data_9HHC
# 
_entry.id   9HHC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9HHC         pdb_00009hhc 10.2210/pdb9hhc/pdb 
WWPDB D_1292143302 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-16 ? 
3 'Structure model' 1 2 2025-06-11 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_first'              
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation_author.identifier_ORCID' 
5 3 'Structure model' '_citation.journal_volume'          
6 3 'Structure model' '_citation.page_first'              
7 3 'Structure model' '_citation.page_last'               
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HHC 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-21 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9HGF 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 Oliver.Einsle@BIOCHEMIE.uni-freiburg.de   Oliver Einsle   ? 'principal investigator/group leader' 0000-0001-8722-2893 
4 stefan.guenther@pharmazie.uni-freiburg.de Stefan Guenther ? 'principal investigator/group leader' 0000-0003-3744-189X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Amann, M.'    1 0000-0001-7594-3810 
'Huegle, M.'   2 0000-0002-2830-7130 
'Einsle, O.'   3 0000-0001-8722-2893 
'Guenther, S.' 4 0000-0003-3744-189X 
# 
_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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemmedchem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1860-7187 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            20 
_citation.language                  ? 
_citation.page_first                e202500024 
_citation.page_last                 e202500024 
_citation.title                     
'A Novel Inhibitor against the Bromodomain Protein 1 of the Malaria Pathogen Plasmodium Falciparum.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cmdc.202500024 
_citation.pdbx_database_id_PubMed   40099623 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Amann, M.'        1  0000-0001-7594-3810 
primary 'Warstat, R.'      2  ?                   
primary 'Rechten, K.K.'    3  ?                   
primary 'Theuer, P.'       4  ?                   
primary 'Schustereder, M.' 5  ?                   
primary 'Clavey, S.'       6  ?                   
primary 'Breit, B.'        7  0000-0002-2514-3898 
primary 'Einsle, O.'       8  0000-0001-8722-2893 
primary 'Hugle, M.'        9  0000-0002-2830-7130 
primary 'Petter, M.'       10 0000-0002-1837-2756 
primary 'Gunther, S.'      11 0000-0003-3744-189X 
# 
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 'Bromodomain protein 1'                                                         15827.206 1   ? ? ? ? 
2 non-polymer syn '(R,R)-2,3-BUTANEDIOL'                                                          90.121    1   ? ? ? ? 
3 non-polymer syn '1-(3-aminophenyl)-3-methyl-5,6,7,8-tetrahydro-2~{H}-cyclohepta[c]pyrrol-4-one' 254.327   1   ? ? ? ? 
4 water       nat water                                                                           18.015    124 ? ? ? ? 
# 
_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       
;GPLGSPEFMNKQWYLLANQLILSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCIKTKLKKGQYAYPSEFVKDVQ
LIFDNCSLYNTSNSVVAITGKNIETYFNNQLIVMGYNNFILKEKKINDMLKLVEEEN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPLGSPEFMNKQWYLLANQLILSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCIKTKLKKGQYAYPSEFVKDVQ
LIFDNCSLYNTSNSVVAITGKNIETYFNNQLIVMGYNNFILKEKKINDMLKLVEEEN
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(R,R)-2,3-BUTANEDIOL'                                                          BU3 
3 '1-(3-aminophenyl)-3-methyl-5,6,7,8-tetrahydro-2~{H}-cyclohepta[c]pyrrol-4-one' I5K 
4 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   PRO n 
1 3   LEU n 
1 4   GLY n 
1 5   SER n 
1 6   PRO n 
1 7   GLU n 
1 8   PHE n 
1 9   MET n 
1 10  ASN n 
1 11  LYS n 
1 12  GLN n 
1 13  TRP n 
1 14  TYR n 
1 15  LEU n 
1 16  LEU n 
1 17  ALA n 
1 18  ASN n 
1 19  GLN n 
1 20  LEU n 
1 21  ILE n 
1 22  LEU n 
1 23  SER n 
1 24  LEU n 
1 25  SER n 
1 26  LYS n 
1 27  TYR n 
1 28  GLU n 
1 29  GLY n 
1 30  GLY n 
1 31  HIS n 
1 32  ILE n 
1 33  PHE n 
1 34  GLU n 
1 35  LYS n 
1 36  LEU n 
1 37  VAL n 
1 38  ASP n 
1 39  ALA n 
1 40  LYS n 
1 41  LYS n 
1 42  GLN n 
1 43  ASN n 
1 44  CYS n 
1 45  PRO n 
1 46  ASP n 
1 47  TYR n 
1 48  TYR n 
1 49  ASP n 
1 50  VAL n 
1 51  ILE n 
1 52  LYS n 
1 53  ASN n 
1 54  PRO n 
1 55  MET n 
1 56  SER n 
1 57  PHE n 
1 58  SER n 
1 59  CYS n 
1 60  ILE n 
1 61  LYS n 
1 62  THR n 
1 63  LYS n 
1 64  LEU n 
1 65  LYS n 
1 66  LYS n 
1 67  GLY n 
1 68  GLN n 
1 69  TYR n 
1 70  ALA n 
1 71  TYR n 
1 72  PRO n 
1 73  SER n 
1 74  GLU n 
1 75  PHE n 
1 76  VAL n 
1 77  LYS n 
1 78  ASP n 
1 79  VAL n 
1 80  GLN n 
1 81  LEU n 
1 82  ILE n 
1 83  PHE n 
1 84  ASP n 
1 85  ASN n 
1 86  CYS n 
1 87  SER n 
1 88  LEU n 
1 89  TYR n 
1 90  ASN n 
1 91  THR n 
1 92  SER n 
1 93  ASN n 
1 94  SER n 
1 95  VAL n 
1 96  VAL n 
1 97  ALA n 
1 98  ILE n 
1 99  THR n 
1 100 GLY n 
1 101 LYS n 
1 102 ASN n 
1 103 ILE n 
1 104 GLU n 
1 105 THR n 
1 106 TYR n 
1 107 PHE n 
1 108 ASN n 
1 109 ASN n 
1 110 GLN n 
1 111 LEU n 
1 112 ILE n 
1 113 VAL n 
1 114 MET n 
1 115 GLY n 
1 116 TYR n 
1 117 ASN n 
1 118 ASN n 
1 119 PHE n 
1 120 ILE n 
1 121 LEU n 
1 122 LYS n 
1 123 GLU n 
1 124 LYS n 
1 125 LYS n 
1 126 ILE n 
1 127 ASN n 
1 128 ASP n 
1 129 MET n 
1 130 LEU n 
1 131 LYS n 
1 132 LEU n 
1 133 VAL n 
1 134 GLU n 
1 135 GLU n 
1 136 GLU n 
1 137 ASN 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                   137 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PF3D7_1033700 
_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      'Plasmodium falciparum 3D7' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     36329 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                         ? 'C3 H7 N O2'     
89.093  
ASN 'L-peptide linking' y ASPARAGINE                                                                      ? 'C4 H8 N2 O3'    
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                 ? 'C4 H7 N O4'     
133.103 
BU3 non-polymer         . '(R,R)-2,3-BUTANEDIOL'                                                          ? 'C4 H10 O2'      
90.121  
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  
I5K non-polymer         . '1-(3-aminophenyl)-3-methyl-5,6,7,8-tetrahydro-2~{H}-cyclohepta[c]pyrrol-4-one' ? 'C16 H18 N2 O'   
254.327 
ILE 'L-peptide linking' y ISOLEUCINE                                                                      ? 'C6 H13 N O2'    
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                         ? 'C6 H13 N O2'    
131.173 
LYS 'L-peptide linking' y LYSINE                                                                          ? 'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE                                                                      ? 'C5 H11 N O2 S'  
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                   ? 'C9 H11 N O2'    
165.189 
PRO 'L-peptide linking' y PROLINE                                                                         ? 'C5 H9 N O2'     
115.130 
SER 'L-peptide linking' y SERINE                                                                          ? 'C3 H7 N O3'     
105.093 
THR 'L-peptide linking' y THREONINE                                                                       ? 'C4 H9 N O3'     
119.119 
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   324 ?   ?   ?   A . n 
A 1 2   PRO 2   325 ?   ?   ?   A . n 
A 1 3   LEU 3   326 ?   ?   ?   A . n 
A 1 4   GLY 4   327 ?   ?   ?   A . n 
A 1 5   SER 5   328 328 SER SER A . n 
A 1 6   PRO 6   329 329 PRO PRO A . n 
A 1 7   GLU 7   330 330 GLU GLU A . n 
A 1 8   PHE 8   331 331 PHE PHE A . n 
A 1 9   MET 9   332 332 MET MET A . n 
A 1 10  ASN 10  333 333 ASN ASN A . n 
A 1 11  LYS 11  334 334 LYS LYS A . n 
A 1 12  GLN 12  335 335 GLN GLN A . n 
A 1 13  TRP 13  336 336 TRP TRP A . n 
A 1 14  TYR 14  337 337 TYR TYR A . n 
A 1 15  LEU 15  338 338 LEU LEU A . n 
A 1 16  LEU 16  339 339 LEU LEU A . n 
A 1 17  ALA 17  340 340 ALA ALA A . n 
A 1 18  ASN 18  341 341 ASN ASN A . n 
A 1 19  GLN 19  342 342 GLN GLN A . n 
A 1 20  LEU 20  343 343 LEU LEU A . n 
A 1 21  ILE 21  344 344 ILE ILE A . n 
A 1 22  LEU 22  345 345 LEU LEU A . n 
A 1 23  SER 23  346 346 SER SER A . n 
A 1 24  LEU 24  347 347 LEU LEU A . n 
A 1 25  SER 25  348 348 SER SER A . n 
A 1 26  LYS 26  349 349 LYS LYS A . n 
A 1 27  TYR 27  350 350 TYR TYR A . n 
A 1 28  GLU 28  351 351 GLU GLU A . n 
A 1 29  GLY 29  352 352 GLY GLY A . n 
A 1 30  GLY 30  353 353 GLY GLY A . n 
A 1 31  HIS 31  354 354 HIS HIS A . n 
A 1 32  ILE 32  355 355 ILE ILE A . n 
A 1 33  PHE 33  356 356 PHE PHE A . n 
A 1 34  GLU 34  357 357 GLU GLU A . n 
A 1 35  LYS 35  358 358 LYS LYS A . n 
A 1 36  LEU 36  359 359 LEU LEU A . n 
A 1 37  VAL 37  360 360 VAL VAL A . n 
A 1 38  ASP 38  361 361 ASP ASP A . n 
A 1 39  ALA 39  362 362 ALA ALA A . n 
A 1 40  LYS 40  363 363 LYS LYS A . n 
A 1 41  LYS 41  364 364 LYS LYS A . n 
A 1 42  GLN 42  365 365 GLN GLN A . n 
A 1 43  ASN 43  366 366 ASN ASN A . n 
A 1 44  CYS 44  367 367 CYS CYS A . n 
A 1 45  PRO 45  368 368 PRO PRO A . n 
A 1 46  ASP 46  369 369 ASP ASP A . n 
A 1 47  TYR 47  370 370 TYR TYR A . n 
A 1 48  TYR 48  371 371 TYR TYR A . n 
A 1 49  ASP 49  372 372 ASP ASP A . n 
A 1 50  VAL 50  373 373 VAL VAL A . n 
A 1 51  ILE 51  374 374 ILE ILE A . n 
A 1 52  LYS 52  375 375 LYS LYS A . n 
A 1 53  ASN 53  376 376 ASN ASN A . n 
A 1 54  PRO 54  377 377 PRO PRO A . n 
A 1 55  MET 55  378 378 MET MET A . n 
A 1 56  SER 56  379 379 SER SER A . n 
A 1 57  PHE 57  380 380 PHE PHE A . n 
A 1 58  SER 58  381 381 SER SER A . n 
A 1 59  CYS 59  382 382 CYS CYS A . n 
A 1 60  ILE 60  383 383 ILE ILE A . n 
A 1 61  LYS 61  384 384 LYS LYS A . n 
A 1 62  THR 62  385 385 THR THR A . n 
A 1 63  LYS 63  386 386 LYS LYS A . n 
A 1 64  LEU 64  387 387 LEU LEU A . n 
A 1 65  LYS 65  388 388 LYS LYS A . n 
A 1 66  LYS 66  389 389 LYS LYS A . n 
A 1 67  GLY 67  390 390 GLY GLY A . n 
A 1 68  GLN 68  391 391 GLN GLN A . n 
A 1 69  TYR 69  392 392 TYR TYR A . n 
A 1 70  ALA 70  393 393 ALA ALA A . n 
A 1 71  TYR 71  394 394 TYR TYR A . n 
A 1 72  PRO 72  395 395 PRO PRO A . n 
A 1 73  SER 73  396 396 SER SER A . n 
A 1 74  GLU 74  397 397 GLU GLU A . n 
A 1 75  PHE 75  398 398 PHE PHE A . n 
A 1 76  VAL 76  399 399 VAL VAL A . n 
A 1 77  LYS 77  400 400 LYS LYS A . n 
A 1 78  ASP 78  401 401 ASP ASP A . n 
A 1 79  VAL 79  402 402 VAL VAL A . n 
A 1 80  GLN 80  403 403 GLN GLN A . n 
A 1 81  LEU 81  404 404 LEU LEU A . n 
A 1 82  ILE 82  405 405 ILE ILE A . n 
A 1 83  PHE 83  406 406 PHE PHE A . n 
A 1 84  ASP 84  407 407 ASP ASP A . n 
A 1 85  ASN 85  408 408 ASN ASN A . n 
A 1 86  CYS 86  409 409 CYS CYS A . n 
A 1 87  SER 87  410 410 SER SER A . n 
A 1 88  LEU 88  411 411 LEU LEU A . n 
A 1 89  TYR 89  412 412 TYR TYR A . n 
A 1 90  ASN 90  413 413 ASN ASN A . n 
A 1 91  THR 91  414 414 THR THR A . n 
A 1 92  SER 92  415 415 SER SER A . n 
A 1 93  ASN 93  416 416 ASN ASN A . n 
A 1 94  SER 94  417 417 SER SER A . n 
A 1 95  VAL 95  418 418 VAL VAL A . n 
A 1 96  VAL 96  419 419 VAL VAL A . n 
A 1 97  ALA 97  420 420 ALA ALA A . n 
A 1 98  ILE 98  421 421 ILE ILE A . n 
A 1 99  THR 99  422 422 THR THR A . n 
A 1 100 GLY 100 423 423 GLY GLY A . n 
A 1 101 LYS 101 424 424 LYS LYS A . n 
A 1 102 ASN 102 425 425 ASN ASN A . n 
A 1 103 ILE 103 426 426 ILE ILE A . n 
A 1 104 GLU 104 427 427 GLU GLU A . n 
A 1 105 THR 105 428 428 THR THR A . n 
A 1 106 TYR 106 429 429 TYR TYR A . n 
A 1 107 PHE 107 430 430 PHE PHE A . n 
A 1 108 ASN 108 431 431 ASN ASN A . n 
A 1 109 ASN 109 432 432 ASN ASN A . n 
A 1 110 GLN 110 433 433 GLN GLN A . n 
A 1 111 LEU 111 434 434 LEU LEU A . n 
A 1 112 ILE 112 435 435 ILE ILE A . n 
A 1 113 VAL 113 436 436 VAL VAL A . n 
A 1 114 MET 114 437 437 MET MET A . n 
A 1 115 GLY 115 438 438 GLY GLY A . n 
A 1 116 TYR 116 439 439 TYR TYR A . n 
A 1 117 ASN 117 440 440 ASN ASN A . n 
A 1 118 ASN 118 441 441 ASN ASN A . n 
A 1 119 PHE 119 442 442 PHE PHE A . n 
A 1 120 ILE 120 443 443 ILE ILE A . n 
A 1 121 LEU 121 444 444 LEU LEU A . n 
A 1 122 LYS 122 445 445 LYS LYS A . n 
A 1 123 GLU 123 446 446 GLU GLU A . n 
A 1 124 LYS 124 447 447 LYS LYS A . n 
A 1 125 LYS 125 448 448 LYS LYS A . n 
A 1 126 ILE 126 449 449 ILE ILE A . n 
A 1 127 ASN 127 450 450 ASN ASN A . n 
A 1 128 ASP 128 451 451 ASP ASP A . n 
A 1 129 MET 129 452 452 MET MET A . n 
A 1 130 LEU 130 453 453 LEU LEU A . n 
A 1 131 LYS 131 454 454 LYS LYS A . n 
A 1 132 LEU 132 455 455 LEU LEU A . n 
A 1 133 VAL 133 456 456 VAL VAL A . n 
A 1 134 GLU 134 457 ?   ?   ?   A . n 
A 1 135 GLU 135 458 ?   ?   ?   A . n 
A 1 136 GLU 136 459 ?   ?   ?   A . n 
A 1 137 ASN 137 460 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        I5K 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   I5K 
_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 
B 2 BU3 1   501 501 BU3 BU3 A . 
C 3 I5K 1   502 502 I5K MPM A . 
D 4 HOH 1   601 118 HOH HOH A . 
D 4 HOH 2   602 132 HOH HOH A . 
D 4 HOH 3   603 126 HOH HOH A . 
D 4 HOH 4   604 117 HOH HOH A . 
D 4 HOH 5   605 7   HOH HOH A . 
D 4 HOH 6   606 41  HOH HOH A . 
D 4 HOH 7   607 112 HOH HOH A . 
D 4 HOH 8   608 119 HOH HOH A . 
D 4 HOH 9   609 15  HOH HOH A . 
D 4 HOH 10  610 23  HOH HOH A . 
D 4 HOH 11  611 84  HOH HOH A . 
D 4 HOH 12  612 17  HOH HOH A . 
D 4 HOH 13  613 113 HOH HOH A . 
D 4 HOH 14  614 125 HOH HOH A . 
D 4 HOH 15  615 33  HOH HOH A . 
D 4 HOH 16  616 97  HOH HOH A . 
D 4 HOH 17  617 96  HOH HOH A . 
D 4 HOH 18  618 27  HOH HOH A . 
D 4 HOH 19  619 8   HOH HOH A . 
D 4 HOH 20  620 71  HOH HOH A . 
D 4 HOH 21  621 16  HOH HOH A . 
D 4 HOH 22  622 43  HOH HOH A . 
D 4 HOH 23  623 36  HOH HOH A . 
D 4 HOH 24  624 19  HOH HOH A . 
D 4 HOH 25  625 135 HOH HOH A . 
D 4 HOH 26  626 31  HOH HOH A . 
D 4 HOH 27  627 73  HOH HOH A . 
D 4 HOH 28  628 39  HOH HOH A . 
D 4 HOH 29  629 35  HOH HOH A . 
D 4 HOH 30  630 77  HOH HOH A . 
D 4 HOH 31  631 14  HOH HOH A . 
D 4 HOH 32  632 5   HOH HOH A . 
D 4 HOH 33  633 74  HOH HOH A . 
D 4 HOH 34  634 66  HOH HOH A . 
D 4 HOH 35  635 25  HOH HOH A . 
D 4 HOH 36  636 114 HOH HOH A . 
D 4 HOH 37  637 47  HOH HOH A . 
D 4 HOH 38  638 1   HOH HOH A . 
D 4 HOH 39  639 3   HOH HOH A . 
D 4 HOH 40  640 49  HOH HOH A . 
D 4 HOH 41  641 42  HOH HOH A . 
D 4 HOH 42  642 2   HOH HOH A . 
D 4 HOH 43  643 83  HOH HOH A . 
D 4 HOH 44  644 24  HOH HOH A . 
D 4 HOH 45  645 9   HOH HOH A . 
D 4 HOH 46  646 46  HOH HOH A . 
D 4 HOH 47  647 28  HOH HOH A . 
D 4 HOH 48  648 22  HOH HOH A . 
D 4 HOH 49  649 80  HOH HOH A . 
D 4 HOH 50  650 90  HOH HOH A . 
D 4 HOH 51  651 88  HOH HOH A . 
D 4 HOH 52  652 38  HOH HOH A . 
D 4 HOH 53  653 99  HOH HOH A . 
D 4 HOH 54  654 26  HOH HOH A . 
D 4 HOH 55  655 6   HOH HOH A . 
D 4 HOH 56  656 13  HOH HOH A . 
D 4 HOH 57  657 10  HOH HOH A . 
D 4 HOH 58  658 116 HOH HOH A . 
D 4 HOH 59  659 21  HOH HOH A . 
D 4 HOH 60  660 30  HOH HOH A . 
D 4 HOH 61  661 40  HOH HOH A . 
D 4 HOH 62  662 4   HOH HOH A . 
D 4 HOH 63  663 98  HOH HOH A . 
D 4 HOH 64  664 92  HOH HOH A . 
D 4 HOH 65  665 63  HOH HOH A . 
D 4 HOH 66  666 89  HOH HOH A . 
D 4 HOH 67  667 85  HOH HOH A . 
D 4 HOH 68  668 12  HOH HOH A . 
D 4 HOH 69  669 121 HOH HOH A . 
D 4 HOH 70  670 111 HOH HOH A . 
D 4 HOH 71  671 34  HOH HOH A . 
D 4 HOH 72  672 37  HOH HOH A . 
D 4 HOH 73  673 69  HOH HOH A . 
D 4 HOH 74  674 82  HOH HOH A . 
D 4 HOH 75  675 45  HOH HOH A . 
D 4 HOH 76  676 68  HOH HOH A . 
D 4 HOH 77  677 67  HOH HOH A . 
D 4 HOH 78  678 50  HOH HOH A . 
D 4 HOH 79  679 58  HOH HOH A . 
D 4 HOH 80  680 20  HOH HOH A . 
D 4 HOH 81  681 134 HOH HOH A . 
D 4 HOH 82  682 110 HOH HOH A . 
D 4 HOH 83  683 56  HOH HOH A . 
D 4 HOH 84  684 32  HOH HOH A . 
D 4 HOH 85  685 51  HOH HOH A . 
D 4 HOH 86  686 137 HOH HOH A . 
D 4 HOH 87  687 55  HOH HOH A . 
D 4 HOH 88  688 138 HOH HOH A . 
D 4 HOH 89  689 104 HOH HOH A . 
D 4 HOH 90  690 123 HOH HOH A . 
D 4 HOH 91  691 62  HOH HOH A . 
D 4 HOH 92  692 95  HOH HOH A . 
D 4 HOH 93  693 57  HOH HOH A . 
