  1.00 59.44  ? 460 HIS A CE1 1 
ATOM   1161 N NE2 . HIS A 1 160 ? 9.340   3.002   16.814  1.00 57.91  ? 460 HIS A NE2 1 
ATOM   1162 N N   . GLN A 1 161 ? 5.491   5.714   16.001  1.00 78.98  ? 461 GLN A N   1 
ATOM   1163 C CA  . GLN A 1 161 ? 5.853   6.746   15.037  1.00 70.87  ? 461 GLN A CA  1 
ATOM   1164 C C   . GLN A 1 161 ? 7.221   6.414   14.497  1.00 61.49  ? 461 GLN A C   1 
ATOM   1165 O O   . GLN A 1 161 ? 8.149   6.252   15.285  1.00 59.01  ? 461 GLN A O   1 
ATOM   1166 C CB  . GLN A 1 161 ? 6.056   8.181   15.531  1.00 73.28  ? 461 GLN A CB  1 
ATOM   1167 C CG  . GLN A 1 161 ? 4.773   9.009   15.553  1.00 78.42  ? 461 GLN A CG  1 
ATOM   1168 C CD  . GLN A 1 161 ? 4.998   10.504  15.477  1.00 75.87  ? 461 GLN A CD  1 
ATOM   1169 O OE1 . GLN A 1 161 ? 5.653   10.994  14.554  1.00 77.82  ? 461 GLN A OE1 1 
ATOM   1170 N NE2 . GLN A 1 161 ? 4.436   11.248  16.419  1.00 76.98  ? 461 GLN A NE2 1 
ATOM   1171 N N   . LEU A 1 162 ? 7.318   6.352   13.165  1.00 58.50  ? 462 LEU A N   1 
ATOM   1172 C CA  . LEU A 1 162 ? 8.579   6.034   12.519  1.00 58.42  ? 462 LEU A CA  1 
ATOM   1173 C C   . LEU A 1 162 ? 8.741   6.887   11.269  1.00 52.65  ? 462 LEU A C   1 
ATOM   1174 O O   . LEU A 1 162 ? 7.773   7.061   10.525  1.00 49.54  ? 462 LEU A O   1 
ATOM   1175 C CB  . LEU A 1 162 ? 8.627   4.544   12.171  1.00 62.20  ? 462 LEU A CB  1 
ATOM   1176 C CG  . LEU A 1 162 ? 10.002  3.990   11.780  1.00 60.67  ? 462 LEU A CG  1 
ATOM   1177 C CD1 . LEU A 1 162 ? 11.028  4.062   12.919  1.00 59.79  ? 462 LEU A CD1 1 
ATOM   1178 C CD2 . LEU A 1 162 ? 9.816   2.559   11.324  1.00 67.70  ? 462 LEU A CD2 1 
ATOM   1179 N N   . THR A 1 163 ? 9.973   7.384   11.062  1.00 50.24  ? 463 THR A N   1 
ATOM   1180 C CA  . THR A 1 163 ? 10.358  7.980   9.790   1.00 52.56  ? 463 THR A CA  1 
ATOM   1181 C C   . THR A 1 163 ? 11.314  7.004   9.117   1.00 48.66  ? 463 THR A C   1 
ATOM   1182 O O   . THR A 1 163 ? 12.362  6.693   9.673   1.00 50.59  ? 463 THR A O   1 
ATOM   1183 C CB  . THR A 1 163 ? 11.001  9.371   9.930   1.00 49.01  ? 463 THR A CB  1 
ATOM   1184 O OG1 . THR A 1 163 ? 10.218  10.169  10.805  1.00 49.36  ? 463 THR A OG1 1 
ATOM   1185 C CG2 . THR A 1 163 ? 11.081  10.086  8.595   1.00 48.05  ? 463 THR A CG2 1 
ATOM   1186 N N   . VAL A 1 164 ? 10.945  6.563   7.915   1.00 49.04  ? 464 VAL A N   1 
ATOM   1187 C CA  . VAL A 1 164 ? 11.769  5.644   7.142   1.00 50.30  ? 464 VAL A CA  1 
ATOM   1188 C C   . VAL A 1 164 ? 12.234  6.342   5.866   1.00 50.33  ? 464 VAL A C   1 
ATOM   1189 O O   . VAL A 1 164 ? 11.426  6.819   5.091   1.00 50.51  ? 464 VAL A O   1 
ATOM   1190 C CB  . VAL A 1 164 ? 11.008  4.346   6.820   1.00 49.54  ? 464 VAL A CB  1 
ATOM   1191 C CG1 . VAL A 1 164 ? 11.814  3.433   5.901   1.00 48.97  ? 464 VAL A CG1 1 
ATOM   1192 C CG2 . VAL A 1 164 ? 10.585  3.618   8.098   1.00 48.59  ? 464 VAL A CG2 1 
ATOM   1193 N N   . LYS A 1 165 ? 13.547  6.412   5.679   1.00 51.51  ? 465 LYS A N   1 
ATOM   1194 C CA  . LYS A 1 165 ? 14.127  6.889   4.441   1.00 52.18  ? 465 LYS A CA  1 
ATOM   1195 C C   . LYS A 1 165 ? 14.747  5.702   3.712   1.00 49.30  ? 465 LYS A C   1 
ATOM   1196 O O   . LYS A 1 165 ? 15.436  4.912   4.338   1.00 45.76  ? 465 LYS A O   1 
ATOM   1197 C CB  . LYS A 1 165 ? 15.182  7.947   4.759   1.00 52.20  ? 465 LYS A CB  1 
ATOM   1198 C CG  . LYS A 1 165 ? 14.557  9.215   5.324   1.00 58.87  ? 465 LYS A CG  1 
ATOM   1199 C CD  . LYS A 1 165 ? 15.409  10.481  5.407   1.00 56.36  ? 465 LYS A CD  1 
ATOM   1200 C CE  . LYS A 1 165 ? 14.598  11.517  6.091   1.00 61.23  ? 465 LYS A CE  1 
ATOM   1201 N NZ  . LYS A 1 165 ? 15.324  12.773  6.288   1.00 70.29  ? 465 LYS A NZ  1 
ATOM   1202 N N   . PHE A 1 166 ? 14.456  5.575   2.412   1.00 46.53  ? 466 PHE A N   1 
ATOM   1203 C CA  . PHE A 1 166 ? 15.268  4.784   1.517   1.00 45.11  ? 466 PHE A CA  1 
ATOM   1204 C C   . PHE A 1 166 ? 16.247  5.716   0.819   1.00 46.14  ? 466 PHE A C   1 
ATOM   1205 O O   . PHE A 1 166 ? 15.867  6.453   -0.080  1.00 50.11  ? 466 PHE A O   1 
ATOM   1206 C CB  . PHE A 1 166 ? 14.441  4.030   0.475   1.00 46.74  ? 466 PHE A CB  1 
ATOM   1207 C CG  . PHE A 1 166 ? 13.388  3.088   1.046   1.00 46.59  ? 466 PHE A CG  1 
ATOM   1208 C CD1 . PHE A 1 166 ? 13.649  2.321   2.183   1.00 44.19  ? 466 PHE A CD1 1 
ATOM   1209 C CD2 . PHE A 1 166 ? 12.142  2.966   0.424   1.00 46.91  ? 466 PHE A CD2 1 
ATOM   1210 C CE1 . PHE A 1 166 ? 12.672  1.476   2.692   1.00 45.96  ? 466 PHE A CE1 1 
ATOM   1211 C CE2 . PHE A 1 166 ? 11.165  2.142   0.945   1.00 47.70  ? 466 PHE A CE2 1 
ATOM   1212 C CZ  . PHE A 1 166 ? 11.423  1.404   2.077   1.00 48.26  ? 466 PHE A CZ  1 
ATOM   1213 N N   . VAL A 1 167 ? 17.519  5.610   1.200   1.00 45.97  ? 467 VAL A N   1 
ATOM   1214 C CA  . VAL A 1 167 ? 18.605  6.368   0.612   1.00 48.05  ? 467 VAL A CA  1 
ATOM   1215 C C   . VAL A 1 167 ? 19.141  5.693   -0.657  1.00 50.20  ? 467 VAL A C   1 
ATOM   1216 O O   . VAL A 1 167 ? 19.776  4.639   -0.611  1.00 50.99  ? 467 VAL A O   1 
ATOM   1217 C CB  . VAL A 1 167 ? 19.666  6.476   1.719   1.00 50.64  ? 467 VAL A CB  1 
ATOM   1218 C CG1 . VAL A 1 167 ? 20.852  7.339   1.295   1.00 53.06  ? 467 VAL A CG1 1 
ATOM   1219 C CG2 . VAL A 1 167 ? 19.059  7.010   3.010   1.00 53.22  ? 467 VAL A CG2 1 
ATOM   1220 N N   . ILE A 1 168 ? 18.908  6.345   -1.801  1.00 53.76  ? 468 ILE A N   1 
ATOM   1221 C CA  . ILE A 1 168 ? 19.401  5.905   -3.100  1.00 56.86  ? 468 ILE A CA  1 
ATOM   1222 C C   . ILE A 1 168 ? 20.658  6.702   -3.440  1.00 61.05  ? 468 ILE A C   1 
ATOM   1223 O O   . ILE A 1 168 ? 20.690  7.921   -3.300  1.00 64.72  ? 468 ILE A O   1 
ATOM   1224 C CB  . ILE A 1 168 ? 18.337  6.100   -4.197  1.00 55.86  ? 468 ILE A CB  1 
ATOM   1225 C CG1 . ILE A 1 168 ? 16.940  5.660   -3.769  1.00 54.37  ? 468 ILE A CG1 1 
ATOM   1226 C CG2 . ILE A 1 168 ? 18.780  5.416   -5.482  1.00 57.43  ? 468 ILE A CG2 1 
ATOM   1227 C CD1 . ILE A 1 168 ? 16.861  4.219   -3.303  1.00 54.40  ? 468 ILE A CD1 1 
ATOM   1228 N N   . PHE A 1 169 ? 21.688  6.039   -3.955  1.00 64.63  ? 469 PHE A N   1 
ATOM   1229 C CA  . PHE A 1 169 ? 22.907  6.772   -4.241  1.00 65.80  ? 469 PHE A CA  1 
ATOM   1230 C C   . PHE A 1 169 ? 22.638  7.695   -5.422  1.00 70.46  ? 469 PHE A C   1 
ATOM   1231 O O   . PHE A 1 169 ? 21.899  7.329   -6.336  1.00 69.81  ? 469 PHE A O   1 
ATOM   1232 C CB  . PHE A 1 169 ? 24.049  5.798   -4.502  1.00 67.53  ? 469 PHE A CB  1 
ATOM   1233 C CG  . PHE A 1 169 ? 25.427  6.432   -4.515  1.00 69.03  ? 469 PHE A CG  1 
ATOM   1234 C CD1 . PHE A 1 169 ? 26.018  6.867   -3.330  1.00 68.25  ? 469 PHE A CD1 1 
ATOM   1235 C CD2 . PHE A 1 169 ? 26.141  6.549   -5.704  1.00 72.77  ? 469 PHE A CD2 1 
ATOM   1236 C CE1 . PHE A 1 169 ? 27.294  7.423   -3.339  1.00 71.66  ? 469 PHE A CE1 1 
ATOM   1237 C CE2 . PHE A 1 169 ? 27.408  7.113   -5.708  1.00 76.10  ? 469 PHE A CE2 1 
ATOM   1238 C CZ  . PHE A 1 169 ? 27.986  7.539   -4.527  1.00 75.54  ? 469 PHE A CZ  1 
ATOM   1239 N N   . PRO A 1 170 ? 23.190  8.933   -5.416  1.00 76.64  ? 470 PRO A N   1 
ATOM   1240 C CA  . PRO A 1 170 ? 22.967  9.890   -6.504  1.00 79.90  ? 470 PRO A CA  1 
ATOM   1241 C C   . PRO A 1 170 ? 23.165  9.392   -7.936  1.00 81.36  ? 470 PRO A C   1 
ATOM   1242 O O   . PRO A 1 170 ? 22.297  9.633   -8.771  1.00 86.63  ? 470 PRO A O   1 
ATOM   1243 C CB  . PRO A 1 170 ? 23.966  11.004  -6.134  1.00 82.98  ? 470 PRO A CB  1 
ATOM   1244 C CG  . PRO A 1 170 ? 23.960  10.994  -4.624  1.00 78.54  ? 470 PRO A CG  1 
ATOM   1245 C CD  . PRO A 1 170 ? 24.013  9.506   -4.333  1.00 76.06  ? 470 PRO A CD  1 
ATOM   1246 N N   . THR A 1 171 ? 24.283  8.700   -8.229  1.00 80.15  ? 471 THR A N   1 
ATOM   1247 C CA  . THR A 1 171 ? 24.566  8.280   -9.602  1.00 83.72  ? 471 THR A CA  1 
ATOM   1248 C C   . THR A 1 171 ? 23.641  7.142   -10.037 1.00 83.15  ? 471 THR A C   1 
ATOM   1249 O O   . THR A 1 171 ? 23.435  6.979   -11.230 1.00 85.64  ? 471 THR A O   1 
ATOM   1250 C CB  . THR A 1 171 ? 26.028  7.876   -9.811  1.00 85.78  ? 471 THR A CB  1 
ATOM   1251 O OG1 . THR A 1 171 ? 26.302  6.838   -8.886  1.00 83.31  ? 471 THR A OG1 1 
ATOM   1252 C CG2 . THR A 1 171 ? 27.026  8.992   -9.560  1.00 88.71  ? 471 THR A CG2 1 
ATOM   1253 N N   . ASP A 1 172 ? 23.102  6.357   -9.085  1.00 82.99  ? 472 ASP A N   1 
ATOM   1254 C CA  . ASP A 1 172 ? 22.175  5.268   -9.373  1.00 83.92  ? 472 ASP A CA  1 
ATOM   1255 C C   . ASP A 1 172 ? 20.788  5.800   -9.731  1.00 80.68  ? 472 ASP A C   1 
ATOM   1256 O O   . ASP A 1 172 ? 19.846  5.665   -8.956  1.00 78.17  ? 472 ASP A O   1 
ATOM   1257 C CB  . ASP A 1 172 ? 21.991  4.340   -8.180  1.00 84.80  ? 472 ASP A CB  1 
ATOM   1258 C CG  . ASP A 1 172 ? 23.214  3.567   -7.708  1.00 88.17  ? 472 ASP A CG  1 
ATOM   1259 O OD1 . ASP A 1 172 ? 24.297  3.751   -8.297  1.00 93.26  ? 472 ASP A OD1 1 
ATOM   1260 O OD2 . ASP A 1 172 ? 23.073  2.800   -6.736  1.00 88.67  ? 472 ASP A OD2 1 
ATOM   1261 N N   . LEU A 1 173 ? 20.651  6.358   -10.932 1.00 85.71  ? 473 LEU A N   1 
ATOM   1262 C CA  . LEU A 1 173 ? 19.388  6.944   -11.347 1.00 92.35  ? 473 LEU A CA  1 
ATOM   1263 C C   . LEU A 1 173 ? 18.324  5.860   -11.537 1.00 92.89  ? 473 LEU A C   1 
ATOM   1264 O O   . LEU A 1 173 ? 17.150  6.111   -11.285 1.00 91.88  ? 473 LEU A O   1 
ATOM   1265 C CB  . LEU A 1 173 ? 19.547  7.798   -12.612 1.00 99.92  ? 473 LEU A CB  1 
ATOM   1266 C CG  . LEU A 1 173 ? 20.412  9.067   -12.526 1.00 101.40 ? 473 LEU A CG  1 
ATOM   1267 C CD1 . LEU A 1 173 ? 20.614  9.756   -13.890 1.00 94.27  ? 473 LEU A CD1 1 
ATOM   1268 C CD2 . LEU A 1 173 ? 19.902  10.059  -11.483 1.00 103.12 ? 473 LEU A CD2 1 
ATOM   1269 N N   . GLU A 1 174 ? 18.726  4.669   -12.003 1.00 95.21  ? 474 GLU A N   1 
ATOM   1270 C CA  . GLU A 1 174 ? 17.783  3.621   -12.384 1.00 96.22  ? 474 GLU A CA  1 
ATOM   1271 C C   . GLU A 1 174 ? 17.074  3.062   -11.144 1.00 89.51  ? 474 GLU A C   1 
ATOM   1272 O O   . GLU A 1 174 ? 15.848  2.891   -11.133 1.00 85.96  ? 474 GLU A O   1 
ATOM   1273 C CB  . GLU A 1 174 ? 18.523  2.536   -13.172 1.00 99.08  ? 474 GLU A CB  1 
ATOM   1274 C CG  . GLU A 1 174 ? 18.940  3.005   -14.562 1.00 107.24 ? 474 GLU A CG  1 
ATOM   1275 C CD  . GLU A 1 174 ? 17.802  3.034   -15.577 1.00 115.46 ? 474 GLU A CD  1 
ATOM   1276 O OE1 . GLU A 1 174 ? 17.388  1.932   -15.998 1.00 120.71 ? 474 GLU A OE1 1 
ATOM   1277 O OE2 . GLU A 1 174 ? 17.328  4.125   -15.968 1.00 114.45 ? 474 GLU A OE2 1 
ATOM   1278 N N   . ILE A 1 175 ? 17.867  2.783   -10.099 1.00 82.70  ? 475 ILE A N   1 
ATOM   1279 C CA  . ILE A 1 175 ? 17.362  2.281   -8.832  1.00 78.39  ? 475 ILE A CA  1 
ATOM   1280 C C   . ILE A 1 175 ? 16.328  3.270   -8.291  1.00 77.26  ? 475 ILE A C   1 
ATOM   1281 O O   . ILE A 1 175 ? 15.268  2.873   -7.802  1.00 72.41  ? 475 ILE A O   1 
ATOM   1282 C CB  . ILE A 1 175 ? 18.537  2.037   -7.854  1.00 73.71  ? 475 ILE A CB  1 
ATOM   1283 C CG1 . ILE A 1 175 ? 19.450  0.912   -8.355  1.00 73.95  ? 475 ILE A CG1 1 
ATOM   1284 C CG2 . ILE A 1 175 ? 18.043  1.746   -6.435  1.00 67.30  ? 475 ILE A CG2 1 
ATOM   1285 C CD1 . ILE A 1 175 ? 20.890  1.008   -7.885  1.00 72.80  ? 475 ILE A CD1 1 
ATOM   1286 N N   . TYR A 1 176 ? 16.655  4.566   -8.407  1.00 80.81  ? 476 TYR A N   1 
ATOM   1287 C CA  . TYR A 1 176 ? 15.767  5.648   -8.007  1.00 80.44  ? 476 TYR A CA  1 
ATOM   1288 C C   . TYR A 1 176 ? 14.435  5.575   -8.766  1.00 80.45  ? 476 TYR A C   1 
ATOM   1289 O O   . TYR A 1 176 ? 13.360  5.725   -8.179  1.00 79.57  ? 476 TYR A O   1 
ATOM   1290 C CB  . TYR A 1 176 ? 16.490  6.982   -8.232  1.00 84.61  ? 476 TYR A CB  1 
ATOM   1291 C CG  . TYR A 1 176 ? 15.613  8.153   -7.820  1.00 89.81  ? 476 TYR A CG  1 
ATOM   1292 C CD1 . TYR A 1 176 ? 15.512  8.513   -6.485  1.00 90.80  ? 476 TYR A CD1 1 
ATOM   1293 C CD2 . TYR A 1 176 ? 14.839  8.850   -8.743  1.00 94.24  ? 476 TYR A CD2 1 
ATOM   1294 C CE1 . TYR A 1 176 ? 14.680  9.540   -6.077  1.00 93.59  ? 476 TYR A CE1 1 
ATOM   1295 C CE2 . TYR A 1 176 ? 14.009  9.884   -8.347  1.00 98.79  ? 476 TYR A CE2 1 
ATOM   1296 C CZ  . TYR A 1 176 ? 13.933  10.230  -7.010  1.00 95.91  ? 476 TYR A CZ  1 
ATOM   1297 O OH  . TYR A 1 176 ? 13.141  11.243  -6.572  1.00 92.26  ? 476 TYR A OH  1 
ATOM   1298 N N   . LYS A 1 177 ? 14.506  5.359   -10.086 1.00 81.46  ? 477 LYS A N   1 
ATOM   1299 C CA  . LYS A 1 177 ? 13.316  5.360   -10.921 1.00 84.00  ? 477 LYS A CA  1 
ATOM   1300 C C   . LYS A 1 177 ? 12.385  4.230   -10.484 1.00 81.76  ? 477 LYS A C   1 
ATOM   1301 O O   . LYS A 1 177 ? 11.169  4.347   -10.609 1.00 82.93  ? 477 LYS A O   1 
ATOM   1302 C CB  . LYS A 1 177 ? 13.650  5.323   -12.419 1.00 89.73  ? 477 LYS A CB  1 
ATOM   1303 C CG  . LYS A 1 177 ? 14.112  6.662   -13.019 1.00 92.97  ? 477 LYS A CG  1 
ATOM   1304 C CD  . LYS A 1 177 ? 13.974  6.835   -14.534 1.00 100.59 ? 477 LYS A CD  1 
ATOM   1305 C CE  . LYS A 1 177 ? 13.980  8.301   -14.954 1.00 103.95 ? 477 LYS A CE  1 
ATOM   1306 N NZ  . LYS A 1 177 ? 13.793  8.564   -16.389 1.00 110.28 ? 477 LYS A NZ  1 
ATOM   1307 N N   . ALA A 1 178 ? 12.952  3.147   -9.949  1.00 79.51  ? 478 ALA A N   1 
ATOM   1308 C CA  . ALA A 1 178 ? 12.155  1.990   -9.578  1.00 81.26  ? 478 ALA A CA  1 
ATOM   1309 C C   . ALA A 1 178 ? 11.464  2.231   -8.236  1.00 80.34  ? 478 ALA A C   1 
ATOM   1310 O O   . ALA A 1 178 ? 10.295  1.890   -8.061  1.00 84.33  ? 478 ALA A O   1 
ATOM   1311 C CB  . ALA A 1 178 ? 13.025  0.754   -9.562  1.00 81.50  ? 478 ALA A CB  1 
ATOM   1312 N N   . PHE A 1 179 ? 12.181  2.841   -7.289  1.00 76.81  ? 479 PHE A N   1 
ATOM   1313 C CA  . PHE A 1 179 ? 11.604  3.105   -5.985  1.00 74.00  ? 479 PHE A CA  1 
ATOM   1314 C C   . PHE A 1 179 ? 10.481  4.128   -6.091  1.00 78.97  ? 479 PHE A C   1 
ATOM   1315 O O   . PHE A 1 179 ? 9.457   3.982   -5.428  1.00 84.45  ? 479 PHE A O   1 
ATOM   1316 C CB  . PHE A 1 179 ? 12.698  3.537   -5.019  1.00 71.66  ? 479 PHE A CB  1 
ATOM   1317 C CG  . PHE A 1 179 ? 13.459  2.369   -4.427  1.00 73.58  ? 479 PHE A CG  1 
ATOM   1318 C CD1 . PHE A 1 179 ? 14.076  1.431   -5.249  1.00 84.25  ? 479 PHE A CD1 1 
ATOM   1319 C CD2 . PHE A 1 179 ? 13.496  2.177   -3.055  1.00 70.24  ? 479 PHE A CD2 1 
ATOM   1320 C CE1 . PHE A 1 179 ? 14.763  0.355   -4.706  1.00 80.81  ? 479 PHE A CE1 1 
ATOM   1321 C CE2 . PHE A 1 179 ? 14.185  1.103   -2.518  1.00 74.98  ? 479 PHE A CE2 1 
ATOM   1322 C CZ  . PHE A 1 179 ? 14.816  0.193   -3.344  1.00 78.01  ? 479 PHE A CZ  1 
ATOM   1323 N N   . SER A 1 180 ? 10.662  5.156   -6.928  1.00 84.80  ? 480 SER A N   1 
ATOM   1324 C CA  . SER A 1 180 ? 9.593   6.117   -7.158  1.00 88.47  ? 480 SER A CA  1 
ATOM   1325 C C   . SER A 1 180 ? 8.349   5.384   -7.650  1.00 87.30  ? 480 SER A C   1 
ATOM   1326 O O   . SER A 1 180 ? 7.270   5.558   -7.100  1.00 84.43  ? 480 SER A O   1 
ATOM   1327 C CB  . SER A 1 180 ? 10.013  7.189   -8.108  1.00 92.69  ? 480 SER A CB  1 
ATOM   1328 O OG  . SER A 1 180 ? 10.436  6.601   -9.326  1.00 105.05 ? 480 SER A OG  1 
ATOM   1329 N N   . SER A 1 181 ? 8.539   4.525   -8.655  1.00 90.55  ? 481 SER A N   1 
ATOM   1330 C CA  . SER A 1 181 ? 7.444   3.820   -9.298  1.00 98.44  ? 481 SER A CA  1 
ATOM   1331 C C   . SER A 1 181 ? 6.741   2.891   -8.315  1.00 95.80  ? 481 SER A C   1 
ATOM   1332 O O   . SER A 1 181 ? 5.517   2.770   -8.349  1.00 99.76  ? 481 SER A O   1 
ATOM   1333 C CB  . SER A 1 181 ? 7.915   3.064   -10.516 1.00 102.74 ? 481 SER A CB  1 
ATOM   1334 O OG  . SER A 1 181 ? 8.327   3.973   -11.527 1.00 109.22 ? 481 SER A OG  1 
ATOM   1335 N N   . GLU A 1 182 ? 7.519   2.225   -7.458  1.00 87.38  ? 482 GLU A N   1 
ATOM   1336 C CA  . GLU A 1 182 ? 6.937   1.290   -6.513  1.00 87.51  ? 482 GLU A CA  1 
ATOM   1337 C C   . GLU A 1 182 ? 6.134   2.086   -5.485  1.00 87.99  ? 482 GLU A C   1 
ATOM   1338 O O   . GLU A 1 182 ? 5.033   1.687   -5.101  1.00 88.46  ? 482 GLU A O   1 
ATOM   1339 C CB  . GLU A 1 182 ? 8.023   0.362   -5.960  1.00 83.28  ? 482 GLU A CB  1 
ATOM   1340 C CG  . GLU A 1 182 ? 7.532   -0.617  -4.894  1.00 82.22  ? 482 GLU A CG  1 
ATOM   1341 C CD  . GLU A 1 182 ? 6.456   -1.637  -5.258  1.00 87.61  ? 482 GLU A CD  1 
ATOM   1342 O OE1 . GLU A 1 182 ? 6.269   -2.031  -6.441  1.00 92.21  ? 482 GLU A OE1 1 
ATOM   1343 O OE2 . GLU A 1 182 ? 5.767   -2.035  -4.288  1.00 84.41  ? 482 GLU A OE2 1 
ATOM   1344 N N   . MET A 1 183 ? 6.674   3.240   -5.075  1.00 89.26  ? 483 MET A N   1 
ATOM   1345 C CA  . MET A 1 183 ? 5.992   4.085   -4.107  1.00 89.03  ? 483 MET A CA  1 
ATOM   1346 C C   . MET A 1 183 ? 4.693   4.604   -4.728  1.00 90.94  ? 483 MET A C   1 
ATOM   1347 O O   . MET A 1 183 ? 3.621   4.447   -4.140  1.00 89.61  ? 483 MET A O   1 
ATOM   1348 C CB  . MET A 1 183 ? 6.890   5.238   -3.643  1.00 84.80  ? 483 MET A CB  1 
ATOM   1349 C CG  . MET A 1 183 ? 6.258   6.088   -2.551  1.00 83.50  ? 483 MET A CG  1 
ATOM   1350 S SD  . MET A 1 183 ? 7.304   7.480   -2.091  1.00 77.91  ? 483 MET A SD  1 
ATOM   1351 C CE  . MET A 1 183 ? 8.280   6.742   -0.781  1.00 74.67  ? 483 MET A CE  1 
ATOM   1352 N N   . ALA A 1 184 ? 4.801   5.198   -5.927  1.00 90.95  ? 484 ALA A N   1 
ATOM   1353 C CA  . ALA A 1 184 ? 3.636   5.611   -6.695  1.00 95.80  ? 484 ALA A CA  1 
ATOM   1354 C C   . ALA A 1 184 ? 2.570   4.518   -6.649  1.00 102.08 ? 484 ALA A C   1 
ATOM   1355 O O   . ALA A 1 184 ? 1.486   4.732   -6.117  1.00 101.94 ? 484 ALA A O   1 
ATOM   1356 C CB  . ALA A 1 184 ? 4.038   5.949   -8.113  1.00 96.97  ? 484 ALA A CB  1 
ATOM   1357 N N   . LYS A 1 185 ? 2.912   3.334   -7.170  1.00 108.54 ? 485 LYS A N   1 
ATOM   1358 C CA  . LYS A 1 185 ? 2.004   2.199   -7.223  1.00 115.39 ? 485 LYS A CA  1 
ATOM   1359 C C   . LYS A 1 185 ? 1.319   1.984   -5.877  1.00 116.07 ? 485 LYS A C   1 
ATOM   1360 O O   . LYS A 1 185 ? 0.110   1.762   -5.841  1.00 124.17 ? 485 LYS A O   1 
ATOM   1361 C CB  . LYS A 1 185 ? 2.751   0.934   -7.665  1.00 118.00 ? 485 LYS A CB  1 
ATOM   1362 C CG  . LYS A 1 185 ? 2.928   0.872   -9.180  1.00 127.40 ? 485 LYS A CG  1 
ATOM   1363 C CD  . LYS A 1 185 ? 3.821   -0.212  -9.771  1.00 128.87 ? 485 LYS A CD  1 
ATOM   1364 C CE  . LYS A 1 185 ? 3.847   -0.061  -11.267 1.00 133.84 ? 485 LYS A CE  1 
ATOM   1365 N NZ  . LYS A 1 185 ? 5.042   -0.665  -11.861 1.00 132.81 ? 485 LYS A NZ  1 
ATOM   1366 N N   . ARG A 1 186 ? 2.093   2.041   -4.785  1.00 111.24 ? 486 ARG A N   1 
ATOM   1367 C CA  . ARG A 1 186 ? 1.596   1.660   -3.471  1.00 112.52 ? 486 ARG A CA  1 
ATOM   1368 C C   . ARG A 1 186 ? 0.589   2.673   -2.941  1.00 113.24 ? 486 ARG A C   1 
ATOM   1369 O O   . ARG A 1 186 ? -0.451  2.291   -2.401  1.00 116.78 ? 486 ARG A O   1 
ATOM   1370 C CB  . ARG A 1 186 ? 2.732   1.531   -2.452  1.00 107.95 ? 486 ARG A CB  1 
ATOM   1371 C CG  . ARG A 1 186 ? 3.606   0.308   -2.673  1.00 108.48 ? 486 ARG A CG  1 
ATOM   1372 C CD  . ARG A 1 186 ? 2.788   -0.959  -2.841  1.00 112.75 ? 486 ARG A CD  1 
ATOM   1373 N NE  . ARG A 1 186 ? 3.676   -2.093  -2.575  1.00 111.05 ? 486 ARG A NE  1 
ATOM   1374 C CZ  . ARG A 1 186 ? 3.564   -2.919  -1.546  1.00 113.22 ? 486 ARG A CZ  1 
ATOM   1375 N NH1 . ARG A 1 186 ? 2.465   -2.914  -0.803  1.00 117.70 ? 486 ARG A NH1 1 
ATOM   1376 N NH2 . ARG A 1 186 ? 4.548   -3.768  -1.291  1.00 107.80 ? 486 ARG A NH2 1 
ATOM   1377 N N   . SER A 1 187 ? 0.939   3.956   -3.071  1.00 109.90 ? 487 SER A N   1 
ATOM   1378 C CA  . SER A 1 187 ? 0.082   5.029   -2.608  1.00 110.82 ? 487 SER A CA  1 
ATOM   1379 C C   . SER A 1 187 ? -1.243  5.017   -3.371  1.00 121.89 ? 487 SER A C   1 
ATOM   1380 O O   . SER A 1 187 ? -2.275  5.304   -2.775  1.00 127.37 ? 487 SER A O   1 
ATOM   1381 C CB  . SER A 1 187 ? 0.787   6.342   -2.724  1.00 106.88 ? 487 SER A CB  1 
ATOM   1382 O OG  . SER A 1 187 ? 1.513   6.376   -3.942  1.00 108.12 ? 487 SER A OG  1 
ATOM   1383 N N   . LYS A 1 188 ? -1.227  4.658   -4.667  1.00 127.36 ? 488 LYS A N   1 
ATOM   1384 C CA  . LYS A 1 188 ? -2.453  4.559   -5.453  1.00 133.16 ? 488 LYS A CA  1 
ATOM   1385 C C   . LYS A 1 188 ? -3.473  3.662   -4.750  1.00 134.21 ? 488 LYS A C   1 
ATOM   1386 O O   . LYS A 1 188 ? -4.666  3.903   -4.877  1.00 139.95 ? 488 LYS A O   1 
ATOM   1387 C CB  . LYS A 1 188 ? -2.248  4.091   -6.902  1.00 137.70 ? 488 LYS A CB  1 
ATOM   1388 C CG  . LYS A 1 188 ? -1.466  5.046   -7.811  1.00 139.22 ? 488 LYS A CG  1 
ATOM   1389 C CD  . LYS A 1 188 ? -2.060  6.441   -7.993  1.00 144.99 ? 488 LYS A CD  1 
ATOM   1390 C CE  . LYS A 1 188 ? -1.306  7.322   -8.950  1.00 146.81 ? 488 LYS A CE  1 
ATOM   1391 N NZ  . LYS A 1 188 ? -2.014  8.586   -9.195  1.00 150.98 ? 488 LYS A NZ  1 
ATOM   1392 N N   . MET A 1 189 ? -3.014  2.641   -4.009  1.00 133.58 ? 489 MET A N   1 
ATOM   1393 C CA  . MET A 1 189 ? -3.856  1.944   -3.035  1.00 137.08 ? 489 MET A CA  1 
ATOM   1394 C C   . MET A 1 189 ? -3.681  2.621   -1.672  1.00 136.77 ? 489 MET A C   1 
ATOM   1395 O O   . MET A 1 189 ? -2.829  3.490   -1.543  1.00 137.70 ? 489 MET A O   1 
ATOM   1396 C CB  . MET A 1 189 ? -3.448  0.476   -2.894  1.00 135.97 ? 489 MET A CB  1 
ATOM   1397 C CG  . MET A 1 189 ? -3.246  -0.244  -4.212  1.00 138.21 ? 489 MET A CG  1 
ATOM   1398 S SD  . MET A 1 189 ? -2.528  -1.882  -3.980  1.00 135.75 ? 489 MET A SD  1 
ATOM   1399 C CE  . MET A 1 189 ? -1.168  -1.639  -2.826  1.00 123.98 ? 489 MET A CE  1 
ATOM   1400 N N   . LEU A 1 190 ? -4.449  2.212   -0.646  1.00 135.99 ? 490 LEU A N   1 
ATOM   1401 C CA  . LEU A 1 190 ? -4.335  2.757   0.711   1.00 129.10 ? 490 LEU A CA  1 
ATOM   1402 C C   . LEU A 1 190 ? -5.147  4.062   0.861   1.00 131.36 ? 490 LEU A C   1 
ATOM   1403 O O   . LEU A 1 190 ? -5.215  4.553   2.011   1.00 127.79 ? 490 LEU A O   1 
ATOM   1404 C CB  . LEU A 1 190 ? -2.898  3.021   1.167   1.00 120.14 ? 490 LEU A CB  1 
ATOM   1405 C CG  . LEU A 1 190 ? -1.913  1.849   1.109   1.00 118.39 ? 490 LEU A CG  1 
ATOM   1406 C CD1 . LEU A 1 190 ? -0.481  2.360   0.954   1.00 110.77 ? 490 LEU A CD1 1 
ATOM   1407 C CD2 . LEU A 1 190 ? -2.054  0.971   2.350   1.00 116.68 ? 490 LEU A CD2 1 
ATOM   1408 N N   . ASN B 1 10  ? -1.268  12.562  12.799  1.00 78.59  ? 310 ASN B N   1 
ATOM   1409 C CA  . ASN B 1 10  ? -0.528  13.824  13.100  1.00 80.11  ? 310 ASN B CA  1 
ATOM   1410 C C   . ASN B 1 10  ? 0.841   13.814  12.401  1.00 68.15  ? 310 ASN B C   1 
ATOM   1411 O O   . ASN B 1 10  ? 1.895   14.015  13.011  1.00 61.07  ? 310 ASN B O   1 
ATOM   1412 C CB  . ASN B 1 10  ? -0.451  14.097  14.604  1.00 87.49  ? 310 ASN B CB  1 
ATOM   1413 C CG  . ASN B 1 10  ? 0.449   13.106  15.305  1.00 94.69  ? 310 ASN B CG  1 
ATOM   1414 O OD1 . ASN B 1 10  ? 0.780   12.060  14.726  1.00 100.50 ? 310 ASN B OD1 1 
ATOM   1415 N ND2 . ASN B 1 10  ? 0.845   13.404  16.535  1.00 94.37  ? 310 ASN B ND2 1 
ATOM   1416 N N   . ALA B 1 11  ? 0.789   13.608  11.087  1.00 62.89  ? 311 ALA B N   1 
ATOM   1417 C CA  . ALA B 1 11  ? 1.913   13.801  10.191  1.00 59.56  ? 311 ALA B CA  1 
ATOM   1418 C C   . ALA B 1 11  ? 1.359   13.884  8.771   1.00 61.31  ? 311 ALA B C   1 
ATOM   1419 O O   . ALA B 1 11  ? 0.318   13.301  8.485   1.00 65.30  ? 311 ALA B O   1 
ATOM   1420 C CB  . ALA B 1 11  ? 2.921   12.679  10.315  1.00 56.93  ? 311 ALA B CB  1 
ATOM   1421 N N   . MET B 1 12  ? 2.015   14.652  7.899   1.00 60.39  ? 312 MET B N   1 
ATOM   1422 C CA  . MET B 1 12  ? 1.454   14.936  6.592   1.00 65.13  ? 312 MET B CA  1 
ATOM   1423 C C   . MET B 1 12  ? 2.573   15.283  5.627   1.00 63.45  ? 312 MET B C   1 
ATOM   1424 O O   . MET B 1 12  ? 3.648   15.713  6.044   1.00 61.99  ? 312 MET B O   1 
ATOM   1425 C CB  . MET B 1 12  ? 0.450   16.093  6.655   1.00 72.44  ? 312 MET B CB  1 
ATOM   1426 C CG  . MET B 1 12  ? 0.999   17.445  7.114   1.00 73.31  ? 312 MET B CG  1 
ATOM   1427 S SD  . MET B 1 12  ? -0.288  18.718  7.048   1.00 80.22  ? 312 MET B SD  1 
ATOM   1428 C CE  . MET B 1 12  ? 0.673   20.084  7.700   1.00 81.35  ? 312 MET B CE  1 
ATOM   1429 N N   . VAL B 1 13  ? 2.319   15.061  4.338   1.00 65.00  ? 313 VAL B N   1 
ATOM   1430 C CA  . VAL B 1 13  ? 3.296   15.434  3.331   1.00 68.21  ? 313 VAL B CA  1 
ATOM   1431 C C   . VAL B 1 13  ? 2.703   16.599  2.553   1.00 72.11  ? 313 VAL B C   1 
ATOM   1432 O O   . VAL B 1 13  ? 1.529   16.546  2.212   1.00 81.50  ? 313 VAL B O   1 
ATOM   1433 C CB  . VAL B 1 13  ? 3.710   14.291  2.381   1.00 66.12  ? 313 VAL B CB  1 
ATOM   1434 C CG1 . VAL B 1 13  ? 4.664   14.764  1.284   1.00 64.90  ? 313 VAL B CG1 1 
ATOM   1435 C CG2 . VAL B 1 13  ? 4.349   13.150  3.148   1.00 64.00  ? 313 VAL B CG2 1 
ATOM   1436 N N   . VAL B 1 14  ? 3.511   17.628  2.282   1.00 69.23  ? 314 VAL B N   1 
ATOM   1437 C CA  . VAL B 1 14  ? 3.073   18.727  1.447   1.00 73.32  ? 314 VAL B CA  1 
ATOM   1438 C C   . VAL B 1 14  ? 4.158   18.966  0.401   1.00 71.47  ? 314 VAL B C   1 
ATOM   1439 O O   . VAL B 1 14  ? 5.269   19.346  0.727   1.00 64.49  ? 314 VAL B O   1 
ATOM   1440 C CB  . VAL B 1 14  ? 2.780   19.989  2.278   1.00 78.50  ? 314 VAL B CB  1 
ATOM   1441 C CG1 . VAL B 1 14  ? 2.035   21.020  1.432   1.00 86.77  ? 314 VAL B CG1 1 
ATOM   1442 C CG2 . VAL B 1 14  ? 2.010   19.686  3.565   1.00 75.59  ? 314 VAL B CG2 1 
ATOM   1443 N N   . ASN B 1 15  ? 3.836   18.714  -0.864  1.00 78.23  ? 315 ASN B N   1 
ATOM   1444 C CA  . ASN B 1 15  ? 4.846   18.683  -1.911  1.00 85.53  ? 315 ASN B CA  1 
ATOM   1445 C C   . ASN B 1 15  ? 6.022   17.793  -1.504  1.00 80.58  ? 315 ASN B C   1 
ATOM   1446 O O   . ASN B 1 15  ? 5.853   16.587  -1.372  1.00 84.55  ? 315 ASN B O   1 
ATOM   1447 C CB  . ASN B 1 15  ? 5.295   20.093  -2.271  1.00 91.91  ? 315 ASN B CB  1 
ATOM   1448 C CG  . ASN B 1 15  ? 4.150   20.948  -2.754  1.00 95.60  ? 315 ASN B CG  1 
ATOM   1449 O OD1 . ASN B 1 15  ? 3.077   20.449  -3.114  1.00 101.92 ? 315 ASN B OD1 1 
ATOM   1450 N ND2 . ASN B 1 15  ? 4.381   22.244  -2.829  1.00 95.85  ? 315 ASN B ND2 1 
ATOM   1451 N N   . ASN B 1 16  ? 7.205   18.391  -1.309  1.00 77.90  ? 316 ASN B N   1 
ATOM   1452 C CA  . ASN B 1 16  ? 8.423   17.658  -0.984  1.00 78.98  ? 316 ASN B CA  1 
ATOM   1453 C C   . ASN B 1 16  ? 8.794   17.851  0.483   1.00 70.94  ? 316 ASN B C   1 
ATOM   1454 O O   . ASN B 1 16  ? 9.962   17.756  0.870   1.00 66.69  ? 316 ASN B O   1 
ATOM   1455 C CB  . ASN B 1 16  ? 9.602   18.102  -1.848  1.00 87.98  ? 316 ASN B CB  1 
ATOM   1456 C CG  . ASN B 1 16  ? 9.962   17.081  -2.902  1.00 99.18  ? 316 ASN B CG  1 
ATOM   1457 O OD1 . ASN B 1 16  ? 9.078   16.462  -3.514  1.00 105.14 ? 316 ASN B OD1 1 
ATOM   1458 N ND2 . ASN B 1 16  ? 11.256  16.901  -3.130  1.00 103.90 ? 316 ASN B ND2 1 
ATOM   1459 N N   . LEU B 1 17  ? 7.786   18.169  1.289   1.00 68.33  ? 317 LEU B N   1 
ATOM   1460 C CA  . LEU B 1 17  ? 7.998   18.457  2.690   1.00 61.65  ? 317 LEU B CA  1 
ATOM   1461 C C   . LEU B 1 17  ? 7.166   17.460  3.482   1.00 60.66  ? 317 LEU B C   1 
ATOM   1462 O O   . LEU B 1 17  ? 5.971   17.277  3.244   1.00 62.63  ? 317 LEU B O   1 
ATOM   1463 C CB  . LEU B 1 17  ? 7.635   19.905  3.026   1.00 60.96  ? 317 LEU B CB  1 
ATOM   1464 C CG  . LEU B 1 17  ? 7.832   20.330  4.480   1.00 57.63  ? 317 LEU B CG  1 
ATOM   1465 C CD1 . LEU B 1 17  ? 8.583   21.629  4.510   1.00 59.55  ? 317 LEU B CD1 1 
ATOM   1466 C CD2 . LEU B 1 17  ? 6.504   20.475  5.167   1.00 59.09  ? 317 LEU B CD2 1 
ATOM   1467 N N   . THR B 1 18  ? 7.853   16.790  4.398   1.00 57.03  ? 318 THR B N   1 
ATOM   1468 C CA  . THR B 1 18  ? 7.228   15.985  5.418   1.00 56.58  ? 318 THR B CA  1 
ATOM   1469 C C   . THR B 1 18  ? 7.211   16.796  6.708   1.00 54.71  ? 318 THR B C   1 
ATOM   1470 O O   . THR B 1 18  ? 8.245   17.316  7.108   1.00 56.15  ? 318 THR B O   1 
ATOM   1471 C CB  . THR B 1 18  ? 8.082   14.727  5.562   1.00 54.74  ? 318 THR B CB  1 
ATOM   1472 O OG1 . THR B 1 18  ? 7.774   13.951  4.411   1.00 55.02  ? 318 THR B OG1 1 
ATOM   1473 C CG2 . THR B 1 18  ? 7.801   14.012  6.868   1.00 53.34  ? 318 THR B CG2 1 
ATOM   1474 N N   . LEU B 1 19  ? 6.059   16.842  7.376   1.00 55.44  ? 319 LEU B N   1 
ATOM   1475 C CA  . LEU B 1 19  ? 5.920   17.516  8.656   1.00 53.90  ? 319 LEU B CA  1 
ATOM   1476 C C   . LEU B 1 19  ? 5.197   16.619  9.663   1.00 53.50  ? 319 LEU B C   1 
ATOM   1477 O O   . LEU B 1 19  ? 4.121   16.097  9.379   1.00 51.17  ? 319 LEU B O   1 
ATOM   1478 C CB  . LEU B 1 19  ? 5.144   18.804  8.413   1.00 57.97  ? 319 LEU B CB  1 
ATOM   1479 C CG  . LEU B 1 19  ? 4.688   19.555  9.665   1.00 61.55  ? 319 LEU B CG  1 
ATOM   1480 C CD1 . LEU B 1 19  ? 5.894   19.928  10.522  1.00 61.32  ? 319 LEU B CD1 1 
ATOM   1481 C CD2 . LEU B 1 19  ? 3.918   20.804  9.281   1.00 63.30  ? 319 LEU B CD2 1 
ATOM   1482 N N   . GLN B 1 20  ? 5.791   16.488  10.857  1.00 56.52  ? 320 GLN B N   1 
ATOM   1483 C CA  . GLN B 1 20  ? 5.341   15.545  11.874  1.00 62.78  ? 320 GLN B CA  1 
ATOM   1484 C C   . GLN B 1 20  ? 5.292   16.238  13.233  1.00 56.86  ? 320 GLN B C   1 
ATOM   1485 O O   . GLN B 1 20  ? 6.192   16.977  13.589  1.00 53.45  ? 320 GLN B O   1 
ATOM   1486 C CB  . GLN B 1 20  ? 6.284   14.342  12.053  1.00 69.04  ? 320 GLN B CB  1 
ATOM   1487 C CG  . GLN B 1 20  ? 6.973   13.867  10.774  1.00 72.75  ? 320 GLN B CG  1 
ATOM   1488 C CD  . GLN B 1 20  ? 7.674   12.530  10.878  1.00 71.17  ? 320 GLN B CD  1 
ATOM   1489 O OE1 . GLN B 1 20  ? 7.297   11.640  11.654  1.00 82.62  ? 320 GLN B OE1 1 
ATOM   1490 N NE2 . GLN B 1 20  ? 8.674   12.361  10.027  1.00 65.38  ? 320 GLN B NE2 1 
ATOM   1491 N N   . ILE B 1 21  ? 4.263   15.933  14.015  1.00 60.51  ? 321 ILE B N   1 
ATOM   1492 C CA  . ILE B 1 21  ? 4.223   16.345  15.403  1.00 60.00  ? 321 ILE B CA  1 
ATOM   1493 C C   . ILE B 1 21  ? 4.643   15.151  16.238  1.00 61.94  ? 321 ILE B C   1 
ATOM   1494 O O   . ILE B 1 21  ? 4.067   14.073  16.128  1.00 67.84  ? 321 ILE B O   1 
ATOM   1495 C CB  . ILE B 1 21  ? 2.827   16.831  15.814  1.00 61.02  ? 321 ILE B CB  1 
ATOM   1496 C CG1 . ILE B 1 21  ? 2.372   18.016  14.995  1.00 62.65  ? 321 ILE B CG1 1 
ATOM   1497 C CG2 . ILE B 1 21  ? 2.793   17.142  17.307  1.00 63.89  ? 321 ILE B CG2 1 
ATOM   1498 C CD1 . ILE B 1 21  ? 0.866   18.128  14.900  1.00 68.57  ? 321 ILE B CD1 1 
ATOM   1499 N N   . VAL B 1 22  ? 5.612   15.389  17.115  1.00 58.95  ? 322 VAL B N   1 
ATOM   1500 C CA  . VAL B 1 22  ? 6.247   14.338  17.867  1.00 55.60  ? 322 VAL B CA  1 
ATOM   1501 C C   . VAL B 1 22  ? 6.339   14.743  19.329  1.00 59.24  ? 322 VAL B C   1 
ATOM   1502 O O   . VAL B 1 22  ? 6.698   15.884  19.607  1.00 63.74  ? 322 VAL B O   1 
ATOM   1503 C CB  . VAL B 1 22  ? 7.617   14.223  17.195  1.00 52.38  ? 322 VAL B CB  1 
ATOM   1504 C CG1 . VAL B 1 22  ? 8.695   13.758  18.152  1.00 53.03  ? 322 VAL B CG1 1 
ATOM   1505 C CG2 . VAL B 1 22  ? 7.542   13.352  15.954  1.00 55.75  ? 322 VAL B CG2 1 
ATOM   1506 N N   . GLN B 1 23  ? 6.041   13.793  20.238  1.00 61.16  ? 323 GLN B N   1 
ATOM   1507 C CA  . GLN B 1 23  ? 6.262   13.970  21.663  1.00 61.31  ? 323 GLN B CA  1 
ATOM   1508 C C   . GLN B 1 23  ? 7.617   13.395  22.040  1.00 57.46  ? 323 GLN B C   1 
ATOM   1509 O O   . GLN B 1 23  ? 7.766   12.193  22.002  1.00 65.47  ? 323 GLN B O   1 
ATOM   1510 C CB  . GLN B 1 23  ? 5.165   13.266  22.454  1.00 68.11  ? 323 GLN B CB  1 
ATOM   1511 C CG  . GLN B 1 23  ? 3.780   13.855  22.203  1.00 75.10  ? 323 GLN B CG  1 
ATOM   1512 C CD  . GLN B 1 23  ? 2.675   13.162  22.969  1.00 83.80  ? 323 GLN B CD  1 
ATOM   1513 O OE1 . GLN B 1 23  ? 2.202   12.087  22.582  1.00 84.31  ? 323 GLN B OE1 1 
ATOM   1514 N NE2 . GLN B 1 23  ? 2.217   13.806  24.035  1.00 89.67  ? 323 GLN B NE2 1 
ATOM   1515 N N   . GLY B 1 24  ? 8.583   14.241  22.407  1.00 52.41  ? 324 GLY B N   1 
ATOM   1516 C CA  . GLY B 1 24  ? 9.851   13.769  22.932  1.00 52.73  ? 324 GLY B CA  1 
ATOM   1517 C C   . GLY B 1 24  ? 10.688  14.921  23.470  1.00 53.03  ? 324 GLY B C   1 
ATOM   1518 O O   . GLY B 1 24  ? 10.160  15.999  23.691  1.00 54.08  ? 324 GLY B O   1 
ATOM   1519 N N   . HIS B 1 25  ? 11.990  14.679  23.667  1.00 55.34  ? 325 HIS B N   1 
ATOM   1520 C CA  . HIS B 1 25  ? 12.936  15.720  24.038  1.00 54.64  ? 325 HIS B CA  1 
ATOM   1521 C C   . HIS B 1 25  ? 13.706  16.183  22.802  1.00 53.96  ? 325 HIS B C   1 
ATOM   1522 O O   . HIS B 1 25  ? 14.158  15.377  21.979  1.00 54.82  ? 325 HIS B O   1 
ATOM   1523 C CB  . HIS B 1 25  ? 13.946  15.225  25.078  1.00 57.78  ? 325 HIS B CB  1 
ATOM   1524 C CG  . HIS B 1 25  ? 13.379  14.745  26.376  1.00 63.76  ? 325 HIS B CG  1 
ATOM   1525 N ND1 . HIS B 1 25  ? 14.090  14.868  27.556  1.00 65.94  ? 325 HIS B ND1 1 
ATOM   1526 C CD2 . HIS B 1 25  ? 12.216  14.135  26.698  1.00 65.06  ? 325 HIS B CD2 1 
ATOM   1527 C CE1 . HIS B 1 25  ? 13.373  14.350  28.546  1.00 68.55  ? 325 HIS B CE1 1 
ATOM   1528 N NE2 . HIS B 1 25  ? 12.234  13.899  28.049  1.00 67.27  ? 325 HIS B NE2 1 
ATOM   1529 N N   . ILE B 1 26  ? 13.878  17.501  22.705  1.00 51.70  ? 326 ILE B N   1 
ATOM   1530 C CA  . ILE B 1 26  ? 14.542  18.145  21.583  1.00 50.16  ? 326 ILE B CA  1 
ATOM   1531 C C   . ILE B 1 26  ? 16.024  17.813  21.589  1.00 50.68  ? 326 ILE B C   1 
ATOM   1532 O O   . ILE B 1 26  ? 16.614  17.689  20.518  1.00 52.60  ? 326 ILE B O   1 
ATOM   1533 C CB  . ILE B 1 26  ? 14.329  19.677  21.604  1.00 50.87  ? 326 ILE B CB  1 
ATOM   1534 C CG1 . ILE B 1 26  ? 14.882  20.317  20.359  1.00 48.79  ? 326 ILE B CG1 1 
ATOM   1535 C CG2 . ILE B 1 26  ? 14.885  20.352  22.860  1.00 53.27  ? 326 ILE B CG2 1 
ATOM   1536 C CD1 . ILE B 1 26  ? 13.991  20.083  19.157  1.00 49.66  ? 326 ILE B CD1 1 
ATOM   1537 N N   . GLU B 1 27  ? 16.620  17.721  22.786  1.00 51.08  ? 327 GLU B N   1 
ATOM   1538 C CA  . GLU B 1 27  ? 18.050  17.488  22.890  1.00 54.29  ? 327 GLU B CA  1 
ATOM   1539 C C   . GLU B 1 27  ? 18.411  16.027  22.604  1.00 55.67  ? 327 GLU B C   1 
ATOM   1540 O O   . GLU B 1 27  ? 19.589  15.688  22.521  1.00 54.22  ? 327 GLU B O   1 
ATOM   1541 C CB  . GLU B 1 27  ? 18.579  17.964  24.243  1.00 57.71  ? 327 GLU B CB  1 
ATOM   1542 C CG  . GLU B 1 27  ? 18.261  17.089  25.454  1.00 61.16  ? 327 GLU B CG  1 
ATOM   1543 C CD  . GLU B 1 27  ? 16.808  17.040  25.891  1.00 63.33  ? 327 GLU B CD  1 
ATOM   1544 O OE1 . GLU B 1 27  ? 16.055  17.634  25.081  1.00 60.26  ? 327 GLU B OE1 1 
ATOM   1545 O OE2 . GLU B 1 27  ? 16.432  16.440  26.967  1.00 63.33  ? 327 GLU B OE2 1 
ATOM   1546 N N   . TRP B 1 28  ? 17.409  15.148  22.487  1.00 57.28  ? 328 TRP B N   1 
ATOM   1547 C CA  . TRP B 1 28  ? 17.666  13.737  22.215  1.00 60.88  ? 328 TRP B CA  1 
ATOM   1548 C C   . TRP B 1 28  ? 17.311  13.409  20.764  1.00 58.46  ? 328 TRP B C   1 
ATOM   1549 O O   . TRP B 1 28  ? 17.091  12.249  20.434  1.00 53.65  ? 328 TRP B O   1 
ATOM   1550 C CB  . TRP B 1 28  ? 16.881  12.833  23.180  1.00 61.44  ? 328 TRP B CB  1 
ATOM   1551 C CG  . TRP B 1 28  ? 17.310  12.887  24.622  1.00 65.78  ? 328 TRP B CG  1 
ATOM   1552 C CD1 . TRP B 1 28  ? 18.473  13.372  25.158  1.00 70.26  ? 328 TRP B CD1 1 
ATOM   1553 C CD2 . TRP B 1 28  ? 16.564  12.352  25.730  1.00 69.44  ? 328 TRP B CD2 1 
ATOM   1554 N NE1 . TRP B 1 28  ? 18.491  13.199  26.519  1.00 72.84  ? 328 TRP B NE1 1 
ATOM   1555 C CE2 . TRP B 1 28  ? 17.341  12.559  26.893  1.00 75.12  ? 328 TRP B CE2 1 
ATOM   1556 C CE3 . TRP B 1 28  ? 15.327  11.720  25.844  1.00 71.99  ? 328 TRP B CE3 1 
ATOM   1557 C CZ2 . TRP B 1 28  ? 16.914  12.147  28.150  1.00 79.12  ? 328 TRP B CZ2 1 
ATOM   1558 C CZ3 . TRP B 1 28  ? 14.909  11.307  27.087  1.00 77.02  ? 328 TRP B CZ3 1 
ATOM   1559 C CH2 . TRP B 1 28  ? 15.696  11.512  28.219  1.00 80.30  ? 328 TRP B CH2 1 
ATOM   1560 N N   . GLN B 1 29  ? 17.273  14.424  19.891  1.00 55.82  ? 329 GLN B N   1 
ATOM   1561 C CA  . GLN B 1 29  ? 16.797  14.198  18.539  1.00 50.74  ? 329 GLN B CA  1 
ATOM   1562 C C   . GLN B 1 29  ? 17.953  13.997  17.585  1.00 48.97  ? 329 GLN B C   1 
ATOM   1563 O O   . GLN B 1 29  ? 19.095  14.396  17.860  1.00 46.85  ? 329 GLN B O   1 
ATOM   1564 C CB  . GLN B 1 29  ? 16.040  15.316  17.843  1.00 49.01  ? 329 GLN B CB  1 
ATOM   1565 C CG  . GLN B 1 29  ? 14.712  15.633  18.509  1.00 50.94  ? 329 GLN B CG  1 
ATOM   1566 C CD  . GLN B 1 29  ? 13.639  14.608  18.274  1.00 48.08  ? 329 GLN B CD  1 
ATOM   1567 O OE1 . GLN B 1 29  ? 13.203  14.406  17.140  1.00 57.83  ? 329 GLN B OE1 1 
ATOM   1568 N NE2 . GLN B 1 29  ? 13.132  14.042  19.357  1.00 50.86  ? 329 GLN B NE2 1 
ATOM   1569 N N   . THR B 1 30  ? 17.565  13.355  16.472  1.00 44.61  ? 330 THR B N   1 
ATOM   1570 C CA  . THR B 1 30  ? 18.440  13.114  15.357  1.00 45.21  ? 330 THR B CA  1 
ATOM   1571 C C   . THR B 1 30  ? 17.921  13.909  14.169  1.00 42.89  ? 330 THR B C   1 
ATOM   1572 O O   . THR B 1 30  ? 16.847  13.657  13.657  1.00 46.84  ? 330 THR B O   1 
ATOM   1573 C CB  . THR B 1 30  ? 18.460  11.623  15.061  1.00 49.17  ? 330 THR B CB  1 
ATOM   1574 O OG1 . THR B 1 30  ? 19.137  10.926  16.097  1.00 53.43  ? 330 THR B OG1 1 
ATOM   1575 C CG2 . THR B 1 30  ? 19.347  11.350  13.877  1.00 52.72  ? 330 THR B CG2 1 
ATOM   1576 N N   . ALA B 1 31  ? 18.658  14.922  13.751  1.00 41.85  ? 331 ALA B N   1 
ATOM   1577 C CA  . ALA B 1 31  ? 18.279  15.648  12.560  1.00 41.41  ? 331 ALA B CA  1 
ATOM   1578 C C   . ALA B 1 31  ? 19.512  16.395  12.074  1.00 42.98  ? 331 ALA B C   1 
ATOM   1579 O O   . ALA B 1 31  ? 20.473  16.531  12.835  1.00 45.46  ? 331 ALA B O   1 
ATOM   1580 C CB  . ALA B 1 31  ? 17.120  16.539  12.855  1.00 40.48  ? 331 ALA B CB  1 
ATOM   1581 N N   . ASP B 1 32  ? 19.534  16.762  10.795  1.00 41.57  ? 332 ASP B N   1 
ATOM   1582 C CA  . ASP B 1 32  ? 20.592  17.645  10.344  1.00 47.17  ? 332 ASP B CA  1 
ATOM   1583 C C   . ASP B 1 32  ? 20.693  18.844  11.286  1.00 46.53  ? 332 ASP B C   1 
ATOM   1584 O O   . ASP B 1 32  ? 21.801  19.220  11.700  1.00 45.81  ? 332 ASP B O   1 
ATOM   1585 C CB  . ASP B 1 32  ? 20.346  18.113  8.929   1.00 50.45  ? 332 ASP B CB  1 
ATOM   1586 C CG  . ASP B 1 32  ? 20.347  17.007  7.893   1.00 52.52  ? 332 ASP B CG  1 
ATOM   1587 O OD1 . ASP B 1 32  ? 20.960  15.949  8.172   1.00 53.14  ? 332 ASP B OD1 1 
ATOM   1588 O OD2 . ASP B 1 32  ? 19.695  17.217  6.847   1.00 53.62  ? 332 ASP B OD2 1 
ATOM   1589 N N   . VAL B 1 33  ? 19.530  19.413  11.644  1.00 41.69  ? 333 VAL B N   1 
ATOM   1590 C CA  . VAL B 1 33  ? 19.519  20.631  12.431  1.00 42.40  ? 333 VAL B CA  1 
ATOM   1591 C C   . VAL B 1 33  ? 18.532  20.470  13.564  1.00 38.40  ? 333 VAL B C   1 
ATOM   1592 O O   . VAL B 1 33  ? 17.419  20.037  13.317  1.00 36.72  ? 333 VAL B O   1 
ATOM   1593 C CB  . VAL B 1 33  ? 19.139  21.841  11.553  1.00 45.02  ? 333 VAL B CB  1 
ATOM   1594 C CG1 . VAL B 1 33  ? 18.726  23.041  12.399  1.00 45.98  ? 333 VAL B CG1 1 
ATOM   1595 C CG2 . VAL B 1 33  ? 20.224  22.190  10.525  1.00 44.55  ? 333 VAL B CG2 1 
ATOM   1596 N N   . ILE B 1 34  ? 18.947  20.865  14.767  1.00 39.80  ? 334 ILE B N   1 
ATOM   1597 C CA  . ILE B 1 34  ? 18.076  20.956  15.931  1.00 43.79  ? 334 ILE B CA  1 
ATOM   1598 C C   . ILE B 1 34  ? 18.009  22.433  16.325  1.00 44.84  ? 334 ILE B C   1 
ATOM   1599 O O   . ILE B 1 34  ? 19.035  23.103  16.360  1.00 44.37  ? 334 ILE B O   1 
ATOM   1600 C CB  . ILE B 1 34  ? 18.600  20.071  17.084  1.00 45.00  ? 334 ILE B CB  1 
ATOM   1601 C CG1 . ILE B 1 34  ? 18.526  18.616  16.739  1.00 46.99  ? 334 ILE B CG1 1 
ATOM   1602 C CG2 . ILE B 1 34  ? 17.875  20.331  18.400  1.00 44.91  ? 334 ILE B CG2 1 
ATOM   1603 C CD1 . ILE B 1 34  ? 19.317  17.736  17.680  1.00 50.50  ? 334 ILE B CD1 1 
ATOM   1604 N N   . VAL B 1 35  ? 16.803  22.921  16.619  1.00 47.01  ? 335 VAL B N   1 
ATOM   1605 C CA  . VAL B 1 35  ? 16.604  24.327  16.945  1.00 50.30  ? 335 VAL B CA  1 
ATOM   1606 C C   . VAL B 1 35  ? 16.613  24.550  18.460  1.00 49.85  ? 335 VAL B C   1 
ATOM   1607 O O   . VAL B 1 35  ? 15.811  23.970  19.200  1.00 47.21  ? 335 VAL B O   1 
ATOM   1608 C CB  . VAL B 1 35  ? 15.330  24.937  16.341  1.00 50.36  ? 335 VAL B CB  1 
ATOM   1609 C CG1 . VAL B 1 35  ? 15.292  26.443  16.589  1.00 57.23  ? 335 VAL B CG1 1 
ATOM   1610 C CG2 . VAL B 1 35  ? 15.248  24.662  14.855  1.00 50.64  ? 335 VAL B CG2 1 
ATOM   1611 N N   . ASN B 1 36  ? 17.520  25.450  18.880  1.00 50.42  ? 336 ASN B N   1 
ATOM   1612 C CA  . ASN B 1 36  ? 17.633  25.908  20.253  1.00 51.76  ? 336 ASN B CA  1 
ATOM   1613 C C   . ASN B 1 36  ? 16.858  27.216  20.374  1.00 52.54  ? 336 ASN B C   1 
ATOM   1614 O O   . ASN B 1 36  ? 16.563  27.891  19.387  1.00 54.87  ? 336 ASN B O   1 
ATOM   1615 C CB  . ASN B 1 36  ? 19.098  26.056  20.672  1.00 54.43  ? 336 ASN B CB  1 
ATOM   1616 C CG  . ASN B 1 36  ? 19.286  26.112  22.174  1.00 57.35  ? 336 ASN B CG  1 
ATOM   1617 O OD1 . ASN B 1 36  ? 18.329  25.879  22.924  1.00 56.52  ? 336 ASN B OD1 1 
ATOM   1618 N ND2 . ASN B 1 36  ? 20.503  26.388  22.637  1.00 59.75  ? 336 ASN B ND2 1 
ATOM   1619 N N   . SER B 1 37  ? 16.530  27.559  21.614  1.00 54.13  ? 337 SER B N   1 
ATOM   1620 C CA  . SER B 1 37  ? 15.757  28.752  21.917  1.00 54.21  ? 337 SER B CA  1 
ATOM   1621 C C   . SER B 1 37  ? 16.331  29.399  23.168  1.00 53.47  ? 337 SER B C   1 
ATOM   1622 O O   . SER B 1 37  ? 16.219  28.835  24.254  1.00 54.27  ? 337 SER B O   1 
ATOM   1623 C CB  . SER B 1 37  ? 14.326  28.389  22.098  1.00 53.82  ? 337 SER B CB  1 
ATOM   1624 O OG  . SER B 1 37  ? 13.547  29.556  21.983  1.00 54.58  ? 337 SER B OG  1 
ATOM   1625 N N   . VAL B 1 38  ? 16.987  30.554  22.992  1.00 57.81  ? 338 VAL B N   1 
ATOM   1626 C CA  . VAL B 1 38  ? 17.805  31.146  24.042  1.00 60.76  ? 338 VAL B CA  1 
ATOM   1627 C C   . VAL B 1 38  ? 17.458  32.611  24.240  1.00 64.52  ? 338 VAL B C   1 
ATOM   1628 O O   . VAL B 1 38  ? 16.994  33.304  23.336  1.00 69.20  ? 338 VAL B O   1 
ATOM   1629 C CB  . VAL B 1 38  ? 19.317  31.063  23.797  1.00 59.61  ? 338 VAL B CB  1 
ATOM   1630 C CG1 . VAL B 1 38  ? 19.788  29.620  23.652  1.00 59.04  ? 338 VAL B CG1 1 
ATOM   1631 C CG2 . VAL B 1 38  ? 19.714  31.912  22.600  1.00 58.88  ? 338 VAL B CG2 1 
ATOM   1632 N N   . ASN B 1 39  ? 17.751  33.048  25.462  1.00 65.36  ? 339 ASN B N   1 
ATOM   1633 C CA  . ASN B 1 39  ? 18.007  34.439  25.738  1.00 67.02  ? 339 ASN B CA  1 
ATOM   1634 C C   . ASN B 1 39  ? 19.487  34.699  25.458  1.00 67.46  ? 339 ASN B C   1 
ATOM   1635 O O   . ASN B 1 39  ? 20.349  34.062  26.054  1.00 64.49  ? 339 ASN B O   1 
ATOM   1636 C CB  . ASN B 1 39  ? 17.553  34.753  27.153  1.00 70.78  ? 339 ASN B CB  1 
ATOM   1637 C CG  . ASN B 1 39  ? 17.957  36.128  27.615  1.00 73.27  ? 339 ASN B CG  1 
ATOM   1638 O OD1 . ASN B 1 39  ? 18.703  36.853  26.944  1.00 72.69  ? 339 ASN B OD1 1 
ATOM   1639 N ND2 . ASN B 1 39  ? 17.469  36.473  28.791  1.00 77.23  ? 339 ASN B ND2 1 
ATOM   1640 N N   . PRO B 1 40  ? 19.829  35.620  24.523  1.00 70.89  ? 340 PRO B N   1 
ATOM   1641 C CA  . PRO B 1 40  ? 21.209  35.764  24.061  1.00 71.62  ? 340 PRO B CA  1 
ATOM   1642 C C   . PRO B 1 40  ? 22.192  36.156  25.162  1.00 74.33  ? 340 PRO B C   1 
ATOM   1643 O O   . PRO B 1 40  ? 23.379  35.838  25.082  1.00 75.07  ? 340 PRO B O   1 
ATOM   1644 C CB  . PRO B 1 40  ? 21.146  36.820  22.936  1.00 74.85  ? 340 PRO B CB  1 
ATOM   1645 C CG  . PRO B 1 40  ? 19.750  37.434  22.997  1.00 74.00  ? 340 PRO B CG  1 
ATOM   1646 C CD  . PRO B 1 40  ? 18.890  36.535  23.843  1.00 72.51  ? 340 PRO B CD  1 
ATOM   1647 N N   . HIS B 1 41  ? 21.677  36.849  26.183  1.00 76.12  ? 341 HIS B N   1 
ATOM   1648 C CA  . HIS B 1 41  ? 22.469  37.276  27.319  1.00 81.36  ? 341 HIS B CA  1 
ATOM   1649 C C   . HIS B 1 41  ? 22.842  36.070  28.187  1.00 78.60  ? 341 HIS B C   1 
ATOM   1650 O O   . HIS B 1 41  ? 23.876  36.100  28.848  1.00 80.09  ? 341 HIS B O   1 
ATOM   1651 C CB  . HIS B 1 41  ? 21.750  38.420  28.054  1.00 87.40  ? 341 HIS B CB  1 
ATOM   1652 C CG  . HIS B 1 41  ? 21.376  39.579  27.175  1.00 93.85  ? 341 HIS B CG  1 
ATOM   1653 N ND1 . HIS B 1 41  ? 20.396  40.499  27.492  1.00 99.07  ? 341 HIS B ND1 1 
ATOM   1654 C CD2 . HIS B 1 41  ? 21.873  39.967  25.979  1.00 96.82  ? 341 HIS B CD2 1 
ATOM   1655 C CE1 . HIS B 1 41  ? 20.312  41.402  26.524  1.00 102.57 ? 341 HIS B CE1 1 
ATOM   1656 N NE2 . HIS B 1 41  ? 21.193  41.092  25.590  1.00 102.70 ? 341 HIS B NE2 1 
ATOM   1657 N N   . ASP B 1 42  ? 22.023  35.006  28.181  1.00 75.65  ? 342 ASP B N   1 
ATOM   1658 C CA  . ASP B 1 42  ? 22.315  33.814  28.974  1.00 75.70  ? 342 ASP B CA  1 
ATOM   1659 C C   . ASP B 1 42  ? 21.649  32.572  28.367  1.00 71.94  ? 342 ASP B C   1 
ATOM   1660 O O   . ASP B 1 42  ? 20.432  32.361  28.454  1.00 69.49  ? 342 ASP B O   1 
ATOM   1661 C CB  . ASP B 1 42  ? 21.948  34.038  30.436  1.00 79.16  ? 342 ASP B CB  1 
ATOM   1662 C CG  . ASP B 1 42  ? 22.707  33.196  31.451  1.00 80.84  ? 342 ASP B CG  1 
ATOM   1663 O OD1 . ASP B 1 42  ? 23.197  32.137  31.047  1.00 79.80  ? 342 ASP B OD1 1 
ATOM   1664 O OD2 . ASP B 1 42  ? 22.830  33.622  32.628  1.00 85.52  ? 342 ASP B OD2 1 
ATOM   1665 N N   . ILE B 1 43  ? 22.478  31.710  27.772  1.00 71.28  ? 343 ILE B N   1 
ATOM   1666 C CA  . ILE B 1 43  ? 21.988  30.504  27.123  1.00 67.58  ? 343 ILE B CA  1 
ATOM   1667 C C   . ILE B 1 43  ? 21.923  29.346  28.114  1.00 66.09  ? 343 ILE B C   1 
ATOM   1668 O O   . ILE B 1 43  ? 21.692  28.211  27.708  1.00 68.20  ? 343 ILE B O   1 
ATOM   1669 C CB  . ILE B 1 43  ? 22.905  30.128  25.953  1.00 66.49  ? 343 ILE B CB  1 
ATOM   1670 C CG1 . ILE B 1 43  ? 24.306  29.778  26.440  1.00 70.22  ? 343 ILE B CG1 1 
ATOM   1671 C CG2 . ILE B 1 43  ? 22.939  31.247  24.925  1.00 66.46  ? 343 ILE B CG2 1 
ATOM   1672 C CD1 . ILE B 1 43  ? 24.990  28.724  25.597  1.00 69.90  ? 343 ILE B CD1 1 
ATOM   1673 N N   . THR B 1 44  ? 22.192  29.618  29.392  1.00 66.44  ? 344 THR B N   1 
ATOM   1674 C CA  . THR B 1 44  ? 22.206  28.580  30.404  1.00 66.97  ? 344 THR B CA  1 
ATOM   1675 C C   . THR B 1 44  ? 20.862  28.536  31.119  1.00 69.05  ? 344 THR B C   1 
ATOM   1676 O O   . THR B 1 44  ? 20.697  27.790  32.082  1.00 70.11  ? 344 THR B O   1 
ATOM   1677 C CB  . THR B 1 44  ? 23.325  28.837  31.402  1.00 69.78  ? 344 THR B CB  1 
ATOM   1678 O OG1 . THR B 1 44  ? 22.735  29.843  32.218  1.00 76.16  ? 344 THR B OG1 1 
ATOM   1679 C CG2 . THR B 1 44  ? 24.628  29.225  30.727  1.00 70.02  ? 344 THR B CG2 1 
ATOM   1680 N N   . VAL B 1 45  ? 19.923  29.358  30.654  1.00 69.29  ? 345 VAL B N   1 
ATOM   1681 C CA  . VAL B 1 45  ? 18.656  29.522  31.334  1.00 70.78  ? 345 VAL B CA  1 
ATOM   1682 C C   . VAL B 1 45  ? 17.555  29.176  30.345  1.00 66.50  ? 345 VAL B C   1 
ATOM   1683 O O   . VAL B 1 45  ? 17.694  29.422  29.143  1.00 61.84  ? 345 VAL B O   1 
ATOM   1684 C CB  . VAL B 1 45  ? 18.531  30.969  31.848  1.00 77.11  ? 345 VAL B CB  1 
ATOM   1685 C CG1 . VAL B 1 45  ? 17.292  31.158  32.706  1.00 80.77  ? 345 VAL B CG1 1 
ATOM   1686 C CG2 . VAL B 1 45  ? 19.760  31.400  32.636  1.00 81.39  ? 345 VAL B CG2 1 
ATOM   1687 N N   . GLY B 1 46  ? 16.464  28.624  30.884  1.00 68.82  ? 346 GLY B N   1 
ATOM   1688 C CA  . GLY B 1 46  ? 15.305  28.246  30.090  1.00 69.81  ? 346 GLY B CA  1 
ATOM   1689 C C   . GLY B 1 46  ? 15.257  26.739  29.864  1.00 68.20  ? 346 GLY B C   1 
ATOM   1690 O O   . GLY B 1 46  ? 16.295  26.121  29.674  1.00 69.23  ? 346 GLY B O   1 
ATOM   1691 N N   . PRO B 1 47  ? 14.067  26.099  29.896  1.00 70.20  ? 347 PRO B N   1 
ATOM   1692 C CA  . PRO B 1 47  ? 13.944  24.659  29.640  1.00 73.30  ? 347 PRO B CA  1 
ATOM   1693 C C   . PRO B 1 47  ? 14.799  24.084  28.502  1.00 71.69  ? 347 PRO B C   1 
ATOM   1694 O O   . PRO B 1 47  ? 15.701  23.281  28.741  1.00 77.71  ? 347 PRO B O   1 
ATOM   1695 C CB  . PRO B 1 47  ? 12.427  24.523  29.381  1.00 72.16  ? 347 PRO B CB  1 
ATOM   1696 C CG  . PRO B 1 47  ? 11.803  25.574  30.264  1.00 75.63  ? 347 PRO B CG  1 
ATOM   1697 C CD  . PRO B 1 47  ? 12.792  26.718  30.276  1.00 74.98  ? 347 PRO B CD  1 
ATOM   1698 N N   . VAL B 1 48  ? 14.540  24.532  27.268  1.00 68.75  ? 348 VAL B N   1 
ATOM   1699 C CA  . VAL B 1 48  ? 15.211  24.047  26.069  1.00 63.00  ? 348 VAL B CA  1 
ATOM   1700 C C   . VAL B 1 48  ? 16.706  24.379  26.118  1.00 61.73  ? 348 VAL B C   1 
ATOM   1701 O O   . VAL B 1 48  ? 17.558  23.526  25.893  1.00 61.38  ? 348 VAL B O   1 
ATOM   1702 C CB  . VAL B 1 48  ? 14.498  24.674  24.852  1.00 60.36  ? 348 VAL B CB  1 
ATOM   1703 C CG1 . VAL B 1 48  ? 15.239  24.465  23.542  1.00 62.54  ? 348 VAL B CG1 1 
ATOM   1704 C CG2 . VAL B 1 48  ? 13.073  24.160  24.723  1.00 59.93  ? 348 VAL B CG2 1 
ATOM   1705 N N   . ALA B 1 49  ? 17.044  25.619  26.452  1.00 61.41  ? 349 ALA B N   1 
ATOM   1706 C CA  . ALA B 1 49  ? 18.438  26.029  26.446  1.00 63.57  ? 349 ALA B CA  1 
ATOM   1707 C C   . ALA B 1 49  ? 19.282  25.125  27.343  1.00 64.16  ? 349 ALA B C   1 
ATOM   1708 O O   . ALA B 1 49  ? 20.432  24.842  27.018  1.00 61.88  ? 349 ALA B O   1 
ATOM   1709 C CB  . ALA B 1 49  ? 18.547  27.470  26.871  1.00 62.80  ? 349 ALA B CB  1 
ATOM   1710 N N   . LYS B 1 50  ? 18.707  24.709  28.478  1.00 66.96  ? 350 LYS B N   1 
ATOM   1711 C CA  . LYS B 1 50  ? 19.412  23.905  29.465  1.00 71.12  ? 350 LYS B CA  1 
ATOM   1712 C C   . LYS B 1 50  ? 19.571  22.475  28.954  1.00 73.00  ? 350 LYS B C   1 
ATOM   1713 O O   . LYS B 1 50  ? 20.695  21.975  28.864  1.00 72.37  ? 350 LYS B O   1 
ATOM   1714 C CB  . LYS B 1 50  ? 18.669  23.890  30.802  1.00 74.09  ? 350 LYS B CB  1 
ATOM   1715 C CG  . LYS B 1 50  ? 18.652  25.222  31.527  1.00 80.21  ? 350 LYS B CG  1 
ATOM   1716 C CD  . LYS B 1 50  ? 17.569  25.361  32.593  1.00 84.04  ? 350 LYS B CD  1 
ATOM   1717 C CE  . LYS B 1 50  ? 18.016  25.009  33.972  1.00 89.80  ? 350 LYS B CE  1 
ATOM   1718 N NZ  . LYS B 1 50  ? 16.956  25.327  34.932  1.00 95.30  ? 350 LYS B NZ  1 
ATOM   1719 N N   . SER B 1 51  ? 18.436  21.833  28.626  1.00 70.26  ? 351 SER B N   1 
ATOM   1720 C CA  . SER B 1 51  ? 18.415  20.507  28.016  1.00 68.45  ? 351 SER B CA  1 
ATOM   1721 C C   . SER B 1 51  ? 19.506  20.372  26.957  1.00 64.17  ? 351 SER B C   1 
ATOM   1722 O O   . SER B 1 51  ? 20.274  19.409  26.974  1.00 68.93  ? 351 SER B O   1 
ATOM   1723 C CB  . SER B 1 51  ? 17.064  20.205  27.421  1.00 66.19  ? 351 SER B CB  1 
ATOM   1724 O OG  . SER B 1 51  ? 16.058  20.374  28.410  1.00 69.86  ? 351 SER B OG  1 
ATOM   1725 N N   . ILE B 1 52  ? 19.573  21.367  26.066  1.00 59.34  ? 352 ILE B N   1 
ATOM   1726 C CA  . ILE B 1 52  ? 20.485  21.353  24.939  1.00 56.02  ? 352 ILE B CA  1 