D 4 HOH 94  694 91  HOH HOH A . 
D 4 HOH 95  695 133 HOH HOH A . 
D 4 HOH 96  696 65  HOH HOH A . 
D 4 HOH 97  697 44  HOH HOH A . 
D 4 HOH 98  698 61  HOH HOH A . 
D 4 HOH 99  699 102 HOH HOH A . 
D 4 HOH 100 700 79  HOH HOH A . 
D 4 HOH 101 701 93  HOH HOH A . 
D 4 HOH 102 702 130 HOH HOH A . 
D 4 HOH 103 703 129 HOH HOH A . 
D 4 HOH 104 704 127 HOH HOH A . 
D 4 HOH 105 705 53  HOH HOH A . 
D 4 HOH 106 706 18  HOH HOH A . 
D 4 HOH 107 707 115 HOH HOH A . 
D 4 HOH 108 708 54  HOH HOH A . 
D 4 HOH 109 709 120 HOH HOH A . 
D 4 HOH 110 710 94  HOH HOH A . 
D 4 HOH 111 711 101 HOH HOH A . 
D 4 HOH 112 712 105 HOH HOH A . 
D 4 HOH 113 713 64  HOH HOH A . 
D 4 HOH 114 714 136 HOH HOH A . 
D 4 HOH 115 715 107 HOH HOH A . 
D 4 HOH 116 716 124 HOH HOH A . 
D 4 HOH 117 717 103 HOH HOH A . 
D 4 HOH 118 718 52  HOH HOH A . 
D 4 HOH 119 719 131 HOH HOH A . 
D 4 HOH 120 720 60  HOH HOH A . 
D 4 HOH 121 721 128 HOH HOH A . 
D 4 HOH 122 722 100 HOH HOH A . 
D 4 HOH 123 723 59  HOH HOH A . 
D 4 HOH 124 724 108 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 330 ? CG  ? A GLU 7   CG  
2  1 Y 1 A GLU 330 ? CD  ? A GLU 7   CD  
3  1 Y 1 A GLU 330 ? OE1 ? A GLU 7   OE1 
4  1 Y 1 A GLU 330 ? OE2 ? A GLU 7   OE2 
5  1 Y 1 A LYS 363 ? CG  ? A LYS 40  CG  
6  1 Y 1 A LYS 363 ? CD  ? A LYS 40  CD  
7  1 Y 1 A LYS 363 ? CE  ? A LYS 40  CE  
8  1 Y 1 A LYS 363 ? NZ  ? A LYS 40  NZ  
9  1 Y 1 A LYS 364 ? CG  ? A LYS 41  CG  
10 1 Y 1 A LYS 364 ? CD  ? A LYS 41  CD  
11 1 Y 1 A LYS 364 ? CE  ? A LYS 41  CE  
12 1 Y 1 A LYS 364 ? NZ  ? A LYS 41  NZ  
13 1 Y 1 A ASN 366 ? CG  ? A ASN 43  CG  
14 1 Y 1 A ASN 366 ? OD1 ? A ASN 43  OD1 
15 1 Y 1 A ASN 366 ? ND2 ? A ASN 43  ND2 
16 1 Y 1 A LYS 388 ? CE  ? A LYS 65  CE  
17 1 Y 1 A LYS 388 ? NZ  ? A LYS 65  NZ  
18 1 Y 1 A LYS 400 ? NZ  ? A LYS 77  NZ  
19 1 Y 1 A LYS 445 ? CD  ? A LYS 122 CD  
20 1 Y 1 A LYS 445 ? CE  ? A LYS 122 CE  
21 1 Y 1 A LYS 445 ? NZ  ? A LYS 122 NZ  
22 1 Y 1 A LYS 447 ? CG  ? A LYS 124 CG  
23 1 Y 1 A LYS 447 ? CD  ? A LYS 124 CD  
24 1 Y 1 A LYS 447 ? CE  ? A LYS 124 CE  
25 1 Y 1 A LYS 447 ? NZ  ? A LYS 124 NZ  
26 1 Y 1 A MET 452 ? SD  ? A MET 129 SD  
27 1 Y 1 A MET 452 ? CE  ? A MET 129 CE  
28 1 Y 1 A LYS 454 ? CG  ? A LYS 131 CG  
29 1 Y 1 A LYS 454 ? CD  ? A LYS 131 CD  
30 1 Y 1 A LYS 454 ? CE  ? A LYS 131 CE  
31 1 Y 1 A LYS 454 ? NZ  ? A LYS 131 NZ  
32 1 Y 1 A LEU 455 ? CG  ? A LEU 132 CG  
33 1 Y 1 A LEU 455 ? CD1 ? A LEU 132 CD1 
34 1 Y 1 A LEU 455 ? CD2 ? A LEU 132 CD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.21_5207 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? autoPROC    ? ? ? .         2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? STARANISO   ? ? ? .         3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .         4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .         5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HHC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     38.360 
_cell.length_a_esd                 ? 
_cell.length_b                     86.720 
_cell.length_b_esd                 ? 
_cell.length_c                     107.820 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9HHC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9HHC 
_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             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.58 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '25% PEG3350, 0.2M LiSO4, 0.1 M Tris pH 8.5' 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-10-18 
_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   1.00000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HHC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.558 
_reflns.d_resolution_low                               67.575 
_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                                     13888 
_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                           89.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13 
_reflns.pdbx_netI_over_av_sigmaI                       13.6 
_reflns.pdbx_netI_over_sigmaI                          13.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.230 
_reflns.pdbx_Rpim_I_all                                0.063 
_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                              0.221 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.558 
_reflns_shell.d_res_low                                     1.662 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             695 
_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                               0.550 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.622 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9HHC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.56 
_refine.ls_d_res_low                             43.36 
_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                     13882 
_refine.ls_number_reflns_R_free                  701 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    52.98 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2000 
_refine.ls_R_factor_R_free                       0.2371 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1981 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.61 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.56 
_refine_hist.d_res_low                        43.36 
_refine_hist.number_atoms_solvent             124 
_refine_hist.number_atoms_total               1168 
_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        1019 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 1113 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.759  ? 1515 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.072 ? 403  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045  ? 164  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 192  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.56 1.68  . . 35  618  13.00 . . . . 0.2681 . . . . . . . . . . . 0.2316 
'X-RAY DIFFRACTION' 1.68 1.85  . . 73  1626 33.00 . . . . 0.2899 . . . . . . . . . . . 0.2474 
'X-RAY DIFFRACTION' 1.85 2.11  . . 133 2463 50.00 . . . . 0.2390 . . . . . . . . . . . 0.2473 
'X-RAY DIFFRACTION' 2.11 2.66  . . 190 3571 72.00 . . . . 0.2248 . . . . . . . . . . . 0.2664 
'X-RAY DIFFRACTION' 2.66 43.36 . . 270 4903 95.00 . . . . 0.1804 . . . . . . . . . . . 0.2270 
# 
_struct.entry_id                     9HHC 
_struct.title                        'Crystal Structure of the Plasmodium falciparum Bromodomain PfBDP1 in complex with MPM2' 
_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        9HHC 
_struct_keywords.text            'plasmodium, bromodomain, inhibitor, complex, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8IJ72_PLAF7 
_struct_ref.pdbx_db_accession          Q8IJ72 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NKQWYLLANQLILSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCIKTKLKKGQYAYPSEFVKDVQLIFDNCSLY
NTSNSVVAITGKNIETYFNNQLIVMGYNNFILKEKKINDMLKLVEEEN
;
_struct_ref.pdbx_align_begin           333 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HHC 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 10 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 137 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8IJ72 
_struct_ref_seq.db_align_beg                  333 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  460 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       333 
_struct_ref_seq.pdbx_auth_seq_align_end       460 
# 
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 9HHC GLY A 1 ? UNP Q8IJ72 ? ? 'expression tag' 324 1 
1 9HHC PRO A 2 ? UNP Q8IJ72 ? ? 'expression tag' 325 2 
1 9HHC LEU A 3 ? UNP Q8IJ72 ? ? 'expression tag' 326 3 
1 9HHC GLY A 4 ? UNP Q8IJ72 ? ? 'expression tag' 327 4 
1 9HHC SER A 5 ? UNP Q8IJ72 ? ? 'expression tag' 328 5 
1 9HHC PRO A 6 ? UNP Q8IJ72 ? ? 'expression tag' 329 6 
1 9HHC GLU A 7 ? UNP Q8IJ72 ? ? 'expression tag' 330 7 
1 9HHC PHE A 8 ? UNP Q8IJ72 ? ? 'expression tag' 331 8 
1 9HHC MET A 9 ? UNP Q8IJ72 ? ? 'expression tag' 332 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 220  ? 
1 MORE         -0   ? 
1 'SSA (A^2)'  7740 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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 SER A 5   ? TYR A 27  ? SER A 328 TYR A 350 1 ? 23 
HELX_P HELX_P2 AA2 GLY A 29  ? GLU A 34  ? GLY A 352 GLU A 357 5 ? 6  
HELX_P HELX_P3 AA3 ASP A 46  ? ILE A 51  ? ASP A 369 ILE A 374 1 ? 6  
HELX_P HELX_P4 AA4 SER A 56  ? LYS A 66  ? SER A 379 LYS A 389 1 ? 11 
HELX_P HELX_P5 AA5 TYR A 71  ? ASN A 90  ? TYR A 394 ASN A 413 1 ? 20 
HELX_P HELX_P6 AA6 SER A 94  ? MET A 114 ? SER A 417 MET A 437 1 ? 21 
HELX_P HELX_P7 AA7 GLY A 115 ? VAL A 133 ? GLY A 438 VAL A 456 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9HHC 
_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 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 678 ? ? O A HOH 709 ? ? 2.11 
2 1 O A HOH 663 ? ? O A HOH 672 ? ? 2.12 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         3.1697 
_pdbx_refine_tls.origin_y         19.7688 
_pdbx_refine_tls.origin_z         13.0079 
_pdbx_refine_tls.T[1][1]          0.1460 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0396 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0020 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1749 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0653 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1441 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          3.0407 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.3484 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.5438 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.8028 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.3729 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.2944 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.1623 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0612 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.2642 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0740 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0292 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.1143 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.1513 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.2214 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.1116 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_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 324 ? A GLY 1   
2 1 Y 1 A PRO 325 ? A PRO 2   
3 1 Y 1 A LEU 326 ? A LEU 3   
4 1 Y 1 A GLY 327 ? A GLY 4   
5 1 Y 1 A GLU 457 ? A GLU 134 
6 1 Y 1 A GLU 458 ? A GLU 135 
7 1 Y 1 A GLU 459 ? A GLU 136 
8 1 Y 1 A ASN 460 ? A ASN 137 
# 
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  
ASN N    N N N 14  
ASN CA   C N S 15  
ASN C    C N N 16  
ASN O    O N N 17  
ASN CB   C N N 18  
ASN CG   C N N 19  
ASN OD1  O N N 20  
ASN ND2  N N N 21  
ASN OXT  O N N 22  
ASN H    H N N 23  
ASN H2   H N N 24  
ASN HA   H N N 25  
ASN HB2  H N N 26  
ASN HB3  H N N 27  
ASN HD21 H N N 28  
ASN HD22 H N N 29  
ASN HXT  H N N 30  
ASP N    N N N 31  
ASP CA   C N S 32  
ASP C    C N N 33  
ASP O    O N N 34  
ASP CB   C N N 35  
ASP CG   C N N 36  
ASP OD1  O N N 37  
ASP OD2  O N N 38  
ASP OXT  O N N 39  
ASP H    H N N 40  
ASP H2   H N N 41  
ASP HA   H N N 42  
ASP HB2  H N N 43  
ASP HB3  H N N 44  
ASP HD2  H N N 45  
ASP HXT  H N N 46  
BU3 O6   O N N 47  
BU3 C3   C N R 48  
BU3 C4   C N N 49  
BU3 C2   C N R 50  
BU3 O5   O N N 51  
BU3 C1   C N N 52  
BU3 HO6  H N N 53  
BU3 H3   H N N 54  
BU3 H41  H N N 55  
BU3 H42  H N N 56  
BU3 H43  H N N 57  
BU3 H2   H N N 58  
BU3 HO5  H N N 59  
BU3 H11  H N N 60  
BU3 H12  H N N 61  
BU3 H13  H N N 62  
CYS N    N N N 63  
CYS CA   C N R 64  
CYS C    C N N 65  
CYS O    O N N 66  
CYS CB   C N N 67  
CYS SG   S N N 68  
CYS OXT  O N N 69  
CYS H    H N N 70  
CYS H2   H N N 71  
CYS HA   H N N 72  
CYS HB2  H N N 73  
CYS HB3  H N N 74  
CYS HG   H N N 75  
CYS HXT  H N N 76  
GLN N    N N N 77  
GLN CA   C N S 78  
GLN C    C N N 79  
GLN O    O N N 80  
GLN CB   C N N 81  
GLN CG   C N N 82  
GLN CD   C N N 83  
GLN OE1  O N N 84  
GLN NE2  N N N 85  
GLN OXT  O N N 86  
GLN H    H N N 87  
GLN H2   H N N 88  
GLN HA   H N N 89  
GLN HB2  H N N 90  
GLN HB3  H N N 91  
GLN HG2  H N N 92  
GLN HG3  H N N 93  
GLN HE21 H N N 94  
GLN HE22 H N N 95  
GLN HXT  H N N 96  
GLU N    N N N 97  
GLU CA   C N S 98  
GLU C    C N N 99  
GLU O    O N N 100 
GLU CB   C N N 101 
GLU CG   C N N 102 
GLU CD   C N N 103 
GLU OE1  O N N 104 
GLU OE2  O N N 105 
GLU OXT  O N N 106 
GLU H    H N N 107 
GLU H2   H N N 108 
GLU HA   H N N 109 
GLU HB2  H N N 110 
GLU HB3  H N N 111 
GLU HG2  H N N 112 
GLU HG3  H N N 113 
GLU HE2  H N N 114 
GLU HXT  H N N 115 
GLY N    N N N 116 
GLY CA   C N N 117 
GLY C    C N N 118 
GLY O    O N N 119 
GLY OXT  O N N 120 
GLY H    H N N 121 
GLY H2   H N N 122 
GLY HA2  H N N 123 
GLY HA3  H N N 124 
GLY HXT  H N N 125 
HIS N    N N N 126 
HIS CA   C N S 127 
HIS C    C N N 128 
HIS O    O N N 129 
HIS CB   C N N 130 
HIS CG   C Y N 131 
HIS ND1  N Y N 132 
HIS CD2  C Y N 133 
HIS CE1  C Y N 134 
HIS NE2  N Y N 135 
HIS OXT  O N N 136 
HIS H    H N N 137 
HIS H2   H N N 138 
HIS HA   H N N 139 
HIS HB2  H N N 140 
HIS HB3  H N N 141 
HIS HD1  H N N 142 
HIS HD2  H N N 143 
HIS HE1  H N N 144 
HIS HE2  H N N 145 
HIS HXT  H N N 146 
HOH O    O N N 147 
HOH H1   H N N 148 
HOH H2   H N N 149 
I5K C15  C Y N 150 
I5K C13  C Y N 151 
I5K N    N Y N 152 
I5K C    C Y N 153 
I5K O    O N N 154 
I5K C1   C N N 155 
I5K C10  C Y N 156 
I5K C11  C Y N 157 
I5K C12  C Y N 158 
I5K C14  C Y N 159 
I5K C2   C Y N 160 
I5K C3   C N N 161 
I5K C4   C N N 162 
I5K C5   C N N 163 
I5K C6   C N N 164 
I5K C7   C N N 165 
I5K C8   C Y N 166 
I5K C9   C Y N 167 
I5K N1   N N N 168 
I5K H1   H N N 169 
I5K H2   H N N 170 
I5K H3   H N N 171 
I5K H4   H N N 172 
I5K H5   H N N 173 
I5K H6   H N N 174 
I5K H7   H N N 175 
I5K H8   H N N 176 
I5K H9   H N N 177 
I5K H10  H N N 178 
I5K H11  H N N 179 
I5K H12  H N N 180 
I5K H13  H N N 181 
I5K H14  H N N 182 
I5K H15  H N N 183 
I5K H16  H N N 184 
I5K H17  H N N 185 
I5K H18  H N N 186 
ILE N    N N N 187 
ILE CA   C N S 188 
ILE C    C N N 189 
ILE O    O N N 190 
ILE CB   C N S 191 
ILE CG1  C N N 192 
ILE CG2  C N N 193 
ILE CD1  C N N 194 
ILE OXT  O N N 195 
ILE H    H N N 196 
ILE H2   H N N 197 
ILE HA   H N N 198 
ILE HB   H N N 199 
ILE HG12 H N N 200 
ILE HG13 H N N 201 
ILE HG21 H N N 202 
ILE HG22 H N N 203 
ILE HG23 H N N 204 
ILE HD11 H N N 205 
ILE HD12 H N N 206 
ILE HD13 H N N 207 
ILE HXT  H N N 208 
LEU N    N N N 209 
LEU CA   C N S 210 
LEU C    C N N 211 
LEU O    O N N 212 
LEU CB   C N N 213 
LEU CG   C N N 214 
LEU CD1  C N N 215 
LEU CD2  C N N 216 
LEU OXT  O N N 217 
LEU H    H N N 218 
LEU H2   H N N 219 
LEU HA   H N N 220 
LEU HB2  H N N 221 
LEU HB3  H N N 222 
LEU HG   H N N 223 
LEU HD11 H N N 224 
LEU HD12 H N N 225 
LEU HD13 H N N 226 
LEU HD21 H N N 227 
LEU HD22 H N N 228 
LEU HD23 H N N 229 
LEU HXT  H N N 230 
LYS N    N N N 231 
LYS CA   C N S 232 
LYS C    C N N 233 
LYS O    O N N 234 
LYS CB   C N N 235 
LYS CG   C N N 236 
LYS CD   C N N 237 
LYS CE   C N N 238 
LYS NZ   N N N 239 
LYS OXT  O N N 240 
LYS H    H N N 241 
LYS H2   H N N 242 
LYS HA   H N N 243 
LYS HB2  H N N 244 
LYS HB3  H N N 245 
LYS HG2  H N N 246 
LYS HG3  H N N 247 
LYS HD2  H N N 248 
LYS HD3  H N N 249 
LYS HE2  H N N 250 
LYS HE3  H N N 251 
LYS HZ1  H N N 252 
LYS HZ2  H N N 253 
LYS HZ3  H N N 254 
LYS HXT  H N N 255 
MET N    N N N 256 
MET CA   C N S 257 
MET C    C N N 258 
MET O    O N N 259 
MET CB   C N N 260 
MET CG   C N N 261 
MET SD   S N N 262 
MET CE   C N N 263 
MET OXT  O N N 264 
MET H    H N N 265 
MET H2   H N N 266 
MET HA   H N N 267 
MET HB2  H N N 268 
MET HB3  H N N 269 
MET HG2  H N N 270 
MET HG3  H N N 271 
MET HE1  H N N 272 
MET HE2  H N N 273 
MET HE3  H N N 274 
MET HXT  H N N 275 
PHE N    N N N 276 
PHE CA   C N S 277 
PHE C    C N N 278 
PHE O    O N N 279 
PHE CB   C N N 280 
PHE CG   C Y N 281 
PHE CD1  C Y N 282 
PHE CD2  C Y N 283 
PHE CE1  C Y N 284 
PHE CE2  C Y N 285 
PHE CZ   C Y N 286 
PHE OXT  O N N 287 
PHE H    H N N 288 
PHE H2   H N N 289 
PHE HA   H N N 290 
PHE HB2  H N N 291 
PHE HB3  H N N 292 
PHE HD1  H N N 293 
PHE HD2  H N N 294 
PHE HE1  H N N 295 
PHE HE2  H N N 296 
PHE HZ   H N N 297 
PHE HXT  H N N 298 
PRO N    N N N 299 
PRO CA   C N S 300 
PRO C    C N N 301 
PRO O    O N N 302 
PRO CB   C N N 303 
PRO CG   C N N 304 
PRO CD   C N N 305 
PRO OXT  O N N 306 
PRO H    H N N 307 
PRO HA   H N N 308 
PRO HB2  H N N 309 
PRO HB3  H N N 310 
PRO HG2  H N N 311 
PRO HG3  H N N 312 
PRO HD2  H N N 313 
PRO HD3  H N N 314 
PRO HXT  H N N 315 
SER N    N N N 316 
SER CA   C N S 317 
SER C    C N N 318 
SER O    O N N 319 
SER CB   C N N 320 
SER OG   O N N 321 
SER OXT  O N N 322 
SER H    H N N 323 
SER H2   H N N 324 
SER HA   H N N 325 
SER HB2  H N N 326 
SER HB3  H N N 327 
SER HG   H N N 328 
SER HXT  H N N 329 
THR N    N N N 330 
THR CA   C N S 331 
THR C    C N N 332 
THR O    O N N 333 
THR CB   C N R 334 
THR OG1  O N N 335 
THR CG2  C N N 336 
THR OXT  O N N 337 
THR H    H N N 338 
THR H2   H N N 339 
THR HA   H N N 340 
THR HB   H N N 341 
THR HG1  H N N 342 
THR HG21 H N N 343 
THR HG22 H N N 344 
THR HG23 H N N 345 
THR HXT  H N N 346 
TRP N    N N N 347 
TRP CA   C N S 348 
TRP C    C N N 349 
TRP O    O N N 350 
TRP CB   C N N 351 
TRP CG   C Y N 352 
TRP CD1  C Y N 353 
TRP CD2  C Y N 354 
TRP NE1  N Y N 355 
TRP CE2  C Y N 356 
TRP CE3  C Y N 357 
TRP CZ2  C Y N 358 
TRP CZ3  C Y N 359 
TRP CH2  C Y N 360 
TRP OXT  O N N 361 
TRP H    H N N 362 
TRP H2   H N N 363 
TRP HA   H N N 364 
TRP HB2  H N N 365 
TRP HB3  H N N 366 
TRP HD1  H N N 367 
TRP HE1  H N N 368 
TRP HE3  H N N 369 
TRP HZ2  H N N 370 
TRP HZ3  H N N 371 
TRP HH2  H N N 372 
TRP HXT  H N N 373 
TYR N    N N N 374 
TYR CA   C N S 375 
TYR C    C N N 376 
TYR O    O N N 377 
TYR CB   C N N 378 
TYR CG   C Y N 379 
TYR CD1  C Y N 380 
TYR CD2  C Y N 381 
TYR CE1  C Y N 382 
TYR CE2  C Y N 383 
TYR CZ   C Y N 384 
TYR OH   O N N 385 
TYR OXT  O N N 386 
TYR H    H N N 387 
TYR H2   H N N 388 
TYR HA   H N N 389 
TYR HB2  H N N 390 
TYR HB3  H N N 391 
TYR HD1  H N N 392 
TYR HD2  H N N 393 
TYR HE1  H N N 394 
TYR HE2  H N N 395 
TYR HH   H N N 396 
TYR HXT  H N N 397 
VAL N    N N N 398 
VAL CA   C N S 399 
VAL C    C N N 400 
VAL O    O N N 401 
VAL CB   C N N 402 
VAL CG1  C N N 403 
VAL CG2  C N N 404 
VAL OXT  O N N 405 
VAL H    H N N 406 
VAL H2   H N N 407 
VAL HA   H N N 408 
VAL HB   H N N 409 
VAL HG11 H N N 410 
VAL HG12 H N N 411 
VAL HG13 H N N 412 
VAL HG21 H N N 413 
VAL HG22 H N N 414 
VAL HG23 H N N 415 
VAL HXT  H N N 416 
# 
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  
ASN N   CA   sing N N 13  
ASN N   H    sing N N 14  
ASN N   H2   sing N N 15  
ASN CA  C    sing N N 16  
ASN CA  CB   sing N N 17  
ASN CA  HA   sing N N 18  
ASN C   O    doub N N 19  
ASN C   OXT  sing N N 20  
ASN CB  CG   sing N N 21  
ASN CB  HB2  sing N N 22  
ASN CB  HB3  sing N N 23  
ASN CG  OD1  doub N N 24  
ASN CG  ND2  sing N N 25  
ASN ND2 HD21 sing N N 26  
ASN ND2 HD22 sing N N 27  
ASN OXT HXT  sing N N 28  
ASP N   CA   sing N N 29  
ASP N   H    sing N N 30  
ASP N   H2   sing N N 31  
ASP CA  C    sing N N 32  
ASP CA  CB   sing N N 33  
ASP CA  HA   sing N N 34  
ASP C   O    doub N N 35  
ASP C   OXT  sing N N 36  
ASP CB  CG   sing N N 37  
ASP CB  HB2  sing N N 38  
ASP CB  HB3  sing N N 39  
ASP CG  OD1  doub N N 40  
ASP CG  OD2  sing N N 41  
ASP OD2 HD2  sing N N 42  
ASP OXT HXT  sing N N 43  
BU3 O6  C3   sing N N 44  
BU3 O6  HO6  sing N N 45  
BU3 C3  C4   sing N N 46  
BU3 C3  C2   sing N N 47  
BU3 C3  H3   sing N N 48  
BU3 C4  H41  sing N N 49  
BU3 C4  H42  sing N N 50  
BU3 C4  H43  sing N N 51  
BU3 C2  O5   sing N N 52  
BU3 C2  C1   sing N N 53  
BU3 C2  H2   sing N N 54  
BU3 O5  HO5  sing N N 55  
BU3 C1  H11  sing N N 56  
BU3 C1  H12  sing N N 57  
BU3 C1  H13  sing N N 58  
CYS N   CA   sing N N 59  
CYS N   H    sing N N 60  
CYS N   H2   sing N N 61  
CYS CA  C    sing N N 62  
CYS CA  CB   sing N N 63  
CYS CA  HA   sing N N 64  
CYS C   O    doub N N 65  
CYS C   OXT  sing N N 66  
CYS CB  SG   sing N N 67  
CYS CB  HB2  sing N N 68  
CYS CB  HB3  sing N N 69  
CYS SG  HG   sing N N 70  
CYS OXT HXT  sing N N 71  
GLN N   CA   sing N N 72  
GLN N   H    sing N N 73  
GLN N   H2   sing N N 74  
GLN CA  C    sing N N 75  
GLN CA  CB   sing N N 76  
GLN CA  HA   sing N N 77  
GLN C   O    doub N N 78  
GLN C   OXT  sing N N 79  
GLN CB  CG   sing N N 80  
GLN CB  HB2  sing N N 81  
GLN CB  HB3  sing N N 82  
GLN CG  CD   sing N N 83  
GLN CG  HG2  sing N N 84  
GLN CG  HG3  sing N N 85  
GLN CD  OE1  doub N N 86  
GLN CD  NE2  sing N N 87  
GLN NE2 HE21 sing N N 88  
GLN NE2 HE22 sing N N 89  
GLN OXT HXT  sing N N 90  
GLU N   CA   sing N N 91  
GLU N   H    sing N N 92  
GLU N   H2   sing N N 93  
GLU CA  C    sing N N 94  
GLU CA  CB   sing N N 95  
GLU CA  HA   sing N N 96  
GLU C   O    doub N N 97  
GLU C   OXT  sing N N 98  
GLU CB  CG   sing N N 99  
GLU CB  HB2  sing N N 100 
GLU CB  HB3  sing N N 101 
GLU CG  CD   sing N N 102 
GLU CG  HG2  sing N N 103 
GLU CG  HG3  sing N N 104 
GLU CD  OE1  doub N N 105 
GLU CD  OE2  sing N N 106 
GLU OE2 HE2  sing N N 107 
GLU OXT HXT  sing N N 108 
GLY N   CA   sing N N 109 
GLY N   H    sing N N 110 
GLY N   H2   sing N N 111 
GLY CA  C    sing N N 112 
GLY CA  HA2  sing N N 113 
GLY CA  HA3  sing N N 114 
GLY C   O    doub N N 115 
GLY C   OXT  sing N N 116 
GLY OXT HXT  sing N N 117 
HIS N   CA   sing N N 118 
HIS N   H    sing N N 119 
HIS N   H2   sing N N 120 
HIS CA  C    sing N N 121 
HIS CA  CB   sing N N 122 
HIS CA  HA   sing N N 123 
HIS C   O    doub N N 124 
HIS C   OXT  sing N N 125 
HIS CB  CG   sing N N 126 
HIS CB  HB2  sing N N 127 
HIS CB  HB3  sing N N 128 
HIS CG  ND1  sing Y N 129 
HIS CG  CD2  doub Y N 130 
HIS ND1 CE1  doub Y N 131 
HIS ND1 HD1  sing N N 132 
HIS CD2 NE2  sing Y N 133 
HIS CD2 HD2  sing N N 134 
HIS CE1 NE2  sing Y N 135 
HIS CE1 HE1  sing N N 136 
HIS NE2 HE2  sing N N 137 
HIS OXT HXT  sing N N 138 
HOH O   H1   sing N N 139 
HOH O   H2   sing N N 140 
I5K C5  C6   sing N N 141 
I5K C5  C4   sing N N 142 
I5K C6  C7   sing N N 143 
I5K C4  C3   sing N N 144 
I5K C7  C8   sing N N 145 
I5K C3  O    doub N N 146 
I5K C3  C2   sing N N 147 
I5K C15 C14  doub Y N 148 
I5K C15 C10  sing Y N 149 
I5K C8  C2   sing Y N 150 
I5K C8  C9   doub Y N 151 
I5K C14 C13  sing Y N 152 
I5K C2  C    doub Y N 153 
I5K C9  C10  sing N N 154 
I5K C9  N    sing Y N 155 
I5K C10 C11  doub Y N 156 
I5K C   N    sing Y N 157 
I5K C   C1   sing N N 158 
I5K C13 C12  doub Y N 159 
I5K C11 C12  sing Y N 160 
I5K C12 N1   sing N N 161 
I5K C15 H1   sing N N 162 
I5K C13 H2   sing N N 163 
I5K N   H3   sing N N 164 
I5K C1  H4   sing N N 165 
I5K C1  H5   sing N N 166 
I5K C1  H6   sing N N 167 
I5K C11 H7   sing N N 168 
I5K C14 H8   sing N N 169 
I5K C4  H9   sing N N 170 
I5K C4  H10  sing N N 171 
I5K C5  H11  sing N N 172 
I5K C5  H12  sing N N 173 
I5K C6  H13  sing N N 174 
I5K C6  H14  sing N N 175 
I5K C7  H15  sing N N 176 
I5K C7  H16  sing N N 177 
I5K N1  H17  sing N N 178 
I5K N1  H18  sing N N 179 
ILE N   CA   sing N N 180 
ILE N   H    sing N N 181 
ILE N   H2   sing N N 182 
ILE CA  C    sing N N 183 
ILE CA  CB   sing N N 184 
ILE CA  HA   sing N N 185 
ILE C   O    doub N N 186 
ILE C   OXT  sing N N 187 
ILE CB  CG1  sing N N 188 
ILE CB  CG2  sing N N 189 
ILE CB  HB   sing N N 190 
ILE CG1 CD1  sing N N 191 
ILE CG1 HG12 sing N N 192 
ILE CG1 HG13 sing N N 193 
ILE CG2 HG21 sing N N 194 
ILE CG2 HG22 sing N N 195 
ILE CG2 HG23 sing N N 196 
ILE CD1 HD11 sing N N 197 
ILE CD1 HD12 sing N N 198 
ILE CD1 HD13 sing N N 199 
ILE OXT HXT  sing N N 200 
LEU N   CA   sing N N 201 
LEU N   H    sing N N 202 
LEU N   H2   sing N N 203 
LEU CA  C    sing N N 204 
LEU CA  CB   sing N N 205 
LEU CA  HA   sing N N 206 
LEU C   O    doub N N 207 
LEU C   OXT  sing N N 208 
LEU CB  CG   sing N N 209 
LEU CB  HB2  sing N N 210 
LEU CB  HB3  sing N N 211 
LEU CG  CD1  sing N N 212 
LEU CG  CD2  sing N N 213 
LEU CG  HG   sing N N 214 
LEU CD1 HD11 sing N N 215 
LEU CD1 HD12 sing N N 216 
LEU CD1 HD13 sing N N 217 
LEU CD2 HD21 sing N N 218 
LEU CD2 HD22 sing N N 219 
LEU CD2 HD23 sing N N 220 
LEU OXT HXT  sing N N 221 
LYS N   CA   sing N N 222 
LYS N   H    sing N N 223 
LYS N   H2   sing N N 224 
LYS CA  C    sing N N 225 
LYS CA  CB   sing N N 226 
LYS CA  HA   sing N N 227 
LYS C   O    doub N N 228 
LYS C   OXT  sing N N 229 
LYS CB  CG   sing N N 230 
LYS CB  HB2  sing N N 231 
LYS CB  HB3  sing N N 232 
LYS CG  CD   sing N N 233 
LYS CG  HG2  sing N N 234 
LYS CG  HG3  sing N N 235 
LYS CD  CE   sing N N 236 
LYS CD  HD2  sing N N 237 
LYS CD  HD3  sing N N 238 
LYS CE  NZ   sing N N 239 
LYS CE  HE2  sing N N 240 
LYS CE  HE3  sing N N 241 
LYS NZ  HZ1  sing N N 242 
LYS NZ  HZ2  sing N N 243 
LYS NZ  HZ3  sing N N 244 
LYS OXT HXT  sing N N 245 
MET N   CA   sing N N 246 
MET N   H    sing N N 247 
MET N   H2   sing N N 248 
MET CA  C    sing N N 249 
MET CA  CB   sing N N 250 
MET CA  HA   sing N N 251 
MET C   O    doub N N 252 
MET C   OXT  sing N N 253 
MET CB  CG   sing N N 254 
MET CB  HB2  sing N N 255 
MET CB  HB3  sing N N 256 
MET CG  SD   sing N N 257 
MET CG  HG2  sing N N 258 
MET CG  HG3  sing N N 259 
MET SD  CE   sing N N 260 
MET CE  HE1  sing N N 261 
MET CE  HE2  sing N N 262 
MET CE  HE3  sing N N 263 
MET OXT HXT  sing N N 264 
PHE N   CA   sing N N 265 
PHE N   H    sing N N 266 
PHE N   H2   sing N N 267 
PHE CA  C    sing N N 268 
PHE CA  CB   sing N N 269 
PHE CA  HA   sing N N 270 
PHE C   O    doub N N 271 
PHE C   OXT  sing N N 272 
PHE CB  CG   sing N N 273 
PHE CB  HB2  sing N N 274 
PHE CB  HB3  sing N N 275 
PHE CG  CD1  doub Y N 276 
PHE CG  CD2  sing Y N 277 
PHE CD1 CE1  sing Y N 278 
PHE CD1 HD1  sing N N 279 
PHE CD2 CE2  doub Y N 280 
PHE CD2 HD2  sing N N 281 
PHE CE1 CZ   doub Y N 282 
PHE CE1 HE1  sing N N 283 
PHE CE2 CZ   sing Y N 284 
PHE CE2 HE2  sing N N 285 
PHE CZ  HZ   sing N N 286 
PHE OXT HXT  sing N N 287 
PRO N   CA   sing N N 288 
PRO N   CD   sing N N 289 
PRO N   H    sing N N 290 
PRO CA  C    sing N N 291 
PRO CA  CB   sing N N 292 
PRO CA  HA   sing N N 293 
PRO C   O    doub N N 294 
PRO C   OXT  sing N N 295 
PRO CB  CG   sing N N 296 
PRO CB  HB2  sing N N 297 
PRO CB  HB3  sing N N 298 
PRO CG  CD   sing N N 299 
PRO CG  HG2  sing N N 300 
PRO CG  HG3  sing N N 301 
PRO CD  HD2  sing N N 302 
PRO CD  HD3  sing N N 303 
PRO OXT HXT  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           RTG2202 
_pdbx_audit_support.ordinal                1 
# 
_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   7M97 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9HHC 
_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]   0.026069 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011531 
_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]   0.009275 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   A SER A 1 5   ? 26.405  28.716 4.092  0.43 55.78 ? 328 SER A N   1 
ATOM   2    N N   B SER A 1 5   ? 25.382  30.551 6.042  0.57 55.20 ? 328 SER A N   1 
ATOM   3    C CA  A SER A 1 5   ? 25.476  29.228 5.095  0.43 56.22 ? 328 SER A CA  1 
ATOM   4    C CA  B SER A 1 5   ? 25.432  29.510 5.019  0.57 56.07 ? 328 SER A CA  1 
ATOM   5    C C   A SER A 1 5   ? 24.009  28.881 4.786  0.43 62.72 ? 328 SER A C   1 
ATOM   6    C C   B SER A 1 5   ? 24.045  28.917 4.768  0.57 62.79 ? 328 SER A C   1 
ATOM   7    O O   A SER A 1 5   ? 23.314  28.377 5.669  0.43 64.63 ? 328 SER A O   1 
ATOM   8    O O   B SER A 1 5   ? 23.473  28.265 5.642  0.57 64.47 ? 328 SER A O   1 
ATOM   9    C CB  A SER A 1 5   ? 25.646  30.746 5.266  0.43 55.43 ? 328 SER A CB  1 
ATOM   10   C CB  B SER A 1 5   ? 26.409  28.407 5.423  0.57 55.04 ? 328 SER A CB  1 
ATOM   11   O OG  A SER A 1 5   ? 24.784  31.247 6.276  0.43 52.69 ? 328 SER A OG  1 
ATOM   12   O OG  B SER A 1 5   ? 27.657  28.934 5.829  0.57 54.79 ? 328 SER A OG  1 
ATOM   13   N N   . PRO A 1 6   ? 23.520  29.136 3.558  1.00 60.29 ? 329 PRO A N   1 
ATOM   14   C CA  . PRO A 1 6   ? 22.125  28.729 3.275  1.00 62.07 ? 329 PRO A CA  1 
ATOM   15   C C   . PRO A 1 6   ? 21.895  27.229 3.366  1.00 61.26 ? 329 PRO A C   1 
ATOM   16   O O   . PRO A 1 6   ? 20.831  26.792 3.832  1.00 49.19 ? 329 PRO A O   1 