ATOM   1727 C C   . ILE B 1 52  ? 21.917  21.541  25.419  1.00 59.09  ? 352 ILE B C   1 
ATOM   1728 O O   . ILE B 1 52  ? 22.800  20.829  24.952  1.00 59.85  ? 352 ILE B O   1 
ATOM   1729 C CB  . ILE B 1 52  ? 20.045  22.388  23.898  1.00 52.58  ? 352 ILE B CB  1 
ATOM   1730 C CG1 . ILE B 1 52  ? 18.874  21.818  23.117  1.00 54.10  ? 352 ILE B CG1 1 
ATOM   1731 C CG2 . ILE B 1 52  ? 21.192  22.827  22.992  1.00 50.40  ? 352 ILE B CG2 1 
ATOM   1732 C CD1 . ILE B 1 52  ? 18.586  22.513  21.802  1.00 55.70  ? 352 ILE B CD1 1 
ATOM   1733 N N   . LEU B 1 53  ? 22.116  22.445  26.384  1.00 61.05  ? 353 LEU B N   1 
ATOM   1734 C CA  . LEU B 1 53  ? 23.443  22.747  26.894  1.00 63.98  ? 353 LEU B CA  1 
ATOM   1735 C C   . LEU B 1 53  ? 24.024  21.514  27.579  1.00 68.21  ? 353 LEU B C   1 
ATOM   1736 O O   . LEU B 1 53  ? 25.207  21.222  27.409  1.00 70.90  ? 353 LEU B O   1 
ATOM   1737 C CB  . LEU B 1 53  ? 23.447  23.941  27.853  1.00 64.11  ? 353 LEU B CB  1 
ATOM   1738 C CG  . LEU B 1 53  ? 24.815  24.337  28.433  1.00 66.34  ? 353 LEU B CG  1 
ATOM   1739 C CD1 . LEU B 1 53  ? 25.877  24.644  27.379  1.00 66.66  ? 353 LEU B CD1 1 
ATOM   1740 C CD2 . LEU B 1 53  ? 24.695  25.515  29.354  1.00 66.83  ? 353 LEU B CD2 1 
ATOM   1741 N N   . GLN B 1 54  ? 23.197  20.830  28.379  1.00 70.42  ? 354 GLN B N   1 
ATOM   1742 C CA  . GLN B 1 54  ? 23.638  19.636  29.073  1.00 76.88  ? 354 GLN B CA  1 
ATOM   1743 C C   . GLN B 1 54  ? 23.992  18.565  28.054  1.00 74.98  ? 354 GLN B C   1 
ATOM   1744 O O   . GLN B 1 54  ? 25.086  18.023  28.096  1.00 76.11  ? 354 GLN B O   1 
ATOM   1745 C CB  . GLN B 1 54  ? 22.631  19.006  30.033  1.00 82.28  ? 354 GLN B CB  1 
ATOM   1746 C CG  . GLN B 1 54  ? 23.297  18.062  31.034  1.00 92.47  ? 354 GLN B CG  1 
ATOM   1747 C CD  . GLN B 1 54  ? 24.512  18.643  31.751  1.00 99.81  ? 354 GLN B CD  1 
ATOM   1748 O OE1 . GLN B 1 54  ? 24.401  19.343  32.767  1.00 101.79 ? 354 GLN B OE1 1 
ATOM   1749 N NE2 . GLN B 1 54  ? 25.708  18.313  31.276  1.00 102.28 ? 354 GLN B NE2 1 
ATOM   1750 N N   . GLN B 1 55  ? 23.068  18.287  27.138  1.00 71.59  ? 355 GLN B N   1 
ATOM   1751 C CA  . GLN B 1 55  ? 23.272  17.198  26.205  1.00 73.11  ? 355 GLN B CA  1 
ATOM   1752 C C   . GLN B 1 55  ? 24.442  17.481  25.265  1.00 70.61  ? 355 GLN B C   1 
ATOM   1753 O O   . GLN B 1 55  ? 25.131  16.557  24.872  1.00 69.58  ? 355 GLN B O   1 
ATOM   1754 C CB  . GLN B 1 55  ? 22.010  16.912  25.391  1.00 74.31  ? 355 GLN B CB  1 
ATOM   1755 C CG  . GLN B 1 55  ? 22.059  15.584  24.633  1.00 70.63  ? 355 GLN B CG  1 
ATOM   1756 C CD  . GLN B 1 55  ? 22.333  14.418  25.561  1.00 71.77  ? 355 GLN B CD  1 
ATOM   1757 O OE1 . GLN B 1 55  ? 21.668  14.259  26.586  1.00 71.02  ? 355 GLN B OE1 1 
ATOM   1758 N NE2 . GLN B 1 55  ? 23.332  13.611  25.241  1.00 73.97  ? 355 GLN B NE2 1 
ATOM   1759 N N   . ALA B 1 56  ? 24.640  18.739  24.864  1.00 69.73  ? 356 ALA B N   1 
ATOM   1760 C CA  . ALA B 1 56  ? 25.577  19.045  23.789  1.00 68.17  ? 356 ALA B CA  1 
ATOM   1761 C C   . ALA B 1 56  ? 26.988  19.213  24.337  1.00 71.57  ? 356 ALA B C   1 
ATOM   1762 O O   . ALA B 1 56  ? 27.961  19.088  23.590  1.00 70.17  ? 356 ALA B O   1 
ATOM   1763 C CB  . ALA B 1 56  ? 25.142  20.292  23.062  1.00 67.84  ? 356 ALA B CB  1 
ATOM   1764 N N   . GLY B 1 57  ? 27.069  19.544  25.633  1.00 76.37  ? 357 GLY B N   1 
ATOM   1765 C CA  . GLY B 1 57  ? 28.330  19.598  26.356  1.00 83.59  ? 357 GLY B CA  1 
ATOM   1766 C C   . GLY B 1 57  ? 28.870  21.021  26.441  1.00 85.19  ? 357 GLY B C   1 
ATOM   1767 O O   . GLY B 1 57  ? 28.408  21.911  25.735  1.00 83.35  ? 357 GLY B O   1 
ATOM   1768 N N   . VAL B 1 58  ? 29.895  21.190  27.277  1.00 90.23  ? 358 VAL B N   1 
ATOM   1769 C CA  . VAL B 1 58  ? 30.406  22.501  27.637  1.00 92.91  ? 358 VAL B CA  1 
ATOM   1770 C C   . VAL B 1 58  ? 30.992  23.223  26.419  1.00 93.38  ? 358 VAL B C   1 
ATOM   1771 O O   . VAL B 1 58  ? 30.976  24.455  26.387  1.00 93.97  ? 358 VAL B O   1 
ATOM   1772 C CB  . VAL B 1 58  ? 31.434  22.341  28.775  1.00 99.24  ? 358 VAL B CB  1 
ATOM   1773 C CG1 . VAL B 1 58  ? 32.095  23.662  29.155  1.00 103.52 ? 358 VAL B CG1 1 
ATOM   1774 C CG2 . VAL B 1 58  ? 30.810  21.691  30.009  1.00 99.83  ? 358 VAL B CG2 1 
ATOM   1775 N N   . GLU B 1 59  ? 31.490  22.476  25.417  1.00 91.79  ? 359 GLU B N   1 
ATOM   1776 C CA  . GLU B 1 59  ? 32.181  23.074  24.280  1.00 94.39  ? 359 GLU B CA  1 
ATOM   1777 C C   . GLU B 1 59  ? 31.204  23.800  23.350  1.00 88.25  ? 359 GLU B C   1 
ATOM   1778 O O   . GLU B 1 59  ? 31.630  24.558  22.481  1.00 86.89  ? 359 GLU B O   1 
ATOM   1779 C CB  . GLU B 1 59  ? 32.949  22.063  23.424  1.00 100.20 ? 359 GLU B CB  1 
ATOM   1780 C CG  . GLU B 1 59  ? 33.987  21.235  24.174  1.00 108.81 ? 359 GLU B CG  1 
ATOM   1781 C CD  . GLU B 1 59  ? 33.524  19.841  24.557  1.00 110.77 ? 359 GLU B CD  1 
ATOM   1782 O OE1 . GLU B 1 59  ? 32.518  19.718  25.296  1.00 112.15 ? 359 GLU B OE1 1 
ATOM   1783 O OE2 . GLU B 1 59  ? 34.173  18.878  24.095  1.00 112.05 ? 359 GLU B OE2 1 
ATOM   1784 N N   . MET B 1 60  ? 29.902  23.534  23.508  1.00 83.85  ? 360 MET B N   1 
ATOM   1785 C CA  . MET B 1 60  ? 28.863  24.152  22.695  1.00 86.26  ? 360 MET B CA  1 
ATOM   1786 C C   . MET B 1 60  ? 28.675  25.618  23.099  1.00 89.48  ? 360 MET B C   1 
ATOM   1787 O O   . MET B 1 60  ? 28.378  26.468  22.262  1.00 88.51  ? 360 MET B O   1 
ATOM   1788 C CB  . MET B 1 60  ? 27.549  23.380  22.880  1.00 86.57  ? 360 MET B CB  1 
ATOM   1789 C CG  . MET B 1 60  ? 26.444  23.734  21.910  1.00 83.50  ? 360 MET B CG  1 
ATOM   1790 S SD  . MET B 1 60  ? 25.318  25.013  22.498  1.00 94.71  ? 360 MET B SD  1 
ATOM   1791 C CE  . MET B 1 60  ? 24.491  24.415  23.978  1.00 93.88  ? 360 MET B CE  1 
ATOM   1792 N N   . LYS B 1 61  ? 28.849  25.892  24.397  1.00 89.87  ? 361 LYS B N   1 
ATOM   1793 C CA  . LYS B 1 61  ? 28.731  27.225  24.960  1.00 89.27  ? 361 LYS B CA  1 
ATOM   1794 C C   . LYS B 1 61  ? 29.935  28.095  24.600  1.00 91.22  ? 361 LYS B C   1 
ATOM   1795 O O   . LYS B 1 61  ? 29.826  29.320  24.648  1.00 91.42  ? 361 LYS B O   1 
ATOM   1796 C CB  . LYS B 1 61  ? 28.577  27.079  26.479  1.00 93.98  ? 361 LYS B CB  1 
ATOM   1797 C CG  . LYS B 1 61  ? 28.485  28.348  27.321  1.00 92.88  ? 361 LYS B CG  1 
ATOM   1798 C CD  . LYS B 1 61  ? 28.457  28.061  28.817  1.00 91.77  ? 361 LYS B CD  1 
ATOM   1799 C CE  . LYS B 1 61  ? 28.832  29.280  29.576  1.00 96.03  ? 361 LYS B CE  1 
ATOM   1800 N NZ  . LYS B 1 61  ? 28.557  29.036  30.988  1.00 99.90  ? 361 LYS B NZ  1 
ATOM   1801 N N   . SER B 1 62  ? 31.075  27.476  24.255  1.00 89.72  ? 362 SER B N   1 
ATOM   1802 C CA  . SER B 1 62  ? 32.245  28.227  23.827  1.00 93.77  ? 362 SER B CA  1 
ATOM   1803 C C   . SER B 1 62  ? 32.046  28.772  22.417  1.00 96.54  ? 362 SER B C   1 
ATOM   1804 O O   . SER B 1 62  ? 32.215  29.961  22.189  1.00 102.01 ? 362 SER B O   1 
ATOM   1805 C CB  . SER B 1 62  ? 33.502  27.412  23.906  1.00 94.37  ? 362 SER B CB  1 
ATOM   1806 O OG  . SER B 1 62  ? 33.855  27.201  25.261  1.00 92.69  ? 362 SER B OG  1 
ATOM   1807 N N   . GLU B 1 63  ? 31.705  27.904  21.464  1.00 98.65  ? 363 GLU B N   1 
ATOM   1808 C CA  . GLU B 1 63  ? 31.551  28.341  20.089  1.00 102.49 ? 363 GLU B CA  1 
ATOM   1809 C C   . GLU B 1 63  ? 30.405  29.350  20.005  1.00 94.17  ? 363 GLU B C   1 
ATOM   1810 O O   . GLU B 1 63  ? 30.419  30.206  19.128  1.00 98.01  ? 363 GLU B O   1 
ATOM   1811 C CB  . GLU B 1 63  ? 31.338  27.177  19.120  1.00 108.64 ? 363 GLU B CB  1 
ATOM   1812 C CG  . GLU B 1 63  ? 31.648  27.556  17.672  1.00 118.05 ? 363 GLU B CG  1 
ATOM   1813 C CD  . GLU B 1 63  ? 31.056  26.642  16.607  1.00 126.91 ? 363 GLU B CD  1 
ATOM   1814 O OE1 . GLU B 1 63  ? 30.298  25.700  16.947  1.00 116.81 ? 363 GLU B OE1 1 
ATOM   1815 O OE2 . GLU B 1 63  ? 31.353  26.890  15.415  1.00 137.39 ? 363 GLU B OE2 1 
ATOM   1816 N N   . PHE B 1 64  ? 29.438  29.257  20.930  1.00 88.08  ? 364 PHE B N   1 
ATOM   1817 C CA  . PHE B 1 64  ? 28.297  30.164  20.966  1.00 84.24  ? 364 PHE B CA  1 
ATOM   1818 C C   . PHE B 1 64  ? 28.669  31.563  21.472  1.00 85.24  ? 364 PHE B C   1 
ATOM   1819 O O   . PHE B 1 64  ? 28.165  32.557  20.944  1.00 82.90  ? 364 PHE B O   1 
ATOM   1820 C CB  . PHE B 1 64  ? 27.183  29.656  21.879  1.00 78.98  ? 364 PHE B CB  1 
ATOM   1821 C CG  . PHE B 1 64  ? 25.986  30.594  21.893  1.00 77.58  ? 364 PHE B CG  1 
ATOM   1822 C CD1 . PHE B 1 64  ? 25.985  31.734  22.691  1.00 78.04  ? 364 PHE B CD1 1 
ATOM   1823 C CD2 . PHE B 1 64  ? 24.858  30.328  21.121  1.00 72.70  ? 364 PHE B CD2 1 
ATOM   1824 C CE1 . PHE B 1 64  ? 24.885  32.582  22.710  1.00 78.72  ? 364 PHE B CE1 1 
ATOM   1825 C CE2 . PHE B 1 64  ? 23.756  31.169  21.159  1.00 72.94  ? 364 PHE B CE2 1 
ATOM   1826 C CZ  . PHE B 1 64  ? 23.774  32.303  21.942  1.00 74.72  ? 364 PHE B CZ  1 
ATOM   1827 N N   . LEU B 1 65  ? 29.498  31.641  22.527  1.00 86.39  ? 365 LEU B N   1 
ATOM   1828 C CA  . LEU B 1 65  ? 29.945  32.917  23.074  1.00 86.55  ? 365 LEU B CA  1 
ATOM   1829 C C   . LEU B 1 65  ? 30.979  33.549  22.145  1.00 89.80  ? 365 LEU B C   1 
ATOM   1830 O O   . LEU B 1 65  ? 31.169  34.753  22.201  1.00 97.70  ? 365 LEU B O   1 
ATOM   1831 C CB  . LEU B 1 65  ? 30.502  32.793  24.494  1.00 87.42  ? 365 LEU B CB  1 
ATOM   1832 C CG  . LEU B 1 65  ? 29.494  32.447  25.600  1.00 86.81  ? 365 LEU B CG  1 
ATOM   1833 C CD1 . LEU B 1 65  ? 30.170  32.011  26.895  1.00 89.31  ? 365 LEU B CD1 1 
ATOM   1834 C CD2 . LEU B 1 65  ? 28.560  33.610  25.903  1.00 86.41  ? 365 LEU B CD2 1 
ATOM   1835 N N   . ALA B 1 66  ? 31.634  32.756  21.287  1.00 91.77  ? 366 ALA B N   1 
ATOM   1836 C CA  . ALA B 1 66  ? 32.733  33.250  20.470  1.00 95.73  ? 366 ALA B CA  1 
ATOM   1837 C C   . ALA B 1 66  ? 32.254  33.734  19.104  1.00 95.58  ? 366 ALA B C   1 
ATOM   1838 O O   . ALA B 1 66  ? 33.029  34.377  18.398  1.00 99.76  ? 366 ALA B O   1 
ATOM   1839 C CB  . ALA B 1 66  ? 33.789  32.182  20.319  1.00 96.80  ? 366 ALA B CB  1 
ATOM   1840 N N   . THR B 1 67  ? 30.989  33.459  18.752  1.00 94.68  ? 367 THR B N   1 
ATOM   1841 C CA  . THR B 1 67  ? 30.494  33.756  17.413  1.00 99.54  ? 367 THR B CA  1 
ATOM   1842 C C   . THR B 1 67  ? 29.300  34.717  17.451  1.00 107.95 ? 367 THR B C   1 
ATOM   1843 O O   . THR B 1 67  ? 28.752  35.066  16.400  1.00 110.28 ? 367 THR B O   1 
ATOM   1844 C CB  . THR B 1 67  ? 30.138  32.447  16.700  1.00 92.20  ? 367 THR B CB  1 
ATOM   1845 O OG1 . THR B 1 67  ? 29.116  31.871  17.507  1.00 86.17  ? 367 THR B OG1 1 
ATOM   1846 C CG2 . THR B 1 67  ? 31.339  31.532  16.513  1.00 91.35  ? 367 THR B CG2 1 
ATOM   1847 N N   . LYS B 1 68  ? 28.912  35.170  18.650  1.00 113.44 ? 368 LYS B N   1 
ATOM   1848 C CA  . LYS B 1 68  ? 27.754  36.033  18.816  1.00 114.67 ? 368 LYS B CA  1 
ATOM   1849 C C   . LYS B 1 68  ? 28.036  37.435  18.256  1.00 113.90 ? 368 LYS B C   1 
ATOM   1850 O O   . LYS B 1 68  ? 29.182  37.872  18.207  1.00 108.83 ? 368 LYS B O   1 
ATOM   1851 C CB  . LYS B 1 68  ? 27.422  36.054  20.314  1.00 115.09 ? 368 LYS B CB  1 
ATOM   1852 C CG  . LYS B 1 68  ? 26.069  36.653  20.698  1.00 117.16 ? 368 LYS B CG  1 
ATOM   1853 C CD  . LYS B 1 68  ? 25.984  37.089  22.156  1.00 121.81 ? 368 LYS B CD  1 
ATOM   1854 C CE  . LYS B 1 68  ? 25.957  35.924  23.086  1.00 123.56 ? 368 LYS B CE  1 
ATOM   1855 N NZ  . LYS B 1 68  ? 26.084  36.315  24.491  1.00 128.99 ? 368 LYS B NZ  1 
ATOM   1856 N N   . ALA B 1 69  ? 26.959  38.130  17.853  1.00 111.33 ? 369 ALA B N   1 
ATOM   1857 C CA  . ALA B 1 69  ? 26.992  39.530  17.434  1.00 109.20 ? 369 ALA B CA  1 
ATOM   1858 C C   . ALA B 1 69  ? 27.847  39.680  16.175  1.00 109.40 ? 369 ALA B C   1 
ATOM   1859 O O   . ALA B 1 69  ? 28.746  40.543  16.213  1.00 114.95 ? 369 ALA B O   1 
ATOM   1860 C CB  . ALA B 1 69  ? 27.462  40.443  18.560  1.00 109.53 ? 369 ALA B CB  1 
ATOM   1861 N N   . ARG B 1 74  ? 22.738  43.173  16.990  1.00 108.51 ? 374 ARG B N   1 
ATOM   1862 C CA  . ARG B 1 74  ? 21.271  43.017  17.194  1.00 110.25 ? 374 ARG B CA  1 
ATOM   1863 C C   . ARG B 1 74  ? 20.617  42.375  15.969  1.00 109.43 ? 374 ARG B C   1 
ATOM   1864 O O   . ARG B 1 74  ? 19.679  41.598  16.133  1.00 110.44 ? 374 ARG B O   1 
ATOM   1865 C CB  . ARG B 1 74  ? 20.570  44.349  17.484  1.00 119.86 ? 374 ARG B CB  1 
ATOM   1866 C CG  . ARG B 1 74  ? 20.944  44.992  18.818  1.00 123.87 ? 374 ARG B CG  1 
ATOM   1867 C CD  . ARG B 1 74  ? 20.213  46.304  19.144  1.00 128.56 ? 374 ARG B CD  1 
ATOM   1868 N NE  . ARG B 1 74  ? 20.666  46.910  20.404  1.00 135.02 ? 374 ARG B NE  1 
ATOM   1869 C CZ  . ARG B 1 74  ? 20.292  48.098  20.876  1.00 140.82 ? 374 ARG B CZ  1 
ATOM   1870 N NH1 . ARG B 1 74  ? 19.246  48.725  20.363  1.00 142.58 ? 374 ARG B NH1 1 
ATOM   1871 N NH2 . ARG B 1 74  ? 20.953  48.645  21.882  1.00 147.20 ? 374 ARG B NH2 1 
ATOM   1872 N N   . SER B 1 75  ? 21.101  42.680  14.751  1.00 108.22 ? 375 SER B N   1 
ATOM   1873 C CA  . SER B 1 75  ? 20.484  42.201  13.519  1.00 104.91 ? 375 SER B CA  1 
ATOM   1874 C C   . SER B 1 75  ? 20.935  40.768  13.194  1.00 105.47 ? 375 SER B C   1 
ATOM   1875 O O   . SER B 1 75  ? 21.535  40.497  12.150  1.00 110.28 ? 375 SER B O   1 
ATOM   1876 C CB  . SER B 1 75  ? 20.746  43.163  12.382  1.00 108.23 ? 375 SER B CB  1 
ATOM   1877 O OG  . SER B 1 75  ? 22.042  43.745  12.459  1.00 109.87 ? 375 SER B OG  1 
ATOM   1878 N N   . GLN B 1 76  ? 20.597  39.839  14.097  1.00 99.19  ? 376 GLN B N   1 
ATOM   1879 C CA  . GLN B 1 76  ? 21.019  38.449  14.037  1.00 91.09  ? 376 GLN B CA  1 
ATOM   1880 C C   . GLN B 1 76  ? 20.043  37.672  14.914  1.00 87.29  ? 376 GLN B C   1 
ATOM   1881 O O   . GLN B 1 76  ? 20.114  37.746  16.138  1.00 89.82  ? 376 GLN B O   1 
ATOM   1882 C CB  . GLN B 1 76  ? 22.475  38.369  14.499  1.00 94.22  ? 376 GLN B CB  1 
ATOM   1883 C CG  . GLN B 1 76  ? 22.922  37.008  15.025  1.00 98.25  ? 376 GLN B CG  1 
ATOM   1884 C CD  . GLN B 1 76  ? 24.299  37.020  15.668  1.00 109.89 ? 376 GLN B CD  1 
ATOM   1885 O OE1 . GLN B 1 76  ? 24.701  37.991  16.321  1.00 119.22 ? 376 GLN B OE1 1 
ATOM   1886 N NE2 . GLN B 1 76  ? 25.054  35.945  15.484  1.00 107.08 ? 376 GLN B NE2 1 
ATOM   1887 N N   . LEU B 1 77  ? 19.103  36.974  14.275  1.00 84.41  ? 377 LEU B N   1 
ATOM   1888 C CA  . LEU B 1 77  ? 18.041  36.271  14.981  1.00 81.22  ? 377 LEU B CA  1 
ATOM   1889 C C   . LEU B 1 77  ? 18.446  34.831  15.296  1.00 75.67  ? 377 LEU B C   1 
ATOM   1890 O O   . LEU B 1 77  ? 18.033  34.295  16.321  1.00 75.22  ? 377 LEU B O   1 
ATOM   1891 C CB  . LEU B 1 77  ? 16.766  36.312  14.141  1.00 83.69  ? 377 LEU B CB  1 
ATOM   1892 C CG  . LEU B 1 77  ? 15.885  37.558  14.291  1.00 87.43  ? 377 LEU B CG  1 
ATOM   1893 C CD1 . LEU B 1 77  ? 16.568  38.823  13.773  1.00 86.60  ? 377 LEU B CD1 1 
ATOM   1894 C CD2 . LEU B 1 77  ? 14.572  37.334  13.559  1.00 86.90  ? 377 LEU B CD2 1 
ATOM   1895 N N   . VAL B 1 78  ? 19.228  34.218  14.389  1.00 74.53  ? 378 VAL B N   1 
ATOM   1896 C CA  . VAL B 1 78  ? 19.579  32.811  14.462  1.00 64.74  ? 378 VAL B CA  1 
ATOM   1897 C C   . VAL B 1 78  ? 21.092  32.658  14.388  1.00 63.65  ? 378 VAL B C   1 
ATOM   1898 O O   . VAL B 1 78  ? 21.688  32.913  13.347  1.00 67.14  ? 378 VAL B O   1 
ATOM   1899 C CB  . VAL B 1 78  ? 18.912  32.065  13.300  1.00 64.44  ? 378 VAL B CB  1 
ATOM   1900 C CG1 . VAL B 1 78  ? 19.343  30.602  13.286  1.00 71.97  ? 378 VAL B CG1 1 
ATOM   1901 C CG2 . VAL B 1 78  ? 17.386  32.179  13.308  1.00 62.32  ? 378 VAL B CG2 1 
ATOM   1902 N N   . LEU B 1 79  ? 21.697  32.231  15.500  1.00 62.33  ? 379 LEU B N   1 
ATOM   1903 C CA  . LEU B 1 79  ? 23.112  31.899  15.566  1.00 65.56  ? 379 LEU B CA  1 
ATOM   1904 C C   . LEU B 1 79  ? 23.293  30.421  15.209  1.00 66.95  ? 379 LEU B C   1 
ATOM   1905 O O   . LEU B 1 79  ? 22.520  29.573  15.656  1.00 66.94  ? 379 LEU B O   1 
ATOM   1906 C CB  . LEU B 1 79  ? 23.588  32.225  16.985  1.00 66.37  ? 379 LEU B CB  1 
ATOM   1907 C CG  . LEU B 1 79  ? 25.100  32.366  17.218  1.00 69.26  ? 379 LEU B CG  1 
ATOM   1908 C CD1 . LEU B 1 79  ? 25.400  33.086  18.520  1.00 70.02  ? 379 LEU B CD1 1 
ATOM   1909 C CD2 . LEU B 1 79  ? 25.783  31.015  17.214  1.00 69.38  ? 379 LEU B CD2 1 
ATOM   1910 N N   . VAL B 1 80  ? 24.308  30.112  14.394  1.00 67.99  ? 380 VAL B N   1 
ATOM   1911 C CA  . VAL B 1 80  ? 24.520  28.754  13.934  1.00 66.59  ? 380 VAL B CA  1 
ATOM   1912 C C   . VAL B 1 80  ? 25.796  28.180  14.532  1.00 66.38  ? 380 VAL B C   1 
ATOM   1913 O O   . VAL B 1 80  ? 26.849  28.781  14.437  1.00 65.38  ? 380 VAL B O   1 
ATOM   1914 C CB  . VAL B 1 80  ? 24.557  28.762  12.402  1.00 73.01  ? 380 VAL B CB  1 
ATOM   1915 C CG1 . VAL B 1 80  ? 25.070  27.445  11.842  1.00 80.02  ? 380 VAL B CG1 1 
ATOM   1916 C CG2 . VAL B 1 80  ? 23.175  29.071  11.843  1.00 77.33  ? 380 VAL B CG2 1 
ATOM   1917 N N   . THR B 1 81  ? 25.694  26.998  15.141  1.00 68.45  ? 381 THR B N   1 
ATOM   1918 C CA  . THR B 1 81  ? 26.872  26.280  15.600  1.00 74.29  ? 381 THR B CA  1 
ATOM   1919 C C   . THR B 1 81  ? 26.805  24.839  15.102  1.00 74.75  ? 381 THR B C   1 
ATOM   1920 O O   . THR B 1 81  ? 25.828  24.427  14.477  1.00 76.69  ? 381 THR B O   1 
ATOM   1921 C CB  . THR B 1 81  ? 27.010  26.358  17.122  1.00 75.51  ? 381 THR B CB  1 
ATOM   1922 O OG1 . THR B 1 81  ? 25.887  25.746  17.742  1.00 69.80  ? 381 THR B OG1 1 
ATOM   1923 C CG2 . THR B 1 81  ? 27.122  27.793  17.595  1.00 79.59  ? 381 THR B CG2 1 
ATOM   1924 N N   . LYS B 1 82  ? 27.892  24.101  15.339  1.00 72.70  ? 382 LYS B N   1 
ATOM   1925 C CA  . LYS B 1 82  ? 27.907  22.671  15.097  1.00 66.95  ? 382 LYS B CA  1 
ATOM   1926 C C   . LYS B 1 82  ? 27.060  22.040  16.193  1.00 63.25  ? 382 LYS B C   1 
ATOM   1927 O O   . LYS B 1 82  ? 26.580  22.774  17.065  1.00 61.05  ? 382 LYS B O   1 
ATOM   1928 C CB  . LYS B 1 82  ? 29.347  22.156  15.041  1.00 67.45  ? 382 LYS B CB  1 
ATOM   1929 C CG  . LYS B 1 82  ? 30.004  22.459  13.717  1.00 70.24  ? 382 LYS B CG  1 
ATOM   1930 C CD  . LYS B 1 82  ? 31.348  21.779  13.510  1.00 78.99  ? 382 LYS B CD  1 
ATOM   1931 C CE  . LYS B 1 82  ? 31.843  21.904  12.077  1.00 82.03  ? 382 LYS B CE  1 
ATOM   1932 N NZ  . LYS B 1 82  ? 33.032  21.112  11.724  1.00 81.86  ? 382 LYS B NZ  1 
ATOM   1933 N N   . GLY B 1 83  ? 26.906  20.702  16.123  1.00 56.96  ? 383 GLY B N   1 
ATOM   1934 C CA  . GLY B 1 83  ? 26.043  19.943  17.015  1.00 53.25  ? 383 GLY B CA  1 
ATOM   1935 C C   . GLY B 1 83  ? 26.750  19.393  18.255  1.00 54.91  ? 383 GLY B C   1 
ATOM   1936 O O   . GLY B 1 83  ? 26.082  19.017  19.221  1.00 55.51  ? 383 GLY B O   1 
ATOM   1937 N N   . PHE B 1 84  ? 28.083  19.286  18.228  1.00 57.73  ? 384 PHE B N   1 
ATOM   1938 C CA  . PHE B 1 84  ? 28.805  18.675  19.334  1.00 63.72  ? 384 PHE B CA  1 
ATOM   1939 C C   . PHE B 1 84  ? 28.198  17.305  19.612  1.00 61.84  ? 384 PHE B C   1 
ATOM   1940 O O   . PHE B 1 84  ? 28.005  16.543  18.678  1.00 59.75  ? 384 PHE B O   1 
ATOM   1941 C CB  . PHE B 1 84  ? 28.785  19.679  20.495  1.00 67.31  ? 384 PHE B CB  1 
ATOM   1942 C CG  . PHE B 1 84  ? 29.393  20.991  20.022  1.00 69.94  ? 384 PHE B CG  1 
ATOM   1943 C CD1 . PHE B 1 84  ? 28.595  21.976  19.443  1.00 65.91  ? 384 PHE B CD1 1 
ATOM   1944 C CD2 . PHE B 1 84  ? 30.771  21.179  20.055  1.00 70.33  ? 384 PHE B CD2 1 
ATOM   1945 C CE1 . PHE B 1 84  ? 29.156  23.139  18.953  1.00 66.04  ? 384 PHE B CE1 1 
ATOM   1946 C CE2 . PHE B 1 84  ? 31.324  22.343  19.563  1.00 71.85  ? 384 PHE B CE2 1 
ATOM   1947 C CZ  . PHE B 1 84  ? 30.516  23.326  19.024  1.00 70.42  ? 384 PHE B CZ  1 
ATOM   1948 N N   . ASN B 1 85  ? 27.854  17.028  20.879  1.00 64.66  ? 385 ASN B N   1 
ATOM   1949 C CA  . ASN B 1 85  ? 27.368  15.721  21.301  1.00 68.62  ? 385 ASN B CA  1 
ATOM   1950 C C   . ASN B 1 85  ? 25.865  15.561  21.057  1.00 65.99  ? 385 ASN B C   1 
ATOM   1951 O O   . ASN B 1 85  ? 25.240  14.661  21.627  1.00 64.79  ? 385 ASN B O   1 
ATOM   1952 C CB  . ASN B 1 85  ? 27.572  15.473  22.794  1.00 73.27  ? 385 ASN B CB  1 
ATOM   1953 C CG  . ASN B 1 85  ? 29.002  15.621  23.255  1.00 81.22  ? 385 ASN B CG  1 
ATOM   1954 O OD1 . ASN B 1 85  ? 29.920  15.795  22.445  1.00 88.37  ? 385 ASN B OD1 1 
ATOM   1955 N ND2 . ASN B 1 85  ? 29.214  15.561  24.562  1.00 85.70  ? 385 ASN B ND2 1 
ATOM   1956 N N   . LEU B 1 86  ? 25.256  16.461  20.280  1.00 61.89  ? 386 LEU B N   1 
ATOM   1957 C CA  . LEU B 1 86  ? 23.908  16.212  19.806  1.00 60.88  ? 386 LEU B CA  1 
ATOM   1958 C C   . LEU B 1 86  ? 24.004  15.426  18.506  1.00 60.84  ? 386 LEU B C   1 
ATOM   1959 O O   . LEU B 1 86  ? 24.937  15.603  17.716  1.00 55.27  ? 386 LEU B O   1 
ATOM   1960 C CB  . LEU B 1 86  ? 23.101  17.487  19.568  1.00 64.77  ? 386 LEU B CB  1 
ATOM   1961 C CG  . LEU B 1 86  ? 22.834  18.381  20.781  1.00 68.53  ? 386 LEU B CG  1 
ATOM   1962 C CD1 . LEU B 1 86  ? 21.688  19.315  20.455  1.00 63.45  ? 386 LEU B CD1 1 
ATOM   1963 C CD2 . LEU B 1 86  ? 22.564  17.571  22.048  1.00 73.12  ? 386 LEU B CD2 1 
ATOM   1964 N N   . PHE B 1 87  ? 22.982  14.596  18.265  1.00 61.15  ? 387 PHE B N   1 
ATOM   1965 C CA  . PHE B 1 87  ? 22.933  13.785  17.063  1.00 54.44  ? 387 PHE B CA  1 
ATOM   1966 C C   . PHE B 1 87  ? 22.403  14.676  15.963  1.00 50.37  ? 387 PHE B C   1 
ATOM   1967 O O   . PHE B 1 87  ? 21.296  14.463  15.493  1.00 51.15  ? 387 PHE B O   1 
ATOM   1968 C CB  . PHE B 1 87  ? 22.101  12.525  17.330  1.00 55.58  ? 387 PHE B CB  1 
ATOM   1969 C CG  . PHE B 1 87  ? 22.802  11.530  18.255  1.00 55.08  ? 387 PHE B CG  1 
ATOM   1970 C CD1 . PHE B 1 87  ? 23.994  10.918  17.870  1.00 56.47  ? 387 PHE B CD1 1 
ATOM   1971 C CD2 . PHE B 1 87  ? 22.273  11.219  19.500  1.00 55.20  ? 387 PHE B CD2 1 
ATOM   1972 C CE1 . PHE B 1 87  ? 24.648  10.035  18.703  1.00 60.02  ? 387 PHE B CE1 1 
ATOM   1973 C CE2 . PHE B 1 87  ? 22.932  10.330  20.335  1.00 62.12  ? 387 PHE B CE2 1 
ATOM   1974 C CZ  . PHE B 1 87  ? 24.116  9.729   19.931  1.00 63.22  ? 387 PHE B CZ  1 
ATOM   1975 N N   . CYS B 1 88  ? 23.183  15.710  15.636  1.00 49.66  ? 388 CYS B N   1 
ATOM   1976 C CA  . CYS B 1 88  ? 22.791  16.694  14.646  1.00 50.68  ? 388 CYS B CA  1 
ATOM   1977 C C   . CYS B 1 88  ? 24.041  17.282  14.014  1.00 54.37  ? 388 CYS B C   1 
ATOM   1978 O O   . CYS B 1 88  ? 25.132  17.181  14.563  1.00 59.05  ? 388 CYS B O   1 
ATOM   1979 C CB  . CYS B 1 88  ? 21.861  17.753  15.241  1.00 55.32  ? 388 CYS B CB  1 
ATOM   1980 S SG  . CYS B 1 88  ? 22.613  18.929  16.407  1.00 59.62  ? 388 CYS B SG  1 
ATOM   1981 N N   . LYS B 1 89  ? 23.873  17.878  12.834  1.00 60.24  ? 389 LYS B N   1 
ATOM   1982 C CA  . LYS B 1 89  ? 24.983  18.465  12.101  1.00 64.49  ? 389 LYS B CA  1 
ATOM   1983 C C   . LYS B 1 89  ? 25.222  19.891  12.591  1.00 65.70  ? 389 LYS B C   1 
ATOM   1984 O O   . LYS B 1 89  ? 26.350  20.357  12.657  1.00 70.80  ? 389 LYS B O   1 
ATOM   1985 C CB  . LYS B 1 89  ? 24.716  18.392  10.593  1.00 64.86  ? 389 LYS B CB  1 
ATOM   1986 C CG  . LYS B 1 89  ? 24.949  17.006  10.002  1.00 66.58  ? 389 LYS B CG  1 
ATOM   1987 C CD  . LYS B 1 89  ? 24.710  16.864  8.505   1.00 68.39  ? 389 LYS B CD  1 
ATOM   1988 C CE  . LYS B 1 89  ? 24.951  15.464  8.000   1.00 67.06  ? 389 LYS B CE  1 
ATOM   1989 N NZ  . LYS B 1 89  ? 24.872  15.411  6.533   1.00 67.72  ? 389 LYS B NZ  1 
ATOM   1990 N N   . TYR B 1 90  ? 24.143  20.574  12.949  1.00 65.97  ? 390 TYR B N   1 
ATOM   1991 C CA  . TYR B 1 90  ? 24.210  21.979  13.305  1.00 66.79  ? 390 TYR B CA  1 
ATOM   1992 C C   . TYR B 1 90  ? 23.157  22.228  14.378  1.00 60.45  ? 390 TYR B C   1 
ATOM   1993 O O   . TYR B 1 90  ? 22.180  21.483  14.464  1.00 62.68  ? 390 TYR B O   1 
ATOM   1994 C CB  . TYR B 1 90  ? 23.943  22.896  12.098  1.00 66.05  ? 390 TYR B CB  1 
ATOM   1995 C CG  . TYR B 1 90  ? 24.911  22.844  10.919  1.00 68.01  ? 390 TYR B CG  1 
ATOM   1996 C CD1 . TYR B 1 90  ? 26.276  23.044  11.078  1.00 71.52  ? 390 TYR B CD1 1 
ATOM   1997 C CD2 . TYR B 1 90  ? 24.442  22.611  9.632   1.00 70.72  ? 390 TYR B CD2 1 
ATOM   1998 C CE1 . TYR B 1 90  ? 27.144  22.990  9.996   1.00 79.14  ? 390 TYR B CE1 1 
ATOM   1999 C CE2 . TYR B 1 90  ? 25.299  22.537  8.546   1.00 75.54  ? 390 TYR B CE2 1 
ATOM   2000 C CZ  . TYR B 1 90  ? 26.656  22.738  8.719   1.00 82.23  ? 390 TYR B CZ  1 
ATOM   2001 O OH  . TYR B 1 90  ? 27.452  22.675  7.597   1.00 79.61  ? 390 TYR B OH  1 
ATOM   2002 N N   . ILE B 1 91  ? 23.386  23.258  15.195  1.00 56.35  ? 391 ILE B N   1 
ATOM   2003 C CA  . ILE B 1 91  ? 22.338  23.828  16.028  1.00 57.71  ? 391 ILE B CA  1 
ATOM   2004 C C   . ILE B 1 91  ? 22.015  25.254  15.567  1.00 57.96  ? 391 ILE B C   1 
ATOM   2005 O O   . ILE B 1 91  ? 22.905  26.101  15.449  1.00 58.90  ? 391 ILE B O   1 
ATOM   2006 C CB  . ILE B 1 91  ? 22.751  23.822  17.502  1.00 57.40  ? 391 ILE B CB  1 
ATOM   2007 C CG1 . ILE B 1 91  ? 23.029  22.424  17.998  1.00 54.57  ? 391 ILE B CG1 1 
ATOM   2008 C CG2 . ILE B 1 91  ? 21.684  24.519  18.342  1.00 60.37  ? 391 ILE B CG2 1 
ATOM   2009 C CD1 . ILE B 1 91  ? 23.905  22.390  19.234  1.00 55.52  ? 391 ILE B CD1 1 
ATOM   2010 N N   . TYR B 1 92  ? 20.732  25.500  15.294  1.00 52.12  ? 392 TYR B N   1 
ATOM   2011 C CA  . TYR B 1 92  ? 20.266  26.842  15.016  1.00 53.54  ? 392 TYR B CA  1 
ATOM   2012 C C   . TYR B 1 92  ? 19.678  27.447  16.300  1.00 54.46  ? 392 TYR B C   1 
ATOM   2013 O O   . TYR B 1 92  ? 18.577  27.081  16.724  1.00 52.28  ? 392 TYR B O   1 
ATOM   2014 C CB  . TYR B 1 92  ? 19.228  26.735  13.899  1.00 48.38  ? 392 TYR B CB  1 
ATOM   2015 C CG  . TYR B 1 92  ? 19.667  26.447  12.473  1.00 43.02  ? 392 TYR B CG  1 
ATOM   2016 C CD1 . TYR B 1 92  ? 20.968  26.100  12.123  1.00 42.06  ? 392 TYR B CD1 1 
ATOM   2017 C CD2 . TYR B 1 92  ? 18.721  26.538  11.459  1.00 40.85  ? 392 TYR B CD2 1 
ATOM   2018 C CE1 . TYR B 1 92  ? 21.296  25.799  10.804  1.00 41.24  ? 392 TYR B CE1 1 
ATOM   2019 C CE2 . TYR B 1 92  ? 19.036  26.245  10.149  1.00 41.04  ? 392 TYR B CE2 1 
ATOM   2020 C CZ  . TYR B 1 92  ? 20.317  25.854  9.823   1.00 42.02  ? 392 TYR B CZ  1 
ATOM   2021 O OH  . TYR B 1 92  ? 20.494  25.592  8.485   1.00 45.82  ? 392 TYR B OH  1 
ATOM   2022 N N   . HIS B 1 93  ? 20.414  28.374  16.924  1.00 55.19  ? 393 HIS B N   1 
ATOM   2023 C CA  . HIS B 1 93  ? 19.953  29.009  18.154  1.00 56.11  ? 393 HIS B CA  1 
ATOM   2024 C C   . HIS B 1 93  ? 19.111  30.235  17.816  1.00 56.19  ? 393 HIS B C   1 
ATOM   2025 O O   . HIS B 1 93  ? 19.612  31.207  17.254  1.00 58.03  ? 393 HIS B O   1 
ATOM   2026 C CB  . HIS B 1 93  ? 21.116  29.455  19.045  1.00 56.04  ? 393 HIS B CB  1 
ATOM   2027 C CG  . HIS B 1 93  ? 22.160  28.418  19.203  1.00 55.23  ? 393 HIS B CG  1 
ATOM   2028 N ND1 . HIS B 1 93  ? 22.235  27.614  20.316  1.00 54.99  ? 393 HIS B ND1 1 
ATOM   2029 C CD2 . HIS B 1 93  ? 23.172  28.063  18.396  1.00 55.60  ? 393 HIS B CD2 1 
ATOM   2030 C CE1 . HIS B 1 93  ? 23.282  26.813  20.184  1.00 58.90  ? 393 HIS B CE1 1 
ATOM   2031 N NE2 . HIS B 1 93  ? 23.863  27.062  19.015  1.00 58.29  ? 393 HIS B NE2 1 
ATOM   2032 N N   . VAL B 1 94  ? 17.828  30.187  18.158  1.00 55.41  ? 394 VAL B N   1 
ATOM   2033 C CA  . VAL B 1 94  ? 16.981  31.357  18.000  1.00 59.50  ? 394 VAL B CA  1 
ATOM   2034 C C   . VAL B 1 94  ? 17.280  32.329  19.139  1.00 57.55  ? 394 VAL B C   1 
ATOM   2035 O O   . VAL B 1 94  ? 17.156  31.969  20.300  1.00 56.28  ? 394 VAL B O   1 
ATOM   2036 C CB  . VAL B 1 94  ? 15.492  30.962  17.966  1.00 63.20  ? 394 VAL B CB  1 
ATOM   2037 C CG1 . VAL B 1 94  ? 14.585  32.178  18.115  1.00 62.86  ? 394 VAL B CG1 1 
ATOM   2038 C CG2 . VAL B 1 94  ? 15.142  30.180  16.697  1.00 63.65  ? 394 VAL B CG2 1 
ATOM   2039 N N   . LEU B 1 95  ? 17.707  33.548  18.802  1.00 57.83  ? 395 LEU B N   1 
ATOM   2040 C CA  . LEU B 1 95  ? 18.009  34.553  19.805  1.00 61.04  ? 395 LEU B CA  1 
ATOM   2041 C C   . LEU B 1 95  ? 16.805  35.470  19.962  1.00 65.72  ? 395 LEU B C   1 
ATOM   2042 O O   . LEU B 1 95  ? 16.538  36.280  19.078  1.00 67.69  ? 395 LEU B O   1 
ATOM   2043 C CB  . LEU B 1 95  ? 19.232  35.355  19.377  1.00 62.48  ? 395 LEU B CB  1 
ATOM   2044 C CG  . LEU B 1 95  ? 20.388  34.522  18.821  1.00 60.17  ? 395 LEU B CG  1 
ATOM   2045 C CD1 . LEU B 1 95  ? 21.566  35.408  18.467  1.00 63.73  ? 395 LEU B CD1 1 
ATOM   2046 C CD2 . LEU B 1 95  ? 20.782  33.448  19.819  1.00 55.99  ? 395 LEU B CD2 1 
ATOM   2047 N N   . TRP B 1 96  ? 16.089  35.334  21.083  1.00 67.50  ? 396 TRP B N   1 
ATOM   2048 C CA  . TRP B 1 96  ? 15.053  36.288  21.441  1.00 72.22  ? 396 TRP B CA  1 
ATOM   2049 C C   . TRP B 1 96  ? 15.663  37.556  22.044  1.00 78.13  ? 396 TRP B C   1 
ATOM   2050 O O   . TRP B 1 96  ? 16.006  37.566  23.225  1.00 78.71  ? 396 TRP B O   1 
ATOM   2051 C CB  . TRP B 1 96  ? 14.092  35.668  22.451  1.00 70.24  ? 396 TRP B CB  1 
ATOM   2052 C CG  . TRP B 1 96  ? 13.484  34.382  21.991  1.00 69.74  ? 396 TRP B CG  1 
ATOM   2053 C CD1 . TRP B 1 96  ? 14.003  33.129  22.140  1.00 65.52  ? 396 TRP B CD1 1 
ATOM   2054 C CD2 . TRP B 1 96  ? 12.191  34.224  21.370  1.00 70.86  ? 396 TRP B CD2 1 
ATOM   2055 N NE1 . TRP B 1 96  ? 13.140  32.210  21.603  1.00 62.41  ? 396 TRP B NE1 1 
ATOM   2056 C CE2 . TRP B 1 96  ? 12.015  32.842  21.147  1.00 62.36  ? 396 TRP B CE2 1 
ATOM   2057 C CE3 . TRP B 1 96  ? 11.174  35.106  20.993  1.00 72.42  ? 396 TRP B CE3 1 
ATOM   2058 C CZ2 . TRP B 1 96  ? 10.871  32.332  20.553  1.00 60.77  ? 396 TRP B CZ2 1 
ATOM   2059 C CZ3 . TRP B 1 96  ? 10.029  34.593  20.426  1.00 70.17  ? 396 TRP B CZ3 1 
ATOM   2060 C CH2 . TRP B 1 96  ? 9.887   33.226  20.207  1.00 63.56  ? 396 TRP B CH2 1 
ATOM   2061 N N   . HIS B 1 97  ? 15.769  38.626  21.245  1.00 82.44  ? 397 HIS B N   1 
ATOM   2062 C CA  . HIS B 1 97  ? 16.096  39.943  21.786  1.00 90.61  ? 397 HIS B CA  1 
ATOM   2063 C C   . HIS B 1 97  ? 14.794  40.555  22.300  1.00 100.70 ? 397 HIS B C   1 
ATOM   2064 O O   . HIS B 1 97  ? 13.764  40.450  21.638  1.00 103.83 ? 397 HIS B O   1 
ATOM   2065 C CB  . HIS B 1 97  ? 16.783  40.845  20.753  1.00 88.19  ? 397 HIS B CB  1 
ATOM   2066 C CG  . HIS B 1 97  ? 17.897  40.181  20.015  1.00 86.54  ? 397 HIS B CG  1 
ATOM   2067 N ND1 . HIS B 1 97  ? 19.196  40.171  20.477  1.00 87.11  ? 397 HIS B ND1 1 
ATOM   2068 C CD2 . HIS B 1 97  ? 17.911  39.481  18.854  1.00 84.58  ? 397 HIS B CD2 1 
ATOM   2069 C CE1 . HIS B 1 97  ? 19.965  39.500  19.618  1.00 83.89  ? 397 HIS B CE1 1 
ATOM   2070 N NE2 . HIS B 1 97  ? 19.208  39.088  18.615  1.00 81.90  ? 397 HIS B NE2 1 
ATOM   2071 N N   . SER B 1 98  ? 14.835  41.196  23.477  1.00 113.19 ? 398 SER B N   1 
ATOM   2072 C CA  . SER B 1 98  ? 13.615  41.617  24.159  1.00 124.09 ? 398 SER B CA  1 
ATOM   2073 C C   . SER B 1 98  ? 13.281  43.077  23.838  1.00 128.87 ? 398 SER B C   1 
ATOM   2074 O O   . SER B 1 98  ? 12.892  43.833  24.728  1.00 145.65 ? 398 SER B O   1 
ATOM   2075 C CB  . SER B 1 98  ? 13.705  41.377  25.663  1.00 125.87 ? 398 SER B CB  1 
ATOM   2076 O OG  . SER B 1 98  ? 14.841  42.018  26.232  1.00 125.00 ? 398 SER B OG  1 
ATOM   2077 N N   . GLU B 1 99  ? 13.396  43.469  22.562  1.00 130.60 ? 399 GLU B N   1 
ATOM   2078 C CA  . GLU B 1 99  ? 13.085  44.828  22.135  1.00 134.84 ? 399 GLU B CA  1 
ATOM   2079 C C   . GLU B 1 99  ? 12.198  44.804  20.883  1.00 131.24 ? 399 GLU B C   1 
ATOM   2080 O O   . GLU B 1 99  ? 12.128  45.803  20.173  1.00 128.95 ? 399 GLU B O   1 
ATOM   2081 C CB  . GLU B 1 99  ? 14.408  45.576  21.918  1.00 140.31 ? 399 GLU B CB  1 
ATOM   2082 C CG  . GLU B 1 99  ? 14.395  47.030  22.399  1.00 151.04 ? 399 GLU B CG  1 
ATOM   2083 C CD  . GLU B 1 99  ? 15.583  47.923  22.025  1.00 155.25 ? 399 GLU B CD  1 
ATOM   2084 O OE1 . GLU B 1 99  ? 15.517  49.171  22.147  1.00 144.45 ? 399 GLU B OE1 1 
ATOM   2085 O OE2 . GLU B 1 99  ? 16.608  47.352  21.601  1.00 171.98 ? 399 GLU B OE2 1 
ATOM   2086 N N   . PHE B 1 100 ? 11.511  43.675  20.614  1.00 122.56 ? 400 PHE B N   1 
ATOM   2087 C CA  . PHE B 1 100 ? 10.793  43.458  19.362  1.00 116.13 ? 400 PHE B CA  1 
ATOM   2088 C C   . PHE B 1 100 ? 9.479   42.723  19.625  1.00 108.50 ? 400 PHE B C   1 
ATOM   2089 O O   . PHE B 1 100 ? 9.385   42.006  20.612  1.00 104.08 ? 400 PHE B O   1 
ATOM   2090 C CB  . PHE B 1 100 ? 11.653  42.624  18.412  1.00 114.88 ? 400 PHE B CB  1 
ATOM   2091 C CG  . PHE B 1 100 ? 12.965  43.283  18.013  1.00 119.58 ? 400 PHE B CG  1 
ATOM   2092 C CD1 . PHE B 1 100 ? 13.003  44.271  17.033  1.00 122.36 ? 400 PHE B CD1 1 
ATOM   2093 C CD2 . PHE B 1 100 ? 14.158  42.910  18.626  1.00 120.76 ? 400 PHE B CD2 1 
ATOM   2094 C CE1 . PHE B 1 100 ? 14.205  44.868  16.681  1.00 126.28 ? 400 PHE B CE1 1 
ATOM   2095 C CE2 . PHE B 1 100 ? 15.359  43.506  18.265  1.00 124.61 ? 400 PHE B CE2 1 
ATOM   2096 C CZ  . PHE B 1 100 ? 15.381  44.484  17.294  1.00 125.16 ? 400 PHE B CZ  1 
ATOM   2097 N N   . PRO B 1 101 ? 8.438   42.848  18.756  1.00 107.77 ? 401 PRO B N   1 
ATOM   2098 C CA  . PRO B 1 101 ? 7.148   42.189  18.983  1.00 105.08 ? 401 PRO B CA  1 
ATOM   2099 C C   . PRO B 1 101 ? 7.342   40.686  18.823  1.00 99.41  ? 401 PRO B C   1 
ATOM   2100 O O   . PRO B 1 101 ? 8.013   40.263  17.888  1.00 97.52  ? 401 PRO B O   1 
ATOM   2101 C CB  . PRO B 1 101 ? 6.179   42.749  17.927  1.00 108.47 ? 401 PRO B CB  1 
ATOM   2102 C CG  . PRO B 1 101 ? 6.985   43.769  17.147  1.00 109.54 ? 401 PRO B CG  1 
ATOM   2103 C CD  . PRO B 1 101 ? 8.456   43.578  17.479  1.00 108.04 ? 401 PRO B CD  1 
ATOM   2104 N N   . LYS B 1 102 ? 6.769   39.902  19.749  1.00 95.86  ? 402 LYS B N   1 
ATOM   2105 C CA  . LYS B 1 102 ? 7.121   38.500  19.926  1.00 88.15  ? 402 LYS B CA  1 
ATOM   2106 C C   . LYS B 1 102 ? 6.638   37.686  18.721  1.00 85.94  ? 402 LYS B C   1 
ATOM   2107 O O   . LYS B 1 102 ? 7.436   37.035  18.024  1.00 76.02  ? 402 LYS B O   1 
ATOM   2108 C CB  . LYS B 1 102 ? 6.579   37.992  21.270  1.00 89.32  ? 402 LYS B CB  1 
ATOM   2109 C CG  . LYS B 1 102 ? 7.191   38.648  22.495  1.00 95.54  ? 402 LYS B CG  1 
ATOM   2110 C CD  . LYS B 1 102 ? 8.651   38.249  22.669  1.00 100.73 ? 402 LYS B CD  1 
ATOM   2111 C CE  . LYS B 1 102 ? 9.529   39.271  23.342  1.00 109.41 ? 402 LYS B CE  1 
ATOM   2112 N NZ  . LYS B 1 102 ? 10.938  38.866  23.232  1.00 107.50 ? 402 LYS B NZ  1 
ATOM   2113 N N   . PRO B 1 103 ? 5.329   37.756  18.373  1.00 85.84  ? 403 PRO B N   1 
ATOM   2114 C CA  . PRO B 1 103 ? 4.842   37.048  17.189  1.00 83.09  ? 403 PRO B CA  1 
ATOM   2115 C C   . PRO B 1 103 ? 5.674   37.315  15.931  1.00 84.01  ? 403 PRO B C   1 
ATOM   2116 O O   . PRO B 1 103 ? 5.753   36.459  15.060  1.00 87.58  ? 403 PRO B O   1 
ATOM   2117 C CB  . PRO B 1 103 ? 3.386   37.557  17.065  1.00 86.65  ? 403 PRO B CB  1 
ATOM   2118 C CG  . PRO B 1 103 ? 3.006   37.947  18.473  1.00 87.29  ? 403 PRO B CG  1 
ATOM   2119 C CD  . PRO B 1 103 ? 4.279   38.558  19.030  1.00 86.68  ? 403 PRO B CD  1 
ATOM   2120 N N   . GLN B 1 104 ? 6.291   38.501  15.835  1.00 89.07  ? 404 GLN B N   1 
ATOM   2121 C CA  . GLN B 1 104 ? 7.090   38.859  14.677  1.00 93.14  ? 404 GLN B CA  1 
ATOM   2122 C C   . GLN B 1 104 ? 8.479   38.228  14.743  1.00 92.57  ? 404 GLN B C   1 
ATOM   2123 O O   . GLN B 1 104 ? 9.085   37.996  13.702  1.00 94.08  ? 404 GLN B O   1 
ATOM   2124 C CB  . GLN B 1 104 ? 7.319   40.360  14.532  1.00 99.47  ? 404 GLN B CB  1 
ATOM   2125 C CG  . GLN B 1 104 ? 6.216   41.101  13.790  1.00 108.61 ? 404 GLN B CG  1 
ATOM   2126 C CD  . GLN B 1 104 ? 6.571   42.557  13.551  1.00 121.01 ? 404 GLN B CD  1 
ATOM   2127 O OE1 . GLN B 1 104 ? 7.734   42.967  13.675  1.00 123.18 ? 404 GLN B OE1 1 
ATOM   2128 N NE2 . GLN B 1 104 ? 5.572   43.362  13.209  1.00 125.00 ? 404 GLN B NE2 1 
ATOM   2129 N N   . ILE B 1 105 ? 9.034   38.023  15.944  1.00 91.71  ? 405 ILE B N   1 
ATOM   2130 C CA  . ILE B 1 105 ? 10.388  37.490  15.983  1.00 90.87  ? 405 ILE B CA  1 
ATOM   2131 C C   . ILE B 1 105 ? 10.326  35.988  15.772  1.00 79.74  ? 405 ILE B C   1 
ATOM   2132 O O   . ILE B 1 105 ? 11.248  35.440  15.194  1.00 79.62  ? 405 ILE B O   1 
ATOM   2133 C CB  . ILE B 1 105 ? 11.198  37.876  17.232  1.00 101.14 ? 405 ILE B CB  1 
ATOM   2134 C CG1 . ILE B 1 105 ? 10.565  37.370  18.510  1.00 107.15 ? 405 ILE B CG1 1 
ATOM   2135 C CG2 . ILE B 1 105 ? 11.462  39.383  17.249  1.00 110.22 ? 405 ILE B CG2 1 
ATOM   2136 C CD1 . ILE B 1 105 ? 11.198  37.945  19.758  1.00 118.57 ? 405 ILE B CD1 1 
ATOM   2137 N N   . LEU B 1 106 ? 9.239   35.346  16.202  1.00 72.87  ? 406 LEU B N   1 
ATOM   2138 C CA  . LEU B 1 106 ? 9.016   33.952  15.866  1.00 68.14  ? 406 LEU B CA  1 
ATOM   2139 C C   . LEU B 1 106 ? 8.899   33.833  14.344  1.00 69.60  ? 406 LEU B C   1 
ATOM   2140 O O   . LEU B 1 106 ? 9.574   33.014  13.700  1.00 63.94  ? 406 LEU B O   1 
ATOM   2141 C CB  . LEU B 1 106 ? 7.764   33.448  16.583  1.00 67.90  ? 406 LEU B CB  1 
ATOM   2142 C CG  . LEU B 1 106 ? 7.410   31.969  16.387  1.00 63.83  ? 406 LEU B CG  1 
ATOM   2143 C CD1 . LEU B 1 106 ? 8.508   31.098  16.967  1.00 58.86  ? 406 LEU B CD1 1 
ATOM   2144 C CD2 . LEU B 1 106 ? 6.044   31.612  16.994  1.00 66.01  ? 406 LEU B CD2 1 
ATOM   2145 N N   . LYS B 1 107 ? 8.043   34.673  13.756  1.00 68.27  ? 407 LYS B N   1 
ATOM   2146 C CA  . LYS B 1 107 ? 7.752   34.516  12.350  1.00 71.53  ? 407 LYS B CA  1 
ATOM   2147 C C   . LYS B 1 107 ? 9.048   34.716  11.576  1.00 70.00  ? 407 LYS B C   1 
ATOM   2148 O O   . LYS B 1 107 ? 9.289   34.016  10.606  1.00 70.05  ? 407 LYS B O   1 
ATOM   2149 C CB  . LYS B 1 107 ? 6.600   35.428  11.934  1.00 83.47  ? 407 LYS B CB  1 
ATOM   2150 C CG  . LYS B 1 107 ? 6.174   35.315  10.483  1.00 96.48  ? 407 LYS B CG  1 
ATOM   2151 C CD  . LYS B 1 107 ? 6.597   36.424  9.516   1.00 105.01 ? 407 LYS B CD  1 
ATOM   2152 C CE  . LYS B 1 107 ? 5.806   36.347  8.233   1.00 108.71 ? 407 LYS B CE  1 
ATOM   2153 N NZ  . LYS B 1 107 ? 6.186   37.375  7.260   1.00 116.96 ? 407 LYS B NZ  1 
ATOM   2154 N N   . HIS B 1 108 ? 9.894   35.646  12.029  1.00 71.93  ? 408 HIS B N   1 
ATOM   2155 C CA  . HIS B 1 108 ? 11.133  35.964  11.334  1.00 73.40  ? 408 HIS B CA  1 
ATOM   2156 C C   . HIS B 1 108 ? 12.162  34.870  11.619  1.00 67.44  ? 408 HIS B C   1 
ATOM   2157 O O   . HIS B 1 108 ? 12.899  34.458  10.730  1.00 65.02  ? 408 HIS B O   1 
ATOM   2158 C CB  . HIS B 1 108 ? 11.652  37.359  11.725  1.00 80.53  ? 408 HIS B CB  1 
ATOM   2159 C CG  . HIS B 1 108 ? 10.934  38.548  11.143  1.00 88.88  ? 408 HIS B CG  1 
ATOM   2160 N ND1 . HIS B 1 108 ? 10.346  38.581  9.894   1.00 95.89  ? 408 HIS B ND1 1 
ATOM   2161 C CD2 . HIS B 1 108 ? 10.771  39.773  11.654  1.00 91.24  ? 408 HIS B CD2 1 
ATOM   2162 C CE1 . HIS B 1 108 ? 9.825   39.778  9.674   1.00 94.71  ? 408 HIS B CE1 1 
ATOM   2163 N NE2 . HIS B 1 108 ? 10.070  40.513  10.732  1.00 98.56  ? 408 HIS B NE2 1 
ATOM   2164 N N   . ALA B 1 109 ? 12.211  34.395  12.864  1.00 64.57  ? 409 ALA B N   1 
ATOM   2165 C CA  . ALA B 1 109 ? 13.164  33.372  13.253  1.00 62.66  ? 409 ALA B CA  1 
ATOM   2166 C C   . ALA B 1 109 ? 12.898  32.064  12.483  1.00 63.07  ? 409 ALA B C   1 
ATOM   2167 O O   . ALA B 1 109 ? 13.840  31.340  12.115  1.00 54.47  ? 409 ALA B O   1 
ATOM   2168 C CB  . ALA B 1 109 ? 13.128  33.178  14.763  1.00 60.25  ? 409 ALA B CB  1 
ATOM   2169 N N   . MET B 1 110 ? 11.625  31.799  12.212  1.00 62.07  ? 410 MET B N   1 
ATOM   2170 C CA  . MET B 1 110 ? 11.261  30.597  11.433  1.00 59.34  ? 410 MET B CA  1 
ATOM   2171 C C   . MET B 1 110 ? 11.801  30.747  10.009  1.00 63.44  ? 410 MET B C   1 
ATOM   2172 O O   . MET B 1 110 ? 12.584  29.888  9.584   1.00 66.12  ? 410 MET B O   1 
ATOM   2173 C CB  . MET B 1 110 ? 9.743   30.436  11.404  1.00 61.36  ? 410 MET B CB  1 
ATOM   2174 C CG  . MET B 1 110 ? 9.160   29.875  12.685  1.00 63.60  ? 410 MET B CG  1 
ATOM   2175 S SD  . MET B 1 110 ? 9.861   28.277  13.140  1.00 60.73  ? 410 MET B SD  1 
ATOM   2176 C CE  . MET B 1 110 ? 9.096   27.232  11.894  1.00 56.47  ? 410 MET B CE  1 
ATOM   2177 N N   . LYS B 1 111 ? 11.406  31.807  9.310   1.00 70.66  ? 411 LYS B N   1 
ATOM   2178 C CA  . LYS B 1 111 ? 11.890  32.048  7.931   1.00 71.08  ? 411 LYS B CA  1 
ATOM   2179 C C   . LYS B 1 111 ? 13.397  31.831  7.857   1.00 62.06  ? 411 LYS B C   1 
ATOM   2180 O O   . LYS B 1 111 ? 13.836  31.083  6.990   1.00 54.83  ? 411 LYS B O   1 
ATOM   2181 C CB  . LYS B 1 111 ? 11.703  33.507  7.519   1.00 85.22  ? 411 LYS B CB  1 
ATOM   2182 C CG  . LYS B 1 111 ? 10.300  34.071  7.488   1.00 95.83  ? 411 LYS B CG  1 
ATOM   2183 C CD  . LYS B 1 111 ? 9.903   34.512  6.085   1.00 103.54 ? 411 LYS B CD  1 
ATOM   2184 C CE  . LYS B 1 111 ? 8.647   35.319  6.073   1.00 111.26 ? 411 LYS B CE  1 
ATOM   2185 N NZ  . LYS B 1 111 ? 7.488   34.521  5.668   1.00 119.98 ? 411 LYS B NZ  1 
ATOM   2186 N N   . GLU B 1 112 ? 14.149  32.484  8.734   1.00 61.90  ? 412 GLU B N   1 
ATOM   2187 C CA  . GLU B 1 112 ? 15.626  32.392  8.691   1.00 64.31  ? 412 GLU B CA  1 
ATOM   2188 C C   . GLU B 1 112 ? 16.041  30.929  8.842   1.00 59.06  ? 412 GLU B C   1 
ATOM   2189 O O   . GLU B 1 112 ? 16.813  30.454  8.001   1.00 59.49  ? 412 GLU B O   1 
ATOM   2190 C CB  . GLU B 1 112 ? 16.213  33.264  9.797   1.00 30.00  ? 412 GLU B CB  1 
ATOM   2191 C CG  . GLU B 1 112 ? 17.722  33.454  9.682   1.00 30.00  ? 412 GLU B CG  1 
ATOM   2192 C CD  . GLU B 1 112 ? 18.270  34.526  10.605  1.00 30.00  ? 412 GLU B CD  1 
ATOM   2193 O OE1 . GLU B 1 112 ? 17.512  35.457  10.941  1.00 30.00  ? 412 GLU B OE1 1 
ATOM   2194 O OE2 . GLU B 1 112 ? 19.454  34.431  10.988  1.00 30.00  ? 412 GLU B OE2 1 
ATOM   2195 N N   . CYS B 1 113 ? 15.535  30.253  9.871   1.00 55.47  ? 413 CYS B N   1 
ATOM   2196 C CA  . CYS B 1 113 ? 15.843  28.819  10.086  1.00 51.79  ? 413 CYS B CA  1 
ATOM   2197 C C   . CYS B 1 113 ? 15.584  28.046  8.784   1.00 50.76  ? 413 CYS B C   1 
ATOM   2198 O O   . CYS B 1 113 ? 16.492  27.330  8.339   1.00 47.75  ? 413 CYS B O   1 
ATOM   2199 C CB  . CYS B 1 113 ? 15.004  28.282  11.237  1.00 52.79  ? 413 CYS B CB  1 
ATOM   2200 S SG  . CYS B 1 113 ? 15.563  28.807  12.875  1.00 57.07  ? 413 CYS B SG  1 
ATOM   2201 N N   . LEU B 1 114 ? 14.412  28.224  8.185   1.00 50.19  ? 414 LEU B N   1 
ATOM   2202 C CA  . LEU B 1 114 ? 14.038  27.477  6.961   1.00 49.84  ? 414 LEU B CA  1 
ATOM   2203 C C   . LEU B 1 114 ? 14.831  27.960  5.736   1.00 55.20  ? 414 LEU B C   1 
ATOM   2204 O O   . LEU B 1 114 ? 15.006  27.159  4.810   1.00 61.12  ? 414 LEU B O   1 
ATOM   2205 C CB  . LEU B 1 114 ? 12.534  27.639  6.771   1.00 50.70  ? 414 LEU B CB  1 
ATOM   2206 C CG  . LEU B 1 114 ? 11.646  27.004  7.843   1.00 49.54  ? 414 LEU B CG  1 
ATOM   2207 C CD1 . LEU B 1 114 ? 10.194  27.362  7.597   1.00 50.73  ? 414 LEU B CD1 1 
ATOM   2208 C CD2 . LEU B 1 114 ? 11.829  25.501  7.852   1.00 47.19  ? 414 LEU B CD2 1 
ATOM   2209 N N   . GLU B 1 115 ? 15.280  29.212  5.712   1.00 57.33  ? 415 GLU B N   1 
ATOM   2210 C CA  . GLU B 1 115 ? 16.075  29.671  4.594   1.00 59.11  ? 415 GLU B CA  1 
ATOM   2211 C C   . GLU B 1 115 ? 17.459  29.073  4.729   1.00 57.25  ? 415 GLU B C   1 
ATOM   2212 O O   . GLU B 1 115 ? 18.087  28.707  3.747   1.00 56.72  ? 415 GLU B O   1 
ATOM   2213 C CB  . GLU B 1 115 ? 16.246  31.187  4.614   1.00 66.22  ? 415 GLU B CB  1 
ATOM   2214 C CG  . GLU B 1 115 ? 14.944  31.925  4.351   1.00 72.01  ? 415 GLU B CG  1 
ATOM   2215 C CD  . GLU B 1 115 ? 14.966  32.606  3.029   1.00 77.25  ? 415 GLU B CD  1 
ATOM   2216 O OE1 . GLU B 1 115 ? 15.714  33.595  2.978   1.00 79.43  ? 415 GLU B OE1 1 
ATOM   2217 O OE2 . GLU B 1 115 ? 14.287  32.112  2.110   1.00 85.37  ? 415 GLU B OE2 1 
ATOM   2218 N N   . LYS B 1 116 ? 17.947  29.002  5.965   1.00 57.08  ? 416 LYS B N   1 
ATOM   2219 C CA  . LYS B 1 116 ? 19.239  28.385  6.174   1.00 60.20  ? 416 LYS B CA  1 
ATOM   2220 C C   . LYS B 1 116 ? 19.171  26.909  5.753   1.00 60.81  ? 416 LYS B C   1 
ATOM   2221 O O   . LYS B 1 116 ? 20.180  26.345  5.326   1.00 59.11  ? 416 LYS B O   1 
ATOM   2222 C CB  . LYS B 1 116 ? 19.696  28.532  7.625   1.00 58.20  ? 416 LYS B CB  1 
ATOM   2223 C CG  . LYS B 1 116 ? 19.990  29.924  8.079   1.00 60.49  ? 416 LYS B CG  1 
ATOM   2224 C CD  . LYS B 1 116 ? 21.196  30.024  9.002   1.00 65.05  ? 416 LYS B CD  1 
ATOM   2225 C CE  . LYS B 1 116 ? 21.456  31.446  9.424   1.00 72.24  ? 416 LYS B CE  1 
ATOM   2226 N NZ  . LYS B 1 116 ? 21.534  32.388  8.297   1.00 79.70  ? 416 LYS B NZ  1 
ATOM   2227 N N   . CYS B 1 117 ? 17.982  26.285  5.842   1.00 57.45  ? 417 CYS B N   1 
ATOM   2228 C CA  . CYS B 1 117 ? 17.856  24.914  5.355   1.00 62.30  ? 417 CYS B CA  1 
ATOM   2229 C C   . CYS B 1 117 ? 18.206  24.829  3.867   1.00 66.71  ? 417 CYS B C   1 
ATOM   2230 O O   . CYS B 1 117 ? 18.796  23.842  3.423   1.00 77.94  ? 417 CYS B O   1 
ATOM   2231 C CB  . CYS B 1 117 ? 16.492  24.267  5.589   1.00 55.21  ? 417 CYS B CB  1 
ATOM   2232 S SG  . CYS B 1 117 ? 16.084  24.051  7.339   1.00 48.71  ? 417 CYS B SG  1 
ATOM   2233 N N   . ILE B 1 118 ? 17.869  25.847  3.077   1.00 62.92  ? 418 ILE B N   1 
ATOM   2234 C CA  . ILE B 1 118 ? 18.278  25.807  1.682   1.00 62.52  ? 418 ILE B CA  1 
ATOM   2235 C C   . ILE B 1 118 ? 19.767  26.116  1.581   1.00 64.46  ? 418 ILE B C   1 
ATOM   2236 O O   . ILE B 1 118 ? 20.441  25.521  0.761   1.00 65.98  ? 418 ILE B O   1 
ATOM   2237 C CB  . ILE B 1 118 ? 17.438  26.726  0.791   1.00 60.09  ? 418 ILE B CB  1 
ATOM   2238 C CG1 . ILE B 1 118 ? 15.969  26.450  0.961   1.00 60.47  ? 418 ILE B CG1 1 
ATOM   2239 C CG2 . ILE B 1 118 ? 17.855  26.556  -0.658  1.00 62.89  ? 418 ILE B CG2 1 
ATOM   2240 C CD1 . ILE B 1 118 ? 15.054  27.437  0.262   1.00 64.69  ? 418 ILE B CD1 1 
ATOM   2241 N N   . GLU B 1 119 ? 20.275  26.999  2.446   1.00 65.50  ? 419 GLU B N   1 
ATOM   2242 C CA  . GLU B 1 119 ? 21.664  27.428  2.387   1.00 68.89  ? 419 GLU B CA  1 
ATOM   2243 C C   . GLU B 1 119 ? 22.580  26.232  2.601   1.00 66.59  ? 419 GLU B C   1 
ATOM   2244 O O   . GLU B 1 119 ? 23.518  26.013  1.841   1.00 70.19  ? 419 GLU B O   1 
ATOM   2245 C CB  . GLU B 1 119 ? 21.994  28.545  3.390   1.00 71.73  ? 419 GLU B CB  1 
ATOM   2246 C CG  . GLU B 1 119 ? 21.283  29.862  3.079   1.00 73.76  ? 419 GLU B CG  1 
ATOM   2247 C CD  . GLU B 1 119 ? 21.476  30.998  4.050   1.00 73.90  ? 419 GLU B CD  1 
ATOM   2248 O OE1 . GLU B 1 119 ? 22.291  30.817  4.965   1.00 78.00  ? 419 GLU B OE1 1 
ATOM   2249 O OE2 . GLU B 1 119 ? 20.833  32.050  3.893   1.00 74.73  ? 419 GLU B OE2 1 
ATOM   2250 N N   . GLN B 1 120 ? 22.282  25.431  3.619   1.00 66.77  ? 420 GLN B N   1 
ATOM   2251 C CA  . GLN B 1 120 ? 23.204  24.382  4.016   1.00 69.34  ? 420 GLN B CA  1 
ATOM   2252 C C   . GLN B 1 120 ? 22.798  23.002  3.494   1.00 65.17  ? 420 GLN B C   1 
ATOM   2253 O O   . GLN B 1 120 ? 23.352  22.017  3.964   1.00 64.69  ? 420 GLN B O   1 
ATOM   2254 C CB  . GLN B 1 120 ? 23.327  24.440  5.534   1.00 67.50  ? 420 GLN B CB  1 
ATOM   2255 C CG  . GLN B 1 120 ? 24.256  25.540  6.016   1.00 67.61  ? 420 GLN B CG  1 
ATOM   2256 C CD  . GLN B 1 120 ? 24.155  25.690  7.507   1.00 67.26  ? 420 GLN B CD  1 
ATOM   2257 O OE1 . GLN B 1 120 ? 23.046  25.675  8.058   1.00 69.35  ? 420 GLN B OE1 1 
ATOM   2258 N NE2 . GLN B 1 120 ? 25.302  25.755  8.165   1.00 69.01  ? 420 GLN B NE2 1 
ATOM   2259 N N   . ASN B 1 121 ? 21.880  22.935  2.515   1.00 64.35  ? 421 ASN B N   1 
ATOM   2260 C CA  . ASN B 1 121 ? 21.404  21.662  2.001   1.00 67.27  ? 421 ASN B CA  1 
ATOM   2261 C C   . ASN B 1 121 ? 21.061  20.743  3.177   1.00 66.13  ? 421 ASN B C   1 
ATOM   2262 O O   . ASN B 1 121 ? 21.640  19.668  3.324   1.00 72.25  ? 421 ASN B O   1 
ATOM   2263 C CB  . ASN B 1 121 ? 22.441  21.009  1.096   1.00 70.68  ? 421 ASN B CB  1 
ATOM   2264 C CG  . ASN B 1 121 ? 22.772  21.850  -0.112  1.00 74.80  ? 421 ASN B CG  1 
ATOM   2265 O OD1 . ASN B 1 121 ? 23.929  22.255  -0.272  1.00 78.85  ? 421 ASN B OD1 1 
ATOM   2266 N ND2 . ASN B 1 121 ? 21.792  22.105  -0.971  1.00 73.95  ? 421 ASN B ND2 1 
ATOM   2267 N N   . ILE B 1 122 ? 20.166  21.237  4.031   1.00 60.47  ? 422 ILE B N   1 
ATOM   2268 C CA  . ILE B 1 122 ? 19.629  20.571  5.203   1.00 56.53  ? 422 ILE B CA  1 
ATOM   2269 C C   . ILE B 1 122 ? 18.474  19.717  4.711   1.00 53.46  ? 422 ILE B C   1 
ATOM   2270 O O   . ILE B 1 122 ? 17.666  20.190  3.920   1.00 51.21  ? 422 ILE B O   1 
ATOM   2271 C CB  . ILE B 1 122 ? 19.177  21.651  6.233   1.00 53.93  ? 422 ILE B CB  1 
ATOM   2272 C CG1 . ILE B 1 122 ? 20.370  22.445  6.789   1.00 54.07  ? 422 ILE B CG1 1 
ATOM   2273 C CG2 . ILE B 1 122 ? 18.295  21.121  7.367   1.00 47.96  ? 422 ILE B CG2 1 
ATOM   2274 C CD1 . ILE B 1 122 ? 21.549  21.606  7.240   1.00 53.47  ? 422 ILE B CD1 1 
ATOM   2275 N N   . THR B 1 123 ? 18.402  18.469  5.183   1.00 56.22  ? 423 THR B N   1 
ATOM   2276 C CA  . THR B 1 123 ? 17.311  17.572  4.798   1.00 59.60  ? 423 THR B CA  1 
ATOM   2277 C C   . THR B 1 123 ? 16.337  17.376  5.956   1.00 51.52  ? 423 THR B C   1 
ATOM   2278 O O   . THR B 1 123 ? 15.196  16.980  5.740   1.00 56.31  ? 423 THR B O   1 
ATOM   2279 C CB  . THR B 1 123 ? 17.820  16.219  4.295   1.00 60.06  ? 423 THR B CB  1 
ATOM   2280 O OG1 . THR B 1 123 ? 18.552  15.662  5.374   1.00 62.32  ? 423 THR B OG1 1 
ATOM   2281 C CG2 . THR B 1 123 ? 18.751  16.333  3.106   1.00 58.73  ? 423 THR B CG2 1 
ATOM   2282 N N   . SER B 1 124 ? 16.751  17.673  7.184   1.00 45.00  ? 424 SER B N   1 
ATOM   2283 C CA  . SER B 1 124 ? 15.807  17.514  8.271   1.00 43.18  ? 424 SER B CA  1 
ATOM   2284 C C   . SER B 1 124 ? 16.088  18.541  9.350   1.00 38.52  ? 424 SER B C   1 
ATOM   2285 O O   . SER B 1 124 ? 17.246  18.839  9.643   1.00 36.19  ? 424 SER B O   1 
ATOM   2286 C CB  . SER B 1 124 ? 15.866  16.105  8.815   1.00 43.59  ? 424 SER B CB  1 
ATOM   2287 O OG  . SER B 1 124 ? 17.163  15.832  9.323   1.00 45.99  ? 424 SER B OG  1 
ATOM   2288 N N   . ILE B 1 125 ? 15.005  19.044  9.948   1.00 37.44  ? 425 ILE B N   1 
ATOM   2289 C CA  . ILE B 1 125 ? 15.118  20.085  10.963  1.00 37.79  ? 425 ILE B CA  1 
ATOM   2290 C C   . ILE B 1 125 ? 14.030  19.843  11.995  1.00 36.00  ? 425 ILE B C   1 
ATOM   2291 O O   . ILE B 1 125 ? 12.876  19.648  11.613  1.00 38.67  ? 425 ILE B O   1 
ATOM   2292 C CB  . ILE B 1 125 ? 15.035  21.518  10.367  1.00 37.59  ? 425 ILE B CB  1 