ATOM   17   C CB  . PRO A 1 6   ? 21.888  29.253 1.848  1.00 59.65 ? 329 PRO A CB  1 
ATOM   18   C CG  . PRO A 1 6   ? 22.949  30.271 1.616  1.00 57.26 ? 329 PRO A CG  1 
ATOM   19   C CD  . PRO A 1 6   ? 24.135  29.811 2.404  1.00 55.60 ? 329 PRO A CD  1 
ATOM   20   N N   . GLU A 1 7   ? 22.864  26.423 2.922  1.00 73.42 ? 330 GLU A N   1 
ATOM   21   C CA  . GLU A 1 7   ? 22.745  24.974 3.047  1.00 62.53 ? 330 GLU A CA  1 
ATOM   22   C C   . GLU A 1 7   ? 22.984  24.522 4.482  1.00 60.92 ? 330 GLU A C   1 
ATOM   23   O O   . GLU A 1 7   ? 22.298  23.616 4.967  1.00 48.79 ? 330 GLU A O   1 
ATOM   24   C CB  . GLU A 1 7   ? 23.726  24.279 2.102  1.00 61.48 ? 330 GLU A CB  1 
ATOM   25   N N   . PHE A 1 8   ? 23.968  25.125 5.159  1.00 53.92 ? 331 PHE A N   1 
ATOM   26   C CA  . PHE A 1 8   ? 24.160  24.881 6.583  1.00 47.82 ? 331 PHE A CA  1 
ATOM   27   C C   . PHE A 1 8   ? 22.888  25.185 7.360  1.00 47.64 ? 331 PHE A C   1 
ATOM   28   O O   . PHE A 1 8   ? 22.476  24.409 8.235  1.00 42.79 ? 331 PHE A O   1 
ATOM   29   C CB  . PHE A 1 8   ? 25.311  25.735 7.099  1.00 47.63 ? 331 PHE A CB  1 
ATOM   30   C CG  . PHE A 1 8   ? 25.744  25.399 8.489  1.00 50.09 ? 331 PHE A CG  1 
ATOM   31   C CD1 . PHE A 1 8   ? 26.722  24.427 8.710  1.00 50.19 ? 331 PHE A CD1 1 
ATOM   32   C CD2 . PHE A 1 8   ? 25.200  26.063 9.579  1.00 46.21 ? 331 PHE A CD2 1 
ATOM   33   C CE1 . PHE A 1 8   ? 27.137  24.106 10.001 1.00 50.29 ? 331 PHE A CE1 1 
ATOM   34   C CE2 . PHE A 1 8   ? 25.606  25.753 10.873 1.00 42.61 ? 331 PHE A CE2 1 
ATOM   35   C CZ  . PHE A 1 8   ? 26.578  24.769 11.085 1.00 49.43 ? 331 PHE A CZ  1 
ATOM   36   N N   . MET A 1 9   ? 22.245  26.314 7.051  1.00 47.78 ? 332 MET A N   1 
ATOM   37   C CA  . MET A 1 9   ? 21.015  26.659 7.751  1.00 43.88 ? 332 MET A CA  1 
ATOM   38   C C   . MET A 1 9   ? 19.931  25.628 7.493  1.00 39.47 ? 332 MET A C   1 
ATOM   39   O O   . MET A 1 9   ? 19.200  25.259 8.413  1.00 33.61 ? 332 MET A O   1 
ATOM   40   C CB  . MET A 1 9   ? 20.538  28.049 7.345  1.00 47.00 ? 332 MET A CB  1 
ATOM   41   C CG  . MET A 1 9   ? 21.208  29.167 8.115  1.00 54.32 ? 332 MET A CG  1 
ATOM   42   S SD  . MET A 1 9   ? 20.800  30.743 7.362  1.00 68.69 ? 332 MET A SD  1 
ATOM   43   C CE  . MET A 1 9   ? 19.044  30.519 7.129  1.00 53.92 ? 332 MET A CE  1 
ATOM   44   N N   . ASN A 1 10  ? 19.817  25.141 6.249  1.00 38.44 ? 333 ASN A N   1 
ATOM   45   C CA  . ASN A 1 10  ? 18.831  24.099 5.969  1.00 36.08 ? 333 ASN A CA  1 
ATOM   46   C C   . ASN A 1 10  ? 19.066  22.871 6.844  1.00 34.24 ? 333 ASN A C   1 
ATOM   47   O O   . ASN A 1 10  ? 18.110  22.294 7.382  1.00 35.65 ? 333 ASN A O   1 
ATOM   48   C CB  . ASN A 1 10  ? 18.857  23.716 4.487  1.00 39.78 ? 333 ASN A CB  1 
ATOM   49   C CG  . ASN A 1 10  ? 18.030  24.653 3.630  1.00 50.30 ? 333 ASN A CG  1 
ATOM   50   O OD1 . ASN A 1 10  ? 17.278  25.487 4.148  1.00 35.99 ? 333 ASN A OD1 1 
ATOM   51   N ND2 . ASN A 1 10  ? 18.143  24.507 2.311  1.00 61.88 ? 333 ASN A ND2 1 
ATOM   52   N N   . LYS A 1 11  ? 20.335  22.457 6.992  1.00 35.63 ? 334 LYS A N   1 
ATOM   53   C CA  . LYS A 1 11  ? 20.645  21.353 7.896  1.00 36.00 ? 334 LYS A CA  1 
ATOM   54   C C   . LYS A 1 11  ? 20.170  21.663 9.306  1.00 29.24 ? 334 LYS A C   1 
ATOM   55   O O   . LYS A 1 11  ? 19.564  20.807 9.962  1.00 33.15 ? 334 LYS A O   1 
ATOM   56   C CB  . LYS A 1 11  ? 22.144  21.044 7.898  1.00 32.76 ? 334 LYS A CB  1 
ATOM   57   C CG  . LYS A 1 11  ? 22.690  20.483 6.604  1.00 34.19 ? 334 LYS A CG  1 
ATOM   58   C CD  . LYS A 1 11  ? 21.816  19.369 6.046  1.00 40.97 ? 334 LYS A CD  1 
ATOM   59   C CE  . LYS A 1 11  ? 22.377  18.866 4.710  1.00 43.71 ? 334 LYS A CE  1 
ATOM   60   N NZ  . LYS A 1 11  ? 22.273  19.892 3.637  1.00 55.83 ? 334 LYS A NZ  1 
ATOM   61   N N   . GLN A 1 12  ? 20.416  22.888 9.784  1.00 34.99 ? 335 GLN A N   1 
ATOM   62   C CA  . GLN A 1 12  ? 20.049  23.242 11.154 1.00 34.78 ? 335 GLN A CA  1 
ATOM   63   C C   . GLN A 1 12  ? 18.556  23.059 11.405 1.00 30.26 ? 335 GLN A C   1 
ATOM   64   O O   . GLN A 1 12  ? 18.157  22.341 12.330 1.00 30.43 ? 335 GLN A O   1 
ATOM   65   C CB  . GLN A 1 12  ? 20.468  24.679 11.469 1.00 33.03 ? 335 GLN A CB  1 
ATOM   66   C CG  . GLN A 1 12  ? 21.959  24.871 11.639 1.00 39.37 ? 335 GLN A CG  1 
ATOM   67   C CD  . GLN A 1 12  ? 22.329  26.327 11.854 1.00 44.13 ? 335 GLN A CD  1 
ATOM   68   O OE1 . GLN A 1 12  ? 22.038  27.178 11.013 1.00 43.94 ? 335 GLN A OE1 1 
ATOM   69   N NE2 . GLN A 1 12  ? 22.967  26.621 12.984 1.00 42.29 ? 335 GLN A NE2 1 
ATOM   70   N N   . TRP A 1 13  ? 17.700  23.710 10.606 1.00 28.63 ? 336 TRP A N   1 
ATOM   71   C CA  . TRP A 1 13  ? 16.285  23.645 10.936 1.00 31.60 ? 336 TRP A CA  1 
ATOM   72   C C   . TRP A 1 13  ? 15.682  22.283 10.619 1.00 28.22 ? 336 TRP A C   1 
ATOM   73   O O   . TRP A 1 13  ? 14.665  21.930 11.223 1.00 25.43 ? 336 TRP A O   1 
ATOM   74   C CB  . TRP A 1 13  ? 15.499  24.783 10.262 1.00 27.36 ? 336 TRP A CB  1 
ATOM   75   C CG  . TRP A 1 13  ? 15.360  24.767 8.759  1.00 27.54 ? 336 TRP A CG  1 
ATOM   76   C CD1 . TRP A 1 13  ? 16.068  25.514 7.859  1.00 33.13 ? 336 TRP A CD1 1 
ATOM   77   C CD2 . TRP A 1 13  ? 14.402  24.018 7.993  1.00 25.14 ? 336 TRP A CD2 1 
ATOM   78   N NE1 . TRP A 1 13  ? 15.630  25.252 6.577  1.00 35.28 ? 336 TRP A NE1 1 
ATOM   79   C CE2 . TRP A 1 13  ? 14.607  24.338 6.636  1.00 28.55 ? 336 TRP A CE2 1 
ATOM   80   C CE3 . TRP A 1 13  ? 13.408  23.092 8.324  1.00 27.51 ? 336 TRP A CE3 1 
ATOM   81   C CZ2 . TRP A 1 13  ? 13.854  23.767 5.611  1.00 28.53 ? 336 TRP A CZ2 1 
ATOM   82   C CZ3 . TRP A 1 13  ? 12.658  22.531 7.302  1.00 23.68 ? 336 TRP A CZ3 1 
ATOM   83   C CH2 . TRP A 1 13  ? 12.888  22.868 5.967  1.00 29.21 ? 336 TRP A CH2 1 
ATOM   84   N N   . TYR A 1 14  ? 16.292  21.496 9.722  1.00 29.61 ? 337 TYR A N   1 
ATOM   85   C CA  . TYR A 1 14  ? 15.870  20.101 9.612  1.00 31.38 ? 337 TYR A CA  1 
ATOM   86   C C   . TYR A 1 14  ? 16.124  19.358 10.918 1.00 28.61 ? 337 TYR A C   1 
ATOM   87   O O   . TYR A 1 14  ? 15.242  18.638 11.405 1.00 26.96 ? 337 TYR A O   1 
ATOM   88   C CB  . TYR A 1 14  ? 16.569  19.404 8.440  1.00 29.58 ? 337 TYR A CB  1 
ATOM   89   C CG  . TYR A 1 14  ? 15.656  19.175 7.230  1.00 34.61 ? 337 TYR A CG  1 
ATOM   90   C CD1 . TYR A 1 14  ? 15.388  20.200 6.327  1.00 28.96 ? 337 TYR A CD1 1 
ATOM   91   C CD2 . TYR A 1 14  ? 15.058  17.934 6.997  1.00 29.55 ? 337 TYR A CD2 1 
ATOM   92   C CE1 . TYR A 1 14  ? 14.549  19.996 5.227  1.00 31.50 ? 337 TYR A CE1 1 
ATOM   93   C CE2 . TYR A 1 14  ? 14.213  17.723 5.900  1.00 32.25 ? 337 TYR A CE2 1 
ATOM   94   C CZ  . TYR A 1 14  ? 13.964  18.755 5.020  1.00 34.40 ? 337 TYR A CZ  1 
ATOM   95   O OH  . TYR A 1 14  ? 13.131  18.551 3.920  1.00 33.63 ? 337 TYR A OH  1 
ATOM   96   N N   . LEU A 1 15  ? 17.305  19.550 11.524 1.00 24.90 ? 338 LEU A N   1 
ATOM   97   C CA  . LEU A 1 15  ? 17.601  18.922 12.811 1.00 24.89 ? 338 LEU A CA  1 
ATOM   98   C C   . LEU A 1 15  ? 16.631  19.371 13.895 1.00 29.52 ? 338 LEU A C   1 
ATOM   99   O O   . LEU A 1 15  ? 16.191  18.562 14.719 1.00 29.02 ? 338 LEU A O   1 
ATOM   100  C CB  . LEU A 1 15  ? 19.037  19.231 13.230 1.00 30.96 ? 338 LEU A CB  1 
ATOM   101  C CG  . LEU A 1 15  ? 20.064  18.495 12.379 1.00 30.33 ? 338 LEU A CG  1 
ATOM   102  C CD1 . LEU A 1 15  ? 21.443  19.119 12.524 1.00 37.74 ? 338 LEU A CD1 1 
ATOM   103  C CD2 . LEU A 1 15  ? 20.117  17.039 12.801 1.00 33.78 ? 338 LEU A CD2 1 
ATOM   104  N N   . LEU A 1 16  ? 16.283  20.655 13.913 1.00 24.59 ? 339 LEU A N   1 
ATOM   105  C CA  . LEU A 1 16  ? 15.310  21.132 14.892 1.00 23.81 ? 339 LEU A CA  1 
ATOM   106  C C   . LEU A 1 16  ? 13.940  20.493 14.689 1.00 28.19 ? 339 LEU A C   1 
ATOM   107  O O   . LEU A 1 16  ? 13.284  20.103 15.662 1.00 23.50 ? 339 LEU A O   1 
ATOM   108  C CB  . LEU A 1 16  ? 15.199  22.653 14.806 1.00 28.70 ? 339 LEU A CB  1 
ATOM   109  C CG  . LEU A 1 16  ? 16.424  23.421 15.293 1.00 34.17 ? 339 LEU A CG  1 
ATOM   110  C CD1 . LEU A 1 16  ? 16.111  24.912 15.348 1.00 29.07 ? 339 LEU A CD1 1 
ATOM   111  C CD2 . LEU A 1 16  ? 16.887  22.896 16.662 1.00 31.28 ? 339 LEU A CD2 1 
ATOM   112  N N   . ALA A 1 17  ? 13.485  20.409 13.434 1.00 24.02 ? 340 ALA A N   1 
ATOM   113  C CA  . ALA A 1 17  ? 12.203  19.790 13.117 1.00 24.41 ? 340 ALA A CA  1 
ATOM   114  C C   . ALA A 1 17  ? 12.176  18.325 13.529 1.00 27.55 ? 340 ALA A C   1 
ATOM   115  O O   . ALA A 1 17  ? 11.180  17.854 14.086 1.00 29.96 ? 340 ALA A O   1 
ATOM   116  C CB  . ALA A 1 17  ? 11.912  19.938 11.619 1.00 21.85 ? 340 ALA A CB  1 
ATOM   117  N N   . ASN A 1 18  ? 13.253  17.581 13.260 1.00 27.41 ? 341 ASN A N   1 
ATOM   118  C CA  . ASN A 1 18  ? 13.299  16.184 13.683 1.00 30.69 ? 341 ASN A CA  1 
ATOM   119  C C   . ASN A 1 18  ? 13.241  16.060 15.203 1.00 35.20 ? 341 ASN A C   1 
ATOM   120  O O   . ASN A 1 18  ? 12.560  15.186 15.738 1.00 35.37 ? 341 ASN A O   1 
ATOM   121  C CB  . ASN A 1 18  ? 14.545  15.495 13.128 1.00 34.97 ? 341 ASN A CB  1 
ATOM   122  C CG  . ASN A 1 18  ? 14.325  14.938 11.730 1.00 40.20 ? 341 ASN A CG  1 
ATOM   123  O OD1 . ASN A 1 18  ? 13.605  13.954 11.555 1.00 43.60 ? 341 ASN A OD1 1 
ATOM   124  N ND2 . ASN A 1 18  ? 14.931  15.573 10.723 1.00 38.26 ? 341 ASN A ND2 1 
ATOM   125  N N   A GLN A 1 19  ? 13.956  16.943 15.905 0.43 30.87 ? 342 GLN A N   1 
ATOM   126  N N   B GLN A 1 19  ? 13.956  16.940 15.906 0.57 30.77 ? 342 GLN A N   1 
ATOM   127  C CA  A GLN A 1 19  ? 13.911  16.926 17.363 0.43 34.68 ? 342 GLN A CA  1 
ATOM   128  C CA  B GLN A 1 19  ? 13.899  16.909 17.362 0.57 34.69 ? 342 GLN A CA  1 
ATOM   129  C C   A GLN A 1 19  ? 12.525  17.291 17.873 0.43 34.22 ? 342 GLN A C   1 
ATOM   130  C C   B GLN A 1 19  ? 12.508  17.269 17.860 0.57 34.23 ? 342 GLN A C   1 
ATOM   131  O O   A GLN A 1 19  ? 12.045  16.712 18.855 0.43 35.29 ? 342 GLN A O   1 
ATOM   132  O O   B GLN A 1 19  ? 12.007  16.664 18.816 0.57 35.31 ? 342 GLN A O   1 
ATOM   133  C CB  A GLN A 1 19  ? 14.965  17.882 17.919 0.43 32.03 ? 342 GLN A CB  1 
ATOM   134  C CB  B GLN A 1 19  ? 14.944  17.857 17.942 0.57 31.92 ? 342 GLN A CB  1 
ATOM   135  C CG  A GLN A 1 19  ? 16.377  17.330 17.863 0.43 35.79 ? 342 GLN A CG  1 
ATOM   136  C CG  B GLN A 1 19  ? 14.976  17.857 19.459 0.57 41.71 ? 342 GLN A CG  1 
ATOM   137  C CD  A GLN A 1 19  ? 17.427  18.401 17.621 0.43 37.27 ? 342 GLN A CD  1 
ATOM   138  C CD  B GLN A 1 19  ? 16.059  18.749 20.017 0.57 38.38 ? 342 GLN A CD  1 
ATOM   139  O OE1 A GLN A 1 19  ? 17.172  19.592 17.791 0.43 41.01 ? 342 GLN A OE1 1 
ATOM   140  O OE1 B GLN A 1 19  ? 16.865  19.309 19.271 0.57 35.64 ? 342 GLN A OE1 1 
ATOM   141  N NE2 A GLN A 1 19  ? 18.617  17.975 17.215 0.43 34.66 ? 342 GLN A NE2 1 
ATOM   142  N NE2 B GLN A 1 19  ? 16.082  18.891 21.335 0.57 38.39 ? 342 GLN A NE2 1 
ATOM   143  N N   . LEU A 1 20  ? 11.861  18.235 17.208 1.00 29.13 ? 343 LEU A N   1 
ATOM   144  C CA  . LEU A 1 20  ? 10.559  18.695 17.657 1.00 29.81 ? 343 LEU A CA  1 
ATOM   145  C C   . LEU A 1 20  ? 9.465   17.671 17.388 1.00 27.92 ? 343 LEU A C   1 
ATOM   146  O O   . LEU A 1 20  ? 8.607   17.445 18.249 1.00 28.83 ? 343 LEU A O   1 
ATOM   147  C CB  . LEU A 1 20  ? 10.220  20.024 16.984 1.00 29.48 ? 343 LEU A CB  1 
ATOM   148  C CG  . LEU A 1 20  ? 9.068   20.767 17.642 1.00 32.19 ? 343 LEU A CG  1 
ATOM   149  C CD1 . LEU A 1 20  ? 9.103   20.551 19.160 1.00 29.55 ? 343 LEU A CD1 1 
ATOM   150  C CD2 . LEU A 1 20  ? 9.174   22.235 17.299 1.00 31.94 ? 343 LEU A CD2 1 
ATOM   151  N N   . ILE A 1 21  ? 9.461   17.051 16.202 1.00 28.49 ? 344 ILE A N   1 
ATOM   152  C CA  . ILE A 1 21  ? 8.440   16.038 15.934 1.00 30.47 ? 344 ILE A CA  1 
ATOM   153  C C   . ILE A 1 21  ? 8.601   14.870 16.901 1.00 33.15 ? 344 ILE A C   1 
ATOM   154  O O   . ILE A 1 21  ? 7.614   14.225 17.272 1.00 30.90 ? 344 ILE A O   1 
ATOM   155  C CB  . ILE A 1 21  ? 8.469   15.566 14.459 1.00 26.95 ? 344 ILE A CB  1 
ATOM   156  C CG1 . ILE A 1 21  ? 7.136   14.907 14.094 1.00 24.27 ? 344 ILE A CG1 1 
ATOM   157  C CG2 . ILE A 1 21  ? 9.571   14.557 14.230 1.00 31.80 ? 344 ILE A CG2 1 
ATOM   158  C CD1 . ILE A 1 21  ? 5.973   15.850 14.130 1.00 27.48 ? 344 ILE A CD1 1 
ATOM   159  N N   . LEU A 1 22  ? 9.827   14.599 17.355 1.00 31.54 ? 345 LEU A N   1 
ATOM   160  C CA  . LEU A 1 22  ? 10.027  13.536 18.332 1.00 32.86 ? 345 LEU A CA  1 
ATOM   161  C C   . LEU A 1 22  ? 9.506   13.953 19.699 1.00 29.75 ? 345 LEU A C   1 
ATOM   162  O O   . LEU A 1 22  ? 8.894   13.147 20.411 1.00 32.18 ? 345 LEU A O   1 
ATOM   163  C CB  . LEU A 1 22  ? 11.502  13.169 18.405 1.00 37.94 ? 345 LEU A CB  1 
ATOM   164  C CG  . LEU A 1 22  ? 12.003  12.343 17.222 1.00 42.77 ? 345 LEU A CG  1 
ATOM   165  C CD1 . LEU A 1 22  ? 13.494  12.108 17.343 1.00 40.43 ? 345 LEU A CD1 1 
ATOM   166  C CD2 . LEU A 1 22  ? 11.244  11.019 17.128 1.00 43.05 ? 345 LEU A CD2 1 
ATOM   167  N N   . SER A 1 23  ? 9.722   15.216 20.075 1.00 31.79 ? 346 SER A N   1 
ATOM   168  C CA  . SER A 1 23  ? 9.229   15.692 21.363 1.00 26.35 ? 346 SER A CA  1 
ATOM   169  C C   . SER A 1 23  ? 7.710   15.654 21.416 1.00 32.19 ? 346 SER A C   1 
ATOM   170  O O   . SER A 1 23  ? 7.130   15.366 22.469 1.00 29.86 ? 346 SER A O   1 
ATOM   171  C CB  . SER A 1 23  ? 9.745   17.107 21.632 1.00 29.11 ? 346 SER A CB  1 
ATOM   172  O OG  . SER A 1 23  ? 11.165  17.125 21.630 1.00 40.75 ? 346 SER A OG  1 
ATOM   173  N N   . LEU A 1 24  ? 7.046   15.948 20.291 1.00 29.88 ? 347 LEU A N   1 
ATOM   174  C CA  . LEU A 1 24  ? 5.587   15.867 20.245 1.00 28.41 ? 347 LEU A CA  1 
ATOM   175  C C   . LEU A 1 24  ? 5.110   14.429 20.408 1.00 29.98 ? 347 LEU A C   1 
ATOM   176  O O   . LEU A 1 24  ? 4.126   14.173 21.109 1.00 33.52 ? 347 LEU A O   1 
ATOM   177  C CB  . LEU A 1 24  ? 5.062   16.456 18.935 1.00 27.13 ? 347 LEU A CB  1 
ATOM   178  C CG  . LEU A 1 24  ? 5.322   17.941 18.676 1.00 23.48 ? 347 LEU A CG  1 
ATOM   179  C CD1 . LEU A 1 24  ? 4.552   18.412 17.461 1.00 25.46 ? 347 LEU A CD1 1 
ATOM   180  C CD2 . LEU A 1 24  ? 4.974   18.772 19.901 1.00 21.43 ? 347 LEU A CD2 1 
ATOM   181  N N   . SER A 1 25  ? 5.793   13.479 19.761 1.00 34.38 ? 348 SER A N   1 
ATOM   182  C CA  . SER A 1 25  ? 5.404   12.078 19.887 1.00 33.42 ? 348 SER A CA  1 
ATOM   183  C C   . SER A 1 25  ? 5.436   11.614 21.336 1.00 31.91 ? 348 SER A C   1 
ATOM   184  O O   . SER A 1 25  ? 4.655   10.734 21.716 1.00 39.18 ? 348 SER A O   1 
ATOM   185  C CB  . SER A 1 25  ? 6.317   11.193 19.039 1.00 32.17 ? 348 SER A CB  1 
ATOM   186  O OG  . SER A 1 25  ? 6.035   11.343 17.657 1.00 38.74 ? 348 SER A OG  1 
ATOM   187  N N   . LYS A 1 26  ? 6.323   12.177 22.160 1.00 33.40 ? 349 LYS A N   1 
ATOM   188  C CA  . LYS A 1 26  ? 6.472   11.722 23.537 1.00 38.54 ? 349 LYS A CA  1 
ATOM   189  C C   . LYS A 1 26  ? 5.824   12.653 24.559 1.00 42.19 ? 349 LYS A C   1 
ATOM   190  O O   . LYS A 1 26  ? 5.755   12.300 25.740 1.00 41.01 ? 349 LYS A O   1 
ATOM   191  C CB  . LYS A 1 26  ? 7.960   11.498 23.877 1.00 40.31 ? 349 LYS A CB  1 
ATOM   192  C CG  . LYS A 1 26  ? 8.837   12.743 23.982 1.00 46.40 ? 349 LYS A CG  1 
ATOM   193  C CD  . LYS A 1 26  ? 10.238  12.387 24.512 1.00 52.01 ? 349 LYS A CD  1 
ATOM   194  C CE  . LYS A 1 26  ? 11.213  13.576 24.446 1.00 72.80 ? 349 LYS A CE  1 
ATOM   195  N NZ  . LYS A 1 26  ? 10.889  14.698 25.387 1.00 56.70 ? 349 LYS A NZ  1 
ATOM   196  N N   . TYR A 1 27  ? 5.320   13.809 24.142 1.00 37.49 ? 350 TYR A N   1 
ATOM   197  C CA  . TYR A 1 27  ? 4.563   14.644 25.061 1.00 34.22 ? 350 TYR A CA  1 
ATOM   198  C C   . TYR A 1 27  ? 3.269   13.943 25.485 1.00 38.24 ? 350 TYR A C   1 
ATOM   199  O O   . TYR A 1 27  ? 2.726   13.094 24.770 1.00 34.05 ? 350 TYR A O   1 
ATOM   200  C CB  . TYR A 1 27  ? 4.236   15.993 24.416 1.00 40.02 ? 350 TYR A CB  1 
ATOM   201  C CG  . TYR A 1 27  ? 3.755   17.013 25.412 1.00 30.41 ? 350 TYR A CG  1 
ATOM   202  C CD1 . TYR A 1 27  ? 2.407   17.326 25.527 1.00 34.95 ? 350 TYR A CD1 1 
ATOM   203  C CD2 . TYR A 1 27  ? 4.652   17.632 26.272 1.00 35.17 ? 350 TYR A CD2 1 
ATOM   204  C CE1 . TYR A 1 27  ? 1.969   18.248 26.455 1.00 36.15 ? 350 TYR A CE1 1 
ATOM   205  C CE2 . TYR A 1 27  ? 4.229   18.552 27.207 1.00 34.49 ? 350 TYR A CE2 1 
ATOM   206  C CZ  . TYR A 1 27  ? 2.889   18.860 27.297 1.00 35.35 ? 350 TYR A CZ  1 
ATOM   207  O OH  . TYR A 1 27  ? 2.467   19.784 28.231 1.00 43.48 ? 350 TYR A OH  1 
ATOM   208  N N   . GLU A 1 28  ? 2.772   14.319 26.663 1.00 39.51 ? 351 GLU A N   1 
ATOM   209  C CA  . GLU A 1 28  ? 1.532   13.753 27.190 1.00 39.67 ? 351 GLU A CA  1 
ATOM   210  C C   . GLU A 1 28  ? 0.402   13.852 26.165 1.00 43.04 ? 351 GLU A C   1 
ATOM   211  O O   . GLU A 1 28  ? 0.077   14.944 25.680 1.00 42.93 ? 351 GLU A O   1 
ATOM   212  C CB  . GLU A 1 28  ? 1.148   14.468 28.485 1.00 51.62 ? 351 GLU A CB  1 
ATOM   213  C CG  . GLU A 1 28  ? -0.234  14.109 29.014 1.00 72.33 ? 351 GLU A CG  1 
ATOM   214  C CD  . GLU A 1 28  ? -0.363  12.641 29.381 1.00 58.51 ? 351 GLU A CD  1 
ATOM   215  O OE1 . GLU A 1 28  ? 0.654   12.047 29.802 1.00 58.93 ? 351 GLU A OE1 1 
ATOM   216  O OE2 . GLU A 1 28  ? -1.477  12.083 29.247 1.00 56.85 ? 351 GLU A OE2 1 
ATOM   217  N N   . GLY A 1 29  ? -0.188  12.704 25.827 1.00 37.15 ? 352 GLY A N   1 
ATOM   218  C CA  . GLY A 1 29  ? -1.249  12.643 24.842 1.00 32.48 ? 352 GLY A CA  1 
ATOM   219  C C   . GLY A 1 29  ? -0.795  12.672 23.397 1.00 37.45 ? 352 GLY A C   1 
ATOM   220  O O   . GLY A 1 29  ? -1.645  12.704 22.491 1.00 33.16 ? 352 GLY A O   1 
ATOM   221  N N   . GLY A 1 30  ? 0.512   12.667 23.140 1.00 36.29 ? 353 GLY A N   1 
ATOM   222  C CA  . GLY A 1 30  ? 0.979   12.742 21.766 1.00 31.40 ? 353 GLY A CA  1 
ATOM   223  C C   . GLY A 1 30  ? 0.594   11.545 20.921 1.00 35.39 ? 353 GLY A C   1 
ATOM   224  O O   . GLY A 1 30  ? 0.420   11.687 19.706 1.00 36.91 ? 353 GLY A O   1 
ATOM   225  N N   . HIS A 1 31  ? 0.433   10.374 21.544 1.00 35.77 ? 354 HIS A N   1 
ATOM   226  C CA  . HIS A 1 31  ? 0.158   9.152  20.796 1.00 37.13 ? 354 HIS A CA  1 
ATOM   227  C C   . HIS A 1 31  ? -1.103  9.252  19.940 1.00 30.82 ? 354 HIS A C   1 
ATOM   228  O O   . HIS A 1 31  ? -1.186  8.594  18.899 1.00 36.61 ? 354 HIS A O   1 
ATOM   229  C CB  . HIS A 1 31  ? 0.050   7.965  21.756 1.00 33.04 ? 354 HIS A CB  1 
ATOM   230  C CG  . HIS A 1 31  ? -1.051  8.102  22.749 1.00 32.49 ? 354 HIS A CG  1 
ATOM   231  N ND1 . HIS A 1 31  ? -0.916  8.827  23.914 1.00 37.14 ? 354 HIS A ND1 1 
ATOM   232  C CD2 . HIS A 1 31  ? -2.313  7.615  22.753 1.00 35.70 ? 354 HIS A CD2 1 
ATOM   233  C CE1 . HIS A 1 31  ? -2.049  8.785  24.588 1.00 39.01 ? 354 HIS A CE1 1 
ATOM   234  N NE2 . HIS A 1 31  ? -2.914  8.056  23.906 1.00 40.28 ? 354 HIS A NE2 1 
ATOM   235  N N   . ILE A 1 32  ? -2.097  10.057 20.334 1.00 33.59 ? 355 ILE A N   1 
ATOM   236  C CA  . ILE A 1 32  ? -3.317  10.096 19.528 1.00 38.05 ? 355 ILE A CA  1 
ATOM   237  C C   . ILE A 1 32  ? -3.129  10.815 18.201 1.00 34.58 ? 355 ILE A C   1 
ATOM   238  O O   . ILE A 1 32  ? -4.015  10.739 17.344 1.00 34.48 ? 355 ILE A O   1 
ATOM   239  C CB  . ILE A 1 32  ? -4.523  10.742 20.246 1.00 36.66 ? 355 ILE A CB  1 
ATOM   240  C CG1 . ILE A 1 32  ? -4.365  12.255 20.349 1.00 38.56 ? 355 ILE A CG1 1 
ATOM   241  C CG2 . ILE A 1 32  ? -4.739  10.118 21.613 1.00 36.50 ? 355 ILE A CG2 1 
ATOM   242  C CD1 . ILE A 1 32  ? -5.590  12.949 20.914 1.00 33.89 ? 355 ILE A CD1 1 
ATOM   243  N N   . PHE A 1 33  ? -2.007  11.512 18.004 1.00 29.53 ? 356 PHE A N   1 
ATOM   244  C CA  . PHE A 1 33  ? -1.708  12.148 16.730 1.00 31.86 ? 356 PHE A CA  1 
ATOM   245  C C   . PHE A 1 33  ? -0.578  11.456 15.979 1.00 33.89 ? 356 PHE A C   1 
ATOM   246  O O   . PHE A 1 33  ? -0.235  11.891 14.878 1.00 33.28 ? 356 PHE A O   1 
ATOM   247  C CB  . PHE A 1 33  ? -1.364  13.633 16.929 1.00 25.20 ? 356 PHE A CB  1 
ATOM   248  C CG  . PHE A 1 33  ? -2.393  14.398 17.732 1.00 30.69 ? 356 PHE A CG  1 
ATOM   249  C CD1 . PHE A 1 33  ? -3.583  14.837 17.146 1.00 25.64 ? 356 PHE A CD1 1 
ATOM   250  C CD2 . PHE A 1 33  ? -2.167  14.685 19.075 1.00 29.10 ? 356 PHE A CD2 1 
ATOM   251  C CE1 . PHE A 1 33  ? -4.535  15.534 17.890 1.00 28.04 ? 356 PHE A CE1 1 
ATOM   252  C CE2 . PHE A 1 33  ? -3.118  15.384 19.830 1.00 33.05 ? 356 PHE A CE2 1 
ATOM   253  C CZ  . PHE A 1 33  ? -4.296  15.809 19.236 1.00 27.29 ? 356 PHE A CZ  1 
ATOM   254  N N   . GLU A 1 34  ? -0.012  10.375 16.530 1.00 27.42 ? 357 GLU A N   1 
ATOM   255  C CA  . GLU A 1 34  ? 1.150   9.738  15.911 1.00 32.71 ? 357 GLU A CA  1 
ATOM   256  C C   . GLU A 1 34  ? 0.837   9.192  14.524 1.00 32.03 ? 357 GLU A C   1 
ATOM   257  O O   . GLU A 1 34  ? 1.655   9.316  13.605 1.00 29.62 ? 357 GLU A O   1 
ATOM   258  C CB  . GLU A 1 34  ? 1.668   8.616  16.808 1.00 31.25 ? 357 GLU A CB  1 
ATOM   259  C CG  . GLU A 1 34  ? 2.879   7.889  16.252 1.00 32.74 ? 357 GLU A CG  1 
ATOM   260  C CD  . GLU A 1 34  ? 4.115   8.766  16.167 1.00 39.73 ? 357 GLU A CD  1 
ATOM   261  O OE1 . GLU A 1 34  ? 4.152   9.809  16.864 1.00 42.81 ? 357 GLU A OE1 1 
ATOM   262  O OE2 . GLU A 1 34  ? 5.051   8.406  15.411 1.00 40.35 ? 357 GLU A OE2 1 
ATOM   263  N N   . LYS A 1 35  ? -0.321  8.563  14.356 1.00 34.32 ? 358 LYS A N   1 
ATOM   264  C CA  . LYS A 1 35  ? -0.677  7.884  13.121 1.00 35.05 ? 358 LYS A CA  1 
ATOM   265  C C   . LYS A 1 35  ? -2.017  8.417  12.634 1.00 40.21 ? 358 LYS A C   1 
ATOM   266  O O   . LYS A 1 35  ? -2.778  9.016  13.397 1.00 41.24 ? 358 LYS A O   1 
ATOM   267  C CB  . LYS A 1 35  ? -0.731  6.361  13.331 1.00 35.00 ? 358 LYS A CB  1 
ATOM   268  C CG  . LYS A 1 35  ? 0.647   5.715  13.518 1.00 37.26 ? 358 LYS A CG  1 
ATOM   269  C CD  . LYS A 1 35  ? 0.576   4.387  14.285 1.00 55.68 ? 358 LYS A CD  1 
ATOM   270  C CE  . LYS A 1 35  ? 0.849   3.167  13.402 1.00 49.49 ? 358 LYS A CE  1 
ATOM   271  N NZ  . LYS A 1 35  ? -0.375  2.653  12.725 1.00 62.45 ? 358 LYS A NZ  1 
ATOM   272  N N   . LEU A 1 36  ? -2.297  8.227  11.345 1.00 40.61 ? 359 LEU A N   1 
ATOM   273  C CA  . LEU A 1 36  ? -3.587  8.655  10.821 1.00 37.69 ? 359 LEU A CA  1 
ATOM   274  C C   . LEU A 1 36  ? -4.699  7.873  11.509 1.00 44.25 ? 359 LEU A C   1 
ATOM   275  O O   . LEU A 1 36  ? -4.525  6.711  11.885 1.00 41.13 ? 359 LEU A O   1 
ATOM   276  C CB  . LEU A 1 36  ? -3.641  8.472  9.303  1.00 33.18 ? 359 LEU A CB  1 
ATOM   277  C CG  . LEU A 1 36  ? -2.745  9.461  8.542  1.00 37.23 ? 359 LEU A CG  1 
ATOM   278  C CD1 . LEU A 1 36  ? -2.698  9.163  7.061  1.00 32.81 ? 359 LEU A CD1 1 
ATOM   279  C CD2 . LEU A 1 36  ? -3.186  10.911 8.780  1.00 31.85 ? 359 LEU A CD2 1 
ATOM   280  N N   . VAL A 1 37  ? -5.839  8.532  11.711 1.00 48.57 ? 360 VAL A N   1 
ATOM   281  C CA  . VAL A 1 37  ? -6.935  7.926  12.456 1.00 50.85 ? 360 VAL A CA  1 
ATOM   282  C C   . VAL A 1 37  ? -7.506  6.762  11.660 1.00 50.68 ? 360 VAL A C   1 
ATOM   283  O O   . VAL A 1 37  ? -7.752  6.876  10.452 1.00 51.35 ? 360 VAL A O   1 
ATOM   284  C CB  . VAL A 1 37  ? -8.013  8.978  12.769 1.00 49.97 ? 360 VAL A CB  1 
ATOM   285  C CG1 . VAL A 1 37  ? -9.217  8.336  13.438 1.00 56.18 ? 360 VAL A CG1 1 
ATOM   286  C CG2 . VAL A 1 37  ? -7.440  10.079 13.648 1.00 45.88 ? 360 VAL A CG2 1 
ATOM   287  N N   . ASP A 1 38  ? -7.697  5.624  12.328 1.00 59.65 ? 361 ASP A N   1 
ATOM   288  C CA  . ASP A 1 38  ? -8.416  4.495  11.742 1.00 67.62 ? 361 ASP A CA  1 
ATOM   289  C C   . ASP A 1 38  ? -9.883  4.683  12.103 1.00 74.14 ? 361 ASP A C   1 
ATOM   290  O O   . ASP A 1 38  ? -10.294 4.412  13.234 1.00 73.40 ? 361 ASP A O   1 
ATOM   291  C CB  . ASP A 1 38  ? -7.880  3.165  12.255 1.00 65.67 ? 361 ASP A CB  1 
ATOM   292  C CG  . ASP A 1 38  ? -8.179  2.023  11.309 1.00 85.01 ? 361 ASP A CG  1 
ATOM   293  O OD1 . ASP A 1 38  ? -7.676  0.904  11.544 1.00 91.63 ? 361 ASP A OD1 1 
ATOM   294  O OD2 . ASP A 1 38  ? -8.902  2.257  10.316 1.00 96.71 ? 361 ASP A OD2 1 
ATOM   295  N N   . ALA A 1 39  ? -10.674 5.154  11.137 1.00 65.78 ? 362 ALA A N   1 
ATOM   296  C CA  . ALA A 1 39  ? -12.014 5.645  11.444 1.00 66.98 ? 362 ALA A CA  1 
ATOM   297  C C   . ALA A 1 39  ? -12.901 4.555  12.048 1.00 68.34 ? 362 ALA A C   1 
ATOM   298  O O   . ALA A 1 39  ? -13.670 4.821  12.982 1.00 61.93 ? 362 ALA A O   1 
ATOM   299  C CB  . ALA A 1 39  ? -12.646 6.238  10.184 1.00 53.83 ? 362 ALA A CB  1 
ATOM   300  N N   . LYS A 1 40  ? -12.802 3.317  11.546 1.00 63.09 ? 363 LYS A N   1 
ATOM   301  C CA  . LYS A 1 40  ? -13.678 2.258  12.048 1.00 67.94 ? 363 LYS A CA  1 
ATOM   302  C C   . LYS A 1 40  ? -13.266 1.807  13.444 1.00 66.16 ? 363 LYS A C   1 
ATOM   303  O O   . LYS A 1 40  ? -14.124 1.572  14.304 1.00 75.93 ? 363 LYS A O   1 
ATOM   304  C CB  . LYS A 1 40  ? -13.693 1.069  11.083 1.00 54.03 ? 363 LYS A CB  1 
ATOM   305  N N   . LYS A 1 41  ? -11.956 1.697  13.694 1.00 69.47 ? 364 LYS A N   1 
ATOM   306  C CA  . LYS A 1 41  ? -11.475 1.179  14.973 1.00 67.35 ? 364 LYS A CA  1 
ATOM   307  C C   . LYS A 1 41  ? -11.638 2.189  16.106 1.00 75.25 ? 364 LYS A C   1 
ATOM   308  O O   . LYS A 1 41  ? -11.840 1.790  17.259 1.00 78.89 ? 364 LYS A O   1 
ATOM   309  C CB  . LYS A 1 41  ? -10.011 0.751  14.847 1.00 67.09 ? 364 LYS A CB  1 
ATOM   310  N N   . GLN A 1 42  ? -11.544 3.486  15.814 1.00 71.11 ? 365 GLN A N   1 
ATOM   311  C CA  . GLN A 1 42  ? -11.749 4.521  16.821 1.00 71.85 ? 365 GLN A CA  1 
ATOM   312  C C   . GLN A 1 42  ? -13.197 5.002  16.892 1.00 70.31 ? 365 GLN A C   1 
ATOM   313  O O   . GLN A 1 42  ? -13.467 6.014  17.550 1.00 73.80 ? 365 GLN A O   1 
ATOM   314  C CB  . GLN A 1 42  ? -10.811 5.706  16.566 1.00 77.57 ? 365 GLN A CB  1 
ATOM   315  C CG  . GLN A 1 42  ? -9.441  5.557  17.219 1.00 67.62 ? 365 GLN A CG  1 
ATOM   316  C CD  . GLN A 1 42  ? -9.536  5.292  18.717 1.00 79.60 ? 365 GLN A CD  1 
ATOM   317  O OE1 . GLN A 1 42  ? -8.881  4.390  19.241 1.00 74.47 ? 365 GLN A OE1 1 
ATOM   318  N NE2 . GLN A 1 42  ? -10.355 6.080  19.411 1.00 80.32 ? 365 GLN A NE2 1 
ATOM   319  N N   . ASN A 1 43  ? -14.122 4.302  16.228 1.00 65.48 ? 366 ASN A N   1 
ATOM   320  C CA  . ASN A 1 43  ? -15.561 4.574  16.302 1.00 63.02 ? 366 ASN A CA  1 
ATOM   321  C C   . ASN A 1 43  ? -15.901 5.987  15.829 1.00 74.61 ? 366 ASN A C   1 
ATOM   322  O O   . ASN A 1 43  ? -16.814 6.632  16.349 1.00 74.76 ? 366 ASN A O   1 
ATOM   323  C CB  . ASN A 1 43  ? -16.100 4.327  17.714 1.00 61.07 ? 366 ASN A CB  1 
ATOM   324  N N   . CYS A 1 44  ? -15.171 6.470  14.827 1.00 64.73 ? 367 CYS A N   1 
ATOM   325  C CA  . CYS A 1 44  ? -15.437 7.768  14.205 1.00 58.56 ? 367 CYS A CA  1 
ATOM   326  C C   . CYS A 1 44  ? -15.523 7.577  12.695 1.00 55.50 ? 367 CYS A C   1 
ATOM   327  O O   . CYS A 1 44  ? -14.617 7.962  11.944 1.00 55.66 ? 367 CYS A O   1 
ATOM   328  C CB  . CYS A 1 44  ? -14.370 8.792  14.592 1.00 53.47 ? 367 CYS A CB  1 
ATOM   329  S SG  . CYS A 1 44  ? -12.680 8.220  14.393 1.00 65.84 ? 367 CYS A SG  1 
ATOM   330  N N   . PRO A 1 45  ? -16.620 6.990  12.211 1.00 58.71 ? 368 PRO A N   1 
ATOM   331  C CA  . PRO A 1 45  ? -16.695 6.615  10.790 1.00 52.54 ? 368 PRO A CA  1 
ATOM   332  C C   . PRO A 1 45  ? -16.771 7.796  9.837  1.00 57.84 ? 368 PRO A C   1 
ATOM   333  O O   . PRO A 1 45  ? -16.442 7.629  8.656  1.00 63.83 ? 368 PRO A O   1 
ATOM   334  C CB  . PRO A 1 45  ? -17.974 5.777  10.721 1.00 58.85 ? 368 PRO A CB  1 
ATOM   335  C CG  . PRO A 1 45  ? -18.827 6.351  11.811 1.00 60.73 ? 368 PRO A CG  1 
ATOM   336  C CD  . PRO A 1 45  ? -17.873 6.691  12.926 1.00 61.67 ? 368 PRO A CD  1 
ATOM   337  N N   . ASP A 1 46  ? -17.198 8.971  10.295 1.00 54.42 ? 369 ASP A N   1 
ATOM   338  C CA  . ASP A 1 46  ? -17.314 10.146 9.441  1.00 50.08 ? 369 ASP A CA  1 
ATOM   339  C C   . ASP A 1 46  ? -16.025 10.964 9.366  1.00 40.17 ? 369 ASP A C   1 
ATOM   340  O O   . ASP A 1 46  ? -16.037 12.050 8.777  1.00 41.04 ? 369 ASP A O   1 
ATOM   341  C CB  . ASP A 1 46  ? -18.460 11.041 9.928  1.00 47.26 ? 369 ASP A CB  1 
ATOM   342  C CG  . ASP A 1 46  ? -18.245 11.547 11.347 1.00 51.11 ? 369 ASP A CG  1 
ATOM   343  O OD1 . ASP A 1 46  ? -17.657 10.801 12.163 1.00 52.23 ? 369 ASP A OD1 1 
ATOM   344  O OD2 . ASP A 1 46  ? -18.660 12.689 11.645 1.00 53.82 ? 369 ASP A OD2 1 
ATOM   345  N N   . TYR A 1 47  ? -14.918 10.466 9.927  1.00 39.46 ? 370 TYR A N   1 
ATOM   346  C CA  . TYR A 1 47  ? -13.742 11.311 10.120 1.00 32.23 ? 370 TYR A CA  1 
ATOM   347  C C   . TYR A 1 47  ? -13.247 11.919 8.812  1.00 36.40 ? 370 TYR A C   1 
ATOM   348  O O   . TYR A 1 47  ? -12.910 13.111 8.757  1.00 35.63 ? 370 TYR A O   1 