ATOM   2293 C CG1 . ILE B 1 125 ? 15.197  22.588  11.451  1.00 37.83  ? 425 ILE B CG1 1 
ATOM   2294 C CG2 . ILE B 1 125 ? 13.737  21.751  9.587   1.00 37.44  ? 425 ILE B CG2 1 
ATOM   2295 C CD1 . ILE B 1 125 ? 15.526  23.965  10.916  1.00 41.67  ? 425 ILE B CD1 1 
ATOM   2296 N N   . SER B 1 126 ? 14.404  19.888  13.281  1.00 34.42  ? 426 SER B N   1 
ATOM   2297 C CA  . SER B 1 126 ? 13.456  19.669  14.350  1.00 37.92  ? 426 SER B CA  1 
ATOM   2298 C C   . SER B 1 126 ? 13.466  20.871  15.279  1.00 40.36  ? 426 SER B C   1 
ATOM   2299 O O   . SER B 1 126 ? 14.530  21.320  15.722  1.00 37.13  ? 426 SER B O   1 
ATOM   2300 C CB  . SER B 1 126 ? 13.752  18.386  15.099  1.00 42.09  ? 426 SER B CB  1 
ATOM   2301 O OG  . SER B 1 126 ? 13.813  17.280  14.193  1.00 51.36  ? 426 SER B OG  1 
ATOM   2302 N N   . PHE B 1 127 ? 12.243  21.311  15.608  1.00 44.25  ? 427 PHE B N   1 
ATOM   2303 C CA  . PHE B 1 127 ? 11.974  22.519  16.357  1.00 45.23  ? 427 PHE B CA  1 
ATOM   2304 C C   . PHE B 1 127 ? 11.211  22.134  17.617  1.00 48.46  ? 427 PHE B C   1 
ATOM   2305 O O   . PHE B 1 127 ? 10.294  21.314  17.533  1.00 47.85  ? 427 PHE B O   1 
ATOM   2306 C CB  . PHE B 1 127 ? 11.069  23.510  15.605  1.00 45.96  ? 427 PHE B CB  1 
ATOM   2307 C CG  . PHE B 1 127 ? 11.515  24.031  14.237  1.00 49.00  ? 427 PHE B CG  1 
ATOM   2308 C CD1 . PHE B 1 127 ? 11.302  23.290  13.072  1.00 47.79  ? 427 PHE B CD1 1 
ATOM   2309 C CD2 . PHE B 1 127 ? 12.055  25.310  14.099  1.00 51.39  ? 427 PHE B CD2 1 
ATOM   2310 C CE1 . PHE B 1 127 ? 11.700  23.761  11.835  1.00 46.42  ? 427 PHE B CE1 1 
ATOM   2311 C CE2 . PHE B 1 127 ? 12.419  25.795  12.853  1.00 50.48  ? 427 PHE B CE2 1 
ATOM   2312 C CZ  . PHE B 1 127 ? 12.253  25.013  11.728  1.00 51.21  ? 427 PHE B CZ  1 
ATOM   2313 N N   . PRO B 1 128 ? 11.478  22.804  18.776  1.00 51.11  ? 428 PRO B N   1 
ATOM   2314 C CA  . PRO B 1 128 ? 10.609  22.725  19.943  1.00 49.37  ? 428 PRO B CA  1 
ATOM   2315 C C   . PRO B 1 128 ? 9.455   23.679  19.693  1.00 50.35  ? 428 PRO B C   1 
ATOM   2316 O O   . PRO B 1 128 ? 9.421   24.311  18.648  1.00 47.89  ? 428 PRO B O   1 
ATOM   2317 C CB  . PRO B 1 128 ? 11.526  23.149  21.071  1.00 49.39  ? 428 PRO B CB  1 
ATOM   2318 C CG  . PRO B 1 128 ? 12.431  24.167  20.440  1.00 48.22  ? 428 PRO B CG  1 
ATOM   2319 C CD  . PRO B 1 128 ? 12.609  23.717  19.018  1.00 50.91  ? 428 PRO B CD  1 
ATOM   2320 N N   . ALA B 1 129 ? 8.492   23.738  20.617  1.00 55.95  ? 429 ALA B N   1 
ATOM   2321 C CA  . ALA B 1 129 ? 7.391   24.675  20.478  1.00 60.35  ? 429 ALA B CA  1 
ATOM   2322 C C   . ALA B 1 129 ? 7.871   26.067  20.889  1.00 66.14  ? 429 ALA B C   1 
ATOM   2323 O O   . ALA B 1 129 ? 7.651   26.507  22.030  1.00 70.48  ? 429 ALA B O   1 
ATOM   2324 C CB  . ALA B 1 129 ? 6.213   24.225  21.298  1.00 67.20  ? 429 ALA B CB  1 
ATOM   2325 N N   . LEU B 1 130 ? 8.512   26.739  19.918  1.00 60.44  ? 430 LEU B N   1 
ATOM   2326 C CA  . LEU B 1 130 ? 9.189   28.009  20.125  1.00 59.73  ? 430 LEU B CA  1 
ATOM   2327 C C   . LEU B 1 130 ? 8.231   29.057  20.674  1.00 62.03  ? 430 LEU B C   1 
ATOM   2328 O O   . LEU B 1 130 ? 7.178   29.320  20.090  1.00 64.32  ? 430 LEU B O   1 
ATOM   2329 C CB  . LEU B 1 130 ? 9.782   28.488  18.804  1.00 57.55  ? 430 LEU B CB  1 
ATOM   2330 C CG  . LEU B 1 130 ? 11.065  27.803  18.332  1.00 51.45  ? 430 LEU B CG  1 
ATOM   2331 C CD1 . LEU B 1 130 ? 11.291  28.221  16.905  1.00 53.87  ? 430 LEU B CD1 1 
ATOM   2332 C CD2 . LEU B 1 130 ? 12.286  28.101  19.167  1.00 49.48  ? 430 LEU B CD2 1 
ATOM   2333 N N   . GLY B 1 131 ? 8.629   29.653  21.800  1.00 65.01  ? 431 GLY B N   1 
ATOM   2334 C CA  . GLY B 1 131 ? 7.966   30.837  22.314  1.00 68.89  ? 431 GLY B CA  1 
ATOM   2335 C C   . GLY B 1 131 ? 6.770   30.499  23.199  1.00 71.72  ? 431 GLY B C   1 
ATOM   2336 O O   . GLY B 1 131 ? 6.026   31.398  23.579  1.00 77.93  ? 431 GLY B O   1 
ATOM   2337 N N   . THR B 1 132 ? 6.604   29.231  23.553  1.00 68.30  ? 432 THR B N   1 
ATOM   2338 C CA  . THR B 1 132 ? 5.444   28.843  24.370  1.00 66.92  ? 432 THR B CA  1 
ATOM   2339 C C   . THR B 1 132 ? 5.851   28.889  25.821  1.00 68.98  ? 432 THR B C   1 
ATOM   2340 O O   . THR B 1 132 ? 4.990   28.643  26.683  1.00 73.83  ? 432 THR B O   1 
ATOM   2341 C CB  . THR B 1 132 ? 4.948   27.466  23.936  1.00 62.89  ? 432 THR B CB  1 
ATOM   2342 O OG1 . THR B 1 132 ? 6.097   26.632  23.896  1.00 60.24  ? 432 THR B OG1 1 
ATOM   2343 C CG2 . THR B 1 132 ? 4.291   27.495  22.570  1.00 63.01  ? 432 THR B CG2 1 
ATOM   2344 N N   . GLY B 1 133 ? 7.102   29.247  26.096  1.00 67.98  ? 433 GLY B N   1 
ATOM   2345 C CA  . GLY B 1 133 ? 7.604   29.212  27.481  1.00 71.61  ? 433 GLY B CA  1 
ATOM   2346 C C   . GLY B 1 133 ? 7.085   30.353  28.325  1.00 78.73  ? 433 GLY B C   1 
ATOM   2347 O O   . GLY B 1 133 ? 6.906   31.454  27.773  1.00 85.02  ? 433 GLY B O   1 
ATOM   2348 N N   . ASN B 1 134 ? 6.853   30.104  29.616  1.00 83.39  ? 434 ASN B N   1 
ATOM   2349 C CA  . ASN B 1 134 ? 6.329   31.142  30.547  1.00 87.80  ? 434 ASN B CA  1 
ATOM   2350 C C   . ASN B 1 134 ? 5.163   31.856  29.869  1.00 95.36  ? 434 ASN B C   1 
ATOM   2351 O O   . ASN B 1 134 ? 5.030   33.077  30.065  1.00 109.43 ? 434 ASN B O   1 
ATOM   2352 C CB  . ASN B 1 134 ? 7.416   32.112  30.988  1.00 86.66  ? 434 ASN B CB  1 
ATOM   2353 C CG  . ASN B 1 134 ? 8.520   31.429  31.754  1.00 86.70  ? 434 ASN B CG  1 
ATOM   2354 O OD1 . ASN B 1 134 ? 8.258   30.772  32.766  1.00 88.24  ? 434 ASN B OD1 1 
ATOM   2355 N ND2 . ASN B 1 134 ? 9.752   31.575  31.293  1.00 81.57  ? 434 ASN B ND2 1 
ATOM   2356 N N   . MET B 1 135 ? 4.355   31.120  29.110  1.00 98.59  ? 435 MET B N   1 
ATOM   2357 C CA  . MET B 1 135 ? 3.230   31.726  28.357  1.00 105.75 ? 435 MET B CA  1 
ATOM   2358 C C   . MET B 1 135 ? 3.660   33.083  27.774  1.00 105.92 ? 435 MET B C   1 
ATOM   2359 O O   . MET B 1 135 ? 3.031   34.095  28.132  1.00 125.18 ? 435 MET B O   1 
ATOM   2360 C CB  . MET B 1 135 ? 2.004   31.883  29.260  1.00 112.81 ? 435 MET B CB  1 
ATOM   2361 C CG  . MET B 1 135 ? 1.448   30.572  29.771  1.00 118.11 ? 435 MET B CG  1 
ATOM   2362 S SD  . MET B 1 135 ? 2.320   30.008  31.245  1.00 131.21 ? 435 MET B SD  1 
ATOM   2363 C CE  . MET B 1 135 ? 2.275   31.512  32.229  1.00 128.99 ? 435 MET B CE  1 
ATOM   2364 N N   . GLU B 1 136 ? 4.671   33.104  26.902  1.00 93.65  ? 436 GLU B N   1 
ATOM   2365 C CA  . GLU B 1 136 ? 5.086   34.362  26.230  1.00 85.17  ? 436 GLU B CA  1 
ATOM   2366 C C   . GLU B 1 136 ? 4.243   34.522  24.962  1.00 81.45  ? 436 GLU B C   1 
ATOM   2367 O O   . GLU B 1 136 ? 3.666   35.606  24.767  1.00 81.79  ? 436 GLU B O   1 
ATOM   2368 C CB  . GLU B 1 136 ? 6.576   34.316  25.907  1.00 79.93  ? 436 GLU B CB  1 
ATOM   2369 C CG  . GLU B 1 136 ? 7.199   35.696  25.733  1.00 83.68  ? 436 GLU B CG  1 
ATOM   2370 C CD  . GLU B 1 136 ? 7.254   36.489  27.024  1.00 86.99  ? 436 GLU B CD  1 
ATOM   2371 O OE1 . GLU B 1 136 ? 8.055   36.126  27.908  1.00 85.41  ? 436 GLU B OE1 1 
ATOM   2372 O OE2 . GLU B 1 136 ? 6.490   37.468  27.144  1.00 87.01  ? 436 GLU B OE2 1 
ATOM   2373 N N   . ILE B 1 137 ? 4.198   33.486  24.128  1.00 80.40  ? 437 ILE B N   1 
ATOM   2374 C CA  . ILE B 1 137 ? 3.321   33.515  22.924  1.00 78.75  ? 437 ILE B CA  1 
ATOM   2375 C C   . ILE B 1 137 ? 2.226   32.468  23.161  1.00 78.83  ? 437 ILE B C   1 
ATOM   2376 O O   . ILE B 1 137 ? 2.536   31.422  23.755  1.00 72.49  ? 437 ILE B O   1 
ATOM   2377 C CB  . ILE B 1 137 ? 4.126   33.273  21.637  1.00 73.82  ? 437 ILE B CB  1 
ATOM   2378 C CG1 . ILE B 1 137 ? 5.363   34.164  21.569  1.00 73.12  ? 437 ILE B CG1 1 
ATOM   2379 C CG2 . ILE B 1 137 ? 3.247   33.439  20.398  1.00 73.67  ? 437 ILE B CG2 1 
ATOM   2380 C CD1 . ILE B 1 137 ? 6.033   34.182  20.208  1.00 70.30  ? 437 ILE B CD1 1 
ATOM   2381 N N   . LYS B 1 138 ? 0.993   32.762  22.755  1.00 85.22  ? 438 LYS B N   1 
ATOM   2382 C CA  . LYS B 1 138 ? -0.141  31.851  23.048  1.00 90.80  ? 438 LYS B CA  1 
ATOM   2383 C C   . LYS B 1 138 ? 0.062   30.522  22.316  1.00 89.77  ? 438 LYS B C   1 
ATOM   2384 O O   . LYS B 1 138 ? 0.622   30.535  21.207  1.00 88.58  ? 438 LYS B O   1 
ATOM   2385 C CB  . LYS B 1 138 ? -1.458  32.538  22.676  1.00 97.64  ? 438 LYS B CB  1 
ATOM   2386 C CG  . LYS B 1 138 ? -1.817  33.740  23.535  1.00 106.81 ? 438 LYS B CG  1 
ATOM   2387 C CD  . LYS B 1 138 ? -3.120  34.414  23.124  1.00 113.13 ? 438 LYS B CD  1 
ATOM   2388 C CE  . LYS B 1 138 ? -3.458  35.577  24.000  1.00 118.05 ? 438 LYS B CE  1 
ATOM   2389 N NZ  . LYS B 1 138 ? -4.699  36.236  23.587  1.00 117.76 ? 438 LYS B NZ  1 
ATOM   2390 N N   . LYS B 1 139 ? -0.431  29.431  22.898  1.00 92.75  ? 439 LYS B N   1 
ATOM   2391 C CA  . LYS B 1 139 ? -0.163  28.123  22.318  1.00 90.38  ? 439 LYS B CA  1 
ATOM   2392 C C   . LYS B 1 139 ? -0.587  28.084  20.856  1.00 85.27  ? 439 LYS B C   1 
ATOM   2393 O O   . LYS B 1 139 ? 0.212   27.757  19.987  1.00 87.05  ? 439 LYS B O   1 
ATOM   2394 C CB  . LYS B 1 139 ? -0.921  27.011  23.046  1.00 99.92  ? 439 LYS B CB  1 
ATOM   2395 C CG  . LYS B 1 139 ? -0.610  26.878  24.522  1.00 115.50 ? 439 LYS B CG  1 
ATOM   2396 C CD  . LYS B 1 139 ? -1.386  25.757  25.205  1.00 128.28 ? 439 LYS B CD  1 
ATOM   2397 C CE  . LYS B 1 139 ? -0.865  25.452  26.582  1.00 137.90 ? 439 LYS B CE  1 
ATOM   2398 N NZ  . LYS B 1 139 ? -1.140  26.535  27.530  1.00 144.51 ? 439 LYS B NZ  1 
ATOM   2399 N N   . GLU B 1 140 ? -1.844  28.440  20.597  1.00 87.90  ? 440 GLU B N   1 
ATOM   2400 C CA  . GLU B 1 140 ? -2.431  28.350  19.267  1.00 90.90  ? 440 GLU B CA  1 
ATOM   2401 C C   . GLU B 1 140 ? -1.724  29.281  18.282  1.00 89.04  ? 440 GLU B C   1 
ATOM   2402 O O   . GLU B 1 140 ? -1.724  29.015  17.086  1.00 91.69  ? 440 GLU B O   1 
ATOM   2403 C CB  . GLU B 1 140 ? -3.910  28.748  19.241  1.00 99.32  ? 440 GLU B CB  1 
ATOM   2404 C CG  . GLU B 1 140 ? -4.837  27.810  20.011  1.00 105.33 ? 440 GLU B CG  1 
ATOM   2405 C CD  . GLU B 1 140 ? -4.856  27.941  21.528  1.00 108.72 ? 440 GLU B CD  1 
ATOM   2406 O OE1 . GLU B 1 140 ? -4.182  28.855  22.065  1.00 108.10 ? 440 GLU B OE1 1 
ATOM   2407 O OE2 . GLU B 1 140 ? -5.536  27.103  22.165  1.00 109.21 ? 440 GLU B OE2 1 
ATOM   2408 N N   . THR B 1 141 ? -1.168  30.394  18.779  1.00 86.46  ? 441 THR B N   1 
ATOM   2409 C CA  . THR B 1 141 ? -0.522  31.390  17.936  1.00 82.08  ? 441 THR B CA  1 
ATOM   2410 C C   . THR B 1 141 ? 0.857   30.877  17.509  1.00 73.68  ? 441 THR B C   1 
ATOM   2411 O O   . THR B 1 141 ? 1.226   30.976  16.339  1.00 68.23  ? 441 THR B O   1 
ATOM   2412 C CB  . THR B 1 141 ? -0.460  32.735  18.672  1.00 81.88  ? 441 THR B CB  1 
ATOM   2413 O OG1 . THR B 1 141 ? -1.780  33.268  18.738  1.00 85.86  ? 441 THR B OG1 1 
ATOM   2414 C CG2 . THR B 1 141 ? 0.349   33.787  17.938  1.00 80.75  ? 441 THR B CG2 1 
ATOM   2415 N N   . ALA B 1 142 ? 1.623   30.344  18.466  1.00 70.27  ? 442 ALA B N   1 
ATOM   2416 C CA  . ALA B 1 142 ? 2.886   29.720  18.131  1.00 70.04  ? 442 ALA B CA  1 
ATOM   2417 C C   . ALA B 1 142 ? 2.634   28.685  17.034  1.00 72.98  ? 442 ALA B C   1 
ATOM   2418 O O   . ALA B 1 142 ? 3.202   28.790  15.947  1.00 76.30  ? 442 ALA B O   1 
ATOM   2419 C CB  . ALA B 1 142 ? 3.508   29.117  19.362  1.00 69.25  ? 442 ALA B CB  1 
ATOM   2420 N N   . ALA B 1 143 ? 1.716   27.745  17.308  1.00 72.43  ? 443 ALA B N   1 
ATOM   2421 C CA  . ALA B 1 143 ? 1.327   26.728  16.343  1.00 68.84  ? 443 ALA B CA  1 
ATOM   2422 C C   . ALA B 1 143 ? 0.885   27.372  15.031  1.00 71.01  ? 443 ALA B C   1 
ATOM   2423 O O   . ALA B 1 143 ? 1.368   26.996  13.973  1.00 74.98  ? 443 ALA B O   1 
ATOM   2424 C CB  . ALA B 1 143 ? 0.253   25.843  16.915  1.00 68.79  ? 443 ALA B CB  1 
ATOM   2425 N N   . GLU B 1 144 ? -0.003  28.361  15.091  1.00 73.13  ? 444 GLU B N   1 
ATOM   2426 C CA  . GLU B 1 144 ? -0.435  29.044  13.885  1.00 78.61  ? 444 GLU B CA  1 
ATOM   2427 C C   . GLU B 1 144 ? 0.782   29.469  13.068  1.00 75.85  ? 444 GLU B C   1 
ATOM   2428 O O   . GLU B 1 144 ? 0.856   29.174  11.874  1.00 75.21  ? 444 GLU B O   1 
ATOM   2429 C CB  . GLU B 1 144 ? -1.327  30.249  14.196  1.00 88.96  ? 444 GLU B CB  1 
ATOM   2430 C CG  . GLU B 1 144 ? -2.783  29.879  14.461  1.00 97.95  ? 444 GLU B CG  1 
ATOM   2431 C CD  . GLU B 1 144 ? -3.615  31.000  15.060  1.00 107.28 ? 444 GLU B CD  1 
ATOM   2432 O OE1 . GLU B 1 144 ? -3.607  32.110  14.482  1.00 115.61 ? 444 GLU B OE1 1 
ATOM   2433 O OE2 . GLU B 1 144 ? -4.267  30.763  16.105  1.00 110.06 ? 444 GLU B OE2 1 
ATOM   2434 N N   . ILE B 1 145 ? 1.739   30.133  13.735  1.00 71.15  ? 445 ILE B N   1 
ATOM   2435 C CA  . ILE B 1 145 ? 2.889   30.721  13.068  1.00 68.59  ? 445 ILE B CA  1 
ATOM   2436 C C   . ILE B 1 145 ? 3.827   29.626  12.571  1.00 63.81  ? 445 ILE B C   1 
ATOM   2437 O O   . ILE B 1 145 ? 4.318   29.703  11.456  1.00 61.68  ? 445 ILE B O   1 
ATOM   2438 C CB  . ILE B 1 145 ? 3.604   31.706  14.007  1.00 69.23  ? 445 ILE B CB  1 
ATOM   2439 C CG1 . ILE B 1 145 ? 2.736   32.924  14.236  1.00 73.12  ? 445 ILE B CG1 1 
ATOM   2440 C CG2 . ILE B 1 145 ? 4.983   32.102  13.474  1.00 68.58  ? 445 ILE B CG2 1 
ATOM   2441 C CD1 . ILE B 1 145 ? 3.305   33.915  15.223  1.00 73.69  ? 445 ILE B CD1 1 
ATOM   2442 N N   . LEU B 1 146 ? 4.088   28.627  13.412  1.00 64.31  ? 446 LEU B N   1 
ATOM   2443 C CA  . LEU B 1 146 ? 4.992   27.536  13.072  1.00 64.19  ? 446 LEU B CA  1 
ATOM   2444 C C   . LEU B 1 146 ? 4.530   26.846  11.790  1.00 62.61  ? 446 LEU B C   1 
ATOM   2445 O O   . LEU B 1 146 ? 5.309   26.752  10.840  1.00 61.80  ? 446 LEU B O   1 
ATOM   2446 C CB  . LEU B 1 146 ? 5.118   26.556  14.240  1.00 64.69  ? 446 LEU B CB  1 
ATOM   2447 C CG  . LEU B 1 146 ? 5.765   27.072  15.538  1.00 63.53  ? 446 LEU B CG  1 
ATOM   2448 C CD1 . LEU B 1 146 ? 5.674   26.035  16.611  1.00 65.50  ? 446 LEU B CD1 1 
ATOM   2449 C CD2 . LEU B 1 146 ? 7.204   27.440  15.437  1.00 64.85  ? 446 LEU B CD2 1 
ATOM   2450 N N   . PHE B 1 147 ? 3.270   26.399  11.744  1.00 63.14  ? 447 PHE B N   1 
ATOM   2451 C CA  . PHE B 1 147 ? 2.726   25.795  10.530  1.00 65.35  ? 447 PHE B CA  1 
ATOM   2452 C C   . PHE B 1 147 ? 2.771   26.789  9.369   1.00 68.33  ? 447 PHE B C   1 
ATOM   2453 O O   . PHE B 1 147 ? 3.216   26.434  8.280   1.00 70.82  ? 447 PHE B O   1 
ATOM   2454 C CB  . PHE B 1 147 ? 1.304   25.253  10.709  1.00 67.22  ? 447 PHE B CB  1 
ATOM   2455 C CG  . PHE B 1 147 ? 1.302   23.952  11.484  1.00 70.08  ? 447 PHE B CG  1 
ATOM   2456 C CD1 . PHE B 1 147 ? 1.463   22.732  10.830  1.00 76.20  ? 447 PHE B CD1 1 
ATOM   2457 C CD2 . PHE B 1 147 ? 1.208   23.947  12.866  1.00 70.73  ? 447 PHE B CD2 1 
ATOM   2458 C CE1 . PHE B 1 147 ? 1.485   21.541  11.543  1.00 74.27  ? 447 PHE B CE1 1 
ATOM   2459 C CE2 . PHE B 1 147 ? 1.232   22.758  13.576  1.00 72.32  ? 447 PHE B CE2 1 
ATOM   2460 C CZ  . PHE B 1 147 ? 1.372   21.558  12.916  1.00 73.87  ? 447 PHE B CZ  1 
ATOM   2461 N N   . ASP B 1 148 ? 2.303   28.021  9.617   1.00 72.27  ? 448 ASP B N   1 
ATOM   2462 C CA  . ASP B 1 148 ? 2.280   29.074  8.620   1.00 74.37  ? 448 ASP B CA  1 
ATOM   2463 C C   . ASP B 1 148 ? 3.585   29.099  7.842   1.00 70.08  ? 448 ASP B C   1 
ATOM   2464 O O   . ASP B 1 148 ? 3.575   28.997  6.622   1.00 70.70  ? 448 ASP B O   1 
ATOM   2465 C CB  . ASP B 1 148 ? 2.040   30.437  9.246   1.00 83.60  ? 448 ASP B CB  1 
ATOM   2466 C CG  . ASP B 1 148 ? 0.639   30.692  9.786   1.00 96.32  ? 448 ASP B CG  1 
ATOM   2467 O OD1 . ASP B 1 148 ? -0.278  29.911  9.434   1.00 99.27  ? 448 ASP B OD1 1 
ATOM   2468 O OD2 . ASP B 1 148 ? 0.475   31.683  10.546  1.00 108.26 ? 448 ASP B OD2 1 
ATOM   2469 N N   . GLU B 1 149 ? 4.709   29.230  8.546   1.00 65.55  ? 449 GLU B N   1 
ATOM   2470 C CA  . GLU B 1 149 ? 5.988   29.415  7.881   1.00 65.81  ? 449 GLU B CA  1 
ATOM   2471 C C   . GLU B 1 149 ? 6.415   28.135  7.163   1.00 64.32  ? 449 GLU B C   1 
ATOM   2472 O O   . GLU B 1 149 ? 6.887   28.179  6.024   1.00 59.67  ? 449 GLU B O   1 
ATOM   2473 C CB  . GLU B 1 149 ? 7.009   29.875  8.918   1.00 63.99  ? 449 GLU B CB  1 
ATOM   2474 C CG  . GLU B 1 149 ? 6.744   31.295  9.398   1.00 68.33  ? 449 GLU B CG  1 
ATOM   2475 C CD  . GLU B 1 149 ? 6.774   32.270  8.243   1.00 76.36  ? 449 GLU B CD  1 
ATOM   2476 O OE1 . GLU B 1 149 ? 7.841   32.333  7.599   1.00 79.02  ? 449 GLU B OE1 1 
ATOM   2477 O OE2 . GLU B 1 149 ? 5.746   32.917  7.950   1.00 85.08  ? 449 GLU B OE2 1 
ATOM   2478 N N   . VAL B 1 150 ? 6.246   26.996  7.848   1.00 63.77  ? 450 VAL B N   1 
ATOM   2479 C CA  . VAL B 1 150 ? 6.624   25.715  7.281   1.00 60.22  ? 450 VAL B CA  1 
ATOM   2480 C C   . VAL B 1 150 ? 5.867   25.534  5.969   1.00 65.20  ? 450 VAL B C   1 
ATOM   2481 O O   . VAL B 1 150 ? 6.496   25.293  4.937   1.00 65.06  ? 450 VAL B O   1 
ATOM   2482 C CB  . VAL B 1 150 ? 6.419   24.534  8.243   1.00 55.48  ? 450 VAL B CB  1 
ATOM   2483 C CG1 . VAL B 1 150 ? 6.615   23.199  7.545   1.00 55.88  ? 450 VAL B CG1 1 
ATOM   2484 C CG2 . VAL B 1 150 ? 7.379   24.621  9.419   1.00 53.58  ? 450 VAL B CG2 1 
ATOM   2485 N N   . LEU B 1 151 ? 4.535   25.695  6.002   1.00 66.52  ? 451 LEU B N   1 
ATOM   2486 C CA  . LEU B 1 151 ? 3.726   25.495  4.808   1.00 69.34  ? 451 LEU B CA  1 
ATOM   2487 C C   . LEU B 1 151 ? 4.148   26.461  3.704   1.00 73.75  ? 451 LEU B C   1 
ATOM   2488 O O   . LEU B 1 151 ? 4.171   26.092  2.531   1.00 80.70  ? 451 LEU B O   1 
ATOM   2489 C CB  . LEU B 1 151 ? 2.243   25.649  5.112   1.00 72.51  ? 451 LEU B CB  1 
ATOM   2490 C CG  . LEU B 1 151 ? 1.631   24.613  6.056   1.00 76.63  ? 451 LEU B CG  1 
ATOM   2491 C CD1 . LEU B 1 151 ? 0.153   24.492  5.727   1.00 83.17  ? 451 LEU B CD1 1 
ATOM   2492 C CD2 . LEU B 1 151 ? 2.312   23.246  6.009   1.00 77.27  ? 451 LEU B CD2 1 
ATOM   2493 N N   . THR B 1 152 ? 4.466   27.699  4.087   1.00 72.14  ? 452 THR B N   1 
ATOM   2494 C CA  . THR B 1 152 ? 4.878   28.717  3.140   1.00 76.76  ? 452 THR B CA  1 
ATOM   2495 C C   . THR B 1 152 ? 6.078   28.208  2.354   1.00 73.63  ? 452 THR B C   1 
ATOM   2496 O O   . THR B 1 152 ? 6.083   28.264  1.130   1.00 74.09  ? 452 THR B O   1 
ATOM   2497 C CB  . THR B 1 152 ? 5.189   30.010  3.907   1.00 82.84  ? 452 THR B CB  1 
ATOM   2498 O OG1 . THR B 1 152 ? 3.927   30.577  4.250   1.00 83.67  ? 452 THR B OG1 1 
ATOM   2499 C CG2 . THR B 1 152 ? 5.971   31.033  3.100   1.00 86.14  ? 452 THR B CG2 1 
ATOM   2500 N N   . PHE B 1 153 ? 7.092   27.743  3.091   1.00 73.28  ? 453 PHE B N   1 
ATOM   2501 C CA  . PHE B 1 153 ? 8.330   27.224  2.535   1.00 76.07  ? 453 PHE B CA  1 
ATOM   2502 C C   . PHE B 1 153 ? 8.054   26.077  1.568   1.00 80.18  ? 453 PHE B C   1 
ATOM   2503 O O   . PHE B 1 153 ? 8.662   25.993  0.504   1.00 86.53  ? 453 PHE B O   1 
ATOM   2504 C CB  . PHE B 1 153 ? 9.189   26.740  3.703   1.00 73.87  ? 453 PHE B CB  1 
ATOM   2505 C CG  . PHE B 1 153 ? 10.458  26.036  3.261   1.00 72.17  ? 453 PHE B CG  1 
ATOM   2506 C CD1 . PHE B 1 153 ? 10.424  24.706  2.870   1.00 73.87  ? 453 PHE B CD1 1 
ATOM   2507 C CD2 . PHE B 1 153 ? 11.669  26.715  3.209   1.00 71.77  ? 453 PHE B CD2 1 
ATOM   2508 C CE1 . PHE B 1 153 ? 11.576  24.063  2.456   1.00 76.79  ? 453 PHE B CE1 1 
ATOM   2509 C CE2 . PHE B 1 153 ? 12.816  26.079  2.783   1.00 73.90  ? 453 PHE B CE2 1 
ATOM   2510 C CZ  . PHE B 1 153 ? 12.767  24.753  2.405   1.00 77.36  ? 453 PHE B CZ  1 
ATOM   2511 N N   . ALA B 1 154 ? 7.135   25.188  1.948   1.00 82.11  ? 454 ALA B N   1 
ATOM   2512 C CA  . ALA B 1 154 ? 6.772   24.052  1.117   1.00 86.01  ? 454 ALA B CA  1 
ATOM   2513 C C   . ALA B 1 154 ? 6.289   24.505  -0.260  1.00 94.89  ? 454 ALA B C   1 
ATOM   2514 O O   . ALA B 1 154 ? 6.568   23.820  -1.247  1.00 108.48 ? 454 ALA B O   1 
ATOM   2515 C CB  . ALA B 1 154 ? 5.732   23.205  1.818   1.00 87.06  ? 454 ALA B CB  1 
ATOM   2516 N N   . LYS B 1 155 ? 5.582   25.648  -0.320  1.00 99.48  ? 455 LYS B N   1 
ATOM   2517 C CA  . LYS B 1 155 ? 5.076   26.201  -1.573  1.00 100.69 ? 455 LYS B CA  1 
ATOM   2518 C C   . LYS B 1 155 ? 6.169   26.982  -2.302  1.00 96.07  ? 455 LYS B C   1 
ATOM   2519 O O   . LYS B 1 155 ? 6.294   26.883  -3.517  1.00 97.03  ? 455 LYS B O   1 
ATOM   2520 C CB  . LYS B 1 155 ? 3.815   27.038  -1.335  1.00 102.71 ? 455 LYS B CB  1 
ATOM   2521 C CG  . LYS B 1 155 ? 2.653   26.167  -0.847  1.00 104.88 ? 455 LYS B CG  1 
ATOM   2522 C CD  . LYS B 1 155 ? 1.238   26.587  -1.239  1.00 109.11 ? 455 LYS B CD  1 
ATOM   2523 C CE  . LYS B 1 155 ? 0.209   25.541  -0.878  1.00 105.68 ? 455 LYS B CE  1 
ATOM   2524 N NZ  . LYS B 1 155 ? 0.336   24.289  -1.632  1.00 103.44 ? 455 LYS B NZ  1 
ATOM   2525 N N   . ASP B 1 156 ? 6.989   27.714  -1.551  1.00 91.11  ? 456 ASP B N   1 
ATOM   2526 C CA  . ASP B 1 156 ? 7.899   28.684  -2.134  1.00 97.05  ? 456 ASP B CA  1 
ATOM   2527 C C   . ASP B 1 156 ? 9.257   28.058  -2.463  1.00 96.24  ? 456 ASP B C   1 
ATOM   2528 O O   . ASP B 1 156 ? 10.083  28.689  -3.120  1.00 103.28 ? 456 ASP B O   1 
ATOM   2529 C CB  . ASP B 1 156 ? 7.993   29.922  -1.252  1.00 98.64  ? 456 ASP B CB  1 
ATOM   2530 C CG  . ASP B 1 156 ? 6.714   30.753  -1.159  1.00 102.08 ? 456 ASP B CG  1 
ATOM   2531 O OD1 . ASP B 1 156 ? 5.712   30.386  -1.818  1.00 101.48 ? 456 ASP B OD1 1 
ATOM   2532 O OD2 . ASP B 1 156 ? 6.717   31.764  -0.424  1.00 103.30 ? 456 ASP B OD2 1 
ATOM   2533 N N   . HIS B 1 157 ? 9.514   26.829  -2.011  1.00 91.65  ? 457 HIS B N   1 
ATOM   2534 C CA  . HIS B 1 157 ? 10.753  26.160  -2.379  1.00 88.79  ? 457 HIS B CA  1 
ATOM   2535 C C   . HIS B 1 157 ? 10.488  24.659  -2.452  1.00 86.81  ? 457 HIS B C   1 
ATOM   2536 O O   . HIS B 1 157 ? 10.923  23.902  -1.583  1.00 85.32  ? 457 HIS B O   1 
ATOM   2537 C CB  . HIS B 1 157 ? 11.894  26.534  -1.425  1.00 85.01  ? 457 HIS B CB  1 
ATOM   2538 C CG  . HIS B 1 157 ? 12.000  27.974  -1.004  1.00 86.87  ? 457 HIS B CG  1 
ATOM   2539 N ND1 . HIS B 1 157 ? 11.317  28.503  0.076   1.00 84.41  ? 457 HIS B ND1 1 
ATOM   2540 C CD2 . HIS B 1 157 ? 12.757  28.974  -1.475  1.00 89.68  ? 457 HIS B CD2 1 
ATOM   2541 C CE1 . HIS B 1 157 ? 11.654  29.772  0.243   1.00 85.67  ? 457 HIS B CE1 1 
ATOM   2542 N NE2 . HIS B 1 157 ? 12.532  30.076  -0.685  1.00 90.77  ? 457 HIS B NE2 1 
ATOM   2543 N N   . VAL B 1 158 ? 9.787   24.262  -3.524  1.00 94.03  ? 458 VAL B N   1 
ATOM   2544 C CA  . VAL B 1 158 ? 9.277   22.909  -3.720  1.00 93.99  ? 458 VAL B CA  1 
ATOM   2545 C C   . VAL B 1 158 ? 10.391  21.999  -4.248  1.00 92.92  ? 458 VAL B C   1 
ATOM   2546 O O   . VAL B 1 158 ? 10.245  20.775  -4.246  1.00 88.54  ? 458 VAL B O   1 
ATOM   2547 C CB  . VAL B 1 158 ? 8.059   22.908  -4.671  1.00 96.83  ? 458 VAL B CB  1 
ATOM   2548 C CG1 . VAL B 1 158 ? 7.378   21.540  -4.749  1.00 93.32  ? 458 VAL B CG1 1 
ATOM   2549 C CG2 . VAL B 1 158 ? 7.046   23.992  -4.313  1.00 98.19  ? 458 VAL B CG2 1 
ATOM   2550 N N   . LYS B 1 159 ? 11.511  22.601  -4.675  1.00 95.96  ? 459 LYS B N   1 
ATOM   2551 C CA  . LYS B 1 159 ? 12.676  21.842  -5.092  1.00 95.65  ? 459 LYS B CA  1 
ATOM   2552 C C   . LYS B 1 159 ? 13.442  21.237  -3.911  1.00 90.23  ? 459 LYS B C   1 
ATOM   2553 O O   . LYS B 1 159 ? 14.303  20.396  -4.147  1.00 88.73  ? 459 LYS B O   1 
ATOM   2554 C CB  . LYS B 1 159 ? 13.614  22.744  -5.893  1.00 99.32  ? 459 LYS B CB  1 
ATOM   2555 C CG  . LYS B 1 159 ? 13.045  23.208  -7.212  1.00 108.81 ? 459 LYS B CG  1 
ATOM   2556 C CD  . LYS B 1 159 ? 14.126  23.607  -8.215  1.00 116.05 ? 459 LYS B CD  1 
ATOM   2557 C CE  . LYS B 1 159 ? 13.589  23.679  -9.613  1.00 125.47 ? 459 LYS B CE  1 
ATOM   2558 N NZ  . LYS B 1 159 ? 14.632  23.788  -10.638 1.00 130.28 ? 459 LYS B NZ  1 
ATOM   2559 N N   . HIS B 1 160 ? 13.156  21.664  -2.665  1.00 84.53  ? 460 HIS B N   1 
ATOM   2560 C CA  . HIS B 1 160 ? 13.944  21.261  -1.502  1.00 79.04  ? 460 HIS B CA  1 
ATOM   2561 C C   . HIS B 1 160 ? 13.166  20.266  -0.643  1.00 78.79  ? 460 HIS B C   1 
ATOM   2562 O O   . HIS B 1 160 ? 12.099  20.617  -0.123  1.00 72.76  ? 460 HIS B O   1 
ATOM   2563 C CB  . HIS B 1 160 ? 14.347  22.465  -0.639  1.00 77.96  ? 460 HIS B CB  1 
ATOM   2564 C CG  . HIS B 1 160 ? 15.394  22.174  0.401   1.00 73.57  ? 460 HIS B CG  1 
ATOM   2565 N ND1 . HIS B 1 160 ? 16.744  22.209  0.110   1.00 71.74  ? 460 HIS B ND1 1 
ATOM   2566 C CD2 . HIS B 1 160 ? 15.310  21.860  1.709   1.00 68.39  ? 460 HIS B CD2 1 
ATOM   2567 C CE1 . HIS B 1 160 ? 17.443  21.907  1.190   1.00 67.60  ? 460 HIS B CE1 1 
ATOM   2568 N NE2 . HIS B 1 160 ? 16.593  21.707  2.180   1.00 67.33  ? 460 HIS B NE2 1 
ATOM   2569 N N   . GLN B 1 161 ? 13.732  19.040  -0.529  1.00 78.62  ? 461 GLN B N   1 
ATOM   2570 C CA  . GLN B 1 161 ? 13.201  17.974  0.306   1.00 69.08  ? 461 GLN B CA  1 
ATOM   2571 C C   . GLN B 1 161 ? 13.585  18.269  1.740   1.00 60.21  ? 461 GLN B C   1 
ATOM   2572 O O   . GLN B 1 161 ? 14.770  18.453  2.023   1.00 59.34  ? 461 GLN B O   1 
ATOM   2573 C CB  . GLN B 1 161 ? 13.830  16.593  0.135   1.00 69.30  ? 461 GLN B CB  1 
ATOM   2574 C CG  . GLN B 1 161 ? 13.077  15.670  -0.805  1.00 75.24  ? 461 GLN B CG  1 
ATOM   2575 C CD  . GLN B 1 161 ? 13.705  14.297  -0.851  1.00 78.69  ? 461 GLN B CD  1 
ATOM   2576 O OE1 . GLN B 1 161 ? 14.933  14.141  -0.861  1.00 86.93  ? 461 GLN B OE1 1 
ATOM   2577 N NE2 . GLN B 1 161 ? 12.860  13.284  -0.865  1.00 79.47  ? 461 GLN B NE2 1 
ATOM   2578 N N   . LEU B 1 162 ? 12.586  18.244  2.620   1.00 53.72  ? 462 LEU B N   1 
ATOM   2579 C CA  . LEU B 1 162 ? 12.807  18.578  4.011   1.00 51.99  ? 462 LEU B CA  1 
ATOM   2580 C C   . LEU B 1 162 ? 11.888  17.730  4.867   1.00 50.53  ? 462 LEU B C   1 
ATOM   2581 O O   . LEU B 1 162 ? 10.714  17.564  4.533   1.00 49.95  ? 462 LEU B O   1 
ATOM   2582 C CB  . LEU B 1 162 ? 12.526  20.062  4.270   1.00 56.06  ? 462 LEU B CB  1 
ATOM   2583 C CG  . LEU B 1 162 ? 13.045  20.642  5.591   1.00 53.21  ? 462 LEU B CG  1 
ATOM   2584 C CD1 . LEU B 1 162 ? 14.557  20.587  5.726   1.00 49.65  ? 462 LEU B CD1 1 
ATOM   2585 C CD2 . LEU B 1 162 ? 12.553  22.075  5.678   1.00 57.69  ? 462 LEU B CD2 1 
ATOM   2586 N N   . THR B 1 163 ? 12.441  17.251  5.986   1.00 50.74  ? 463 THR B N   1 
ATOM   2587 C CA  . THR B 1 163 ? 11.635  16.669  7.045   1.00 52.63  ? 463 THR B CA  1 
ATOM   2588 C C   . THR B 1 163 ? 11.665  17.647  8.218   1.00 49.33  ? 463 THR B C   1 
ATOM   2589 O O   . THR B 1 163 ? 12.739  18.002  8.718   1.00 45.08  ? 463 THR B O   1 
ATOM   2590 C CB  . THR B 1 163 ? 12.123  15.273  7.466   1.00 50.88  ? 463 THR B CB  1 
ATOM   2591 O OG1 . THR B 1 163 ? 12.430  14.459  6.337   1.00 50.05  ? 463 THR B OG1 1 
ATOM   2592 C CG2 . THR B 1 163 ? 11.074  14.571  8.310   1.00 50.52  ? 463 THR B CG2 1 
ATOM   2593 N N   . VAL B 1 164 ? 10.471  18.066  8.637   1.00 49.85  ? 464 VAL B N   1 
ATOM   2594 C CA  . VAL B 1 164 ? 10.316  19.001  9.735   1.00 50.96  ? 464 VAL B CA  1 
ATOM   2595 C C   . VAL B 1 164 ? 9.558   18.311  10.865  1.00 51.81  ? 464 VAL B C   1 
ATOM   2596 O O   . VAL B 1 164 ? 8.440   17.839  10.677  1.00 51.69  ? 464 VAL B O   1 
ATOM   2597 C CB  . VAL B 1 164 ? 9.592   20.278  9.281   1.00 51.82  ? 464 VAL B CB  1 
ATOM   2598 C CG1 . VAL B 1 164 ? 9.292   21.212  10.449  1.00 53.50  ? 464 VAL B CG1 1 
ATOM   2599 C CG2 . VAL B 1 164 ? 10.377  21.000  8.189   1.00 54.33  ? 464 VAL B CG2 1 
ATOM   2600 N N   . LYS B 1 165 ? 10.182  18.271  12.045  1.00 49.83  ? 465 LYS B N   1 
ATOM   2601 C CA  . LYS B 1 165 ? 9.520   17.785  13.233  1.00 51.35  ? 465 LYS B CA  1 
ATOM   2602 C C   . LYS B 1 165 ? 9.266   18.965  14.148  1.00 50.32  ? 465 LYS B C   1 
ATOM   2603 O O   . LYS B 1 165 ? 10.162  19.786  14.322  1.00 51.96  ? 465 LYS B O   1 
ATOM   2604 C CB  . LYS B 1 165 ? 10.411  16.735  13.900  1.00 56.03  ? 465 LYS B CB  1 
ATOM   2605 C CG  . LYS B 1 165 ? 10.518  15.462  13.060  1.00 64.85  ? 465 LYS B CG  1 
ATOM   2606 C CD  . LYS B 1 165 ? 11.119  14.200  13.672  1.00 65.40  ? 465 LYS B CD  1 
ATOM   2607 C CE  . LYS B 1 165 ? 11.278  13.206  12.562  1.00 68.81  ? 465 LYS B CE  1 
ATOM   2608 N NZ  . LYS B 1 165 ? 11.676  11.863  12.995  1.00 75.08  ? 465 LYS B NZ  1 
ATOM   2609 N N   . PHE B 1 166 ? 8.048   19.044  14.690  1.00 48.60  ? 466 PHE B N   1 
ATOM   2610 C CA  . PHE B 1 166 ? 7.790   19.845  15.872  1.00 48.56  ? 466 PHE B CA  1 
ATOM   2611 C C   . PHE B 1 166 ? 7.810   18.906  17.075  1.00 49.94  ? 466 PHE B C   1 
ATOM   2612 O O   . PHE B 1 166 ? 6.853   18.169  17.301  1.00 48.15  ? 466 PHE B O   1 
ATOM   2613 C CB  . PHE B 1 166 ? 6.449   20.588  15.814  1.00 48.63  ? 466 PHE B CB  1 
ATOM   2614 C CG  . PHE B 1 166 ? 6.247   21.501  14.612  1.00 46.21  ? 466 PHE B CG  1 
ATOM   2615 C CD1 . PHE B 1 166 ? 7.290   22.273  14.114  1.00 43.73  ? 466 PHE B CD1 1 
ATOM   2616 C CD2 . PHE B 1 166 ? 5.007   21.581  13.983  1.00 48.07  ? 466 PHE B CD2 1 
ATOM   2617 C CE1 . PHE B 1 166 ? 7.105   23.080  13.002  1.00 44.07  ? 466 PHE B CE1 1 
ATOM   2618 C CE2 . PHE B 1 166 ? 4.817   22.409  12.889  1.00 48.60  ? 466 PHE B CE2 1 
ATOM   2619 C CZ  . PHE B 1 166 ? 5.872   23.146  12.390  1.00 46.59  ? 466 PHE B CZ  1 
ATOM   2620 N N   . VAL B 1 167 ? 8.873   19.018  17.873  1.00 51.23  ? 467 VAL B N   1 
ATOM   2621 C CA  . VAL B 1 167 ? 9.053   18.252  19.095  1.00 53.94  ? 467 VAL B CA  1 
ATOM   2622 C C   . VAL B 1 167 ? 8.348   18.925  20.283  1.00 56.16  ? 467 VAL B C   1 
ATOM   2623 O O   . VAL B 1 167 ? 8.769   19.988  20.769  1.00 56.47  ? 467 VAL B O   1 
ATOM   2624 C CB  . VAL B 1 167 ? 10.581  18.171  19.296  1.00 55.12  ? 467 VAL B CB  1 
ATOM   2625 C CG1 . VAL B 1 167 ? 10.972  17.317  20.501  1.00 56.29  ? 467 VAL B CG1 1 
ATOM   2626 C CG2 . VAL B 1 167 ? 11.288  17.668  18.042  1.00 55.82  ? 467 VAL B CG2 1 
ATOM   2627 N N   . ILE B 1 168 ? 7.284   18.276  20.766  1.00 55.27  ? 468 ILE B N   1 
ATOM   2628 C CA  . ILE B 1 168 ? 6.527   18.723  21.929  1.00 57.53  ? 468 ILE B CA  1 
ATOM   2629 C C   . ILE B 1 168 ? 6.994   17.948  23.160  1.00 61.69  ? 468 ILE B C   1 
ATOM   2630 O O   . ILE B 1 168 ? 7.120   16.732  23.115  1.00 64.20  ? 468 ILE B O   1 
ATOM   2631 C CB  . ILE B 1 168 ? 5.016   18.515  21.720  1.00 55.82  ? 468 ILE B CB  1 
ATOM   2632 C CG1 . ILE B 1 168 ? 4.535   18.958  20.338  1.00 52.93  ? 468 ILE B CG1 1 
ATOM   2633 C CG2 . ILE B 1 168 ? 4.240   19.194  22.841  1.00 58.91  ? 468 ILE B CG2 1 
ATOM   2634 C CD1 . ILE B 1 168 ? 4.851   20.404  20.022  1.00 53.69  ? 468 ILE B CD1 1 
ATOM   2635 N N   . PHE B 1 169 ? 7.207   18.623  24.290  1.00 64.27  ? 469 PHE B N   1 
ATOM   2636 C CA  . PHE B 1 169 ? 7.726   17.919  25.447  1.00 65.70  ? 469 PHE B CA  1 
ATOM   2637 C C   . PHE B 1 169 ? 6.626   16.986  25.940  1.00 70.42  ? 469 PHE B C   1 
ATOM   2638 O O   . PHE B 1 169 ? 5.450   17.357  25.899  1.00 73.28  ? 469 PHE B O   1 
ATOM   2639 C CB  . PHE B 1 169 ? 8.207   18.902  26.514  1.00 70.88  ? 469 PHE B CB  1 
ATOM   2640 C CG  . PHE B 1 169 ? 9.000   18.272  27.655  1.00 78.23  ? 469 PHE B CG  1 
ATOM   2641 C CD1 . PHE B 1 169 ? 10.300  17.808  27.457  1.00 80.05  ? 469 PHE B CD1 1 
ATOM   2642 C CD2 . PHE B 1 169 ? 8.457   18.151  28.933  1.00 84.00  ? 469 PHE B CD2 1 
ATOM   2643 C CE1 . PHE B 1 169 ? 11.023  17.222  28.497  1.00 81.93  ? 469 PHE B CE1 1 
ATOM   2644 C CE2 . PHE B 1 169 ? 9.176   17.553  29.961  1.00 85.64  ? 469 PHE B CE2 1 
ATOM   2645 C CZ  . PHE B 1 169 ? 10.458  17.092  29.743  1.00 84.01  ? 469 PHE B CZ  1 
ATOM   2646 N N   . PRO B 1 170 ? 6.964   15.749  26.386  1.00 71.42  ? 470 PRO B N   1 
ATOM   2647 C CA  . PRO B 1 170 ? 5.965   14.796  26.877  1.00 76.01  ? 470 PRO B CA  1 
ATOM   2648 C C   . PRO B 1 170 ? 4.940   15.305  27.896  1.00 80.29  ? 470 PRO B C   1 
ATOM   2649 O O   . PRO B 1 170 ? 3.753   15.042  27.718  1.00 80.03  ? 470 PRO B O   1 
ATOM   2650 C CB  . PRO B 1 170 ? 6.857   13.688  27.461  1.00 77.64  ? 470 PRO B CB  1 
ATOM   2651 C CG  . PRO B 1 170 ? 8.081   13.706  26.576  1.00 72.40  ? 470 PRO B CG  1 
ATOM   2652 C CD  . PRO B 1 170 ? 8.323   15.183  26.401  1.00 69.89  ? 470 PRO B CD  1 
ATOM   2653 N N   . THR B 1 171 ? 5.368   16.031  28.946  1.00 81.61  ? 471 THR B N   1 
ATOM   2654 C CA  . THR B 1 171 ? 4.430   16.464  29.981  1.00 86.41  ? 471 THR B CA  1 
ATOM   2655 C C   . THR B 1 171 ? 3.517   17.584  29.476  1.00 87.39  ? 471 THR B C   1 
ATOM   2656 O O   . THR B 1 171 ? 2.433   17.738  30.024  1.00 94.91  ? 471 THR B O   1 
ATOM   2657 C CB  . THR B 1 171 ? 5.123   16.882  31.281  1.00 86.72  ? 471 THR B CB  1 
ATOM   2658 O OG1 . THR B 1 171 ? 5.992   17.960  30.956  1.00 84.41  ? 471 THR B OG1 1 
ATOM   2659 C CG2 . THR B 1 171 ? 5.876   15.745  31.952  1.00 86.90  ? 471 THR B CG2 1 
ATOM   2660 N N   . ASP B 1 172 ? 3.949   18.358  28.462  1.00 84.10  ? 472 ASP B N   1 
ATOM   2661 C CA  . ASP B 1 172 ? 3.152   19.438  27.888  1.00 82.83  ? 472 ASP B CA  1 
ATOM   2662 C C   . ASP B 1 172 ? 2.048   18.884  26.988  1.00 81.17  ? 472 ASP B C   1 
ATOM   2663 O O   . ASP B 1 172 ? 2.105   19.003  25.772  1.00 77.65  ? 472 ASP B O   1 
ATOM   2664 C CB  . ASP B 1 172 ? 3.983   20.367  27.014  1.00 82.73  ? 472 ASP B CB  1 
ATOM   2665 C CG  . ASP B 1 172 ? 5.095   21.162  27.685  1.00 81.08  ? 472 ASP B CG  1 
ATOM   2666 O OD1 . ASP B 1 172 ? 5.247   21.029  28.911  1.00 83.65  ? 472 ASP B OD1 1 
ATOM   2667 O OD2 . ASP B 1 172 ? 5.802   21.898  26.961  1.00 75.18  ? 472 ASP B OD2 1 
ATOM   2668 N N   . LEU B 1 173 ? 1.012   18.304  27.588  1.00 84.28  ? 473 LEU B N   1 
ATOM   2669 C CA  . LEU B 1 173 ? -0.054  17.677  26.827  1.00 87.29  ? 473 LEU B CA  1 
ATOM   2670 C C   . LEU B 1 173 ? -0.866  18.742  26.088  1.00 87.71  ? 473 LEU B C   1 
ATOM   2671 O O   . LEU B 1 173 ? -1.377  18.474  25.006  1.00 84.21  ? 473 LEU B O   1 
ATOM   2672 C CB  . LEU B 1 173 ? -0.955  16.828  27.730  1.00 96.07  ? 473 LEU B CB  1 
ATOM   2673 C CG  . LEU B 1 173 ? -0.451  15.433  28.132  1.00 98.66  ? 473 LEU B CG  1 
ATOM   2674 C CD1 . LEU B 1 173 ? 0.975   15.484  28.648  1.00 96.04  ? 473 LEU B CD1 1 
ATOM   2675 C CD2 . LEU B 1 173 ? -1.363  14.792  29.186  1.00 103.83 ? 473 LEU B CD2 1 
ATOM   2676 N N   . GLU B 1 174 ? -1.012  19.938  26.680  1.00 92.90  ? 474 GLU B N   1 
ATOM   2677 C CA  . GLU B 1 174 ? -1.901  20.953  26.129  1.00 93.79  ? 474 GLU B CA  1 
ATOM   2678 C C   . GLU B 1 174 ? -1.319  21.537  24.842  1.00 87.29  ? 474 GLU B C   1 
ATOM   2679 O O   . GLU B 1 174 ? -2.039  21.712  23.859  1.00 83.67  ? 474 GLU B O   1 
ATOM   2680 C CB  . GLU B 1 174 ? -2.236  22.001  27.193  1.00 98.27  ? 474 GLU B CB  1 
ATOM   2681 C CG  . GLU B 1 174 ? -3.217  21.488  28.245  1.00 103.75 ? 474 GLU B CG  1 
ATOM   2682 C CD  . GLU B 1 174 ? -4.656  21.303  27.762  1.00 107.47 ? 474 GLU B CD  1 
ATOM   2683 O OE1 . GLU B 1 174 ? -5.315  22.330  27.525  1.00 109.28 ? 474 GLU B OE1 1 
ATOM   2684 O OE2 . GLU B 1 174 ? -5.136  20.159  27.600  1.00 107.38 ? 474 GLU B OE2 1 
ATOM   2685 N N   . ILE B 1 175 ? -0.012  21.820  24.858  1.00 83.86  ? 475 ILE B N   1 
ATOM   2686 C CA  . ILE B 1 175 ? 0.704   22.316  23.688  1.00 79.15  ? 475 ILE B CA  1 
ATOM   2687 C C   . ILE B 1 175 ? 0.538   21.312  22.548  1.00 76.53  ? 475 ILE B C   1 
ATOM   2688 O O   . ILE B 1 175 ? 0.301   21.690  21.404  1.00 75.91  ? 475 ILE B O   1 
ATOM   2689 C CB  . ILE B 1 175 ? 2.181   22.600  24.047  1.00 74.98  ? 475 ILE B CB  1 
ATOM   2690 C CG1 . ILE B 1 175 ? 2.291   23.761  25.055  1.00 75.07  ? 475 ILE B CG1 1 
ATOM   2691 C CG2 . ILE B 1 175 ? 3.023   22.879  22.806  1.00 70.99  ? 475 ILE B CG2 1 
ATOM   2692 C CD1 . ILE B 1 175 ? 3.499   23.695  25.970  1.00 74.18  ? 475 ILE B CD1 1 
ATOM   2693 N N   . TYR B 1 176 ? 0.624   20.023  22.887  1.00 78.54  ? 476 TYR B N   1 
ATOM   2694 C CA  . TYR B 1 176 ? 0.408   18.933  21.941  1.00 77.12  ? 476 TYR B CA  1 
ATOM   2695 C C   . TYR B 1 176 ? -0.995  19.005  21.323  1.00 77.25  ? 476 TYR B C   1 
ATOM   2696 O O   . TYR B 1 176 ? -1.165  18.848  20.111  1.00 71.11  ? 476 TYR B O   1 
ATOM   2697 C CB  . TYR B 1 176 ? 0.666   17.602  22.665  1.00 79.41  ? 476 TYR B CB  1 
ATOM   2698 C CG  . TYR B 1 176 ? 0.471   16.417  21.736  1.00 81.14  ? 476 TYR B CG  1 
ATOM   2699 C CD1 . TYR B 1 176 ? 1.475   16.062  20.851  1.00 78.97  ? 476 TYR B CD1 1 
ATOM   2700 C CD2 . TYR B 1 176 ? -0.730  15.719  21.678  1.00 85.66  ? 476 TYR B CD2 1 
ATOM   2701 C CE1 . TYR B 1 176 ? 1.313   15.019  19.961  1.00 81.41  ? 476 TYR B CE1 1 
ATOM   2702 C CE2 . TYR B 1 176 ? -0.904  14.665  20.796  1.00 89.00  ? 476 TYR B CE2 1 
ATOM   2703 C CZ  . TYR B 1 176 ? 0.124   14.316  19.934  1.00 87.44  ? 476 TYR B CZ  1 
ATOM   2704 O OH  . TYR B 1 176 ? 0.025   13.310  19.017  1.00 91.83  ? 476 TYR B OH  1 
ATOM   2705 N N   . LYS B 1 177 ? -2.008  19.230  22.173  1.00 83.67  ? 477 LYS B N   1 
ATOM   2706 C CA  . LYS B 1 177 ? -3.395  19.248  21.734  1.00 87.38  ? 477 LYS B CA  1 
ATOM   2707 C C   . LYS B 1 177 ? -3.587  20.369  20.712  1.00 84.98  ? 477 LYS B C   1 
ATOM   2708 O O   . LYS B 1 177 ? -4.424  20.257  19.821  1.00 86.99  ? 477 LYS B O   1 
ATOM   2709 C CB  . LYS B 1 177 ? -4.388  19.363  22.903  1.00 92.72  ? 477 LYS B CB  1 
ATOM   2710 C CG  . LYS B 1 177 ? -4.660  18.086  23.710  1.00 96.67  ? 477 LYS B CG  1 
ATOM   2711 C CD  . LYS B 1 177 ? -5.936  18.098  24.565  1.00 103.33 ? 477 LYS B CD  1 
ATOM   2712 C CE  . LYS B 1 177 ? -6.296  16.725  25.110  1.00 106.85 ? 477 LYS B CE  1 
ATOM   2713 N NZ  . LYS B 1 177 ? -7.551  16.625  25.868  1.00 112.44 ? 477 LYS B NZ  1 
ATOM   2714 N N   . ALA B 1 178 ? -2.794  21.439  20.829  1.00 80.83  ? 478 ALA B N   1 
ATOM   2715 C CA  . ALA B 1 178 ? -2.973  22.599  19.976  1.00 80.87  ? 478 ALA B CA  1 
ATOM   2716 C C   . ALA B 1 178 ? -2.341  22.348  18.612  1.00 76.69  ? 478 ALA B C   1 
ATOM   2717 O O   . ALA B 1 178 ? -2.915  22.687  17.576  1.00 79.00  ? 478 ALA B O   1 
ATOM   2718 C CB  . ALA B 1 178 ? -2.405  23.833  20.650  1.00 80.65  ? 478 ALA B CB  1 
ATOM   2719 N N   . PHE B 1 179 ? -1.158  21.737  18.615  1.00 73.40  ? 479 PHE B N   1 
ATOM   2720 C CA  . PHE B 1 179 ? -0.466  21.465  17.369  1.00 71.54  ? 479 PHE B CA  1 
ATOM   2721 C C   . PHE B 1 179 ? -1.240  20.437  16.545  1.00 75.07  ? 479 PHE B C   1 
ATOM   2722 O O   . PHE B 1 179 ? -1.335  20.576  15.328  1.00 74.12  ? 479 PHE B O   1 
ATOM   2723 C CB  . PHE B 1 179 ? 0.966   21.036  17.675  1.00 67.96  ? 479 PHE B CB  1 
ATOM   2724 C CG  . PHE B 1 179 ? 1.890   22.219  17.933  1.00 66.84  ? 479 PHE B CG  1 
ATOM   2725 C CD1 . PHE B 1 179 ? 1.588   23.167  18.908  1.00 69.83  ? 479 PHE B CD1 1 
ATOM   2726 C CD2 . PHE B 1 179 ? 3.023   22.413  17.152  1.00 60.35  ? 479 PHE B CD2 1 
ATOM   2727 C CE1 . PHE B 1 179 ? 2.426   24.248  19.126  1.00 68.45  ? 479 PHE B CE1 1 
ATOM   2728 C CE2 . PHE B 1 179 ? 3.851   23.493  17.371  1.00 59.67  ? 479 PHE B CE2 1 
ATOM   2729 C CZ  . PHE B 1 179 ? 3.564   24.400  18.366  1.00 63.63  ? 479 PHE B CZ  1 
ATOM   2730 N N   . SER B 1 180 ? -1.792  19.406  17.200  1.00 78.49  ? 480 SER B N   1 
ATOM   2731 C CA  . SER B 1 180 ? -2.634  18.453  16.497  1.00 82.38  ? 480 SER B CA  1 
ATOM   2732 C C   . SER B 1 180 ? -3.778  19.192  15.805  1.00 83.08  ? 480 SER B C   1 
ATOM   2733 O O   . SER B 1 180 ? -4.002  19.010  14.612  1.00 87.57  ? 480 SER B O   1 
ATOM   2734 C CB  . SER B 1 180 ? -3.145  17.385  17.415  1.00 86.33  ? 480 SER B CB  1 
ATOM   2735 O OG  . SER B 1 180 ? -3.869  17.977  18.479  1.00 96.44  ? 480 SER B OG  1 
ATOM   2736 N N   . SER B 1 181 ? -4.461  20.059  16.556  1.00 83.31  ? 481 SER B N   1 
ATOM   2737 C CA  . SER B 1 181 ? -5.635  20.758  16.060  1.00 89.06  ? 481 SER B CA  1 
ATOM   2738 C C   . SER B 1 181 ? -5.269  21.684  14.902  1.00 85.53  ? 481 SER B C   1 
ATOM   2739 O O   . SER B 1 181 ? -6.030  21.805  13.940  1.00 89.47  ? 481 SER B O   1 
ATOM   2740 C CB  . SER B 1 181 ? -6.324  21.518  17.171  1.00 95.20  ? 481 SER B CB  1 
ATOM   2741 O OG  . SER B 1 181 ? -7.680  21.803  16.844  1.00 103.96 ? 481 SER B OG  1 
ATOM   2742 N N   . GLU B 1 182 ? -4.117  22.353  15.010  1.00 80.11  ? 482 GLU B N   1 
ATOM   2743 C CA  . GLU B 1 182 ? -3.695  23.276  13.970  1.00 81.26  ? 482 GLU B CA  1 
ATOM   2744 C C   . GLU B 1 182 ? -3.361  22.464  12.715  1.00 84.89  ? 482 GLU B C   1 
ATOM   2745 O O   . GLU B 1 182 ? -3.713  22.866  11.604  1.00 89.31  ? 482 GLU B O   1 
ATOM   2746 C CB  . GLU B 1 182 ? -2.576  24.180  14.498  1.00 76.40  ? 482 GLU B CB  1 
ATOM   2747 C CG  . GLU B 1 182 ? -1.997  25.143  13.461  1.00 75.82  ? 482 GLU B CG  1 
ATOM   2748 C CD  . GLU B 1 182 ? -2.922  26.190  12.840  1.00 80.40  ? 482 GLU B CD  1 
ATOM   2749 O OE1 . GLU B 1 182 ? -3.956  26.610  13.427  1.00 82.89  ? 482 GLU B OE1 1 
ATOM   2750 O OE2 . GLU B 1 182 ? -2.576  26.587  11.700  1.00 79.39  ? 482 GLU B OE2 1 
ATOM   2751 N N   . MET B 1 183 ? -2.719  21.298  12.899  1.00 82.09  ? 483 MET B N   1 
ATOM   2752 C CA  . MET B 1 183 ? -2.366  20.448  11.776  1.00 78.45  ? 483 MET B CA  1 
ATOM   2753 C C   . MET B 1 183 ? -3.643  19.926  11.115  1.00 81.76  ? 483 MET B C   1 
ATOM   2754 O O   . MET B 1 183 ? -3.817  20.067  9.906   1.00 83.61  ? 483 MET B O   1 
ATOM   2755 C CB  . MET B 1 183 ? -1.451  19.294  12.195  1.00 75.25  ? 483 MET B CB  1 
ATOM   2756 C CG  . MET B 1 183 ? -0.923  18.499  11.000  1.00 74.76  ? 483 MET B CG  1 
ATOM   2757 S SD  . MET B 1 183 ? 0.068   17.081  11.500  1.00 69.84  ? 483 MET B SD  1 
ATOM   2758 C CE  . MET B 1 183 ? 1.711   17.820  11.517  1.00 72.11  ? 483 MET B CE  1 
ATOM   2759 N N   . ALA B 1 184 ? -4.537  19.343  11.916  1.00 85.89  ? 484 ALA B N   1 
ATOM   2760 C CA  . ALA B 1 184 ? -5.865  18.955  11.447  1.00 94.90  ? 484 ALA B CA  1 
ATOM   2761 C C   . ALA B 1 184 ? -6.456  20.048  10.558  1.00 98.86  ? 484 ALA B C   1 
ATOM   2762 O O   . ALA B 1 184 ? -6.684  19.820  9.370   1.00 102.81 ? 484 ALA B O   1 
ATOM   2763 C CB  . ALA B 1 184 ? -6.783  18.651  12.622  1.00 97.75  ? 484 ALA B CB  1 
ATOM   2764 N N   . LYS B 1 185 ? -6.663  21.238  11.140  1.00 100.43 ? 485 LYS B N   1 
ATOM   2765 C CA  . LYS B 1 185 ? -7.226  22.368  10.424  1.00 105.73 ? 485 LYS B CA  1 
ATOM   2766 C C   . LYS B 1 185 ? -6.538  22.569  9.074   1.00 104.56 ? 485 LYS B C   1 
ATOM   2767 O O   . LYS B 1 185 ? -7.212  22.799  8.072   1.00 112.79 ? 485 LYS B O   1 
ATOM   2768 C CB  . LYS B 1 185 ? -7.070  23.653  11.241  1.00 111.09 ? 485 LYS B CB  1 
ATOM   2769 C CG  . LYS B 1 185 ? -8.042  23.882  12.376  1.00 119.68 ? 485 LYS B CG  1 
ATOM   2770 C CD  . LYS B 1 185 ? -7.654  25.106  13.205  1.00 122.36 ? 485 LYS B CD  1 
ATOM   2771 C CE  . LYS B 1 185 ? -8.672  25.488  14.234  1.00 132.33 ? 485 LYS B CE  1 
ATOM   2772 N NZ  . LYS B 1 185 ? -8.899  24.405  15.196  1.00 137.32 ? 485 LYS B NZ  1 
ATOM   2773 N N   . ARG B 1 186 ? -5.202  22.491  9.053   1.00 97.12  ? 486 ARG B N   1 
ATOM   2774 C CA  . ARG B 1 186 ? -4.431  22.860  7.877   1.00 98.63  ? 486 ARG B CA  1 
ATOM   2775 C C   . ARG B 1 186 ? -4.588  21.836  6.762   1.00 99.93  ? 486 ARG B C   1 
ATOM   2776 O O   . ARG B 1 186 ? -4.730  22.202  5.600   1.00 105.28 ? 486 ARG B O   1 
ATOM   2777 C CB  . ARG B 1 186 ? -2.943  22.999  8.203   1.00 94.16  ? 486 ARG B CB  1 
ATOM   2778 C CG  . ARG B 1 186 ? -2.636  24.252  9.007   1.00 97.43  ? 486 ARG B CG  1 
ATOM   2779 C CD  . ARG B 1 186 ? -3.301  25.518  8.456   1.00 103.73 ? 486 ARG B CD  1 
ATOM   2780 N NE  . ARG B 1 186 ? -2.545  26.652  8.992   1.00 105.70 ? 486 ARG B NE  1 
ATOM   2781 C CZ  . ARG B 1 186 ? -1.772  27.454  8.272   1.00 110.77 ? 486 ARG B CZ  1 
ATOM   2782 N NH1 . ARG B 1 186 ? -1.892  27.485  6.955   1.00 116.42 ? 486 ARG B NH1 1 
ATOM   2783 N NH2 . ARG B 1 186 ? -0.910  28.255  8.876   1.00 108.98 ? 486 ARG B NH2 1 
ATOM   2784 N N   . SER B 1 187 ? -4.530  20.556  7.120   1.00 97.53  ? 487 SER B N   1 
ATOM   2785 C CA  . SER B 1 187 ? -4.696  19.487  6.155   1.00 96.94  ? 487 SER B CA  1 
ATOM   2786 C C   . SER B 1 187 ? -6.092  19.546  5.535   1.00 100.05 ? 487 SER B C   1 
ATOM   2787 O O   . SER B 1 187 ? -6.230  19.316  4.338   1.00 103.68 ? 487 SER B O   1 
ATOM   2788 C CB  . SER B 1 187 ? -4.409  18.165  6.795   1.00 97.23  ? 487 SER B CB  1 
ATOM   2789 O OG  . SER B 1 187 ? -4.960  18.143  8.103   1.00 99.73  ? 487 SER B OG  1 
ATOM   2790 N N   . LYS B 1 188 ? -7.121  19.885  6.325   1.00 100.88 ? 488 LYS B N   1 
ATOM   2791 C CA  . LYS B 1 188 ? -8.474  20.026  5.794   1.00 108.29 ? 488 LYS B CA  1 
ATOM   2792 C C   . LYS B 1 188 ? -8.473  21.003  4.613   1.00 110.18 ? 488 LYS B C   1 
ATOM   2793 O O   . LYS B 1 188 ? -9.246  20.832  3.672   1.00 117.47 ? 488 LYS B O   1 
ATOM   2794 C CB  . LYS B 1 188 ? -9.530  20.483  6.817   1.00 111.69 ? 488 LYS B CB  1 
ATOM   2795 C CG  . LYS B 1 188 ? -9.896  19.526  7.966   1.00 116.16 ? 488 LYS B CG  1 
ATOM   2796 C CD  . LYS B 1 188 ? -10.931 20.052  8.956   1.00 114.10 ? 488 LYS B CD  1 
ATOM   2797 C CE  . LYS B 1 188 ? -11.287 19.093  10.052  1.00 111.02 ? 488 LYS B CE  1 
ATOM   2798 N NZ  . LYS B 1 188 ? -12.268 19.668  10.979  1.00 107.66 ? 488 LYS B NZ  1 
ATOM   2799 N N   . MET B 1 189 ? -7.595  21.996  4.676   1.00 106.01 ? 489 MET B N   1 
ATOM   2800 C CA  . MET B 1 189 ? -7.577  23.022  3.612   1.00 108.60 ? 489 MET B CA  1 
ATOM   2801 C C   . MET B 1 189 ? -6.756  22.494  2.440   1.00 108.45 ? 489 MET B C   1 
ATOM   2802 O O   . MET B 1 189 ? -7.243  22.544  1.302   1.00 116.52 ? 489 MET B O   1 
ATOM   2803 C CB  . MET B 1 189 ? -6.944  24.312  4.128   1.00 106.59 ? 489 MET B CB  1 
ATOM   2804 C CG  . MET B 1 189 ? -7.708  24.952  5.263   1.00 107.49 ? 489 MET B CG  1 
ATOM   2805 S SD  . MET B 1 189 ? -9.029  26.006  4.635   1.00 113.30 ? 489 MET B SD  1 
ATOM   2806 C CE  . MET B 1 189 ? -8.295  26.577  3.096   1.00 113.97 ? 489 MET B CE  1 
ATOM   2807 N N   . LEU B 1 190 ? -5.564  21.979  2.725   1.00 102.01 ? 490 LEU B N   1 
ATOM   2808 C CA  . LEU B 1 190 ? -4.694  21.450  1.648   1.00 100.91 ? 490 LEU B CA  1 
ATOM   2809 C C   . LEU B 1 190 ? -5.437  20.306  0.956   1.00 103.55 ? 490 LEU B C   1 
ATOM   2810 O O   . LEU B 1 190 ? -5.107  20.006  -0.206  1.00 105.35 ? 490 LEU B O   1 
ATOM   2811 C CB  . LEU B 1 190 ? -3.365  21.005  2.245   1.00 98.89  ? 490 LEU B CB  1 
ATOM   2812 C CG  . LEU B 1 190 ? -2.508  22.115  2.858   1.00 98.46  ? 490 LEU B CG  1 
ATOM   2813 C CD1 . LEU B 1 190 ? -1.780  21.618  4.091   1.00 94.20  ? 490 LEU B CD1 1 
ATOM   2814 C CD2 . LEU B 1 190 ? -1.526  22.644  1.831   1.00 100.02 ? 490 LEU B CD2 1 
ATOM   2815 N N   . SER B 1 191 ? -6.406  19.703  1.643   1.00 106.32 ? 491 SER B N   1 
ATOM   2816 C CA  . SER B 1 191 ? -7.236  18.650  1.009   1.00 109.73 ? 491 SER B CA  1 
ATOM   2817 C C   . SER B 1 191 ? -7.827  19.198  -0.292  1.00 117.17 ? 491 SER B C   1 
ATOM   2818 O O   . SER B 1 191 ? -7.782  18.484  -1.311  1.00 121.81 ? 491 SER B O   1 
ATOM   2819 C CB  . SER B 1 191 ? -8.320  18.191  1.933   1.00 110.33 ? 491 SER B CB  1 
ATOM   2820 O OG  . SER B 1 191 ? -9.463  19.027  1.834   1.00 115.22 ? 491 SER B OG  1 
ATOM   2821 N N   . LEU B 1 192 ? -8.353  20.420  -0.251  1.00 122.54 ? 492 LEU B N   1 
ATOM   2822 C CA  . LEU B 1 192 ? -8.982  21.022  -1.452  1.00 131.16 ? 492 LEU B CA  1 
ATOM   2823 C C   . LEU B 1 192 ? -7.888  21.571  -2.375  1.00 133.41 ? 492 LEU B C   1 
ATOM   2824 O O   . LEU B 1 192 ? -8.137  21.663  -3.590  1.00 137.26 ? 492 LEU B O   1 
ATOM   2825 C CB  . LEU B 1 192 ? -9.946  22.111  -0.996  1.00 133.60 ? 492 LEU B CB  1 
ATOM   2826 C CG  . LEU B 1 192 ? -11.152 21.634  -0.182  1.00 132.54 ? 492 LEU B CG  1 
ATOM   2827 C CD1 . LEU B 1 192 ? -11.955 22.810  0.336   1.00 136.05 ? 492 LEU B CD1 1 
ATOM   2828 C CD2 . LEU B 1 192 ? -12.025 20.711  -1.009  1.00 134.93 ? 492 LEU B CD2 1 
ATOM   2829 N N   . ASN B 1 193 ? -6.723  21.905  -1.819  1.00 133.14 ? 493 ASN B N   1 
ATOM   2830 C CA  . ASN B 1 193 ? -5.632  22.512  -2.631  1.00 134.94 ? 493 ASN B CA  1 
ATOM   2831 C C   . ASN B 1 193 ? -4.625  21.437  -3.049  1.00 134.35 ? 493 ASN B C   1 
ATOM   2832 O O   . ASN B 1 193 ? -4.971  20.630  -3.934  1.00 131.78 ? 493 ASN B O   1 
ATOM   2833 C CB  . ASN B 1 193 ? -4.948  23.655  -1.892  1.00 132.66 ? 493 ASN B CB  1 
ATOM   2834 C CG  . ASN B 1 193 ? -5.829  24.875  -1.781  1.00 135.52 ? 493 ASN B CG  1 
ATOM   2835 O OD1 . ASN B 1 193 ? -6.753  25.050  -2.581  1.00 144.55 ? 493 ASN B OD1 1 
ATOM   2836 N ND2 . ASN B 1 193 ? -5.563  25.727  -0.801  1.00 130.18 ? 493 ASN B ND2 1 
ATOM   2837 N N   . ASN B 1 194 ? -3.438  21.414  -2.429  1.00 140.55 ? 494 ASN B N   1 
ATOM   2838 C CA  . ASN B 1 194 ? -2.369  20.469  -2.867  1.00 136.47 ? 494 ASN B CA  1 
ATOM   2839 C C   . ASN B 1 194 ? -1.869  19.613  -1.700  1.00 138.52 ? 494 ASN B C   1 
ATOM   2840 O O   . ASN B 1 194 ? -1.671  20.177  -0.603  1.00 144.19 ? 494 ASN B O   1 
ATOM   2841 C CB  . ASN B 1 194 ? -1.224  21.215  -3.540  1.00 131.66 ? 494 ASN B CB  1 
ATOM   2842 C CG  . ASN B 1 194 ? -0.262  20.300  -4.252  1.00 120.35 ? 494 ASN B CG  1 
ATOM   2843 O OD1 . ASN B 1 194 ? -0.664  19.243  -4.749  1.00 118.02 ? 494 ASN B OD1 1 
ATOM   2844 N ND2 . ASN B 1 194 ? 1.004   20.684  -4.297  1.00 115.07 ? 494 ASN B ND2 1 
ATOM   2845 N N   . TYR B 1 195 ? -1.696  18.307  -1.928  1.00 134.55 ? 495 TYR B N   1 
ATOM   2846 C CA  . TYR B 1 195 ? -1.155  17.372  -0.900  1.00 120.59 ? 495 TYR B CA  1 
ATOM   2847 C C   . TYR B 1 195 ? -1.995  17.389  0.372   1.00 111.90 ? 495 TYR B C   1 
ATOM   2848 O O   . TYR B 1 195 ? -3.146  17.854  0.359   1.00 120.01 ? 495 TYR B O   1 
ATOM   2849 C CB  . TYR B 1 195 ? 0.323   17.697  -0.685  1.00 118.84 ? 495 TYR B CB  1 
ATOM   2850 C CG  . TYR B 1 195 ? 1.149   17.423  -1.933  1.00 140.55 ? 495 TYR B CG  1 
ATOM   2851 C CD1 . TYR B 1 195 ? 1.677   16.164  -2.181  1.00 147.86 ? 495 TYR B CD1 1 
ATOM   2852 C CD2 . TYR B 1 195 ? 1.367   18.412  -2.882  1.00 153.88 ? 495 TYR B CD2 1 
ATOM   2853 C CE1 . TYR B 1 195 ? 2.421   15.903  -3.319  1.00 143.43 ? 495 TYR B CE1 1 
ATOM   2854 C CE2 . TYR B 1 195 ? 2.112   18.167  -4.023  1.00 152.19 ? 495 TYR B CE2 1 
ATOM   2855 C CZ  . TYR B 1 195 ? 2.640   16.908  -4.242  1.00 143.72 ? 495 TYR B CZ  1 
ATOM   2856 O OH  . TYR B 1 195 ? 3.371   16.658  -5.367  1.00 135.17 ? 495 TYR B OH  1 
ATOM   2857 N N   . SER B 1 196 ? -1.445  16.826  1.444   1.00 103.68 ? 496 SER B N   1 