ATOM   349  C CB  . TYR A 1 47  ? -12.611 10.531 10.795 1.00 37.41 ? 370 TYR A CB  1 
ATOM   350  C CG  . TYR A 1 47  ? -11.413 11.418 11.091 1.00 37.72 ? 370 TYR A CG  1 
ATOM   351  C CD1 . TYR A 1 47  ? -11.425 12.292 12.172 1.00 36.25 ? 370 TYR A CD1 1 
ATOM   352  C CD2 . TYR A 1 47  ? -10.282 11.403 10.272 1.00 38.24 ? 370 TYR A CD2 1 
ATOM   353  C CE1 . TYR A 1 47  ? -10.339 13.120 12.435 1.00 38.51 ? 370 TYR A CE1 1 
ATOM   354  C CE2 . TYR A 1 47  ? -9.197  12.225 10.529 1.00 38.58 ? 370 TYR A CE2 1 
ATOM   355  C CZ  . TYR A 1 47  ? -9.232  13.078 11.611 1.00 36.20 ? 370 TYR A CZ  1 
ATOM   356  O OH  . TYR A 1 47  ? -8.162  13.895 11.875 1.00 31.25 ? 370 TYR A OH  1 
ATOM   357  N N   . TYR A 1 48  ? -13.168 11.117 7.755  1.00 40.39 ? 371 TYR A N   1 
ATOM   358  C CA  . TYR A 1 48  ? -12.606 11.582 6.492  1.00 40.07 ? 371 TYR A CA  1 
ATOM   359  C C   . TYR A 1 48  ? -13.643 12.227 5.588  1.00 38.44 ? 371 TYR A C   1 
ATOM   360  O O   . TYR A 1 48  ? -13.288 12.725 4.513  1.00 38.87 ? 371 TYR A O   1 
ATOM   361  C CB  . TYR A 1 48  ? -11.900 10.421 5.780  1.00 32.27 ? 371 TYR A CB  1 
ATOM   362  C CG  . TYR A 1 48  ? -10.685 9.973  6.561  1.00 34.06 ? 371 TYR A CG  1 
ATOM   363  C CD1 . TYR A 1 48  ? -9.510  10.718 6.533  1.00 33.53 ? 371 TYR A CD1 1 
ATOM   364  C CD2 . TYR A 1 48  ? -10.728 8.838  7.365  1.00 40.34 ? 371 TYR A CD2 1 
ATOM   365  C CE1 . TYR A 1 48  ? -8.396  10.330 7.268  1.00 37.34 ? 371 TYR A CE1 1 
ATOM   366  C CE2 . TYR A 1 48  ? -9.620  8.439  8.099  1.00 40.46 ? 371 TYR A CE2 1 
ATOM   367  C CZ  . TYR A 1 48  ? -8.458  9.189  8.043  1.00 39.48 ? 371 TYR A CZ  1 
ATOM   368  O OH  . TYR A 1 48  ? -7.355  8.805  8.772  1.00 43.01 ? 371 TYR A OH  1 
ATOM   369  N N   . ASP A 1 49  ? -14.913 12.224 6.000  1.00 35.95 ? 372 ASP A N   1 
ATOM   370  C CA  . ASP A 1 49  ? -15.913 13.091 5.393  1.00 37.21 ? 372 ASP A CA  1 
ATOM   371  C C   . ASP A 1 49  ? -15.775 14.528 5.882  1.00 39.98 ? 372 ASP A C   1 
ATOM   372  O O   . ASP A 1 49  ? -16.166 15.456 5.163  1.00 40.25 ? 372 ASP A O   1 
ATOM   373  C CB  . ASP A 1 49  ? -17.312 12.556 5.698  1.00 46.56 ? 372 ASP A CB  1 
ATOM   374  C CG  . ASP A 1 49  ? -17.545 11.172 5.112  1.00 58.83 ? 372 ASP A CG  1 
ATOM   375  O OD1 . ASP A 1 49  ? -17.274 10.981 3.906  1.00 58.39 ? 372 ASP A OD1 1 
ATOM   376  O OD2 . ASP A 1 49  ? -17.983 10.272 5.860  1.00 51.51 ? 372 ASP A OD2 1 
ATOM   377  N N   . VAL A 1 50  ? -15.213 14.717 7.067  1.00 30.26 ? 373 VAL A N   1 
ATOM   378  C CA  . VAL A 1 50  ? -14.969 16.034 7.641  1.00 30.45 ? 373 VAL A CA  1 
ATOM   379  C C   . VAL A 1 50  ? -13.553 16.511 7.358  1.00 33.56 ? 373 VAL A C   1 
ATOM   380  O O   . VAL A 1 50  ? -13.350 17.659 6.952  1.00 32.31 ? 373 VAL A O   1 
ATOM   381  C CB  . VAL A 1 50  ? -15.236 16.003 9.160  1.00 35.16 ? 373 VAL A CB  1 
ATOM   382  C CG1 . VAL A 1 50  ? -14.836 17.326 9.794  1.00 30.84 ? 373 VAL A CG1 1 
ATOM   383  C CG2 . VAL A 1 50  ? -16.685 15.662 9.453  1.00 38.09 ? 373 VAL A CG2 1 
ATOM   384  N N   . ILE A 1 51  ? -12.575 15.632 7.580  1.00 28.61 ? 374 ILE A N   1 
ATOM   385  C CA  . ILE A 1 51  ? -11.154 15.947 7.477  1.00 27.18 ? 374 ILE A CA  1 
ATOM   386  C C   . ILE A 1 51  ? -10.685 15.535 6.084  1.00 28.29 ? 374 ILE A C   1 
ATOM   387  O O   . ILE A 1 51  ? -10.457 14.352 5.805  1.00 29.21 ? 374 ILE A O   1 
ATOM   388  C CB  . ILE A 1 51  ? -10.349 15.246 8.572  1.00 28.35 ? 374 ILE A CB  1 
ATOM   389  C CG1 . ILE A 1 51  ? -10.810 15.715 9.953  1.00 30.84 ? 374 ILE A CG1 1 
ATOM   390  C CG2 . ILE A 1 51  ? -8.857  15.472 8.366  1.00 29.55 ? 374 ILE A CG2 1 
ATOM   391  C CD1 . ILE A 1 51  ? -10.922 17.219 10.081 1.00 26.65 ? 374 ILE A CD1 1 
ATOM   392  N N   . LYS A 1 52  ? -10.526 16.516 5.200  1.00 24.80 ? 375 LYS A N   1 
ATOM   393  C CA  . LYS A 1 52  ? -10.118 16.264 3.824  1.00 30.63 ? 375 LYS A CA  1 
ATOM   394  C C   . LYS A 1 52  ? -8.618  16.458 3.580  1.00 30.24 ? 375 LYS A C   1 
ATOM   395  O O   . LYS A 1 52  ? -8.143  16.218 2.462  1.00 31.30 ? 375 LYS A O   1 
ATOM   396  C CB  . LYS A 1 52  ? -10.942 17.156 2.888  1.00 29.57 ? 375 LYS A CB  1 
ATOM   397  C CG  . LYS A 1 52  ? -12.448 16.884 2.983  1.00 31.66 ? 375 LYS A CG  1 
ATOM   398  C CD  . LYS A 1 52  ? -12.736 15.534 2.357  1.00 35.46 ? 375 LYS A CD  1 
ATOM   399  C CE  . LYS A 1 52  ? -14.175 15.123 2.473  1.00 35.55 ? 375 LYS A CE  1 
ATOM   400  N NZ  . LYS A 1 52  ? -14.412 13.912 1.636  1.00 37.05 ? 375 LYS A NZ  1 
ATOM   401  N N   . ASN A 1 53  ? -7.855  16.858 4.599  1.00 31.73 ? 376 ASN A N   1 
ATOM   402  C CA  . ASN A 1 53  ? -6.405  17.027 4.507  1.00 28.91 ? 376 ASN A CA  1 
ATOM   403  C C   . ASN A 1 53  ? -5.785  16.428 5.771  1.00 28.07 ? 376 ASN A C   1 
ATOM   404  O O   . ASN A 1 53  ? -5.315  17.152 6.650  1.00 25.18 ? 376 ASN A O   1 
ATOM   405  C CB  . ASN A 1 53  ? -6.053  18.511 4.352  1.00 28.76 ? 376 ASN A CB  1 
ATOM   406  C CG  . ASN A 1 53  ? -4.602  18.753 3.948  1.00 52.58 ? 376 ASN A CG  1 
ATOM   407  O OD1 . ASN A 1 53  ? -4.171  19.904 3.864  1.00 46.27 ? 376 ASN A OD1 1 
ATOM   408  N ND2 . ASN A 1 53  ? -3.847  17.684 3.689  1.00 34.92 ? 376 ASN A ND2 1 
ATOM   409  N N   . PRO A 1 54  ? -5.825  15.102 5.906  1.00 25.05 ? 377 PRO A N   1 
ATOM   410  C CA  . PRO A 1 54  ? -5.361  14.490 7.159  1.00 30.37 ? 377 PRO A CA  1 
ATOM   411  C C   . PRO A 1 54  ? -3.855  14.580 7.300  1.00 33.62 ? 377 PRO A C   1 
ATOM   412  O O   . PRO A 1 54  ? -3.115  14.671 6.319  1.00 30.51 ? 377 PRO A O   1 
ATOM   413  C CB  . PRO A 1 54  ? -5.820  13.032 7.032  1.00 33.93 ? 377 PRO A CB  1 
ATOM   414  C CG  . PRO A 1 54  ? -5.972  12.808 5.584  1.00 29.33 ? 377 PRO A CG  1 
ATOM   415  C CD  . PRO A 1 54  ? -6.387  14.107 4.980  1.00 35.31 ? 377 PRO A CD  1 
ATOM   416  N N   . MET A 1 55  ? -3.405  14.535 8.550  1.00 26.84 ? 378 MET A N   1 
ATOM   417  C CA  . MET A 1 55  ? -1.992  14.697 8.861  1.00 25.27 ? 378 MET A CA  1 
ATOM   418  C C   . MET A 1 55  ? -1.734  14.054 10.217 1.00 28.70 ? 378 MET A C   1 
ATOM   419  O O   . MET A 1 55  ? -2.612  14.047 11.086 1.00 26.66 ? 378 MET A O   1 
ATOM   420  C CB  . MET A 1 55  ? -1.591  16.182 8.863  1.00 27.44 ? 378 MET A CB  1 
ATOM   421  C CG  . MET A 1 55  ? -0.095  16.449 8.953  1.00 19.31 ? 378 MET A CG  1 
ATOM   422  S SD  . MET A 1 55  ? 0.823   15.721 7.587  1.00 26.96 ? 378 MET A SD  1 
ATOM   423  C CE  . MET A 1 55  ? 0.226   16.641 6.184  1.00 23.57 ? 378 MET A CE  1 
ATOM   424  N N   . SER A 1 56  ? -0.535  13.493 10.376 1.00 28.82 ? 379 SER A N   1 
ATOM   425  C CA  . SER A 1 56  ? -0.119  12.851 11.621 1.00 29.17 ? 379 SER A CA  1 
ATOM   426  C C   . SER A 1 56  ? 1.379   13.050 11.806 1.00 28.39 ? 379 SER A C   1 
ATOM   427  O O   . SER A 1 56  ? 2.095   13.417 10.869 1.00 26.97 ? 379 SER A O   1 
ATOM   428  C CB  . SER A 1 56  ? -0.444  11.352 11.628 1.00 28.94 ? 379 SER A CB  1 
ATOM   429  O OG  . SER A 1 56  ? 0.417   10.657 10.736 1.00 31.41 ? 379 SER A OG  1 
ATOM   430  N N   . PHE A 1 57  ? 1.858   12.773 13.027 1.00 25.57 ? 380 PHE A N   1 
ATOM   431  C CA  . PHE A 1 57  ? 3.290   12.874 13.281 1.00 25.34 ? 380 PHE A CA  1 
ATOM   432  C C   . PHE A 1 57  ? 4.077   11.968 12.342 1.00 29.35 ? 380 PHE A C   1 
ATOM   433  O O   . PHE A 1 57  ? 5.159   12.336 11.866 1.00 30.13 ? 380 PHE A O   1 
ATOM   434  C CB  . PHE A 1 57  ? 3.595   12.539 14.747 1.00 28.04 ? 380 PHE A CB  1 
ATOM   435  C CG  . PHE A 1 57  ? 3.006   13.517 15.731 1.00 29.27 ? 380 PHE A CG  1 
ATOM   436  C CD1 . PHE A 1 57  ? 2.685   14.811 15.337 1.00 28.10 ? 380 PHE A CD1 1 
ATOM   437  C CD2 . PHE A 1 57  ? 2.792   13.151 17.047 1.00 24.20 ? 380 PHE A CD2 1 
ATOM   438  C CE1 . PHE A 1 57  ? 2.154   15.714 16.232 1.00 23.26 ? 380 PHE A CE1 1 
ATOM   439  C CE2 . PHE A 1 57  ? 2.258   14.051 17.954 1.00 27.20 ? 380 PHE A CE2 1 
ATOM   440  C CZ  . PHE A 1 57  ? 1.938   15.339 17.542 1.00 25.20 ? 380 PHE A CZ  1 
ATOM   441  N N   . SER A 1 58  ? 3.551   10.777 12.052 1.00 32.14 ? 381 SER A N   1 
ATOM   442  C CA  . SER A 1 58  ? 4.305   9.861  11.201 1.00 34.97 ? 381 SER A CA  1 
ATOM   443  C C   . SER A 1 58  ? 4.388   10.367 9.759  1.00 35.39 ? 381 SER A C   1 
ATOM   444  O O   . SER A 1 58  ? 5.410   10.152 9.093  1.00 31.22 ? 381 SER A O   1 
ATOM   445  C CB  . SER A 1 58  ? 3.689   8.463  11.269 1.00 33.63 ? 381 SER A CB  1 
ATOM   446  O OG  . SER A 1 58  ? 2.306   8.500  10.971 1.00 46.58 ? 381 SER A OG  1 
ATOM   447  N N   . CYS A 1 59  ? 3.342   11.050 9.266  1.00 32.69 ? 382 CYS A N   1 
ATOM   448  C CA  . CYS A 1 59  ? 3.407   11.664 7.936  1.00 34.95 ? 382 CYS A CA  1 
ATOM   449  C C   . CYS A 1 59  ? 4.520   12.696 7.868  1.00 32.49 ? 382 CYS A C   1 
ATOM   450  O O   . CYS A 1 59  ? 5.263   12.767 6.880  1.00 34.30 ? 382 CYS A O   1 
ATOM   451  C CB  . CYS A 1 59  ? 2.082   12.347 7.579  1.00 30.12 ? 382 CYS A CB  1 
ATOM   452  S SG  . CYS A 1 59  ? 0.589   11.330 7.646  1.00 37.57 ? 382 CYS A SG  1 
ATOM   453  N N   . ILE A 1 60  ? 4.619   13.527 8.906  1.00 29.21 ? 383 ILE A N   1 
ATOM   454  C CA  . ILE A 1 60  ? 5.627   14.577 8.954  1.00 30.31 ? 383 ILE A CA  1 
ATOM   455  C C   . ILE A 1 60  ? 7.022   13.972 9.060  1.00 30.12 ? 383 ILE A C   1 
ATOM   456  O O   . ILE A 1 60  ? 7.968   14.426 8.397  1.00 26.19 ? 383 ILE A O   1 
ATOM   457  C CB  . ILE A 1 60  ? 5.291   15.532 10.117 1.00 30.76 ? 383 ILE A CB  1 
ATOM   458  C CG1 . ILE A 1 60  ? 3.936   16.200 9.836  1.00 22.60 ? 383 ILE A CG1 1 
ATOM   459  C CG2 . ILE A 1 60  ? 6.378   16.567 10.323 1.00 25.23 ? 383 ILE A CG2 1 
ATOM   460  C CD1 . ILE A 1 60  ? 3.461   17.177 10.898 1.00 18.20 ? 383 ILE A CD1 1 
ATOM   461  N N   . LYS A 1 61  ? 7.168   12.909 9.851  1.00 31.81 ? 384 LYS A N   1 
ATOM   462  C CA  . LYS A 1 61  ? 8.461   12.243 9.946  1.00 31.36 ? 384 LYS A CA  1 
ATOM   463  C C   . LYS A 1 61  ? 8.888   11.688 8.600  1.00 33.67 ? 384 LYS A C   1 
ATOM   464  O O   . LYS A 1 61  ? 10.080  11.687 8.264  1.00 28.82 ? 384 LYS A O   1 
ATOM   465  C CB  . LYS A 1 61  ? 8.406   11.127 10.987 1.00 35.24 ? 384 LYS A CB  1 
ATOM   466  C CG  . LYS A 1 61  ? 8.313   11.618 12.425 1.00 34.77 ? 384 LYS A CG  1 
ATOM   467  C CD  . LYS A 1 61  ? 8.118   10.446 13.382 1.00 36.06 ? 384 LYS A CD  1 
ATOM   468  C CE  . LYS A 1 61  ? 7.963   10.921 14.815 1.00 40.80 ? 384 LYS A CE  1 
ATOM   469  N NZ  . LYS A 1 61  ? 7.542   9.800  15.696 1.00 30.81 ? 384 LYS A NZ  1 
ATOM   470  N N   . THR A 1 62  ? 7.929   11.199 7.816  1.00 33.96 ? 385 THR A N   1 
ATOM   471  C CA  . THR A 1 62  ? 8.265   10.653 6.507  1.00 36.73 ? 385 THR A CA  1 
ATOM   472  C C   . THR A 1 62  ? 8.703   11.751 5.543  1.00 34.54 ? 385 THR A C   1 
ATOM   473  O O   . THR A 1 62  ? 9.673   11.574 4.793  1.00 33.18 ? 385 THR A O   1 
ATOM   474  C CB  . THR A 1 62  ? 7.071   9.875  5.962  1.00 35.15 ? 385 THR A CB  1 
ATOM   475  O OG1 . THR A 1 62  ? 6.956   8.641  6.683  1.00 39.36 ? 385 THR A OG1 1 
ATOM   476  C CG2 . THR A 1 62  ? 7.228   9.595  4.474  1.00 38.18 ? 385 THR A CG2 1 
ATOM   477  N N   . LYS A 1 63  ? 8.013   12.899 5.558  1.00 29.80 ? 386 LYS A N   1 
ATOM   478  C CA  . LYS A 1 63  ? 8.436   14.017 4.716  1.00 32.30 ? 386 LYS A CA  1 
ATOM   479  C C   . LYS A 1 63  ? 9.807   14.543 5.132  1.00 32.92 ? 386 LYS A C   1 
ATOM   480  O O   . LYS A 1 63  ? 10.603  14.941 4.273  1.00 31.39 ? 386 LYS A O   1 
ATOM   481  C CB  . LYS A 1 63  ? 7.400   15.145 4.755  1.00 27.46 ? 386 LYS A CB  1 
ATOM   482  C CG  . LYS A 1 63  ? 6.052   14.748 4.170  1.00 29.77 ? 386 LYS A CG  1 
ATOM   483  C CD  . LYS A 1 63  ? 4.973   15.781 4.415  1.00 33.21 ? 386 LYS A CD  1 
ATOM   484  C CE  . LYS A 1 63  ? 5.071   16.979 3.490  1.00 34.69 ? 386 LYS A CE  1 
ATOM   485  N NZ  . LYS A 1 63  ? 3.763   17.701 3.451  1.00 27.96 ? 386 LYS A NZ  1 
ATOM   486  N N   . LEU A 1 64  ? 10.092  14.579 6.443  1.00 26.47 ? 387 LEU A N   1 
ATOM   487  C CA  . LEU A 1 64  ? 11.430  14.947 6.892  1.00 29.28 ? 387 LEU A CA  1 
ATOM   488  C C   . LEU A 1 64  ? 12.461  13.945 6.403  1.00 33.44 ? 387 LEU A C   1 
ATOM   489  O O   . LEU A 1 64  ? 13.512  14.333 5.888  1.00 35.38 ? 387 LEU A O   1 
ATOM   490  C CB  . LEU A 1 64  ? 11.479  15.040 8.413  1.00 22.19 ? 387 LEU A CB  1 
ATOM   491  C CG  . LEU A 1 64  ? 10.885  16.303 9.024  1.00 26.47 ? 387 LEU A CG  1 
ATOM   492  C CD1 . LEU A 1 64  ? 10.661  16.163 10.533 1.00 28.78 ? 387 LEU A CD1 1 
ATOM   493  C CD2 . LEU A 1 64  ? 11.846  17.437 8.723  1.00 31.98 ? 387 LEU A CD2 1 
ATOM   494  N N   . LYS A 1 65  ? 12.171  12.648 6.549  1.00 34.07 ? 388 LYS A N   1 
ATOM   495  C CA  . LYS A 1 65  ? 13.105  11.624 6.092  1.00 31.86 ? 388 LYS A CA  1 
ATOM   496  C C   . LYS A 1 65  ? 13.358  11.709 4.586  1.00 40.42 ? 388 LYS A C   1 
ATOM   497  O O   . LYS A 1 65  ? 14.471  11.420 4.129  1.00 40.68 ? 388 LYS A O   1 
ATOM   498  C CB  . LYS A 1 65  ? 12.580  10.236 6.471  1.00 39.72 ? 388 LYS A CB  1 
ATOM   499  C CG  . LYS A 1 65  ? 13.543  9.093  6.159  1.00 43.62 ? 388 LYS A CG  1 
ATOM   500  C CD  . LYS A 1 65  ? 12.927  7.731  6.462  1.00 52.78 ? 388 LYS A CD  1 
ATOM   501  N N   . LYS A 1 66  ? 12.355  12.105 3.801  1.00 34.05 ? 389 LYS A N   1 
ATOM   502  C CA  . LYS A 1 66  ? 12.483  12.185 2.351  1.00 31.87 ? 389 LYS A CA  1 
ATOM   503  C C   . LYS A 1 66  ? 12.938  13.556 1.867  1.00 32.77 ? 389 LYS A C   1 
ATOM   504  O O   . LYS A 1 66  ? 13.058  13.767 0.657  1.00 33.31 ? 389 LYS A O   1 
ATOM   505  C CB  . LYS A 1 66  ? 11.156  11.807 1.685  1.00 36.26 ? 389 LYS A CB  1 
ATOM   506  C CG  . LYS A 1 66  ? 10.756  10.354 1.929  1.00 40.78 ? 389 LYS A CG  1 
ATOM   507  C CD  . LYS A 1 66  ? 9.643   9.891  1.002  1.00 43.78 ? 389 LYS A CD  1 
ATOM   508  C CE  . LYS A 1 66  ? 9.315   8.423  1.255  1.00 45.78 ? 389 LYS A CE  1 
ATOM   509  N NZ  . LYS A 1 66  ? 9.026   7.678  0.001  1.00 60.24 ? 389 LYS A NZ  1 
ATOM   510  N N   . GLY A 1 67  ? 13.221  14.484 2.771  1.00 29.55 ? 390 GLY A N   1 
ATOM   511  C CA  . GLY A 1 67  ? 13.650  15.794 2.315  1.00 29.58 ? 390 GLY A CA  1 
ATOM   512  C C   . GLY A 1 67  ? 12.572  16.550 1.563  1.00 32.91 ? 390 GLY A C   1 
ATOM   513  O O   . GLY A 1 67  ? 12.880  17.268 0.604  1.00 39.69 ? 390 GLY A O   1 
ATOM   514  N N   . GLN A 1 68  ? 11.315  16.416 1.984  1.00 32.89 ? 391 GLN A N   1 