ATOM   2858 C CA  . SER B 1 196 ? -2.163  16.782  2.742   1.00 103.57 ? 496 SER B CA  1 
ATOM   2859 C C   . SER B 1 196 ? -3.667  16.581  2.529   1.00 102.57 ? 496 SER B C   1 
ATOM   2860 O O   . SER B 1 196 ? -4.335  16.273  3.536   1.00 94.64  ? 496 SER B O   1 
ATOM   2861 C CB  . SER B 1 196 ? -1.905  18.018  3.526   1.00 106.54 ? 496 SER B CB  1 
ATOM   2862 O OG  . SER B 1 196 ? -0.605  17.981  4.092   1.00 113.97 ? 496 SER B OG  1 
HETATM 2863 P PA  . NAD C 2 .   ? 26.229  -2.586  -1.744  1.00 68.07  ? 501 NAD A PA  1 
HETATM 2864 O O1A . NAD C 2 .   ? 27.305  -2.174  -0.796  1.00 71.60  ? 501 NAD A O1A 1 
HETATM 2865 O O2A . NAD C 2 .   ? 26.701  -3.120  -3.057  1.00 81.61  ? 501 NAD A O2A 1 
HETATM 2866 O O5B . NAD C 2 .   ? 25.166  -1.408  -2.035  1.00 77.79  ? 501 NAD A O5B 1 
HETATM 2867 C C5B . NAD C 2 .   ? 23.867  -1.804  -2.583  1.00 67.96  ? 501 NAD A C5B 1 
HETATM 2868 C C4B . NAD C 2 .   ? 23.166  -0.688  -3.329  1.00 72.95  ? 501 NAD A C4B 1 
HETATM 2869 O O4B . NAD C 2 .   ? 23.144  0.547   -2.562  1.00 81.16  ? 501 NAD A O4B 1 
HETATM 2870 C C3B . NAD C 2 .   ? 23.773  -0.279  -4.675  1.00 76.78  ? 501 NAD A C3B 1 
HETATM 2871 O O3B . NAD C 2 .   ? 22.709  0.108   -5.539  1.00 76.76  ? 501 NAD A O3B 1 
HETATM 2872 C C2B . NAD C 2 .   ? 24.670  0.887   -4.252  1.00 75.48  ? 501 NAD A C2B 1 
HETATM 2873 O O2B . NAD C 2 .   ? 25.178  1.478   -5.429  1.00 68.49  ? 501 NAD A O2B 1 
HETATM 2874 C C1B . NAD C 2 .   ? 23.631  1.596   -3.376  1.00 81.83  ? 501 NAD A C1B 1 
HETATM 2875 N N9A . NAD C 2 .   ? 24.072  2.654   -2.469  1.00 82.35  ? 501 NAD A N9A 1 
HETATM 2876 C C8A . NAD C 2 .   ? 23.242  3.395   -1.651  1.00 81.74  ? 501 NAD A C8A 1 
HETATM 2877 N N7A . NAD C 2 .   ? 23.881  4.243   -0.879  1.00 68.90  ? 501 NAD A N7A 1 
HETATM 2878 C C5A . NAD C 2 .   ? 25.211  4.061   -1.219  1.00 62.56  ? 501 NAD A C5A 1 
HETATM 2879 C C6A . NAD C 2 .   ? 26.386  4.648   -0.732  1.00 58.80  ? 501 NAD A C6A 1 
HETATM 2880 N N6A . NAD C 2 .   ? 26.402  5.602   0.180   1.00 56.46  ? 501 NAD A N6A 1 
HETATM 2881 N N1A . NAD C 2 .   ? 27.558  4.235   -1.267  1.00 68.08  ? 501 NAD A N1A 1 
HETATM 2882 C C2A . NAD C 2 .   ? 27.532  3.284   -2.213  1.00 65.13  ? 501 NAD A C2A 1 
HETATM 2883 N N3A . NAD C 2 .   ? 26.497  2.616   -2.712  1.00 59.38  ? 501 NAD A N3A 1 
HETATM 2884 C C4A . NAD C 2 .   ? 25.350  3.064   -2.176  1.00 67.34  ? 501 NAD A C4A 1 
HETATM 2885 O O3  . NAD C 2 .   ? 25.326  -3.624  -0.907  1.00 71.30  ? 501 NAD A O3  1 
HETATM 2886 P PN  . NAD C 2 .   ? 24.116  -4.673  -1.084  1.00 80.74  ? 501 NAD A PN  1 
HETATM 2887 O O1N . NAD C 2 .   ? 23.344  -4.517  -2.359  1.00 72.55  ? 501 NAD A O1N 1 
HETATM 2888 O O2N . NAD C 2 .   ? 23.331  -4.603  0.181   1.00 70.90  ? 501 NAD A O2N 1 
HETATM 2889 O O5D . NAD C 2 .   ? 24.908  -6.064  -1.169  1.00 102.35 ? 501 NAD A O5D 1 
HETATM 2890 C C5D . NAD C 2 .   ? 26.326  -6.109  -1.479  1.00 116.56 ? 501 NAD A C5D 1 
HETATM 2891 C C4D . NAD C 2 .   ? 27.097  -6.150  -0.186  1.00 110.44 ? 501 NAD A C4D 1 
HETATM 2892 O O4D . NAD C 2 .   ? 26.485  -7.120  0.692   1.00 98.75  ? 501 NAD A O4D 1 
HETATM 2893 C C3D . NAD C 2 .   ? 28.553  -6.606  -0.311  1.00 107.05 ? 501 NAD A C3D 1 
HETATM 2894 O O3D . NAD C 2 .   ? 29.346  -6.128  0.770   1.00 130.40 ? 501 NAD A O3D 1 
HETATM 2895 C C2D . NAD C 2 .   ? 28.399  -8.131  -0.309  1.00 93.34  ? 501 NAD A C2D 1 
HETATM 2896 O O2D . NAD C 2 .   ? 29.409  -8.795  0.427   1.00 93.26  ? 501 NAD A O2D 1 
HETATM 2897 C C1D . NAD C 2 .   ? 27.108  -8.380  0.483   1.00 92.71  ? 501 NAD A C1D 1 
HETATM 2898 N N1N . NAD C 2 .   ? 26.215  -9.303  -0.252  1.00 95.35  ? 501 NAD A N1N 1 
HETATM 2899 C C2N . NAD C 2 .   ? 26.738  -10.511 -0.645  1.00 119.57 ? 501 NAD A C2N 1 
HETATM 2900 C C3N . NAD C 2 .   ? 25.977  -11.408 -1.387  1.00 121.39 ? 501 NAD A C3N 1 
HETATM 2901 C C7N . NAD C 2 .   ? 26.637  -12.709 -1.749  1.00 113.97 ? 501 NAD A C7N 1 
HETATM 2902 O O7N . NAD C 2 .   ? 26.165  -13.400 -2.664  1.00 121.30 ? 501 NAD A O7N 1 
HETATM 2903 N N7N . NAD C 2 .   ? 27.669  -13.130 -1.023  1.00 105.83 ? 501 NAD A N7N 1 
HETATM 2904 C C4N . NAD C 2 .   ? 24.654  -11.098 -1.691  1.00 105.90 ? 501 NAD A C4N 1 
HETATM 2905 C C5N . NAD C 2 .   ? 24.126  -9.886  -1.287  1.00 96.61  ? 501 NAD A C5N 1 
HETATM 2906 C C6N . NAD C 2 .   ? 24.911  -8.993  -0.571  1.00 97.87  ? 501 NAD A C6N 1 
HETATM 2907 P PA  . NAD D 2 .   ? 11.547  27.433  26.597  1.00 69.43  ? 501 NAD B PA  1 
HETATM 2908 O O1A . NAD D 2 .   ? 12.948  27.101  27.027  1.00 62.23  ? 501 NAD B O1A 1 
HETATM 2909 O O2A . NAD D 2 .   ? 10.759  28.218  27.593  1.00 95.85  ? 501 NAD B O2A 1 
HETATM 2910 O O5B . NAD D 2 .   ? 10.691  26.137  26.127  1.00 78.15  ? 501 NAD B O5B 1 
HETATM 2911 C C5B . NAD D 2 .   ? 9.920   26.129  24.864  1.00 69.40  ? 501 NAD B C5B 1 
HETATM 2912 C C4B . NAD D 2 .   ? 8.782   25.129  24.881  1.00 73.31  ? 501 NAD B C4B 1 
HETATM 2913 O O4B . NAD D 2 .   ? 9.293   23.771  24.817  1.00 79.29  ? 501 NAD B O4B 1 
HETATM 2914 C C3B . NAD D 2 .   ? 7.861   25.133  26.110  1.00 80.97  ? 501 NAD B C3B 1 
HETATM 2915 O O3B . NAD D 2 .   ? 6.532   24.744  25.782  1.00 87.26  ? 501 NAD B O3B 1 
HETATM 2916 C C2B . NAD D 2 .   ? 8.537   24.103  27.021  1.00 78.79  ? 501 NAD B C2B 1 
HETATM 2917 O O2B . NAD D 2 .   ? 7.689   23.566  28.014  1.00 80.19  ? 501 NAD B O2B 1 
HETATM 2918 C C1B . NAD D 2 .   ? 8.962   23.057  25.994  1.00 80.25  ? 501 NAD B C1B 1 
HETATM 2919 N N9A . NAD D 2 .   ? 10.139  22.286  26.388  1.00 77.55  ? 501 NAD B N9A 1 
HETATM 2920 C C8A . NAD D 2 .   ? 10.840  22.336  27.568  1.00 75.89  ? 501 NAD B C8A 1 
HETATM 2921 N N7A . NAD D 2 .   ? 11.870  21.525  27.606  1.00 66.68  ? 501 NAD B N7A 1 
HETATM 2922 C C5A . NAD D 2 .   ? 11.854  20.911  26.366  1.00 60.02  ? 501 NAD B C5A 1 
HETATM 2923 C C6A . NAD D 2 .   ? 12.705  19.962  25.781  1.00 54.20  ? 501 NAD B C6A 1 
HETATM 2924 N N6A . NAD D 2 .   ? 13.784  19.449  26.372  1.00 50.32  ? 501 NAD B N6A 1 
HETATM 2925 N N1A . NAD D 2 .   ? 12.406  19.587  24.519  1.00 62.42  ? 501 NAD B N1A 1 
HETATM 2926 C C2A . NAD D 2 .   ? 11.336  20.115  23.909  1.00 73.34  ? 501 NAD B C2A 1 
HETATM 2927 N N3A . NAD D 2 .   ? 10.456  20.997  24.363  1.00 72.84  ? 501 NAD B N3A 1 
HETATM 2928 C C4A . NAD D 2 .   ? 10.790  21.368  25.609  1.00 68.75  ? 501 NAD B C4A 1 
HETATM 2929 O O3  . NAD D 2 .   ? 11.600  28.162  25.171  1.00 75.59  ? 501 NAD B O3  1 
HETATM 2930 P PN  . NAD D 2 .   ? 10.876  29.369  24.401  1.00 80.80  ? 501 NAD B PN  1 
HETATM 2931 O O1N . NAD D 2 .   ? 9.444   29.481  24.828  1.00 71.15  ? 501 NAD B O1N 1 
HETATM 2932 O O2N . NAD D 2 .   ? 11.098  29.236  22.928  1.00 67.22  ? 501 NAD B O2N 1 
HETATM 2933 O O5D . NAD D 2 .   ? 11.795  30.545  25.018  1.00 81.57  ? 501 NAD B O5D 1 
HETATM 2934 C C5D . NAD D 2 .   ? 13.110  30.093  25.471  1.00 85.90  ? 501 NAD B C5D 1 
HETATM 2935 C C4D . NAD D 2 .   ? 13.855  31.193  26.181  1.00 90.60  ? 501 NAD B C4D 1 
HETATM 2936 O O4D . NAD D 2 .   ? 13.926  32.374  25.358  1.00 92.12  ? 501 NAD B O4D 1 
HETATM 2937 C C3D . NAD D 2 .   ? 13.243  31.710  27.483  1.00 88.79  ? 501 NAD B C3D 1 
HETATM 2938 O O3D . NAD D 2 .   ? 13.428  30.782  28.540  1.00 84.28  ? 501 NAD B O3D 1 
HETATM 2939 C C2D . NAD D 2 .   ? 14.068  32.986  27.645  1.00 88.76  ? 501 NAD B C2D 1 
HETATM 2940 O O2D . NAD D 2 .   ? 15.402  32.687  28.018  1.00 98.55  ? 501 NAD B O2D 1 
HETATM 2941 C C1D . NAD D 2 .   ? 14.047  33.512  26.208  1.00 89.99  ? 501 NAD B C1D 1 
HETATM 2942 N N1N . NAD D 2 .   ? 12.924  34.419  25.918  1.00 99.71  ? 501 NAD B N1N 1 
HETATM 2943 C C2N . NAD D 2 .   ? 12.894  35.656  26.516  1.00 116.80 ? 501 NAD B C2N 1 
HETATM 2944 C C3N . NAD D 2 .   ? 11.837  36.524  26.251  1.00 124.55 ? 501 NAD B C3N 1 
HETATM 2945 C C7N . NAD D 2 .   ? 11.867  37.844  26.957  1.00 125.93 ? 501 NAD B C7N 1 
HETATM 2946 O O7N . NAD D 2 .   ? 12.856  38.134  27.651  1.00 113.23 ? 501 NAD B O7N 1 
HETATM 2947 N N7N . NAD D 2 .   ? 10.815  38.649  26.852  1.00 130.86 ? 501 NAD B N7N 1 
HETATM 2948 C C4N . NAD D 2 .   ? 10.832  36.155  25.361  1.00 113.20 ? 501 NAD B C4N 1 
HETATM 2949 C C5N . NAD D 2 .   ? 10.881  34.914  24.757  1.00 106.58 ? 501 NAD B C5N 1 
HETATM 2950 C C6N . NAD D 2 .   ? 11.926  34.053  25.041  1.00 104.06 ? 501 NAD B C6N 1 
HETATM 2951 O O   . HOH E 3 .   ? 19.495  9.638   23.086  1.00 51.34  ? 601 HOH A O   1 
HETATM 2952 O O   . HOH E 3 .   ? 3.202   8.682   18.822  1.00 59.57  ? 602 HOH A O   1 
HETATM 2953 O O   . HOH E 3 .   ? 27.140  11.958  16.859  1.00 48.91  ? 603 HOH A O   1 
HETATM 2954 O O   . HOH E 3 .   ? 31.046  8.541   19.940  1.00 71.53  ? 604 HOH A O   1 
HETATM 2955 O O   . HOH E 3 .   ? 30.766  16.003  3.054   1.00 74.40  ? 605 HOH A O   1 
HETATM 2956 O O   . HOH E 3 .   ? 1.588   2.255   -12.492 1.00 76.57  ? 606 HOH A O   1 
HETATM 2957 O O   . HOH F 3 .   ? 24.128  39.780  11.565  1.00 64.97  ? 601 HOH B O   1 
HETATM 2958 O O   . HOH F 3 .   ? 28.241  15.535  7.316   1.00 55.15  ? 602 HOH B O   1 
HETATM 2959 O O   . HOH F 3 .   ? -8.174  16.914  -4.790  1.00 87.53  ? 603 HOH B O   1 
HETATM 2960 O O   . HOH F 3 .   ? 25.650  45.428  13.159  1.00 57.95  ? 604 HOH B O   1 
HETATM 2961 O O   . HOH F 3 .   ? 26.448  44.413  15.838  1.00 59.38  ? 605 HOH B O   1 
HETATM 2962 O O   . HOH F 3 .   ? 18.294  8.729   26.389  1.00 80.41  ? 606 HOH B O   1 
HETATM 2963 O O   . HOH F 3 .   ? 32.595  15.713  18.154  1.00 66.60  ? 607 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   . ASN A 10  ? 1.3335 1.2084 1.0734 0.2805  -0.1198 0.0986  310 ASN A N   
2    C CA  . ASN A 10  ? 1.2538 1.1360 1.0143 0.2352  -0.1100 0.0709  310 ASN A CA  
3    C C   . ASN A 10  ? 1.0420 0.9102 0.8612 0.2048  -0.0830 0.0640  310 ASN A C   
4    O O   . ASN A 10  ? 0.9612 0.7931 0.7722 0.1770  -0.0564 0.0647  310 ASN A O   
5    C CB  . ASN A 10  ? 1.3720 1.2135 1.0637 0.2268  -0.0915 0.0819  310 ASN A CB  
6    C CG  . ASN A 10  ? 1.5178 1.2914 1.1863 0.2218  -0.0498 0.1135  310 ASN A CG  
7    O OD1 . ASN A 10  ? 1.5345 1.2840 1.2250 0.2315  -0.0380 0.1294  310 ASN A OD1 
8    N ND2 . ASN A 10  ? 1.6036 1.3465 1.2329 0.2061  -0.0260 0.1201  310 ASN A ND2 
9    N N   . ALA A 11  ? 0.9391 0.8424 0.8180 0.2123  -0.0916 0.0553  311 ALA A N   
10   C CA  . ALA A 11  ? 0.8648 0.7720 0.8005 0.1846  -0.0712 0.0416  311 ALA A CA  
11   C C   . ALA A 11  ? 0.8231 0.7944 0.8284 0.1951  -0.0891 0.0254  311 ALA A C   
12   O O   . ALA A 11  ? 0.8493 0.8479 0.8581 0.2307  -0.1122 0.0318  311 ALA A O   
13   C CB  . ALA A 11  ? 0.8794 0.7274 0.8013 0.1849  -0.0381 0.0603  311 ALA A CB  
14   N N   . MET A 12  ? 0.7990 0.7953 0.8601 0.1656  -0.0775 0.0060  312 MET A N   
15   C CA  . MET A 12  ? 0.8369 0.8993 0.9758 0.1699  -0.0878 -0.0106 312 MET A CA  
16   C C   . MET A 12  ? 0.7777 0.8381 0.9589 0.1423  -0.0540 -0.0173 312 MET A C   
17   O O   . MET A 12  ? 0.8226 0.8416 0.9754 0.1157  -0.0334 -0.0154 312 MET A O   
18   C CB  . MET A 12  ? 0.9055 1.0278 1.0776 0.1608  -0.1230 -0.0363 312 MET A CB  
19   C CG  . MET A 12  ? 0.9504 1.0603 1.1207 0.1196  -0.1173 -0.0529 312 MET A CG  
20   S SD  . MET A 12  ? 1.0332 1.2063 1.2404 0.1110  -0.1621 -0.0895 312 MET A SD  
21   C CE  . MET A 12  ? 1.0365 1.1672 1.2395 0.0632  -0.1382 -0.1002 312 MET A CE  
22   N N   . VAL A 13  ? 0.7443 0.8505 0.9910 0.1523  -0.0473 -0.0239 313 VAL A N   
23   C CA  . VAL A 13  ? 0.7419 0.8491 1.0236 0.1294  -0.0111 -0.0287 313 VAL A CA  
24   C C   . VAL A 13  ? 0.7304 0.9079 1.0952 0.1083  -0.0175 -0.0494 313 VAL A C   
25   O O   . VAL A 13  ? 0.7733 1.0133 1.1919 0.1259  -0.0446 -0.0613 313 VAL A O   
26   C CB  . VAL A 13  ? 0.7350 0.8338 1.0279 0.1547  0.0144  -0.0210 313 VAL A CB  
27   C CG1 . VAL A 13  ? 0.7076 0.8129 1.0304 0.1329  0.0538  -0.0272 313 VAL A CG1 
28   C CG2 . VAL A 13  ? 0.7533 0.7776 0.9728 0.1723  0.0217  -0.0037 313 VAL A CG2 
29   N N   . VAL A 14  ? 0.6704 0.8378 1.0487 0.0717  0.0078  -0.0535 314 VAL A N   
30   C CA  . VAL A 14  ? 0.6875 0.9147 1.1536 0.0474  0.0130  -0.0706 314 VAL A CA  
31   C C   . VAL A 14  ? 0.7006 0.9165 1.1822 0.0320  0.0634  -0.0614 314 VAL A C   
32   O O   . VAL A 14  ? 0.7137 0.8724 1.1400 0.0142  0.0852  -0.0496 314 VAL A O   
33   C CB  . VAL A 14  ? 0.7180 0.9404 1.1863 0.0159  -0.0065 -0.0847 314 VAL A CB  
34   C CG1 . VAL A 14  ? 0.7114 0.9998 1.2847 -0.0107 -0.0064 -0.1072 314 VAL A CG1 
35   C CG2 . VAL A 14  ? 0.7157 0.9299 1.1344 0.0339  -0.0509 -0.0909 314 VAL A CG2 
36   N N   . ASN A 15  ? 0.7224 0.9945 1.2758 0.0425  0.0817  -0.0667 315 ASN A N   
37   C CA  . ASN A 15  ? 0.7908 1.0525 1.3475 0.0367  0.1335  -0.0568 315 ASN A CA  
38   C C   . ASN A 15  ? 0.8059 0.9902 1.2611 0.0516  0.1481  -0.0412 315 ASN A C   
39   O O   . ASN A 15  ? 0.7829 0.9534 1.2111 0.0845  0.1372  -0.0396 315 ASN A O   
40   C CB  . ASN A 15  ? 0.8432 1.1068 1.4326 -0.0057 0.1637  -0.0551 315 ASN A CB  
41   C CG  . ASN A 15  ? 0.8616 1.1979 1.5590 -0.0276 0.1484  -0.0755 315 ASN A CG  
42   O OD1 . ASN A 15  ? 0.8678 1.2753 1.6372 -0.0078 0.1291  -0.0913 315 ASN A OD1 
43   N ND2 . ASN A 15  ? 0.8857 1.2032 1.5950 -0.0661 0.1516  -0.0775 315 ASN A ND2 
44   N N   . ASN A 16  ? 0.8391 0.9727 1.2413 0.0280  0.1718  -0.0306 316 ASN A N   
45   C CA  . ASN A 16  ? 0.9260 0.9938 1.2391 0.0385  0.1849  -0.0210 316 ASN A CA  
46   C C   . ASN A 16  ? 0.8799 0.8965 1.1302 0.0284  0.1570  -0.0164 316 ASN A C   
47   O O   . ASN A 16  ? 0.9361 0.9015 1.1198 0.0259  0.1662  -0.0100 316 ASN A O   
48   C CB  . ASN A 16  ? 1.0354 1.0853 1.3246 0.0263  0.2301  -0.0123 316 ASN A CB  
49   C CG  . ASN A 16  ? 1.1186 1.1771 1.4048 0.0519  0.2614  -0.0165 316 ASN A CG  
50   O OD1 . ASN A 16  ? 1.1386 1.2390 1.4785 0.0747  0.2577  -0.0262 316 ASN A OD1 
51   N ND2 . ASN A 16  ? 1.1845 1.2043 1.4064 0.0516  0.2919  -0.0107 316 ASN A ND2 
52   N N   . LEU A 17  ? 0.8318 0.8667 1.1048 0.0240  0.1226  -0.0223 317 LEU A N   
53   C CA  . LEU A 17  ? 0.7769 0.7695 0.9955 0.0171  0.0985  -0.0196 317 LEU A CA  
54   C C   . LEU A 17  ? 0.7928 0.7851 0.9953 0.0426  0.0695  -0.0207 317 LEU A C   
55   O O   . LEU A 17  ? 0.8249 0.8634 1.0718 0.0558  0.0495  -0.0278 317 LEU A O   
56   C CB  . LEU A 17  ? 0.7670 0.7690 1.0103 -0.0102 0.0870  -0.0255 317 LEU A CB  
57   C CG  . LEU A 17  ? 0.7363 0.6980 0.9274 -0.0161 0.0649  -0.0252 317 LEU A CG  
58   C CD1 . LEU A 17  ? 0.7739 0.7086 0.9584 -0.0419 0.0776  -0.0216 317 LEU A CD1 
59   C CD2 . LEU A 17  ? 0.7240 0.7126 0.9315 -0.0105 0.0294  -0.0387 317 LEU A CD2 
60   N N   . THR A 18  ? 0.7643 0.7044 0.9038 0.0498  0.0688  -0.0128 318 THR A N   
61   C CA  . THR A 18  ? 0.7296 0.6527 0.8398 0.0690  0.0471  -0.0076 318 THR A CA  
62   C C   . THR A 18  ? 0.7182 0.6228 0.7963 0.0532  0.0307  -0.0079 318 THR A C   
63   O O   . THR A 18  ? 0.7345 0.6091 0.7864 0.0351  0.0412  -0.0072 318 THR A O   
64   C CB  . THR A 18  ? 0.7354 0.6110 0.8071 0.0823  0.0637  -0.0008 318 THR A CB  
65   O OG1 . THR A 18  ? 0.7069 0.6055 0.8134 0.1047  0.0742  -0.0028 318 THR A OG1 
66   C CG2 . THR A 18  ? 0.7443 0.5825 0.7742 0.0926  0.0508  0.0093  318 THR A CG2 
67   N N   . LEU A 19  ? 0.7322 0.6547 0.8083 0.0638  0.0047  -0.0095 319 LEU A N   
68   C CA  . LEU A 19  ? 0.7527 0.6577 0.7931 0.0541  -0.0089 -0.0115 319 LEU A CA  
69   C C   . LEU A 19  ? 0.7374 0.6264 0.7346 0.0783  -0.0214 0.0005  319 LEU A C   
70   O O   . LEU A 19  ? 0.6955 0.6119 0.7016 0.1022  -0.0393 0.0025  319 LEU A O   
71   C CB  . LEU A 19  ? 0.7810 0.7256 0.8587 0.0398  -0.0273 -0.0301 319 LEU A CB  
72   C CG  . LEU A 19  ? 0.8315 0.7670 0.8757 0.0359  -0.0459 -0.0388 319 LEU A CG  
73   C CD1 . LEU A 19  ? 0.8439 0.7339 0.8528 0.0206  -0.0288 -0.0331 319 LEU A CD1 
74   C CD2 . LEU A 19  ? 0.9048 0.8801 0.9954 0.0216  -0.0657 -0.0637 319 LEU A CD2 
75   N N   . GLN A 20  ? 0.7691 0.6159 0.7209 0.0724  -0.0116 0.0091  320 GLN A N   
76   C CA  . GLN A 20  ? 0.8518 0.6708 0.7580 0.0915  -0.0114 0.0265  320 GLN A CA  
77   C C   . GLN A 20  ? 0.8551 0.6626 0.7256 0.0814  -0.0132 0.0241  320 GLN A C   
78   O O   . GLN A 20  ? 0.8489 0.6469 0.7240 0.0592  -0.0043 0.0149  320 GLN A O   
79   C CB  . GLN A 20  ? 0.9041 0.6756 0.7966 0.0923  0.0136  0.0408  320 GLN A CB  
80   C CG  . GLN A 20  ? 0.9565 0.7299 0.8812 0.0991  0.0230  0.0384  320 GLN A CG  
81   C CD  . GLN A 20  ? 1.0167 0.7390 0.9277 0.0995  0.0455  0.0457  320 GLN A CD  
82   O OE1 . GLN A 20  ? 1.2629 0.9475 1.1468 0.1095  0.0527  0.0623  320 GLN A OE1 
83   N NE2 . GLN A 20  ? 0.9894 0.7068 0.9177 0.0887  0.0582  0.0328  320 GLN A NE2 
84   N N   . ILE A 21  ? 0.8850 0.6921 0.7153 0.1018  -0.0234 0.0337  321 ILE A N   
85   C CA  . ILE A 21  ? 0.8920 0.6843 0.6812 0.0968  -0.0177 0.0341  321 ILE A CA  
86   C C   . ILE A 21  ? 0.9392 0.6850 0.6969 0.1012  0.0101  0.0604  321 ILE A C   
87   O O   . ILE A 21  ? 0.9697 0.6970 0.7068 0.1239  0.0134  0.0825  321 ILE A O   
88   C CB  . ILE A 21  ? 0.9592 0.7793 0.7151 0.1164  -0.0436 0.0264  321 ILE A CB  
89   C CG1 . ILE A 21  ? 0.9466 0.8122 0.7451 0.1066  -0.0712 -0.0050 321 ILE A CG1 
90   C CG2 . ILE A 21  ? 0.9837 0.7856 0.6884 0.1156  -0.0312 0.0283  321 ILE A CG2 
91   C CD1 . ILE A 21  ? 0.9940 0.8981 0.7746 0.1319  -0.1062 -0.0158 321 ILE A CD1 
92   N N   . VAL A 22  ? 0.9284 0.6559 0.6862 0.0800  0.0301  0.0573  322 VAL A N   
93   C CA  . VAL A 22  ? 0.8975 0.5845 0.6432 0.0750  0.0596  0.0767  322 VAL A CA  
94   C C   . VAL A 22  ? 0.9785 0.6626 0.6983 0.0683  0.0753  0.0778  322 VAL A C   
95   O O   . VAL A 22  ? 0.9082 0.6154 0.6416 0.0559  0.0679  0.0561  322 VAL A O   
96   C CB  . VAL A 22  ? 0.8403 0.5185 0.6308 0.0532  0.0672  0.0648  322 VAL A CB  
97   C CG1 . VAL A 22  ? 0.8556 0.5104 0.6554 0.0331  0.0918  0.0659  322 VAL A CG1 
98   C CG2 . VAL A 22  ? 0.8891 0.5528 0.6928 0.0653  0.0663  0.0723  322 VAL A CG2 
99   N N   . GLN A 23  ? 1.0215 0.6744 0.7050 0.0780  0.0999  0.1046  323 GLN A N   
100  C CA  . GLN A 23  ? 1.0011 0.6471 0.6661 0.0696  0.1271  0.1102  323 GLN A CA  
101  C C   . GLN A 23  ? 0.9471 0.5726 0.6593 0.0419  0.1543  0.1102  323 GLN A C   
102  O O   . GLN A 23  ? 1.0737 0.6608 0.7889 0.0407  0.1736  0.1306  323 GLN A O   
103  C CB  . GLN A 23  ? 1.1292 0.7499 0.7278 0.0947  0.1447  0.1431  323 GLN A CB  
104  C CG  . GLN A 23  ? 1.2545 0.9000 0.8007 0.1262  0.1123  0.1405  323 GLN A CG  
105  C CD  . GLN A 23  ? 1.4026 1.0263 0.8667 0.1562  0.1275  0.1727  323 GLN A CD  
106  O OE1 . GLN A 23  ? 1.5364 1.1612 0.9617 0.1566  0.1497  0.1749  323 GLN A OE1 
107  N NE2 . GLN A 23  ? 1.4501 1.0546 0.8830 0.1853  0.1158  0.1985  323 GLN A NE2 
108  N N   . GLY A 24  ? 0.8390 0.4892 0.5901 0.0210  0.1540  0.0859  324 GLY A N   
109  C CA  . GLY A 24  ? 0.8047 0.4467 0.6050 -0.0047 0.1752  0.0805  324 GLY A CA  
110  C C   . GLY A 24  ? 0.7839 0.4635 0.6174 -0.0174 0.1693  0.0545  324 GLY A C   
111  O O   . GLY A 24  ? 0.8321 0.5342 0.6434 -0.0058 0.1577  0.0452  324 GLY A O   
112  N N   . HIS A 25  ? 0.7632 0.4494 0.6511 -0.0391 0.1745  0.0404  325 HIS A N   
113  C CA  . HIS A 25  ? 0.7393 0.4623 0.6638 -0.0467 0.1630  0.0157  325 HIS A CA  
114  C C   . HIS A 25  ? 0.7293 0.4589 0.6683 -0.0477 0.1305  -0.0013 325 HIS A C   
115  O O   . HIS A 25  ? 0.7908 0.5021 0.7378 -0.0538 0.1250  -0.0017 325 HIS A O   
116  C CB  . HIS A 25  ? 0.7953 0.5321 0.7755 -0.0677 0.1859  0.0081  325 HIS A CB  
117  C CG  . HIS A 25  ? 0.8870 0.6192 0.8617 -0.0708 0.2271  0.0261  325 HIS A CG  
118  N ND1 . HIS A 25  ? 0.8981 0.6621 0.9267 -0.0854 0.2492  0.0152  325 HIS A ND1 
119  C CD2 . HIS A 25  ? 0.9619 0.6634 0.8846 -0.0601 0.2526  0.0554  325 HIS A CD2 
120  C CE1 . HIS A 25  ? 0.9865 0.7378 0.9962 -0.0859 0.2916  0.0380  325 HIS A CE1 
121  N NE2 . HIS A 25  ? 0.9960 0.7065 0.9355 -0.0693 0.2937  0.0642  325 HIS A NE2 
122  N N   . ILE A 26  ? 0.6834 0.4358 0.6232 -0.0405 0.1115  -0.0150 326 ILE A N   
123  C CA  . ILE A 26  ? 0.6708 0.4267 0.6160 -0.0389 0.0850  -0.0261 326 ILE A CA  
124  C C   . ILE A 26  ? 0.6634 0.4299 0.6468 -0.0505 0.0785  -0.0401 326 ILE A C   
125  O O   . ILE A 26  ? 0.6927 0.4512 0.6714 -0.0508 0.0632  -0.0447 326 ILE A O   
126  C CB  . ILE A 26  ? 0.6772 0.4462 0.6141 -0.0280 0.0706  -0.0344 326 ILE A CB  
127  C CG1 . ILE A 26  ? 0.6250 0.3894 0.5615 -0.0262 0.0493  -0.0386 326 ILE A CG1 
128  C CG2 . ILE A 26  ? 0.6715 0.4634 0.6335 -0.0262 0.0777  -0.0456 326 ILE A CG2 
129  C CD1 . ILE A 26  ? 0.6569 0.4069 0.5702 -0.0236 0.0447  -0.0296 326 ILE A CD1 
130  N N   . GLU A 27  ? 0.6558 0.4447 0.6773 -0.0586 0.0891  -0.0491 327 GLU A N   
131  C CA  . GLU A 27  ? 0.6897 0.4984 0.7545 -0.0689 0.0771  -0.0680 327 GLU A CA  
132  C C   . GLU A 27  ? 0.7647 0.5535 0.8451 -0.0865 0.0861  -0.0711 327 GLU A C   
133  O O   . GLU A 27  ? 0.7700 0.5729 0.8833 -0.0962 0.0719  -0.0921 327 GLU A O   
134  C CB  . GLU A 27  ? 0.6966 0.5454 0.8107 -0.0714 0.0839  -0.0804 327 GLU A CB  
135  C CG  . GLU A 27  ? 0.7325 0.5873 0.8792 -0.0876 0.1202  -0.0755 327 GLU A CG  
136  C CD  . GLU A 27  ? 0.7676 0.6000 0.8698 -0.0802 0.1485  -0.0521 327 GLU A CD  
137  O OE1 . GLU A 27  ? 0.6979 0.5116 0.7484 -0.0641 0.1337  -0.0441 327 GLU A OE1 
138  O OE2 . GLU A 27  ? 0.8016 0.6353 0.9186 -0.0898 0.1844  -0.0421 327 GLU A OE2 
139  N N   . TRP A 28  ? 0.7715 0.5260 0.8285 -0.0889 0.1083  -0.0518 328 TRP A N   
140  C CA  . TRP A 28  ? 0.8196 0.5439 0.8905 -0.1036 0.1196  -0.0534 328 TRP A CA  
141  C C   . TRP A 28  ? 0.8447 0.5378 0.8737 -0.0913 0.1080  -0.0472 328 TRP A C   
142  O O   . TRP A 28  ? 0.8095 0.4657 0.8349 -0.0952 0.1216  -0.0407 328 TRP A O   
143  C CB  . TRP A 28  ? 0.8347 0.5358 0.9130 -0.1134 0.1578  -0.0327 328 TRP A CB  
144  C CG  . TRP A 28  ? 0.8288 0.5604 0.9597 -0.1302 0.1791  -0.0392 328 TRP A CG  
145  C CD1 . TRP A 28  ? 0.8294 0.6083 1.0178 -0.1408 0.1655  -0.0668 328 TRP A CD1 
146  C CD2 . TRP A 28  ? 0.8432 0.5616 0.9773 -0.1373 0.2214  -0.0162 328 TRP A CD2 
147  N NE1 . TRP A 28  ? 0.7928 0.5944 1.0295 -0.1557 0.1971  -0.0652 328 TRP A NE1 
148  C CE2 . TRP A 28  ? 0.8337 0.5962 1.0355 -0.1551 0.2348  -0.0331 328 TRP A CE2 
149  C CE3 . TRP A 28  ? 0.9056 0.5801 0.9897 -0.1280 0.2497  0.0184  328 TRP A CE3 
150  C CZ2 . TRP A 28  ? 0.8991 0.6624 1.1216 -0.1667 0.2810  -0.0160 328 TRP A CZ2 
151  C CZ3 . TRP A 28  ? 0.9652 0.6344 1.0591 -0.1372 0.2938  0.0381  328 TRP A CZ3 
152  C CH2 . TRP A 28  ? 0.9697 0.6823 1.1330 -0.1579 0.3120  0.0213  328 TRP A CH2 
153  N N   . GLN A 29  ? 0.7970 0.5033 0.7981 -0.0761 0.0856  -0.0490 329 GLN A N   
154  C CA  . GLN A 29  ? 0.7411 0.4257 0.7093 -0.0642 0.0795  -0.0423 329 GLN A CA  
155  C C   . GLN A 29  ? 0.7240 0.4076 0.6936 -0.0664 0.0638  -0.0635 329 GLN A C   
156  O O   . GLN A 29  ? 0.7023 0.4082 0.6892 -0.0723 0.0488  -0.0825 329 GLN A O   
157  C CB  . GLN A 29  ? 0.7182 0.4137 0.6573 -0.0485 0.0684  -0.0321 329 GLN A CB  
158  C CG  . GLN A 29  ? 0.7444 0.4426 0.6690 -0.0408 0.0770  -0.0153 329 GLN A CG  
159  C CD  . GLN A 29  ? 0.7234 0.3966 0.6298 -0.0323 0.0899  0.0027  329 GLN A CD  
160  O OE1 . GLN A 29  ? 0.7700 0.4357 0.6649 -0.0218 0.0839  0.0068  329 GLN A OE1 
161  N NE2 . GLN A 29  ? 0.7723 0.4340 0.6741 -0.0335 0.1090  0.0161  329 GLN A NE2 
162  N N   . THR A 30  ? 0.7111 0.3703 0.6595 -0.0580 0.0674  -0.0596 330 THR A N   
163  C CA  . THR A 30  ? 0.7270 0.3812 0.6605 -0.0537 0.0569  -0.0766 330 THR A CA  
164  C C   . THR A 30  ? 0.7270 0.3894 0.6315 -0.0377 0.0538  -0.0635 330 THR A C   
165  O O   . THR A 30  ? 0.8149 0.4688 0.7140 -0.0285 0.0636  -0.0481 330 THR A O   
166  C CB  . THR A 30  ? 0.7584 0.3756 0.6977 -0.0563 0.0700  -0.0848 330 THR A CB  
167  O OG1 . THR A 30  ? 0.8011 0.4101 0.7758 -0.0763 0.0735  -0.1015 330 THR A OG1 
168  C CG2 . THR A 30  ? 0.8056 0.4170 0.7232 -0.0490 0.0613  -0.1062 330 THR A CG2 
169  N N   . ALA A 31  ? 0.6812 0.3615 0.5699 -0.0338 0.0404  -0.0684 331 ALA A N   
170  C CA  . ALA A 31  ? 0.6606 0.3445 0.5269 -0.0227 0.0434  -0.0570 331 ALA A CA  
171  C C   . ALA A 31  ? 0.6829 0.3741 0.5231 -0.0180 0.0318  -0.0642 331 ALA A C   
172  O O   . ALA A 31  ? 0.6872 0.3874 0.5311 -0.0214 0.0163  -0.0765 331 ALA A O   
173  C CB  . ALA A 31  ? 0.6478 0.3435 0.5239 -0.0216 0.0451  -0.0390 331 ALA A CB  
174  N N   . ASP A 32  ? 0.6862 0.3748 0.5002 -0.0088 0.0403  -0.0571 332 ASP A N   
175  C CA  . ASP A 32  ? 0.7533 0.4445 0.5326 -0.0011 0.0327  -0.0549 332 ASP A CA  
176  C C   . ASP A 32  ? 0.7293 0.4298 0.5194 -0.0027 0.0190  -0.0449 332 ASP A C   
177  O O   . ASP A 32  ? 0.7244 0.4302 0.4991 0.0037  0.0010  -0.0517 332 ASP A O   
178  C CB  . ASP A 32  ? 0.8321 0.5198 0.5899 0.0061  0.0526  -0.0394 332 ASP A CB  
179  C CG  . ASP A 32  ? 0.8669 0.5479 0.6116 0.0129  0.0691  -0.0502 332 ASP A CG  
180  O OD1 . ASP A 32  ? 0.9082 0.5803 0.6435 0.0143  0.0607  -0.0734 332 ASP A OD1 
181  O OD2 . ASP A 32  ? 0.8790 0.5653 0.6289 0.0161  0.0905  -0.0375 332 ASP A OD2 
182  N N   . VAL A 33  ? 0.6550 0.3587 0.4719 -0.0087 0.0256  -0.0316 333 VAL A N   
183  C CA  . VAL A 33  ? 0.6677 0.3752 0.4949 -0.0082 0.0161  -0.0241 333 VAL A CA  
184  C C   . VAL A 33  ? 0.6455 0.3621 0.5063 -0.0162 0.0163  -0.0276 333 VAL A C   
185  O O   . VAL A 33  ? 0.6122 0.3289 0.4834 -0.0201 0.0264  -0.0238 333 VAL A O   
186  C CB  . VAL A 33  ? 0.7093 0.4059 0.5280 -0.0067 0.0265  -0.0052 333 VAL A CB  
187  C CG1 . VAL A 33  ? 0.6924 0.3863 0.5307 -0.0080 0.0199  -0.0004 333 VAL A CG1 
188  C CG2 . VAL A 33  ? 0.7479 0.4310 0.5233 0.0040  0.0306  0.0048  333 VAL A CG2 
189  N N   . ILE A 34  ? 0.6768 0.4034 0.5524 -0.0154 0.0054  -0.0341 334 ILE A N   
190  C CA  . ILE A 34  ? 0.6897 0.4252 0.5901 -0.0201 0.0091  -0.0361 334 ILE A CA  
191  C C   . ILE A 34  ? 0.6954 0.4298 0.5993 -0.0133 0.0030  -0.0323 334 ILE A C   
192  O O   . ILE A 34  ? 0.6758 0.4092 0.5740 -0.0040 -0.0082 -0.0319 334 ILE A O   
193  C CB  . ILE A 34  ? 0.7057 0.4555 0.6292 -0.0260 0.0083  -0.0492 334 ILE A CB  
194  C CG1 . ILE A 34  ? 0.7393 0.4793 0.6628 -0.0341 0.0174  -0.0533 334 ILE A CG1 
195  C CG2 . ILE A 34  ? 0.7003 0.4616 0.6451 -0.0280 0.0163  -0.0498 334 ILE A CG2 
196  C CD1 . ILE A 34  ? 0.7340 0.4846 0.6871 -0.0444 0.0167  -0.0695 334 ILE A CD1 
197  N N   . VAL A 35  ? 0.6910 0.4235 0.6020 -0.0156 0.0089  -0.0309 335 VAL A N   
198  C CA  . VAL A 35  ? 0.7417 0.4662 0.6580 -0.0099 0.0047  -0.0315 335 VAL A CA  
199  C C   . VAL A 35  ? 0.7250 0.4646 0.6586 -0.0044 0.0041  -0.0430 335 VAL A C   
200  O O   . VAL A 35  ? 0.7240 0.4751 0.6612 -0.0082 0.0131  -0.0481 335 VAL A O   
201  C CB  . VAL A 35  ? 0.7537 0.4681 0.6710 -0.0157 0.0086  -0.0302 335 VAL A CB  
202  C CG1 . VAL A 35  ? 0.8079 0.5041 0.7329 -0.0113 0.0049  -0.0335 335 VAL A CG1 
203  C CG2 . VAL A 35  ? 0.7904 0.4982 0.7015 -0.0220 0.0142  -0.0194 335 VAL A CG2 
204  N N   . ASN A 36  ? 0.7443 0.4827 0.6866 0.0075  -0.0049 -0.0451 336 ASN A N   
205  C CA  . ASN A 36  ? 0.7133 0.4672 0.6782 0.0169  -0.0042 -0.0572 336 ASN A CA  
206  C C   . ASN A 36  ? 0.7203 0.4516 0.6825 0.0231  -0.0026 -0.0615 336 ASN A C   
207  O O   . ASN A 36  ? 0.6810 0.3834 0.6311 0.0199  -0.0048 -0.0539 336 ASN A O   
208  C CB  . ASN A 36  ? 0.7296 0.5003 0.7123 0.0304  -0.0181 -0.0599 336 ASN A CB  
209  C CG  . ASN A 36  ? 0.7519 0.5555 0.7723 0.0375  -0.0137 -0.0752 336 ASN A CG  
210  O OD1 . ASN A 36  ? 0.7829 0.5941 0.8088 0.0313  0.0041  -0.0819 336 ASN A OD1 
211  N ND2 . ASN A 36  ? 0.8230 0.6506 0.8698 0.0520  -0.0290 -0.0810 336 ASN A ND2 
212  N N   . SER A 37  ? 0.7254 0.4700 0.7019 0.0308  0.0040  -0.0761 337 SER A N   
213  C CA  . SER A 37  ? 0.7685 0.4917 0.7436 0.0385  0.0054  -0.0881 337 SER A CA  
214  C C   . SER A 37  ? 0.7686 0.5045 0.7685 0.0586  0.0073  -0.1008 337 SER A C   
215  O O   . SER A 37  ? 0.7248 0.4944 0.7378 0.0605  0.0198  -0.1104 337 SER A O   
216  C CB  . SER A 37  ? 0.7679 0.4951 0.7249 0.0294  0.0137  -0.0983 337 SER A CB  
217  O OG  . SER A 37  ? 0.7934 0.4946 0.7467 0.0323  0.0098  -0.1136 337 SER A OG  
218  N N   . VAL A 38  ? 0.7820 0.4913 0.7906 0.0746  -0.0029 -0.0980 338 VAL A N   
219  C CA  . VAL A 38  ? 0.8266 0.5511 0.8650 0.0995  -0.0056 -0.1066 338 VAL A CA  
220  C C   . VAL A 38  ? 0.8967 0.5792 0.9378 0.1167  -0.0053 -0.1171 338 VAL A C   
221  O O   . VAL A 38  ? 0.9261 0.5605 0.9499 0.1091  -0.0077 -0.1114 338 VAL A O   
222  C CB  . VAL A 38  ? 0.8022 0.5400 0.8538 0.1135  -0.0237 -0.0920 338 VAL A CB  
223  C CG1 . VAL A 38  ? 0.7598 0.5380 0.8154 0.0971  -0.0259 -0.0884 338 VAL A CG1 
224  C CG2 . VAL A 38  ? 0.8194 0.5054 0.8442 0.1201  -0.0354 -0.0703 338 VAL A CG2 
225  N N   . ASN A 39  ? 0.8977 0.6001 0.9678 0.1401  -0.0009 -0.1334 339 ASN A N   
226  C CA  . ASN A 39  ? 0.9346 0.5983 1.0173 0.1668  -0.0046 -0.1402 339 ASN A CA  
227  C C   . ASN A 39  ? 0.9824 0.6466 1.0790 0.1895  -0.0242 -0.1180 339 ASN A C   
228  O O   . ASN A 39  ? 0.9427 0.6625 1.0669 0.1991  -0.0313 -0.1187 339 ASN A O   
229  C CB  . ASN A 39  ? 0.9320 0.6185 1.0367 0.1839  0.0118  -0.1708 339 ASN A CB  
230  C CG  . ASN A 39  ? 0.9814 0.6348 1.1089 0.2186  0.0084  -0.1804 339 ASN A CG  
231  O OD1 . ASN A 39  ? 0.9846 0.5970 1.1125 0.2332  -0.0073 -0.1601 339 ASN A OD1 
232  N ND2 . ASN A 39  ? 1.0473 0.7152 1.1907 0.2351  0.0255  -0.2105 339 ASN A ND2 
233  N N   . PRO A 40  ? 1.0576 0.6603 1.1349 0.1987  -0.0338 -0.0973 340 PRO A N   
234  C CA  . PRO A 40  ? 1.0634 0.6628 1.1352 0.2215  -0.0543 -0.0701 340 PRO A CA  
235  C C   . PRO A 40  ? 1.0371 0.6697 1.1490 0.2625  -0.0676 -0.0781 340 PRO A C   
236  O O   . PRO A 40  ? 0.9939 0.6575 1.1091 0.2803  -0.0900 -0.0641 340 PRO A O   
237  C CB  . PRO A 40  ? 1.1640 0.6797 1.2028 0.2220  -0.0524 -0.0444 340 PRO A CB  
238  C CG  . PRO A 40  ? 1.1634 0.6376 1.2084 0.2040  -0.0334 -0.0670 340 PRO A CG  
239  C CD  . PRO A 40  ? 1.1073 0.6408 1.1659 0.1862  -0.0244 -0.0985 340 PRO A CD  
240  N N   . HIS A 41  ? 1.0376 0.6686 1.1806 0.2780  -0.0545 -0.1037 341 HIS A N   
241  C CA  . HIS A 41  ? 1.0797 0.7487 1.2716 0.3189  -0.0629 -0.1158 341 HIS A CA  
242  C C   . HIS A 41  ? 1.0064 0.7726 1.2408 0.3102  -0.0631 -0.1323 341 HIS A C   
243  O O   . HIS A 41  ? 0.9521 0.7706 1.2326 0.3391  -0.0800 -0.1362 341 HIS A O   
244  C CB  . HIS A 41  ? 1.1806 0.8158 1.3924 0.3395  -0.0449 -0.1411 341 HIS A CB  
245  C CG  . HIS A 41  ? 1.2949 0.8318 1.4730 0.3363  -0.0379 -0.1350 341 HIS A CG  
246  N ND1 . HIS A 41  ? 1.3791 0.8798 1.5709 0.3495  -0.0213 -0.1649 341 HIS A ND1 
247  C CD2 . HIS A 41  ? 1.3634 0.8313 1.5017 0.3213  -0.0421 -0.1066 341 HIS A CD2 
248  C CE1 . HIS A 41  ? 1.4274 0.8391 1.5931 0.3399  -0.0179 -0.1572 341 HIS A CE1 
249  N NE2 . HIS A 41  ? 1.4454 0.8374 1.5807 0.3214  -0.0284 -0.1202 341 HIS A NE2 
250  N N   . ASP A 42  ? 1.0249 0.8160 1.2476 0.2704  -0.0448 -0.1413 342 ASP A N   
251  C CA  . ASP A 42  ? 0.9392 0.8127 1.2042 0.2567  -0.0376 -0.1554 342 ASP A CA  
252  C C   . ASP A 42  ? 0.8685 0.7448 1.0998 0.2129  -0.0267 -0.1489 342 ASP A C   
253  O O   . ASP A 42  ? 0.8321 0.6908 1.0376 0.1929  -0.0031 -0.1563 342 ASP A O   
254  C CB  . ASP A 42  ? 0.9545 0.8668 1.2667 0.2712  -0.0118 -0.1838 342 ASP A CB  
255  C CG  . ASP A 42  ? 0.9399 0.9444 1.3242 0.2723  -0.0074 -0.1978 342 ASP A CG  
256  O OD1 . ASP A 42  ? 0.9800 1.0168 1.3710 0.2486  -0.0188 -0.1897 342 ASP A OD1 
257  O OD2 . ASP A 42  ? 0.9650 1.0087 1.4031 0.2970  0.0079  -0.2187 342 ASP A OD2 
258  N N   . ILE A 43  ? 0.8612 0.7618 1.0921 0.2009  -0.0458 -0.1369 343 ILE A N   
259  C CA  . ILE A 43  ? 0.8195 0.7192 1.0209 0.1634  -0.0373 -0.1298 343 ILE A CA  
260  C C   . ILE A 43  ? 0.8091 0.7703 1.0555 0.1445  -0.0176 -0.1457 343 ILE A C   
261  O O   . ILE A 43  ? 0.7816 0.7465 1.0135 0.1156  -0.0104 -0.1405 343 ILE A O   
262  C CB  . ILE A 43  ? 0.8169 0.7069 0.9916 0.1604  -0.0647 -0.1121 343 ILE A CB  
263  C CG1 . ILE A 43  ? 0.8557 0.8081 1.0795 0.1745  -0.0893 -0.1224 343 ILE A CG1 
264  C CG2 . ILE A 43  ? 0.8477 0.6722 0.9752 0.1779  -0.0773 -0.0905 343 ILE A CG2 
265  C CD1 . ILE A 43  ? 0.8626 0.8278 1.0681 0.1562  -0.1071 -0.1187 343 ILE A CD1 
266  N N   . THR A 44  ? 0.8053 0.8139 1.1103 0.1616  -0.0069 -0.1639 344 THR A N   
267  C CA  . THR A 44  ? 0.7853 0.8544 1.1430 0.1430  0.0180  -0.1776 344 THR A CA  
268  C C   . THR A 44  ? 0.8035 0.8604 1.1400 0.1354  0.0594  -0.1827 344 THR A C   
269  O O   . THR A 44  ? 0.8512 0.9512 1.2244 0.1223  0.0905  -0.1907 344 THR A O   
270  C CB  . THR A 44  ? 0.7828 0.9214 1.2258 0.1660  0.0082  -0.1958 344 THR A CB  
271  O OG1 . THR A 44  ? 0.8170 0.9501 1.2678 0.1917  0.0293  -0.2065 344 THR A OG1 
272  C CG2 . THR A 44  ? 0.7767 0.9218 1.2275 0.1880  -0.0400 -0.1914 344 THR A CG2 
273  N N   . VAL A 45  ? 0.7836 0.7822 1.0608 0.1439  0.0603  -0.1791 345 VAL A N   
274  C CA  . VAL A 45  ? 0.8076 0.7932 1.0549 0.1431  0.0930  -0.1888 345 VAL A CA  
275  C C   . VAL A 45  ? 0.7887 0.7251 0.9647 0.1214  0.0921  -0.1755 345 VAL A C   
276  O O   . VAL A 45  ? 0.7531 0.6525 0.9034 0.1165  0.0659  -0.1629 345 VAL A O   
277  C CB  . VAL A 45  ? 0.9060 0.8714 1.1570 0.1772  0.0915  -0.2064 345 VAL A CB  
278  C CG1 . VAL A 45  ? 0.9277 0.8793 1.1420 0.1814  0.1229  -0.2239 345 VAL A CG1 
279  C CG2 . VAL A 45  ? 0.9530 0.9710 1.2814 0.2042  0.0867  -0.2181 345 VAL A CG2 
280  N N   . GLY A 46  ? 0.8311 0.7706 0.9764 0.1115  0.1220  -0.1780 346 GLY A N   
281  C CA  . GLY A 46  ? 0.8640 0.7672 0.9446 0.0948  0.1216  -0.1671 346 GLY A CA  
282  C C   . GLY A 46  ? 0.8340 0.7514 0.9124 0.0695  0.1327  -0.1469 346 GLY A C   
283  O O   . GLY A 46  ? 0.8069 0.7456 0.9283 0.0590  0.1240  -0.1399 346 GLY A O   
284  N N   . PRO A 47  ? 0.8823 0.7856 0.9086 0.0611  0.1506  -0.1380 347 PRO A N   
285  C CA  . PRO A 47  ? 0.8889 0.7928 0.9072 0.0397  0.1626  -0.1157 347 PRO A CA  
286  C C   . PRO A 47  ? 0.8430 0.7379 0.8817 0.0239  0.1366  -0.1045 347 PRO A C   
287  O O   . PRO A 47  ? 0.8232 0.7409 0.9077 0.0105  0.1425  -0.1013 347 PRO A O   
288  C CB  . PRO A 47  ? 0.9137 0.7894 0.8565 0.0432  0.1686  -0.1084 347 PRO A CB  
289  C CG  . PRO A 47  ? 1.0083 0.8872 0.9283 0.0648  0.1780  -0.1312 347 PRO A CG  
290  C CD  . PRO A 47  ? 0.9596 0.8449 0.9300 0.0752  0.1596  -0.1505 347 PRO A CD  
291  N N   . VAL A 48  ? 0.8033 0.6668 0.8108 0.0253  0.1090  -0.1016 348 VAL A N   
292  C CA  . VAL A 48  ? 0.7481 0.5993 0.7618 0.0137  0.0872  -0.0913 348 VAL A CA  
293  C C   . VAL A 48  ? 0.7407 0.6132 0.8031 0.0173  0.0712  -0.0989 348 VAL A C   
294  O O   . VAL A 48  ? 0.7882 0.6739 0.8755 0.0054  0.0662  -0.0964 348 VAL A O   
295  C CB  . VAL A 48  ? 0.7465 0.5645 0.7214 0.0167  0.0672  -0.0887 348 VAL A CB  
296  C CG1 . VAL A 48  ? 0.7611 0.5655 0.7392 0.0091  0.0471  -0.0791 348 VAL A CG1 
297  C CG2 . VAL A 48  ? 0.7450 0.5505 0.6749 0.0150  0.0757  -0.0829 348 VAL A CG2 
298  N N   . ALA A 49  ? 0.7633 0.6395 0.8401 0.0361  0.0616  -0.1103 349 ALA A N   
299  C CA  . ALA A 49  ? 0.7748 0.6704 0.8912 0.0467  0.0409  -0.1154 349 ALA A CA  
300  C C   . ALA A 49  ? 0.7804 0.7261 0.9537 0.0380  0.0498  -0.1237 349 ALA A C   
301  O O   . ALA A 49  ? 0.7738 0.7390 0.9750 0.0373  0.0280  -0.1271 349 ALA A O   
302  C CB  . ALA A 49  ? 0.7644 0.6538 0.8898 0.0726  0.0346  -0.1256 349 ALA A CB  
303  N N   . LYS A 50  ? 0.8330 0.8013 1.0248 0.0319  0.0824  -0.1285 350 LYS A N   
304  C CA  . LYS A 50  ? 0.8644 0.8836 1.1231 0.0200  0.0986  -0.1376 350 LYS A CA  
305  C C   . LYS A 50  ? 0.8300 0.8417 1.0906 -0.0086 0.1018  -0.1291 350 LYS A C   
306  O O   . LYS A 50  ? 0.8924 0.9327 1.2019 -0.0181 0.0850  -0.1402 350 LYS A O   
307  C CB  . LYS A 50  ? 0.9036 0.9437 1.1751 0.0222  0.1407  -0.1416 350 LYS A CB  
308  C CG  . LYS A 50  ? 1.0209 1.0945 1.3320 0.0493  0.1420  -0.1602 350 LYS A CG  
309  C CD  . LYS A 50  ? 1.1338 1.1992 1.4121 0.0639  0.1754  -0.1649 350 LYS A CD  
310  C CE  . LYS A 50  ? 1.1732 1.2320 1.4187 0.0458  0.2174  -0.1512 350 LYS A CE  
311  N NZ  . LYS A 50  ? 1.1796 1.2554 1.4168 0.0622  0.2561  -0.1613 350 LYS A NZ  
312  N N   . SER A 51  ? 0.7239 0.6971 0.9317 -0.0198 0.1217  -0.1116 351 SER A N   
313  C CA  . SER A 51  ? 0.7015 0.6537 0.9015 -0.0428 0.1260  -0.1009 351 SER A CA  
314  C C   . SER A 51  ? 0.6763 0.6271 0.8860 -0.0456 0.0888  -0.1095 351 SER A C   
315  O O   . SER A 51  ? 0.7212 0.6852 0.9699 -0.0640 0.0866  -0.1186 351 SER A O   
316  C CB  . SER A 51  ? 0.7116 0.6173 0.8404 -0.0417 0.1364  -0.0803 351 SER A CB  
317  O OG  . SER A 51  ? 0.7440 0.6509 0.8511 -0.0349 0.1680  -0.0734 351 SER A OG  
318  N N   . ILE A 52  ? 0.6564 0.5896 0.8290 -0.0269 0.0613  -0.1076 352 ILE A N   
319  C CA  . ILE A 52  ? 0.6296 0.5537 0.7897 -0.0240 0.0290  -0.1105 352 ILE A CA  
320  C C   . ILE A 52  ? 0.6660 0.6361 0.8811 -0.0182 0.0067  -0.1306 352 ILE A C   
321  O O   . ILE A 52  ? 0.7620 0.7402 0.9880 -0.0269 -0.0117 -0.1412 352 ILE A O   
322  C CB  . ILE A 52  ? 0.5937 0.4827 0.6995 -0.0069 0.0148  -0.0981 352 ILE A CB  
323  C CG1 . ILE A 52  ? 0.5941 0.4461 0.6542 -0.0170 0.0288  -0.0828 352 ILE A CG1 
324  C CG2 . ILE A 52  ? 0.5967 0.4829 0.6909 0.0052  -0.0165 -0.0995 352 ILE A CG2 
325  C CD1 . ILE A 52  ? 0.6100 0.4302 0.6272 -0.0097 0.0147  -0.0722 352 ILE A CD1 
326  N N   . LEU A 53  ? 0.7398 0.7422 0.9908 -0.0018 0.0074  -0.1385 353 LEU A N   
327  C CA  . LEU A 53  ? 0.7947 0.8482 1.1026 0.0108  -0.0184 -0.1581 353 LEU A CA  
328  C C   . LEU A 53  ? 0.7574 0.8551 1.1350 -0.0156 -0.0104 -0.1777 353 LEU A C   
329  O O   . LEU A 53  ? 0.7740 0.9036 1.1835 -0.0152 -0.0420 -0.1968 353 LEU A O   
330  C CB  . LEU A 53  ? 0.8615 0.9401 1.1985 0.0371  -0.0152 -0.1627 353 LEU A CB  
331  C CG  . LEU A 53  ? 0.9112 1.0504 1.3145 0.0572  -0.0445 -0.1829 353 LEU A CG  
332  C CD1 . LEU A 53  ? 0.9422 1.0722 1.3127 0.0758  -0.0915 -0.1812 353 LEU A CD1 
333  C CD2 . LEU A 53  ? 0.8814 1.0381 1.3113 0.0864  -0.0356 -0.1863 353 LEU A CD2 
334  N N   . GLN A 54  ? 0.7859 0.8849 1.1867 -0.0374 0.0317  -0.1735 354 GLN A N   
335  C CA  . GLN A 54  ? 0.8399 0.9719 1.3119 -0.0682 0.0484  -0.1891 354 GLN A CA  
336  C C   . GLN A 54  ? 0.8215 0.9229 1.2717 -0.0875 0.0317  -0.1934 354 GLN A C   
337  O O   . GLN A 54  ? 0.8481 0.9846 1.3513 -0.0987 0.0082  -0.2202 354 GLN A O   
338  C CB  . GLN A 54  ? 0.8854 1.0039 1.3670 -0.0908 0.1029  -0.1745 354 GLN A CB  
339  C CG  . GLN A 54  ? 0.9612 1.1312 1.5046 -0.0866 0.1339  -0.1810 354 GLN A CG  
340  C CD  . GLN A 54  ? 1.0510 1.1986 1.5852 -0.1068 0.1915  -0.1605 354 GLN A CD  
341  O OE1 . GLN A 54  ? 1.0591 1.1506 1.5092 -0.1008 0.2066  -0.1352 354 GLN A OE1 
342  N NE2 . GLN A 54  ? 1.1133 1.3051 1.7353 -0.1312 0.2237  -0.1709 354 GLN A NE2 
343  N N   . GLN A 55  ? 0.7707 0.8096 1.1446 -0.0891 0.0421  -0.1703 355 GLN A N   
344  C CA  . GLN A 55  ? 0.8004 0.8052 1.1526 -0.1059 0.0340  -0.1738 355 GLN A CA  
345  C C   . GLN A 55  ? 0.7659 0.7816 1.1021 -0.0919 -0.0136 -0.1924 355 GLN A C   
346  O O   . GLN A 55  ? 0.8329 0.8483 1.1849 -0.1074 -0.0274 -0.2133 355 GLN A O   
347  C CB  . GLN A 55  ? 0.8540 0.7961 1.1304 -0.1039 0.0527  -0.1449 355 GLN A CB  
348  C CG  . GLN A 55  ? 0.8515 0.7547 1.1144 -0.1219 0.0558  -0.1472 355 GLN A CG  
349  C CD  . GLN A 55  ? 0.8391 0.7491 1.1695 -0.1529 0.0808  -0.1593 355 GLN A CD  
350  O OE1 . GLN A 55  ? 0.7430 0.6560 1.0993 -0.1635 0.1181  -0.1451 355 GLN A OE1 
351  N NE2 . GLN A 55  ? 0.8776 0.7890 1.2368 -0.1682 0.0617  -0.1870 355 GLN A NE2 
352  N N   . ALA A 56  ? 0.7390 0.7584 1.0380 -0.0617 -0.0372 -0.1844 356 ALA A N   
353  C CA  . ALA A 56  ? 0.7946 0.8096 1.0525 -0.0438 -0.0769 -0.1916 356 ALA A CA  
354  C C   . ALA A 56  ? 0.8308 0.9075 1.1444 -0.0348 -0.1134 -0.2219 356 ALA A C   
355  O O   . ALA A 56  ? 0.8057 0.8878 1.0945 -0.0254 -0.1487 -0.2375 356 ALA A O   
356  C CB  . ALA A 56  ? 0.7674 0.7494 0.9583 -0.0169 -0.0819 -0.1652 356 ALA A CB  
357  N N   . GLY A 57  ? 0.8583 0.9844 1.2451 -0.0346 -0.1047 -0.2306 357 GLY A N   
358  C CA  . GLY A 57  ? 0.9180 1.1168 1.3810 -0.0285 -0.1366 -0.2629 357 GLY A CA  
359  C C   . GLY A 57  ? 0.9179 1.1394 1.3683 0.0149  -0.1666 -0.2559 357 GLY A C   
360  O O   . GLY A 57  ? 0.8914 1.0631 1.2656 0.0376  -0.1659 -0.2272 357 GLY A O   
361  N N   . VAL A 58  ? 0.9520 1.2488 1.4823 0.0261  -0.1942 -0.2837 358 VAL A N   
362  C CA  . VAL A 58  ? 0.9787 1.3056 1.5163 0.0707  -0.2216 -0.2791 358 VAL A CA  
363  C C   . VAL A 58  ? 1.0408 1.3259 1.4798 0.1060  -0.2601 -0.2610 358 VAL A C   
364  O O   . VAL A 58  ? 1.0369 1.3044 1.4449 0.1434  -0.2681 -0.2388 358 VAL A O   
365  C CB  . VAL A 58  ? 0.9334 1.3602 1.5861 0.0759  -0.2486 -0.3172 358 VAL A CB  
366  C CG1 . VAL A 58  ? 0.9534 1.4182 1.6135 0.0765  -0.3029 -0.3499 358 VAL A CG1 
367  C CG2 . VAL A 58  ? 0.9143 1.3753 1.5943 0.1223  -0.2633 -0.3107 358 VAL A CG2 
368  N N   . GLU A 59  ? 0.9995 1.2654 1.3885 0.0954  -0.2807 -0.2699 359 GLU A N   
369  C CA  . GLU A 59  ? 1.0181 1.2528 1.3135 0.1297  -0.3168 -0.2552 359 GLU A CA  
370  C C   . GLU A 59  ? 1.0116 1.1614 1.2153 0.1380  -0.2873 -0.2102 359 GLU A C   
371  O O   . GLU A 59  ? 1.0562 1.1721 1.1827 0.1698  -0.3067 -0.1876 359 GLU A O   
372  C CB  . GLU A 59  ? 1.0485 1.2860 1.3120 0.1159  -0.3425 -0.2811 359 GLU A CB  
373  C CG  . GLU A 59  ? 1.0723 1.3954 1.4296 0.1052  -0.3782 -0.3327 359 GLU A CG  
374  C CD  . GLU A 59  ? 1.1440 1.4699 1.4653 0.0961  -0.4109 -0.3655 359 GLU A CD  
375  O OE1 . GLU A 59  ? 1.2699 1.5812 1.5022 0.1333  -0.4466 -0.3570 359 GLU A OE1 
376  O OE2 . GLU A 59  ? 1.1026 1.4405 1.4791 0.0539  -0.3994 -0.3988 359 GLU A OE2 
377  N N   . MET A 60  ? 0.9675 1.0843 1.1804 0.1091  -0.2404 -0.1977 360 MET A N   
378  C CA  . MET A 60  ? 0.9648 1.0099 1.1077 0.1111  -0.2120 -0.1616 360 MET A CA  
379  C C   . MET A 60  ? 0.9434 0.9751 1.0844 0.1430  -0.2115 -0.1409 360 MET A C   
380  O O   . MET A 60  ? 0.9160 0.8911 0.9921 0.1586  -0.2065 -0.1117 360 MET A O   
381  C CB  . MET A 60  ? 0.9389 0.9639 1.0992 0.0738  -0.1684 -0.1599 360 MET A CB  
382  C CG  . MET A 60  ? 0.9595 0.9184 1.0530 0.0692  -0.1427 -0.1303 360 MET A CG  
383  S SD  . MET A 60  ? 1.0363 0.9711 1.1352 0.0799  -0.1182 -0.1115 360 MET A SD  
384  C CE  . MET A 60  ? 0.9603 0.9322 1.1298 0.0581  -0.0877 -0.1285 360 MET A CE  
385  N N   . LYS A 61  ? 0.9215 1.0051 1.1397 0.1517  -0.2138 -0.1577 361 LYS A N   
386  C CA  . LYS A 61  ? 0.9374 1.0137 1.1671 0.1845  -0.2132 -0.1451 361 LYS A CA  
387  C C   . LYS A 61  ? 1.0324 1.1113 1.2331 0.2305  -0.2568 -0.1351 361 LYS A C   
388  O O   . LYS A 61  ? 1.1040 1.1486 1.2867 0.2620  -0.2564 -0.1143 361 LYS A O   
389  C CB  . LYS A 61  ? 0.9083 1.0466 1.2344 0.1788  -0.1978 -0.1695 361 LYS A CB  
390  C CG  . LYS A 61  ? 0.9139 1.0538 1.2667 0.2139  -0.1940 -0.1646 361 LYS A CG  
391  C CD  . LYS A 61  ? 0.8823 1.0953 1.3360 0.2118  -0.1781 -0.1918 361 LYS A CD  
392  C CE  . LYS A 61  ? 0.9181 1.1224 1.3867 0.2525  -0.1754 -0.1867 361 LYS A CE  
393  N NZ  . LYS A 61  ? 0.9120 1.1913 1.4797 0.2566  -0.1584 -0.2132 361 LYS A NZ  
394  N N   . SER A 62  ? 1.0425 1.1587 1.2360 0.2367  -0.2950 -0.1506 362 SER A N   
395  C CA  . SER A 62  ? 1.0854 1.2026 1.2350 0.2844  -0.3397 -0.1386 362 SER A CA  
396  C C   . SER A 62  ? 1.1979 1.2279 1.2348 0.2957  -0.3309 -0.0975 362 SER A C   
397  O O   . SER A 62  ? 1.3381 1.3259 1.3365 0.3331  -0.3363 -0.0669 362 SER A O   
398  C CB  . SER A 62  ? 1.0565 1.2422 1.2271 0.2888  -0.3857 -0.1715 362 SER A CB  
399  O OG  . SER A 62  ? 1.0068 1.2790 1.2918 0.2884  -0.3988 -0.2065 362 SER A OG  
400  N N   . GLU A 63  ? 1.2021 1.2035 1.1892 0.2641  -0.3148 -0.0961 363 GLU A N   
401  C CA  . GLU A 63  ? 1.2714 1.1979 1.1582 0.2725  -0.3022 -0.0585 363 GLU A CA  
402  C C   . GLU A 63  ? 1.2176 1.0814 1.0997 0.2681  -0.2634 -0.0286 363 GLU A C   
403  O O   . GLU A 63  ? 1.2748 1.0758 1.0908 0.2862  -0.2549 0.0077  363 GLU A O   
404  C CB  . GLU A 63  ? 1.3203 1.2336 1.1635 0.2406  -0.2893 -0.0664 363 GLU A CB  
405  C CG  . GLU A 63  ? 1.4730 1.3257 1.2096 0.2573  -0.2837 -0.0315 363 GLU A CG  
406  C CD  . GLU A 63  ? 1.5610 1.3870 1.2590 0.2243  -0.2546 -0.0325 363 GLU A CD  
407  O OE1 . GLU A 63  ? 1.5162 1.3609 1.2675 0.1877  -0.2367 -0.0561 363 GLU A OE1 
408  O OE2 . GLU A 63  ? 1.6524 1.4379 1.2656 0.2369  -0.2475 -0.0083 363 GLU A OE2 
409  N N   . PHE A 64  ? 1.0958 0.9758 1.0472 0.2445  -0.2392 -0.0448 364 PHE A N   
410  C CA  . PHE A 64  ? 1.0618 0.8885 1.0141 0.2389  -0.2060 -0.0264 364 PHE A CA  
411  C C   . PHE A 64  ? 1.0838 0.8902 1.0443 0.2813  -0.2176 -0.0113 364 PHE A C   
412  O O   . PHE A 64  ? 1.0842 0.8215 1.0109 0.2881  -0.1990 0.0157  364 PHE A O   
413  C CB  . PHE A 64  ? 0.9463 0.7979 0.9607 0.2072  -0.1787 -0.0497 364 PHE A CB  
414  C CG  . PHE A 64  ? 0.9620 0.7601 0.9718 0.2026  -0.1490 -0.0370 364 PHE A CG  
415  C CD1 . PHE A 64  ? 0.9774 0.7649 1.0145 0.2308  -0.1502 -0.0366 364 PHE A CD1 
416  C CD2 . PHE A 64  ? 0.9588 0.7193 0.9411 0.1712  -0.1217 -0.0294 364 PHE A CD2 
417  C CE1 . PHE A 64  ? 0.9731 0.7099 1.0072 0.2249  -0.1246 -0.0320 364 PHE A CE1 
418  C CE2 . PHE A 64  ? 0.9649 0.6822 0.9480 0.1655  -0.0993 -0.0247 364 PHE A CE2 
419  C CZ  . PHE A 64  ? 0.9455 0.6484 0.9528 0.1912  -0.1008 -0.0273 364 PHE A CZ  
420  N N   . LEU A 65  ? 1.0760 0.9429 1.0903 0.3087  -0.2465 -0.0308 365 LEU A N   
421  C CA  . LEU A 65  ? 1.1213 0.9746 1.1501 0.3555  -0.2607 -0.0186 365 LEU A CA  
422  C C   . LEU A 65  ? 1.2266 1.0396 1.1784 0.3961  -0.2885 0.0161  365 LEU A C   
423  O O   . LEU A 65  ? 1.3029 1.0700 1.2407 0.4343  -0.2918 0.0406  365 LEU A O   
424  C CB  . LEU A 65  ? 1.0599 0.9986 1.1801 0.3748  -0.2817 -0.0516 365 LEU A CB  
425  C CG  . LEU A 65  ? 0.9853 0.9595 1.1811 0.3438  -0.2481 -0.0809 365 LEU A CG  
426  C CD1 . LEU A 65  ? 0.9549 1.0282 1.2457 0.3576  -0.2685 -0.1148 365 LEU A CD1 
427  C CD2 . LEU A 65  ? 0.9906 0.9049 1.1851 0.3486  -0.2150 -0.0716 365 LEU A CD2 
428  N N   . ALA A 66  ? 1.2821 1.1067 1.1790 0.3899  -0.3061 0.0190  366 ALA A N   
429  C CA  . ALA A 66  ? 1.3770 1.1706 1.1903 0.4322  -0.3341 0.0511  366 ALA A CA  
430  C C   . ALA A 66  ? 1.4469 1.1445 1.1717 0.4223  -0.2994 0.0954  366 ALA A C   
431  O O   . ALA A 66  ? 1.5282 1.1821 1.1731 0.4582  -0.3115 0.1322  366 ALA A O   
432  C CB  . ALA A 66  ? 1.3786 1.2398 1.1765 0.4350  -0.3741 0.0257  366 ALA A CB  
433  N N   . THR A 67  ? 1.4508 1.1185 1.1905 0.3747  -0.2561 0.0926  367 THR A N   
434  C CA  . THR A 67  ? 1.5536 1.1444 1.2271 0.3569  -0.2203 0.1278  367 THR A CA  
435  C C   . THR A 67  ? 1.6619 1.1872 1.3615 0.3448  -0.1845 0.1434  367 THR A C   
436  O O   . THR A 67  ? 1.6982 1.1571 1.3562 0.3296  -0.1528 0.1733  367 THR A O   
437  C CB  . THR A 67  ? 1.5031 1.1185 1.1700 0.3116  -0.2035 0.1086  367 THR A CB  
438  O OG1 . THR A 67  ? 1.3899 1.0461 1.1390 0.2814  -0.1942 0.0732  367 THR A OG1 
439  C CG2 . THR A 67  ? 1.5295 1.1911 1.1540 0.3233  -0.2354 0.0952  367 THR A CG2 
440  N N   . LYS A 68  ? 1.7391 1.2855 1.5113 0.3488  -0.1872 0.1193  368 LYS A N   
441  C CA  . LYS A 68  ? 1.8069 1.2870 1.5991 0.3524  -0.1633 0.1317  368 LYS A CA  
442  C C   . LYS A 68  ? 1.9418 1.3763 1.7010 0.4088  -0.1823 0.1659  368 LYS A C   
443  O O   . LYS A 68  ? 2.0316 1.5184 1.8009 0.4475  -0.2205 0.1579  368 LYS A O   
444  C CB  . LYS A 68  ? 1.7857 1.3127 1.6590 0.3347  -0.1572 0.0885  368 LYS A CB  
445  C CG  . LYS A 68  ? 1.9420 1.4092 1.8421 0.3283  -0.1303 0.0861  368 LYS A CG  
446  C CD  . LYS A 68  ? 1.9233 1.4352 1.8936 0.3278  -0.1277 0.0453  368 LYS A CD  
447  C CE  . LYS A 68  ? 2.0006 1.4444 1.9883 0.3344  -0.1075 0.0423  368 LYS A CE  
448  N NZ  . LYS A 68  ? 2.0629 1.4488 2.0289 0.2941  -0.0797 0.0485  368 LYS A NZ  
449  N N   . ALA A 69  ? 1.9393 1.2770 1.6579 0.4146  -0.1569 0.2060  369 ALA A N   
450  C CA  . ALA A 69  ? 1.8901 1.1698 1.5613 0.4698  -0.1709 0.2489  369 ALA A CA  
451  C C   . ALA A 69  ? 1.9422 1.1069 1.5964 0.4626  -0.1306 0.2847  369 ALA A C   
452  O O   . ALA A 69  ? 2.0328 1.1417 1.6910 0.5049  -0.1357 0.3045  369 ALA A O   
453  C CB  . ALA A 69  ? 1.8795 1.1745 1.4666 0.4937  -0.1936 0.2766  369 ALA A CB  
454  N N   . ARG A 74  ? 2.1464 1.1617 2.0437 0.3007  -0.0089 0.1580  374 ARG A N   
455  C CA  . ARG A 74  ? 2.2187 1.2204 2.0705 0.2733  0.0076  0.1941  374 ARG A CA  
456  C C   . ARG A 74  ? 2.1737 1.2024 2.0554 0.2146  0.0263  0.1643  374 ARG A C   
457  O O   . ARG A 74  ? 2.1261 1.2186 2.0425 0.1995  0.0158  0.1194  374 ARG A O   
458  C CB  . ARG A 74  ? 2.2849 1.3535 2.0888 0.2958  -0.0173 0.2118  374 ARG A CB  
459  C CG  . ARG A 74  ? 2.4632 1.4800 2.2009 0.3394  -0.0227 0.2675  374 ARG A CG  
460  C CD  . ARG A 74  ? 2.5953 1.5661 2.2779 0.3156  0.0080  0.3103  374 ARG A CD  
461  N NE  . ARG A 74  ? 2.5883 1.6296 2.2532 0.2837  0.0089  0.2984  374 ARG A NE  
462  C CZ  . ARG A 74  ? 2.5223 1.6407 2.1592 0.2995  -0.0211 0.2879  374 ARG A CZ  
463  N NH1 . ARG A 74  ? 2.5712 1.7333 2.2177 0.3390  -0.0598 0.2725  374 ARG A NH1 
464  N NH2 . ARG A 74  ? 2.4103 1.5656 2.0181 0.2736  -0.0121 0.2879  374 ARG A NH2 
465  N N   . SER A 75  ? 2.1406 1.1234 2.0072 0.1840  0.0549  0.1922  375 SER A N   
466  C CA  . SER A 75  ? 1.9827 0.9850 1.8858 0.1301  0.0731  0.1665  375 SER A CA  
467  C C   . SER A 75  ? 1.8995 0.9936 1.7896 0.1118  0.0633  0.1540  375 SER A C   
468  O O   . SER A 75  ? 1.9714 1.0974 1.8953 0.0737  0.0706  0.1263  375 SER A O   
469  C CB  . SER A 75  ? 1.9391 0.8618 1.8463 0.1028  0.1104  0.1984  375 SER A CB  
470  O OG  . SER A 75  ? 1.9891 0.8646 1.8343 0.1295  0.1229  0.2576  375 SER A OG  
471  N N   . GLN A 76  ? 1.7376 0.8734 1.5810 0.1395  0.0452  0.1717  376 GLN A N   
472  C CA  . GLN A 76  ? 1.5272 0.7434 1.3594 0.1255  0.0349  0.1571  376 GLN A CA  
473  C C   . GLN A 76  ? 1.4537 0.7234 1.3358 0.1034  0.0261  0.1080  376 GLN A C   
474  O O   . GLN A 76  ? 1.4752 0.7652 1.3777 0.1221  0.0090  0.0837  376 GLN A O   
475  C CB  . GLN A 76  ? 1.5695 0.8256 1.3589 0.1626  0.0076  0.1680  376 GLN A CB  
476  C CG  . GLN A 76  ? 1.7015 0.9663 1.5085 0.2012  -0.0188 0.1551  376 GLN A CG  
477  C CD  . GLN A 76  ? 1.7600 1.0806 1.5406 0.2344  -0.0510 0.1566  376 GLN A CD  
478  O OE1 . GLN A 76  ? 1.7985 1.1294 1.5925 0.2715  -0.0739 0.1520  376 GLN A OE1 
479  N NE2 . GLN A 76  ? 1.7525 1.1123 1.4995 0.2226  -0.0545 0.1600  376 GLN A NE2 
480  N N   . LEU A 77  ? 1.3902 0.6827 1.2916 0.0658  0.0391  0.0940  377 LEU A N   
481  C CA  . LEU A 77  ? 1.2919 0.6349 1.2283 0.0476  0.0303  0.0518  377 LEU A CA  
482  C C   . LEU A 77  ? 1.1714 0.5854 1.0918 0.0485  0.0174  0.0437  377 LEU A C   