ATOM   515  C CA  . GLN A 1 68  ? 10.215  16.994 1.226  1.00 31.63 ? 391 GLN A CA  1 
ATOM   516  C C   . GLN A 1 68  ? 9.771   18.354 1.743  1.00 34.91 ? 391 GLN A C   1 
ATOM   517  O O   . GLN A 1 68  ? 8.796   18.905 1.222  1.00 38.75 ? 391 GLN A O   1 
ATOM   518  C CB  . GLN A 1 68  ? 9.033   16.028 1.198  1.00 26.60 ? 391 GLN A CB  1 
ATOM   519  C CG  . GLN A 1 68  ? 9.309   14.851 0.295  1.00 36.56 ? 391 GLN A CG  1 
ATOM   520  C CD  . GLN A 1 68  ? 8.194   13.848 0.300  1.00 36.71 ? 391 GLN A CD  1 
ATOM   521  O OE1 . GLN A 1 68  ? 7.631   13.540 1.349  1.00 36.54 ? 391 GLN A OE1 1 
ATOM   522  N NE2 . GLN A 1 68  ? 7.860   13.328 -0.879 1.00 38.91 ? 391 GLN A NE2 1 
ATOM   523  N N   . TYR A 1 69  ? 10.464  18.918 2.732  1.00 27.56 ? 392 TYR A N   1 
ATOM   524  C CA  . TYR A 1 69  ? 10.221  20.290 3.166  1.00 30.34 ? 392 TYR A CA  1 
ATOM   525  C C   . TYR A 1 69  ? 11.294  21.194 2.578  1.00 35.19 ? 392 TYR A C   1 
ATOM   526  O O   . TYR A 1 69  ? 12.494  20.960 2.776  1.00 31.56 ? 392 TYR A O   1 
ATOM   527  C CB  . TYR A 1 69  ? 10.208  20.407 4.685  1.00 26.36 ? 392 TYR A CB  1 
ATOM   528  C CG  . TYR A 1 69  ? 9.034   19.730 5.342  1.00 25.68 ? 392 TYR A CG  1 
ATOM   529  C CD1 . TYR A 1 69  ? 7.738   20.134 5.082  1.00 25.76 ? 392 TYR A CD1 1 
ATOM   530  C CD2 . TYR A 1 69  ? 9.232   18.686 6.234  1.00 22.40 ? 392 TYR A CD2 1 
ATOM   531  C CE1 . TYR A 1 69  ? 6.649   19.502 5.706  1.00 23.85 ? 392 TYR A CE1 1 
ATOM   532  C CE2 . TYR A 1 69  ? 8.171   18.057 6.856  1.00 26.53 ? 392 TYR A CE2 1 
ATOM   533  C CZ  . TYR A 1 69  ? 6.882   18.463 6.588  1.00 25.67 ? 392 TYR A CZ  1 
ATOM   534  O OH  . TYR A 1 69  ? 5.823   17.833 7.203  1.00 22.61 ? 392 TYR A OH  1 
ATOM   535  N N   . ALA A 1 70  ? 10.861  22.226 1.861  1.00 27.49 ? 393 ALA A N   1 
ATOM   536  C CA  . ALA A 1 70  ? 11.785  23.164 1.236  1.00 34.81 ? 393 ALA A CA  1 
ATOM   537  C C   . ALA A 1 70  ? 12.085  24.365 2.117  1.00 36.75 ? 393 ALA A C   1 
ATOM   538  O O   . ALA A 1 70  ? 13.182  24.932 2.029  1.00 29.61 ? 393 ALA A O   1 
ATOM   539  C CB  . ALA A 1 70  ? 11.222  23.659 -0.099 1.00 36.04 ? 393 ALA A CB  1 
ATOM   540  N N   . TYR A 1 71  ? 11.129  24.768 2.945  1.00 30.67 ? 394 TYR A N   1 
ATOM   541  C CA  . TYR A 1 71  ? 11.231  25.934 3.800  1.00 32.55 ? 394 TYR A CA  1 
ATOM   542  C C   . TYR A 1 71  ? 10.854  25.570 5.232  1.00 29.39 ? 394 TYR A C   1 
ATOM   543  O O   . TYR A 1 71  ? 10.046  24.664 5.461  1.00 25.30 ? 394 TYR A O   1 
ATOM   544  C CB  . TYR A 1 71  ? 10.316  27.072 3.318  1.00 32.04 ? 394 TYR A CB  1 
ATOM   545  C CG  . TYR A 1 71  ? 10.560  27.535 1.904  1.00 44.19 ? 394 TYR A CG  1 
ATOM   546  C CD1 . TYR A 1 71  ? 9.794   27.041 0.852  1.00 45.45 ? 394 TYR A CD1 1 
ATOM   547  C CD2 . TYR A 1 71  ? 11.541  28.474 1.616  1.00 47.77 ? 394 TYR A CD2 1 
ATOM   548  C CE1 . TYR A 1 71  ? 10.007  27.459 -0.448 1.00 48.07 ? 394 TYR A CE1 1 
ATOM   549  C CE2 . TYR A 1 71  ? 11.761  28.901 0.315  1.00 55.18 ? 394 TYR A CE2 1 
ATOM   550  C CZ  . TYR A 1 71  ? 10.991  28.388 -0.710 1.00 58.02 ? 394 TYR A CZ  1 
ATOM   551  O OH  . TYR A 1 71  ? 11.200  28.802 -2.004 1.00 64.96 ? 394 TYR A OH  1 
ATOM   552  N N   . PRO A 1 72  ? 11.430  26.276 6.203  1.00 27.11 ? 395 PRO A N   1 
ATOM   553  C CA  . PRO A 1 72  ? 11.066  26.023 7.609  1.00 29.68 ? 395 PRO A CA  1 
ATOM   554  C C   . PRO A 1 72  ? 9.578   26.157 7.908  1.00 29.10 ? 395 PRO A C   1 
ATOM   555  O O   . PRO A 1 72  ? 9.065   25.399 8.739  1.00 26.72 ? 395 PRO A O   1 
ATOM   556  C CB  . PRO A 1 72  ? 11.885  27.074 8.364  1.00 24.89 ? 395 PRO A CB  1 
ATOM   557  C CG  . PRO A 1 72  ? 13.008  27.370 7.503  1.00 28.11 ? 395 PRO A CG  1 
ATOM   558  C CD  . PRO A 1 72  ? 12.578  27.189 6.085  1.00 30.92 ? 395 PRO A CD  1 
ATOM   559  N N   . SER A 1 73  ? 8.867   27.080 7.242  1.00 27.35 ? 396 SER A N   1 
ATOM   560  C CA  . SER A 1 73  ? 7.441   27.295 7.494  1.00 26.56 ? 396 SER A CA  1 
ATOM   561  C C   . SER A 1 73  ? 6.585   26.107 7.066  1.00 25.55 ? 396 SER A C   1 
ATOM   562  O O   . SER A 1 73  ? 5.468   25.919 7.578  1.00 25.61 ? 396 SER A O   1 
ATOM   563  C CB  . SER A 1 73  ? 6.976   28.534 6.739  1.00 26.76 ? 396 SER A CB  1 
ATOM   564  O OG  . SER A 1 73  ? 7.119   28.310 5.344  1.00 29.43 ? 396 SER A OG  1 
ATOM   565  N N   . GLU A 1 74  ? 7.058   25.333 6.095  1.00 26.47 ? 397 GLU A N   1 
ATOM   566  C CA  . GLU A 1 74  ? 6.263   24.222 5.592  1.00 23.99 ? 397 GLU A CA  1 
ATOM   567  C C   . GLU A 1 74  ? 6.117   23.143 6.645  1.00 23.42 ? 397 GLU A C   1 
ATOM   568  O O   . GLU A 1 74  ? 5.062   22.502 6.742  1.00 24.37 ? 397 GLU A O   1 
ATOM   569  C CB  . GLU A 1 74  ? 6.908   23.653 4.332  1.00 25.94 ? 397 GLU A CB  1 
ATOM   570  C CG  . GLU A 1 74  ? 6.765   24.536 3.118  1.00 25.85 ? 397 GLU A CG  1 
ATOM   571  C CD  . GLU A 1 74  ? 7.599   24.042 1.954  1.00 34.38 ? 397 GLU A CD  1 
ATOM   572  O OE1 . GLU A 1 74  ? 8.280   22.998 2.110  1.00 34.15 ? 397 GLU A OE1 1 
ATOM   573  O OE2 . GLU A 1 74  ? 7.581   24.700 0.891  1.00 42.89 ? 397 GLU A OE2 1 
ATOM   574  N N   . PHE A 1 75  ? 7.153   22.943 7.460  1.00 22.62 ? 398 PHE A N   1 
ATOM   575  C CA  . PHE A 1 75  ? 7.059   21.988 8.553  1.00 22.32 ? 398 PHE A CA  1 
ATOM   576  C C   . PHE A 1 75  ? 6.042   22.455 9.590  1.00 25.95 ? 398 PHE A C   1 
ATOM   577  O O   . PHE A 1 75  ? 5.197   21.674 10.050 1.00 20.50 ? 398 PHE A O   1 
ATOM   578  C CB  . PHE A 1 75  ? 8.437   21.796 9.189  1.00 21.79 ? 398 PHE A CB  1 
ATOM   579  C CG  . PHE A 1 75  ? 8.411   21.122 10.541 1.00 22.86 ? 398 PHE A CG  1 
ATOM   580  C CD1 . PHE A 1 75  ? 8.336   19.736 10.636 1.00 21.92 ? 398 PHE A CD1 1 
ATOM   581  C CD2 . PHE A 1 75  ? 8.484   21.869 11.719 1.00 21.14 ? 398 PHE A CD2 1 
ATOM   582  C CE1 . PHE A 1 75  ? 8.331   19.102 11.869 1.00 20.95 ? 398 PHE A CE1 1 
ATOM   583  C CE2 . PHE A 1 75  ? 8.478   21.250 12.960 1.00 26.83 ? 398 PHE A CE2 1 
ATOM   584  C CZ  . PHE A 1 75  ? 8.404   19.853 13.039 1.00 20.05 ? 398 PHE A CZ  1 
ATOM   585  N N   . VAL A 1 76  ? 6.112   23.739 9.965  1.00 22.05 ? 399 VAL A N   1 
ATOM   586  C CA  . VAL A 1 76  ? 5.170   24.273 10.953 1.00 18.06 ? 399 VAL A CA  1 
ATOM   587  C C   . VAL A 1 76  ? 3.741   24.194 10.425 1.00 23.39 ? 399 VAL A C   1 
ATOM   588  O O   . VAL A 1 76  ? 2.809   23.815 11.161 1.00 23.55 ? 399 VAL A O   1 
ATOM   589  C CB  . VAL A 1 76  ? 5.569   25.718 11.339 1.00 25.83 ? 399 VAL A CB  1 
ATOM   590  C CG1 . VAL A 1 76  ? 4.456   26.397 12.154 1.00 23.45 ? 399 VAL A CG1 1 
ATOM   591  C CG2 . VAL A 1 76  ? 6.902   25.735 12.107 1.00 18.32 ? 399 VAL A CG2 1 
ATOM   592  N N   . LYS A 1 77  ? 3.538   24.518 9.135  1.00 24.08 ? 400 LYS A N   1 
ATOM   593  C CA  . LYS A 1 77  ? 2.211   24.442 8.538  1.00 25.00 ? 400 LYS A CA  1 
ATOM   594  C C   . LYS A 1 77  ? 1.637   23.032 8.636  1.00 23.29 ? 400 LYS A C   1 
ATOM   595  O O   . LYS A 1 77  ? 0.451   22.859 8.921  1.00 26.19 ? 400 LYS A O   1 
ATOM   596  C CB  . LYS A 1 77  ? 2.264   24.913 7.086  1.00 27.32 ? 400 LYS A CB  1 
ATOM   597  C CG  . LYS A 1 77  ? 0.913   25.229 6.478  1.00 35.70 ? 400 LYS A CG  1 
ATOM   598  C CD  . LYS A 1 77  ? 1.049   25.719 5.039  1.00 45.36 ? 400 LYS A CD  1 
ATOM   599  C CE  . LYS A 1 77  ? 1.442   24.585 4.100  1.00 48.24 ? 400 LYS A CE  1 
ATOM   600  N N   . ASP A 1 78  ? 2.470   22.007 8.442  1.00 22.12 ? 401 ASP A N   1 
ATOM   601  C CA  . ASP A 1 78  ? 1.950   20.646 8.568  1.00 21.78 ? 401 ASP A CA  1 
ATOM   602  C C   . ASP A 1 78  ? 1.616   20.300 10.017 1.00 24.13 ? 401 ASP A C   1 
ATOM   603  O O   . ASP A 1 78  ? 0.589   19.655 10.283 1.00 22.86 ? 401 ASP A O   1 
ATOM   604  C CB  . ASP A 1 78  ? 2.950   19.650 7.993  1.00 19.64 ? 401 ASP A CB  1 
ATOM   605  C CG  . ASP A 1 78  ? 2.717   19.360 6.499  1.00 25.01 ? 401 ASP A CG  1 
ATOM   606  O OD1 . ASP A 1 78  ? 1.754   19.883 5.881  1.00 24.24 ? 401 ASP A OD1 1 
ATOM   607  O OD2 . ASP A 1 78  ? 3.496   18.570 5.937  1.00 26.32 ? 401 ASP A OD2 1 
ATOM   608  N N   . VAL A 1 79  ? 2.459   20.708 10.974 1.00 21.83 ? 402 VAL A N   1 
ATOM   609  C CA  . VAL A 1 79  ? 2.131   20.437 12.378 1.00 22.30 ? 402 VAL A CA  1 
ATOM   610  C C   . VAL A 1 79  ? 0.871   21.192 12.777 1.00 20.34 ? 402 VAL A C   1 
ATOM   611  O O   . VAL A 1 79  ? -0.038  20.630 13.401 1.00 21.29 ? 402 VAL A O   1 
ATOM   612  C CB  . VAL A 1 79  ? 3.307   20.784 13.310 1.00 21.75 ? 402 VAL A CB  1 
ATOM   613  C CG1 . VAL A 1 79  ? 2.874   20.554 14.778 1.00 19.51 ? 402 VAL A CG1 1 
ATOM   614  C CG2 . VAL A 1 79  ? 4.545   19.947 12.983 1.00 21.02 ? 402 VAL A CG2 1 
ATOM   615  N N   . GLN A 1 80  ? 0.769   22.462 12.380 1.00 21.56 ? 403 GLN A N   1 
ATOM   616  C CA  . GLN A 1 80  ? -0.423  23.221 12.715 1.00 19.88 ? 403 GLN A CA  1 
ATOM   617  C C   . GLN A 1 80  ? -1.672  22.577 12.134 1.00 22.51 ? 403 GLN A C   1 
ATOM   618  O O   . GLN A 1 80  ? -2.747  22.635 12.745 1.00 23.68 ? 403 GLN A O   1 
ATOM   619  C CB  . GLN A 1 80  ? -0.285  24.656 12.213 1.00 22.79 ? 403 GLN A CB  1 
ATOM   620  C CG  . GLN A 1 80  ? -1.413  25.542 12.695 1.00 21.92 ? 403 GLN A CG  1 
ATOM   621  C CD  . GLN A 1 80  ? -1.573  25.483 14.221 1.00 30.60 ? 403 GLN A CD  1 
ATOM   622  O OE1 . GLN A 1 80  ? -0.593  25.502 14.978 1.00 27.75 ? 403 GLN A OE1 1 
ATOM   623  N NE2 . GLN A 1 80  ? -2.820  25.403 14.677 1.00 26.88 ? 403 GLN A NE2 1 
ATOM   624  N N   . LEU A 1 81  ? -1.539  21.957 10.961 1.00 23.86 ? 404 LEU A N   1 
ATOM   625  C CA  . LEU A 1 81  ? -2.663  21.288 10.317 1.00 21.35 ? 404 LEU A CA  1 
ATOM   626  C C   . LEU A 1 81  ? -3.200  20.160 11.195 1.00 20.51 ? 404 LEU A C   1 
ATOM   627  O O   . LEU A 1 81  ? -4.417  19.959 11.277 1.00 22.98 ? 404 LEU A O   1 
ATOM   628  C CB  . LEU A 1 81  ? -2.219  20.776 8.947  1.00 19.14 ? 404 LEU A CB  1 
ATOM   629  C CG  . LEU A 1 81  ? -3.195  19.903 8.180  1.00 22.22 ? 404 LEU A CG  1 
ATOM   630  C CD1 . LEU A 1 81  ? -4.489  20.690 7.892  1.00 21.03 ? 404 LEU A CD1 1 
ATOM   631  C CD2 . LEU A 1 81  ? -2.537  19.369 6.906  1.00 22.77 ? 404 LEU A CD2 1 
ATOM   632  N N   . ILE A 1 82  ? -2.316  19.423 11.869 1.00 23.95 ? 405 ILE A N   1 
ATOM   633  C CA  . ILE A 1 82  ? -2.789  18.419 12.821 1.00 20.74 ? 405 ILE A CA  1 
ATOM   634  C C   . ILE A 1 82  ? -3.686  19.063 13.865 1.00 22.10 ? 405 ILE A C   1 
ATOM   635  O O   . ILE A 1 82  ? -4.760  18.545 14.200 1.00 23.77 ? 405 ILE A O   1 
ATOM   636  C CB  . ILE A 1 82  ? -1.601  17.702 13.483 1.00 19.46 ? 405 ILE A CB  1 
ATOM   637  C CG1 . ILE A 1 82  ? -0.683  17.070 12.428 1.00 23.22 ? 405 ILE A CG1 1 
ATOM   638  C CG2 . ILE A 1 82  ? -2.116  16.663 14.451 1.00 19.05 ? 405 ILE A CG2 1 
ATOM   639  C CD1 . ILE A 1 82  ? 0.483   16.272 13.031 1.00 24.38 ? 405 ILE A CD1 1 
ATOM   640  N N   . PHE A 1 83  ? -3.266  20.200 14.408 1.00 20.57 ? 406 PHE A N   1 
ATOM   641  C CA  . PHE A 1 83  ? -4.042  20.783 15.495 1.00 18.82 ? 406 PHE A CA  1 
ATOM   642  C C   . PHE A 1 83  ? -5.342  21.398 14.991 1.00 24.51 ? 406 PHE A C   1 
ATOM   643  O O   . PHE A 1 83  ? -6.349  21.408 15.717 1.00 23.07 ? 406 PHE A O   1 
ATOM   644  C CB  . PHE A 1 83  ? -3.206  21.816 16.226 1.00 20.92 ? 406 PHE A CB  1 
ATOM   645  C CG  . PHE A 1 83  ? -1.903  21.281 16.738 1.00 21.11 ? 406 PHE A CG  1 
ATOM   646  C CD1 . PHE A 1 83  ? -0.749  22.053 16.674 1.00 28.24 ? 406 PHE A CD1 1 
ATOM   647  C CD2 . PHE A 1 83  ? -1.826  20.015 17.309 1.00 21.91 ? 406 PHE A CD2 1 
ATOM   648  C CE1 . PHE A 1 83  ? 0.461   21.580 17.155 1.00 24.38 ? 406 PHE A CE1 1 
ATOM   649  C CE2 . PHE A 1 83  ? -0.615  19.529 17.794 1.00 26.05 ? 406 PHE A CE2 1 
ATOM   650  C CZ  . PHE A 1 83  ? 0.532   20.316 17.722 1.00 23.39 ? 406 PHE A CZ  1 
ATOM   651  N N   . ASP A 1 84  ? -5.346  21.909 13.759 1.00 25.02 ? 407 ASP A N   1 
ATOM   652  C CA  . ASP A 1 84  ? -6.579  22.432 13.192 1.00 20.12 ? 407 ASP A CA  1 
ATOM   653  C C   . ASP A 1 84  ? -7.577  21.314 12.895 1.00 22.59 ? 407 ASP A C   1 
ATOM   654  O O   . ASP A 1 84  ? -8.785  21.501 13.065 1.00 22.65 ? 407 ASP A O   1 
ATOM   655  C CB  . ASP A 1 84  ? -6.281  23.233 11.924 1.00 23.70 ? 407 ASP A CB  1 
ATOM   656  C CG  . ASP A 1 84  ? -5.547  24.543 12.216 1.00 28.28 ? 407 ASP A CG  1 
ATOM   657  O OD1 . ASP A 1 84  ? -5.506  24.966 13.391 1.00 31.14 ? 407 ASP A OD1 1 
ATOM   658  O OD2 . ASP A 1 84  ? -5.012  25.150 11.265 1.00 31.13 ? 407 ASP A OD2 1 
ATOM   659  N N   . ASN A 1 85  ? -7.105  20.163 12.390 1.00 21.61 ? 408 ASN A N   1 
ATOM   660  C CA  . ASN A 1 85  ? -8.023  19.047 12.172 1.00 21.31 ? 408 ASN A CA  1 
ATOM   661  C C   . ASN A 1 85  ? -8.592  18.568 13.490 1.00 22.17 ? 408 ASN A C   1 
ATOM   662  O O   . ASN A 1 85  ? -9.783  18.243 13.578 1.00 23.12 ? 408 ASN A O   1 
ATOM   663  C CB  . ASN A 1 85  ? -7.331  17.885 11.469 1.00 19.57 ? 408 ASN A CB  1 
ATOM   664  C CG  . ASN A 1 85  ? -7.045  18.163 10.013 1.00 22.41 ? 408 ASN A CG  1 
ATOM   665  O OD1 . ASN A 1 85  ? -7.618  19.068 9.407  1.00 27.86 ? 408 ASN A OD1 1 
ATOM   666  N ND2 . ASN A 1 85  ? -6.158  17.376 9.442  1.00 22.51 ? 408 ASN A ND2 1 
ATOM   667  N N   . CYS A 1 86  ? -7.755  18.524 14.528 1.00 19.76 ? 409 CYS A N   1 
ATOM   668  C CA  . CYS A 1 86  ? -8.213  18.125 15.854 1.00 21.70 ? 409 CYS A CA  1 
ATOM   669  C C   . CYS A 1 86  ? -9.325  19.036 16.354 1.00 22.91 ? 409 CYS A C   1 
ATOM   670  O O   . CYS A 1 86  ? -10.361 18.556 16.828 1.00 22.15 ? 409 CYS A O   1 
ATOM   671  C CB  . CYS A 1 86  ? -7.039  18.128 16.832 1.00 19.41 ? 409 CYS A CB  1 
ATOM   672  S SG  . CYS A 1 86  ? -7.482  17.626 18.467 1.00 22.72 ? 409 CYS A SG  1 
ATOM   673  N N   . SER A 1 87  ? -9.127  20.359 16.275 1.00 22.82 ? 410 SER A N   1 
ATOM   674  C CA  . SER A 1 87  ? -10.122 21.277 16.818 1.00 27.83 ? 410 SER A CA  1 
ATOM   675  C C   . SER A 1 87  ? -11.366 21.360 15.936 1.00 24.78 ? 410 SER A C   1 
ATOM   676  O O   . SER A 1 87  ? -12.464 21.602 16.450 1.00 28.20 ? 410 SER A O   1 
ATOM   677  C CB  . SER A 1 87  ? -9.506  22.662 17.029 1.00 28.70 ? 410 SER A CB  1 
ATOM   678  O OG  . SER A 1 87  ? -9.322  23.339 15.802 1.00 33.92 ? 410 SER A OG  1 
ATOM   679  N N   . LEU A 1 88  ? -11.231 21.147 14.622 1.00 23.21 ? 411 LEU A N   1 
ATOM   680  C CA  . LEU A 1 88  ? -12.403 21.072 13.755 1.00 26.15 ? 411 LEU A CA  1 
ATOM   681  C C   . LEU A 1 88  ? -13.288 19.886 14.122 1.00 25.96 ? 411 LEU A C   1 