483  O O   . LEU A 77  ? 1.1063 0.5632 1.0430 0.0490  0.0062  0.0154  377 LEU A O   
484  C CB  . LEU A 77  ? 1.3474 0.6752 1.3160 0.0101  0.0481  0.0421  377 LEU A CB  
485  C CG  . LEU A 77  ? 1.3645 0.7346 1.3657 -0.0088 0.0385  -0.0011 377 LEU A CG  
486  C CD1 . LEU A 77  ? 1.4039 0.7609 1.4206 0.0057  0.0274  -0.0320 377 LEU A CD1 
487  C CD2 . LEU A 77  ? 1.3964 0.7582 1.4334 -0.0443 0.0522  -0.0087 377 LEU A CD2 
488  N N   . VAL A 78  ? 1.1092 0.5317 0.9955 0.0492  0.0216  0.0689  378 VAL A N   
489  C CA  . VAL A 78  ? 0.9593 0.4383 0.8295 0.0498  0.0110  0.0619  378 VAL A CA  
490  C C   . VAL A 78  ? 0.9742 0.4524 0.8015 0.0781  -0.0017 0.0831  378 VAL A C   
491  O O   . VAL A 78  ? 1.0618 0.5085 0.8506 0.0831  0.0096  0.1126  378 VAL A O   
492  C CB  . VAL A 78  ? 0.9701 0.4632 0.8395 0.0232  0.0276  0.0651  378 VAL A CB  
493  C CG1 . VAL A 78  ? 1.0824 0.6228 0.9321 0.0250  0.0191  0.0590  378 VAL A CG1 
494  C CG2 . VAL A 78  ? 0.9259 0.4282 0.8383 -0.0022 0.0339  0.0421  378 VAL A CG2 
495  N N   . LEU A 79  ? 0.9456 0.4615 0.7802 0.0969  -0.0247 0.0669  379 LEU A N   
496  C CA  . LEU A 79  ? 0.9960 0.5295 0.7973 0.1234  -0.0455 0.0766  379 LEU A CA  
497  C C   . LEU A 79  ? 1.0230 0.6015 0.8122 0.1090  -0.0492 0.0638  379 LEU A C   
498  O O   . LEU A 79  ? 0.9718 0.5835 0.7933 0.0882  -0.0457 0.0406  379 LEU A O   
499  C CB  . LEU A 79  ? 0.9878 0.5460 0.8210 0.1481  -0.0678 0.0600  379 LEU A CB  
500  C CG  . LEU A 79  ? 1.0575 0.6295 0.8665 0.1855  -0.0965 0.0699  379 LEU A CG  
501  C CD1 . LEU A 79  ? 1.0494 0.6364 0.9002 0.2136  -0.1137 0.0575  379 LEU A CD1 
502  C CD2 . LEU A 79  ? 1.0922 0.7217 0.8943 0.1806  -0.1145 0.0523  379 LEU A CD2 
503  N N   . VAL A 80  ? 1.0670 0.6425 0.8050 0.1219  -0.0555 0.0792  380 VAL A N   
504  C CA  . VAL A 80  ? 1.0533 0.6624 0.7761 0.1099  -0.0577 0.0649  380 VAL A CA  
505  C C   . VAL A 80  ? 1.1055 0.7530 0.8174 0.1313  -0.0912 0.0490  380 VAL A C   
506  O O   . VAL A 80  ? 1.1327 0.7693 0.8063 0.1616  -0.1095 0.0642  380 VAL A O   
507  C CB  . VAL A 80  ? 1.1316 0.7088 0.8037 0.1049  -0.0340 0.0895  380 VAL A CB  
508  C CG1 . VAL A 80  ? 1.2053 0.8108 0.8483 0.1016  -0.0383 0.0747  380 VAL A CG1 
509  C CG2 . VAL A 80  ? 1.1196 0.6752 0.8226 0.0774  -0.0029 0.0961  380 VAL A CG2 
510  N N   . THR A 81  ? 1.1070 0.7994 0.8542 0.1155  -0.0998 0.0179  381 THR A N   
511  C CA  . THR A 81  ? 1.1779 0.9119 0.9239 0.1284  -0.1314 -0.0044 381 THR A CA  
512  C C   . THR A 81  ? 1.1696 0.9196 0.9095 0.1069  -0.1261 -0.0254 381 THR A C   
513  O O   . THR A 81  ? 1.1342 0.8656 0.8730 0.0858  -0.0986 -0.0202 381 THR A O   
514  C CB  . THR A 81  ? 1.1491 0.9254 0.9623 0.1326  -0.1494 -0.0261 381 THR A CB  
515  O OG1 . THR A 81  ? 1.0745 0.8635 0.9385 0.1027  -0.1276 -0.0410 381 THR A OG1 
516  C CG2 . THR A 81  ? 1.1748 0.9320 0.9934 0.1592  -0.1550 -0.0074 381 THR A CG2 
517  N N   . LYS A 82  ? 1.1815 0.9658 0.9180 0.1149  -0.1549 -0.0507 382 LYS A N   
518  C CA  . LYS A 82  ? 1.0965 0.8965 0.8411 0.0939  -0.1531 -0.0788 382 LYS A CA  
519  C C   . LYS A 82  ? 0.9556 0.7767 0.7778 0.0667  -0.1405 -0.0956 382 LYS A C   
520  O O   . LYS A 82  ? 0.9031 0.7307 0.7635 0.0680  -0.1356 -0.0871 382 LYS A O   
521  C CB  . LYS A 82  ? 1.1651 0.9973 0.8904 0.1094  -0.1916 -0.1072 382 LYS A CB  
522  C CG  . LYS A 82  ? 1.2930 1.1034 0.9291 0.1272  -0.1966 -0.1028 382 LYS A CG  
523  C CD  . LYS A 82  ? 1.4183 1.2630 1.0524 0.1266  -0.2288 -0.1485 382 LYS A CD  
524  C CE  . LYS A 82  ? 1.3902 1.2405 1.0794 0.0906  -0.2134 -0.1802 382 LYS A CE  
525  N NZ  . LYS A 82  ? 1.4304 1.3220 1.1506 0.0854  -0.2498 -0.2299 382 LYS A NZ  
526  N N   . GLY A 83  ? 0.8479 0.6753 0.6882 0.0447  -0.1335 -0.1185 383 GLY A N   
527  C CA  . GLY A 83  ? 0.7886 0.6266 0.6919 0.0186  -0.1153 -0.1293 383 GLY A CA  
528  C C   . GLY A 83  ? 0.7953 0.6792 0.7632 0.0091  -0.1341 -0.1612 383 GLY A C   
529  O O   . GLY A 83  ? 0.7814 0.6766 0.8053 -0.0101 -0.1154 -0.1649 383 GLY A O   
530  N N   . PHE A 84  ? 0.8146 0.7270 0.7763 0.0221  -0.1698 -0.1849 384 PHE A N   
531  C CA  . PHE A 84  ? 0.8570 0.8207 0.8923 0.0097  -0.1900 -0.2214 384 PHE A CA  
532  C C   . PHE A 84  ? 0.8534 0.8058 0.9330 -0.0266 -0.1639 -0.2382 384 PHE A C   
533  O O   . PHE A 84  ? 0.9033 0.8180 0.9426 -0.0339 -0.1530 -0.2401 384 PHE A O   
534  C CB  . PHE A 84  ? 0.8711 0.8717 0.9587 0.0211  -0.1946 -0.2139 384 PHE A CB  
535  C CG  . PHE A 84  ? 1.0000 0.9950 1.0320 0.0605  -0.2189 -0.1930 384 PHE A CG  
536  C CD1 . PHE A 84  ? 1.0819 1.1138 1.1046 0.0857  -0.2645 -0.2119 384 PHE A CD1 
537  C CD2 . PHE A 84  ? 1.0075 0.9558 0.9916 0.0725  -0.1967 -0.1545 384 PHE A CD2 
538  C CE1 . PHE A 84  ? 1.1360 1.1533 1.0971 0.1254  -0.2847 -0.1868 384 PHE A CE1 
539  C CE2 . PHE A 84  ? 1.0491 0.9812 0.9810 0.1071  -0.2143 -0.1319 384 PHE A CE2 
540  C CZ  . PHE A 84  ? 1.1248 1.0886 1.0418 0.1350  -0.2568 -0.1450 384 PHE A CZ  
541  N N   . ASN A 85  ? 0.8520 0.8326 1.0123 -0.0474 -0.1491 -0.2467 385 ASN A N   
542  C CA  . ASN A 85  ? 0.8561 0.8224 1.0636 -0.0820 -0.1204 -0.2582 385 ASN A CA  
543  C C   . ASN A 85  ? 0.8667 0.7820 1.0446 -0.0888 -0.0780 -0.2226 385 ASN A C   
544  O O   . ASN A 85  ? 0.8727 0.7737 1.0892 -0.1132 -0.0484 -0.2218 385 ASN A O   
545  C CB  . ASN A 85  ? 0.8466 0.8616 1.1527 -0.1024 -0.1119 -0.2747 385 ASN A CB  
546  C CG  . ASN A 85  ? 0.9066 0.9867 1.2665 -0.0985 -0.1547 -0.3145 385 ASN A CG  
547  O OD1 . ASN A 85  ? 0.9729 1.0581 1.2881 -0.0800 -0.1938 -0.3319 385 ASN A OD1 
548  N ND2 . ASN A 85  ? 0.9281 1.0621 1.3836 -0.1137 -0.1480 -0.3297 385 ASN A ND2 
549  N N   . LEU A 86  ? 0.8305 0.7199 0.9443 -0.0673 -0.0745 -0.1930 386 LEU A N   
550  C CA  . LEU A 86  ? 0.8567 0.7016 0.9388 -0.0716 -0.0428 -0.1658 386 LEU A CA  
551  C C   . LEU A 86  ? 0.8895 0.6985 0.9271 -0.0713 -0.0433 -0.1708 386 LEU A C   
552  O O   . LEU A 86  ? 0.9070 0.7201 0.9104 -0.0585 -0.0672 -0.1846 386 LEU A O   
553  C CB  . LEU A 86  ? 0.8857 0.7212 0.9315 -0.0533 -0.0369 -0.1363 386 LEU A CB  
554  C CG  . LEU A 86  ? 0.8728 0.7358 0.9543 -0.0495 -0.0315 -0.1306 386 LEU A CG  
555  C CD1 . LEU A 86  ? 0.8435 0.6825 0.8876 -0.0380 -0.0187 -0.1048 386 LEU A CD1 
556  C CD2 . LEU A 86  ? 0.8693 0.7489 1.0091 -0.0709 -0.0089 -0.1389 386 LEU A CD2 
557  N N   . PHE A 87  ? 0.8721 0.6454 0.9051 -0.0811 -0.0156 -0.1577 387 PHE A N   
558  C CA  . PHE A 87  ? 0.8425 0.5806 0.8391 -0.0781 -0.0108 -0.1615 387 PHE A CA  
559  C C   . PHE A 87  ? 0.8131 0.5418 0.7557 -0.0576 -0.0097 -0.1376 387 PHE A C   
560  O O   . PHE A 87  ? 0.8342 0.5403 0.7636 -0.0548 0.0100  -0.1177 387 PHE A O   
561  C CB  . PHE A 87  ? 0.8482 0.5515 0.8675 -0.0933 0.0176  -0.1554 387 PHE A CB  
562  C CG  . PHE A 87  ? 0.8587 0.5630 0.9351 -0.1182 0.0198  -0.1828 387 PHE A CG  
563  C CD1 . PHE A 87  ? 0.8727 0.5764 0.9551 -0.1245 0.0000  -0.2213 387 PHE A CD1 
564  C CD2 . PHE A 87  ? 0.8447 0.5499 0.9689 -0.1361 0.0435  -0.1717 387 PHE A CD2 
565  C CE1 . PHE A 87  ? 0.9154 0.6209 1.0603 -0.1513 0.0011  -0.2512 387 PHE A CE1 
566  C CE2 . PHE A 87  ? 0.9207 0.6261 1.1075 -0.1634 0.0502  -0.1967 387 PHE A CE2 
567  C CZ  . PHE A 87  ? 0.9268 0.6329 1.1289 -0.1727 0.0278  -0.2380 387 PHE A CZ  
568  N N   . CYS A 88  ? 0.7873 0.5351 0.7037 -0.0430 -0.0306 -0.1384 388 CYS A N   
569  C CA  . CYS A 88  ? 0.7803 0.5183 0.6516 -0.0266 -0.0266 -0.1146 388 CYS A CA  
570  C C   . CYS A 88  ? 0.8099 0.5560 0.6389 -0.0098 -0.0485 -0.1218 388 CYS A C   
571  O O   . CYS A 88  ? 0.8178 0.5867 0.6574 -0.0077 -0.0734 -0.1437 388 CYS A O   
572  C CB  . CYS A 88  ? 0.8379 0.5821 0.7242 -0.0254 -0.0191 -0.0914 388 CYS A CB  
573  S SG  . CYS A 88  ? 0.7924 0.5670 0.7011 -0.0175 -0.0400 -0.0940 388 CYS A SG  
574  N N   . LYS A 89  ? 0.8854 0.6146 0.6668 0.0032  -0.0386 -0.1026 389 LYS A N   
575  C CA  . LYS A 89  ? 1.0051 0.7343 0.7313 0.0229  -0.0534 -0.1015 389 LYS A CA  
576  C C   . LYS A 89  ? 1.0400 0.7762 0.7633 0.0353  -0.0653 -0.0808 389 LYS A C   
577  O O   . LYS A 89  ? 1.1033 0.8498 0.7976 0.0536  -0.0899 -0.0847 389 LYS A O   
578  C CB  . LYS A 89  ? 1.0807 0.7868 0.7576 0.0309  -0.0301 -0.0880 389 LYS A CB  
579  C CG  . LYS A 89  ? 1.1410 0.8389 0.8030 0.0291  -0.0251 -0.1153 389 LYS A CG  
580  C CD  . LYS A 89  ? 1.2078 0.8879 0.8294 0.0382  0.0037  -0.1036 389 LYS A CD  
581  C CE  . LYS A 89  ? 1.2560 0.9250 0.8656 0.0393  0.0095  -0.1343 389 LYS A CE  
582  N NZ  . LYS A 89  ? 1.3048 0.9625 0.8753 0.0519  0.0396  -0.1236 389 LYS A NZ  
583  N N   . TYR A 90  ? 0.9879 0.7175 0.7406 0.0278  -0.0495 -0.0606 390 TYR A N   
584  C CA  . TYR A 90  ? 1.0012 0.7268 0.7523 0.0396  -0.0553 -0.0405 390 TYR A CA  
585  C C   . TYR A 90  ? 0.9366 0.6707 0.7423 0.0266  -0.0481 -0.0406 390 TYR A C   
586  O O   . TYR A 90  ? 0.9902 0.7250 0.8192 0.0104  -0.0329 -0.0455 390 TYR A O   
587  C CB  . TYR A 90  ? 1.0164 0.7108 0.7258 0.0470  -0.0359 -0.0109 390 TYR A CB  
588  C CG  . TYR A 90  ? 1.0763 0.7571 0.7178 0.0637  -0.0352 -0.0034 390 TYR A CG  
589  C CD1 . TYR A 90  ? 1.1225 0.8107 0.7244 0.0867  -0.0632 -0.0084 390 TYR A CD1 
590  C CD2 . TYR A 90  ? 1.1015 0.7657 0.7168 0.0591  -0.0063 0.0079  390 TYR A CD2 
591  C CE1 . TYR A 90  ? 1.1691 0.8442 0.6964 0.1053  -0.0625 -0.0019 390 TYR A CE1 
592  C CE2 . TYR A 90  ? 1.1209 0.7728 0.6678 0.0758  -0.0001 0.0146  390 TYR A CE2 
593  C CZ  . TYR A 90  ? 1.1824 0.8377 0.6794 0.0995  -0.0284 0.0099  390 TYR A CZ  
594  O OH  . TYR A 90  ? 1.2666 0.9088 0.6829 0.1201  -0.0236 0.0168  390 TYR A OH  
595  N N   . ILE A 91  ? 0.8644 0.6038 0.6856 0.0373  -0.0593 -0.0353 391 ILE A N   
596  C CA  . ILE A 91  ? 0.8308 0.5707 0.6895 0.0301  -0.0489 -0.0325 391 ILE A CA  
597  C C   . ILE A 91  ? 0.8445 0.5533 0.6864 0.0397  -0.0427 -0.0106 391 ILE A C   
598  O O   . ILE A 91  ? 0.9511 0.6480 0.7713 0.0596  -0.0549 0.0006  391 ILE A O   
599  C CB  . ILE A 91  ? 0.8175 0.5903 0.7203 0.0337  -0.0620 -0.0498 391 ILE A CB  
600  C CG1 . ILE A 91  ? 0.8290 0.6293 0.7594 0.0189  -0.0638 -0.0715 391 ILE A CG1 
601  C CG2 . ILE A 91  ? 0.8184 0.5887 0.7489 0.0308  -0.0489 -0.0476 391 ILE A CG2 
602  C CD1 . ILE A 91  ? 0.8595 0.7013 0.8364 0.0240  -0.0812 -0.0911 391 ILE A CD1 
603  N N   . TYR A 92  ? 0.7736 0.4678 0.6267 0.0261  -0.0245 -0.0050 392 TYR A N   
604  C CA  . TYR A 92  ? 0.7764 0.4401 0.6286 0.0291  -0.0171 0.0094  392 TYR A CA  
605  C C   . TYR A 92  ? 0.7831 0.4533 0.6692 0.0312  -0.0206 -0.0037 392 TYR A C   
606  O O   . TYR A 92  ? 0.7704 0.4532 0.6759 0.0186  -0.0131 -0.0159 392 TYR A O   
607  C CB  . TYR A 92  ? 0.7325 0.3841 0.5841 0.0117  0.0023  0.0167  392 TYR A CB  
608  C CG  . TYR A 92  ? 0.7074 0.3473 0.5270 0.0108  0.0145  0.0325  392 TYR A CG  
609  C CD1 . TYR A 92  ? 0.7193 0.3585 0.4985 0.0256  0.0069  0.0381  392 TYR A CD1 
610  C CD2 . TYR A 92  ? 0.6939 0.3282 0.5258 -0.0045 0.0342  0.0391  392 TYR A CD2 
611  C CE1 . TYR A 92  ? 0.7396 0.3689 0.4835 0.0261  0.0227  0.0507  392 TYR A CE1 
612  C CE2 . TYR A 92  ? 0.7050 0.3332 0.5130 -0.0056 0.0518  0.0527  392 TYR A CE2 
613  C CZ  . TYR A 92  ? 0.7431 0.3672 0.5032 0.0102  0.0479  0.0588  392 TYR A CZ  
614  O OH  . TYR A 92  ? 0.7974 0.4154 0.5321 0.0092  0.0709  0.0714  392 TYR A OH  
615  N N   . HIS A 93  ? 0.7923 0.4539 0.6817 0.0510  -0.0319 -0.0012 393 HIS A N   
616  C CA  . HIS A 93  ? 0.8048 0.4719 0.7259 0.0573  -0.0328 -0.0157 393 HIS A CA  
617  C C   . HIS A 93  ? 0.7807 0.4055 0.7035 0.0538  -0.0224 -0.0110 393 HIS A C   
618  O O   . HIS A 93  ? 0.8346 0.4203 0.7433 0.0645  -0.0223 0.0071  393 HIS A O   
619  C CB  . HIS A 93  ? 0.8189 0.4999 0.7525 0.0839  -0.0504 -0.0184 393 HIS A CB  
620  C CG  . HIS A 93  ? 0.8105 0.5324 0.7461 0.0871  -0.0657 -0.0252 393 HIS A CG  
621  N ND1 . HIS A 93  ? 0.7677 0.5366 0.7428 0.0814  -0.0674 -0.0469 393 HIS A ND1 
622  C CD2 . HIS A 93  ? 0.8398 0.5615 0.7428 0.0942  -0.0790 -0.0155 393 HIS A CD2 
623  C CE1 . HIS A 93  ? 0.7894 0.5859 0.7638 0.0829  -0.0840 -0.0529 393 HIS A CE1 
624  N NE2 . HIS A 93  ? 0.8239 0.5930 0.7505 0.0925  -0.0933 -0.0356 393 HIS A NE2 
625  N N   . VAL A 94  ? 0.7623 0.3928 0.7011 0.0391  -0.0138 -0.0276 394 VAL A N   
626  C CA  . VAL A 94  ? 0.8396 0.4339 0.7883 0.0344  -0.0076 -0.0332 394 VAL A CA  
627  C C   . VAL A 94  ? 0.8181 0.4001 0.7821 0.0561  -0.0123 -0.0449 394 VAL A C   
628  O O   . VAL A 94  ? 0.7766 0.3920 0.7531 0.0638  -0.0136 -0.0630 394 VAL A O   
629  C CB  . VAL A 94  ? 0.8428 0.4531 0.7994 0.0148  -0.0026 -0.0516 394 VAL A CB  
630  C CG1 . VAL A 94  ? 0.8652 0.4469 0.8376 0.0114  -0.0016 -0.0706 394 VAL A CG1 
631  C CG2 . VAL A 94  ? 0.8355 0.4536 0.7850 -0.0033 0.0026  -0.0391 394 VAL A CG2 
632  N N   . LEU A 95  ? 0.8498 0.3823 0.8134 0.0675  -0.0119 -0.0325 395 LEU A N   
633  C CA  . LEU A 95  ? 0.9048 0.4190 0.8848 0.0930  -0.0161 -0.0429 395 LEU A CA  
634  C C   . LEU A 95  ? 0.9371 0.4168 0.9330 0.0829  -0.0077 -0.0663 395 LEU A C   
635  O O   . LEU A 95  ? 0.9725 0.4006 0.9704 0.0714  -0.0008 -0.0570 395 LEU A O   
636  C CB  . LEU A 95  ? 0.9292 0.4042 0.8964 0.1183  -0.0224 -0.0144 395 LEU A CB  
637  C CG  . LEU A 95  ? 0.9204 0.4196 0.8591 0.1251  -0.0327 0.0101  395 LEU A CG  
638  C CD1 . LEU A 95  ? 0.9931 0.4515 0.9093 0.1570  -0.0416 0.0393  395 LEU A CD1 
639  C CD2 . LEU A 95  ? 0.8827 0.4501 0.8374 0.1305  -0.0450 -0.0084 395 LEU A CD2 
640  N N   . TRP A 96  ? 0.9378 0.4460 0.9450 0.0870  -0.0070 -0.0977 396 TRP A N   
641  C CA  . TRP A 96  ? 1.0141 0.4898 1.0330 0.0851  -0.0026 -0.1275 396 TRP A CA  
642  C C   . TRP A 96  ? 1.0818 0.5118 1.1162 0.1144  -0.0024 -0.1299 396 TRP A C   
643  O O   . TRP A 96  ? 1.0895 0.5446 1.1344 0.1403  -0.0027 -0.1433 396 TRP A O   
644  C CB  . TRP A 96  ? 0.9866 0.5078 0.9999 0.0841  0.0001  -0.1595 396 TRP A CB  
645  C CG  . TRP A 96  ? 0.9338 0.4967 0.9295 0.0615  -0.0005 -0.1548 396 TRP A CG  
646  C CD1 . TRP A 96  ? 0.8337 0.4408 0.8212 0.0604  0.0008  -0.1377 396 TRP A CD1 
647  C CD2 . TRP A 96  ? 0.9276 0.4913 0.9150 0.0393  -0.0041 -0.1705 396 TRP A CD2 
648  N NE1 . TRP A 96  ? 0.8241 0.4522 0.7955 0.0409  0.0006  -0.1376 396 TRP A NE1 
649  C CE2 . TRP A 96  ? 0.8520 0.4590 0.8229 0.0294  -0.0040 -0.1571 396 TRP A CE2 
650  C CE3 . TRP A 96  ? 0.9720 0.5055 0.9685 0.0274  -0.0093 -0.1970 396 TRP A CE3 
651  C CZ2 . TRP A 96  ? 0.8717 0.4949 0.8327 0.0127  -0.0101 -0.1659 396 TRP A CZ2 
652  C CZ3 . TRP A 96  ? 0.9513 0.5076 0.9417 0.0079  -0.0177 -0.2098 396 TRP A CZ3 
653  C CH2 . TRP A 96  ? 0.9246 0.5264 0.8961 0.0030  -0.0186 -0.1928 396 TRP A CH2 
654  N N   . HIS A 97  ? 1.1746 0.5362 1.2144 0.1105  0.0010  -0.1165 397 HIS A N   
655  C CA  . HIS A 97  ? 1.2889 0.5913 1.3445 0.1368  0.0034  -0.1223 397 HIS A CA  
656  C C   . HIS A 97  ? 1.3608 0.6440 1.4315 0.1292  0.0077  -0.1704 397 HIS A C   
657  O O   . HIS A 97  ? 1.3759 0.6626 1.4468 0.0970  0.0080  -0.1897 397 HIS A O   
658  C CB  . HIS A 97  ? 1.3349 0.5629 1.3869 0.1359  0.0093  -0.0848 397 HIS A CB  
659  C CG  . HIS A 97  ? 1.3063 0.5537 1.3308 0.1451  0.0041  -0.0400 397 HIS A CG  
660  N ND1 . HIS A 97  ? 1.2939 0.5491 1.3085 0.1854  -0.0080 -0.0190 397 HIS A ND1 
661  C CD2 . HIS A 97  ? 1.2513 0.5144 1.2553 0.1208  0.0081  -0.0157 397 HIS A CD2 
662  C CE1 . HIS A 97  ? 1.2576 0.5297 1.2407 0.1845  -0.0131 0.0155  397 HIS A CE1 
663  N NE2 . HIS A 97  ? 1.2494 0.5247 1.2245 0.1456  -0.0012 0.0182  397 HIS A NE2 
664  N N   . SER A 98  ? 1.4867 0.7492 1.5709 0.1618  0.0096  -0.1909 398 SER A N   
665  C CA  . SER A 98  ? 1.5325 0.7892 1.6233 0.1646  0.0135  -0.2430 398 SER A CA  
666  C C   . SER A 98  ? 1.5654 0.7404 1.6729 0.1470  0.0166  -0.2658 398 SER A C   
667  O O   . SER A 98  ? 1.5632 0.7411 1.6694 0.1370  0.0152  -0.3140 398 SER A O   
668  C CB  . SER A 98  ? 1.5708 0.8448 1.6729 0.2081  0.0177  -0.2585 398 SER A CB  
669  O OG  . SER A 98  ? 1.6825 0.9009 1.8034 0.2397  0.0168  -0.2348 398 SER A OG  
670  N N   . GLU A 99  ? 1.6085 0.7128 1.7298 0.1404  0.0213  -0.2327 399 GLU A N   
671  C CA  . GLU A 99  ? 1.7216 0.7374 1.8697 0.1245  0.0285  -0.2536 399 GLU A CA  
672  C C   . GLU A 99  ? 1.7362 0.7500 1.8981 0.0722  0.0288  -0.2577 399 GLU A C   
673  O O   . GLU A 99  ? 1.7647 0.7033 1.9560 0.0511  0.0395  -0.2523 399 GLU A O   
674  C CB  . GLU A 99  ? 1.7827 0.7107 1.9413 0.1499  0.0388  -0.2143 399 GLU A CB  
675  C CG  . GLU A 99  ? 1.8175 0.7216 1.9818 0.2030  0.0385  -0.2265 399 GLU A CG  
676  C CD  . GLU A 99  ? 1.9385 0.7383 2.1149 0.2327  0.0480  -0.1939 399 GLU A CD  
677  O OE1 . GLU A 99  ? 1.9984 0.7026 2.1968 0.2129  0.0612  -0.1987 399 GLU A OE1 
678  O OE2 . GLU A 99  ? 1.8968 0.7094 2.0634 0.2793  0.0417  -0.1634 399 GLU A OE2 
679  N N   . PHE A 100 ? 1.7498 0.8451 1.8961 0.0514  0.0182  -0.2699 400 PHE A N   
680  C CA  . PHE A 100 ? 1.7387 0.8493 1.9026 0.0063  0.0161  -0.2708 400 PHE A CA  
681  C C   . PHE A 100 ? 1.6108 0.7882 1.7648 -0.0077 -0.0016 -0.3191 400 PHE A C   
682  O O   . PHE A 100 ? 1.5878 0.8169 1.7067 0.0164  -0.0076 -0.3306 400 PHE A O   
683  C CB  . PHE A 100 ? 1.7484 0.8936 1.8962 -0.0008 0.0218  -0.2148 400 PHE A CB  
684  C CG  . PHE A 100 ? 1.8945 0.9731 2.0423 0.0114  0.0387  -0.1630 400 PHE A CG  
685  C CD1 . PHE A 100 ? 1.9758 0.9845 2.1556 -0.0159 0.0565  -0.1480 400 PHE A CD1 
686  C CD2 . PHE A 100 ? 1.9079 0.9937 2.0242 0.0510  0.0370  -0.1296 400 PHE A CD2 
687  C CE1 . PHE A 100 ? 2.0342 0.9753 2.2031 -0.0012 0.0750  -0.0954 400 PHE A CE1 
688  C CE2 . PHE A 100 ? 1.9616 0.9853 2.0680 0.0680  0.0489  -0.0812 400 PHE A CE2 
689  C CZ  . PHE A 100 ? 1.9872 0.9355 2.1141 0.0432  0.0693  -0.0615 400 PHE A CZ  
690  N N   . PRO A 101 ? 1.5454 0.7293 1.7294 -0.0458 -0.0102 -0.3452 401 PRO A N   
691  C CA  . PRO A 101 ? 1.5085 0.7621 1.6761 -0.0550 -0.0318 -0.3858 401 PRO A CA  
692  C C   . PRO A 101 ? 1.4298 0.7566 1.5649 -0.0506 -0.0332 -0.3472 401 PRO A C   
693  O O   . PRO A 101 ? 1.3487 0.6760 1.4970 -0.0634 -0.0226 -0.3030 401 PRO A O   
694  C CB  . PRO A 101 ? 1.5188 0.7609 1.7403 -0.0968 -0.0423 -0.4187 401 PRO A CB  
695  C CG  . PRO A 101 ? 1.5473 0.7082 1.8178 -0.1151 -0.0187 -0.3892 401 PRO A CG  
696  C CD  . PRO A 101 ? 1.5442 0.6757 1.7811 -0.0817 0.0011  -0.3333 401 PRO A CD  
697  N N   . LYS A 102 ? 1.3970 0.7809 1.4872 -0.0319 -0.0438 -0.3646 402 LYS A N   
698  C CA  . LYS A 102 ? 1.3096 0.7530 1.3665 -0.0229 -0.0417 -0.3290 402 LYS A CA  
699  C C   . LYS A 102 ? 1.2341 0.7156 1.3074 -0.0502 -0.0512 -0.3175 402 LYS A C   
700  O O   . LYS A 102 ? 1.1656 0.6571 1.2438 -0.0560 -0.0410 -0.2746 402 LYS A O   
701  C CB  . LYS A 102 ? 1.3380 0.8217 1.3449 0.0039  -0.0439 -0.3491 402 LYS A CB  
702  C CG  . LYS A 102 ? 1.4248 0.8833 1.4232 0.0341  -0.0286 -0.3510 402 LYS A CG  
703  C CD  . LYS A 102 ? 1.5040 0.9577 1.5133 0.0455  -0.0150 -0.3022 402 LYS A CD  
704  C CE  . LYS A 102 ? 1.6311 1.0385 1.6567 0.0713  -0.0054 -0.3063 402 LYS A CE  
705  N NZ  . LYS A 102 ? 1.6082 1.0009 1.6483 0.0812  0.0005  -0.2604 402 LYS A NZ  
706  N N   . PRO A 103 ? 1.2031 0.7080 1.2891 -0.0667 -0.0719 -0.3570 403 PRO A N   
707  C CA  . PRO A 103 ? 1.1731 0.7181 1.2880 -0.0910 -0.0815 -0.3474 403 PRO A CA  
708  C C   . PRO A 103 ? 1.2083 0.7233 1.3725 -0.1145 -0.0617 -0.3109 403 PRO A C   
709  O O   . PRO A 103 ? 1.3325 0.8835 1.5094 -0.1255 -0.0588 -0.2854 403 PRO A O   
710  C CB  . PRO A 103 ? 1.2059 0.7672 1.3429 -0.1055 -0.1095 -0.4057 403 PRO A CB  
711  C CG  . PRO A 103 ? 1.2304 0.7779 1.3176 -0.0791 -0.1163 -0.4431 403 PRO A CG  
712  C CD  . PRO A 103 ? 1.2330 0.7283 1.3101 -0.0616 -0.0886 -0.4155 403 PRO A CD  
713  N N   . GLN A 104 ? 1.3054 0.7515 1.4942 -0.1195 -0.0455 -0.3066 404 GLN A N   
714  C CA  . GLN A 104 ? 1.3246 0.7324 1.5500 -0.1389 -0.0215 -0.2674 404 GLN A CA  
715  C C   . GLN A 104 ? 1.2230 0.6295 1.4066 -0.1168 -0.0047 -0.2134 404 GLN A C   
716  O O   . GLN A 104 ? 1.2250 0.6276 1.4209 -0.1293 0.0127  -0.1765 404 GLN A O   
717  C CB  . GLN A 104 ? 1.4413 0.7650 1.7042 -0.1504 -0.0070 -0.2749 404 GLN A CB  
718  C CG  . GLN A 104 ? 1.5600 0.8762 1.8916 -0.1885 -0.0151 -0.3185 404 GLN A CG  
719  C CD  . GLN A 104 ? 1.6838 0.9083 2.0632 -0.2075 0.0073  -0.3168 404 GLN A CD  
720  O OE1 . GLN A 104 ? 1.7235 0.8837 2.0791 -0.1878 0.0287  -0.2795 404 GLN A OE1 
721  N NE2 . GLN A 104 ? 1.7091 0.9271 2.1597 -0.2458 0.0013  -0.3579 404 GLN A NE2 
722  N N   . ILE A 105 ? 1.1808 0.5896 1.3189 -0.0845 -0.0086 -0.2114 405 ILE A N   
723  C CA  . ILE A 105 ? 1.1717 0.5846 1.2747 -0.0622 0.0014  -0.1686 405 ILE A CA  
724  C C   . ILE A 105 ? 1.0985 0.5742 1.1841 -0.0664 -0.0020 -0.1522 405 ILE A C   
725  O O   . ILE A 105 ? 1.0197 0.4981 1.0934 -0.0648 0.0089  -0.1156 405 ILE A O   
726  C CB  . ILE A 105 ? 1.2335 0.6458 1.3071 -0.0290 -0.0032 -0.1789 405 ILE A CB  
727  C CG1 . ILE A 105 ? 1.4272 0.7698 1.5161 -0.0164 0.0034  -0.1856 405 ILE A CG1 
728  C CG2 . ILE A 105 ? 1.1960 0.6412 1.2386 -0.0090 -0.0006 -0.1460 405 ILE A CG2 
729  C CD1 . ILE A 105 ? 1.5181 0.8177 1.6009 -0.0016 0.0160  -0.1392 405 ILE A CD1 
730  N N   . LEU A 106 ? 1.0470 0.5699 1.1253 -0.0681 -0.0178 -0.1809 406 LEU A N   
731  C CA  . LEU A 106 ? 1.0000 0.5773 1.0645 -0.0704 -0.0221 -0.1685 406 LEU A CA  
732  C C   . LEU A 106 ? 0.9747 0.5563 1.0766 -0.0951 -0.0142 -0.1531 406 LEU A C   
733  O O   . LEU A 106 ? 0.8839 0.4791 0.9757 -0.0942 -0.0029 -0.1216 406 LEU A O   
734  C CB  . LEU A 106 ? 1.0047 0.6223 1.0523 -0.0650 -0.0413 -0.2021 406 LEU A CB  
735  C CG  . LEU A 106 ? 0.9789 0.6485 1.0065 -0.0611 -0.0471 -0.1891 406 LEU A CG  
736  C CD1 . LEU A 106 ? 0.9197 0.5933 0.9144 -0.0449 -0.0339 -0.1590 406 LEU A CD1 
737  C CD2 . LEU A 106 ? 1.0165 0.7204 1.0206 -0.0524 -0.0675 -0.2199 406 LEU A CD2 
738  N N   . LYS A 107 ? 0.9663 0.5371 1.1150 -0.1178 -0.0185 -0.1783 407 LYS A N   
739  C CA  . LYS A 107 ? 0.9725 0.5619 1.1682 -0.1433 -0.0101 -0.1695 407 LYS A CA  
740  C C   . LYS A 107 ? 0.9928 0.5439 1.1851 -0.1460 0.0199  -0.1245 407 LYS A C   
741  O O   . LYS A 107 ? 0.9801 0.5563 1.1792 -0.1526 0.0332  -0.1011 407 LYS A O   
742  C CB  . LYS A 107 ? 1.0240 0.6113 1.2825 -0.1709 -0.0203 -0.2088 407 LYS A CB  
743  C CG  . LYS A 107 ? 1.0713 0.6968 1.3909 -0.1978 -0.0124 -0.2037 407 LYS A CG  
744  C CD  . LYS A 107 ? 1.1547 0.7450 1.5501 -0.2341 0.0041  -0.2142 407 LYS A CD  
745  C CE  . LYS A 107 ? 1.1590 0.7687 1.6048 -0.2571 0.0327  -0.1862 407 LYS A CE  
746  N NZ  . LYS A 107 ? 1.1531 0.8463 1.6466 -0.2663 0.0130  -0.2104 407 LYS A NZ  
747  N N   . HIS A 108 ? 1.0390 0.5291 1.2148 -0.1363 0.0303  -0.1121 408 HIS A N   
748  C CA  . HIS A 108 ? 1.0614 0.5072 1.2256 -0.1350 0.0573  -0.0681 408 HIS A CA  
749  C C   . HIS A 108 ? 0.9742 0.4431 1.0807 -0.1086 0.0563  -0.0402 408 HIS A C   
750  O O   . HIS A 108 ? 0.9469 0.4166 1.0382 -0.1092 0.0739  -0.0083 408 HIS A O   
751  C CB  . HIS A 108 ? 1.1280 0.4956 1.3007 -0.1333 0.0678  -0.0640 408 HIS A CB  
752  C CG  . HIS A 108 ? 1.2388 0.5729 1.4776 -0.1667 0.0766  -0.0867 408 HIS A CG  
753  N ND1 . HIS A 108 ? 1.3048 0.6635 1.6000 -0.2014 0.0893  -0.0901 408 HIS A ND1 
754  C CD2 . HIS A 108 ? 1.2828 0.5590 1.5470 -0.1715 0.0751  -0.1104 408 HIS A CD2 
755  C CE1 . HIS A 108 ? 1.2590 0.5791 1.6153 -0.2293 0.0941  -0.1162 408 HIS A CE1 
756  N NE2 . HIS A 108 ? 1.2995 0.5659 1.6351 -0.2113 0.0851  -0.1298 408 HIS A NE2 
757  N N   . ALA A 109 ? 0.9275 0.4171 1.0038 -0.0863 0.0368  -0.0548 409 ALA A N   
758  C CA  . ALA A 109 ? 0.9097 0.4224 0.9419 -0.0647 0.0339  -0.0349 409 ALA A CA  
759  C C   . ALA A 109 ? 0.8995 0.4603 0.9290 -0.0731 0.0361  -0.0291 409 ALA A C   
760  O O   . ALA A 109 ? 0.8267 0.3940 0.8269 -0.0636 0.0428  -0.0059 409 ALA A O   
761  C CB  . ALA A 109 ? 0.8800 0.4083 0.8946 -0.0443 0.0175  -0.0546 409 ALA A CB  
762  N N   . MET A 110 ? 0.8803 0.4745 0.9404 -0.0884 0.0285  -0.0522 410 MET A N   
763  C CA  . MET A 110 ? 0.8388 0.4768 0.9051 -0.0940 0.0306  -0.0477 410 MET A CA  
764  C C   . MET A 110 ? 0.8738 0.5002 0.9568 -0.1075 0.0557  -0.0231 410 MET A C   
765  O O   . MET A 110 ? 0.9657 0.5997 1.0208 -0.0987 0.0668  -0.0019 410 MET A O   
766  C CB  . MET A 110 ? 0.8362 0.5141 0.9339 -0.1032 0.0133  -0.0778 410 MET A CB  
767  C CG  . MET A 110 ? 0.8176 0.5171 0.8837 -0.0857 -0.0071 -0.0960 410 MET A CG  
768  S SD  . MET A 110 ? 0.8243 0.5450 0.8452 -0.0658 -0.0047 -0.0759 410 MET A SD  
769  C CE  . MET A 110 ? 0.7605 0.5151 0.8038 -0.0718 0.0015  -0.0646 410 MET A CE  
770  N N   . LYS A 111 ? 0.9502 0.5560 1.0786 -0.1294 0.0675  -0.0267 411 LYS A N   
771  C CA  . LYS A 111 ? 0.9561 0.5508 1.1046 -0.1447 0.0987  -0.0012 411 LYS A CA  
772  C C   . LYS A 111 ? 0.8911 0.4525 0.9780 -0.1254 0.1153  0.0355  411 LYS A C   
773  O O   . LYS A 111 ? 0.8186 0.3909 0.8935 -0.1256 0.1370  0.0563  411 LYS A O   
774  C CB  . LYS A 111 ? 1.0790 0.6381 1.2832 -0.1717 0.1129  -0.0071 411 LYS A CB  
775  C CG  . LYS A 111 ? 1.1674 0.7200 1.4113 -0.1955 0.1514  0.0161  411 LYS A CG  
776  C CD  . LYS A 111 ? 1.1968 0.7519 1.5300 -0.2317 0.1559  -0.0098 411 LYS A CD  
777  C CE  . LYS A 111 ? 1.2430 0.8087 1.6306 -0.2586 0.1966  0.0095  411 LYS A CE  
778  N NZ  . LYS A 111 ? 1.3316 0.8303 1.6757 -0.2547 0.2377  0.0585  411 LYS A NZ  
779  N N   . GLU A 112 ? 0.9000 0.4243 0.9484 -0.1064 0.1038  0.0407  412 GLU A N   
780  C CA  . GLU A 112 ? 0.9498 0.4419 0.9402 -0.0848 0.1128  0.0730  412 GLU A CA  
781  C C   . GLU A 112 ? 0.9136 0.4461 0.8640 -0.0680 0.1026  0.0732  412 GLU A C   
782  O O   . GLU A 112 ? 0.9173 0.4439 0.8302 -0.0598 0.1182  0.0964  412 GLU A O   
788  N N   . CYS A 113 ? 0.8718 0.4400 0.8277 -0.0626 0.0783  0.0472  413 CYS A N   
789  C CA  . CYS A 113 ? 0.8534 0.4568 0.7830 -0.0510 0.0690  0.0426  413 CYS A CA  
790  C C   . CYS A 113 ? 0.8619 0.4882 0.7977 -0.0597 0.0874  0.0492  413 CYS A C   
791  O O   . CYS A 113 ? 0.8985 0.5259 0.7964 -0.0487 0.0949  0.0609  413 CYS A O   
792  C CB  . CYS A 113 ? 0.8227 0.4555 0.7661 -0.0490 0.0481  0.0168  413 CYS A CB  
793  S SG  . CYS A 113 ? 0.8457 0.4665 0.7729 -0.0308 0.0298  0.0085  413 CYS A SG  
794  N N   . LEU A 114 ? 0.8044 0.4501 0.7901 -0.0783 0.0946  0.0395  414 LEU A N   
795  C CA  . LEU A 114 ? 0.7846 0.4609 0.7896 -0.0848 0.1121  0.0423  414 LEU A CA  
796  C C   . LEU A 114 ? 0.8454 0.4995 0.8360 -0.0886 0.1459  0.0693  414 LEU A C   
797  O O   . LEU A 114 ? 0.8839 0.5590 0.8702 -0.0859 0.1648  0.0751  414 LEU A O   
798  C CB  . LEU A 114 ? 0.7638 0.4738 0.8339 -0.1019 0.1053  0.0213  414 LEU A CB  
799  C CG  . LEU A 114 ? 0.7563 0.4928 0.8287 -0.0934 0.0744  -0.0026 414 LEU A CG  
800  C CD1 . LEU A 114 ? 0.7958 0.5661 0.9275 -0.1076 0.0627  -0.0253 414 LEU A CD1 
801  C CD2 . LEU A 114 ? 0.7298 0.4878 0.7749 -0.0763 0.0716  -0.0004 414 LEU A CD2 
802  N N   . GLU A 115 ? 0.9193 0.5283 0.9027 -0.0937 0.1575  0.0870  415 GLU A N   
803  C CA  . GLU A 115 ? 0.9903 0.5709 0.9495 -0.0950 0.1937  0.1187  415 GLU A CA  
804  C C   . GLU A 115 ? 0.9899 0.5568 0.8666 -0.0667 0.1892  0.1332  415 GLU A C   
805  O O   . GLU A 115 ? 1.0224 0.5891 0.8635 -0.0598 0.2149  0.1503  415 GLU A O   
806  C CB  . GLU A 115 ? 1.1358 0.6600 1.1023 -0.1043 0.2067  0.1379  415 GLU A CB  
807  C CG  . GLU A 115 ? 1.1640 0.6937 1.2167 -0.1372 0.2161  0.1229  415 GLU A CG  
808  C CD  . GLU A 115 ? 1.2125 0.7115 1.2795 -0.1546 0.2640  0.1547  415 GLU A CD  
809  O OE1 . GLU A 115 ? 1.2778 0.8102 1.3449 -0.1562 0.2894  0.1635  415 GLU A OE1 
810  O OE2 . GLU A 115 ? 1.2563 0.6954 1.3290 -0.1632 0.2776  0.1722  415 GLU A OE2 
811  N N   . LYS A 116 ? 0.9427 0.5013 0.7915 -0.0500 0.1564  0.1234  416 LYS A N   
812  C CA  . LYS A 116 ? 1.0186 0.5728 0.7984 -0.0242 0.1448  0.1295  416 LYS A CA  
813  C C   . LYS A 116 ? 1.0270 0.6205 0.7991 -0.0214 0.1460  0.1132  416 LYS A C   
814  O O   . LYS A 116 ? 1.0748 0.6651 0.7897 -0.0044 0.1493  0.1188  416 LYS A O   
815  C CB  . LYS A 116 ? 1.0091 0.5585 0.7781 -0.0090 0.1092  0.1175  416 LYS A CB  
816  C CG  . LYS A 116 ? 1.0644 0.5694 0.8305 -0.0026 0.1070  0.1344  416 LYS A CG  
817  C CD  . LYS A 116 ? 1.1318 0.6304 0.8595 0.0259  0.0779  0.1345  416 LYS A CD  
818  C CE  . LYS A 116 ? 1.2462 0.6952 0.9724 0.0370  0.0778  0.1540  416 LYS A CE  
819  N NZ  . LYS A 116 ? 1.3502 0.7480 1.0527 0.0344  0.1108  0.1913  416 LYS A NZ  
820  N N   . CYS A 117 ? 0.9707 0.5992 0.7967 -0.0353 0.1421  0.0919  417 CYS A N   
821  C CA  . CYS A 117 ? 0.9493 0.6083 0.7717 -0.0301 0.1457  0.0781  417 CYS A CA  
822  C C   . CYS A 117 ? 0.9771 0.6356 0.7805 -0.0285 0.1823  0.0940  417 CYS A C   
823  O O   . CYS A 117 ? 1.1020 0.7682 0.8683 -0.0146 0.1873  0.0872  417 CYS A O   
824  C CB  . CYS A 117 ? 0.8471 0.5411 0.7274 -0.0401 0.1361  0.0577  417 CYS A CB  
825  S SG  . CYS A 117 ? 0.7753 0.4723 0.6642 -0.0379 0.0994  0.0390  417 CYS A SG  
826  N N   . ILE A 118 ? 0.9490 0.5968 0.7779 -0.0431 0.2109  0.1139  418 ILE A N   
827  C CA  . ILE A 118 ? 0.9529 0.5990 0.7588 -0.0407 0.2526  0.1328  418 ILE A CA  
828  C C   . ILE A 118 ? 1.0165 0.6214 0.7297 -0.0193 0.2575  0.1554  418 ILE A C   
829  O O   . ILE A 118 ? 1.0392 0.6458 0.6999 -0.0044 0.2777  0.1600  418 ILE A O   
830  C CB  . ILE A 118 ? 0.9218 0.5733 0.7933 -0.0662 0.2879  0.1472  418 ILE A CB  
831  C CG1 . ILE A 118 ? 0.8595 0.5578 0.8213 -0.0837 0.2732  0.1205  418 ILE A CG1 
832  C CG2 . ILE A 118 ? 0.9816 0.6373 0.8304 -0.0627 0.3373  0.1666  418 ILE A CG2 
833  C CD1 . ILE A 118 ? 0.8756 0.5893 0.9200 -0.1129 0.3011  0.1257  418 ILE A CD1 
834  N N   . GLU A 119 ? 1.0866 0.6565 0.7770 -0.0141 0.2365  0.1670  419 GLU A N   
835  C CA  . GLU A 119 ? 1.2044 0.7354 0.8066 0.0106  0.2366  0.1915  419 GLU A CA  
836  C C   . GLU A 119 ? 1.1967 0.7458 0.7385 0.0347  0.2116  0.1698  419 GLU A C   
837  O O   . GLU A 119 ? 1.3090 0.8470 0.7758 0.0544  0.2263  0.1812  419 GLU A O   
838  C CB  . GLU A 119 ? 1.2529 0.7462 0.8510 0.0161  0.2140  0.2051  419 GLU A CB  
839  C CG  . GLU A 119 ? 1.3152 0.7765 0.9654 -0.0071 0.2412  0.2272  419 GLU A CG  
840  C CD  . GLU A 119 ? 1.3898 0.8094 1.0450 -0.0013 0.2201  0.2364  419 GLU A CD  
841  O OE1 . GLU A 119 ? 1.4866 0.9028 1.0966 0.0256  0.1859  0.2320  419 GLU A OE1 
842  O OE2 . GLU A 119 ? 1.4630 0.8561 1.1729 -0.0233 0.2364  0.2441  419 GLU A OE2 
843  N N   . GLN A 120 ? 1.1690 0.7456 0.7441 0.0323  0.1759  0.1366  420 GLN A N   
844  C CA  . GLN A 120 ? 1.2308 0.8207 0.7603 0.0511  0.1477  0.1120  420 GLN A CA  
845  C C   . GLN A 120 ? 1.1713 0.7892 0.7154 0.0473  0.1571  0.0855  420 GLN A C   
846  O O   . GLN A 120 ? 1.1454 0.7738 0.6700 0.0567  0.1326  0.0580  420 GLN A O   
847  C CB  . GLN A 120 ? 1.2107 0.8075 0.7662 0.0519  0.1055  0.0953  420 GLN A CB  
848  C CG  . GLN A 120 ? 1.2756 0.8450 0.7915 0.0703  0.0894  0.1167  420 GLN A CG  
849  C CD  . GLN A 120 ? 1.2820 0.8648 0.8340 0.0720  0.0517  0.0987  420 GLN A CD  
850  O OE1 . GLN A 120 ? 1.3082 0.8920 0.8275 0.0938  0.0228  0.0960  420 GLN A OE1 
851  N NE2 . GLN A 120 ? 1.2762 0.8742 0.8969 0.0506  0.0516  0.0848  420 GLN A NE2 
852  N N   . ASN A 121 ? 1.1422 0.7718 0.7234 0.0348  0.1927  0.0926  421 ASN A N   
853  C CA  . ASN A 121 ? 1.1488 0.8039 0.7500 0.0353  0.2032  0.0691  421 ASN A CA  
854  C C   . ASN A 121 ? 1.1305 0.7985 0.7659 0.0319  0.1676  0.0398  421 ASN A C   
855  O O   . ASN A 121 ? 1.2180 0.8863 0.8266 0.0426  0.1556  0.0156  421 ASN A O   
856  C CB  . ASN A 121 ? 1.2175 0.8655 0.7428 0.0566  0.2194  0.0630  421 ASN A CB  
857  C CG  . ASN A 121 ? 1.3015 0.9352 0.7862 0.0614  0.2626  0.0959  421 ASN A CG  
858  O OD1 . ASN A 121 ? 1.4276 1.0357 0.8290 0.0798  0.2619  0.1108  421 ASN A OD1 
859  N ND2 . ASN A 121 ? 1.2734 0.9250 0.8161 0.0462  0.3009  0.1082  421 ASN A ND2 
860  N N   . ILE A 122 ? 1.0060 0.6811 0.6980 0.0167  0.1531  0.0424  422 ILE A N   
861  C CA  . ILE A 122 ? 0.9314 0.6173 0.6602 0.0112  0.1264  0.0226  422 ILE A CA  
862  C C   . ILE A 122 ? 0.9225 0.6301 0.6977 0.0078  0.1396  0.0142  422 ILE A C   
863  O O   . ILE A 122 ? 0.8456 0.5688 0.6557 0.0008  0.1600  0.0256  422 ILE A O   
864  C CB  . ILE A 122 ? 0.8709 0.5534 0.6288 0.0005  0.1096  0.0314  422 ILE A CB  
865  C CG1 . ILE A 122 ? 0.9059 0.5681 0.6219 0.0096  0.0937  0.0394  422 ILE A CG1 
866  C CG2 . ILE A 122 ? 0.7980 0.4942 0.5976 -0.0066 0.0903  0.0164  422 ILE A CG2 
867  C CD1 . ILE A 122 ? 0.9209 0.5836 0.5972 0.0230  0.0724  0.0209  422 ILE A CD1 
868  N N   . THR A 123 ? 0.9254 0.6335 0.7051 0.0132  0.1280  -0.0055 423 THR A N   
869  C CA  . THR A 123 ? 0.9658 0.6902 0.7874 0.0159  0.1363  -0.0115 423 THR A CA  
870  C C   . THR A 123 ? 0.8719 0.6013 0.7289 0.0096  0.1155  -0.0129 423 THR A C   
871  O O   . THR A 123 ? 0.8851 0.6320 0.7792 0.0130  0.1175  -0.0117 423 THR A O   
872  C CB  . THR A 123 ? 0.9985 0.7121 0.7995 0.0303  0.1449  -0.0299 423 THR A CB  
873  O OG1 . THR A 123 ? 1.0486 0.7408 0.8302 0.0283  0.1226  -0.0453 423 THR A OG1 
874  C CG2 . THR A 123 ? 1.0131 0.7238 0.7709 0.0404  0.1688  -0.0307 423 THR A CG2 
875  N N   . SER A 124 ? 0.8100 0.5269 0.6550 0.0032  0.0958  -0.0153 424 SER A N   
876  C CA  . SER A 124 ? 0.7209 0.4418 0.5920 -0.0011 0.0818  -0.0152 424 SER A CA  
877  C C   . SER A 124 ? 0.6886 0.4070 0.5558 -0.0100 0.0671  -0.0124 424 SER A C   
878  O O   . SER A 124 ? 0.7288 0.4373 0.5716 -0.0100 0.0608  -0.0157 424 SER A O   
879  C CB  . SER A 124 ? 0.6990 0.4040 0.5677 0.0038  0.0795  -0.0255 424 SER A CB  
880  O OG  . SER A 124 ? 0.7214 0.4104 0.5663 0.0001  0.0723  -0.0386 424 SER A OG  
881  N N   . ILE A 125 ? 0.6481 0.3776 0.5387 -0.0144 0.0602  -0.0082 425 ILE A N   
882  C CA  . ILE A 125 ? 0.6348 0.3620 0.5258 -0.0203 0.0487  -0.0077 425 ILE A CA  
883  C C   . ILE A 125 ? 0.6071 0.3422 0.5113 -0.0201 0.0412  -0.0104 425 ILE A C   
884  O O   . ILE A 125 ? 0.5850 0.3333 0.5035 -0.0169 0.0410  -0.0087 425 ILE A O   
885  C CB  . ILE A 125 ? 0.6353 0.3624 0.5343 -0.0261 0.0521  0.0000  425 ILE A CB  
886  C CG1 . ILE A 125 ? 0.6533 0.3718 0.5526 -0.0285 0.0406  -0.0016 425 ILE A CG1 
887  C CG2 . ILE A 125 ? 0.6023 0.3489 0.5347 -0.0310 0.0572  0.0007  425 ILE A CG2 
888  C CD1 . ILE A 125 ? 0.7129 0.4152 0.6124 -0.0323 0.0459  0.0084  425 ILE A CD1 
889  N N   . SER A 126 ? 0.6052 0.3354 0.5041 -0.0217 0.0352  -0.0145 426 SER A N   
890  C CA  . SER A 126 ? 0.6287 0.3639 0.5303 -0.0200 0.0331  -0.0151 426 SER A CA  
891  C C   . SER A 126 ? 0.6144 0.3531 0.5187 -0.0221 0.0264  -0.0207 426 SER A C   
892  O O   . SER A 126 ? 0.6268 0.3618 0.5322 -0.0233 0.0239  -0.0240 426 SER A O   
893  C CB  . SER A 126 ? 0.6962 0.4214 0.5938 -0.0201 0.0406  -0.0146 426 SER A CB  
894  O OG  . SER A 126 ? 0.7913 0.5057 0.6869 -0.0164 0.0473  -0.0119 426 SER A OG  
895  N N   . PHE A 127 ? 0.6338 0.3809 0.5384 -0.0195 0.0218  -0.0237 427 PHE A N   
896  C CA  . PHE A 127 ? 0.6605 0.4086 0.5671 -0.0194 0.0159  -0.0336 427 PHE A CA  
897  C C   . PHE A 127 ? 0.7035 0.4583 0.5939 -0.0125 0.0190  -0.0369 427 PHE A C   
898  O O   . PHE A 127 ? 0.7476 0.5074 0.6239 -0.0064 0.0197  -0.0307 427 PHE A O   
899  C CB  . PHE A 127 ? 0.6724 0.4249 0.5919 -0.0231 0.0068  -0.0413 427 PHE A CB  
900  C CG  . PHE A 127 ? 0.6540 0.4001 0.5924 -0.0320 0.0097  -0.0357 427 PHE A CG  
901  C CD1 . PHE A 127 ? 0.6418 0.3992 0.5890 -0.0332 0.0147  -0.0282 427 PHE A CD1 
902  C CD2 . PHE A 127 ? 0.6658 0.3929 0.6134 -0.0374 0.0104  -0.0368 427 PHE A CD2 
903  C CE1 . PHE A 127 ? 0.6562 0.4097 0.6193 -0.0411 0.0240  -0.0215 427 PHE A CE1 
904  C CE2 . PHE A 127 ? 0.6813 0.3983 0.6420 -0.0457 0.0191  -0.0269 427 PHE A CE2 
905  C CZ  . PHE A 127 ? 0.7160 0.4483 0.6838 -0.0484 0.0275  -0.0192 427 PHE A CZ  
906  N N   . PRO A 128 ? 0.7088 0.4640 0.5984 -0.0100 0.0218  -0.0459 428 PRO A N   
907  C CA  . PRO A 128 ? 0.7063 0.4685 0.5745 -0.0016 0.0283  -0.0507 428 PRO A CA  
908  C C   . PRO A 128 ? 0.7270 0.4930 0.5848 0.0030  0.0135  -0.0659 428 PRO A C   
909  O O   . PRO A 128 ? 0.7034 0.4670 0.5802 -0.0040 0.0014  -0.0707 428 PRO A O   
910  C CB  . PRO A 128 ? 0.7385 0.5038 0.6207 -0.0006 0.0379  -0.0576 428 PRO A CB  
911  C CG  . PRO A 128 ? 0.7145 0.4708 0.6194 -0.0034 0.0258  -0.0630 428 PRO A CG  
912  C CD  . PRO A 128 ? 0.7111 0.4607 0.6180 -0.0111 0.0201  -0.0511 428 PRO A CD  
913  N N   . ALA A 129 ? 0.8111 0.5839 0.6383 0.0141  0.0156  -0.0744 429 ALA A N   
914  C CA  . ALA A 129 ? 0.8588 0.6375 0.6748 0.0189  -0.0028 -0.0968 429 ALA A CA  
915  C C   . ALA A 129 ? 0.8967 0.6632 0.7319 0.0158  -0.0044 -0.1185 429 ALA A C   
916  O O   . ALA A 129 ? 0.9173 0.6837 0.7326 0.0265  0.0029  -0.1333 429 ALA A O   
917  C CB  . ALA A 129 ? 0.9309 0.7199 0.6963 0.0359  -0.0016 -0.0991 429 ALA A CB  
918  N N   . LEU A 130 ? 0.8588 0.6119 0.7310 0.0033  -0.0109 -0.1182 430 LEU A N   
919  C CA  . LEU A 130 ? 0.8617 0.5928 0.7556 0.0019  -0.0100 -0.1300 430 LEU A CA  
920  C C   . LEU A 130 ? 0.8791 0.6031 0.7649 0.0072  -0.0189 -0.1625 430 LEU A C   
921  O O   . LEU A 130 ? 0.8789 0.6091 0.7653 0.0013  -0.0351 -0.1796 430 LEU A O   
922  C CB  . LEU A 130 ? 0.8333 0.5473 0.7588 -0.0123 -0.0142 -0.1196 430 LEU A CB  
923  C CG  . LEU A 130 ? 0.7802 0.4918 0.7113 -0.0143 -0.0054 -0.0930 430 LEU A CG  
924  C CD1 . LEU A 130 ? 0.8077 0.5053 0.7596 -0.0274 -0.0066 -0.0838 430 LEU A CD1 
925  C CD2 . LEU A 130 ? 0.8035 0.5045 0.7384 -0.0039 0.0002  -0.0897 430 LEU A CD2 
926  N N   . GLY A 131 ? 0.9193 0.6336 0.8008 0.0195  -0.0090 -0.1742 431 GLY A N   
927  C CA  . GLY A 131 ? 1.0016 0.6999 0.8789 0.0261  -0.0154 -0.2091 431 GLY A CA  
928  C C   . GLY A 131 ? 1.0596 0.7794 0.8885 0.0399  -0.0158 -0.2296 431 GLY A C   
929  O O   . GLY A 131 ? 1.1802 0.8896 0.9969 0.0468  -0.0238 -0.2653 431 GLY A O   
930  N N   . THR A 132 ? 0.9625 0.7080 0.7599 0.0456  -0.0058 -0.2073 432 THR A N   
931  C CA  . THR A 132 ? 0.9802 0.7426 0.7195 0.0627  -0.0021 -0.2196 432 THR A CA  
932  C C   . THR A 132 ? 0.9670 0.7317 0.6914 0.0783  0.0272  -0.2229 432 THR A C   
933  O O   . THR A 132 ? 1.0112 0.7844 0.6842 0.0957  0.0360  -0.2394 432 THR A O   
934  C CB  . THR A 132 ? 0.9653 0.7464 0.6756 0.0636  -0.0044 -0.1921 432 THR A CB  
935  O OG1 . THR A 132 ? 0.8908 0.6714 0.6268 0.0546  0.0137  -0.1571 432 THR A OG1 
936  C CG2 . THR A 132 ? 0.9555 0.7437 0.6806 0.0540  -0.0363 -0.2007 432 THR A CG2 
937  N N   . GLY A 133 ? 0.9562 0.7158 0.7270 0.0740  0.0413  -0.2103 433 GLY A N   
938  C CA  . GLY A 133 ? 0.9973 0.7692 0.7732 0.0873  0.0703  -0.2112 433 GLY A CA  
939  C C   . GLY A 133 ? 1.1132 0.8759 0.8711 0.1056  0.0735  -0.2500 433 GLY A C   
940  O O   . GLY A 133 ? 1.1721 0.9077 0.9507 0.1043  0.0541  -0.2738 433 GLY A O   
941  N N   . ASN A 134 ? 1.2239 1.0058 0.9402 0.1222  0.1004  -0.2555 434 ASN A N   
942  C CA  . ASN A 134 ? 1.3816 1.1601 1.0734 0.1445  0.1126  -0.2932 434 ASN A CA  
943  C C   . ASN A 134 ? 1.5152 1.2782 1.1513 0.1504  0.0867  -0.3278 434 ASN A C   
944  O O   . ASN A 134 ? 1.6001 1.3558 1.2084 0.1695  0.0927  -0.3664 434 ASN A O   
945  C CB  . ASN A 134 ? 1.3613 1.1249 1.1133 0.1518  0.1137  -0.3114 434 ASN A CB  
946  C CG  . ASN A 134 ? 1.3272 1.1202 1.1287 0.1559  0.1421  -0.2898 434 ASN A CG  
947  O OD1 . ASN A 134 ? 1.2185 1.0080 1.0788 0.1486  0.1309  -0.2749 434 ASN A OD1 
948  N ND2 . ASN A 134 ? 1.3565 1.1807 1.1357 0.1682  0.1792  -0.2888 434 ASN A ND2 
949  N N   . MET A 135 ? 1.5829 1.3453 1.2038 0.1361  0.0583  -0.3170 435 MET A N   
950  C CA  . MET A 135 ? 1.8000 1.5517 1.3939 0.1359  0.0232  -0.3542 435 MET A CA  
951  C C   . MET A 135 ? 1.8316 1.5486 1.4839 0.1265  0.0076  -0.3859 435 MET A C   
952  O O   . MET A 135 ? 2.1788 1.8788 1.8161 0.1405  0.0075  -0.4294 435 MET A O   
953  C CB  . MET A 135 ? 2.0368 1.8013 1.5436 0.1624  0.0298  -0.3815 435 MET A CB  
954  C CG  . MET A 135 ? 2.3337 2.0925 1.8068 0.1664  -0.0095 -0.4321 435 MET A CG  
955  S SD  . MET A 135 ? 2.6692 2.4526 2.1208 0.1571  -0.0528 -0.4213 435 MET A SD  
956  C CE  . MET A 135 ? 2.7123 2.4985 2.1058 0.1738  -0.0900 -0.4946 435 MET A CE  
957  N N   . GLU A 136 ? 1.5774 1.2797 1.2930 0.1044  -0.0019 -0.3624 436 GLU A N   
958  C CA  . GLU A 136 ? 1.4213 1.0827 1.1926 0.0932  -0.0140 -0.3810 436 GLU A CA  
959  C C   . GLU A 136 ? 1.3398 0.9942 1.1288 0.0699  -0.0461 -0.3954 436 GLU A C   
960  O O   . GLU A 136 ? 1.3084 0.9342 1.1157 0.0634  -0.0620 -0.4359 436 GLU A O   
961  C CB  . GLU A 136 ? 1.4100 1.0604 1.2331 0.0875  -0.0001 -0.3422 436 GLU A CB  
962  C CG  . GLU A 136 ? 1.4814 1.1335 1.3122 0.1111  0.0260  -0.3430 436 GLU A CG  
963  C CD  . GLU A 136 ? 1.5222 1.1313 1.3768 0.1247  0.0259  -0.3772 436 GLU A CD  
964  O OE1 . GLU A 136 ? 1.4437 1.0319 1.2769 0.1303  0.0177  -0.4222 436 GLU A OE1 
965  O OE2 . GLU A 136 ? 1.6160 1.2115 1.5128 0.1319  0.0336  -0.3577 436 GLU A OE2 
966  N N   . ILE A 137 ? 1.3291 1.0105 1.1205 0.0566  -0.0540 -0.3627 437 ILE A N   
967  C CA  . ILE A 137 ? 1.2560 0.9505 1.0617 0.0383  -0.0834 -0.3746 437 ILE A CA  
968  C C   . ILE A 137 ? 1.2475 0.9854 0.9915 0.0532  -0.0936 -0.3709 437 ILE A C   
969  O O   . ILE A 137 ? 1.1695 0.9232 0.8823 0.0648  -0.0733 -0.3345 437 ILE A O   
970  C CB  . ILE A 137 ? 1.2041 0.8933 1.0663 0.0145  -0.0825 -0.3387 437 ILE A CB  
971  C CG1 . ILE A 137 ? 1.1762 0.8177 1.0857 0.0059  -0.0682 -0.3315 437 ILE A CG1 
972  C CG2 . ILE A 137 ? 1.2326 0.9433 1.1227 -0.0050 -0.1103 -0.3534 437 ILE A CG2 
973  C CD1 . ILE A 137 ? 1.1381 0.7727 1.0891 -0.0131 -0.0621 -0.2920 437 ILE A CD1 
974  N N   . LYS A 138 ? 1.2859 1.0412 1.0149 0.0530  -0.1259 -0.4095 438 LYS A N   
975  C CA  . LYS A 138 ? 1.3457 1.1405 1.0075 0.0732  -0.1422 -0.4099 438 LYS A CA  
976  C C   . LYS A 138 ? 1.2714 1.0912 0.9484 0.0673  -0.1435 -0.3629 438 LYS A C   
977  O O   . LYS A 138 ? 1.2502 1.0665 0.9958 0.0432  -0.1467 -0.3496 438 LYS A O   
978  C CB  . LYS A 138 ? 1.4674 1.2766 1.1247 0.0722  -0.1837 -0.4688 438 LYS A CB  
979  C CG  . LYS A 138 ? 1.6207 1.4711 1.1963 0.1002  -0.2092 -0.4802 438 LYS A CG  
980  C CD  . LYS A 138 ? 1.7442 1.5886 1.2214 0.1338  -0.1924 -0.4940 438 LYS A CD  
981  C CE  . LYS A 138 ? 1.7951 1.6753 1.1772 0.1664  -0.2081 -0.4831 438 LYS A CE  
982  N NZ  . LYS A 138 ? 1.6930 1.5816 1.0630 0.1723  -0.1861 -0.4158 438 LYS A NZ  
983  N N   . LYS A 139 ? 1.2543 1.0953 0.8646 0.0909  -0.1380 -0.3368 439 LYS A N   
984  C CA  . LYS A 139 ? 1.1977 1.0514 0.8164 0.0899  -0.1302 -0.2879 439 LYS A CA  
985  C C   . LYS A 139 ? 1.1431 1.0227 0.8176 0.0751  -0.1630 -0.2947 439 LYS A C   
986  O O   . LYS A 139 ? 1.0376 0.9126 0.7678 0.0568  -0.1527 -0.2686 439 LYS A O   
987  C CB  . LYS A 139 ? 1.2631 1.1268 0.7961 0.1200  -0.1181 -0.2603 439 LYS A CB  
988  C CG  . LYS A 139 ? 1.3926 1.2834 0.8575 0.1465  -0.1516 -0.2857 439 LYS A CG  
989  C CD  . LYS A 139 ? 1.4975 1.3837 0.8572 0.1799  -0.1298 -0.2693 439 LYS A CD  
990  C CE  . LYS A 139 ? 1.5779 1.4928 0.8630 0.2099  -0.1696 -0.2952 439 LYS A CE  
991  N NZ  . LYS A 139 ? 1.6772 1.5837 0.8565 0.2406  -0.1495 -0.3005 439 LYS A NZ  
992  N N   . GLU A 140 ? 1.2206 1.1303 0.8832 0.0829  -0.2025 -0.3332 440 GLU A N   
993  C CA  . GLU A 140 ? 1.2433 1.1903 0.9661 0.0707  -0.2357 -0.3437 440 GLU A CA  
994  C C   . GLU A 140 ? 1.2035 1.1356 1.0247 0.0320  -0.2308 -0.3567 440 GLU A C   
995  O O   . GLU A 140 ? 1.2278 1.1841 1.1124 0.0167  -0.2385 -0.3465 440 GLU A O   
996  C CB  . GLU A 140 ? 1.3195 1.3073 1.0194 0.0849  -0.2843 -0.3926 440 GLU A CB  
997  C CG  . GLU A 140 ? 1.4058 1.4151 1.0041 0.1281  -0.2966 -0.3766 440 GLU A CG  
998  C CD  . GLU A 140 ? 1.4895 1.4716 0.9882 0.1524  -0.2766 -0.3812 440 GLU A CD  
999  O OE1 . GLU A 140 ? 1.4742 1.4194 0.9828 0.1381  -0.2487 -0.3935 440 GLU A OE1 
1000 O OE2 . GLU A 140 ? 1.5881 1.5873 0.9957 0.1892  -0.2892 -0.3725 440 GLU A OE2 
1001 N N   . THR A 141 ? 1.1449 1.0363 0.9777 0.0186  -0.2159 -0.3782 441 THR A N   
1002 C CA  . THR A 141 ? 1.0939 0.9597 1.0112 -0.0156 -0.2081 -0.3881 441 THR A CA  
1003 C C   . THR A 141 ? 1.0410 0.8833 0.9822 -0.0251 -0.1726 -0.3355 441 THR A C   
1004 O O   . THR A 141 ? 0.9713 0.8158 0.9773 -0.0482 -0.1679 -0.3235 441 THR A O   
1005 C CB  . THR A 141 ? 1.1299 0.9536 1.0450 -0.0206 -0.2054 -0.4284 441 THR A CB  
1006 O OG1 . THR A 141 ? 1.1723 1.0205 1.0770 -0.0169 -0.2434 -0.4853 441 THR A OG1 
1007 C CG2 . THR A 141 ? 1.1052 0.8862 1.0995 -0.0528 -0.1903 -0.4308 441 THR A CG2 
1008 N N   . ALA A 142 ? 1.0528 0.8745 0.9425 -0.0074 -0.1468 -0.3065 442 ALA A N   
1009 C CA  . ALA A 142 ? 1.0207 0.8268 0.9255 -0.0130 -0.1187 -0.2607 442 ALA A CA  
1010 C C   . ALA A 142 ? 0.9909 0.8303 0.9170 -0.0161 -0.1256 -0.2380 442 ALA A C   
1011 O O   . ALA A 142 ? 0.9963 0.8316 0.9748 -0.0353 -0.1170 -0.2243 442 ALA A O   
1012 C CB  . ALA A 142 ? 1.0229 0.8169 0.8740 0.0067  -0.0953 -0.2379 442 ALA A CB  
1013 N N   . ALA A 143 ? 0.9877 0.8588 0.8707 0.0055  -0.1406 -0.2349 443 ALA A N   
1014 C CA  . ALA A 143 ? 0.9838 0.8882 0.8846 0.0099  -0.1499 -0.2155 443 ALA A CA  
1015 C C   . ALA A 143 ? 0.9681 0.8994 0.9468 -0.0125 -0.1683 -0.2382 443 ALA A C   
1016 O O   . ALA A 143 ? 0.9542 0.8927 0.9792 -0.0245 -0.1558 -0.2175 443 ALA A O   
1017 C CB  . ALA A 143 ? 1.0076 0.9380 0.8462 0.0410  -0.1682 -0.2129 443 ALA A CB  
1018 N N   . GLU A 144 ? 1.0284 0.9744 1.0253 -0.0199 -0.1953 -0.2829 444 GLU A N   
1019 C CA  . GLU A 144 ? 1.0511 1.0239 1.1353 -0.0468 -0.2104 -0.3083 444 GLU A CA  
1020 C C   . GLU A 144 ? 1.0124 0.9506 1.1512 -0.0750 -0.1753 -0.2846 444 GLU A C   
1021 O O   . GLU A 144 ? 0.9860 0.9496 1.1817 -0.0878 -0.1682 -0.2712 444 GLU A O   
1022 C CB  . GLU A 144 ? 1.1033 1.0823 1.2029 -0.0566 -0.2403 -0.3649 444 GLU A CB  
1023 C CG  . GLU A 144 ? 1.2148 1.2495 1.2813 -0.0312 -0.2855 -0.3945 444 GLU A CG  
1024 C CD  . GLU A 144 ? 1.3612 1.3995 1.4217 -0.0349 -0.3180 -0.4563 444 GLU A CD  
1025 O OE1 . GLU A 144 ? 1.3551 1.3952 1.5020 -0.0694 -0.3257 -0.4905 444 GLU A OE1 
1026 O OE2 . GLU A 144 ? 1.4013 1.4389 1.3742 -0.0050 -0.3335 -0.4717 444 GLU A OE2 
1027 N N   . ILE A 145 ? 0.9617 0.8437 1.0783 -0.0802 -0.1524 -0.2775 445 ILE A N   
1028 C CA  . ILE A 145 ? 0.9001 0.7418 1.0560 -0.1026 -0.1216 -0.2555 445 ILE A CA  
1029 C C   . ILE A 145 ? 0.8308 0.6739 0.9735 -0.0952 -0.0976 -0.2094 445 ILE A C   
1030 O O   . ILE A 145 ? 0.7849 0.6261 0.9724 -0.1126 -0.0790 -0.1923 445 ILE A O   
1031 C CB  . ILE A 145 ? 0.9731 0.7565 1.1034 -0.1018 -0.1087 -0.2608 445 ILE A CB  
1032 C CG1 . ILE A 145 ? 1.0539 0.8266 1.2106 -0.1143 -0.1287 -0.3109 445 ILE A CG1 
1033 C CG2 . ILE A 145 ? 0.9557 0.6937 1.1050 -0.1140 -0.0765 -0.2267 445 ILE A CG2 
1034 C CD1 . ILE A 145 ? 1.0825 0.7965 1.2153 -0.1087 -0.1170 -0.3208 445 ILE A CD1 
1035 N N   . LEU A 146 ? 0.8361 0.6798 0.9167 -0.0702 -0.0954 -0.1907 446 LEU A N   
1036 C CA  . LEU A 146 ? 0.8045 0.6445 0.8688 -0.0627 -0.0746 -0.1529 446 LEU A CA  
1037 C C   . LEU A 146 ? 0.7888 0.6690 0.8935 -0.0658 -0.0770 -0.1458 446 LEU A C   
1038 O O   . LEU A 146 ? 0.8216 0.6944 0.9519 -0.0765 -0.0551 -0.1259 446 LEU A O   
1039 C CB  . LEU A 146 ? 0.8741 0.7100 0.8746 -0.0385 -0.0730 -0.1395 446 LEU A CB  
1040 C CG  . LEU A 146 ? 0.8999 0.6992 0.8675 -0.0340 -0.0586 -0.1349 446 LEU A CG  
1041 C CD1 . LEU A 146 ? 0.9507 0.7479 0.8818 -0.0201 -0.0445 -0.1086 446 LEU A CD1 
1042 C CD2 . LEU A 146 ? 0.8850 0.6501 0.8781 -0.0483 -0.0442 -0.1291 446 LEU A CD2 
1043 N N   . PHE A 147 ? 0.8108 0.7353 0.9205 -0.0539 -0.1036 -0.1627 447 PHE A N   
1044 C CA  . PHE A 147 ? 0.8160 0.7871 0.9748 -0.0534 -0.1091 -0.1601 447 PHE A CA  
1045 C C   . PHE A 147 ? 0.8548 0.8371 1.0951 -0.0851 -0.0999 -0.1730 447 PHE A C   
1046 O O   . PHE A 147 ? 0.8098 0.8048 1.0877 -0.0921 -0.0785 -0.1552 447 PHE A O   
1047 C CB  . PHE A 147 ? 0.8094 0.8299 0.9601 -0.0305 -0.1452 -0.1774 447 PHE A CB  
1048 C CG  . PHE A 147 ? 0.8492 0.8581 0.9266 0.0021  -0.1442 -0.1515 447 PHE A CG  
1049 C CD1 . PHE A 147 ? 0.9003 0.8822 0.9067 0.0160  -0.1477 -0.1520 447 PHE A CD1 
1050 C CD2 . PHE A 147 ? 0.9253 0.9448 1.0061 0.0181  -0.1342 -0.1253 447 PHE A CD2 
1051 C CE1 . PHE A 147 ? 0.9385 0.9045 0.8818 0.0423  -0.1399 -0.1246 447 PHE A CE1 
1052 C CE2 . PHE A 147 ? 0.9341 0.9325 0.9510 0.0455  -0.1294 -0.0999 447 PHE A CE2 
1053 C CZ  . PHE A 147 ? 0.9137 0.8848 0.8632 0.0559  -0.1310 -0.0981 447 PHE A CZ  
1054 N N   . ASP A 148 ? 0.9418 0.9171 1.2094 -0.1042 -0.1132 -0.2047 448 ASP A N   
1055 C CA  . ASP A 148 ? 0.9992 0.9775 1.3496 -0.1388 -0.1022 -0.2191 448 ASP A CA  
1056 C C   . ASP A 148 ? 0.9084 0.8521 1.2666 -0.1508 -0.0581 -0.1808 448 ASP A C   
1057 O O   . ASP A 148 ? 0.9120 0.8844 1.3297 -0.1648 -0.0406 -0.1731 448 ASP A O   
1058 C CB  . ASP A 148 ? 1.1676 1.1123 1.5260 -0.1561 -0.1134 -0.2519 448 ASP A CB  
1059 C CG  . ASP A 148 ? 1.2594 1.2251 1.7122 -0.1906 -0.1233 -0.2898 448 ASP A CG  
1060 O OD1 . ASP A 148 ? 1.3131 1.3386 1.8365 -0.2009 -0.1285 -0.2971 448 ASP A OD1 
1061 O OD2 . ASP A 148 ? 1.2508 1.1736 1.7115 -0.2070 -0.1257 -0.3147 448 ASP A OD2 
1062 N N   . GLU A 149 ? 0.8339 0.7193 1.1315 -0.1436 -0.0404 -0.1581 449 GLU A N   
1063 C CA  . GLU A 149 ? 0.8606 0.7087 1.1548 -0.1523 -0.0026 -0.1241 449 GLU A CA  
1064 C C   . GLU A 149 ? 0.8313 0.7047 1.1112 -0.1374 0.0122  -0.0986 449 GLU A C   
1065 O O   . GLU A 149 ? 0.8408 0.7160 1.1498 -0.1489 0.0414  -0.0809 449 GLU A O   
1066 C CB  . GLU A 149 ? 0.8751 0.6624 1.1096 -0.1432 0.0042  -0.1110 449 GLU A CB  
1067 C CG  . GLU A 149 ? 0.9560 0.7066 1.2137 -0.1597 -0.0008 -0.1331 449 GLU A CG  
1068 C CD  . GLU A 149 ? 1.0242 0.7587 1.3485 -0.1910 0.0232  -0.1291 449 GLU A CD  
1069 O OE1 . GLU A 149 ? 1.0191 0.7233 1.3304 -0.1929 0.0552  -0.0930 449 GLU A OE1 
1070 O OE2 . GLU A 149 ? 1.0316 0.7853 1.4206 -0.2136 0.0109  -0.1619 449 GLU A OE2 
1071 N N   . VAL A 150 ? 0.7719 0.6604 1.0049 -0.1112 -0.0048 -0.0968 450 VAL A N   
1072 C CA  . VAL A 150 ? 0.7522 0.6579 0.9703 -0.0948 0.0074  -0.0768 450 VAL A CA  
1073 C C   . VAL A 150 ? 0.7478 0.7067 1.0379 -0.1026 0.0120  -0.0840 450 VAL A C   
1074 O O   . VAL A 150 ? 0.7510 0.7117 1.0572 -0.1068 0.0419  -0.0667 450 VAL A O   
1075 C CB  . VAL A 150 ? 0.7466 0.6561 0.9113 -0.0671 -0.0106 -0.0742 450 VAL A CB  
1076 C CG1 . VAL A 150 ? 0.7506 0.6786 0.9130 -0.0500 0.0000  -0.0590 450 VAL A CG1 
1077 C CG2 . VAL A 150 ? 0.7346 0.5969 0.8383 -0.0613 -0.0062 -0.0639 450 VAL A CG2 
1078 N N   . LEU A 151 ? 0.7893 0.7948 1.1239 -0.1037 -0.0176 -0.1115 451 LEU A N   
1079 C CA  . LEU A 151 ? 0.8096 0.8788 1.2245 -0.1088 -0.0184 -0.1227 451 LEU A CA  
1080 C C   . LEU A 151 ? 0.8680 0.9338 1.3478 -0.1426 0.0163  -0.1189 451 LEU A C   
1081 O O   . LEU A 151 ? 0.8990 1.0013 1.4290 -0.1452 0.0393  -0.1112 451 LEU A O   
1082 C CB  . LEU A 151 ? 0.7964 0.9199 1.2488 -0.1038 -0.0630 -0.1577 451 LEU A CB  
1083 C CG  . LEU A 151 ? 0.8168 0.9506 1.2059 -0.0657 -0.0952 -0.1570 451 LEU A CG  
1084 C CD1 . LEU A 151 ? 0.8235 1.0334 1.2670 -0.0529 -0.1339 -0.1842 451 LEU A CD1 
1085 C CD2 . LEU A 151 ? 0.8243 0.9349 1.1600 -0.0396 -0.0752 -0.1234 451 LEU A CD2 
1086 N N   . THR A 152 ? 0.9570 0.9770 1.4361 -0.1668 0.0230  -0.1231 452 THR A N   
1087 C CA  . THR A 152 ? 1.0267 1.0296 1.5617 -0.2000 0.0600  -0.1145 452 THR A CA  
1088 C C   . THR A 152 ? 1.0139 0.9968 1.5177 -0.1928 0.1043  -0.0760 452 THR A C   
1089 O O   . THR A 152 ? 0.9695 0.9826 1.5331 -0.2070 0.1359  -0.0686 452 THR A O   
1090 C CB  . THR A 152 ? 1.0915 1.0290 1.6077 -0.2181 0.0602  -0.1187 452 THR A CB  
1091 O OG1 . THR A 152 ? 1.0892 1.0574 1.6576 -0.2310 0.0239  -0.1624 452 THR A OG1 
1092 C CG2 . THR A 152 ? 1.1361 1.0309 1.6845 -0.2471 0.1064  -0.0960 452 THR A CG2 
1093 N N   . PHE A 153 ? 1.0588 0.9934 1.4696 -0.1704 0.1059  -0.0545 453 PHE A N   
1094 C CA  . PHE A 153 ? 1.0402 0.9506 1.4020 -0.1584 0.1402  -0.0228 453 PHE A CA  
1095 C C   . PHE A 153 ? 1.0536 1.0193 1.4444 -0.1446 0.1512  -0.0229 453 PHE A C   
1096 O O   . PHE A 153 ? 1.0604 1.0291 1.4600 -0.1480 0.1908  -0.0051 453 PHE A O   
1097 C CB  . PHE A 153 ? 1.0048 0.8716 1.2742 -0.1345 0.1241  -0.0132 453 PHE A CB  
1098 C CG  . PHE A 153 ? 1.0046 0.8501 1.2164 -0.1184 0.1501  0.0117  453 PHE A CG  
1099 C CD1 . PHE A 153 ? 1.0096 0.8854 1.2130 -0.0986 0.1515  0.0101  453 PHE A CD1 
1100 C CD2 . PHE A 153 ? 1.0124 0.8060 1.1768 -0.1206 0.1716  0.0352  453 PHE A CD2 
1101 C CE1 . PHE A 153 ? 1.0274 0.8828 1.1772 -0.0842 0.1742  0.0263  453 PHE A CE1 
1102 C CE2 . PHE A 153 ? 1.0634 0.8408 1.1693 -0.1039 0.1916  0.0536  453 PHE A CE2 
1103 C CZ  . PHE A 153 ? 1.0697 0.8783 1.1686 -0.0870 0.1927  0.0465  453 PHE A CZ  
1104 N N   . ALA A 154 ? 1.0581 1.0654 1.4590 -0.1257 0.1171  -0.0420 454 ALA A N   
1105 C CA  . ALA A 154 ? 1.1726 1.2309 1.6023 -0.1062 0.1223  -0.0437 454 ALA A CA  
1106 C C   . ALA A 154 ? 1.2608 1.3737 1.7894 -0.1264 0.1485  -0.0499 454 ALA A C   
1107 O O   . ALA A 154 ? 1.4622 1.6022 2.0085 -0.1145 0.1764  -0.0415 454 ALA A O   
1108 C CB  . ALA A 154 ? 1.1852 1.2748 1.6120 -0.0820 0.0782  -0.0612 454 ALA A CB  
1109 N N   . LYS A 155 ? 1.1828 1.3127 1.7801 -0.1572 0.1407  -0.0673 455 LYS A N   
1110 C CA  . LYS A 155 ? 1.0880 1.2743 1.7961 -0.1832 0.1651  -0.0771 455 LYS A CA  
1111 C C   . LYS A 155 ? 1.0296 1.1712 1.7321 -0.2074 0.2241  -0.0476 455 LYS A C   
1112 O O   . LYS A 155 ? 0.9694 1.1474 1.7275 -0.2153 0.2657  -0.0390 455 LYS A O   
1113 C CB  . LYS A 155 ? 1.1028 1.3255 1.8913 -0.2081 0.1292  -0.1133 455 LYS A CB  
1114 C CG  . LYS A 155 ? 1.2021 1.5008 2.1269 -0.2364 0.1452  -0.1331 455 LYS A CG  
1115 C CD  . LYS A 155 ? 1.2697 1.5639 2.2693 -0.2813 0.1382  -0.1586 455 LYS A CD  
1116 C CE  . LYS A 155 ? 1.2942 1.5747 2.2604 -0.2754 0.0784  -0.1901 455 LYS A CE  
1117 N NZ  . LYS A 155 ? 1.3170 1.6017 2.3692 -0.3186 0.0688  -0.2242 455 LYS A NZ  
1118 N N   . ASP A 156 ? 1.0608 1.1233 1.6918 -0.2152 0.2294  -0.0299 456 ASP A N   
1119 C CA  . ASP A 156 ? 1.1328 1.1454 1.7575 -0.2386 0.2810  -0.0003 456 ASP A CA  
1120 C C   . ASP A 156 ? 1.1653 1.1412 1.6965 -0.2137 0.3153  0.0343  456 ASP A C   
1121 O O   . ASP A 156 ? 1.1671 1.1058 1.6805 -0.2258 0.3636  0.0642  456 ASP A O   
1122 C CB  . ASP A 156 ? 1.2115 1.1588 1.8184 -0.2585 0.2686  -0.0003 456 ASP A CB  
1123 C CG  . ASP A 156 ? 1.2287 1.2056 1.9350 -0.2900 0.2436  -0.0375 456 ASP A CG  
1124 O OD1 . ASP A 156 ? 1.1607 1.2183 1.9566 -0.2971 0.2313  -0.0650 456 ASP A OD1 
1125 O OD2 . ASP A 156 ? 1.3252 1.2448 2.0199 -0.3056 0.2348  -0.0412 456 ASP A OD2 
1126 N N   . HIS A 157 ? 1.1607 1.1425 1.6278 -0.1787 0.2915  0.0304  457 HIS A N   
1127 C CA  . HIS A 157 ? 1.1500 1.1024 1.5330 -0.1553 0.3203  0.0546  457 HIS A CA  
1128 C C   . HIS A 157 ? 1.1663 1.1583 1.5387 -0.1239 0.3023  0.0388  457 HIS A C   
1129 O O   . HIS A 157 ? 1.2512 1.2146 1.5508 -0.1008 0.2757  0.0366  457 HIS A O   
1130 C CB  . HIS A 157 ? 1.1510 1.0267 1.4320 -0.1465 0.3119  0.0740  457 HIS A CB  
1131 C CG  . HIS A 157 ? 1.1218 0.9495 1.4094 -0.1706 0.3142  0.0853  457 HIS A CG  
1132 N ND1 . HIS A 157 ? 1.0390 0.8573 1.3456 -0.1788 0.2730  0.0649  457 HIS A ND1 
1133 C CD2 . HIS A 157 ? 1.1677 0.9471 1.4366 -0.1842 0.3530  0.1159  457 HIS A CD2 
1134 C CE1 . HIS A 157 ? 1.0868 0.8526 1.3927 -0.1973 0.2862  0.0798  457 HIS A CE1 
1135 N NE2 . HIS A 157 ? 1.1650 0.9043 1.4480 -0.2007 0.3346  0.1130  457 HIS A NE2 
1136 N N   . VAL A 158 ? 1.1835 1.2413 1.6359 -0.1239 0.3202  0.0282  458 VAL A N   
1137 C CA  . VAL A 158 ? 1.1289 1.2317 1.5952 -0.0935 0.3037  0.0115  458 VAL A CA  
1138 C C   . VAL A 158 ? 1.0801 1.1597 1.4755 -0.0677 0.3363  0.0239  458 VAL A C   
1139 O O   . VAL A 158 ? 0.9581 1.0524 1.3414 -0.0382 0.3244  0.0123  458 VAL A O   
1140 C CB  . VAL A 158 ? 1.0985 1.2874 1.6908 -0.1031 0.3077  -0.0071 458 VAL A CB  
1141 C CG1 . VAL A 158 ? 1.1119 1.3254 1.7612 -0.1248 0.3694  0.0059  458 VAL A CG1 
1142 C CG2 . VAL A 158 ? 1.0860 1.3239 1.7008 -0.0671 0.2843  -0.0242 458 VAL A CG2 
1143 N N   . LYS A 159 ? 1.1024 1.1410 1.4461 -0.0771 0.3773  0.0472  459 LYS A N   
1144 C CA  . LYS A 159 ? 1.1367 1.1488 1.3993 -0.0525 0.4068  0.0562  459 LYS A CA  
1145 C C   . LYS A 159 ? 1.0933 1.0488 1.2553 -0.0334 0.3713  0.0533  459 LYS A C   
1146 O O   . LYS A 159 ? 1.1514 1.0874 1.2476 -0.0102 0.3835  0.0506  459 LYS A O   
1147 C CB  . LYS A 159 ? 1.2105 1.1977 1.4435 -0.0667 0.4623  0.0847  459 LYS A CB  
1148 C CG  . LYS A 159 ? 1.2700 1.3132 1.6083 -0.0895 0.5088  0.0895  459 LYS A CG  
1149 C CD  . LYS A 159 ? 1.3756 1.3825 1.7057 -0.1184 0.5538  0.1226  459 LYS A CD  
1150 C CE  . LYS A 159 ? 1.3340 1.3875 1.7952 -0.1572 0.5747  0.1209  459 LYS A CE  
1151 N NZ  . LYS A 159 ? 1.3998 1.3956 1.8434 -0.1863 0.6068  0.1539  459 LYS A NZ  
1152 N N   . HIS A 160 ? 1.0280 0.9595 1.1812 -0.0436 0.3290  0.0509  460 HIS A N   
1153 C CA  . HIS A 160 ? 1.0017 0.8843 1.0718 -0.0302 0.2976  0.0486  460 HIS A CA  
1154 C C   . HIS A 160 ? 1.0062 0.9029 1.0941 -0.0172 0.2573  0.0281  460 HIS A C   
1155 O O   . HIS A 160 ? 0.9951 0.9150 1.1361 -0.0275 0.2323  0.0212  460 HIS A O   
1156 C CB  . HIS A 160 ? 0.9406 0.7825 0.9824 -0.0472 0.2831  0.0626  460 HIS A CB  
1157 C CG  . HIS A 160 ? 0.8862 0.6830 0.8447 -0.0335 0.2584  0.0626  460 HIS A CG  
1158 N ND1 . HIS A 160 ? 0.9189 0.6817 0.7985 -0.0215 0.2741  0.0752  460 HIS A ND1 
1159 C CD2 . HIS A 160 ? 0.8359 0.6200 0.7811 -0.0300 0.2193  0.0508  460 HIS A CD2 
1160 C CE1 . HIS A 160 ? 0.8981 0.6336 0.7269 -0.0120 0.2413  0.0680  460 HIS A CE1 
1161 N NE2 . HIS A 160 ? 0.8606 0.6086 0.7311 -0.0182 0.2108  0.0539  460 HIS A NE2 
1162 N N   . GLN A 161 ? 1.0271 0.9062 1.0674 0.0058  0.2528  0.0182  461 GLN A N   
1163 C CA  . GLN A 161 ? 0.9235 0.8011 0.9681 0.0199  0.2206  0.0041  461 GLN A CA  
1164 C C   . GLN A 161 ? 0.8300 0.6717 0.8347 0.0113  0.1898  0.0057  461 GLN A C   
1165 O O   . GLN A 161 ? 0.8294 0.6368 0.7758 0.0104  0.1916  0.0088  461 GLN A O   
1166 C CB  . GLN A 161 ? 0.9728 0.8306 0.9808 0.0443  0.2246  -0.0088 461 GLN A CB  
1167 C CG  . GLN A 161 ? 1.0090 0.9037 1.0669 0.0640  0.2430  -0.0170 461 GLN A CG  
1168 C CD  . GLN A 161 ? 0.9918 0.8613 1.0296 0.0894  0.2354  -0.0313 461 GLN A CD  
1169 O OE1 . GLN A 161 ? 1.0260 0.8736 1.0572 0.0921  0.2066  -0.0322 461 GLN A OE1 
1170 N NE2 . GLN A 161 ? 1.0088 0.8783 1.0376 0.1087  0.2642  -0.0424 461 GLN A NE2 
1171 N N   . LEU A 162 ? 0.7776 0.6317 0.8135 0.0079  0.1619  0.0022  462 LEU A N   
1172 C CA  . LEU A 162 ? 0.7961 0.6222 0.8014 0.0007  0.1360  0.0026  462 LEU A CA  
1173 C C   . LEU A 162 ? 0.7185 0.5485 0.7335 0.0120  0.1125  -0.0034 462 LEU A C   
1174 O O   . LEU A 162 ? 0.6532 0.5173 0.7117 0.0192  0.1061  -0.0057 462 LEU A O   
1175 C CB  . LEU A 162 ? 0.8360 0.6662 0.8610 -0.0197 0.1310  0.0086  462 LEU A CB  
1176 C CG  . LEU A 162 ? 0.8385 0.6377 0.8289 -0.0258 0.1110  0.0095  462 LEU A CG  
1177 C CD1 . LEU A 162 ? 0.8576 0.6230 0.7910 -0.0214 0.1171  0.0147  462 LEU A CD1 
1178 C CD2 . LEU A 162 ? 0.9165 0.7192 0.9365 -0.0436 0.1074  0.0117  462 LEU A CD2 
1179 N N   . THR A 163 ? 0.7122 0.5090 0.6876 0.0139  0.1005  -0.0050 463 THR A N   
1180 C CA  . THR A 163 ? 0.7433 0.5353 0.7186 0.0212  0.0819  -0.0048 463 THR A CA  
1181 C C   . THR A 163 ? 0.6998 0.4853 0.6637 0.0073  0.0669  -0.0039 463 THR A C   
1182 O O   . THR A 163 ? 0.7401 0.5038 0.6782 -0.0010 0.0678  -0.0049 463 THR A O   
1183 C CB  . THR A 163 ? 0.7181 0.4765 0.6674 0.0322  0.0853  -0.0072 463 THR A CB  
1184 O OG1 . THR A 163 ? 0.7210 0.4789 0.6758 0.0454  0.1023  -0.0123 463 THR A OG1 
1185 C CG2 . THR A 163 ? 0.7075 0.4597 0.6586 0.0438  0.0737  0.0001  463 THR A CG2 
1186 N N   . VAL A 164 ? 0.6913 0.4979 0.6742 0.0079  0.0515  -0.0045 464 VAL A N   
1187 C CA  . VAL A 164 ? 0.7125 0.5138 0.6848 -0.0019 0.0382  -0.0075 464 VAL A CA  
1188 C C   . VAL A 164 ? 0.7213 0.5172 0.6738 0.0099  0.0271  -0.0048 464 VAL A C   
1189 O O   . VAL A 164 ? 0.7147 0.5288 0.6756 0.0243  0.0181  -0.0028 464 VAL A O   
1190 C CB  . VAL A 164 ? 0.6831 0.5098 0.6892 -0.0132 0.0306  -0.0150 464 VAL A CB  
1191 C CG1 . VAL A 164 ? 0.6827 0.5013 0.6766 -0.0197 0.0162  -0.0227 464 VAL A CG1 
1192 C CG2 . VAL A 164 ? 0.6662 0.4907 0.6893 -0.0264 0.0490  -0.0116 464 VAL A CG2 
1193 N N   . LYS A 165 ? 0.7528 0.5250 0.6793 0.0055  0.0292  -0.0034 465 LYS A N   
1194 C CA  . LYS A 165 ? 0.7713 0.5360 0.6754 0.0139  0.0254  0.0018  465 LYS A CA  
1195 C C   . LYS A 165 ? 0.7346 0.5065 0.6321 0.0070  0.0166  -0.0071 465 LYS A C   
1196 O O   . LYS A 165 ? 0.6901 0.4554 0.5932 -0.0049 0.0191  -0.0133 465 LYS A O   
1197 C CB  . LYS A 165 ? 0.7866 0.5210 0.6757 0.0121  0.0401  0.0084  465 LYS A CB  
1198 C CG  . LYS A 165 ? 0.8747 0.5943 0.7678 0.0218  0.0491  0.0143  465 LYS A CG  
1199 C CD  . LYS A 165 ? 0.8582 0.5416 0.7416 0.0206  0.0639  0.0196  465 LYS A CD  
1200 C CE  . LYS A 165 ? 0.9225 0.5906 0.8132 0.0319  0.0712  0.0200  465 LYS A CE  
1201 N NZ  . LYS A 165 ? 1.0523 0.6785 0.9398 0.0287  0.0862  0.0209  465 LYS A NZ  
1202 N N   . PHE A 166 ? 0.7002 0.4849 0.5829 0.0178  0.0051  -0.0088 466 PHE A N   
1203 C CA  . PHE A 166 ? 0.6886 0.4731 0.5522 0.0164  0.0016  -0.0178 466 PHE A CA  
1204 C C   . PHE A 166 ? 0.7188 0.4852 0.5492 0.0244  0.0169  -0.0037 466 PHE A C   
1205 O O   . PHE A 166 ? 0.7786 0.5439 0.5815 0.0411  0.0157  0.0083  466 PHE A O   
1206 C CB  . PHE A 166 ? 0.7021 0.5114 0.5625 0.0238  -0.0201 -0.0329 466 PHE A CB  
1207 C CG  . PHE A 166 ? 0.6787 0.5080 0.5834 0.0117  -0.0329 -0.0485 466 PHE A CG  
1208 C CD1 . PHE A 166 ? 0.6439 0.4599 0.5750 -0.0064 -0.0229 -0.0508 466 PHE A CD1 
1209 C CD2 . PHE A 166 ? 0.6661 0.5287 0.5877 0.0190  -0.0545 -0.0601 466 PHE A CD2 
1210 C CE1 . PHE A 166 ? 0.6480 0.4774 0.6210 -0.0195 -0.0277 -0.0608 466 PHE A CE1 
1211 C CE2 . PHE A 166 ? 0.6514 0.5354 0.6257 0.0038  -0.0621 -0.0750 466 PHE A CE2 
1212 C CZ  . PHE A 166 ? 0.6564 0.5209 0.6562 -0.0169 -0.0456 -0.0736 466 PHE A CZ  
1213 N N   . VAL A 167 ? 0.7193 0.4731 0.5542 0.0133  0.0314  -0.0048 467 VAL A N   
1214 C CA  . VAL A 167 ? 0.7564 0.4960 0.5733 0.0146  0.0518  0.0065  467 VAL A CA  
1215 C C   . VAL A 167 ? 0.7901 0.5387 0.5787 0.0226  0.0546  0.0005  467 VAL A C   
1216 O O   . VAL A 167 ? 0.7929 0.5509 0.5935 0.0171  0.0526  -0.0163 467 VAL A O   
1217 C CB  . VAL A 167 ? 0.7810 0.5143 0.6288 -0.0019 0.0621  0.0018  467 VAL A CB  
1218 C CG1 . VAL A 167 ? 0.8152 0.5373 0.6635 -0.0073 0.0867  0.0109  467 VAL A CG1 
1219 C CG2 . VAL A 167 ? 0.8103 0.5353 0.6763 -0.0070 0.0572  0.0024  467 VAL A CG2 
1220 N N   . ILE A 168 ? 0.8511 0.5940 0.5974 0.0388  0.0609  0.0153  468 ILE A N   
1221 C CA  . ILE A 168 ? 0.9023 0.6513 0.6068 0.0508  0.0681  0.0119  468 ILE A CA  
1222 C C   . ILE A 168 ? 0.9636 0.6962 0.6599 0.0465  0.1052  0.0304  468 ILE A C   
1223 O O   . ILE A 168 ? 1.0182 0.7273 0.7135 0.0449  0.1221  0.0543  468 ILE A O   
1224 C CB  . ILE A 168 ? 0.9048 0.6598 0.5579 0.0756  0.0508  0.0177  468 ILE A CB  
1225 C CG1 . ILE A 168 ? 0.8709 0.6464 0.5483 0.0775  0.0158  0.0027  468 ILE A CG1 
1226 C CG2 . ILE A 168 ? 0.9383 0.7027 0.5411 0.0896  0.0536  0.0059  468 ILE A CG2 
1227 C CD1 . ILE A 168 ? 0.8535 0.6460 0.5676 0.0621  -0.0007 -0.0292 468 ILE A CD1 
1228 N N   . PHE A 169 ? 1.0064 0.7501 0.6990 0.0450  0.1210  0.0192  469 PHE A N   
1229 C CA  . PHE A 169 ? 1.0225 0.7573 0.7205 0.0373  0.1607  0.0355  469 PHE A CA  
1230 C C   . PHE A 169 ? 1.1105 0.8232 0.7435 0.0555  0.1810  0.0657  469 PHE A C   
1231 O O   . PHE A 169 ? 1.1203 0.8377 0.6946 0.0787  0.1648  0.0641  469 PHE A O   
1232 C CB  . PHE A 169 ? 1.0306 0.7890 0.7464 0.0343  0.1742  0.0147  469 PHE A CB  
1233 C CG  . PHE A 169 ? 1.0368 0.7987 0.7871 0.0198  0.2150  0.0251  469 PHE A CG  
1234 C CD1 . PHE A 169 ? 1.0026 0.7688 0.8219 -0.0029 0.2161  0.0215  469 PHE A CD1 
1235 C CD2 . PHE A 169 ? 1.0946 0.8596 0.8108 0.0288  0.2525  0.0353  469 PHE A CD2 
1236 C CE1 . PHE A 169 ? 1.0269 0.8040 0.8917 -0.0194 0.2515  0.0257  469 PHE A CE1 
1237 C CE2 . PHE A 169 ? 1.1191 0.8927 0.8797 0.0120  0.2941  0.0439  469 PHE A CE2 
1238 C CZ  . PHE A 169 ? 1.0825 0.8643 0.9232 -0.0135 0.2921  0.0374  469 PHE A CZ  
1239 N N   . PRO A 170 ? 1.1953 0.8808 0.8359 0.0462  0.2155  0.0941  470 PRO A N   
1240 C CA  . PRO A 170 ? 1.2693 0.9230 0.8435 0.0653  0.2399  0.1309  470 PRO A CA  
1241 C C   . PRO A 170 ? 1.3100 0.9728 0.8083 0.0894  0.2539  0.1353  470 PRO A C   
1242 O O   . PRO A 170 ? 1.4053 1.0559 0.8302 0.1185  0.2412  0.1519  470 PRO A O   
1243 C CB  . PRO A 170 ? 1.3025 0.9289 0.9214 0.0405  0.2835  0.1518  470 PRO A CB  
1244 C CG  . PRO A 170 ? 1.2172 0.8526 0.9143 0.0163  0.2608  0.1281  470 PRO A CG  
1245 C CD  . PRO A 170 ? 1.1653 0.8457 0.8788 0.0172  0.2312  0.0920  470 PRO A CD  
1246 N N   . THR A 171 ? 1.2820 0.9683 0.7951 0.0808  0.2785  0.1188  471 THR A N   
1247 C CA  . THR A 171 ? 1.3506 1.0438 0.7865 0.1049  0.2988  0.1216  471 THR A CA  
1248 C C   . THR A 171 ? 1.3510 1.0670 0.7411 0.1283  0.2516  0.0894  471 THR A C   
1249 O O   . THR A 171 ? 1.4114 1.1270 0.7155 0.1563  0.2553  0.0931  471 THR A O   
1250 C CB  . THR A 171 ? 1.3580 1.0734 0.8277 0.0914  0.3425  0.1111  471 THR A CB  
1251 O OG1 . THR A 171 ? 1.2916 1.0395 0.8342 0.0766  0.3151  0.0706  471 THR A OG1 
1252 C CG2 . THR A 171 ? 1.3842 1.0825 0.9037 0.0660  0.3943  0.1404  471 THR A CG2 
1253 N N   . ASP A 172 ? 1.3242 1.0588 0.7701 0.1165  0.2091  0.0573  472 ASP A N   
1254 C CA  . ASP A 172 ? 1.3378 1.0922 0.7586 0.1315  0.1638  0.0233  472 ASP A CA  
1255 C C   . ASP A 172 ? 1.3147 1.0629 0.6880 0.1525  0.1310  0.0368  472 ASP A C   
1256 O O   . ASP A 172 ? 1.2662 1.0225 0.6813 0.1452  0.0954  0.0259  472 ASP A O   
1257 C CB  . ASP A 172 ? 1.3177 1.0873 0.8171 0.1103  0.1343  -0.0085 472 ASP A CB  
1258 C CG  . ASP A 172 ? 1.3385 1.1198 0.8915 0.0949  0.1532  -0.0286 472 ASP A CG  
1259 O OD1 . ASP A 172 ? 1.4063 1.1907 0.9464 0.0979  0.1925  -0.0210 472 ASP A OD1 
1260 O OD2 . ASP A 172 ? 1.3241 1.1119 0.9330 0.0813  0.1299  -0.0498 472 ASP A OD2 
1261 N N   . LEU A 173 ? 1.4119 1.1484 0.6961 0.1815  0.1429  0.0601  473 LEU A N   
1262 C CA  . LEU A 173 ? 1.5134 1.2464 0.7489 0.2083  0.1106  0.0763  473 LEU A CA  
1263 C C   . LEU A 173 ? 1.5085 1.2790 0.7419 0.2185  0.0538  0.0313  473 LEU A C   
1264 O O   . LEU A 173 ? 1.4869 1.2694 0.7345 0.2270  0.0163  0.0313  473 LEU A O   
1265 C CB  . LEU A 173 ? 1.6526 1.3606 0.7832 0.2416  0.1375  0.1164  473 LEU A CB  
1266 C CG  . LEU A 173 ? 1.6875 1.3477 0.8174 0.2359  0.1875  0.1718  473 LEU A CG  
1267 C CD1 . LEU A 173 ? 1.5730 1.2185 0.7904 0.2124  0.1781  0.1808  473 LEU A CD1 
1268 C CD2 . LEU A 173 ? 1.7109 1.3592 0.8479 0.2170  0.2492  0.1823  473 LEU A CD2 
1269 N N   . GLU A 174 ? 1.5360 1.3252 0.7561 0.2179  0.0487  -0.0088 474 GLU A N   
1270 C CA  . GLU A 174 ? 1.5411 1.3621 0.7528 0.2276  -0.0028 -0.0560 474 GLU A CA  
1271 C C   . GLU A 174 ? 1.4173 1.2532 0.7306 0.1985  -0.0335 -0.0795 474 GLU A C   
1272 O O   . GLU A 174 ? 1.3590 1.2200 0.6873 0.2042  -0.0774 -0.0968 474 GLU A O   
1273 C CB  . GLU A 174 ? 1.5882 1.4158 0.7606 0.2338  0.0065  -0.0937 474 GLU A CB  
1274 C CG  . GLU A 174 ? 1.7338 1.5531 0.7879 0.2696  0.0304  -0.0750 474 GLU A CG  
1275 C CD  . GLU A 174 ? 1.8589 1.6984 0.8296 0.3063  -0.0171 -0.0877 474 GLU A CD  
1276 O OE1 . GLU A 174 ? 1.9200 1.7846 0.8819 0.3110  -0.0547 -0.1431 474 GLU A OE1 
1277 O OE2 . GLU A 174 ? 1.8678 1.6979 0.7828 0.3318  -0.0190 -0.0450 474 GLU A OE2 
1278 N N   . ILE A 175 ? 1.3121 1.1347 0.6953 0.1685  -0.0087 -0.0794 475 ILE A N   
1279 C CA  . ILE A 175 ? 1.2257 1.0549 0.6978 0.1411  -0.0277 -0.0945 475 ILE A CA  
1280 C C   . ILE A 175 ? 1.2028 1.0363 0.6965 0.1432  -0.0430 -0.0689 475 ILE A C   
1281 O O   . ILE A 175 ? 1.1187 0.9735 0.6591 0.1352  -0.0747 -0.0872 475 ILE A O   
1282 C CB  . ILE A 175 ? 1.1540 0.9658 0.6806 0.1164  0.0044  -0.0898 475 ILE A CB  
1283 C CG1 . ILE A 175 ? 1.1605 0.9724 0.6767 0.1177  0.0154  -0.1206 475 ILE A CG1 
1284 C CG2 . ILE A 175 ? 1.0463 0.8585 0.6524 0.0915  -0.0096 -0.0940 475 ILE A CG2 
1285 C CD1 . ILE A 175 ? 1.1400 0.9412 0.6849 0.1069  0.0553  -0.1080 475 ILE A CD1 
1286 N N   . TYR A 176 ? 1.2656 1.0772 0.7277 0.1544  -0.0169 -0.0266 476 TYR A N   
1287 C CA  . TYR A 176 ? 1.2581 1.0662 0.7321 0.1630  -0.0264 0.0008  476 TYR A CA  
1288 C C   . TYR A 176 ? 1.2572 1.0975 0.7021 0.1906  -0.0711 -0.0115 476 TYR A C   
1289 O O   . TYR A 176 ? 1.2227 1.0842 0.7166 0.1893  -0.0966 -0.0157 476 TYR A O   
1290 C CB  . TYR A 176 ? 1.3368 1.1059 0.7722 0.1724  0.0134  0.0469  476 TYR A CB  
1291 C CG  . TYR A 176 ? 1.4030 1.1595 0.8500 0.1846  0.0062  0.0756  476 TYR A CG  
1292 C CD1 . TYR A 176 ? 1.3949 1.1421 0.9131 0.1617  0.0127  0.0781  476 TYR A CD1 
1293 C CD2 . TYR A 176 ? 1.4800 1.2352 0.8654 0.2225  -0.0099 0.0977  476 TYR A CD2 
1294 C CE1 . TYR A 176 ? 1.4294 1.1650 0.9615 0.1748  0.0068  0.0994  476 TYR A CE1 
1295 C CE2 . TYR A 176 ? 1.5362 1.2797 0.9377 0.2376  -0.0176 0.1223  476 TYR A CE2 
1296 C CZ  . TYR A 176 ? 1.4778 1.2109 0.9552 0.2129  -0.0077 0.1219  476 TYR A CZ  
1297 O OH  . TYR A 176 ? 1.4298 1.1495 0.9263 0.2287  -0.0121 0.1426  476 TYR A OH  
1298 N N   . LYS A 177 ? 1.2940 1.1422 0.6587 0.2174  -0.0809 -0.0187 477 LYS A N   
1299 C CA  . LYS A 177 ? 1.3271 1.2099 0.6545 0.2490  -0.1276 -0.0312 477 LYS A CA  
1300 C C   . LYS A 177 ? 1.2591 1.1865 0.6609 0.2298  -0.1700 -0.0817 477 LYS A C   
1301 O O   . LYS A 177 ? 1.2545 1.2203 0.6760 0.2444  -0.2106 -0.0924 477 LYS A O   
1302 C CB  . LYS A 177 ? 1.4379 1.3190 0.6526 0.2839  -0.1293 -0.0308 477 LYS A CB  
1303 C CG  . LYS A 177 ? 1.5199 1.3603 0.6521 0.3133  -0.0946 0.0280  477 LYS A CG  
1304 C CD  . LYS A 177 ? 1.6568 1.5009 0.6643 0.3608  -0.1076 0.0363  477 LYS A CD  
1305 C CE  . LYS A 177 ? 1.7361 1.5386 0.6747 0.3942  -0.0832 0.1019  477 LYS A CE  
1306 N NZ  . LYS A 177 ? 1.8607 1.6623 0.6670 0.4462  -0.0953 0.1185  477 LYS A NZ  
1307 N N   . ALA A 178 ? 1.2167 1.1386 0.6656 0.1971  -0.1592 -0.1115 478 ALA A N   
1308 C CA  . ALA A 178 ? 1.2046 1.1590 0.7239 0.1755  -0.1929 -0.1584 478 ALA A CA  
1309 C C   . ALA A 178 ? 1.1596 1.1221 0.7709 0.1523  -0.1920 -0.1473 478 ALA A C   
1310 O O   . ALA A 178 ? 1.1784 1.1810 0.8448 0.1471  -0.2251 -0.1708 478 ALA A O   
1311 C CB  . ALA A 178 ? 1.2106 1.1471 0.7390 0.1542  -0.1796 -0.1909 478 ALA A CB  
1312 N N   . PHE A 179 ? 1.1206 1.0482 0.7498 0.1388  -0.1533 -0.1133 479 PHE A N   
1313 C CA  . PHE A 179 ? 1.0586 0.9902 0.7631 0.1196  -0.1481 -0.1027 479 PHE A CA  
1314 C C   . PHE A 179 ? 1.1112 1.0687 0.8206 0.1436  -0.1673 -0.0855 479 PHE A C   
1315 O O   . PHE A 179 ? 1.1473 1.1363 0.9253 0.1338  -0.1823 -0.0966 479 PHE A O   
1316 C CB  . PHE A 179 ? 1.0401 0.9296 0.7531 0.1030  -0.1065 -0.0756 479 PHE A CB  
1317 C CG  . PHE A 179 ? 1.0589 0.9336 0.8032 0.0757  -0.0942 -0.0958 479 PHE A CG  
1318 C CD1 . PHE A 179 ? 1.2052 1.0764 0.9196 0.0773  -0.0976 -0.1209 479 PHE A CD1 
1319 C CD2 . PHE A 179 ? 1.0017 0.8653 0.8019 0.0523  -0.0805 -0.0904 479 PHE A CD2 
1320 C CE1 . PHE A 179 ? 1.1572 1.0110 0.9023 0.0568  -0.0868 -0.1381 479 PHE A CE1 
1321 C CE2 . PHE A 179 ? 1.0596 0.9062 0.8833 0.0328  -0.0709 -0.1048 479 PHE A CE2 
1322 C CZ  . PHE A 179 ? 1.1080 0.9488 0.9074 0.0354  -0.0744 -0.1281 479 PHE A CZ  
1323 N N   . SER A 180 ? 1.2133 1.1572 0.8515 0.1768  -0.1645 -0.0568 480 SER A N   
1324 C CA  . SER A 180 ? 1.2529 1.2194 0.8892 0.2078  -0.1863 -0.0393 480 SER A CA  
1325 C C   . SER A 180 ? 1.2053 1.2368 0.8748 0.2157  -0.2374 -0.0788 480 SER A C   
1326 O O   . SER A 180 ? 1.1335 1.2028 0.8714 0.2159  -0.2546 -0.0845 480 SER A O   
1327 C CB  . SER A 180 ? 1.3472 1.2825 0.8922 0.2447  -0.1758 -0.0015 480 SER A CB  
1328 O OG  . SER A 180 ? 1.5265 1.4669 0.9979 0.2588  -0.1876 -0.0169 480 SER A OG  
1329 N N   . SER A 181 ? 1.2560 1.3022 0.8823 0.2203  -0.2598 -0.1099 481 SER A N   
1330 C CA  . SER A 181 ? 1.3267 1.4358 0.9776 0.2287  -0.3132 -0.1541 481 SER A CA  
1331 C C   . SER A 181 ? 1.2437 1.3849 1.0112 0.1879  -0.3208 -0.1884 481 SER A C   
1332 O O   . SER A 181 ? 1.2532 1.4546 1.0824 0.1918  -0.3575 -0.2119 481 SER A O   
1333 C CB  . SER A 181 ? 1.4059 1.5162 0.9816 0.2399  -0.3318 -0.1849 481 SER A CB  
1334 O OG  . SER A 181 ? 1.5323 1.6217 0.9959 0.2836  -0.3280 -0.1513 481 SER A OG  
1335 N N   . GLU A 182 ? 1.1396 1.2421 0.9382 0.1502  -0.2855 -0.1905 482 GLU A N   
1336 C CA  . GLU A 182 ? 1.1009 1.2226 1.0013 0.1110  -0.2855 -0.2173 482 GLU A CA  
1337 C C   . GLU A 182 ? 1.0790 1.2201 1.0439 0.1096  -0.2742 -0.1923 482 GLU A C   
1338 O O   . GLU A 182 ? 1.0399 1.2300 1.0910 0.0949  -0.2910 -0.2149 482 GLU A O   
1339 C CB  . GLU A 182 ? 1.0636 1.1341 0.9666 0.0790  -0.2530 -0.2228 482 GLU A CB  
1340 C CG  . GLU A 182 ? 1.0164 1.0914 1.0161 0.0385  -0.2444 -0.2414 482 GLU A CG  
1341 C CD  . GLU A 182 ? 1.0459 1.1680 1.1150 0.0207  -0.2802 -0.2915 482 GLU A CD  
1342 O OE1 . GLU A 182 ? 1.1058 1.2524 1.1455 0.0341  -0.3175 -0.3284 482 GLU A OE1 
1343 O OE2 . GLU A 182 ? 0.9715 1.1068 1.1289 -0.0083 -0.2686 -0.2943 482 GLU A OE2 
1344 N N   . MET A 183 ? 1.1207 1.2246 1.0462 0.1255  -0.2446 -0.1477 483 MET A N   
1345 C CA  . MET A 183 ? 1.0968 1.2122 1.0738 0.1286  -0.2307 -0.1250 483 MET A CA  
1346 C C   . MET A 183 ? 1.0917 1.2704 1.0931 0.1607  -0.2707 -0.1330 483 MET A C   
1347 O O   . MET A 183 ? 1.0289 1.2571 1.1186 0.1509  -0.2788 -0.1476 483 MET A O   
1348 C CB  . MET A 183 ? 1.0795 1.1369 1.0057 0.1398  -0.1935 -0.0812 483 MET A CB  
1349 C CG  . MET A 183 ? 1.0448 1.1064 1.0212 0.1425  -0.1756 -0.0623 483 MET A CG  
1350 S SD  . MET A 183 ? 1.0170 1.0070 0.9362 0.1547  -0.1360 -0.0186 483 MET A SD  
1351 C CE  . MET A 183 ? 0.9804 0.9348 0.9217 0.1106  -0.1008 -0.0239 483 MET A CE  
1352 N N   . ALA A 184 ? 1.1180 1.2970 1.0408 0.2006  -0.2948 -0.1227 484 ALA A N   
1353 C CA  . ALA A 184 ? 1.1548 1.3968 1.0884 0.2383  -0.3417 -0.1323 484 ALA A CA  
1354 C C   . ALA A 184 ? 1.1765 1.4939 1.2081 0.2148  -0.3767 -0.1844 484 ALA A C   
1355 O O   . ALA A 184 ? 1.1275 1.4987 1.2472 0.2159  -0.3861 -0.1908 484 ALA A O   
1356 C CB  . ALA A 184 ? 1.2105 1.4405 1.0332 0.2788  -0.3660 -0.1234 484 ALA A CB  
1357 N N   . LYS A 185 ? 1.2611 1.5801 1.2830 0.1915  -0.3918 -0.2228 485 LYS A N   
1358 C CA  . LYS A 185 ? 1.2957 1.6779 1.4106 0.1637  -0.4245 -0.2774 485 LYS A CA  
1359 C C   . LYS A 185 ? 1.2572 1.6610 1.4922 0.1281  -0.3974 -0.2776 485 LYS A C   
1360 O O   . LYS A 185 ? 1.3026 1.7824 1.6330 0.1233  -0.4253 -0.3064 485 LYS A O   
1361 C CB  . LYS A 185 ? 1.3480 1.7001 1.4354 0.1354  -0.4263 -0.3134 485 LYS A CB  
1362 C CG  . LYS A 185 ? 1.4938 1.8593 1.4876 0.1705  -0.4702 -0.3362 485 LYS A CG  
1363 C CD  . LYS A 185 ? 1.5423 1.8696 1.4845 0.1534  -0.4690 -0.3695 485 LYS A CD  
1364 C CE  . LYS A 185 ? 1.6321 1.9804 1.4726 0.1971  -0.5131 -0.3888 485 LYS A CE  
1365 N NZ  . LYS A 185 ? 1.6668 1.9600 1.4192 0.1951  -0.4952 -0.4002 485 LYS A NZ  
1366 N N   . ARG A 186 ? 1.2186 1.5592 1.4487 0.1041  -0.3433 -0.2467 486 ARG A N   
1367 C CA  . ARG A 186 ? 1.1990 1.5489 1.5273 0.0673  -0.3108 -0.2463 486 ARG A CA  
1368 C C   . ARG A 186 ? 1.1737 1.5710 1.5578 0.0890  -0.3079 -0.2285 486 ARG A C   
1369 O O   . ARG A 186 ? 1.1637 1.6184 1.6550 0.0689  -0.3073 -0.2481 486 ARG A O   
1370 C CB  . ARG A 186 ? 1.1794 1.4493 1.4730 0.0436  -0.2576 -0.2165 486 ARG A CB  
1371 C CG  . ARG A 186 ? 1.2086 1.4353 1.4777 0.0153  -0.2532 -0.2370 486 ARG A CG  
1372 C CD  . ARG A 186 ? 1.2200 1.4877 1.5762 -0.0169 -0.2746 -0.2842 486 ARG A CD  
1373 N NE  . ARG A 186 ? 1.2228 1.4303 1.5665 -0.0480 -0.2530 -0.2930 486 ARG A NE  
1374 C CZ  . ARG A 186 ? 1.2365 1.4216 1.6437 -0.0859 -0.2214 -0.2918 486 ARG A CZ  
1375 N NH1 . ARG A 186 ? 1.2478 1.4764 1.7478 -0.1038 -0.2099 -0.2918 486 ARG A NH1 
1376 N NH2 . ARG A 186 ? 1.1995 1.3192 1.5771 -0.1037 -0.2002 -0.2900 486 ARG A NH2 
1377 N N   . SER A 187 ? 1.1641 1.5333 1.4781 0.1291  -0.3014 -0.1908 487 SER A N   
1378 C CA  . SER A 187 ? 1.1504 1.5538 1.5065 0.1570  -0.2970 -0.1718 487 SER A CA  
1379 C C   . SER A 187 ? 1.2359 1.7363 1.6592 0.1806  -0.3498 -0.2021 487 SER A C   
1380 O O   . SER A 187 ? 1.2555 1.8129 1.7710 0.1841  -0.3457 -0.2062 487 SER A O   
1381 C CB  . SER A 187 ? 1.1510 1.4947 1.4151 0.1946  -0.2816 -0.1280 487 SER A CB  
1382 O OG  . SER A 187 ? 1.2082 1.5240 1.3757 0.2153  -0.3057 -0.1242 487 SER A OG  
1383 N N   . LYS A 188 ? 1.3117 1.8356 1.6917 0.1973  -0.3996 -0.2262 488 LYS A N   
1384 C CA  . LYS A 188 ? 1.3312 1.9543 1.7740 0.2202  -0.4586 -0.2619 488 LYS A CA  
1385 C C   . LYS A 188 ? 1.2704 1.9656 1.8631 0.1763  -0.4562 -0.3012 488 LYS A C   
1386 O O   . LYS A 188 ? 1.2833 2.0691 1.9650 0.1943  -0.4874 -0.3206 488 LYS A O   
1387 C CB  . LYS A 188 ? 1.4073 2.0454 1.7791 0.2385  -0.5137 -0.2914 488 LYS A CB  
1388 C CG  . LYS A 188 ? 1.4936 2.0769 1.7190 0.2909  -0.5221 -0.2525 488 LYS A CG  
1389 C CD  . LYS A 188 ? 1.5658 2.1688 1.7741 0.3508  -0.5363 -0.2159 488 LYS A CD  
1390 C CE  . LYS A 188 ? 1.6577 2.2008 1.7197 0.4011  -0.5418 -0.1749 488 LYS A CE  
1391 N NZ  . LYS A 188 ? 1.7067 2.2712 1.7588 0.4626  -0.5617 -0.1421 488 LYS A NZ  
1392 N N   . MET A 189 ? 1.2652 1.9211 1.8890 0.1201  -0.4179 -0.3113 489 MET A N   
1393 C CA  . MET A 189 ? 1.2487 1.9508 2.0091 0.0753  -0.3928 -0.3317 489 MET A CA  
1394 C C   . MET A 189 ? 1.2571 1.9175 2.0221 0.0720  -0.3296 -0.2869 489 MET A C   
1395 O O   . MET A 189 ? 1.3246 1.9172 1.9900 0.0983  -0.3100 -0.2474 489 MET A O   
1396 C CB  . MET A 189 ? 1.2365 1.9069 2.0228 0.0182  -0.3800 -0.3612 489 MET A CB  
1397 C CG  . MET A 189 ? 1.2736 1.9550 2.0227 0.0199  -0.4350 -0.4052 489 MET A CG  
1398 S SD  . MET A 189 ? 1.2602 1.8765 2.0210 -0.0421 -0.4110 -0.4328 489 MET A SD  
1399 C CE  . MET A 189 ? 1.1783 1.6790 1.8534 -0.0512 -0.3386 -0.3714 489 MET A CE  
1400 N N   . LEU A 190 ? 1.1970 1.8948 2.0750 0.0384  -0.2951 -0.2941 490 LEU A N   
1401 C CA  . LEU A 190 ? 1.1210 1.7820 2.0020 0.0340  -0.2331 -0.2566 490 LEU A CA  
1402 C C   . LEU A 190 ? 1.1224 1.8351 2.0334 0.0817  -0.2365 -0.2418 490 LEU A C   
1403 O O   . LEU A 190 ? 1.0798 1.7722 2.0033 0.0807  -0.1853 -0.2169 490 LEU A O   
1404 C CB  . LEU A 190 ? 1.0860 1.6356 1.8432 0.0338  -0.1984 -0.2188 490 LEU A CB  
1405 C CG  . LEU A 190 ? 1.0995 1.5855 1.8135 -0.0052 -0.1900 -0.2263 490 LEU A CG  
1406 C CD1 . LEU A 190 ? 1.0762 1.4738 1.6587 0.0132  -0.1818 -0.1962 490 LEU A CD1 
1407 C CD2 . LEU A 190 ? 1.0628 1.5318 1.8386 -0.0523 -0.1389 -0.2226 490 LEU A CD2 
1408 N N   . ASN B 10  ? 0.8477 0.9691 1.1693 -0.1722 0.0881  -0.1251 310 ASN B N   
1409 C CA  . ASN B 10  ? 0.8800 0.9895 1.1741 -0.1324 0.0844  -0.1119 310 ASN B CA  
1410 C C   . ASN B 10  ? 0.7717 0.8158 1.0020 -0.1144 0.0660  -0.0973 310 ASN B C   
1411 O O   . ASN B 10  ? 0.7127 0.7105 0.8973 -0.1026 0.0767  -0.0808 310 ASN B O   
1412 C CB  . ASN B 10  ? 0.9786 1.0835 1.2620 -0.1347 0.1198  -0.1027 310 ASN B CB  
1413 C CG  . ASN B 10  ? 1.1148 1.1469 1.3359 -0.1536 0.1392  -0.0834 310 ASN B CG  
1414 O OD1 . ASN B 10  ? 1.2088 1.2005 1.4091 -0.1708 0.1310  -0.0808 310 ASN B OD1 
1415 N ND2 . ASN B 10  ? 1.1282 1.1404 1.3171 -0.1491 0.1627  -0.0712 310 ASN B ND2 
1416 N N   . ALA B 11  ? 0.7041 0.7510 0.9343 -0.1121 0.0375  -0.1063 311 ALA B N   
1417 C CA  . ALA B 11  ? 0.6942 0.6962 0.8724 -0.0927 0.0192  -0.0973 311 ALA B CA  
1418 C C   . ALA B 11  ? 0.7032 0.7334 0.8929 -0.0882 -0.0141 -0.1117 311 ALA B C   
1419 O O   . ALA B 11  ? 0.7267 0.7961 0.9582 -0.1087 -0.0225 -0.1303 311 ALA B O   
1420 C CB  . ALA B 11  ? 0.6976 0.6356 0.8297 -0.1069 0.0312  -0.0904 311 ALA B CB  
1421 N N   . MET B 12  ? 0.7098 0.7223 0.8625 -0.0627 -0.0335 -0.1034 312 MET B N   
1422 C CA  . MET B 12  ? 0.7608 0.7992 0.9145 -0.0534 -0.0682 -0.1135 312 MET B CA  
1423 C C   . MET B 12  ? 0.7776 0.7697 0.8636 -0.0371 -0.0782 -0.1013 312 MET B C   
1424 O O   . MET B 12  ? 0.7818 0.7365 0.8369 -0.0267 -0.0605 -0.0845 312 MET B O   
1425 C CB  . MET B 12  ? 0.8193 0.9125 1.0205 -0.0310 -0.0859 -0.1153 312 MET B CB  
1426 C CG  . MET B 12  ? 0.8415 0.9162 1.0277 -0.0009 -0.0802 -0.0955 312 MET B CG  
1427 S SD  . MET B 12  ? 0.8889 1.0243 1.1347 0.0300  -0.1067 -0.1022 312 MET B SD  
1428 C CE  . MET B 12  ? 0.9299 1.0174 1.1437 0.0576  -0.0919 -0.0791 312 MET B CE  
1429 N N   . VAL B 13  ? 0.8033 0.8003 0.8661 -0.0372 -0.1058 -0.1118 313 VAL B N   
1430 C CA  . VAL B 13  ? 0.8803 0.8374 0.8739 -0.0236 -0.1130 -0.1008 313 VAL B CA  
1431 C C   . VAL B 13  ? 0.9258 0.9034 0.9105 0.0009  -0.1457 -0.0922 313 VAL B C   
1432 O O   . VAL B 13  ? 1.0173 1.0409 1.0382 0.0016  -0.1740 -0.1068 313 VAL B O   
1433 C CB  . VAL B 13  ? 0.8763 0.8084 0.8275 -0.0403 -0.1164 -0.1180 313 VAL B CB  
1434 C CG1 . VAL B 13  ? 0.8973 0.7947 0.7740 -0.0267 -0.1203 -0.1078 313 VAL B CG1 
1435 C CG2 . VAL B 13  ? 0.8575 0.7590 0.8152 -0.0597 -0.0866 -0.1247 313 VAL B CG2 
1436 N N   . VAL B 14  ? 0.9164 0.8589 0.8550 0.0202  -0.1427 -0.0688 314 VAL B N   
1437 C CA  . VAL B 14  ? 0.9759 0.9202 0.8898 0.0445  -0.1748 -0.0555 314 VAL B CA  
1438 C C   . VAL B 14  ? 0.9990 0.8916 0.8251 0.0461  -0.1712 -0.0399 314 VAL B C   
1439 O O   . VAL B 14  ? 0.9309 0.7868 0.7327 0.0453  -0.1426 -0.0243 314 VAL B O   
1440 C CB  . VAL B 14  ? 1.0270 0.9775 0.9782 0.0676  -0.1741 -0.0398 314 VAL B CB  
1441 C CG1 . VAL B 14  ? 1.1346 1.0905 1.0717 0.0963  -0.2156 -0.0289 314 VAL B CG1 
1442 C CG2 . VAL B 14  ? 0.9468 0.9443 0.9810 0.0613  -0.1606 -0.0559 314 VAL B CG2 
1443 N N   . ASN B 15  ? 1.1004 0.9935 0.8785 0.0465  -0.1994 -0.0464 315 ASN B N   
1444 C CA  . ASN B 15  ? 1.2374 1.0857 0.9268 0.0419  -0.1903 -0.0375 315 ASN B CA  
1445 C C   . ASN B 15  ? 1.1827 1.0107 0.8684 0.0218  -0.1478 -0.0479 315 ASN B C   
1446 O O   . ASN B 15  ? 1.2202 1.0629 0.9295 0.0055  -0.1438 -0.0740 315 ASN B O   
1447 C CB  . ASN B 15  ? 1.3484 1.1570 0.9869 0.0605  -0.1922 -0.0029 315 ASN B CB  
1448 C CG  . ASN B 15  ? 1.3916 1.2128 1.0280 0.0859  -0.2394 0.0083  315 ASN B CG  
1449 O OD1 . ASN B 15  ? 1.4495 1.3132 1.1099 0.0889  -0.2746 -0.0120 315 ASN B OD1 
1450 N ND2 . ASN B 15  ? 1.4178 1.1999 1.0240 0.1047  -0.2431 0.0400  315 ASN B ND2 
1451 N N   . ASN B 16  ? 1.1690 0.9626 0.8281 0.0233  -0.1176 -0.0285 316 ASN B N   
1452 C CA  . ASN B 16  ? 1.1887 0.9662 0.8458 0.0094  -0.0799 -0.0381 316 ASN B CA  
1453 C C   . ASN B 16  ? 1.0653 0.8466 0.7833 0.0102  -0.0582 -0.0319 316 ASN B C   
1454 O O   . ASN B 16  ? 1.0171 0.7824 0.7344 0.0057  -0.0289 -0.0303 316 ASN B O   
1455 C CB  . ASN B 16  ? 1.3371 1.0814 0.9244 0.0071  -0.0585 -0.0256 316 ASN B CB  
1456 C CG  . ASN B 16  ? 1.4978 1.2365 1.0342 -0.0035 -0.0530 -0.0490 316 ASN B CG  
1457 O OD1 . ASN B 16  ? 1.5733 1.3251 1.0963 -0.0054 -0.0808 -0.0669 316 ASN B OD1 
1458 N ND2 . ASN B 16  ? 1.5715 1.2940 1.0824 -0.0104 -0.0175 -0.0524 316 ASN B ND2 
1459 N N   . LEU B 17  ? 1.0064 0.8126 0.7771 0.0172  -0.0735 -0.0300 317 LEU B N   
1460 C CA  . LEU B 17  ? 0.9038 0.7141 0.7244 0.0192  -0.0556 -0.0244 317 LEU B CA  
1461 C C   . LEU B 17  ? 0.8641 0.7035 0.7371 0.0090  -0.0575 -0.0429 317 LEU B C   
1462 O O   . LEU B 17  ? 0.8710 0.7412 0.7675 0.0083  -0.0802 -0.0530 317 LEU B O   
1463 C CB  . LEU B 17  ? 0.8919 0.7003 0.7242 0.0369  -0.0654 -0.0048 317 LEU B CB  
1464 C CG  . LEU B 17  ? 0.8333 0.6451 0.7115 0.0402  -0.0478 -0.0017 317 LEU B CG  
1465 C CD1 . LEU B 17  ? 0.8754 0.6547 0.7326 0.0494  -0.0403 0.0183  317 LEU B CD1 
1466 C CD2 . LEU B 17  ? 0.8214 0.6705 0.7533 0.0485  -0.0621 -0.0096 317 LEU B CD2 
1467 N N   . THR B 18  ? 0.8164 0.6446 0.7060 0.0001  -0.0334 -0.0471 318 THR B N   
1468 C CA  . THR B 18  ? 0.7905 0.6348 0.7243 -0.0113 -0.0276 -0.0573 318 THR B CA  
1469 C C   . THR B 18  ? 0.7544 0.6059 0.7184 -0.0028 -0.0160 -0.0456 318 THR B C   
1470 O O   . THR B 18  ? 0.7846 0.6144 0.7346 0.0044  -0.0025 -0.0350 318 THR B O   
1471 C CB  . THR B 18  ? 0.7813 0.5972 0.7016 -0.0233 -0.0110 -0.0671 318 THR B CB  
1472 O OG1 . THR B 18  ? 0.7925 0.6069 0.6913 -0.0324 -0.0242 -0.0841 318 THR B OG1 
1473 C CG2 . THR B 18  ? 0.7529 0.5675 0.7063 -0.0343 0.0019  -0.0687 318 THR B CG2 
1474 N N   . LEU B 19  ? 0.7382 0.6228 0.7455 -0.0055 -0.0197 -0.0509 319 LEU B N   
1475 C CA  . LEU B 19  ? 0.7063 0.6006 0.7409 0.0015  -0.0065 -0.0448 319 LEU B CA  
1476 C C   . LEU B 19  ? 0.6839 0.5974 0.7514 -0.0169 0.0078  -0.0541 319 LEU B C   
1477 O O   . LEU B 19  ? 0.6337 0.5794 0.7310 -0.0293 -0.0002 -0.0668 319 LEU B O   
1478 C CB  . LEU B 19  ? 0.7429 0.6621 0.7976 0.0216  -0.0235 -0.0418 319 LEU B CB  
1479 C CG  . LEU B 19  ? 0.7698 0.7082 0.8608 0.0312  -0.0119 -0.0427 319 LEU B CG  
1480 C CD1 . LEU B 19  ? 0.7869 0.6892 0.8536 0.0338  0.0073  -0.0331 319 LEU B CD1 
1481 C CD2 . LEU B 19  ? 0.7781 0.7363 0.8906 0.0560  -0.0326 -0.0419 319 LEU B CD2 
1482 N N   . GLN B 20  ? 0.7311 0.6249 0.7915 -0.0195 0.0288  -0.0475 320 GLN B N   
1483 C CA  . GLN B 20  ? 0.8055 0.7013 0.8787 -0.0398 0.0470  -0.0507 320 GLN B CA  
1484 C C   . GLN B 20  ? 0.7256 0.6292 0.8057 -0.0329 0.0640  -0.0458 320 GLN B C   
1485 O O   . GLN B 20  ? 0.6960 0.5795 0.7554 -0.0170 0.0649  -0.0382 320 GLN B O   
1486 C CB  . GLN B 20  ? 0.9124 0.7597 0.9512 -0.0514 0.0554  -0.0458 320 GLN B CB  
1487 C CG  . GLN B 20  ? 0.9748 0.7991 0.9902 -0.0489 0.0418  -0.0504 320 GLN B CG  
1488 C CD  . GLN B 20  ? 0.9778 0.7567 0.9694 -0.0592 0.0484  -0.0514 320 GLN B CD  
1489 O OE1 . GLN B 20  ? 1.1277 0.8897 1.1217 -0.0765 0.0594  -0.0495 320 GLN B OE1 
1490 N NE2 . GLN B 20  ? 0.9198 0.6767 0.8875 -0.0488 0.0423  -0.0550 320 GLN B NE2 
1491 N N   . ILE B 21  ? 0.7527 0.6855 0.8608 -0.0481 0.0796  -0.0522 321 ILE B N   
1492 C CA  . ILE B 21  ? 0.7467 0.6826 0.8506 -0.0461 0.1010  -0.0495 321 ILE B CA  
1493 C C   . ILE B 21  ? 0.7966 0.6925 0.8642 -0.0672 0.1186  -0.0390 321 ILE B C   
1494 O O   . ILE B 21  ? 0.8693 0.7634 0.9447 -0.0927 0.1260  -0.0406 321 ILE B O   
1495 C CB  . ILE B 21  ? 0.7222 0.7183 0.8779 -0.0486 0.1122  -0.0642 321 ILE B CB  
1496 C CG1 . ILE B 21  ? 0.7194 0.7500 0.9111 -0.0225 0.0900  -0.0735 321 ILE B CG1 
1497 C CG2 . ILE B 21  ? 0.7628 0.7598 0.9050 -0.0495 0.1395  -0.0637 321 ILE B CG2 
1498 C CD1 . ILE B 21  ? 0.7492 0.8489 1.0074 -0.0263 0.0912  -0.0926 321 ILE B CD1 
1499 N N   . VAL B 22  ? 0.7831 0.6458 0.8111 -0.0565 0.1238  -0.0286 322 VAL B N   
1500 C CA  . VAL B 22  ? 0.7720 0.5856 0.7548 -0.0684 0.1327  -0.0148 322 VAL B CA  
1501 C C   . VAL B 22  ? 0.8295 0.6381 0.7832 -0.0656 0.1495  -0.0095 322 VAL B C   
1502 O O   . VAL B 22  ? 0.8815 0.7037 0.8366 -0.0452 0.1445  -0.0153 322 VAL B O   
1503 C CB  . VAL B 22  ? 0.7506 0.5281 0.7114 -0.0514 0.1120  -0.0097 322 VAL B CB  
1504 C CG1 . VAL B 22  ? 0.7899 0.5211 0.7041 -0.0452 0.1121  0.0035  322 VAL B CG1 
1505 C CG2 . VAL B 22  ? 0.7930 0.5607 0.7645 -0.0608 0.1015  -0.0142 322 VAL B CG2 
1506 N N   . GLN B 23  ? 0.8727 0.6563 0.7947 -0.0875 0.1691  0.0016  323 GLN B N   
1507 C CA  . GLN B 23  ? 0.8961 0.6626 0.7707 -0.0864 0.1842  0.0098  323 GLN B CA  
1508 C C   . GLN B 23  ? 0.8869 0.5914 0.7049 -0.0747 0.1669  0.0271  323 GLN B C   
1509 O O   . GLN B 23  ? 1.0117 0.6712 0.8046 -0.0880 0.1666  0.0415  323 GLN B O   
1510 C CB  . GLN B 23  ? 0.9843 0.7553 0.8484 -0.1187 0.2175  0.0149  323 GLN B CB  
1511 C CG  . GLN B 23  ? 1.0262 0.8709 0.9565 -0.1290 0.2361  -0.0064 323 GLN B CG  
1512 C CD  . GLN B 23  ? 1.1323 0.9908 1.0609 -0.1657 0.2745  -0.0042 323 GLN B CD  
1513 O OE1 . GLN B 23  ? 1.1392 0.9849 1.0794 -0.1955 0.2818  0.0016  323 GLN B OE1 
1514 N NE2 . GLN B 23  ? 1.2008 1.0882 1.1179 -0.1656 0.3015  -0.0118 323 GLN B NE2 
1515 N N   . GLY B 24  ? 0.8291 0.5313 0.6308 -0.0497 0.1514  0.0240  324 GLY B N   
1516 C CA  . GLY B 24  ? 0.8659 0.5192 0.6184 -0.0359 0.1328  0.0374  324 GLY B CA  
1517 C C   . GLY B 24  ? 0.8681 0.5348 0.6121 -0.0131 0.1188  0.0274  324 GLY B C   
1518 O O   . GLY B 24  ? 0.8628 0.5661 0.6257 -0.0110 0.1290  0.0126  324 GLY B O   
1519 N N   . HIS B 25  ? 0.9151 0.5525 0.6350 0.0044  0.0941  0.0332  325 HIS B N   
1520 C CA  . HIS B 25  ? 0.9009 0.5530 0.6221 0.0239  0.0762  0.0205  325 HIS B CA  
1521 C C   . HIS B 25  ? 0.8678 0.5397 0.6427 0.0350  0.0607  0.0094  325 HIS B C   
1522 O O   . HIS B 25  ? 0.8787 0.5366 0.6674 0.0373  0.0525  0.0148  325 HIS B O   
1523 C CB  . HIS B 25  ? 0.9712 0.5873 0.6370 0.0370  0.0554  0.0308  325 HIS B CB  
1524 C CG  . HIS B 25  ? 1.0804 0.6669 0.6753 0.0268  0.0687  0.0457  325 HIS B CG  
1525 N ND1 . HIS B 25  ? 1.1339 0.7007 0.6709 0.0398  0.0509  0.0484  325 HIS B ND1 
1526 C CD2 . HIS B 25  ? 1.1101 0.6831 0.6788 0.0035  0.0982  0.0586  325 HIS B CD2 
1527 C CE1 . HIS B 25  ? 1.1991 0.7368 0.6687 0.0253  0.0703  0.0648  325 HIS B CE1 
1528 N NE2 . HIS B 25  ? 1.1746 0.7164 0.6649 0.0015  0.1014  0.0712  325 HIS B NE2 
1529 N N   . ILE B 26  ? 0.8207 0.5216 0.6221 0.0413  0.0584  -0.0069 326 ILE B N   
1530 C CA  . ILE B 26  ? 0.7799 0.4987 0.6271 0.0473  0.0490  -0.0164 326 ILE B CA  
1531 C C   . ILE B 26  ? 0.7887 0.4994 0.6375 0.0597  0.0273  -0.0178 326 ILE B C   
1532 O O   . ILE B 26  ? 0.7997 0.5183 0.6807 0.0619  0.0236  -0.0204 326 ILE B O   
1533 C CB  . ILE B 26  ? 0.7741 0.5151 0.6436 0.0493  0.0525  -0.0318 326 ILE B CB  
1534 C CG1 . ILE B 26  ? 0.7307 0.4825 0.6405 0.0506  0.0473  -0.0365 326 ILE B CG1 
1535 C CG2 . ILE B 26  ? 0.8135 0.5520 0.6586 0.0561  0.0434  -0.0432 326 ILE B CG2 
1536 C CD1 . ILE B 26  ? 0.7329 0.4916 0.6622 0.0443  0.0570  -0.0299 326 ILE B CD1 
1537 N N   . GLU B 27  ? 0.8088 0.5079 0.6239 0.0685  0.0129  -0.0181 327 GLU B N   
1538 C CA  . GLU B 27  ? 0.8460 0.5463 0.6706 0.0835  -0.0123 -0.0233 327 GLU B CA  
1539 C C   . GLU B 27  ? 0.8757 0.5492 0.6903 0.0923  -0.0208 -0.0095 327 GLU B C   
1540 O O   . GLU B 27  ? 0.8496 0.5279 0.6824 0.1085  -0.0417 -0.0152 327 GLU B O   
1541 C CB  . GLU B 27  ? 0.9001 0.5999 0.6927 0.0921  -0.0308 -0.0312 327 GLU B CB  
1542 C CG  . GLU B 27  ? 0.9797 0.6432 0.7011 0.0964  -0.0365 -0.0145 327 GLU B CG  
1543 C CD  . GLU B 27  ? 1.0247 0.6742 0.7074 0.0798  -0.0074 -0.0045 327 GLU B CD  
1544 O OE1 . GLU B 27  ? 0.9647 0.6371 0.6878 0.0685  0.0136  -0.0117 327 GLU B OE1 
1545 O OE2 . GLU B 27  ? 1.0575 0.6758 0.6728 0.0779  -0.0050 0.0101  327 GLU B OE2 
1546 N N   . TRP B 28  ? 0.9140 0.5593 0.7031 0.0818  -0.0052 0.0064  328 TRP B N   
1547 C CA  . TRP B 28  ? 0.9760 0.5847 0.7526 0.0887  -0.0124 0.0189  328 TRP B CA  
1548 C C   . TRP B 28  ? 0.9300 0.5464 0.7450 0.0797  0.0018  0.0143  328 TRP B C   
1549 O O   . TRP B 28  ? 0.8844 0.4663 0.6877 0.0780  0.0035  0.0230  328 TRP B O   
1550 C CB  . TRP B 28  ? 1.0203 0.5804 0.7335 0.0803  -0.0062 0.0412  328 TRP B CB  
1551 C CG  . TRP B 28  ? 1.1005 0.6408 0.7580 0.0916  -0.0235 0.0495  328 TRP B CG  
1552 C CD1 . TRP B 28  ? 1.1510 0.7074 0.8109 0.1131  -0.0523 0.0388  328 TRP B CD1 
1553 C CD2 . TRP B 28  ? 1.1853 0.6832 0.7699 0.0805  -0.0136 0.0708  328 TRP B CD2 
1554 N NE1 . TRP B 28  ? 1.2173 0.7436 0.8067 0.1184  -0.0646 0.0515  328 TRP B NE1 
1555 C CE2 . TRP B 28  ? 1.2764 0.7635 0.8144 0.0985  -0.0395 0.0730  328 TRP B CE2 
1556 C CE3 . TRP B 28  ? 1.2368 0.7068 0.7916 0.0549  0.0154  0.0874  328 TRP B CE3 
1557 C CZ2 . TRP B 28  ? 1.3701 0.8139 0.8222 0.0928  -0.0363 0.0938  328 TRP B CZ2 
1558 C CZ3 . TRP B 28  ? 1.3403 0.7694 0.8166 0.0463  0.0225  0.1080  328 TRP B CZ3 
1559 C CH2 . TRP B 28  ? 1.4057 0.8190 0.8262 0.0657  -0.0026 0.1125  328 TRP B CH2 
1560 N N   . GLN B 29  ? 0.8694 0.5258 0.7256 0.0738  0.0107  0.0004  329 GLN B N   
1561 C CA  . GLN B 29  ? 0.7944 0.4579 0.6754 0.0639  0.0235  -0.0033 329 GLN B CA  
1562 C C   . GLN B 29  ? 0.7575 0.4329 0.6702 0.0762  0.0167  -0.0154 329 GLN B C   
1563 O O   . GLN B 29  ? 0.7185 0.4120 0.6495 0.0896  0.0047  -0.0242 329 GLN B O   
1564 C CB  . GLN B 29  ? 0.7548 0.4494 0.6580 0.0515  0.0369  -0.0092 329 GLN B CB  
1565 C CG  . GLN B 29  ? 0.7839 0.4803 0.6711 0.0390  0.0487  -0.0032 329 GLN B CG  
1566 C CD  . GLN B 29  ? 0.7565 0.4368 0.6337 0.0241  0.0592  0.0043  329 GLN B CD  
1567 O OE1 . GLN B 29  ? 0.8705 0.5593 0.7675 0.0169  0.0624  -0.0002 329 GLN B OE1 
1568 N NE2 . GLN B 29  ? 0.8099 0.4682 0.6545 0.0165  0.0656  0.0150  329 GLN B NE2 
1569 N N   . THR B 30  ? 0.7027 0.3702 0.6220 0.0695  0.0258  -0.0181 330 THR B N   
1570 C CA  . THR B 30  ? 0.6973 0.3774 0.6429 0.0776  0.0269  -0.0321 330 THR B CA  
1571 C C   . THR B 30  ? 0.6558 0.3609 0.6130 0.0630  0.0412  -0.0371 330 THR B C   
1572 O O   . THR B 30  ? 0.7127 0.4090 0.6579 0.0502  0.0474  -0.0337 330 THR B O   
1573 C CB  . THR B 30  ? 0.7641 0.4059 0.6981 0.0842  0.0236  -0.0333 330 THR B CB  
1574 O OG1 . THR B 30  ? 0.8315 0.4455 0.7532 0.1032  0.0063  -0.0272 330 THR B OG1 
1575 C CG2 . THR B 30  ? 0.7951 0.4525 0.7557 0.0940  0.0281  -0.0525 330 THR B CG2 
1576 N N   . ALA B 31  ? 0.6250 0.3605 0.6046 0.0636  0.0454  -0.0444 331 ALA B N   
1577 C CA  . ALA B 31  ? 0.6140 0.3642 0.5952 0.0513  0.0577  -0.0457 331 ALA B CA  
1578 C C   . ALA B 31  ? 0.6168 0.3935 0.6229 0.0521  0.0651  -0.0552 331 ALA B C   
1579 O O   . ALA B 31  ? 0.6363 0.4262 0.6647 0.0608  0.0582  -0.0614 331 ALA B O   
1580 C CB  . ALA B 31  ? 0.6054 0.3564 0.5764 0.0415  0.0578  -0.0348 331 ALA B CB  
1581 N N   . ASP B 32  ? 0.5977 0.3827 0.5991 0.0426  0.0790  -0.0575 332 ASP B N   
1582 C CA  . ASP B 32  ? 0.6536 0.4627 0.6760 0.0364  0.0917  -0.0635 332 ASP B CA  
1583 C C   . ASP B 32  ? 0.6391 0.4532 0.6755 0.0317  0.0855  -0.0576 332 ASP B C   
1584 O O   . ASP B 32  ? 0.6118 0.4481 0.6806 0.0317  0.0860  -0.0678 332 ASP B O   
1585 C CB  . ASP B 32  ? 0.7034 0.5109 0.7024 0.0228  0.1079  -0.0594 332 ASP B CB  
1586 C CG  . ASP B 32  ? 0.7365 0.5409 0.7181 0.0260  0.1157  -0.0705 332 ASP B CG  
1587 O OD1 . ASP B 32  ? 0.7364 0.5454 0.7373 0.0396  0.1135  -0.0856 332 ASP B OD1 
1588 O OD2 . ASP B 32  ? 0.7656 0.5597 0.7121 0.0167  0.1211  -0.0645 332 ASP B OD2 
1589 N N   . VAL B 33  ? 0.5909 0.3866 0.6066 0.0284  0.0787  -0.0446 333 VAL B N   
1590 C CA  . VAL B 33  ? 0.5971 0.3919 0.6219 0.0243  0.0743  -0.0418 333 VAL B CA  
1591 C C   . VAL B 33  ? 0.5547 0.3377 0.5664 0.0321  0.0619  -0.0375 333 VAL B C   
1592 O O   . VAL B 33  ? 0.5427 0.3159 0.5363 0.0328  0.0615  -0.0302 333 VAL B O   
1593 C CB  . VAL B 33  ? 0.6384 0.4207 0.6514 0.0120  0.0837  -0.0313 333 VAL B CB  
1594 C CG1 . VAL B 33  ? 0.6537 0.4229 0.6703 0.0112  0.0766  -0.0285 333 VAL B CG1 
1595 C CG2 . VAL B 33  ? 0.6264 0.4186 0.6478 -0.0016 0.1016  -0.0340 333 VAL B CG2 
1596 N N   . ILE B 34  ? 0.5680 0.3549 0.5892 0.0360  0.0529  -0.0438 334 ILE B N   
1597 C CA  . ILE B 34  ? 0.6276 0.4045 0.6316 0.0412  0.0454  -0.0415 334 ILE B CA  
1598 C C   . ILE B 34  ? 0.6395 0.4134 0.6509 0.0368  0.0453  -0.0463 334 ILE B C   
1599 O O   . ILE B 34  ? 0.6243 0.4053 0.6561 0.0312  0.0438  -0.0552 334 ILE B O   
1600 C CB  . ILE B 34  ? 0.6458 0.4226 0.6414 0.0515  0.0327  -0.0456 334 ILE B CB  
1601 C CG1 . ILE B 34  ? 0.6778 0.4448 0.6626 0.0570  0.0323  -0.0397 334 ILE B CG1 
1602 C CG2 . ILE B 34  ? 0.6562 0.4234 0.6269 0.0544  0.0281  -0.0448 334 ILE B CG2 
1603 C CD1 . ILE B 34  ? 0.7268 0.4875 0.7042 0.0708  0.0163  -0.0418 334 ILE B CD1 
1604 N N   . VAL B 35  ? 0.6743 0.4385 0.6735 0.0392  0.0474  -0.0428 335 VAL B N   
1605 C CA  . VAL B 35  ? 0.7172 0.4712 0.7227 0.0384  0.0472  -0.0489 335 VAL B CA  
1606 C C   . VAL B 35  ? 0.7144 0.4693 0.7102 0.0440  0.0406  -0.0624 335 VAL B C   
1607 O O   . VAL B 35  ? 0.6867 0.4446 0.6626 0.0499  0.0425  -0.0616 335 VAL B O   
1608 C CB  . VAL B 35  ? 0.7221 0.4658 0.7254 0.0424  0.0514  -0.0412 335 VAL B CB  
1609 C CG1 . VAL B 35  ? 0.8132 0.5366 0.8246 0.0439  0.0499  -0.0483 335 VAL B CG1 
1610 C CG2 . VAL B 35  ? 0.7272 0.4684 0.7285 0.0378  0.0546  -0.0275 335 VAL B CG2 
1611 N N   . ASN B 36  ? 0.7186 0.4701 0.7270 0.0393  0.0343  -0.0759 336 ASN B N   
1612 C CA  . ASN B 36  ? 0.7401 0.4899 0.7367 0.0434  0.0257  -0.0934 336 ASN B CA  
1613 C C   . ASN B 36  ? 0.7558 0.4854 0.7549 0.0455  0.0312  -0.1019 336 ASN B C   
1614 O O   . ASN B 36  ? 0.7858 0.4996 0.7996 0.0427  0.0372  -0.0935 336 ASN B O   
1615 C CB  . ASN B 36  ? 0.7645 0.5260 0.7777 0.0371  0.0115  -0.1078 336 ASN B CB  
1616 C CG  . ASN B 36  ? 0.8087 0.5727 0.7978 0.0438  -0.0034 -0.1252 336 ASN B CG  
1617 O OD1 . ASN B 36  ? 0.8126 0.5689 0.7662 0.0525  0.0010  -0.1241 336 ASN B OD1 
1618 N ND2 . ASN B 36  ? 0.8286 0.6062 0.8353 0.0390  -0.0208 -0.1426 336 ASN B ND2 
1619 N N   . SER B 37  ? 0.7831 0.5103 0.7633 0.0523  0.0283  -0.1190 337 SER B N   
1620 C CA  . SER B 37  ? 0.7898 0.4979 0.7722 0.0589  0.0335  -0.1329 337 SER B CA  
1621 C C   . SER B 37  ? 0.7869 0.4884 0.7562 0.0580  0.0236  -0.1604 337 SER B C   
1622 O O   . SER B 37  ? 0.8037 0.5181 0.7401 0.0632  0.0213  -0.1686 337 SER B O   
1623 C CB  . SER B 37  ? 0.7850 0.5036 0.7562 0.0713  0.0464  -0.1288 337 SER B CB  
1624 O OG  . SER B 37  ? 0.7954 0.4967 0.7819 0.0818  0.0509  -0.1396 337 SER B OG  
1625 N N   . VAL B 38  ? 0.8422 0.5209 0.8335 0.0490  0.0173  -0.1741 338 VAL B N   
1626 C CA  . VAL B 38  ? 0.8829 0.5574 0.8683 0.0429  0.0032  -0.2030 338 VAL B CA  
1627 C C   . VAL B 38  ? 0.9405 0.5767 0.9343 0.0442  0.0055  -0.2250 338 VAL B C   
1628 O O   . VAL B 38  ? 1.0029 0.6100 1.0163 0.0454  0.0140  -0.2142 338 VAL B O   
1629 C CB  . VAL B 38  ? 0.8548 0.5431 0.8671 0.0244  -0.0113 -0.2063 338 VAL B CB  
1630 C CG1 . VAL B 38  ? 0.8373 0.5610 0.8449 0.0273  -0.0169 -0.1887 338 VAL B CG1 
1631 C CG2 . VAL B 38  ? 0.8406 0.5055 0.8911 0.0073  -0.0033 -0.1978 338 VAL B CG2 
1632 N N   . ASN B 39  ? 0.9586 0.5918 0.9330 0.0447  -0.0050 -0.2569 339 ASN B N   
1633 C CA  . ASN B 39  ? 0.9879 0.5828 0.9756 0.0379  -0.0103 -0.2855 339 ASN B CA  
1634 C C   . ASN B 39  ? 0.9818 0.5794 1.0017 0.0110  -0.0255 -0.2914 339 ASN B C   
1635 O O   . ASN B 39  ? 0.9341 0.5673 0.9489 0.0050  -0.0421 -0.3004 339 ASN B O   
1636 C CB  . ASN B 39  ? 1.0492 0.6419 0.9984 0.0511  -0.0129 -0.3203 339 ASN B CB  
1637 C CG  . ASN B 39  ? 1.0908 0.6431 1.0499 0.0429  -0.0223 -0.3576 339 ASN B CG  
1638 O OD1 . ASN B 39  ? 1.0801 0.6051 1.0767 0.0229  -0.0282 -0.3574 339 ASN B OD1 
1639 N ND2 . ASN B 39  ? 1.1550 0.7019 1.0774 0.0562  -0.0219 -0.3913 339 ASN B ND2 
1640 N N   . PRO B 40  ? 1.0257 0.5869 1.0809 -0.0063 -0.0200 -0.2855 340 PRO B N   
1641 C CA  . PRO B 40  ? 1.0183 0.5904 1.1124 -0.0366 -0.0270 -0.2869 340 PRO B CA  
1642 C C   . PRO B 40  ? 1.0452 0.6310 1.1480 -0.0510 -0.0495 -0.3274 340 PRO B C   
1643 O O   . PRO B 40  ? 1.0308 0.6545 1.1668 -0.0706 -0.0609 -0.3328 340 PRO B O   
1644 C CB  . PRO B 40  ? 1.0704 0.5863 1.1874 -0.0526 -0.0123 -0.2719 340 PRO B CB  
1645 C CG  . PRO B 40  ? 1.0839 0.5525 1.1753 -0.0260 -0.0049 -0.2703 340 PRO B CG  
1646 C CD  . PRO B 40  ? 1.0629 0.5706 1.1216 0.0029  -0.0063 -0.2756 340 PRO B CD  
1647 N N   . HIS B 41  ? 1.0864 0.6446 1.1611 -0.0401 -0.0564 -0.3585 341 HIS B N   
1648 C CA  . HIS B 41  ? 1.1504 0.7175 1.2233 -0.0513 -0.0806 -0.4018 341 HIS B CA  
1649 C C   . HIS B 41  ? 1.1054 0.7319 1.1490 -0.0386 -0.1007 -0.4052 341 HIS B C   
1650 O O   . HIS B 41  ? 1.1112 0.7652 1.1665 -0.0514 -0.1275 -0.4327 341 HIS B O   
1651 C CB  . HIS B 41  ? 1.2533 0.7663 1.3011 -0.0422 -0.0791 -0.4356 341 HIS B CB  
1652 C CG  . HIS B 41  ? 1.3489 0.7938 1.4231 -0.0506 -0.0625 -0.4285 341 HIS B CG  
1653 N ND1 . HIS B 41  ? 1.4402 0.8289 1.4951 -0.0317 -0.0545 -0.4470 341 HIS B ND1 
1654 C CD2 . HIS B 41  ? 1.3811 0.8013 1.4963 -0.0753 -0.0525 -0.4041 341 HIS B CD2 
1655 C CE1 . HIS B 41  ? 1.4958 0.8231 1.5782 -0.0425 -0.0441 -0.4321 341 HIS B CE1 
1656 N NE2 . HIS B 41  ? 1.4811 0.8250 1.5959 -0.0707 -0.0415 -0.4041 341 HIS B NE2 
1657 N N   . ASP B 42  ? 1.0746 0.7192 1.0806 -0.0143 -0.0901 -0.3774 342 ASP B N   
1658 C CA  . ASP B 42  ? 1.0730 0.7612 1.0422 -0.0011 -0.1085 -0.3744 342 ASP B CA  
1659 C C   . ASP B 42  ? 1.0251 0.7293 0.9788 0.0146  -0.0913 -0.3319 342 ASP B C   
1660 O O   . ASP B 42  ? 1.0106 0.7004 0.9293 0.0305  -0.0710 -0.3195 342 ASP B O   
1661 C CB  . ASP B 42  ? 1.1403 0.8204 1.0470 0.0116  -0.1207 -0.4065 342 ASP B CB  
1662 C CG  . ASP B 42  ? 1.1620 0.8785 1.0308 0.0181  -0.1534 -0.4157 342 ASP B CG  
1663 O OD1 . ASP B 42  ? 1.1340 0.8820 1.0160 0.0218  -0.1617 -0.3887 342 ASP B OD1 
1664 O OD2 . ASP B 42  ? 1.2378 0.9488 1.0628 0.0207  -0.1725 -0.4512 342 ASP B OD2 
1665 N N   . ILE B 43  ? 0.9957 0.7333 0.9793 0.0098  -0.0999 -0.3126 343 ILE B N   
1666 C CA  . ILE B 43  ? 0.9481 0.6981 0.9217 0.0220  -0.0859 -0.2753 343 ILE B CA  
1667 C C   . ILE B 43  ? 0.9423 0.7086 0.8601 0.0402  -0.1015 -0.2693 343 ILE B C   
1668 O O   . ILE B 43  ? 0.9695 0.7445 0.8774 0.0493  -0.0951 -0.2406 343 ILE B O   
1669 C CB  . ILE B 43  ? 0.9068 0.6811 0.9382 0.0095  -0.0848 -0.2596 343 ILE B CB  
1670 C CG1 . ILE B 43  ? 0.9318 0.7472 0.9891 0.0059  -0.1157 -0.2779 343 ILE B CG1 
1671 C CG2 . ILE B 43  ? 0.8999 0.6501 0.9750 -0.0112 -0.0662 -0.2596 343 ILE B CG2 
1672 C CD1 . ILE B 43  ? 0.9041 0.7544 0.9975 0.0087  -0.1158 -0.2581 343 ILE B CD1 
1673 N N   . THR B 44  ? 0.9599 0.7264 0.8382 0.0443  -0.1235 -0.2963 344 THR B N   
1674 C CA  . THR B 44  ? 0.9856 0.7598 0.7991 0.0610  -0.1414 -0.2891 344 THR B CA  
1675 C C   . THR B 44  ? 1.0436 0.7925 0.7872 0.0703  -0.1181 -0.2857 344 THR B C   
1676 O O   . THR B 44  ? 1.0815 0.8270 0.7551 0.0813  -0.1269 -0.2794 344 THR B O   
1677 C CB  . THR B 44  ? 1.0186 0.8107 0.8221 0.0609  -0.1826 -0.3204 344 THR B CB  
1678 O OG1 . THR B 44  ? 1.1204 0.8882 0.8852 0.0580  -0.1762 -0.3500 344 THR B OG1 
1679 C CG2 . THR B 44  ? 0.9825 0.8066 0.8714 0.0457  -0.2013 -0.3351 344 THR B CG2 
1680 N N   . VAL B 45  ? 1.0463 0.7775 0.8090 0.0661  -0.0884 -0.2905 345 VAL B N   
1681 C CA  . VAL B 45  ? 1.0875 0.8033 0.7984 0.0746  -0.0636 -0.2964 345 VAL B CA  
1682 C C   . VAL B 45  ? 1.0253 0.7401 0.7615 0.0768  -0.0309 -0.2683 345 VAL B C   
1683 O O   . VAL B 45  ? 0.9466 0.6610 0.7421 0.0708  -0.0267 -0.2562 345 VAL B O   
1684 C CB  . VAL B 45  ? 1.1729 0.8702 0.8867 0.0723  -0.0629 -0.3386 345 VAL B CB  
1685 C CG1 . VAL B 45  ? 1.2409 0.9286 0.8993 0.0836  -0.0367 -0.3525 345 VAL B CG1 
1686 C CG2 . VAL B 45  ? 1.2290 0.9304 0.9328 0.0656  -0.1001 -0.3702 345 VAL B CG2 
1687 N N   . GLY B 46  ? 1.0702 0.7859 0.7588 0.0837  -0.0077 -0.2594 346 GLY B N   
1688 C CA  . GLY B 46  ? 1.0730 0.7948 0.7849 0.0853  0.0223  -0.2371 346 GLY B CA  
1689 C C   . GLY B 46  ? 1.0569 0.7862 0.7482 0.0824  0.0245  -0.2012 346 GLY B C   
1690 O O   . GLY B 46  ? 1.0694 0.7985 0.7625 0.0808  0.0003  -0.1884 346 GLY B O   
1691 N N   . PRO B 47  ? 1.0857 0.8218 0.7598 0.0813  0.0533  -0.1860 347 PRO B N   
1692 C CA  . PRO B 47  ? 1.1315 0.8665 0.7871 0.0754  0.0574  -0.1522 347 PRO B CA  
1693 C C   . PRO B 47  ? 1.0973 0.8311 0.7955 0.0740  0.0378  -0.1319 347 PRO B C   
1694 O O   . PRO B 47  ? 1.1849 0.9089 0.8587 0.0762  0.0161  -0.1196 347 PRO B O   
1695 C CB  . PRO B 47  ? 1.1068 0.8579 0.7770 0.0710  0.0941  -0.1474 347 PRO B CB  
1696 C CG  . PRO B 47  ? 1.1536 0.9122 0.8077 0.0773  0.1107  -0.1797 347 PRO B CG  
1697 C CD  . PRO B 47  ? 1.1435 0.8895 0.8157 0.0851  0.0840  -0.2042 347 PRO B CD  
1698 N N   . VAL B 48  ? 1.0363 0.7795 0.7964 0.0723  0.0445  -0.1301 348 VAL B N   
1699 C CA  . VAL B 48  ? 0.9497 0.6944 0.7496 0.0696  0.0331  -0.1132 348 VAL B CA  
1700 C C   . VAL B 48  ? 0.9290 0.6737 0.7426 0.0712  0.0053  -0.1239 348 VAL B C   
1701 O O   . VAL B 48  ? 0.9231 0.6697 0.7392 0.0731  -0.0104 -0.1123 348 VAL B O   
1702 C CB  . VAL B 48  ? 0.8968 0.6489 0.7478 0.0679  0.0469  -0.1118 348 VAL B CB  
1703 C CG1 . VAL B 48  ? 0.9113 0.6642 0.8006 0.0640  0.0376  -0.0993 348 VAL B CG1 
1704 C CG2 . VAL B 48  ? 0.8886 0.6514 0.7371 0.0661  0.0704  -0.1021 348 VAL B CG2 
1705 N N   . ALA B 49  ? 0.9211 0.6649 0.7472 0.0706  -0.0016 -0.1489 349 ALA B N   
1706 C CA  . ALA B 49  ? 0.9381 0.6883 0.7890 0.0674  -0.0265 -0.1628 349 ALA B CA  
1707 C C   . ALA B 49  ? 0.9558 0.7116 0.7702 0.0748  -0.0519 -0.1613 349 ALA B C   
1708 O O   . ALA B 49  ? 0.9115 0.6829 0.7568 0.0753  -0.0724 -0.1622 349 ALA B O   
1709 C CB  . ALA B 49  ? 0.9277 0.6694 0.7891 0.0632  -0.0297 -0.1927 349 ALA B CB  
1710 N N   . LYS B 50  ? 1.0175 0.7611 0.7656 0.0813  -0.0502 -0.1596 350 LYS B N   
1711 C CA  . LYS B 50  ? 1.0886 0.8280 0.7857 0.0910  -0.0773 -0.1559 350 LYS B CA  
1712 C C   . LYS B 50  ? 1.1154 0.8482 0.8100 0.0971  -0.0804 -0.1246 350 LYS B C   
1713 O O   . LYS B 50  ? 1.0985 0.8407 0.8107 0.1065  -0.1089 -0.1234 350 LYS B O   
1714 C CB  . LYS B 50  ? 1.1596 0.8812 0.7743 0.0938  -0.0697 -0.1605 350 LYS B CB  
1715 C CG  . LYS B 50  ? 1.2392 0.9637 0.8449 0.0915  -0.0720 -0.1973 350 LYS B CG  
1716 C CD  . LYS B 50  ? 1.3162 1.0271 0.8496 0.0921  -0.0484 -0.2048 350 LYS B CD  
1717 C CE  . LYS B 50  ? 1.4227 1.1209 0.8684 0.0989  -0.0715 -0.2104 350 LYS B CE  
1718 N NZ  . LYS B 50  ? 1.5178 1.2063 0.8968 0.0967  -0.0420 -0.2233 350 LYS B NZ  
1719 N N   . SER B 51  ? 1.0915 0.8093 0.7686 0.0920  -0.0515 -0.1025 351 SER B N   
1720 C CA  . SER B 51  ? 1.0728 0.7774 0.7507 0.0945  -0.0497 -0.0746 351 SER B CA  
1721 C C   . SER B 51  ? 0.9905 0.7140 0.7337 0.0995  -0.0663 -0.0772 351 SER B C   
1722 O O   . SER B 51  ? 1.0547 0.7711 0.7932 0.1122  -0.0874 -0.0669 351 SER B O   
1723 C CB  . SER B 51  ? 1.0447 0.7434 0.7266 0.0822  -0.0145 -0.0600 351 SER B CB  
1724 O OG  . SER B 51  ? 1.1118 0.8018 0.7407 0.0762  0.0056  -0.0614 351 SER B OG  
1725 N N   . ILE B 52  ? 0.9023 0.6481 0.7042 0.0903  -0.0559 -0.0915 352 ILE B N   
1726 C CA  . ILE B 52  ? 0.8326 0.5993 0.6967 0.0897  -0.0617 -0.0946 352 ILE B CA  
1727 C C   . ILE B 52  ? 0.8568 0.6461 0.7423 0.0979  -0.0936 -0.1130 352 ILE B C   
1728 O O   . ILE B 52  ? 0.8512 0.6552 0.7676 0.1071  -0.1068 -0.1108 352 ILE B O   
1729 C CB  . ILE B 52  ? 0.7718 0.5471 0.6789 0.0753  -0.0394 -0.1004 352 ILE B CB  
1730 C CG1 . ILE B 52  ? 0.7976 0.5603 0.6977 0.0714  -0.0156 -0.0806 352 ILE B CG1 
1731 C CG2 . ILE B 52  ? 0.7161 0.5157 0.6831 0.0691  -0.0446 -0.1111 352 ILE B CG2 
1732 C CD1 . ILE B 52  ? 0.8022 0.5714 0.7428 0.0616  0.0006  -0.0799 352 ILE B CD1 
1733 N N   . LEU B 53  ? 0.8855 0.6790 0.7551 0.0958  -0.1070 -0.1336 353 LEU B N   
1734 C CA  . LEU B 53  ? 0.9051 0.7261 0.7998 0.1010  -0.1406 -0.1563 353 LEU B CA  
1735 C C   . LEU B 53  ? 0.9713 0.7882 0.8320 0.1241  -0.1716 -0.1454 353 LEU B C   
1736 O O   . LEU B 53  ? 0.9799 0.8277 0.8863 0.1345  -0.1971 -0.1557 353 LEU B O   
1737 C CB  . LEU B 53  ? 0.9128 0.7339 0.7893 0.0933  -0.1503 -0.1833 353 LEU B CB  
1738 C CG  . LEU B 53  ? 0.9200 0.7742 0.8263 0.0955  -0.1888 -0.2123 353 LEU B CG  
1739 C CD1 . LEU B 53  ? 0.8795 0.7742 0.8789 0.0839  -0.1892 -0.2245 353 LEU B CD1 
1740 C CD2 . LEU B 53  ? 0.9365 0.7839 0.8190 0.0859  -0.1966 -0.2414 353 LEU B CD2 
1741 N N   . GLN B 54  ? 1.0387 0.8172 0.8196 0.1320  -0.1692 -0.1253 354 GLN B N   
1742 C CA  . GLN B 54  ? 1.1429 0.9016 0.8764 0.1546  -0.1988 -0.1090 354 GLN B CA  
1743 C C   . GLN B 54  ? 1.1053 0.8638 0.8800 0.1651  -0.1970 -0.0926 354 GLN B C   
1744 O O   . GLN B 54  ? 1.1053 0.8804 0.9064 0.1857  -0.2293 -0.0976 354 GLN B O   
1745 C CB  . GLN B 54  ? 1.2613 0.9701 0.8950 0.1566  -0.1901 -0.0848 354 GLN B CB  
1746 C CG  . GLN B 54  ? 1.4194 1.1029 0.9910 0.1813  -0.2312 -0.0716 354 GLN B CG  
1747 C CD  . GLN B 54  ? 1.4970 1.2145 1.0811 0.1953  -0.2779 -0.1001 354 GLN B CD  
1748 O OE1 . GLN B 54  ? 1.5396 1.2557 1.0724 0.1913  -0.2883 -0.1158 354 GLN B OE1 
1749 N NE2 . GLN B 54  ? 1.4944 1.2452 1.1465 0.2128  -0.3087 -0.1097 354 GLN B NE2 
1750 N N   . GLN B 55  ? 1.0650 0.8074 0.8479 0.1521  -0.1605 -0.0765 355 GLN B N   
1751 C CA  . GLN B 55  ? 1.0778 0.8118 0.8882 0.1613  -0.1567 -0.0624 355 GLN B CA  
1752 C C   . GLN B 55  ? 1.0003 0.7840 0.8984 0.1654  -0.1643 -0.0839 355 GLN B C   
1753 O O   . GLN B 55  ? 0.9780 0.7645 0.9010 0.1842  -0.1778 -0.0817 355 GLN B O   
1754 C CB  . GLN B 55  ? 1.1035 0.8143 0.9058 0.1437  -0.1178 -0.0451 355 GLN B CB  
1755 C CG  . GLN B 55  ? 1.0623 0.7492 0.8720 0.1533  -0.1154 -0.0292 355 GLN B CG  
1756 C CD  . GLN B 55  ? 1.1108 0.7527 0.8633 0.1746  -0.1418 -0.0107 355 GLN B CD  
1757 O OE1 . GLN B 55  ? 1.1374 0.7434 0.8175 0.1702  -0.1413 0.0056  355 GLN B OE1 
1758 N NE2 . GLN B 55  ? 1.1290 0.7708 0.9107 0.1990  -0.1653 -0.0131 355 GLN B NE2 
1759 N N   . ALA B 56  ? 0.9613 0.7816 0.9066 0.1469  -0.1526 -0.1049 356 ALA B N   
1760 C CA  . ALA B 56  ? 0.8991 0.7648 0.9263 0.1420  -0.1470 -0.1224 356 ALA B CA  
1761 C C   . ALA B 56  ? 0.9126 0.8229 0.9837 0.1552  -0.1830 -0.1471 356 ALA B C   
1762 O O   . ALA B 56  ? 0.8569 0.8104 0.9986 0.1585  -0.1837 -0.1621 356 ALA B O   
1763 C CB  . ALA B 56  ? 0.8826 0.7587 0.9365 0.1138  -0.1169 -0.1299 356 ALA B CB  
1764 N N   . GLY B 57  ? 0.9891 0.8931 1.0193 0.1614  -0.2116 -0.1539 357 GLY B N   
1765 C CA  . GLY B 57  ? 1.0568 1.0013 1.1180 0.1777  -0.2552 -0.1773 357 GLY B CA  
1766 C C   . GLY B 57  ? 1.0459 1.0330 1.1578 0.1533  -0.2567 -0.2096 357 GLY B C   
1767 O O   . GLY B 57  ? 1.0166 1.0013 1.1492 0.1254  -0.2218 -0.2122 357 GLY B O   
1768 N N   . VAL B 58  ? 1.0900 1.1146 1.2238 0.1648  -0.3000 -0.2344 358 VAL B N   
1769 C CA  . VAL B 58  ? 1.0999 1.1588 1.2714 0.1414  -0.3094 -0.2683 358 VAL B CA  
1770 C C   . VAL B 58  ? 1.0580 1.1619 1.3280 0.1127  -0.2795 -0.2856 358 VAL B C   
1771 O O   . VAL B 58  ? 1.0573 1.1650 1.3483 0.0821  -0.2668 -0.3040 358 VAL B O   
1772 C CB  . VAL B 58  ? 1.1666 1.2613 1.3426 0.1632  -0.3686 -0.2921 358 VAL B CB  
1773 C CG1 . VAL B 58  ? 1.1907 1.3270 1.4157 0.1369  -0.3831 -0.3335 358 VAL B CG1 
1774 C CG2 . VAL B 58  ? 1.2304 1.2710 1.2918 0.1887  -0.3959 -0.2714 358 VAL B CG2 
1775 N N   . GLU B 59  ? 1.0096 1.1426 1.3353 0.1212  -0.2661 -0.2799 359 GLU B N   
1776 C CA  . GLU B 59  ? 0.9959 1.1773 1.4131 0.0938  -0.2367 -0.2970 359 GLU B CA  
1777 C C   . GLU B 59  ? 0.9399 1.0782 1.3349 0.0629  -0.1863 -0.2786 359 GLU B C   
1778 O O   . GLU B 59  ? 0.8950 1.0582 1.3481 0.0326  -0.1584 -0.2895 359 GLU B O   
1779 C CB  . GLU B 59  ? 1.0341 1.2595 1.5133 0.1124  -0.2315 -0.2987 359 GLU B CB  
1780 C CG  . GLU B 59  ? 1.1162 1.3883 1.6298 0.1500  -0.2829 -0.3167 359 GLU B CG  
1781 C CD  . GLU B 59  ? 1.1795 1.4038 1.6255 0.1929  -0.3039 -0.2890 359 GLU B CD  
1782 O OE1 . GLU B 59  ? 1.2518 1.4091 1.6004 0.1979  -0.3107 -0.2643 359 GLU B OE1 
1783 O OE2 . GLU B 59  ? 1.1708 1.4237 1.6631 0.2203  -0.3111 -0.2931 359 GLU B OE2 
1784 N N   . MET B 60  ? 0.9331 1.0077 1.2450 0.0707  -0.1746 -0.2500 360 MET B N   
1785 C CA  . MET B 60  ? 0.9861 1.0186 1.2726 0.0484  -0.1337 -0.2314 360 MET B CA  
1786 C C   . MET B 60  ? 1.0327 1.0497 1.3175 0.0220  -0.1305 -0.2471 360 MET B C   
1787 O O   . MET B 60  ? 1.0214 1.0211 1.3206 -0.0033 -0.0998 -0.2424 360 MET B O   
1788 C CB  . MET B 60  ? 1.0346 1.0134 1.2414 0.0663  -0.1269 -0.2012 360 MET B CB  
1789 C CG  . MET B 60  ? 1.0148 0.9575 1.2004 0.0508  -0.0887 -0.1805 360 MET B CG  
1790 S SD  . MET B 60  ? 1.1861 1.0855 1.3270 0.0367  -0.0799 -0.1810 360 MET B SD  
1791 C CE  . MET B 60  ? 1.2110 1.0826 1.2734 0.0591  -0.1001 -0.1748 360 MET B CE  
1792 N N   . LYS B 61  ? 1.0447 1.0631 1.3067 0.0295  -0.1640 -0.2658 361 LYS B N   
1793 C CA  . LYS B 61  ? 1.0441 1.0459 1.3017 0.0079  -0.1668 -0.2872 361 LYS B CA  
1794 C C   . LYS B 61  ? 1.0257 1.0714 1.3688 -0.0218 -0.1679 -0.3168 361 LYS B C   
1795 O O   . LYS B 61  ? 1.0332 1.0560 1.3842 -0.0484 -0.1584 -0.3313 361 LYS B O   
1796 C CB  . LYS B 61  ? 1.1269 1.1187 1.3252 0.0275  -0.2038 -0.2996 361 LYS B CB  
1797 C CG  . LYS B 61  ? 1.1239 1.0981 1.3072 0.0108  -0.2142 -0.3290 361 LYS B CG  
1798 C CD  . LYS B 61  ? 1.1328 1.1031 1.2508 0.0321  -0.2530 -0.3426 361 LYS B CD  
1799 C CE  . LYS B 61  ? 1.1837 1.1553 1.3099 0.0134  -0.2716 -0.3832 361 LYS B CE  
1800 N NZ  . LYS B 61  ? 1.2654 1.2223 1.3079 0.0342  -0.3027 -0.3933 361 LYS B NZ  
1801 N N   . SER B 62  ? 0.9638 1.0718 1.3735 -0.0178 -0.1786 -0.3274 362 SER B N   
1802 C CA  . SER B 62  ? 0.9672 1.1270 1.4685 -0.0498 -0.1740 -0.3562 362 SER B CA  
1803 C C   . SER B 62  ? 1.0006 1.1418 1.5258 -0.0810 -0.1227 -0.3392 362 SER B C   
1804 O O   . SER B 62  ? 1.0661 1.1929 1.6169 -0.1175 -0.1067 -0.3510 362 SER B O   
1805 C CB  . SER B 62  ? 0.9246 1.1645 1.4965 -0.0340 -0.2002 -0.3762 362 SER B CB  
1806 O OG  . SER B 62  ? 0.9028 1.1611 1.4578 -0.0113 -0.2535 -0.3973 362 SER B OG  
1807 N N   . GLU B 63  ? 1.0326 1.1699 1.5458 -0.0676 -0.0978 -0.3117 363 GLU B N   
1808 C CA  . GLU B 63  ? 1.0824 1.2027 1.6090 -0.0953 -0.0510 -0.2943 363 GLU B CA  
1809 C C   . GLU B 63  ? 1.0230 1.0650 1.4901 -0.1099 -0.0344 -0.2761 363 GLU B C   
1810 O O   . GLU B 63  ? 1.0752 1.0938 1.5551 -0.1417 -0.0032 -0.2684 363 GLU B O   
1811 C CB  . GLU B 63  ? 1.1613 1.2894 1.6771 -0.0757 -0.0306 -0.2712 363 GLU B CB  
1812 C CG  . GLU B 63  ? 1.2681 1.4031 1.8143 -0.1069 0.0155  -0.2627 363 GLU B CG  
1813 C CD  . GLU B 63  ? 1.3981 1.5163 1.9075 -0.0915 0.0405  -0.2359 363 GLU B CD  
1814 O OE1 . GLU B 63  ? 1.2940 1.3896 1.7546 -0.0580 0.0238  -0.2217 363 GLU B OE1 
1815 O OE2 . GLU B 63  ? 1.5227 1.6483 2.0493 -0.1160 0.0783  -0.2296 363 GLU B OE2 
1816 N N   . PHE B 64  ? 0.9808 0.9824 1.3835 -0.0864 -0.0549 -0.2701 364 PHE B N   
1817 C CA  . PHE B 64  ? 0.9725 0.9049 1.3233 -0.0928 -0.0425 -0.2573 364 PHE B CA  
1818 C C   . PHE B 64  ? 0.9836 0.8979 1.3571 -0.1212 -0.0486 -0.2840 364 PHE B C   
1819 O O   . PHE B 64  ? 0.9759 0.8368 1.3371 -0.1403 -0.0269 -0.2741 364 PHE B O   
1820 C CB  . PHE B 64  ? 0.9389 0.8420 1.2200 -0.0607 -0.0591 -0.2483 364 PHE B CB  
1821 C CG  . PHE B 64  ? 0.9568 0.7965 1.1943 -0.0637 -0.0452 -0.2392 364 PHE B CG  
1822 C CD1 . PHE B 64  ? 0.9720 0.7864 1.2069 -0.0750 -0.0561 -0.2644 364 PHE B CD1 
1823 C CD2 . PHE B 64  ? 0.9178 0.7248 1.1198 -0.0532 -0.0235 -0.2087 364 PHE B CD2 
1824 C CE1 . PHE B 64  ? 1.0119 0.7679 1.2112 -0.0727 -0.0440 -0.2589 364 PHE B CE1 
1825 C CE2 . PHE B 64  ? 0.9490 0.7039 1.1184 -0.0507 -0.0142 -0.2028 364 PHE B CE2 
1826 C CZ  . PHE B 64  ? 0.9805 0.7088 1.1496 -0.0592 -0.0235 -0.2277 364 PHE B CZ  
1827 N N   . LEU B 65  ? 0.9757 0.9290 1.3777 -0.1219 -0.0813 -0.3182 365 LEU B N   
1828 C CA  . LEU B 65  ? 0.9734 0.9134 1.4015 -0.1508 -0.0911 -0.3500 365 LEU B CA  
1829 C C   . LEU B 65  ? 0.9810 0.9450 1.4858 -0.1940 -0.0680 -0.3582 365 LEU B C   
1830 O O   . LEU B 65  ? 1.0858 1.0172 1.6091 -0.2268 -0.0621 -0.3746 365 LEU B O   
1831 C CB  . LEU B 65  ? 0.9714 0.9477 1.4023 -0.1387 -0.1368 -0.3866 365 LEU B CB  
1832 C CG  . LEU B 65  ? 1.0033 0.9464 1.3488 -0.1040 -0.1575 -0.3838 365 LEU B CG  
1833 C CD1 . LEU B 65  ? 1.0220 1.0091 1.3621 -0.0873 -0.2054 -0.4136 365 LEU B CD1 
1834 C CD2 . LEU B 65  ? 1.0358 0.9083 1.3391 -0.1126 -0.1460 -0.3903 365 LEU B CD2 
1835 N N   . ALA B 66  ? 0.9736 0.9915 1.5218 -0.1957 -0.0521 -0.3478 366 ALA B N   
1836 C CA  . ALA B 66  ? 0.9850 1.0405 1.6117 -0.2383 -0.0275 -0.3594 366 ALA B CA  
1837 C C   . ALA B 66  ? 1.0088 1.0098 1.6129 -0.2620 0.0208  -0.3245 366 ALA B C   
1838 O O   . ALA B 66  ? 1.0407 1.0535 1.6961 -0.3052 0.0485  -0.3298 366 ALA B O   
1839 C CB  . ALA B 66  ? 0.9451 1.0954 1.6374 -0.2269 -0.0355 -0.3734 366 ALA B CB  
1840 N N   . THR B 67  ? 1.0428 0.9846 1.5700 -0.2360 0.0301  -0.2895 367 THR B N   
1841 C CA  . THR B 67  ? 1.1306 1.0236 1.6276 -0.2514 0.0701  -0.2536 367 THR B CA  
1842 C C   . THR B 67  ? 1.2901 1.0877 1.7236 -0.2490 0.0722  -0.2348 367 THR B C   
1843 O O   . THR B 67  ? 1.3490 1.0941 1.7468 -0.2577 0.0990  -0.2025 367 THR B O   
1844 C CB  . THR B 67  ? 1.0377 0.9560 1.5096 -0.2221 0.0805  -0.2295 367 THR B CB  
1845 O OG1 . THR B 67  ? 0.9857 0.8838 1.4047 -0.1810 0.0533  -0.2235 367 THR B OG1 
1846 C CG2 . THR B 67  ? 0.9745 0.9831 1.5133 -0.2225 0.0824  -0.2487 367 THR B CG2 
1847 N N   . LYS B 68  ? 1.3723 1.1470 1.7908 -0.2361 0.0432  -0.2562 368 LYS B N   
1848 C CA  . LYS B 68  ? 1.4342 1.1243 1.7984 -0.2266 0.0424  -0.2448 368 LYS B CA  
1849 C C   . LYS B 68  ? 1.4413 1.0679 1.8186 -0.2682 0.0626  -0.2422 368 LYS B C   
1850 O O   . LYS B 68  ? 1.3494 1.0020 1.7835 -0.3077 0.0694  -0.2623 368 LYS B O   
1851 C CB  . LYS B 68  ? 1.4436 1.1377 1.7918 -0.2026 0.0081  -0.2753 368 LYS B CB  
1852 C CG  . LYS B 68  ? 1.5125 1.1355 1.8035 -0.1792 0.0046  -0.2691 368 LYS B CG  
1853 C CD  . LYS B 68  ? 1.5766 1.1943 1.8574 -0.1696 -0.0231 -0.3083 368 LYS B CD  
1854 C CE  . LYS B 68  ? 1.5854 1.2616 1.8476 -0.1402 -0.0461 -0.3183 368 LYS B CE  
1855 N NZ  . LYS B 68  ? 1.6580 1.3358 1.9071 -0.1351 -0.0741 -0.3586 368 LYS B NZ  
1856 N N   . ALA B 69  ? 1.4540 0.9962 1.7797 -0.2585 0.0710  -0.2175 369 ALA B N   
1857 C CA  . ALA B 69  ? 1.4562 0.9143 1.7787 -0.2904 0.0853  -0.2115 369 ALA B CA  
1858 C C   . ALA B 69  ? 1.4510 0.9109 1.7950 -0.3338 0.1200  -0.1889 369 ALA B C   
1859 O O   . ALA B 69  ? 1.5123 0.9574 1.8977 -0.3793 0.1298  -0.2061 369 ALA B O   
1860 C CB  . ALA B 69  ? 1.4554 0.8972 1.8089 -0.3088 0.0658  -0.2553 369 ALA B CB  
1861 N N   . ARG B 74  ? 1.6284 0.7111 1.7835 -0.2132 0.0705  -0.1568 374 ARG B N   
1862 C CA  . ARG B 74  ? 1.6670 0.7341 1.7879 -0.1579 0.0558  -0.1502 374 ARG B CA  
1863 C C   . ARG B 74  ? 1.6663 0.7383 1.7531 -0.1396 0.0641  -0.1026 374 ARG B C   
1864 O O   . ARG B 74  ? 1.6693 0.7834 1.7434 -0.1003 0.0546  -0.0999 374 ARG B O   
1865 C CB  . ARG B 74  ? 1.8274 0.7927 1.9340 -0.1419 0.0457  -0.1601 374 ARG B CB  
1866 C CG  . ARG B 74  ? 1.8842 0.8501 1.9721 -0.0840 0.0304  -0.1675 374 ARG B CG  
1867 C CD  . ARG B 74  ? 1.9265 0.9284 2.0298 -0.0659 0.0176  -0.2206 374 ARG B CD  
1868 N NE  . ARG B 74  ? 2.0233 0.9646 2.1422 -0.0905 0.0126  -0.2568 374 ARG B NE  
1869 C CZ  . ARG B 74  ? 2.1351 0.9680 2.2474 -0.0955 0.0122  -0.2526 374 ARG B CZ  
1870 N NH1 . ARG B 74  ? 2.1864 0.9577 2.2733 -0.0652 0.0113  -0.2179 374 ARG B NH1 
1871 N NH2 . ARG B 74  ? 2.2260 1.0097 2.3570 -0.1300 0.0099  -0.2845 374 ARG B NH2 
1872 N N   . SER B 75  ? 1.6708 0.7007 1.7403 -0.1697 0.0825  -0.0662 375 SER B N   
1873 C CA  . SER B 75  ? 1.6454 0.6683 1.6723 -0.1537 0.0883  -0.0211 375 SER B CA  
1874 C C   . SER B 75  ? 1.6159 0.7390 1.6526 -0.1594 0.0991  -0.0168 375 SER B C   
1875 O O   . SER B 75  ? 1.6797 0.8083 1.7020 -0.1862 0.1201  0.0093  375 SER B O   
1876 C CB  . SER B 75  ? 1.7316 0.6584 1.7223 -0.1816 0.1032  0.0171  375 SER B CB  
1877 O OG  . SER B 75  ? 1.7484 0.6585 1.7675 -0.2368 0.1233  0.0055  375 SER B OG  
1878 N N   . GLN B 76  ? 1.5045 0.7026 1.5615 -0.1325 0.0855  -0.0425 376 GLN B N   
1879 C CA  . GLN B 76  ? 1.3668 0.6563 1.4378 -0.1334 0.0912  -0.0452 376 GLN B CA  
1880 C C   . GLN B 76  ? 1.3041 0.6384 1.3742 -0.0920 0.0724  -0.0615 376 GLN B C   
1881 O O   . GLN B 76  ? 1.3229 0.6766 1.4134 -0.0853 0.0609  -0.0945 376 GLN B O   
1882 C CB  . GLN B 76  ? 1.3761 0.7100 1.4940 -0.1712 0.1004  -0.0712 376 GLN B CB  
1883 C CG  . GLN B 76  ? 1.3862 0.8162 1.5306 -0.1625 0.0953  -0.0896 376 GLN B CG  
1884 C CD  . GLN B 76  ? 1.4999 0.9772 1.6984 -0.1928 0.0956  -0.1216 376 GLN B CD  
1885 O OE1 . GLN B 76  ? 1.6205 1.0687 1.8405 -0.2115 0.0891  -0.1451 376 GLN B OE1 
1886 N NE2 . GLN B 76  ? 1.4307 0.9825 1.6554 -0.1975 0.1013  -0.1257 376 GLN B NE2 
1887 N N   . LEU B 77  ? 1.2720 0.6196 1.3154 -0.0661 0.0699  -0.0385 377 LEU B N   
1888 C CA  . LEU B 77  ? 1.2194 0.6052 1.2613 -0.0300 0.0563  -0.0501 377 LEU B CA  
1889 C C   . LEU B 77  ? 1.1192 0.5832 1.1725 -0.0311 0.0585  -0.0583 377 LEU B C   
1890 O O   . LEU B 77  ? 1.1001 0.5991 1.1589 -0.0132 0.0497  -0.0778 377 LEU B O   
1891 C CB  . LEU B 77  ? 1.2686 0.6288 1.2826 -0.0024 0.0495  -0.0241 377 LEU B CB  
1892 C CG  . LEU B 77  ? 1.3253 0.6551 1.3415 0.0314  0.0350  -0.0363 377 LEU B CG  
1893 C CD1 . LEU B 77  ? 1.3320 0.6322 1.3261 0.0578  0.0243  -0.0088 377 LEU B CD1 
1894 C CD2 . LEU B 77  ? 1.2921 0.6840 1.3256 0.0498  0.0317  -0.0646 377 LEU B CD2 
1895 N N   . VAL B 78  ? 1.0972 0.5840 1.1504 -0.0511 0.0714  -0.0426 378 VAL B N   
1896 C CA  . VAL B 78  ? 0.9487 0.5007 1.0105 -0.0487 0.0732  -0.0467 378 VAL B CA  
1897 C C   . VAL B 78  ? 0.9146 0.4965 1.0073 -0.0781 0.0841  -0.0575 378 VAL B C   
1898 O O   . VAL B 78  ? 0.9636 0.5330 1.0544 -0.1009 0.1020  -0.0423 378 VAL B O   
1899 C CB  . VAL B 78  ? 0.9526 0.5098 0.9861 -0.0385 0.0780  -0.0206 378 VAL B CB  
1900 C CG1 . VAL B 78  ? 1.0254 0.6413 1.0677 -0.0372 0.0812  -0.0257 378 VAL B CG1 
1901 C CG2 . VAL B 78  ? 0.9388 0.4773 0.9518 -0.0092 0.0651  -0.0120 378 VAL B CG2 
1902 N N   . LEU B 79  ? 0.8747 0.4985 0.9951 -0.0767 0.0732  -0.0841 379 LEU B N   
1903 C CA  . LEU B 79  ? 0.8871 0.5561 1.0479 -0.0980 0.0779  -0.0998 379 LEU B CA  
1904 C C   . LEU B 79  ? 0.8875 0.6070 1.0494 -0.0852 0.0801  -0.0945 379 LEU B C   
1905 O O   . LEU B 79  ? 0.8912 0.6207 1.0315 -0.0596 0.0682  -0.0920 379 LEU B O   
1906 C CB  . LEU B 79  ? 0.8839 0.5686 1.0693 -0.0982 0.0579  -0.1322 379 LEU B CB  
1907 C CG  . LEU B 79  ? 0.8887 0.6145 1.1283 -0.1247 0.0571  -0.1561 379 LEU B CG  
1908 C CD1 . LEU B 79  ? 0.8943 0.6166 1.1494 -0.1287 0.0351  -0.1882 379 LEU B CD1 
1909 C CD2 . LEU B 79  ? 0.8603 0.6530 1.1229 -0.1140 0.0525  -0.1613 379 LEU B CD2 
1910 N N   . VAL B 80  ? 0.8818 0.6314 1.0698 -0.1041 0.0974  -0.0940 380 VAL B N   
1911 C CA  . VAL B 80  ? 0.8494 0.6410 1.0396 -0.0913 0.1016  -0.0913 380 VAL B CA  
1912 C C   . VAL B 80  ? 0.8086 0.6607 1.0528 -0.0928 0.0935  -0.1179 380 VAL B C   
1913 O O   . VAL B 80  ? 0.7738 0.6477 1.0624 -0.1182 0.1031  -0.1324 380 VAL B O   
1914 C CB  . VAL B 80  ? 0.9413 0.7206 1.1123 -0.1064 0.1295  -0.0706 380 VAL B CB  
1915 C CG1 . VAL B 80  ? 1.0102 0.8369 1.1932 -0.0980 0.1386  -0.0756 380 VAL B CG1 
1916 C CG2 . VAL B 80  ? 1.0328 0.7583 1.1471 -0.0953 0.1281  -0.0441 380 VAL B CG2 
1917 N N   . THR B 81  ? 0.8269 0.7054 1.0684 -0.0656 0.0750  -0.1240 381 THR B N   
1918 C CA  . THR B 81  ? 0.8654 0.8012 1.1562 -0.0591 0.0632  -0.1468 381 THR B CA  
1919 C C   . THR B 81  ? 0.8681 0.8219 1.1501 -0.0367 0.0655  -0.1405 381 THR B C   
1920 O O   . THR B 81  ? 0.9180 0.8406 1.1552 -0.0293 0.0751  -0.1202 381 THR B O   
1921 C CB  . THR B 81  ? 0.8761 0.8204 1.1724 -0.0461 0.0296  -0.1649 381 THR B CB  
1922 O OG1 . THR B 81  ? 0.8322 0.7463 1.0737 -0.0209 0.0153  -0.1514 381 THR B OG1 
1923 C CG2 . THR B 81  ? 0.9309 0.8554 1.2378 -0.0693 0.0273  -0.1767 381 THR B CG2 
1924 N N   . LYS B 82  ? 0.8090 0.8144 1.1389 -0.0261 0.0558  -0.1607 382 LYS B N   
1925 C CA  . LYS B 82  ? 0.7338 0.7515 1.0584 0.0006  0.0516  -0.1592 382 LYS B CA  
1926 C C   . LYS B 82  ? 0.7132 0.6986 0.9915 0.0262  0.0225  -0.1493 382 LYS B C   
1927 O O   . LYS B 82  ? 0.6999 0.6635 0.9561 0.0218  0.0095  -0.1472 382 LYS B O   
1928 C CB  . LYS B 82  ? 0.6948 0.7777 1.0905 0.0075  0.0485  -0.1860 382 LYS B CB  
1929 C CG  . LYS B 82  ? 0.7083 0.8215 1.1389 -0.0170 0.0878  -0.1927 382 LYS B CG  
1930 C CD  . LYS B 82  ? 0.7700 0.9552 1.2762 -0.0063 0.0904  -0.2219 382 LYS B CD  
1931 C CE  . LYS B 82  ? 0.7925 1.0043 1.3200 -0.0297 0.1373  -0.2270 382 LYS B CE  
1932 N NZ  . LYS B 82  ? 0.7420 1.0260 1.3421 -0.0155 0.1463  -0.2575 382 LYS B NZ  
1933 N N   . GLY B 83  ? 0.6403 0.6207 0.9034 0.0508  0.0152  -0.1444 383 GLY B N   
1934 C CA  . GLY B 83  ? 0.6227 0.5657 0.8350 0.0714  -0.0058 -0.1305 383 GLY B CA  
1935 C C   . GLY B 83  ? 0.6357 0.5930 0.8576 0.0951  -0.0413 -0.1413 383 GLY B C   
1936 O O   . GLY B 83  ? 0.6712 0.5945 0.8434 0.1073  -0.0592 -0.1289 383 GLY B O   
1937 N N   . PHE B 84  ? 0.6337 0.6420 0.9177 0.1027  -0.0517 -0.1641 384 PHE B N   
1938 C CA  . PHE B 84  ? 0.7008 0.7247 0.9954 0.1306  -0.0913 -0.1745 384 PHE B CA  
1939 C C   . PHE B 84  ? 0.7108 0.6866 0.9523 0.1579  -0.1038 -0.1545 384 PHE B C   
1940 O O   . PHE B 84  ? 0.6878 0.6518 0.9305 0.1626  -0.0851 -0.1493 384 PHE B O   
1941 C CB  . PHE B 84  ? 0.7508 0.7754 1.0312 0.1209  -0.1125 -0.1811 384 PHE B CB  
1942 C CG  . PHE B 84  ? 0.7516 0.8165 1.0894 0.0895  -0.0952 -0.2011 384 PHE B CG  
1943 C CD1 . PHE B 84  ? 0.7170 0.7536 1.0337 0.0604  -0.0647 -0.1901 384 PHE B CD1 
1944 C CD2 . PHE B 84  ? 0.7083 0.8390 1.1249 0.0888  -0.1080 -0.2304 384 PHE B CD2 
1945 C CE1 . PHE B 84  ? 0.6945 0.7564 1.0583 0.0296  -0.0469 -0.2047 384 PHE B CE1 
1946 C CE2 . PHE B 84  ? 0.6985 0.8629 1.1687 0.0543  -0.0874 -0.2476 384 PHE B CE2 
1947 C CZ  . PHE B 84  ? 0.7039 0.8285 1.1434 0.0238  -0.0564 -0.2331 384 PHE B CZ  
1948 N N   . ASN B 85  ? 0.7748 0.7180 0.9639 0.1726  -0.1332 -0.1431 385 ASN B N   
1949 C CA  . ASN B 85  ? 0.8607 0.7514 0.9952 0.1967  -0.1475 -0.1221 385 ASN B CA  
1950 C C   . ASN B 85  ? 0.8662 0.7026 0.9385 0.1792  -0.1208 -0.0966 385 ASN B C   
1951 O O   . ASN B 85  ? 0.8873 0.6724 0.9021 0.1900  -0.1296 -0.0759 385 ASN B O   
1952 C CB  . ASN B 85  ? 0.9405 0.8122 1.0312 0.2175  -0.1886 -0.1164 385 ASN B CB  
1953 C CG  . ASN B 85  ? 1.0034 0.9305 1.1519 0.2379  -0.2250 -0.1424 385 ASN B CG  
1954 O OD1 . ASN B 85  ? 1.0475 1.0320 1.2781 0.2378  -0.2177 -0.1663 385 ASN B OD1 
1955 N ND2 . ASN B 85  ? 1.0782 0.9927 1.1852 0.2550  -0.2647 -0.1397 385 ASN B ND2 
1956 N N   . LEU B 86  ? 0.8077 0.6539 0.8898 0.1516  -0.0898 -0.0974 386 LEU B N   
1957 C CA  . LEU B 86  ? 0.8220 0.6289 0.8623 0.1377  -0.0656 -0.0779 386 LEU B CA  
1958 C C   . LEU B 86  ? 0.8140 0.6207 0.8770 0.1401  -0.0488 -0.0799 386 LEU B C   
1959 O O   . LEU B 86  ? 0.7129 0.5589 0.8280 0.1413  -0.0420 -0.0978 386 LEU B O   
1960 C CB  . LEU B 86  ? 0.8711 0.6832 0.9066 0.1122  -0.0445 -0.0767 386 LEU B CB  
1961 C CG  . LEU B 86  ? 0.9283 0.7373 0.9382 0.1077  -0.0555 -0.0787 386 LEU B CG  
1962 C CD1 . LEU B 86  ? 0.8716 0.6707 0.8686 0.0881  -0.0323 -0.0733 386 LEU B CD1 
1963 C CD2 . LEU B 86  ? 1.0158 0.7928 0.9699 0.1229  -0.0755 -0.0666 386 LEU B CD2 
1964 N N   . PHE B 87  ? 0.8455 0.6093 0.8687 0.1374  -0.0392 -0.0635 387 PHE B N   
1965 C CA  . PHE B 87  ? 0.7591 0.5152 0.7942 0.1386  -0.0245 -0.0673 387 PHE B CA  
1966 C C   . PHE B 87  ? 0.6975 0.4734 0.7427 0.1146  0.0018  -0.0698 387 PHE B C   
1967 O O   . PHE B 87  ? 0.7243 0.4768 0.7422 0.1021  0.0140  -0.0594 387 PHE B O   
1968 C CB  . PHE B 87  ? 0.8079 0.5067 0.7973 0.1433  -0.0283 -0.0506 387 PHE B CB  
1969 C CG  . PHE B 87  ? 0.8154 0.4852 0.7919 0.1715  -0.0564 -0.0464 387 PHE B CG  
1970 C CD1 . PHE B 87  ? 0.8144 0.4992 0.8319 0.1977  -0.0687 -0.0638 387 PHE B CD1 
1971 C CD2 . PHE B 87  ? 0.8493 0.4768 0.7713 0.1731  -0.0704 -0.0252 387 PHE B CD2 
1972 C CE1 . PHE B 87  ? 0.8723 0.5287 0.8795 0.2286  -0.0994 -0.0595 387 PHE B CE1 
1973 C CE2 . PHE B 87  ? 0.9549 0.5488 0.8565 0.2009  -0.0996 -0.0178 387 PHE B CE2 
1974 C CZ  . PHE B 87  ? 0.9500 0.5567 0.8952 0.2306  -0.1166 -0.0345 387 PHE B CZ  
1975 N N   . CYS B 88  ? 0.6620 0.4797 0.7453 0.1075  0.0083  -0.0827 388 CYS B N   
1976 C CA  . CYS B 88  ? 0.6695 0.4996 0.7565 0.0852  0.0312  -0.0817 388 CYS B CA  
1977 C C   . CYS B 88  ? 0.6855 0.5594 0.8210 0.0800  0.0422  -0.0994 388 CYS B C   
1978 O O   . CYS B 88  ? 0.7225 0.6253 0.8959 0.0921  0.0291  -0.1141 388 CYS B O   
1979 C CB  . CYS B 88  ? 0.7400 0.5580 0.8038 0.0717  0.0307  -0.0698 388 CYS B CB  
1980 S SG  . CYS B 88  ? 0.7800 0.6196 0.8656 0.0700  0.0163  -0.0797 388 CYS B SG  
1981 N N   . LYS B 89  ? 0.7585 0.6382 0.8920 0.0614  0.0664  -0.0979 389 LYS B N   
1982 C CA  . LYS B 89  ? 0.7858 0.7048 0.9599 0.0496  0.0853  -0.1125 389 LYS B CA  
1983 C C   . LYS B 89  ? 0.7922 0.7212 0.9827 0.0311  0.0851  -0.1113 389 LYS B C   
1984 O O   . LYS B 89  ? 0.8278 0.7956 1.0666 0.0234  0.0896  -0.1276 389 LYS B O   
1985 C CB  . LYS B 89  ? 0.7995 0.7132 0.9517 0.0370  0.1126  -0.1098 389 LYS B CB  
1986 C CG  . LYS B 89  ? 0.8204 0.7363 0.9731 0.0545  0.1165  -0.1231 389 LYS B CG  
1987 C CD  . LYS B 89  ? 0.8546 0.7657 0.9783 0.0429  0.1427  -0.1245 389 LYS B CD  
1988 C CE  . LYS B 89  ? 0.8377 0.7475 0.9626 0.0620  0.1453  -0.1430 389 LYS B CE  
1989 N NZ  . LYS B 89  ? 0.8558 0.7667 0.9506 0.0495  0.1726  -0.1493 389 LYS B NZ  
1990 N N   . TYR B 90  ? 0.8192 0.7139 0.9732 0.0240  0.0797  -0.0944 390 TYR B N   
1991 C CA  . TYR B 90  ? 0.8278 0.7193 0.9904 0.0064  0.0809  -0.0932 390 TYR B CA  
1992 C C   . TYR B 90  ? 0.7679 0.6297 0.8994 0.0147  0.0623  -0.0841 390 TYR B C   
1993 O O   . TYR B 90  ? 0.8139 0.6552 0.9125 0.0263  0.0574  -0.0732 390 TYR B O   
1994 C CB  . TYR B 90  ? 0.8296 0.7042 0.9756 -0.0162 0.1055  -0.0807 390 TYR B CB  
1995 C CG  . TYR B 90  ? 0.8388 0.7399 1.0055 -0.0312 0.1326  -0.0878 390 TYR B CG  
1996 C CD1 . TYR B 90  ? 0.8492 0.7952 1.0731 -0.0410 0.1402  -0.1085 390 TYR B CD1 
1997 C CD2 . TYR B 90  ? 0.8914 0.7758 1.0197 -0.0366 0.1515  -0.0756 390 TYR B CD2 
1998 C CE1 . TYR B 90  ? 0.9285 0.9047 1.1738 -0.0566 0.1706  -0.1170 390 TYR B CE1 
1999 C CE2 . TYR B 90  ? 0.9410 0.8495 1.0797 -0.0510 0.1804  -0.0830 390 TYR B CE2 
2000 C CZ  . TYR B 90  ? 0.9902 0.9456 1.1887 -0.0620 0.1929  -0.1037 390 TYR B CZ  
2001 O OH  . TYR B 90  ? 0.9446 0.9273 1.1529 -0.0785 0.2275  -0.1121 390 TYR B OH  
2002 N N   . ILE B 91  ? 0.7119 0.5734 0.8558 0.0071  0.0538  -0.0914 391 ILE B N   
2003 C CA  . ILE B 91  ? 0.7490 0.5811 0.8626 0.0109  0.0440  -0.0852 391 ILE B CA  
2004 C C   . ILE B 91  ? 0.7609 0.5688 0.8727 -0.0065 0.0557  -0.0801 391 ILE B C   
2005 O O   . ILE B 91  ? 0.7607 0.5757 0.9016 -0.0240 0.0610  -0.0898 391 ILE B O   
2006 C CB  . ILE B 91  ? 0.7399 0.5826 0.8583 0.0203  0.0212  -0.1003 391 ILE B CB  
2007 C CG1 . ILE B 91  ? 0.7023 0.5572 0.8138 0.0403  0.0062  -0.1008 391 ILE B CG1 
2008 C CG2 . ILE B 91  ? 0.7978 0.6121 0.8838 0.0228  0.0165  -0.0981 391 ILE B CG2 
2009 C CD1 . ILE B 91  ? 0.7038 0.5782 0.8276 0.0498  -0.0201 -0.1178 391 ILE B CD1 
2010 N N   . TYR B 92  ? 0.7074 0.4856 0.7873 -0.0016 0.0589  -0.0651 392 TYR B N   
2011 C CA  . TYR B 92  ? 0.7384 0.4841 0.8116 -0.0106 0.0642  -0.0592 392 TYR B CA  
2012 C C   . TYR B 92  ? 0.7566 0.4889 0.8237 -0.0011 0.0514  -0.0705 392 TYR B C   
2013 O O   . TYR B 92  ? 0.7372 0.4658 0.7835 0.0142  0.0473  -0.0668 392 TYR B O   
2014 C CB  . TYR B 92  ? 0.6889 0.4148 0.7344 -0.0064 0.0715  -0.0383 392 TYR B CB  
2015 C CG  . TYR B 92  ? 0.6229 0.3508 0.6609 -0.0180 0.0866  -0.0265 392 TYR B CG  
2016 C CD1 . TYR B 92  ? 0.5941 0.3486 0.6553 -0.0312 0.0985  -0.0352 392 TYR B CD1 
2017 C CD2 . TYR B 92  ? 0.6135 0.3190 0.6196 -0.0144 0.0886  -0.0081 392 TYR B CD2 
2018 C CE1 . TYR B 92  ? 0.5869 0.3446 0.6353 -0.0413 0.1165  -0.0265 392 TYR B CE1 
2019 C CE2 . TYR B 92  ? 0.6224 0.3273 0.6095 -0.0243 0.1021  0.0023  392 TYR B CE2 
2020 C CZ  . TYR B 92  ? 0.6201 0.3504 0.6260 -0.0382 0.1183  -0.0072 392 TYR B CZ  
2021 O OH  . TYR B 92  ? 0.6782 0.4059 0.6569 -0.0474 0.1346  0.0023  392 TYR B OH  
2022 N N   . HIS B 93  ? 0.7610 0.4884 0.8474 -0.0119 0.0467  -0.0871 393 HIS B N   
2023 C CA  . HIS B 93  ? 0.7803 0.4938 0.8578 -0.0035 0.0353  -0.1031 393 HIS B CA  
2024 C C   . HIS B 93  ? 0.7990 0.4680 0.8680 -0.0029 0.0408  -0.0978 393 HIS B C   
2025 O O   . HIS B 93  ? 0.8272 0.4689 0.9089 -0.0199 0.0466  -0.0959 393 HIS B O   
2026 C CB  . HIS B 93  ? 0.7669 0.4942 0.8681 -0.0148 0.0233  -0.1284 393 HIS B CB  
2027 C CG  . HIS B 93  ? 0.7357 0.5069 0.8559 -0.0148 0.0149  -0.1344 393 HIS B CG  
2028 N ND1 . HIS B 93  ? 0.7313 0.5225 0.8356 0.0013  -0.0035 -0.1439 393 HIS B ND1 
2029 C CD2 . HIS B 93  ? 0.7203 0.5186 0.8738 -0.0270 0.0221  -0.1328 393 HIS B CD2 
2030 C CE1 . HIS B 93  ? 0.7602 0.5872 0.8907 0.0018  -0.0113 -0.1478 393 HIS B CE1 
2031 N NE2 . HIS B 93  ? 0.7380 0.5740 0.9027 -0.0151 0.0056  -0.1433 393 HIS B NE2 
2032 N N   . VAL B 94  ? 0.7984 0.4592 0.8477 0.0167  0.0395  -0.0954 394 VAL B N   
2033 C CA  . VAL B 94  ? 0.8648 0.4851 0.9108 0.0247  0.0405  -0.0949 394 VAL B CA  
2034 C C   . VAL B 94  ? 0.8444 0.4463 0.8959 0.0231  0.0339  -0.1228 394 VAL B C   
2035 O O   . VAL B 94  ? 0.8244 0.4478 0.8659 0.0316  0.0286  -0.1416 394 VAL B O   
2036 C CB  . VAL B 94  ? 0.9128 0.5416 0.9468 0.0477  0.0416  -0.0875 394 VAL B CB  
2037 C CG1 . VAL B 94  ? 0.9192 0.5125 0.9565 0.0636  0.0392  -0.0951 394 VAL B CG1 
2038 C CG2 . VAL B 94  ? 0.9169 0.5566 0.9451 0.0477  0.0450  -0.0620 394 VAL B CG2 
2039 N N   . LEU B 95  ? 0.8588 0.4169 0.9216 0.0101  0.0344  -0.1258 395 LEU B N   
2040 C CA  . LEU B 95  ? 0.9055 0.4390 0.9747 0.0062  0.0273  -0.1557 395 LEU B CA  
2041 C C   . LEU B 95  ? 0.9818 0.4730 1.0424 0.0289  0.0271  -0.1613 395 LEU B C   
2042 O O   . LEU B 95  ? 1.0225 0.4647 1.0847 0.0291  0.0293  -0.1450 395 LEU B O   
2043 C CB  . LEU B 95  ? 0.9251 0.4322 1.0167 -0.0254 0.0289  -0.1584 395 LEU B CB  
2044 C CG  . LEU B 95  ? 0.8749 0.4257 0.9855 -0.0474 0.0339  -0.1487 395 LEU B CG  
2045 C CD1 . LEU B 95  ? 0.9172 0.4469 1.0572 -0.0827 0.0396  -0.1554 395 LEU B CD1 
2046 C CD2 . LEU B 95  ? 0.8020 0.4111 0.9143 -0.0391 0.0217  -0.1660 395 LEU B CD2 
2047 N N   . TRP B 96  ? 1.0020 0.5113 1.0515 0.0492  0.0250  -0.1843 396 TRP B N   
2048 C CA  . TRP B 96  ? 1.0736 0.5481 1.1224 0.0726  0.0256  -0.2003 396 TRP B CA  
2049 C C   . TRP B 96  ? 1.1630 0.5881 1.2175 0.0622  0.0191  -0.2299 396 TRP B C   
2050 O O   . TRP B 96  ? 1.1682 0.6091 1.2132 0.0595  0.0146  -0.2619 396 TRP B O   
2051 C CB  . TRP B 96  ? 1.0389 0.5559 1.0738 0.0949  0.0314  -0.2176 396 TRP B CB  
2052 C CG  . TRP B 96  ? 1.0180 0.5828 1.0491 0.1008  0.0383  -0.1927 396 TRP B CG  
2053 C CD1 . TRP B 96  ? 0.9554 0.5610 0.9730 0.0882  0.0390  -0.1819 396 TRP B CD1 
2054 C CD2 . TRP B 96  ? 1.0245 0.6006 1.0675 0.1222  0.0436  -0.1789 396 TRP B CD2 
2055 N NE1 . TRP B 96  ? 0.9057 0.5411 0.9244 0.0967  0.0463  -0.1616 396 TRP B NE1 
2056 C CE2 . TRP B 96  ? 0.9034 0.5267 0.9392 0.1165  0.0489  -0.1606 396 TRP B CE2 
2057 C CE3 . TRP B 96  ? 1.0461 0.5975 1.1079 0.1468  0.0420  -0.1819 396 TRP B CE3 
2058 C CZ2 . TRP B 96  ? 0.8702 0.5198 0.9190 0.1302  0.0532  -0.1471 396 TRP B CZ2 
2059 C CZ3 . TRP B 96  ? 1.0019 0.5854 1.0790 0.1643  0.0442  -0.1684 396 TRP B CZ3 
2060 C CH2 . TRP B 96  ? 0.9033 0.5369 0.9747 0.1539  0.0501  -0.1520 396 TRP B CH2 
2061 N N   . HIS B 97  ? 1.2355 0.5962 1.3007 0.0563  0.0177  -0.2194 397 HIS B N   
2062 C CA  . HIS B 97  ? 1.3572 0.6573 1.4284 0.0498  0.0121  -0.2489 397 HIS B CA  
2063 C C   . HIS B 97  ? 1.4939 0.7705 1.5618 0.0886  0.0121  -0.2695 397 HIS B C   
2064 O O   . HIS B 97  ? 1.5329 0.8086 1.6037 0.1148  0.0142  -0.2483 397 HIS B O   
2065 C CB  . HIS B 97  ? 1.3461 0.5778 1.4269 0.0240  0.0127  -0.2279 397 HIS B CB  
2066 C CG  . HIS B 97  ? 1.3123 0.5750 1.4008 -0.0109 0.0188  -0.2037 397 HIS B CG  
2067 N ND1 . HIS B 97  ? 1.3061 0.5898 1.4137 -0.0452 0.0168  -0.2238 397 HIS B ND1 
2068 C CD2 . HIS B 97  ? 1.2833 0.5648 1.3656 -0.0158 0.0270  -0.1645 397 HIS B CD2 
2069 C CE1 . HIS B 97  ? 1.2512 0.5675 1.3688 -0.0686 0.0258  -0.1981 397 HIS B CE1 
2070 N NE2 . HIS B 97  ? 1.2338 0.5456 1.3324 -0.0519 0.0332  -0.1620 397 HIS B NE2 
2071 N N   . SER B 98  ? 1.6585 0.9195 1.7225 0.0932  0.0091  -0.3139 398 SER B N   
2072 C CA  . SER B 98  ? 1.7991 1.0549 1.8610 0.1318  0.0134  -0.3418 398 SER B CA  
2073 C C   . SER B 98  ? 1.8854 1.0502 1.9608 0.1467  0.0073  -0.3518 398 SER B C   
2074 O O   . SER B 98  ? 2.1070 1.2453 2.1817 0.1654  0.0075  -0.3943 398 SER B O   
2075 C CB  . SER B 98  ? 1.8159 1.1104 1.8563 0.1332  0.0162  -0.3863 398 SER B CB  
2076 O OG  . SER B 98  ? 1.8174 1.0790 1.8531 0.1054  0.0047  -0.4147 398 SER B OG  
2077 N N   . GLU B 99  ? 1.9222 1.0346 2.0052 0.1403  0.0022  -0.3125 399 GLU B N   
2078 C CA  . GLU B 99  ? 2.0067 1.0200 2.0964 0.1552  -0.0059 -0.3134 399 GLU B CA  
2079 C C   . GLU B 99  ? 1.9666 0.9610 2.0588 0.1825  -0.0114 -0.2694 399 GLU B C   
2080 O O   . GLU B 99  ? 1.9690 0.8726 2.0578 0.1887  -0.0210 -0.2521 399 GLU B O   
2081 C CB  . GLU B 99  ? 2.0996 1.0451 2.1866 0.1094  -0.0091 -0.3119 399 GLU B CB  
2082 C CG  . GLU B 99  ? 2.2665 1.1145 2.3578 0.1154  -0.0161 -0.3467 399 GLU B CG  
2083 C CD  . GLU B 99  ? 2.3472 1.1118 2.4397 0.0678  -0.0182 -0.3415 399 GLU B CD  
2084 O OE1 . GLU B 99  ? 2.2431 0.9079 2.3372 0.0717  -0.0245 -0.3602 399 GLU B OE1 
2085 O OE2 . GLU B 99  ? 2.5465 1.3467 2.6412 0.0247  -0.0121 -0.3196 399 GLU B OE2 
2086 N N   . PHE B 100 ? 1.8285 0.9043 1.9240 0.1986  -0.0075 -0.2514 400 PHE B N   
2087 C CA  . PHE B 100 ? 1.7484 0.8201 1.8438 0.2187  -0.0161 -0.2086 400 PHE B CA  
2088 C C   . PHE B 100 ? 1.6178 0.7695 1.7352 0.2571  -0.0142 -0.2187 400 PHE B C   
2089 O O   . PHE B 100 ? 1.5367 0.7589 1.6590 0.2540  -0.0003 -0.2460 400 PHE B O   
2090 C CB  . PHE B 100 ? 1.7319 0.8257 1.8074 0.1809  -0.0121 -0.1669 400 PHE B CB  
2091 C CG  . PHE B 100 ? 1.8196 0.8444 1.8793 0.1380  -0.0095 -0.1538 400 PHE B CG  
2092 C CD1 . PHE B 100 ? 1.8929 0.8211 1.9351 0.1370  -0.0175 -0.1240 400 PHE B CD1 
2093 C CD2 . PHE B 100 ? 1.8227 0.8800 1.8857 0.0979  0.0008  -0.1713 400 PHE B CD2 
2094 C CE1 . PHE B 100 ? 1.9675 0.8336 1.9968 0.0919  -0.0100 -0.1121 400 PHE B CE1 
2095 C CE2 . PHE B 100 ? 1.8905 0.8947 1.9494 0.0553  0.0053  -0.1628 400 PHE B CE2 
2096 C CZ  . PHE B 100 ? 1.9348 0.8435 1.9772 0.0498  0.0026  -0.1332 400 PHE B CZ  
2097 N N   . PRO B 101 ? 1.6063 0.7517 1.7368 0.2924  -0.0282 -0.1968 401 PRO B N   
2098 C CA  . PRO B 101 ? 1.5340 0.7619 1.6968 0.3270  -0.0262 -0.2098 401 PRO B CA  
2099 C C   . PRO B 101 ? 1.4364 0.7501 1.5908 0.3002  -0.0148 -0.1921 401 PRO B C   
2100 O O   . PRO B 101 ? 1.4249 0.7263 1.5543 0.2742  -0.0197 -0.1552 401 PRO B O   
2101 C CB  . PRO B 101 ? 1.5833 0.7763 1.7618 0.3678  -0.0512 -0.1868 401 PRO B CB  
2102 C CG  . PRO B 101 ? 1.6472 0.7243 1.7904 0.3544  -0.0655 -0.1578 401 PRO B CG  
2103 C CD  . PRO B 101 ? 1.6432 0.7052 1.7565 0.2990  -0.0478 -0.1568 401 PRO B CD  
2104 N N   . LYS B 102 ? 1.3580 0.7536 1.5305 0.3058  0.0022  -0.2192 402 LYS B N   
2105 C CA  . LYS B 102 ? 1.2418 0.7073 1.4001 0.2761  0.0163  -0.2092 402 LYS B CA  
2106 C C   . LYS B 102 ? 1.2004 0.6995 1.3654 0.2775  0.0061  -0.1736 402 LYS B C   
2107 O O   . LYS B 102 ? 1.0844 0.5810 1.2231 0.2486  0.0041  -0.1442 402 LYS B O   
2108 C CB  . LYS B 102 ? 1.2315 0.7625 1.3996 0.2815  0.0387  -0.2464 402 LYS B CB  
2109 C CG  . LYS B 102 ? 1.3265 0.8281 1.4754 0.2750  0.0480  -0.2829 402 LYS B CG  
2110 C CD  . LYS B 102 ? 1.4101 0.8962 1.5211 0.2341  0.0469  -0.2720 402 LYS B CD  
2111 C CE  . LYS B 102 ? 1.5448 0.9717 1.6405 0.2241  0.0424  -0.2989 402 LYS B CE  
2112 N NZ  . LYS B 102 ? 1.5309 0.9502 1.6035 0.1848  0.0369  -0.2835 402 LYS B NZ  
2113 N N   . PRO B 103 ? 1.1763 0.7065 1.3786 0.3125  -0.0030 -0.1770 403 PRO B N   
2114 C CA  . PRO B 103 ? 1.1296 0.6900 1.3375 0.3146  -0.0179 -0.1462 403 PRO B CA  
2115 C C   . PRO B 103 ? 1.1770 0.6707 1.3442 0.2992  -0.0358 -0.1056 403 PRO B C   
2116 O O   . PRO B 103 ? 1.2191 0.7374 1.3712 0.2844  -0.0412 -0.0799 403 PRO B O   
2117 C CB  . PRO B 103 ? 1.1485 0.7347 1.4089 0.3619  -0.0319 -0.1623 403 PRO B CB  
2118 C CG  . PRO B 103 ? 1.1401 0.7494 1.4273 0.3762  -0.0095 -0.2080 403 PRO B CG  
2119 C CD  . PRO B 103 ? 1.1705 0.7086 1.4142 0.3532  -0.0018 -0.2125 403 PRO B CD  
2120 N N   . GLN B 104 ? 1.2765 0.6839 1.4238 0.3007  -0.0429 -0.1010 404 GLN B N   
2121 C CA  . GLN B 104 ? 1.3655 0.7034 1.4700 0.2828  -0.0546 -0.0621 404 GLN B CA  
2122 C C   . GLN B 104 ? 1.3671 0.7088 1.4415 0.2344  -0.0355 -0.0530 404 GLN B C   
2123 O O   . GLN B 104 ? 1.4047 0.7239 1.4461 0.2133  -0.0380 -0.0204 404 GLN B O   
2124 C CB  . GLN B 104 ? 1.4842 0.7193 1.5757 0.2957  -0.0665 -0.0579 404 GLN B CB  
2125 C CG  . GLN B 104 ? 1.6092 0.8073 1.7103 0.3426  -0.0963 -0.0447 404 GLN B CG  
2126 C CD  . GLN B 104 ? 1.8138 0.8925 1.8914 0.3514  -0.1083 -0.0338 404 GLN B CD  
2127 O OE1 . GLN B 104 ? 1.8703 0.8911 1.9188 0.3141  -0.0940 -0.0283 404 GLN B OE1 
2128 N NE2 . GLN B 104 ? 1.8724 0.9115 1.9654 0.4008  -0.1358 -0.0314 404 GLN B NE2 
2129 N N   . ILE B 105 ? 1.3448 0.7113 1.4284 0.2176  -0.0174 -0.0822 405 ILE B N   
2130 C CA  . ILE B 105 ? 1.3400 0.7109 1.4018 0.1758  -0.0042 -0.0750 405 ILE B CA  
2131 C C   . ILE B 105 ? 1.1750 0.6198 1.2349 0.1645  0.0026  -0.0656 405 ILE B C   
2132 O O   . ILE B 105 ? 1.1793 0.6263 1.2197 0.1370  0.0081  -0.0473 405 ILE B O   
2133 C CB  . ILE B 105 ? 1.4716 0.8334 1.5378 0.1595  0.0064  -0.1070 405 ILE B CB  
2134 C CG1 . ILE B 105 ? 1.5225 0.9436 1.6050 0.1745  0.0150  -0.1407 405 ILE B CG1 
2135 C CG2 . ILE B 105 ? 1.6164 0.8908 1.6807 0.1626  -0.0004 -0.1135 405 ILE B CG2 
2136 C CD1 . ILE B 105 ? 1.6738 1.0777 1.7538 0.1652  0.0205  -0.1761 405 ILE B CD1 
2137 N N   . LEU B 106 ? 1.0612 0.5642 1.1432 0.1849  0.0036  -0.0792 406 LEU B N   
2138 C CA  . LEU B 106 ? 0.9814 0.5451 1.0623 0.1751  0.0079  -0.0684 406 LEU B CA  
2139 C C   . LEU B 106 ? 1.0114 0.5578 1.0752 0.1754  -0.0066 -0.0358 406 LEU B C   
2140 O O   . LEU B 106 ? 0.9434 0.5006 0.9854 0.1523  -0.0022 -0.0186 406 LEU B O   
2141 C CB  . LEU B 106 ? 0.9478 0.5721 1.0598 0.1950  0.0133  -0.0897 406 LEU B CB  
2142 C CG  . LEU B 106 ? 0.8748 0.5606 0.9896 0.1825  0.0196  -0.0825 406 LEU B CG  
2143 C CD1 . LEU B 106 ? 0.8174 0.5122 0.9070 0.1534  0.0337  -0.0825 406 LEU B CD1 
2144 C CD2 . LEU B 106 ? 0.8702 0.6153 1.0227 0.2000  0.0270  -0.1032 406 LEU B CD2 
2145 N N   . LYS B 107 ? 1.0018 0.5193 1.0730 0.2039  -0.0252 -0.0282 407 LYS B N   
2146 C CA  . LYS B 107 ? 1.0543 0.5599 1.1034 0.2085  -0.0431 0.0016  407 LYS B CA  
2147 C C   . LYS B 107 ? 1.0686 0.5203 1.0710 0.1786  -0.0367 0.0275  407 LYS B C   
2148 O O   . LYS B 107 ? 1.0749 0.5371 1.0495 0.1646  -0.0379 0.0478  407 LYS B O   
2149 C CB  . LYS B 107 ? 1.2080 0.6902 1.2733 0.2492  -0.0691 0.0046  407 LYS B CB  
2150 C CG  . LYS B 107 ? 1.3864 0.8558 1.4236 0.2592  -0.0945 0.0353  407 LYS B CG  
2151 C CD  . LYS B 107 ? 1.5431 0.9171 1.5298 0.2635  -0.1103 0.0682  407 LYS B CD  
2152 C CE  . LYS B 107 ? 1.5993 0.9697 1.5616 0.2856  -0.1429 0.0933  407 LYS B CE  
2153 N NZ  . LYS B 107 ? 1.7572 1.0286 1.6581 0.2892  -0.1584 0.1302  407 LYS B NZ  
2154 N N   . HIS B 108 ? 1.1132 0.5108 1.1089 0.1664  -0.0277 0.0236  408 HIS B N   
2155 C CA  . HIS B 108 ? 1.1609 0.5084 1.1197 0.1346  -0.0177 0.0459  408 HIS B CA  
2156 C C   . HIS B 108 ? 1.0676 0.4658 1.0292 0.1022  0.0031  0.0377  408 HIS B C   
2157 O O   . HIS B 108 ? 1.0468 0.4421 0.9814 0.0793  0.0120  0.0570  408 HIS B O   
2158 C CB  . HIS B 108 ? 1.2771 0.5484 1.2342 0.1297  -0.0157 0.0421  408 HIS B CB  
2159 C CG  . HIS B 108 ? 1.4138 0.6089 1.3543 0.1573  -0.0366 0.0600  408 HIS B CG  
2160 N ND1 . HIS B 108 ? 1.5224 0.6932 1.4280 0.1731  -0.0552 0.0930  408 HIS B ND1 
2161 C CD2 . HIS B 108 ? 1.4616 0.5929 1.4124 0.1726  -0.0435 0.0489  408 HIS B CD2 
2162 C CE1 . HIS B 108 ? 1.5363 0.6305 1.4317 0.1996  -0.0747 0.1039  408 HIS B CE1 
2163 N NE2 . HIS B 108 ? 1.5841 0.6519 1.5087 0.1999  -0.0668 0.0767  408 HIS B NE2 
2164 N N   . ALA B 109 ? 1.0059 0.4497 0.9979 0.1023  0.0106  0.0085  409 ALA B N   
2165 C CA  . ALA B 109 ? 0.9653 0.4539 0.9616 0.0776  0.0252  -0.0003 409 ALA B CA  
2166 C C   . ALA B 109 ? 0.9595 0.4922 0.9446 0.0760  0.0256  0.0127  409 ALA B C   
2167 O O   . ALA B 109 ? 0.8479 0.3976 0.8241 0.0543  0.0366  0.0176  409 ALA B O   
2168 C CB  . ALA B 109 ? 0.9162 0.4366 0.9365 0.0824  0.0288  -0.0315 409 ALA B CB  
2169 N N   . MET B 110 ? 0.9387 0.4911 0.9285 0.0994  0.0129  0.0153  410 MET B N   
2170 C CA  . MET B 110 ? 0.8955 0.4841 0.8750 0.0979  0.0097  0.0253  410 MET B CA  
2171 C C   . MET B 110 ? 0.9724 0.5264 0.9117 0.0867  0.0078  0.0518  410 MET B C   
2172 O O   . MET B 110 ? 1.0066 0.5757 0.9298 0.0668  0.0196  0.0562  410 MET B O   
2173 C CB  . MET B 110 ? 0.9031 0.5239 0.9043 0.1235  -0.0051 0.0190  410 MET B CB  
2174 C CG  . MET B 110 ? 0.9042 0.5731 0.9391 0.1275  0.0045  -0.0064 410 MET B CG  
2175 S SD  . MET B 110 ? 0.8558 0.5658 0.8859 0.1033  0.0208  -0.0125 410 MET B SD  
2176 C CE  . MET B 110 ? 0.7994 0.5294 0.8168 0.0991  0.0108  0.0020  410 MET B CE  
2177 N N   . LYS B 111 ? 1.0872 0.5912 1.0063 0.1002  -0.0064 0.0695  411 LYS B N   
2178 C CA  . LYS B 111 ? 1.1231 0.5864 0.9910 0.0885  -0.0071 0.0982  411 LYS B CA  
2179 C C   . LYS B 111 ? 1.0154 0.4720 0.8706 0.0533  0.0202  0.1002  411 LYS B C   
2180 O O   . LYS B 111 ? 0.9338 0.3941 0.7552 0.0376  0.0294  0.1130  411 LYS B O   
2181 C CB  . LYS B 111 ? 1.3357 0.7253 1.1769 0.1033  -0.0228 0.1201  411 LYS B CB  
2182 C CG  . LYS B 111 ? 1.4664 0.8580 1.3167 0.1426  -0.0547 0.1223  411 LYS B CG  
2183 C CD  . LYS B 111 ? 1.6039 0.9303 1.4000 0.1574  -0.0780 0.1562  411 LYS B CD  
2184 C CE  . LYS B 111 ? 1.6897 1.0234 1.5141 0.2024  -0.1126 0.1508  411 LYS B CE  
2185 N NZ  . LYS B 111 ? 1.8236 1.1347 1.6004 0.2217  -0.1445 0.1780  411 LYS B NZ  
2186 N N   . GLU B 112 ? 1.0058 0.4559 0.8901 0.0413  0.0327  0.0845  412 GLU B N   
2187 C CA  . GLU B 112 ? 1.0377 0.4840 0.9218 0.0082  0.0566  0.0833  412 GLU B CA  
2188 C C   . GLU B 112 ? 0.9446 0.4552 0.8443 -0.0013 0.0678  0.0687  412 GLU B C   
2189 O O   . GLU B 112 ? 0.9531 0.4701 0.8370 -0.0225 0.0854  0.0755  412 GLU B O   
2195 N N   . CYS B 113 ? 0.8748 0.4290 0.8040 0.0143  0.0593  0.0486  413 CYS B N   
2196 C CA  . CYS B 113 ? 0.8069 0.4130 0.7478 0.0107  0.0652  0.0364  413 CYS B CA  
2197 C C   . CYS B 113 ? 0.8020 0.4157 0.7108 0.0089  0.0668  0.0499  413 CYS B C   
2198 O O   . CYS B 113 ? 0.7600 0.3905 0.6636 -0.0064 0.0822  0.0475  413 CYS B O   
2199 C CB  . CYS B 113 ? 0.8013 0.4391 0.7653 0.0284  0.0548  0.0198  413 CYS B CB  
2200 S SG  . CYS B 113 ? 0.8447 0.4852 0.8383 0.0288  0.0550  -0.0029 413 CYS B SG  
2201 N N   . LEU B 114 ? 0.8061 0.4074 0.6936 0.0253  0.0500  0.0620  414 LEU B N   
2202 C CA  . LEU B 114 ? 0.8105 0.4194 0.6636 0.0257  0.0456  0.0717  414 LEU B CA  
2203 C C   . LEU B 114 ? 0.9052 0.4805 0.7117 0.0078  0.0597  0.0908  414 LEU B C   
2204 O O   . LEU B 114 ? 0.9874 0.5730 0.7619 0.0014  0.0648  0.0936  414 LEU B O   
2205 C CB  . LEU B 114 ? 0.8233 0.4314 0.6719 0.0491  0.0191  0.0775  414 LEU B CB  
2206 C CG  . LEU B 114 ? 0.7797 0.4294 0.6732 0.0634  0.0098  0.0579  414 LEU B CG  
2207 C CD1 . LEU B 114 ? 0.7902 0.4461 0.6911 0.0869  -0.0157 0.0608  414 LEU B CD1 
2208 C CD2 . LEU B 114 ? 0.7348 0.4229 0.6354 0.0533  0.0176  0.0445  414 LEU B CD2 
2209 N N   . GLU B 115 ? 0.9505 0.4805 0.7472 -0.0013 0.0666  0.1045  415 GLU B N   
2210 C CA  . GLU B 115 ? 1.0005 0.4957 0.7497 -0.0235 0.0854  0.1247  415 GLU B CA  
2211 C C   . GLU B 115 ? 0.9571 0.4877 0.7305 -0.0485 0.1158  0.1082  415 GLU B C   
2212 O O   . GLU B 115 ? 0.9597 0.4947 0.7007 -0.0652 0.1361  0.1134  415 GLU B O   
2213 C CB  . GLU B 115 ? 1.1169 0.5471 0.8521 -0.0306 0.0867  0.1441  415 GLU B CB  
2214 C CG  . GLU B 115 ? 1.2137 0.6000 0.9223 -0.0021 0.0550  0.1629  415 GLU B CG  
2215 C CD  . GLU B 115 ? 1.3263 0.6496 0.9594 -0.0096 0.0551  0.1981  415 GLU B CD  
2216 O OE1 . GLU B 115 ? 1.3761 0.6463 0.9956 -0.0313 0.0727  0.2126  415 GLU B OE1 
2217 O OE2 . GLU B 115 ? 1.4419 0.7706 1.0310 0.0035  0.0385  0.2092  415 GLU B OE2 
2218 N N   . LYS B 116 ? 0.9268 0.4844 0.7575 -0.0499 0.1184  0.0865  416 LYS B N   
2219 C CA  . LYS B 116 ? 0.9417 0.5406 0.8052 -0.0681 0.1413  0.0676  416 LYS B CA  
2220 C C   . LYS B 116 ? 0.9370 0.5780 0.7953 -0.0593 0.1427  0.0559  416 LYS B C   
2221 O O   . LYS B 116 ? 0.9037 0.5724 0.7699 -0.0730 0.1651  0.0452  416 LYS B O   
2222 C CB  . LYS B 116 ? 0.8897 0.5104 0.8112 -0.0669 0.1361  0.0459  416 LYS B CB  
2223 C CG  . LYS B 116 ? 0.9279 0.5096 0.8608 -0.0801 0.1376  0.0498  416 LYS B CG  
2224 C CD  . LYS B 116 ? 0.9569 0.5700 0.9446 -0.0966 0.1462  0.0254  416 LYS B CD  
2225 C CE  . LYS B 116 ? 1.0593 0.6280 1.0576 -0.1129 0.1469  0.0266  416 LYS B CE  
2226 N NZ  . LYS B 116 ? 1.1865 0.6978 1.1440 -0.1341 0.1636  0.0542  416 LYS B NZ  
2227 N N   . CYS B 117 ? 0.8963 0.5422 0.7442 -0.0373 0.1199  0.0557  417 CYS B N   
2228 C CA  . CYS B 117 ? 0.9510 0.6265 0.7894 -0.0315 0.1203  0.0444  417 CYS B CA  
2229 C C   . CYS B 117 ? 1.0280 0.6924 0.8142 -0.0445 0.1372  0.0540  417 CYS B C   
2230 O O   . CYS B 117 ? 1.1614 0.8526 0.9471 -0.0485 0.1521  0.0384  417 CYS B O   
2231 C CB  . CYS B 117 ? 0.8595 0.5422 0.6961 -0.0117 0.0948  0.0421  417 CYS B CB  
2232 S SG  . CYS B 117 ? 0.7530 0.4552 0.6426 0.0015  0.0818  0.0279  417 CYS B SG  
2233 N N   . ILE B 118 ? 1.0105 0.6322 0.7482 -0.0502 0.1357  0.0791  418 ILE B N   
2234 C CA  . ILE B 118 ? 1.0302 0.6380 0.7074 -0.0653 0.1551  0.0897  418 ILE B CA  
2235 C C   . ILE B 118 ? 1.0458 0.6638 0.7395 -0.0924 0.1937  0.0847  418 ILE B C   
2236 O O   . ILE B 118 ? 1.0655 0.7032 0.7384 -0.1043 0.2189  0.0757  418 ILE B O   
2237 C CB  . ILE B 118 ? 1.0404 0.5940 0.6487 -0.0617 0.1389  0.1214  418 ILE B CB  
2238 C CG1 . ILE B 118 ? 1.0446 0.6003 0.6526 -0.0337 0.0988  0.1217  418 ILE B CG1 
2239 C CG2 . ILE B 118 ? 1.1054 0.6450 0.6389 -0.0777 0.1595  0.1317  418 ILE B CG2 
2240 C CD1 . ILE B 118 ? 1.1340 0.6382 0.6859 -0.0220 0.0736  0.1519  418 ILE B CD1 
2241 N N   . GLU B 119 ? 1.0473 0.6573 0.7840 -0.1023 0.1986  0.0861  419 GLU B N   
2242 C CA  . GLU B 119 ? 1.0778 0.7004 0.8394 -0.1321 0.2342  0.0804  419 GLU B CA  
2243 C C   . GLU B 119 ? 1.0098 0.6991 0.8214 -0.1312 0.2505  0.0474  419 GLU B C   
2244 O O   . GLU B 119 ? 1.0495 0.7614 0.8560 -0.1504 0.2844  0.0397  419 GLU B O   
2245 C CB  . GLU B 119 ? 1.1052 0.7092 0.9109 -0.1427 0.2311  0.0823  419 GLU B CB  
2246 C CG  . GLU B 119 ? 1.1728 0.7010 0.9290 -0.1457 0.2200  0.1152  419 GLU B CG  
2247 C CD  . GLU B 119 ? 1.1714 0.6704 0.9660 -0.1541 0.2142  0.1149  419 GLU B CD  
2248 O OE1 . GLU B 119 ? 1.1868 0.7294 1.0473 -0.1623 0.2205  0.0884  419 GLU B OE1 
2249 O OE2 . GLU B 119 ? 1.2163 0.6482 0.9748 -0.1512 0.2014  0.1395  419 GLU B OE2 
2250 N N   . GLN B 120 ? 0.9868 0.7059 0.8443 -0.1074 0.2267  0.0279  420 GLN B N   
2251 C CA  . GLN B 120 ? 0.9825 0.7581 0.8941 -0.1023 0.2366  -0.0026 420 GLN B CA  
2252 C C   . GLN B 120 ? 0.9318 0.7224 0.8219 -0.0836 0.2315  -0.0151 420 GLN B C   
2253 O O   . GLN B 120 ? 0.8985 0.7266 0.8326 -0.0711 0.2311  -0.0397 420 GLN B O   
2254 C CB  . GLN B 120 ? 0.9332 0.7257 0.9055 -0.0908 0.2147  -0.0153 420 GLN B CB  
2255 C CG  . GLN B 120 ? 0.9195 0.7171 0.9320 -0.1139 0.2271  -0.0179 420 GLN B CG  
2256 C CD  . GLN B 120 ? 0.8982 0.7032 0.9540 -0.1007 0.1998  -0.0289 420 GLN B CD  
2257 O OE1 . GLN B 120 ? 0.9404 0.7193 0.9754 -0.0819 0.1748  -0.0201 420 GLN B OE1 
2258 N NE2 . GLN B 120 ? 0.8865 0.7325 1.0032 -0.1093 0.2042  -0.0508 420 GLN B NE2 
2259 N N   . ASN B 121 ? 0.9542 0.7137 0.7771 -0.0814 0.2261  0.0004  421 ASN B N   
2260 C CA  . ASN B 121 ? 0.9957 0.7645 0.7958 -0.0662 0.2186  -0.0137 421 ASN B CA  
2261 C C   . ASN B 121 ? 0.9597 0.7450 0.8081 -0.0445 0.1939  -0.0295 421 ASN B C   
2262 O O   . ASN B 121 ? 1.0189 0.8304 0.8959 -0.0350 0.1994  -0.0532 421 ASN B O   
2263 C CB  . ASN B 121 ? 1.0313 0.8286 0.8257 -0.0749 0.2524  -0.0344 421 ASN B CB  
2264 C CG  . ASN B 121 ? 1.1094 0.8879 0.8446 -0.0998 0.2818  -0.0173 421 ASN B CG  
2265 O OD1 . ASN B 121 ? 1.1450 0.9467 0.9044 -0.1198 0.3163  -0.0235 421 ASN B OD1 
2266 N ND2 . ASN B 121 ? 1.1378 0.8762 0.7956 -0.0998 0.2689  0.0038  421 ASN B ND2 
2267 N N   . ILE B 122 ? 0.8913 0.6585 0.7477 -0.0368 0.1685  -0.0157 422 ILE B N   
2268 C CA  . ILE B 122 ? 0.8282 0.6021 0.7175 -0.0200 0.1457  -0.0236 422 ILE B CA  
2269 C C   . ILE B 122 ? 0.8035 0.5666 0.6611 -0.0115 0.1298  -0.0244 422 ILE B C   
2270 O O   . ILE B 122 ? 0.7947 0.5398 0.6112 -0.0147 0.1224  -0.0106 422 ILE B O   
2271 C CB  . ILE B 122 ? 0.7938 0.5545 0.7007 -0.0189 0.1314  -0.0101 422 ILE B CB  
2272 C CG1 . ILE B 122 ? 0.7797 0.5520 0.7229 -0.0299 0.1447  -0.0143 422 ILE B CG1 
2273 C CG2 . ILE B 122 ? 0.7117 0.4737 0.6367 -0.0038 0.1092  -0.0134 422 ILE B CG2 
2274 C CD1 . ILE B 122 ? 0.7449 0.5544 0.7322 -0.0261 0.1527  -0.0373 422 ILE B CD1 
2275 N N   . THR B 123 ? 0.8290 0.6010 0.7060 -0.0011 0.1226  -0.0407 423 THR B N   
2276 C CA  . THR B 123 ? 0.8827 0.6447 0.7371 0.0027  0.1076  -0.0451 423 THR B CA  
2277 C C   . THR B 123 ? 0.7740 0.5325 0.6510 0.0088  0.0881  -0.0401 423 THR B C   
2278 O O   . THR B 123 ? 0.8401 0.5942 0.7052 0.0078  0.0740  -0.0399 423 THR B O   
2279 C CB  . THR B 123 ? 0.8886 0.6532 0.7401 0.0066  0.1159  -0.0683 423 THR B CB  
2280 O OG1 . THR B 123 ? 0.9008 0.6722 0.7948 0.0169  0.1165  -0.0773 423 THR B OG1 
2281 C CG2 . THR B 123 ? 0.8769 0.6502 0.7042 0.0003  0.1402  -0.0776 423 THR B CG2 
2282 N N   . SER B 124 ? 0.6792 0.4424 0.5880 0.0134  0.0876  -0.0374 424 SER B N   
2283 C CA  . SER B 124 ? 0.6529 0.4128 0.5750 0.0171  0.0739  -0.0326 424 SER B CA  
2284 C C   . SER B 124 ? 0.5860 0.3497 0.5280 0.0199  0.0732  -0.0254 424 SER B C   
2285 O O   . SER B 124 ? 0.5491 0.3194 0.5066 0.0206  0.0805  -0.0296 424 SER B O   
2286 C CB  . SER B 124 ? 0.6582 0.4101 0.5880 0.0212  0.0711  -0.0428 424 SER B CB  
2287 O OG  . SER B 124 ? 0.6816 0.4365 0.6293 0.0297  0.0766  -0.0500 424 SER B OG  
2288 N N   . ILE B 125 ? 0.5716 0.3345 0.5166 0.0214  0.0642  -0.0180 425 ILE B N   
2289 C CA  . ILE B 125 ? 0.5710 0.3343 0.5305 0.0247  0.0631  -0.0145 425 ILE B CA  
2290 C C   . ILE B 125 ? 0.5449 0.3122 0.5108 0.0281  0.0572  -0.0146 425 ILE B C   
2291 O O   . ILE B 125 ? 0.5771 0.3506 0.5416 0.0268  0.0526  -0.0129 425 ILE B O   
2292 C CB  . ILE B 125 ? 0.5734 0.3279 0.5270 0.0230  0.0635  -0.0052 425 ILE B CB  
2293 C CG1 . ILE B 125 ? 0.5727 0.3223 0.5425 0.0261  0.0622  -0.0062 425 ILE B CG1 
2294 C CG2 . ILE B 125 ? 0.5771 0.3290 0.5165 0.0264  0.0532  0.0026  425 ILE B CG2 
2295 C CD1 . ILE B 125 ? 0.6296 0.3593 0.5945 0.0216  0.0650  0.0021  425 ILE B CD1 
2296 N N   . SER B 126 ? 0.5228 0.2897 0.4954 0.0316  0.0576  -0.0178 426 SER B N   
2297 C CA  . SER B 126 ? 0.5660 0.3365 0.5382 0.0326  0.0575  -0.0181 426 SER B CA  
2298 C C   . SER B 126 ? 0.5945 0.3665 0.5725 0.0382  0.0574  -0.0217 426 SER B C   
2299 O O   . SER B 126 ? 0.5549 0.3218 0.5342 0.0401  0.0552  -0.0260 426 SER B O   
2300 C CB  . SER B 126 ? 0.6263 0.3865 0.5862 0.0311  0.0580  -0.0180 426 SER B CB  
2301 O OG  . SER B 126 ? 0.7479 0.5002 0.7034 0.0268  0.0578  -0.0181 426 SER B OG  
2302 N N   . PHE B 127 ? 0.6381 0.4203 0.6230 0.0408  0.0597  -0.0233 427 PHE B N   
2303 C CA  . PHE B 127 ? 0.6477 0.4307 0.6399 0.0486  0.0607  -0.0305 427 PHE B CA  
2304 C C   . PHE B 127 ? 0.6868 0.4816 0.6729 0.0482  0.0698  -0.0367 427 PHE B C   
2305 O O   . PHE B 127 ? 0.6730 0.4822 0.6627 0.0417  0.0761  -0.0342 427 PHE B O   
2306 C CB  . PHE B 127 ? 0.6501 0.4368 0.6596 0.0570  0.0564  -0.0297 427 PHE B CB  
2307 C CG  . PHE B 127 ? 0.6952 0.4653 0.7012 0.0569  0.0485  -0.0194 427 PHE B CG  
2308 C CD1 . PHE B 127 ? 0.6807 0.4559 0.6792 0.0519  0.0445  -0.0114 427 PHE B CD1 
2309 C CD2 . PHE B 127 ? 0.7337 0.4794 0.7395 0.0604  0.0460  -0.0179 427 PHE B CD2 
2310 C CE1 . PHE B 127 ? 0.6739 0.4318 0.6579 0.0507  0.0395  -0.0011 427 PHE B CE1 
2311 C CE2 . PHE B 127 ? 0.7331 0.4579 0.7271 0.0574  0.0421  -0.0049 427 PHE B CE2 
2312 C CZ  . PHE B 127 ? 0.7445 0.4765 0.7245 0.0529  0.0395  0.0041  427 PHE B CZ  
2313 N N   . PRO B 128 ? 0.7250 0.5153 0.7016 0.0534  0.0722  -0.0469 428 PRO B N   
2314 C CA  . PRO B 128 ? 0.7018 0.5051 0.6688 0.0538  0.0853  -0.0552 428 PRO B CA  
2315 C C   . PRO B 128 ? 0.6975 0.5200 0.6958 0.0639  0.0900  -0.0653 428 PRO B C   
2316 O O   . PRO B 128 ? 0.6609 0.4788 0.6801 0.0709  0.0794  -0.0619 428 PRO B O   
2317 C CB  . PRO B 128 ? 0.7158 0.5039 0.6568 0.0571  0.0814  -0.0643 428 PRO B CB  
2318 C CG  . PRO B 128 ? 0.6996 0.4742 0.6582 0.0617  0.0683  -0.0682 428 PRO B CG  
2319 C CD  . PRO B 128 ? 0.7285 0.5025 0.7031 0.0571  0.0638  -0.0536 428 PRO B CD  
2320 N N   . ALA B 129 ? 0.7603 0.6045 0.7609 0.0654  0.1062  -0.0773 429 ALA B N   
2321 C CA  . ALA B 129 ? 0.7957 0.6635 0.8337 0.0801  0.1103  -0.0916 429 ALA B CA  
2322 C C   . ALA B 129 ? 0.8775 0.7220 0.9136 0.0960  0.1041  -0.1061 429 ALA B C   
2323 O O   . ALA B 129 ? 0.9345 0.7838 0.9597 0.1013  0.1167  -0.1250 429 ALA B O   
2324 C CB  . ALA B 129 ? 0.8667 0.7725 0.9139 0.0748  0.1342  -0.1027 429 ALA B CB  
2325 N N   . LEU B 130 ? 0.8117 0.6287 0.8560 0.1015  0.0860  -0.0976 430 LEU B N   
2326 C CA  . LEU B 130 ? 0.8150 0.5981 0.8563 0.1103  0.0779  -0.1078 430 LEU B CA  
2327 C C   . LEU B 130 ? 0.8351 0.6237 0.8981 0.1311  0.0839  -0.1305 430 LEU B C   
2328 O O   . LEU B 130 ? 0.8471 0.6535 0.9433 0.1463  0.0817  -0.1311 430 LEU B O   
2329 C CB  . LEU B 130 ? 0.7952 0.5485 0.8430 0.1095  0.0621  -0.0907 430 LEU B CB  
2330 C CG  . LEU B 130 ? 0.7281 0.4701 0.7568 0.0907  0.0576  -0.0755 430 LEU B CG  
2331 C CD1 . LEU B 130 ? 0.7645 0.4845 0.7978 0.0897  0.0482  -0.0580 430 LEU B CD1 
2332 C CD2 . LEU B 130 ? 0.7133 0.4391 0.7275 0.0821  0.0560  -0.0864 430 LEU B CD2 
2333 N N   . GLY B 131 ? 0.8836 0.6578 0.9286 0.1334  0.0894  -0.1518 431 GLY B N   
2334 C CA  . GLY B 131 ? 0.9290 0.6963 0.9922 0.1551  0.0937  -0.1781 431 GLY B CA  
2335 C C   . GLY B 131 ? 0.9459 0.7608 1.0183 0.1631  0.1172  -0.1979 431 GLY B C   
2336 O O   . GLY B 131 ? 1.0150 0.8349 1.1112 0.1851  0.1239  -0.2233 431 GLY B O   
2337 N N   . THR B 132 ? 0.8978 0.7458 0.9517 0.1450  0.1317  -0.1877 432 THR B N   
2338 C CA  . THR B 132 ? 0.8630 0.7572 0.9226 0.1460  0.1600  -0.2051 432 THR B CA  
2339 C C   . THR B 132 ? 0.9098 0.7939 0.9174 0.1412  0.1752  -0.2254 432 THR B C   
2340 O O   . THR B 132 ? 0.9612 0.8772 0.9669 0.1453  0.2025  -0.2479 432 THR B O   
2341 C CB  . THR B 132 ? 0.7982 0.7274 0.8641 0.1262  0.1698  -0.1841 432 THR B CB  
2342 O OG1 . THR B 132 ? 0.7883 0.6891 0.8115 0.1057  0.1591  -0.1591 432 THR B OG1 
2343 C CG2 . THR B 132 ? 0.7739 0.7235 0.8966 0.1365  0.1553  -0.1751 432 THR B CG2 
2344 N N   . GLY B 133 ? 0.9246 0.7667 0.8917 0.1336  0.1571  -0.2204 433 GLY B N   
2345 C CA  . GLY B 133 ? 0.9941 0.8245 0.9023 0.1273  0.1640  -0.2365 433 GLY B CA  
2346 C C   . GLY B 133 ? 1.0831 0.9134 0.9948 0.1463  0.1764  -0.2764 433 GLY B C   
2347 O O   . GLY B 133 ? 1.1579 0.9658 1.1066 0.1633  0.1631  -0.2896 433 GLY B O   
2348 N N   . ASN B 134 ? 1.1479 1.0010 1.0196 0.1430  0.2038  -0.2943 434 ASN B N   
2349 C CA  . ASN B 134 ? 1.2052 1.0623 1.0685 0.1599  0.2215  -0.3372 434 ASN B CA  
2350 C C   . ASN B 134 ? 1.2649 1.1599 1.1984 0.1821  0.2412  -0.3564 434 ASN B C   
2351 O O   . ASN B 134 ? 1.4397 1.3417 1.3765 0.2006  0.2583  -0.3959 434 ASN B O   
2352 C CB  . ASN B 134 ? 1.2113 1.0189 1.0624 0.1695  0.1960  -0.3605 434 ASN B CB  
2353 C CG  . ASN B 134 ? 1.2447 1.0287 1.0209 0.1525  0.1819  -0.3600 434 ASN B CG  
2354 O OD1 . ASN B 134 ? 1.2801 1.0775 0.9953 0.1473  0.2019  -0.3734 434 ASN B OD1 
2355 N ND2 . ASN B 134 ? 1.1897 0.9404 0.9690 0.1443  0.1482  -0.3467 434 ASN B ND2 
2356 N N   . MET B 135 ? 1.2783 1.2005 1.2672 0.1816  0.2383  -0.3319 435 MET B N   
2357 C CA  . MET B 135 ? 1.3334 1.2840 1.4007 0.2089  0.2408  -0.3475 435 MET B CA  
2358 C C   . MET B 135 ? 1.3477 1.2430 1.4338 0.2339  0.2126  -0.3614 435 MET B C   
2359 O O   . MET B 135 ? 1.5901 1.4788 1.6874 0.2578  0.2216  -0.3998 435 MET B O   
2360 C CB  . MET B 135 ? 1.3960 1.4045 1.4857 0.2213  0.2809  -0.3846 435 MET B CB  
2361 C CG  . MET B 135 ? 1.4491 1.5139 1.5245 0.1939  0.3167  -0.3744 435 MET B CG  
2362 S SD  . MET B 135 ? 1.6626 1.7007 1.6221 0.1642  0.3366  -0.3712 435 MET B SD  
2363 C CE  . MET B 135 ? 1.6369 1.6848 1.5793 0.1882  0.3655  -0.4301 435 MET B CE  
2364 N N   . GLU B 136 ? 1.2069 1.0586 1.2930 0.2265  0.1804  -0.3307 436 GLU B N   
2365 C CA  . GLU B 136 ? 1.1131 0.9056 1.2174 0.2436  0.1534  -0.3341 436 GLU B CA  
2366 C C   . GLU B 136 ? 1.0432 0.8437 1.2078 0.2649  0.1387  -0.3179 436 GLU B C   
2367 O O   . GLU B 136 ? 1.0430 0.8209 1.2435 0.2960  0.1295  -0.3352 436 GLU B O   
2368 C CB  . GLU B 136 ? 1.0764 0.8220 1.1386 0.2175  0.1323  -0.3112 436 GLU B CB  
2369 C CG  . GLU B 136 ? 1.1476 0.8259 1.2060 0.2231  0.1131  -0.3258 436 GLU B CG  
2370 C CD  . GLU B 136 ? 1.2016 0.8631 1.2404 0.2345  0.1230  -0.3725 436 GLU B CD  
2371 O OE1 . GLU B 136 ? 1.1989 0.8580 1.1884 0.2152  0.1241  -0.3836 436 GLU B OE1 
2372 O OE2 . GLU B 136 ? 1.1941 0.8456 1.2661 0.2646  0.1281  -0.3992 436 GLU B OE2 
2373 N N   . ILE B 137 ? 1.0181 0.8469 1.1897 0.2486  0.1337  -0.2843 437 ILE B N   
2374 C CA  . ILE B 137 ? 0.9708 0.8261 1.1953 0.2654  0.1214  -0.2702 437 ILE B CA  
2375 C C   . ILE B 137 ? 0.9366 0.8725 1.1862 0.2566  0.1457  -0.2747 437 ILE B C   
2376 O O   . ILE B 137 ? 0.8631 0.8157 1.0754 0.2264  0.1624  -0.2645 437 ILE B O   
2377 C CB  . ILE B 137 ? 0.9251 0.7439 1.1357 0.2517  0.0943  -0.2300 437 ILE B CB  
2378 C CG1 . ILE B 137 ? 0.9524 0.6920 1.1337 0.2500  0.0768  -0.2243 437 ILE B CG1 
2379 C CG2 . ILE B 137 ? 0.8992 0.7424 1.1575 0.2719  0.0763  -0.2168 437 ILE B CG2 
2380 C CD1 . ILE B 137 ? 0.9346 0.6400 1.0964 0.2318  0.0572  -0.1863 437 ILE B CD1 
2381 N N   . LYS B 138 ? 0.9799 0.9635 1.2945 0.2833  0.1469  -0.2908 438 LYS B N   
2382 C CA  . LYS B 138 ? 1.0094 1.0771 1.3633 0.2747  0.1719  -0.3006 438 LYS B CA  
2383 C C   . LYS B 138 ? 0.9945 1.0767 1.3397 0.2444  0.1622  -0.2653 438 LYS B C   
2384 O O   . LYS B 138 ? 0.9949 1.0388 1.3319 0.2459  0.1306  -0.2386 438 LYS B O   
2385 C CB  . LYS B 138 ? 1.0528 1.1675 1.4897 0.3152  0.1666  -0.3270 438 LYS B CB  
2386 C CG  . LYS B 138 ? 1.1491 1.2980 1.6111 0.3362  0.1988  -0.3737 438 LYS B CG  
2387 C CD  . LYS B 138 ? 1.2051 1.4273 1.6659 0.3067  0.2461  -0.3885 438 LYS B CD  
2388 C CE  . LYS B 138 ? 1.2133 1.5234 1.7488 0.3015  0.2528  -0.3891 438 LYS B CE  
2389 N NZ  . LYS B 138 ? 1.2123 1.5492 1.7129 0.2515  0.2799  -0.3695 438 LYS B NZ  
2390 N N   . LYS B 139 ? 1.0148 1.1496 1.3595 0.2161  0.1916  -0.2664 439 LYS B N   
2391 C CA  . LYS B 139 ? 0.9896 1.1289 1.3154 0.1827  0.1875  -0.2361 439 LYS B CA  
2392 C C   . LYS B 139 ? 0.9053 1.0578 1.2769 0.1938  0.1541  -0.2219 439 LYS B C   
2393 O O   . LYS B 139 ? 0.9527 1.0628 1.2919 0.1836  0.1303  -0.1939 439 LYS B O   
2394 C CB  . LYS B 139 ? 1.0879 1.2864 1.4221 0.1532  0.2255  -0.2433 439 LYS B CB  
2395 C CG  . LYS B 139 ? 1.3075 1.4959 1.5851 0.1384  0.2614  -0.2546 439 LYS B CG  
2396 C CD  . LYS B 139 ? 1.4514 1.6919 1.7306 0.1050  0.3026  -0.2572 439 LYS B CD  
2397 C CE  . LYS B 139 ? 1.6095 1.8227 1.8073 0.0859  0.3333  -0.2576 439 LYS B CE  
2398 N NZ  . LYS B 139 ? 1.6894 1.9152 1.8863 0.1100  0.3531  -0.2939 439 LYS B NZ  
2399 N N   . GLU B 140 ? 0.8929 1.1070 1.3398 0.2165  0.1519  -0.2434 440 GLU B N   
2400 C CA  . GLU B 140 ? 0.9070 1.1458 1.4010 0.2286  0.1180  -0.2338 440 GLU B CA  
2401 C C   . GLU B 140 ? 0.9159 1.0836 1.3835 0.2544  0.0771  -0.2136 440 GLU B C   
2402 O O   . GLU B 140 ? 0.9515 1.1126 1.4197 0.2544  0.0467  -0.1932 440 GLU B O   
2403 C CB  . GLU B 140 ? 0.9546 1.2764 1.5426 0.2561  0.1185  -0.2654 440 GLU B CB  
2404 C CG  . GLU B 140 ? 0.9877 1.3952 1.6191 0.2278  0.1599  -0.2869 440 GLU B CG  
2405 C CD  . GLU B 140 ? 1.0333 1.4519 1.6458 0.2194  0.2090  -0.3100 440 GLU B CD  
2406 O OE1 . GLU B 140 ? 1.0582 1.4206 1.6286 0.2397  0.2093  -0.3152 440 GLU B OE1 
2407 O OE2 . GLU B 140 ? 1.0107 1.4922 1.6466 0.1896  0.2476  -0.3227 440 GLU B OE2 
2408 N N   . THR B 141 ? 0.9092 1.0230 1.3527 0.2754  0.0772  -0.2207 441 THR B N   
2409 C CA  . THR B 141 ? 0.8870 0.9266 1.3050 0.2976  0.0430  -0.2020 441 THR B CA  
2410 C C   . THR B 141 ? 0.8242 0.8044 1.1710 0.2657  0.0380  -0.1695 441 THR B C   
2411 O O   . THR B 141 ? 0.7737 0.7181 1.1006 0.2676  0.0104  -0.1436 441 THR B O   
2412 C CB  . THR B 141 ? 0.8955 0.8976 1.3181 0.3281  0.0472  -0.2251 441 THR B CB  
2413 O OG1 . THR B 141 ? 0.9028 0.9593 1.4001 0.3659  0.0435  -0.2535 441 THR B OG1 
2414 C CG2 . THR B 141 ? 0.9234 0.8341 1.3106 0.3438  0.0173  -0.2041 441 THR B CG2 
2415 N N   . ALA B 142 ? 0.7972 0.7681 1.1044 0.2380  0.0646  -0.1717 442 ALA B N   
2416 C CA  . ALA B 142 ? 0.8274 0.7558 1.0781 0.2090  0.0613  -0.1453 442 ALA B CA  
2417 C C   . ALA B 142 ? 0.8546 0.8078 1.1105 0.1944  0.0484  -0.1254 442 ALA B C   
2418 O O   . ALA B 142 ? 0.9171 0.8329 1.1492 0.1935  0.0265  -0.1029 442 ALA B O   
2419 C CB  . ALA B 142 ? 0.8288 0.7581 1.0442 0.1850  0.0885  -0.1528 442 ALA B CB  
2420 N N   . ALA B 143 ? 0.8158 0.8322 1.1040 0.1827  0.0631  -0.1360 443 ALA B N   
2421 C CA  . ALA B 143 ? 0.7569 0.8019 1.0567 0.1674  0.0511  -0.1239 443 ALA B CA  
2422 C C   . ALA B 143 ? 0.7790 0.8198 1.0993 0.1930  0.0145  -0.1158 443 ALA B C   
2423 O O   . ALA B 143 ? 0.8480 0.8633 1.1374 0.1839  -0.0045 -0.0950 443 ALA B O   
2424 C CB  . ALA B 143 ? 0.7185 0.8339 1.0614 0.1518  0.0736  -0.1416 443 ALA B CB  
2425 N N   . GLU B 144 ? 0.7829 0.8450 1.1506 0.2272  0.0037  -0.1324 444 GLU B N   
2426 C CA  . GLU B 144 ? 0.8514 0.9026 1.2329 0.2566  -0.0359 -0.1225 444 GLU B CA  
2427 C C   . GLU B 144 ? 0.8677 0.8348 1.1795 0.2531  -0.0525 -0.0914 444 GLU B C   
2428 O O   . GLU B 144 ? 0.8712 0.8267 1.1597 0.2502  -0.0771 -0.0719 444 GLU B O   
2429 C CB  . GLU B 144 ? 0.9594 1.0261 1.3944 0.3004  -0.0460 -0.1438 444 GLU B CB  
2430 C CG  . GLU B 144 ? 1.0120 1.1773 1.5322 0.3108  -0.0419 -0.1737 444 GLU B CG  
2431 C CD  . GLU B 144 ? 1.1023 1.2914 1.6826 0.3542  -0.0417 -0.2031 444 GLU B CD  
2432 O OE1 . GLU B 144 ? 1.2255 1.3653 1.8019 0.3926  -0.0742 -0.1949 444 GLU B OE1 
2433 O OE2 . GLU B 144 ? 1.0997 1.3536 1.7285 0.3496  -0.0077 -0.2344 444 GLU B OE2 
2434 N N   . ILE B 145 ? 0.8378 0.7494 1.1160 0.2507  -0.0374 -0.0891 445 ILE B N   
2435 C CA  . ILE B 145 ? 0.8505 0.6838 1.0716 0.2463  -0.0485 -0.0630 445 ILE B CA  
2436 C C   . ILE B 145 ? 0.8073 0.6331 0.9842 0.2107  -0.0408 -0.0447 445 ILE B C   
2437 O O   . ILE B 145 ? 0.8053 0.5944 0.9440 0.2068  -0.0568 -0.0215 445 ILE B O   
2438 C CB  . ILE B 145 ? 0.8794 0.6636 1.0875 0.2503  -0.0338 -0.0719 445 ILE B CB  
2439 C CG1 . ILE B 145 ? 0.9188 0.6942 1.1651 0.2908  -0.0467 -0.0882 445 ILE B CG1 
2440 C CG2 . ILE B 145 ? 0.9143 0.6253 1.0662 0.2326  -0.0362 -0.0473 445 ILE B CG2 
2441 C CD1 . ILE B 145 ? 0.9446 0.6727 1.1824 0.2962  -0.0327 -0.1041 445 ILE B CD1 
2442 N N   . LEU B 146 ? 0.8028 0.6595 0.9813 0.1862  -0.0156 -0.0554 446 LEU B N   
2443 C CA  . LEU B 146 ? 0.8159 0.6651 0.9577 0.1561  -0.0075 -0.0420 446 LEU B CA  
2444 C C   . LEU B 146 ? 0.7912 0.6584 0.9293 0.1526  -0.0269 -0.0313 446 LEU B C   
2445 O O   . LEU B 146 ? 0.8066 0.6389 0.9028 0.1437  -0.0347 -0.0130 446 LEU B O   
2446 C CB  . LEU B 146 ? 0.8111 0.6893 0.9575 0.1357  0.0187  -0.0551 446 LEU B CB  
2447 C CG  . LEU B 146 ? 0.8140 0.6628 0.9371 0.1289  0.0357  -0.0600 446 LEU B CG  
2448 C CD1 . LEU B 146 ? 0.8612 0.6814 0.9460 0.1083  0.0377  -0.0454 446 LEU B CD1 
2449 C CD2 . LEU B 146 ? 0.8429 0.6547 0.9664 0.1475  0.0300  -0.0647 446 LEU B CD2 
2450 N N   . PHE B 147 ? 0.7643 0.6879 0.9467 0.1588  -0.0342 -0.0450 447 PHE B N   
2451 C CA  . PHE B 147 ? 0.7853 0.7301 0.9675 0.1566  -0.0576 -0.0396 447 PHE B CA  
2452 C C   . PHE B 147 ? 0.8457 0.7507 0.9999 0.1800  -0.0887 -0.0212 447 PHE B C   
2453 O O   . PHE B 147 ? 0.8998 0.7819 1.0091 0.1704  -0.1013 -0.0054 447 PHE B O   
2454 C CB  . PHE B 147 ? 0.7631 0.7821 1.0089 0.1589  -0.0623 -0.0613 447 PHE B CB  
2455 C CG  . PHE B 147 ? 0.7858 0.8347 1.0422 0.1260  -0.0333 -0.0723 447 PHE B CG  
2456 C CD1 . PHE B 147 ? 0.8686 0.9203 1.1062 0.1003  -0.0362 -0.0689 447 PHE B CD1 
2457 C CD2 . PHE B 147 ? 0.7822 0.8469 1.0584 0.1202  -0.0027 -0.0849 447 PHE B CD2 
2458 C CE1 . PHE B 147 ? 0.8378 0.9038 1.0803 0.0702  -0.0104 -0.0760 447 PHE B CE1 
2459 C CE2 . PHE B 147 ? 0.7976 0.8782 1.0722 0.0893  0.0236  -0.0898 447 PHE B CE2 
2460 C CZ  . PHE B 147 ? 0.8231 0.9015 1.0819 0.0645  0.0193  -0.0842 447 PHE B CZ  
2461 N N   . ASP B 148 ? 0.8920 0.7851 1.0688 0.2110  -0.1003 -0.0235 448 ASP B N   
2462 C CA  . ASP B 148 ? 0.9446 0.7891 1.0919 0.2366  -0.1311 -0.0031 448 ASP B CA  
2463 C C   . ASP B 148 ? 0.9375 0.7165 1.0089 0.2164  -0.1265 0.0243  448 ASP B C   
2464 O O   . ASP B 148 ? 0.9646 0.7266 0.9949 0.2174  -0.1486 0.0418  448 ASP B O   
2465 C CB  . ASP B 148 ? 1.0633 0.8792 1.2339 0.2678  -0.1344 -0.0080 448 ASP B CB  
2466 C CG  . ASP B 148 ? 1.1990 1.0429 1.4179 0.3101  -0.1683 -0.0171 448 ASP B CG  
2467 O OD1 . ASP B 148 ? 1.2233 1.1012 1.4474 0.3164  -0.1971 -0.0135 448 ASP B OD1 
2468 O OD2 . ASP B 148 ? 1.3430 1.1749 1.5952 0.3381  -0.1675 -0.0298 448 ASP B OD2 
2469 N N   . GLU B 149 ? 0.8971 0.6433 0.9502 0.1975  -0.0976 0.0259  449 GLU B N   
2470 C CA  . GLU B 149 ? 0.9403 0.6284 0.9318 0.1783  -0.0893 0.0490  449 GLU B CA  
2471 C C   . GLU B 149 ? 0.9242 0.6330 0.8868 0.1531  -0.0833 0.0521  449 GLU B C   
2472 O O   . GLU B 149 ? 0.8939 0.5701 0.8032 0.1462  -0.0903 0.0716  449 GLU B O   
2473 C CB  . GLU B 149 ? 0.9258 0.5858 0.9196 0.1654  -0.0626 0.0436  449 GLU B CB  
2474 C CG  . GLU B 149 ? 0.9892 0.6094 0.9977 0.1894  -0.0701 0.0422  449 GLU B CG  
2475 C CD  . GLU B 149 ? 1.1268 0.6824 1.0921 0.2022  -0.0920 0.0707  449 GLU B CD  
2476 O OE1 . GLU B 149 ? 1.1912 0.7043 1.1068 0.1784  -0.0812 0.0912  449 GLU B OE1 
2477 O OE2 . GLU B 149 ? 1.2348 0.7836 1.2143 0.2356  -0.1194 0.0732  449 GLU B OE2 
2478 N N   . VAL B 150 ? 0.8898 0.6487 0.8845 0.1391  -0.0689 0.0323  450 VAL B N   
2479 C CA  . VAL B 150 ? 0.8467 0.6219 0.8194 0.1166  -0.0627 0.0307  450 VAL B CA  
2480 C C   . VAL B 150 ? 0.9139 0.6978 0.8656 0.1250  -0.0920 0.0369  450 VAL B C   
2481 O O   . VAL B 150 ? 0.9387 0.6968 0.8367 0.1143  -0.0933 0.0492  450 VAL B O   
2482 C CB  . VAL B 150 ? 0.7600 0.5788 0.7690 0.1017  -0.0455 0.0104  450 VAL B CB  
2483 C CG1 . VAL B 150 ? 0.7678 0.5985 0.7568 0.0822  -0.0443 0.0067  450 VAL B CG1 
2484 C CG2 . VAL B 150 ? 0.7399 0.5436 0.7523 0.0924  -0.0198 0.0070  450 VAL B CG2 
2485 N N   . LEU B 151 ? 0.9038 0.7261 0.8975 0.1450  -0.1158 0.0268  451 LEU B N   
2486 C CA  . LEU B 151 ? 0.9389 0.7775 0.9182 0.1548  -0.1501 0.0290  451 LEU B CA  
2487 C C   . LEU B 151 ? 1.0377 0.8154 0.9489 0.1680  -0.1688 0.0576  451 LEU B C   
2488 O O   . LEU B 151 ? 1.1458 0.9146 1.0060 0.1633  -0.1859 0.0658  451 LEU B O   
2489 C CB  . LEU B 151 ? 0.9369 0.8333 0.9848 0.1772  -0.1739 0.0112  451 LEU B CB  
2490 C CG  . LEU B 151 ? 0.9454 0.9072 1.0588 0.1598  -0.1554 -0.0168 451 LEU B CG  
2491 C CD1 . LEU B 151 ? 0.9871 1.0148 1.1583 0.1753  -0.1869 -0.0350 451 LEU B CD1 
2492 C CD2 . LEU B 151 ? 0.9621 0.9228 1.0510 0.1241  -0.1335 -0.0219 451 LEU B CD2 
2493 N N   . THR B 152 ? 1.0342 0.7662 0.9405 0.1831  -0.1651 0.0724  452 THR B N   
2494 C CA  . THR B 152 ? 1.1383 0.8008 0.9774 0.1934  -0.1796 0.1034  452 THR B CA  
2495 C C   . THR B 152 ? 1.1325 0.7636 0.9014 0.1627  -0.1580 0.1171  452 THR B C   
2496 O O   . THR B 152 ? 1.1690 0.7734 0.8725 0.1638  -0.1757 0.1351  452 THR B O   
2497 C CB  . THR B 152 ? 1.2269 0.8413 1.0793 0.2067  -0.1701 0.1122  452 THR B CB  
2498 O OG1 . THR B 152 ? 1.2114 0.8503 1.1172 0.2434  -0.1987 0.1016  452 THR B OG1 
2499 C CG2 . THR B 152 ? 1.3225 0.8501 1.1002 0.2048  -0.1713 0.1470  452 THR B CG2 
2500 N N   . PHE B 153 ? 1.1219 0.7576 0.9048 0.1373  -0.1201 0.1072  453 PHE B N   
2501 C CA  . PHE B 153 ? 1.1801 0.7964 0.9137 0.1088  -0.0935 0.1135  453 PHE B CA  
2502 C C   . PHE B 153 ? 1.2327 0.8774 0.9364 0.1008  -0.1039 0.1048  453 PHE B C   
2503 O O   . PHE B 153 ? 1.3450 0.9616 0.9813 0.0889  -0.0982 0.1177  453 PHE B O   
2504 C CB  . PHE B 153 ? 1.1315 0.7673 0.9078 0.0906  -0.0598 0.0961  453 PHE B CB  
2505 C CG  . PHE B 153 ? 1.1225 0.7534 0.8663 0.0642  -0.0317 0.0949  453 PHE B CG  
2506 C CD1 . PHE B 153 ? 1.1344 0.7986 0.8737 0.0547  -0.0295 0.0786  453 PHE B CD1 
2507 C CD2 . PHE B 153 ? 1.1370 0.7311 0.8588 0.0487  -0.0072 0.1076  453 PHE B CD2 
2508 C CE1 . PHE B 153 ? 1.1807 0.8421 0.8948 0.0350  -0.0035 0.0738  453 PHE B CE1 
2509 C CE2 . PHE B 153 ? 1.1694 0.7683 0.8702 0.0264  0.0200  0.1029  453 PHE B CE2 
2510 C CZ  . PHE B 153 ? 1.2032 0.8361 0.9001 0.0219  0.0216  0.0855  453 PHE B CZ  
2511 N N   . ALA B 154 ? 1.2223 0.9220 0.9754 0.1050  -0.1171 0.0810  454 ALA B N   
2512 C CA  . ALA B 154 ? 1.2689 0.9968 1.0021 0.0961  -0.1296 0.0670  454 ALA B CA  
2513 C C   . ALA B 154 ? 1.4106 1.1161 1.0788 0.1094  -0.1635 0.0838  454 ALA B C   
2514 O O   . ALA B 154 ? 1.6022 1.3040 1.2157 0.0966  -0.1645 0.0801  454 ALA B O   
2515 C CB  . ALA B 154 ? 1.2387 1.0264 1.0427 0.0971  -0.1398 0.0403  454 ALA B CB  
2516 N N   . LYS B 155 ? 1.4737 1.1617 1.1444 0.1366  -0.1920 0.1011  455 LYS B N   
2517 C CA  . LYS B 155 ? 1.5208 1.1801 1.1249 0.1548  -0.2305 0.1216  455 LYS B CA  
2518 C C   . LYS B 155 ? 1.5181 1.1008 1.0311 0.1451  -0.2123 0.1555  455 LYS B C   
2519 O O   . LYS B 155 ? 1.5668 1.1240 0.9959 0.1412  -0.2243 0.1689  455 LYS B O   
2520 C CB  . LYS B 155 ? 1.5266 1.2000 1.1761 0.1923  -0.2723 0.1246  455 LYS B CB  
2521 C CG  . LYS B 155 ? 1.4967 1.2557 1.2327 0.1973  -0.2906 0.0889  455 LYS B CG  
2522 C CD  . LYS B 155 ? 1.5284 1.3217 1.2955 0.2332  -0.3457 0.0846  455 LYS B CD  
2523 C CE  . LYS B 155 ? 1.4265 1.3110 1.2778 0.2270  -0.3575 0.0459  455 LYS B CE  
2524 N NZ  . LYS B 155 ? 1.4029 1.3077 1.2199 0.1987  -0.3593 0.0298  455 LYS B NZ  
2525 N N   . ASP B 156 ? 1.4621 1.0097 0.9901 0.1377  -0.1810 0.1674  456 ASP B N   
2526 C CA  . ASP B 156 ? 1.5878 1.0593 1.0405 0.1283  -0.1646 0.2017  456 ASP B CA  
2527 C C   . ASP B 156 ? 1.5918 1.0584 1.0063 0.0914  -0.1186 0.1985  456 ASP B C   
2528 O O   . ASP B 156 ? 1.7229 1.1334 1.0679 0.0759  -0.0988 0.2249  456 ASP B O   
2529 C CB  . ASP B 156 ? 1.6094 1.0407 1.0976 0.1402  -0.1599 0.2152  456 ASP B CB  
2530 C CG  . ASP B 156 ? 1.6485 1.0700 1.1601 0.1820  -0.2066 0.2228  456 ASP B CG  
2531 O OD1 . ASP B 156 ? 1.6343 1.0851 1.1364 0.2026  -0.2465 0.2189  456 ASP B OD1 
2532 O OD2 . ASP B 156 ? 1.6652 1.0518 1.2080 0.1951  -0.2045 0.2298  456 ASP B OD2 
2533 N N   . HIS B 157 ? 1.4996 1.0230 0.9597 0.0768  -0.0997 0.1662  457 HIS B N   
2534 C CA  . HIS B 157 ? 1.4731 0.9980 0.9026 0.0474  -0.0592 0.1586  457 HIS B CA  
2535 C C   . HIS B 157 ? 1.4222 1.0021 0.8740 0.0428  -0.0617 0.1247  457 HIS B C   
2536 O O   . HIS B 157 ? 1.3725 0.9856 0.8836 0.0335  -0.0402 0.1015  457 HIS B O   
2537 C CB  . HIS B 157 ? 1.4132 0.9308 0.8859 0.0304  -0.0198 0.1575  457 HIS B CB  
2538 C CG  . HIS B 157 ? 1.4525 0.9199 0.9283 0.0355  -0.0204 0.1828  457 HIS B CG  
2539 N ND1 . HIS B 157 ? 1.3983 0.8714 0.9375 0.0557  -0.0383 0.1780  457 HIS B ND1 
2540 C CD2 . HIS B 157 ? 1.5247 0.9331 0.9496 0.0204  -0.0016 0.2107  457 HIS B CD2 
2541 C CE1 . HIS B 157 ? 1.4370 0.8537 0.9642 0.0550  -0.0331 0.2002  457 HIS B CE1 
2542 N NE2 . HIS B 157 ? 1.5385 0.9134 0.9971 0.0320  -0.0109 0.2217  457 HIS B NE2 
2543 N N   . VAL B 158 ? 1.5303 1.1136 0.9287 0.0493  -0.0902 0.1230  458 VAL B N   
2544 C CA  . VAL B 158 ? 1.5087 1.1382 0.9242 0.0464  -0.1024 0.0901  458 VAL B CA  
2545 C C   . VAL B 158 ? 1.5073 1.1371 0.8860 0.0235  -0.0657 0.0733  458 VAL B C   
2546 O O   . VAL B 158 ? 1.4341 1.0956 0.8343 0.0174  -0.0659 0.0422  458 VAL B O   
2547 C CB  . VAL B 158 ? 1.5564 1.1916 0.9309 0.0631  -0.1524 0.0916  458 VAL B CB  
2548 C CG1 . VAL B 158 ? 1.4843 1.1704 0.8912 0.0579  -0.1691 0.0538  458 VAL B CG1 
2549 C CG2 . VAL B 158 ? 1.5656 1.1954 0.9696 0.0910  -0.1894 0.1112  458 VAL B CG2 
2550 N N   . LYS B 159 ? 1.5747 1.1688 0.9024 0.0102  -0.0323 0.0922  459 LYS B N   
2551 C CA  . LYS B 159 ? 1.5766 1.1770 0.8806 -0.0100 0.0086  0.0741  459 LYS B CA  
2552 C C   . LYS B 159 ? 1.4691 1.0997 0.8594 -0.0164 0.0375  0.0522  459 LYS B C   
2553 O O   . LYS B 159 ? 1.4462 1.0912 0.8340 -0.0275 0.0664  0.0296  459 LYS B O   
2554 C CB  . LYS B 159 ? 1.6626 1.2206 0.8904 -0.0251 0.0386  0.1014  459 LYS B CB  
2555 C CG  . LYS B 159 ? 1.8311 1.3515 0.9515 -0.0209 0.0142  0.1241  459 LYS B CG  
2556 C CD  . LYS B 159 ? 1.9648 1.4501 0.9944 -0.0440 0.0557  0.1409  459 LYS B CD  
2557 C CE  . LYS B 159 ? 2.1345 1.5884 1.0444 -0.0406 0.0323  0.1545  459 LYS B CE  
2558 N NZ  . LYS B 159 ? 2.2352 1.6637 1.0513 -0.0661 0.0785  0.1628  459 LYS B NZ  
2559 N N   . HIS B 160 ? 1.3702 1.0092 0.8325 -0.0078 0.0293  0.0578  460 HIS B N   
2560 C CA  . HIS B 160 ? 1.2692 0.9305 0.8034 -0.0127 0.0539  0.0423  460 HIS B CA  
2561 C C   . HIS B 160 ? 1.2360 0.9279 0.8298 -0.0038 0.0352  0.0201  460 HIS B C   
2562 O O   . HIS B 160 ? 1.1482 0.8464 0.7698 0.0077  0.0086  0.0267  460 HIS B O   
2563 C CB  . HIS B 160 ? 1.2501 0.8953 0.8167 -0.0132 0.0632  0.0627  460 HIS B CB  
2564 C CG  . HIS B 160 ? 1.1673 0.8334 0.7947 -0.0203 0.0894  0.0479  460 HIS B CG  
2565 N ND1 . HIS B 160 ? 1.1451 0.8140 0.7669 -0.0365 0.1248  0.0436  460 HIS B ND1 
2566 C CD2 . HIS B 160 ? 1.0728 0.7598 0.7658 -0.0131 0.0846  0.0360  460 HIS B CD2 
2567 C CE1 . HIS B 160 ? 1.0631 0.7564 0.7490 -0.0364 0.1362  0.0285  460 HIS B CE1 
2568 N NE2 . HIS B 160 ? 1.0447 0.7450 0.7687 -0.0223 0.1116  0.0254  460 HIS B NE2 
2569 N N   . GLN B 161 ? 1.2220 0.9309 0.8341 -0.0095 0.0514  -0.0062 461 GLN B N   
2570 C CA  . GLN B 161 ? 1.0775 0.8059 0.7411 -0.0059 0.0406  -0.0263 461 GLN B CA  
2571 C C   . GLN B 161 ? 0.9434 0.6782 0.6660 -0.0025 0.0501  -0.0210 461 GLN B C   
2572 O O   . GLN B 161 ? 0.9290 0.6628 0.6627 -0.0057 0.0740  -0.0212 461 GLN B O   
2573 C CB  . GLN B 161 ? 1.0776 0.8106 0.7448 -0.0105 0.0559  -0.0546 461 GLN B CB  
2574 C CG  . GLN B 161 ? 1.1643 0.8968 0.7978 -0.0138 0.0386  -0.0744 461 GLN B CG  
2575 C CD  . GLN B 161 ? 1.2060 0.9352 0.8487 -0.0161 0.0537  -0.1046 461 GLN B CD  
2576 O OE1 . GLN B 161 ? 1.3096 1.0379 0.9553 -0.0142 0.0816  -0.1123 461 GLN B OE1 
2577 N NE2 . GLN B 161 ? 1.2131 0.9409 0.8653 -0.0200 0.0351  -0.1238 461 GLN B NE2 
2578 N N   . LEU B 162 ? 0.8449 0.5906 0.6055 0.0031  0.0317  -0.0197 462 LEU B N   
2579 C CA  . LEU B 162 ? 0.8058 0.5564 0.6132 0.0069  0.0382  -0.0149 462 LEU B CA  
2580 C C   . LEU B 162 ? 0.7706 0.5356 0.6138 0.0070  0.0274  -0.0253 462 LEU B C   
2581 O O   . LEU B 162 ? 0.7587 0.5359 0.6033 0.0066  0.0086  -0.0285 462 LEU B O   
2582 C CB  . LEU B 162 ? 0.8592 0.6018 0.6689 0.0137  0.0317  0.0055  462 LEU B CB  
2583 C CG  . LEU B 162 ? 0.8106 0.5531 0.6580 0.0162  0.0420  0.0088  462 LEU B CG  
2584 C CD1 . LEU B 162 ? 0.7656 0.5046 0.6162 0.0088  0.0649  0.0048  462 LEU B CD1 
2585 C CD2 . LEU B 162 ? 0.8727 0.6010 0.7184 0.0243  0.0319  0.0256  462 LEU B CD2 
2586 N N   . THR B 163 ? 0.7640 0.5282 0.6356 0.0069  0.0391  -0.0299 463 THR B N   
2587 C CA  . THR B 163 ? 0.7752 0.5474 0.6770 0.0048  0.0341  -0.0336 463 THR B CA  
2588 C C   . THR B 163 ? 0.7244 0.5014 0.6484 0.0116  0.0375  -0.0230 463 THR B C   
2589 O O   . THR B 163 ? 0.6726 0.4414 0.5988 0.0152  0.0477  -0.0201 463 THR B O   
2590 C CB  . THR B 163 ? 0.7563 0.5142 0.6625 0.0000  0.0419  -0.0453 463 THR B CB  
2591 O OG1 . THR B 163 ? 0.7570 0.5049 0.6399 -0.0036 0.0424  -0.0591 463 THR B OG1 
2592 C CG2 . THR B 163 ? 0.7440 0.5047 0.6708 -0.0088 0.0379  -0.0473 463 THR B CG2 
2593 N N   . VAL B 164 ? 0.7188 0.5129 0.6623 0.0134  0.0285  -0.0207 464 VAL B N   
2594 C CA  . VAL B 164 ? 0.7243 0.5239 0.6878 0.0211  0.0319  -0.0152 464 VAL B CA  
2595 C C   . VAL B 164 ? 0.7233 0.5366 0.7087 0.0148  0.0373  -0.0211 464 VAL B C   
2596 O O   . VAL B 164 ? 0.7096 0.5432 0.7110 0.0079  0.0320  -0.0272 464 VAL B O   
2597 C CB  . VAL B 164 ? 0.7313 0.5382 0.6993 0.0325  0.0193  -0.0086 464 VAL B CB  
2598 C CG1 . VAL B 164 ? 0.7427 0.5552 0.7347 0.0422  0.0231  -0.0084 464 VAL B CG1 
2599 C CG2 . VAL B 164 ? 0.7817 0.5652 0.7173 0.0352  0.0169  0.0021  464 VAL B CG2 
2600 N N   . LYS B 165 ? 0.7019 0.5048 0.6867 0.0157  0.0481  -0.0195 465 LYS B N   
2601 C CA  . LYS B 165 ? 0.7153 0.5259 0.7100 0.0091  0.0569  -0.0216 465 LYS B CA  
2602 C C   . LYS B 165 ? 0.6945 0.5169 0.7006 0.0193  0.0610  -0.0224 465 LYS B C   
2603 O O   . LYS B 165 ? 0.7224 0.5314 0.7205 0.0286  0.0593  -0.0203 465 LYS B O   
2604 C CB  . LYS B 165 ? 0.7906 0.5736 0.7646 0.0042  0.0633  -0.0188 465 LYS B CB  
2605 C CG  . LYS B 165 ? 0.9106 0.6774 0.8758 -0.0050 0.0604  -0.0219 465 LYS B CG  
2606 C CD  . LYS B 165 ? 0.9352 0.6677 0.8819 -0.0089 0.0642  -0.0191 465 LYS B CD  
2607 C CE  . LYS B 165 ? 0.9855 0.7019 0.9271 -0.0141 0.0596  -0.0273 465 LYS B CE  
2608 N NZ  . LYS B 165 ? 1.0841 0.7593 1.0094 -0.0174 0.0612  -0.0259 465 LYS B NZ  
2609 N N   . PHE B 166 ? 0.6565 0.5057 0.6845 0.0164  0.0672  -0.0282 466 PHE B N   
2610 C CA  . PHE B 166 ? 0.6508 0.5095 0.6849 0.0240  0.0773  -0.0333 466 PHE B CA  
2611 C C   . PHE B 166 ? 0.6778 0.5282 0.6914 0.0103  0.0938  -0.0314 466 PHE B C   
2612 O O   . PHE B 166 ? 0.6455 0.5136 0.6704 -0.0049 0.1054  -0.0335 466 PHE B O   
2613 C CB  . PHE B 166 ? 0.6257 0.5232 0.6987 0.0322  0.0774  -0.0438 466 PHE B CB  
2614 C CG  . PHE B 166 ? 0.5886 0.4897 0.6773 0.0484  0.0569  -0.0426 466 PHE B CG  
2615 C CD1 . PHE B 166 ? 0.5762 0.4431 0.6424 0.0579  0.0472  -0.0338 466 PHE B CD1 
2616 C CD2 . PHE B 166 ? 0.5876 0.5260 0.7127 0.0532  0.0466  -0.0497 466 PHE B CD2 
2617 C CE1 . PHE B 166 ? 0.5817 0.4422 0.6506 0.0709  0.0294  -0.0279 466 PHE B CE1 
2618 C CE2 . PHE B 166 ? 0.5935 0.5290 0.7239 0.0708  0.0235  -0.0455 466 PHE B CE2 
2619 C CZ  . PHE B 166 ? 0.5939 0.4855 0.6907 0.0791  0.0157  -0.0325 466 PHE B CZ  
2620 N N   . VAL B 167 ? 0.7130 0.5371 0.6963 0.0153  0.0943  -0.0276 467 VAL B N   
2621 C CA  . VAL B 167 ? 0.7642 0.5709 0.7142 0.0065  0.1057  -0.0225 467 VAL B CA  
2622 C C   . VAL B 167 ? 0.7872 0.6128 0.7339 0.0080  0.1221  -0.0316 467 VAL B C   
2623 O O   . VAL B 167 ? 0.7926 0.6179 0.7351 0.0220  0.1184  -0.0405 467 VAL B O   
2624 C CB  . VAL B 167 ? 0.7987 0.5741 0.7215 0.0159  0.0920  -0.0171 467 VAL B CB  
2625 C CG1 . VAL B 167 ? 0.8374 0.5853 0.7160 0.0118  0.0955  -0.0082 467 VAL B CG1 
2626 C CG2 . VAL B 167 ? 0.8081 0.5724 0.7404 0.0171  0.0796  -0.0134 467 VAL B CG2 
2627 N N   . ILE B 168 ? 0.7700 0.6117 0.7183 -0.0087 0.1425  -0.0316 468 ILE B N   
2628 C CA  . ILE B 168 ? 0.7933 0.6570 0.7356 -0.0110 0.1654  -0.0418 468 ILE B CA  
2629 C C   . ILE B 168 ? 0.8792 0.7074 0.7573 -0.0221 0.1766  -0.0292 468 ILE B C   
2630 O O   . ILE B 168 ? 0.9285 0.7280 0.7828 -0.0383 0.1781  -0.0124 468 ILE B O   
2631 C CB  . ILE B 168 ? 0.7404 0.6518 0.7287 -0.0252 0.1851  -0.0514 468 ILE B CB  
2632 C CG1 . ILE B 168 ? 0.6743 0.6160 0.7207 -0.0153 0.1668  -0.0593 468 ILE B CG1 
2633 C CG2 . ILE B 168 ? 0.7677 0.7115 0.7590 -0.0231 0.2116  -0.0680 468 ILE B CG2 
2634 C CD1 . ILE B 168 ? 0.6771 0.6225 0.7404 0.0135  0.1502  -0.0692 468 ILE B CD1 
2635 N N   . PHE B 169 ? 0.9237 0.7494 0.7688 -0.0135 0.1838  -0.0374 469 PHE B N   
2636 C CA  . PHE B 169 ? 0.9786 0.7657 0.7518 -0.0213 0.1890  -0.0233 469 PHE B CA  
2637 C C   . PHE B 169 ? 1.0420 0.8340 0.7996 -0.0493 0.2220  -0.0142 469 PHE B C   
2638 O O   . PHE B 169 ? 1.0480 0.8882 0.8480 -0.0576 0.2464  -0.0297 469 PHE B O   
2639 C CB  . PHE B 169 ? 1.0570 0.8416 0.7943 -0.0059 0.1866  -0.0376 469 PHE B CB  
2640 C CG  . PHE B 169 ? 1.1926 0.9326 0.8471 -0.0077 0.1803  -0.0225 469 PHE B CG  
2641 C CD1 . PHE B 169 ? 1.2346 0.9381 0.8687 0.0032  0.1475  -0.0090 469 PHE B CD1 
2642 C CD2 . PHE B 169 ? 1.2869 1.0225 0.8820 -0.0186 0.2064  -0.0225 469 PHE B CD2 
2643 C CE1 . PHE B 169 ? 1.2975 0.9597 0.8557 0.0061  0.1355  0.0055  469 PHE B CE1 
2644 C CE2 . PHE B 169 ? 1.3519 1.0409 0.8609 -0.0187 0.1967  -0.0055 469 PHE B CE2 
2645 C CZ  . PHE B 169 ? 1.3497 1.0012 0.8410 -0.0047 0.1584  0.0090  469 PHE B CZ  
2646 N N   . PRO B 170 ? 1.0903 0.8325 0.7909 -0.0649 0.2239  0.0109  470 PRO B N   
2647 C CA  . PRO B 170 ? 1.1572 0.8941 0.8367 -0.0977 0.2582  0.0231  470 PRO B CA  
2648 C C   . PRO B 170 ? 1.2021 0.9777 0.8710 -0.1104 0.2981  0.0092  470 PRO B C   
2649 O O   . PRO B 170 ? 1.1714 0.9866 0.8827 -0.1345 0.3282  0.0024  470 PRO B O   
2650 C CB  . PRO B 170 ? 1.2306 0.8907 0.8287 -0.1016 0.2457  0.0535  470 PRO B CB  
2651 C CG  . PRO B 170 ? 1.1644 0.8042 0.7824 -0.0755 0.2036  0.0546  470 PRO B CG  
2652 C CD  . PRO B 170 ? 1.1038 0.7907 0.7608 -0.0518 0.1926  0.0287  470 PRO B CD  
2653 N N   . THR B 171 ? 1.2385 1.0077 0.8547 -0.0951 0.2993  0.0016  471 THR B N   
2654 C CA  . THR B 171 ? 1.2942 1.0978 0.8912 -0.1070 0.3411  -0.0139 471 THR B CA  
2655 C C   . THR B 171 ? 1.2507 1.1310 0.9387 -0.0953 0.3534  -0.0495 471 THR B C   
2656 O O   . THR B 171 ? 1.3263 1.2515 1.0284 -0.1102 0.3943  -0.0651 471 THR B O   
2657 C CB  . THR B 171 ? 1.3389 1.1112 0.8449 -0.0945 0.3386  -0.0147 471 THR B CB  
2658 O OG1 . THR B 171 ? 1.2993 1.0776 0.8302 -0.0609 0.3022  -0.0339 471 THR B OG1 
2659 C CG2 . THR B 171 ? 1.3997 1.0957 0.8063 -0.1050 0.3280  0.0221  471 THR B CG2 
2660 N N   . ASP B 172 ? 1.1846 1.0785 0.9321 -0.0686 0.3193  -0.0618 472 ASP B N   
2661 C CA  . ASP B 172 ? 1.1199 1.0759 0.9515 -0.0519 0.3229  -0.0921 472 ASP B CA  
2662 C C   . ASP B 172 ? 1.0588 1.0604 0.9647 -0.0701 0.3349  -0.0931 472 ASP B C   
2663 O O   . ASP B 172 ? 0.9932 1.0042 0.9532 -0.0596 0.3076  -0.0931 472 ASP B O   
2664 C CB  . ASP B 172 ? 1.1117 1.0567 0.9750 -0.0210 0.2820  -0.0990 472 ASP B CB  
2665 C CG  . ASP B 172 ? 1.1193 1.0289 0.9325 -0.0007 0.2634  -0.1058 472 ASP B CG  
2666 O OD1 . ASP B 172 ? 1.1798 1.0729 0.9257 -0.0070 0.2793  -0.1066 472 ASP B OD1 
2667 O OD2 . ASP B 172 ? 1.0394 0.9377 0.8795 0.0192  0.2329  -0.1102 472 ASP B OD2 
2668 N N   . LEU B 173 ? 1.0868 1.1201 0.9954 -0.0990 0.3768  -0.0959 473 LEU B N   
2669 C CA  . LEU B 173 ? 1.0851 1.1655 1.0662 -0.1224 0.3893  -0.0990 473 LEU B CA  
2670 C C   . LEU B 173 ? 1.0330 1.1869 1.1126 -0.0969 0.3806  -0.1311 473 LEU B C   
2671 O O   . LEU B 173 ? 0.9561 1.1413 1.1023 -0.1011 0.3650  -0.1337 473 LEU B O   
2672 C CB  . LEU B 173 ? 1.1969 1.2952 1.1583 -0.1642 0.4410  -0.0953 473 LEU B CB  
2673 C CG  . LEU B 173 ? 1.2824 1.3053 1.1611 -0.1983 0.4485  -0.0576 473 LEU B CG  
2674 C CD1 . LEU B 173 ? 1.3073 1.2507 1.0908 -0.1771 0.4209  -0.0363 473 LEU B CD1 
2675 C CD2 . LEU B 173 ? 1.3529 1.3906 1.2017 -0.2408 0.5065  -0.0539 473 LEU B CD2 
2676 N N   . GLU B 174 ? 1.0875 1.2673 1.1751 -0.0693 0.3892  -0.1567 474 GLU B N   
2677 C CA  . GLU B 174 ? 1.0445 1.2933 1.2257 -0.0423 0.3841  -0.1886 474 GLU B CA  
2678 C C   . GLU B 174 ? 0.9598 1.1863 1.1705 -0.0123 0.3322  -0.1829 474 GLU B C   
2679 O O   . GLU B 174 ? 0.8732 1.1454 1.1603 -0.0027 0.3158  -0.1929 474 GLU B O   
2680 C CB  . GLU B 174 ? 1.0934 1.3696 1.2708 -0.0217 0.4112  -0.2197 474 GLU B CB  
2681 C CG  . GLU B 174 ? 1.1470 1.4729 1.3222 -0.0524 0.4697  -0.2329 474 GLU B CG  
2682 C CD  . GLU B 174 ? 1.1261 1.5468 1.4103 -0.0636 0.4904  -0.2553 474 GLU B CD  
2683 O OE1 . GLU B 174 ? 1.1036 1.5828 1.4657 -0.0295 0.4859  -0.2892 474 GLU B OE1 
2684 O OE2 . GLU B 174 ? 1.1152 1.5526 1.4122 -0.1051 0.5088  -0.2410 474 GLU B OE2 
2685 N N   . ILE B 175 ? 0.9602 1.1178 1.1084 0.0010  0.3067  -0.1668 475 ILE B N   
2686 C CA  . ILE B 175 ? 0.9062 1.0333 1.0680 0.0236  0.2626  -0.1572 475 ILE B CA  
2687 C C   . ILE B 175 ? 0.8632 0.9947 1.0498 0.0050  0.2465  -0.1397 475 ILE B C   
2688 O O   . ILE B 175 ? 0.8345 0.9818 1.0679 0.0210  0.2191  -0.1422 475 ILE B O   
2689 C CB  . ILE B 175 ? 0.9003 0.9580 0.9905 0.0320  0.2450  -0.1437 475 ILE B CB  
2690 C CG1 . ILE B 175 ? 0.9081 0.9632 0.9810 0.0531  0.2554  -0.1676 475 ILE B CG1 
2691 C CG2 . ILE B 175 ? 0.8586 0.8825 0.9564 0.0458  0.2056  -0.1293 475 ILE B CG2 
2692 C CD1 . ILE B 175 ? 0.9419 0.9431 0.9335 0.0489  0.2523  -0.1592 475 ILE B CD1 
2693 N N   . TYR B 176 ? 0.9066 1.0204 1.0572 -0.0290 0.2635  -0.1226 476 TYR B N   
2694 C CA  . TYR B 176 ? 0.8818 0.9961 1.0521 -0.0517 0.2530  -0.1098 476 TYR B CA  
2695 C C   . TYR B 176 ? 0.8282 1.0200 1.0869 -0.0553 0.2564  -0.1310 476 TYR B C   
2696 O O   . TYR B 176 ? 0.7345 0.9377 1.0296 -0.0520 0.2280  -0.1304 476 TYR B O   
2697 C CB  . TYR B 176 ? 0.9433 1.0181 1.0557 -0.0876 0.2761  -0.0895 476 TYR B CB  
2698 C CG  . TYR B 176 ? 0.9624 1.0286 1.0921 -0.1132 0.2662  -0.0787 476 TYR B CG  
2699 C CD1 . TYR B 176 ? 0.9601 0.9760 1.0645 -0.1049 0.2337  -0.0635 476 TYR B CD1 
2700 C CD2 . TYR B 176 ? 0.9880 1.1010 1.1658 -0.1451 0.2889  -0.0880 476 TYR B CD2 
2701 C CE1 . TYR B 176 ? 0.9897 0.9953 1.1082 -0.1259 0.2234  -0.0583 476 TYR B CE1 
2702 C CE2 . TYR B 176 ? 1.0281 1.1305 1.2230 -0.1694 0.2772  -0.0822 476 TYR B CE2 
2703 C CZ  . TYR B 176 ? 1.0381 1.0840 1.2003 -0.1584 0.2436  -0.0677 476 TYR B CZ  
2704 O OH  . TYR B 176 ? 1.0948 1.1252 1.2690 -0.1792 0.2300  -0.0656 476 TYR B OH  
2705 N N   . LYS B 177 ? 0.8788 1.1280 1.1724 -0.0622 0.2916  -0.1518 477 LYS B N   
2706 C CA  . LYS B 177 ? 0.8658 1.2010 1.2533 -0.0673 0.2984  -0.1762 477 LYS B CA  
2707 C C   . LYS B 177 ? 0.8082 1.1696 1.2511 -0.0241 0.2580  -0.1900 477 LYS B C   
2708 O O   . LYS B 177 ? 0.7923 1.2076 1.3054 -0.0232 0.2401  -0.2022 477 LYS B O   
2709 C CB  . LYS B 177 ? 0.9031 1.3000 1.3199 -0.0808 0.3485  -0.1992 477 LYS B CB  
2710 C CG  . LYS B 177 ? 0.9668 1.3569 1.3494 -0.1335 0.3928  -0.1871 477 LYS B CG  
2711 C CD  . LYS B 177 ? 1.0050 1.4792 1.4418 -0.1542 0.4454  -0.2144 477 LYS B CD  
2712 C CE  . LYS B 177 ? 1.0614 1.5268 1.4716 -0.2139 0.4872  -0.1988 477 LYS B CE  
2713 N NZ  . LYS B 177 ? 1.0851 1.6361 1.5511 -0.2425 0.5436  -0.2245 477 LYS B NZ  
2714 N N   . ALA B 178 ? 0.7812 1.1002 1.1897 0.0107  0.2416  -0.1874 478 ALA B N   
2715 C CA  . ALA B 178 ? 0.7629 1.0949 1.2150 0.0527  0.2059  -0.1979 478 ALA B CA  
2716 C C   . ALA B 178 ? 0.7299 1.0211 1.1630 0.0555  0.1638  -0.1755 478 ALA B C   
2717 O O   . ALA B 178 ? 0.7327 1.0543 1.2147 0.0740  0.1332  -0.1817 478 ALA B O   
2718 C CB  . ALA B 178 ? 0.7814 1.0787 1.2042 0.0842  0.2076  -0.2051 478 ALA B CB  
2719 N N   . PHE B 179 ? 0.7349 0.9585 1.0954 0.0382  0.1618  -0.1507 479 PHE B N   
2720 C CA  . PHE B 179 ? 0.7326 0.9167 1.0690 0.0394  0.1278  -0.1317 479 PHE B CA  
2721 C C   . PHE B 179 ? 0.7521 0.9743 1.1258 0.0165  0.1193  -0.1349 479 PHE B C   
2722 O O   . PHE B 179 ? 0.7346 0.9598 1.1220 0.0284  0.0857  -0.1326 479 PHE B O   
2723 C CB  . PHE B 179 ? 0.7368 0.8488 0.9963 0.0279  0.1312  -0.1097 479 PHE B CB  
2724 C CG  . PHE B 179 ? 0.7469 0.8172 0.9753 0.0543  0.1224  -0.1063 479 PHE B CG  
2725 C CD1 . PHE B 179 ? 0.7764 0.8606 1.0163 0.0713  0.1377  -0.1233 479 PHE B CD1 
2726 C CD2 . PHE B 179 ? 0.6939 0.7134 0.8856 0.0609  0.0997  -0.0892 479 PHE B CD2 
2727 C CE1 . PHE B 179 ? 0.7817 0.8240 0.9951 0.0924  0.1283  -0.1230 479 PHE B CE1 
2728 C CE2 . PHE B 179 ? 0.7051 0.6879 0.8742 0.0797  0.0929  -0.0875 479 PHE B CE2 
2729 C CZ  . PHE B 179 ? 0.7491 0.7404 0.9283 0.0947  0.1059  -0.1043 479 PHE B CZ  
2730 N N   . SER B 180 ? 0.7826 1.0308 1.1687 -0.0183 0.1495  -0.1402 480 SER B N   
2731 C CA  . SER B 180 ? 0.8033 1.0926 1.2342 -0.0442 0.1434  -0.1485 480 SER B CA  
2732 C C   . SER B 180 ? 0.7594 1.1244 1.2729 -0.0206 0.1201  -0.1718 480 SER B C   
2733 O O   . SER B 180 ? 0.8064 1.1828 1.3383 -0.0171 0.0853  -0.1734 480 SER B O   
2734 C CB  . SER B 180 ? 0.8457 1.1519 1.2825 -0.0869 0.1841  -0.1517 480 SER B CB  
2735 O OG  . SER B 180 ? 0.9452 1.3024 1.4166 -0.0824 0.2165  -0.1690 480 SER B OG  
2736 N N   . SER B 181 ? 0.7304 1.1449 1.2902 -0.0010 0.1371  -0.1909 481 SER B N   
2737 C CA  . SER B 181 ? 0.7469 1.2413 1.3957 0.0253  0.1169  -0.2167 481 SER B CA  
2738 C C   . SER B 181 ? 0.7165 1.1805 1.3526 0.0674  0.0656  -0.2070 481 SER B C   
2739 O O   . SER B 181 ? 0.7333 1.2440 1.4220 0.0817  0.0307  -0.2182 481 SER B O   
2740 C CB  . SER B 181 ? 0.7913 1.3384 1.4876 0.0413  0.1491  -0.2409 481 SER B CB  
2741 O OG  . SER B 181 ? 0.8341 1.4800 1.6360 0.0553  0.1390  -0.2721 481 SER B OG  
2742 N N   . GLU B 182 ? 0.6974 1.0834 1.2629 0.0862  0.0608  -0.1863 482 GLU B N   
2743 C CA  . GLU B 182 ? 0.7327 1.0789 1.2760 0.1221  0.0179  -0.1731 482 GLU B CA  
2744 C C   . GLU B 182 ? 0.7969 1.1205 1.3080 0.1051  -0.0106 -0.1575 482 GLU B C   
2745 O O   . GLU B 182 ? 0.8456 1.1785 1.3691 0.1275  -0.0511 -0.1563 482 GLU B O   
2746 C CB  . GLU B 182 ? 0.7157 0.9886 1.1987 0.1398  0.0258  -0.1582 482 GLU B CB  
2747 C CG  . GLU B 182 ? 0.7383 0.9556 1.1869 0.1706  -0.0128 -0.1397 482 GLU B CG  
2748 C CD  . GLU B 182 ? 0.7696 1.0155 1.2696 0.2136  -0.0471 -0.1498 482 GLU B CD  
2749 O OE1 . GLU B 182 ? 0.7569 1.0643 1.3283 0.2328  -0.0396 -0.1767 482 GLU B OE1 
2750 O OE2 . GLU B 182 ? 0.7828 0.9862 1.2475 0.2292  -0.0831 -0.1296 482 GLU B OE2 
2751 N N   . MET B 183 ? 0.7859 1.0792 1.2539 0.0669  0.0097  -0.1471 483 MET B N   
2752 C CA  . MET B 183 ? 0.7586 1.0281 1.1940 0.0495  -0.0129 -0.1370 483 MET B CA  
2753 C C   . MET B 183 ? 0.7534 1.0967 1.2564 0.0401  -0.0330 -0.1588 483 MET B C   
2754 O O   . MET B 183 ? 0.7770 1.1236 1.2762 0.0540  -0.0731 -0.1580 483 MET B O   
2755 C CB  . MET B 183 ? 0.7524 0.9728 1.1340 0.0141  0.0134  -0.1245 483 MET B CB  
2756 C CG  . MET B 183 ? 0.7711 0.9574 1.1120 0.0010  -0.0091 -0.1163 483 MET B CG  
2757 S SD  . MET B 183 ? 0.7457 0.8745 1.0333 -0.0355 0.0193  -0.1053 483 MET B SD  
2758 C CE  . MET B 183 ? 0.8221 0.8790 1.0387 -0.0125 0.0188  -0.0821 483 MET B CE  
2759 N N   . ALA B 184 ? 0.7653 1.1691 1.3289 0.0153  -0.0050 -0.1790 484 ALA B N   
2760 C CA  . ALA B 184 ? 0.8228 1.3128 1.4700 0.0054  -0.0211 -0.2058 484 ALA B CA  
2761 C C   . ALA B 184 ? 0.8485 1.3746 1.5332 0.0519  -0.0688 -0.2138 484 ALA B C   
2762 O O   . ALA B 184 ? 0.8959 1.4309 1.5794 0.0552  -0.1103 -0.2161 484 ALA B O   
2763 C CB  . ALA B 184 ? 0.8128 1.3711 1.5300 -0.0180 0.0218  -0.2277 484 ALA B CB  
2764 N N   . LYS B 185 ? 0.8550 1.3948 1.5661 0.0892  -0.0643 -0.2177 485 LYS B N   
2765 C CA  . LYS B 185 ? 0.9019 1.4672 1.6481 0.1392  -0.1093 -0.2235 485 LYS B CA  
2766 C C   . LYS B 185 ? 0.9336 1.4338 1.6054 0.1549  -0.1553 -0.1983 485 LYS B C   
2767 O O   . LYS B 185 ? 1.0173 1.5518 1.7162 0.1769  -0.2027 -0.2053 485 LYS B O   
2768 C CB  . LYS B 185 ? 0.9747 1.5212 1.7248 0.1775  -0.0952 -0.2227 485 LYS B CB  
2769 C CG  . LYS B 185 ? 1.0271 1.6545 1.8656 0.1815  -0.0614 -0.2549 485 LYS B CG  
2770 C CD  . LYS B 185 ? 1.0796 1.6683 1.9014 0.2169  -0.0450 -0.2537 485 LYS B CD  
2771 C CE  . LYS B 185 ? 1.1484 1.8202 2.0591 0.2295  -0.0141 -0.2901 485 LYS B CE  
2772 N NZ  . LYS B 185 ? 1.1927 1.9067 2.1182 0.1779  0.0401  -0.3023 485 LYS B NZ  
2773 N N   . ARG B 186 ? 0.9010 1.3102 1.4790 0.1441  -0.1414 -0.1700 486 ARG B N   
2774 C CA  . ARG B 186 ? 0.9685 1.3101 1.4688 0.1601  -0.1761 -0.1443 486 ARG B CA  
2775 C C   . ARG B 186 ? 0.9869 1.3405 1.4696 0.1370  -0.2020 -0.1482 486 ARG B C   
2776 O O   . ARG B 186 ? 1.0666 1.4107 1.5228 0.1587  -0.2466 -0.1409 486 ARG B O   
2777 C CB  . ARG B 186 ? 0.9700 1.2220 1.3857 0.1508  -0.1493 -0.1177 486 ARG B CB  
2778 C CG  . ARG B 186 ? 1.0214 1.2437 1.4367 0.1795  -0.1361 -0.1110 486 ARG B CG  
2779 C CD  . ARG B 186 ? 1.0908 1.3192 1.5311 0.2273  -0.1753 -0.1104 486 ARG B CD  
2780 N NE  . ARG B 186 ? 1.1486 1.3122 1.5553 0.2479  -0.1629 -0.0960 486 ARG B NE  
2781 C CZ  . ARG B 186 ? 1.2603 1.3471 1.6012 0.2640  -0.1822 -0.0685 486 ARG B CZ  
2782 N NH1 . ARG B 186 ? 1.3487 1.4197 1.6551 0.2740  -0.2214 -0.0529 486 ARG B NH1 
2783 N NH2 . ARG B 186 ? 1.2687 1.2944 1.5774 0.2690  -0.1626 -0.0576 486 ARG B NH2 
2784 N N   . SER B 187 ? 0.9495 1.3166 1.4395 0.0931  -0.1744 -0.1592 487 SER B N   
2785 C CA  . SER B 187 ? 0.9432 1.3200 1.4200 0.0671  -0.1955 -0.1687 487 SER B CA  
2786 C C   . SER B 187 ? 0.9279 1.3915 1.4819 0.0787  -0.2369 -0.1951 487 SER B C   
2787 O O   . SER B 187 ? 0.9831 1.4463 1.5100 0.0816  -0.2784 -0.1978 487 SER B O   
2788 C CB  . SER B 187 ? 0.9504 1.3183 1.4256 0.0194  -0.1561 -0.1757 487 SER B CB  
2789 O OG  . SER B 187 ? 0.9465 1.3578 1.4851 0.0080  -0.1189 -0.1872 487 SER B OG  
2790 N N   . LYS B 188 ? 0.8807 1.4217 1.5306 0.0871  -0.2272 -0.2165 488 LYS B N   
2791 C CA  . LYS B 188 ? 0.9137 1.5490 1.6518 0.1026  -0.2683 -0.2451 488 LYS B CA  
2792 C C   . LYS B 188 ? 0.9588 1.5706 1.6569 0.1516  -0.3286 -0.2305 488 LYS B C   
2793 O O   . LYS B 188 ? 1.0248 1.6869 1.7518 0.1595  -0.3776 -0.2472 488 LYS B O   
2794 C CB  . LYS B 188 ? 0.8894 1.6140 1.7401 0.1143  -0.2482 -0.2709 488 LYS B CB  
2795 C CG  . LYS B 188 ? 0.8838 1.7000 1.8299 0.0681  -0.2206 -0.3056 488 LYS B CG  
2796 C CD  . LYS B 188 ? 0.8726 1.6606 1.8019 0.0228  -0.1521 -0.3001 488 LYS B CD  
2797 C CE  . LYS B 188 ? 0.8894 1.5968 1.7320 -0.0186 -0.1391 -0.2818 488 LYS B CE  
2798 N NZ  . LYS B 188 ? 0.8687 1.5372 1.6845 -0.0527 -0.0782 -0.2707 488 LYS B NZ  
2799 N N   . MET B 189 ? 0.9551 1.4882 1.5845 0.1828  -0.3252 -0.1991 489 MET B N   
2800 C CA  . MET B 189 ? 1.0165 1.5109 1.5988 0.2303  -0.3756 -0.1783 489 MET B CA  
2801 C C   . MET B 189 ? 1.0732 1.5000 1.5474 0.2173  -0.3980 -0.1571 489 MET B C   
2802 O O   . MET B 189 ? 1.1833 1.6125 1.6313 0.2416  -0.4525 -0.1532 489 MET B O   
2803 C CB  . MET B 189 ? 1.0246 1.4521 1.5734 0.2612  -0.3561 -0.1532 489 MET B CB  
2804 C CG  . MET B 189 ? 0.9841 1.4700 1.6299 0.2904  -0.3454 -0.1741 489 MET B CG  
2805 S SD  . MET B 189 ? 1.0185 1.5587 1.7278 0.3535  -0.4159 -0.1855 489 MET B SD  
2806 C CE  . MET B 189 ? 1.1045 1.5404 1.6855 0.3804  -0.4705 -0.1415 489 MET B CE  
2807 N N   . LEU B 190 ? 1.0327 1.4000 1.4430 0.1810  -0.3559 -0.1442 490 LEU B N   
2808 C CA  . LEU B 190 ? 1.0722 1.3787 1.3832 0.1643  -0.3662 -0.1290 490 LEU B CA  
2809 C C   . LEU B 190 ? 1.0801 1.4401 1.4141 0.1373  -0.3906 -0.1584 490 LEU B C   
2810 O O   . LEU B 190 ? 1.1411 1.4639 1.3977 0.1288  -0.4107 -0.1532 490 LEU B O   
2811 C CB  . LEU B 190 ? 1.0869 1.3271 1.3432 0.1360  -0.3127 -0.1133 490 LEU B CB  
2812 C CG  . LEU B 190 ? 1.1125 1.2925 1.3362 0.1570  -0.2890 -0.0854 490 LEU B CG  
2813 C CD1 . LEU B 190 ? 1.0606 1.2245 1.2940 0.1294  -0.2342 -0.0867 490 LEU B CD1 
2814 C CD2 . LEU B 190 ? 1.1936 1.2940 1.3126 0.1679  -0.3024 -0.0546 490 LEU B CD2 
2815 N N   . SER B 191 ? 1.0509 1.4983 1.4906 0.1215  -0.3870 -0.1912 491 SER B N   
2816 C CA  . SER B 191 ? 1.0630 1.5679 1.5382 0.0933  -0.4124 -0.2237 491 SER B CA  
2817 C C   . SER B 191 ? 1.1546 1.6841 1.6132 0.1260  -0.4831 -0.2278 491 SER B C   
2818 O O   . SER B 191 ? 1.2186 1.7582 1.6513 0.1066  -0.5124 -0.2453 491 SER B O   
2819 C CB  . SER B 191 ? 0.9996 1.5955 1.5970 0.0668  -0.3900 -0.2572 491 SER B CB  
2820 O OG  . SER B 191 ? 1.0002 1.6857 1.6921 0.0988  -0.4254 -0.2766 491 SER B OG  
2821 N N   . LEU B 192 ? 1.2187 1.7511 1.6861 0.1771  -0.5121 -0.2114 492 LEU B N   
2822 C CA  . LEU B 192 ? 1.3250 1.8797 1.7787 0.2161  -0.5842 -0.2119 492 LEU B CA  
2823 C C   . LEU B 192 ? 1.4376 1.8861 1.7454 0.2328  -0.6005 -0.1719 492 LEU B C   
2824 O O   . LEU B 192 ? 1.5052 1.9512 1.7588 0.2461  -0.6550 -0.1719 492 LEU B O   
2825 C CB  . LEU B 192 ? 1.3072 1.9186 1.8503 0.2660  -0.6099 -0.2161 492 LEU B CB  
2826 C CG  . LEU B 192 ? 1.2375 1.9058 1.8926 0.2575  -0.5587 -0.2348 492 LEU B CG  
2827 C CD1 . LEU B 192 ? 1.2721 1.9374 1.9599 0.3155  -0.5716 -0.2218 492 LEU B CD1 
2828 C CD2 . LEU B 192 ? 1.1843 1.9743 1.9681 0.2296  -0.5579 -0.2827 492 LEU B CD2 
2829 N N   . ASN B 193 ? 1.4830 1.8473 1.7283 0.2301  -0.5527 -0.1395 493 ASN B N   
2830 C CA  . ASN B 193 ? 1.5839 1.8463 1.6968 0.2413  -0.5552 -0.0997 493 ASN B CA  
2831 C C   . ASN B 193 ? 1.6155 1.8370 1.6522 0.1968  -0.5258 -0.1028 493 ASN B C   
2832 O O   . ASN B 193 ? 1.5918 1.8259 1.5893 0.1866  -0.5592 -0.1179 493 ASN B O   
2833 C CB  . ASN B 193 ? 1.5860 1.7801 1.6743 0.2611  -0.5219 -0.0652 493 ASN B CB  
2834 C CG  . ASN B 193 ? 1.5787 1.8121 1.7584 0.2999  -0.5331 -0.0692 493 ASN B CG  
2835 O OD1 . ASN B 193 ? 1.6682 1.9420 1.8821 0.3374  -0.5884 -0.0756 493 ASN B OD1 
2836 N ND2 . ASN B 193 ? 1.5025 1.7235 1.7202 0.2946  -0.4835 -0.0668 493 ASN B ND2 
2837 N N   . ASN B 194 ? 1.7144 1.8908 1.7351 0.1719  -0.4651 -0.0924 494 ASN B N   
2838 C CA  . ASN B 194 ? 1.7111 1.8287 1.6453 0.1411  -0.4339 -0.0864 494 ASN B CA  
2839 C C   . ASN B 194 ? 1.7249 1.8387 1.6995 0.1086  -0.3744 -0.0956 494 ASN B C   
2840 O O   . ASN B 194 ? 1.8002 1.8891 1.7892 0.1152  -0.3410 -0.0778 494 ASN B O   
2841 C CB  . ASN B 194 ? 1.7150 1.7490 1.5384 0.1592  -0.4337 -0.0467 494 ASN B CB  
2842 C CG  . ASN B 194 ? 1.6067 1.5818 1.3840 0.1355  -0.3763 -0.0326 494 ASN B CG  
2843 O OD1 . ASN B 194 ? 1.5905 1.5279 1.3657 0.1462  -0.3511 -0.0080 494 ASN B OD1 
2844 N ND2 . ASN B 194 ? 1.5528 1.5212 1.2982 0.1047  -0.3567 -0.0507 494 ASN B ND2 
2845 N N   . TYR B 195 ? 1.6645 1.7972 1.6504 0.0738  -0.3642 -0.1237 495 TYR B N   
2846 C CA  . TYR B 195 ? 1.4821 1.6045 1.4953 0.0413  -0.3143 -0.1335 495 TYR B CA  
2847 C C   . TYR B 195 ? 1.3176 1.4973 1.4366 0.0351  -0.2985 -0.1465 495 TYR B C   
2848 O O   . TYR B 195 ? 1.3803 1.6183 1.5611 0.0535  -0.3269 -0.1551 495 TYR B O   
2849 C CB  . TYR B 195 ? 1.5065 1.5563 1.4527 0.0414  -0.2750 -0.1071 495 TYR B CB  
2850 C CG  . TYR B 195 ? 1.8151 1.8270 1.6979 0.0176  -0.2612 -0.1182 495 TYR B CG  
2851 C CD1 . TYR B 195 ? 1.8971 1.9101 1.8107 -0.0123 -0.2347 -0.1397 495 TYR B CD1 
2852 C CD2 . TYR B 195 ? 2.0281 2.0008 1.8178 0.0255  -0.2743 -0.1085 495 TYR B CD2 
2853 C CE1 . TYR B 195 ? 1.8711 1.8472 1.7312 -0.0301 -0.2229 -0.1536 495 TYR B CE1 
2854 C CE2 . TYR B 195 ? 2.0354 1.9775 1.7697 0.0058  -0.2593 -0.1238 495 TYR B CE2 
2855 C CZ  . TYR B 195 ? 1.9145 1.8587 1.6873 -0.0203 -0.2345 -0.1479 495 TYR B CZ  
2856 O OH  . TYR B 195 ? 1.8341 1.7454 1.5563 -0.0359 -0.2205 -0.1661 495 TYR B OH  
2857 N N   . SER B 196 ? 1.2112 1.3769 1.3511 0.0082  -0.2538 -0.1502 496 SER B N   
2858 C CA  . SER B 196 ? 1.1668 1.3767 1.3918 -0.0010 -0.2292 -0.1585 496 SER B CA  
2859 C C   . SER B 196 ? 1.0978 1.3916 1.4080 -0.0133 -0.2534 -0.1899 496 SER B C   
2860 O O   . SER B 196 ? 0.9575 1.2958 1.3425 -0.0229 -0.2293 -0.1987 496 SER B O   
2861 C CB  . SER B 196 ? 1.2006 1.4076 1.4396 0.0304  -0.2200 -0.1380 496 SER B CB  
2862 O OG  . SER B 196 ? 1.3339 1.4757 1.5206 0.0293  -0.1850 -0.1156 496 SER B OG  
# 