ATOM   682  O O   . LEU A 1 88  ? -14.487 20.050 14.376 1.00 27.89 ? 411 LEU A O   1 
ATOM   683  C CB  . LEU A 1 88  ? -11.964 20.991 12.293 1.00 22.33 ? 411 LEU A CB  1 
ATOM   684  C CG  . LEU A 1 88  ? -13.072 20.669 11.283 1.00 23.41 ? 411 LEU A CG  1 
ATOM   685  C CD1 . LEU A 1 88  ? -14.267 21.618 11.437 1.00 24.98 ? 411 LEU A CD1 1 
ATOM   686  C CD2 . LEU A 1 88  ? -12.561 20.666 9.823  1.00 23.52 ? 411 LEU A CD2 1 
ATOM   687  N N   . TYR A 1 89  ? -12.700 18.688 14.218 1.00 23.92 ? 412 TYR A N   1 
ATOM   688  C CA  . TYR A 1 89  ? -13.512 17.479 14.333 1.00 25.70 ? 412 TYR A CA  1 
ATOM   689  C C   . TYR A 1 89  ? -14.064 17.279 15.742 1.00 30.95 ? 412 TYR A C   1 
ATOM   690  O O   . TYR A 1 89  ? -15.195 16.808 15.897 1.00 30.69 ? 412 TYR A O   1 
ATOM   691  C CB  . TYR A 1 89  ? -12.700 16.249 13.908 1.00 25.89 ? 412 TYR A CB  1 
ATOM   692  C CG  . TYR A 1 89  ? -13.518 14.970 13.933 1.00 30.50 ? 412 TYR A CG  1 
ATOM   693  C CD1 . TYR A 1 89  ? -14.364 14.638 12.881 1.00 35.33 ? 412 TYR A CD1 1 
ATOM   694  C CD2 . TYR A 1 89  ? -13.455 14.108 15.022 1.00 32.61 ? 412 TYR A CD2 1 
ATOM   695  C CE1 . TYR A 1 89  ? -15.123 13.468 12.909 1.00 35.31 ? 412 TYR A CE1 1 
ATOM   696  C CE2 . TYR A 1 89  ? -14.207 12.947 15.059 1.00 39.00 ? 412 TYR A CE2 1 
ATOM   697  C CZ  . TYR A 1 89  ? -15.034 12.631 14.003 1.00 40.17 ? 412 TYR A CZ  1 
ATOM   698  O OH  . TYR A 1 89  ? -15.777 11.474 14.048 1.00 45.82 ? 412 TYR A OH  1 
ATOM   699  N N   . ASN A 1 90  ? -13.296 17.622 16.775 1.00 25.25 ? 413 ASN A N   1 
ATOM   700  C CA  . ASN A 1 90  ? -13.662 17.327 18.157 1.00 23.13 ? 413 ASN A CA  1 
ATOM   701  C C   . ASN A 1 90  ? -14.257 18.564 18.826 1.00 29.29 ? 413 ASN A C   1 
ATOM   702  O O   . ASN A 1 90  ? -13.760 19.682 18.640 1.00 27.39 ? 413 ASN A O   1 
ATOM   703  C CB  . ASN A 1 90  ? -12.436 16.836 18.935 1.00 25.03 ? 413 ASN A CB  1 
ATOM   704  C CG  . ASN A 1 90  ? -11.780 15.610 18.292 1.00 21.87 ? 413 ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 90  ? -12.230 14.484 18.504 1.00 26.51 ? 413 ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 90  ? -10.735 15.829 17.498 1.00 22.66 ? 413 ASN A ND2 1 
ATOM   707  N N   . THR A 1 91  ? -15.317 18.359 19.610 1.00 28.50 ? 414 THR A N   1 
ATOM   708  C CA  . THR A 1 91  ? -15.937 19.469 20.334 1.00 24.81 ? 414 THR A CA  1 
ATOM   709  C C   . THR A 1 91  ? -14.965 20.049 21.355 1.00 24.16 ? 414 THR A C   1 
ATOM   710  O O   . THR A 1 91  ? -14.082 19.357 21.872 1.00 26.56 ? 414 THR A O   1 
ATOM   711  C CB  . THR A 1 91  ? -17.234 19.033 21.026 1.00 31.41 ? 414 THR A CB  1 
ATOM   712  O OG1 . THR A 1 91  ? -16.999 17.871 21.835 1.00 36.07 ? 414 THR A OG1 1 
ATOM   713  C CG2 . THR A 1 91  ? -18.297 18.725 20.021 1.00 37.25 ? 414 THR A CG2 1 
ATOM   714  N N   . SER A 1 92  ? -15.147 21.339 21.655 1.00 31.74 ? 415 SER A N   1 
ATOM   715  C CA  . SER A 1 92  ? -14.168 22.053 22.468 1.00 31.16 ? 415 SER A CA  1 
ATOM   716  C C   . SER A 1 92  ? -14.024 21.456 23.863 1.00 26.03 ? 415 SER A C   1 
ATOM   717  O O   . SER A 1 92  ? -12.975 21.612 24.492 1.00 29.35 ? 415 SER A O   1 
ATOM   718  C CB  . SER A 1 92  ? -14.532 23.537 22.562 1.00 31.77 ? 415 SER A CB  1 
ATOM   719  O OG  . SER A 1 92  ? -15.873 23.732 22.969 1.00 43.30 ? 415 SER A OG  1 
ATOM   720  N N   . ASN A 1 93  ? -15.058 20.790 24.388 1.00 26.04 ? 416 ASN A N   1 
ATOM   721  C CA  . ASN A 1 93  ? -14.966 20.246 25.737 1.00 22.72 ? 416 ASN A CA  1 
ATOM   722  C C   . ASN A 1 93  ? -14.597 18.763 25.775 1.00 28.80 ? 416 ASN A C   1 
ATOM   723  O O   . ASN A 1 93  ? -14.629 18.155 26.852 1.00 24.26 ? 416 ASN A O   1 
ATOM   724  C CB  . ASN A 1 93  ? -16.271 20.495 26.507 1.00 27.75 ? 416 ASN A CB  1 
ATOM   725  C CG  . ASN A 1 93  ? -17.503 19.801 25.890 1.00 29.96 ? 416 ASN A CG  1 
ATOM   726  O OD1 . ASN A 1 93  ? -17.396 19.009 24.953 1.00 29.68 ? 416 ASN A OD1 1 
ATOM   727  N ND2 . ASN A 1 93  ? -18.682 20.111 26.427 1.00 33.90 ? 416 ASN A ND2 1 
ATOM   728  N N   . SER A 1 94  ? -14.214 18.182 24.643 1.00 26.21 ? 417 SER A N   1 
ATOM   729  C CA  . SER A 1 94  ? -13.821 16.775 24.579 1.00 25.45 ? 417 SER A CA  1 
ATOM   730  C C   . SER A 1 94  ? -12.375 16.570 25.014 1.00 20.63 ? 417 SER A C   1 
ATOM   731  O O   . SER A 1 94  ? -11.523 17.445 24.842 1.00 23.71 ? 417 SER A O   1 
ATOM   732  C CB  . SER A 1 94  ? -13.982 16.245 23.153 1.00 22.48 ? 417 SER A CB  1 
ATOM   733  O OG  . SER A 1 94  ? -13.034 16.825 22.264 1.00 23.97 ? 417 SER A OG  1 
ATOM   734  N N   . VAL A 1 95  ? -12.091 15.381 25.563 1.00 24.14 ? 418 VAL A N   1 
ATOM   735  C CA  . VAL A 1 95  ? -10.718 15.041 25.950 1.00 29.40 ? 418 VAL A CA  1 
ATOM   736  C C   . VAL A 1 95  ? -9.750  15.267 24.786 1.00 25.75 ? 418 VAL A C   1 
ATOM   737  O O   . VAL A 1 95  ? -8.686  15.888 24.948 1.00 23.84 ? 418 VAL A O   1 
ATOM   738  C CB  . VAL A 1 95  ? -10.656 13.589 26.478 1.00 27.01 ? 418 VAL A CB  1 
ATOM   739  C CG1 . VAL A 1 95  ? -9.208  13.169 26.739 1.00 32.82 ? 418 VAL A CG1 1 
ATOM   740  C CG2 . VAL A 1 95  ? -11.502 13.416 27.742 1.00 25.72 ? 418 VAL A CG2 1 
ATOM   741  N N   . VAL A 1 96  ? -10.112 14.793 23.587 1.00 20.99 ? 419 VAL A N   1 
ATOM   742  C CA  . VAL A 1 96  ? -9.214  14.901 22.447 1.00 20.41 ? 419 VAL A CA  1 
ATOM   743  C C   . VAL A 1 96  ? -8.947  16.362 22.116 1.00 26.62 ? 419 VAL A C   1 
ATOM   744  O O   . VAL A 1 96  ? -7.798  16.758 21.887 1.00 23.51 ? 419 VAL A O   1 
ATOM   745  C CB  . VAL A 1 96  ? -9.783  14.138 21.239 1.00 25.25 ? 419 VAL A CB  1 
ATOM   746  C CG1 . VAL A 1 96  ? -8.953  14.420 20.005 1.00 26.78 ? 419 VAL A CG1 1 
ATOM   747  C CG2 . VAL A 1 96  ? -9.822  12.640 21.540 1.00 29.72 ? 419 VAL A CG2 1 
ATOM   748  N N   . ALA A 1 97  ? -9.988  17.197 22.124 1.00 24.17 ? 420 ALA A N   1 
ATOM   749  C CA  . ALA A 1 97  ? -9.736  18.592 21.793 1.00 23.07 ? 420 ALA A CA  1 
ATOM   750  C C   . ALA A 1 97  ? -8.861  19.243 22.847 1.00 24.29 ? 420 ALA A C   1 
ATOM   751  O O   . ALA A 1 97  ? -7.942  19.998 22.513 1.00 22.08 ? 420 ALA A O   1 
ATOM   752  C CB  . ALA A 1 97  ? -11.035 19.359 21.644 1.00 21.27 ? 420 ALA A CB  1 
ATOM   753  N N   . ILE A 1 98  ? -9.108  18.945 24.123 1.00 21.79 ? 421 ILE A N   1 
ATOM   754  C CA  . ILE A 1 98  ? -8.279  19.524 25.178 1.00 21.23 ? 421 ILE A CA  1 
ATOM   755  C C   . ILE A 1 98  ? -6.834  19.091 25.005 1.00 24.07 ? 421 ILE A C   1 
ATOM   756  O O   . ILE A 1 98  ? -5.907  19.908 25.095 1.00 29.70 ? 421 ILE A O   1 
ATOM   757  C CB  . ILE A 1 98  ? -8.813  19.137 26.568 1.00 24.20 ? 421 ILE A CB  1 
ATOM   758  C CG1 . ILE A 1 98  ? -10.175 19.785 26.843 1.00 23.26 ? 421 ILE A CG1 1 
ATOM   759  C CG2 . ILE A 1 98  ? -7.832  19.581 27.653 1.00 25.37 ? 421 ILE A CG2 1 
ATOM   760  C CD1 . ILE A 1 98  ? -10.940 19.147 27.992 1.00 21.96 ? 421 ILE A CD1 1 
ATOM   761  N N   . THR A 1 99  ? -6.616  17.789 24.779 1.00 23.72 ? 422 THR A N   1 
ATOM   762  C CA  . THR A 1 99  ? -5.270  17.275 24.558 1.00 21.88 ? 422 THR A CA  1 
ATOM   763  C C   . THR A 1 99  ? -4.597  17.966 23.379 1.00 27.87 ? 422 THR A C   1 
ATOM   764  O O   . THR A 1 99  ? -3.414  18.327 23.461 1.00 23.98 ? 422 THR A O   1 
ATOM   765  C CB  . THR A 1 99  ? -5.313  15.764 24.318 1.00 27.62 ? 422 THR A CB  1 
ATOM   766  O OG1 . THR A 1 99  ? -5.912  15.118 25.431 1.00 27.38 ? 422 THR A OG1 1 
ATOM   767  C CG2 . THR A 1 99  ? -3.915  15.205 24.146 1.00 27.28 ? 422 THR A CG2 1 
ATOM   768  N N   . GLY A 1 100 ? -5.331  18.140 22.267 1.00 19.92 ? 423 GLY A N   1 
ATOM   769  C CA  . GLY A 1 100 ? -4.758  18.797 21.109 1.00 21.07 ? 423 GLY A CA  1 
ATOM   770  C C   . GLY A 1 100 ? -4.352  20.226 21.405 1.00 25.73 ? 423 GLY A C   1 
ATOM   771  O O   . GLY A 1 100 ? -3.309  20.697 20.936 1.00 23.98 ? 423 GLY A O   1 
ATOM   772  N N   . LYS A 1 101 ? -5.177  20.936 22.177 1.00 26.26 ? 424 LYS A N   1 
ATOM   773  C CA  . LYS A 1 101 ? -4.847  22.301 22.566 1.00 22.47 ? 424 LYS A CA  1 
ATOM   774  C C   . LYS A 1 101 ? -3.585  22.335 23.420 1.00 24.51 ? 424 LYS A C   1 
ATOM   775  O O   . LYS A 1 101 ? -2.727  23.208 23.241 1.00 23.86 ? 424 LYS A O   1 
ATOM   776  C CB  . LYS A 1 101 ? -6.024  22.912 23.322 1.00 28.39 ? 424 LYS A CB  1 
ATOM   777  C CG  . LYS A 1 101 ? -6.051  24.427 23.328 1.00 37.69 ? 424 LYS A CG  1 
ATOM   778  C CD  . LYS A 1 101 ? -6.400  24.992 21.958 1.00 42.72 ? 424 LYS A CD  1 
ATOM   779  C CE  . LYS A 1 101 ? -7.644  24.338 21.402 1.00 56.29 ? 424 LYS A CE  1 
ATOM   780  N NZ  . LYS A 1 101 ? -8.237  25.087 20.247 1.00 54.52 ? 424 LYS A NZ  1 
ATOM   781  N N   . ASN A 1 102 ? -3.444  21.383 24.349 1.00 24.11 ? 425 ASN A N   1 
ATOM   782  C CA  . ASN A 1 102 ? -2.268  21.347 25.209 1.00 21.12 ? 425 ASN A CA  1 
ATOM   783  C C   . ASN A 1 102 ? -0.994  21.091 24.408 1.00 27.60 ? 425 ASN A C   1 
ATOM   784  O O   . ASN A 1 102 ? 0.038   21.705 24.663 1.00 20.60 ? 425 ASN A O   1 
ATOM   785  C CB  . ASN A 1 102 ? -2.425  20.281 26.281 1.00 20.62 ? 425 ASN A CB  1 
ATOM   786  C CG  . ASN A 1 102 ? -3.453  20.649 27.317 1.00 27.86 ? 425 ASN A CG  1 
ATOM   787  O OD1 . ASN A 1 102 ? -3.871  21.808 27.416 1.00 31.47 ? 425 ASN A OD1 1 
ATOM   788  N ND2 . ASN A 1 102 ? -3.859  19.670 28.112 1.00 25.93 ? 425 ASN A ND2 1 
ATOM   789  N N   A ILE A 1 103 ? -1.051  20.188 23.423 0.41 21.74 ? 426 ILE A N   1 
ATOM   790  N N   B ILE A 1 103 ? -1.052  20.158 23.450 0.59 21.47 ? 426 ILE A N   1 
ATOM   791  C CA  A ILE A 1 103 ? 0.165   19.904 22.663 0.41 20.76 ? 426 ILE A CA  1 
ATOM   792  C CA  B ILE A 1 103 ? 0.124   19.876 22.630 0.59 20.81 ? 426 ILE A CA  1 
ATOM   793  C C   A ILE A 1 103 ? 0.421   20.979 21.607 0.41 20.17 ? 426 ILE A C   1 
ATOM   794  C C   B ILE A 1 103 ? 0.423   21.041 21.701 0.59 20.27 ? 426 ILE A C   1 
ATOM   795  O O   A ILE A 1 103 ? 1.571   21.166 21.179 0.41 21.08 ? 426 ILE A O   1 
ATOM   796  O O   B ILE A 1 103 ? 1.604   21.353 21.456 0.59 21.60 ? 426 ILE A O   1 
ATOM   797  C CB  A ILE A 1 103 ? 0.095   18.499 22.041 0.41 23.71 ? 426 ILE A CB  1 
ATOM   798  C CB  B ILE A 1 103 ? -0.074  18.567 21.844 0.59 23.76 ? 426 ILE A CB  1 
ATOM   799  C CG1 A ILE A 1 103 ? 1.474   18.080 21.523 0.41 25.35 ? 426 ILE A CG1 1 
ATOM   800  C CG1 B ILE A 1 103 ? -0.225  17.398 22.813 0.59 24.48 ? 426 ILE A CG1 1 
ATOM   801  C CG2 A ILE A 1 103 ? -0.937  18.454 20.936 0.41 20.43 ? 426 ILE A CG2 1 
ATOM   802  C CG2 B ILE A 1 103 ? 1.098   18.325 20.884 0.59 24.13 ? 426 ILE A CG2 1 
ATOM   803  C CD1 A ILE A 1 103 ? 1.511   16.692 20.950 0.41 25.86 ? 426 ILE A CD1 1 
ATOM   804  C CD1 B ILE A 1 103 ? -0.404  16.074 22.122 0.59 32.76 ? 426 ILE A CD1 1 
ATOM   805  N N   . GLU A 1 104 ? -0.610  21.702 21.182 1.00 19.86 ? 427 GLU A N   1 
ATOM   806  C CA  . GLU A 1 104 ? -0.408  22.875 20.332 1.00 19.34 ? 427 GLU A CA  1 
ATOM   807  C C   . GLU A 1 104 ? 0.380   23.949 21.080 1.00 20.35 ? 427 GLU A C   1 
ATOM   808  O O   . GLU A 1 104 ? 1.333   24.522 20.546 1.00 21.54 ? 427 GLU A O   1 
ATOM   809  C CB  . GLU A 1 104 ? -1.750  23.428 19.880 1.00 22.70 ? 427 GLU A CB  1 
ATOM   810  C CG  . GLU A 1 104 ? -1.652  24.694 19.056 1.00 18.71 ? 427 GLU A CG  1 
ATOM   811  C CD  . GLU A 1 104 ? -3.021  25.310 18.781 1.00 30.25 ? 427 GLU A CD  1 
ATOM   812  O OE1 . GLU A 1 104 ? -3.822  25.442 19.732 1.00 34.26 ? 427 GLU A OE1 1 
ATOM   813  O OE2 . GLU A 1 104 ? -3.303  25.669 17.614 1.00 28.85 ? 427 GLU A OE2 1 
ATOM   814  N N   . THR A 1 105 ? -0.040  24.253 22.309 1.00 23.99 ? 428 THR A N   1 
ATOM   815  C CA  . THR A 1 105 ? 0.686   25.207 23.148 1.00 23.80 ? 428 THR A CA  1 
ATOM   816  C C   . THR A 1 105 ? 2.151   24.819 23.306 1.00 25.03 ? 428 THR A C   1 
ATOM   817  O O   . THR A 1 105 ? 3.046   25.658 23.153 1.00 27.60 ? 428 THR A O   1 
ATOM   818  C CB  . THR A 1 105 ? 0.005   25.291 24.511 1.00 24.11 ? 428 THR A CB  1 
ATOM   819  O OG1 . THR A 1 105 ? -1.326  25.800 24.332 1.00 28.30 ? 428 THR A OG1 1 
ATOM   820  C CG2 . THR A 1 105 ? 0.809   26.190 25.467 1.00 27.35 ? 428 THR A CG2 1 
ATOM   821  N N   . TYR A 1 106 ? 2.409   23.556 23.647 1.00 21.48 ? 429 TYR A N   1 
ATOM   822  C CA  . TYR A 1 106 ? 3.770   23.049 23.782 1.00 20.75 ? 429 TYR A CA  1 
ATOM   823  C C   . TYR A 1 106 ? 4.583   23.276 22.510 1.00 22.10 ? 429 TYR A C   1 
ATOM   824  O O   . TYR A 1 106 ? 5.714   23.787 22.564 1.00 20.86 ? 429 TYR A O   1 
ATOM   825  C CB  . TYR A 1 106 ? 3.690   21.566 24.131 1.00 21.10 ? 429 TYR A CB  1 
ATOM   826  C CG  . TYR A 1 106 ? 4.995   20.849 24.245 1.00 24.64 ? 429 TYR A CG  1 
ATOM   827  C CD1 . TYR A 1 106 ? 5.861   21.099 25.296 1.00 32.19 ? 429 TYR A CD1 1 
ATOM   828  C CD2 . TYR A 1 106 ? 5.355   19.900 23.308 1.00 31.59 ? 429 TYR A CD2 1 
ATOM   829  C CE1 . TYR A 1 106 ? 7.064   20.423 25.410 1.00 31.25 ? 429 TYR A CE1 1 
ATOM   830  C CE2 . TYR A 1 106 ? 6.556   19.222 23.409 1.00 37.01 ? 429 TYR A CE2 1 
ATOM   831  C CZ  . TYR A 1 106 ? 7.403   19.489 24.460 1.00 35.53 ? 429 TYR A CZ  1 
ATOM   832  O OH  . TYR A 1 106 ? 8.591   18.811 24.561 1.00 40.06 ? 429 TYR A OH  1 
ATOM   833  N N   . PHE A 1 107 ? 4.040   22.856 21.362 1.00 18.52 ? 430 PHE A N   1 
ATOM   834  C CA  . PHE A 1 107 ? 4.715   23.031 20.081 1.00 18.62 ? 430 PHE A CA  1 
ATOM   835  C C   . PHE A 1 107 ? 5.084   24.489 19.856 1.00 21.05 ? 430 PHE A C   1 
ATOM   836  O O   . PHE A 1 107 ? 6.245   24.811 19.578 1.00 23.15 ? 430 PHE A O   1 
ATOM   837  C CB  . PHE A 1 107 ? 3.820   22.523 18.956 1.00 16.94 ? 430 PHE A CB  1 
ATOM   838  C CG  . PHE A 1 107 ? 4.368   22.744 17.577 1.00 22.22 ? 430 PHE A CG  1 
ATOM   839  C CD1 . PHE A 1 107 ? 5.450   21.990 17.116 1.00 20.84 ? 430 PHE A CD1 1 
ATOM   840  C CD2 . PHE A 1 107 ? 3.795   23.691 16.731 1.00 23.42 ? 430 PHE A CD2 1 
ATOM   841  C CE1 . PHE A 1 107 ? 5.965   22.179 15.844 1.00 22.27 ? 430 PHE A CE1 1 
ATOM   842  C CE2 . PHE A 1 107 ? 4.305   23.898 15.439 1.00 23.47 ? 430 PHE A CE2 1 
ATOM   843  C CZ  . PHE A 1 107 ? 5.398   23.133 14.998 1.00 21.45 ? 430 PHE A CZ  1 
ATOM   844  N N   . ASN A 1 108 ? 4.113   25.391 20.011 1.00 20.59 ? 431 ASN A N   1 
ATOM   845  C CA  . ASN A 1 108 ? 4.402   26.799 19.756 1.00 23.43 ? 431 ASN A CA  1 
ATOM   846  C C   . ASN A 1 108 ? 5.433   27.357 20.722 1.00 23.34 ? 431 ASN A C   1 
ATOM   847  O O   . ASN A 1 108 ? 6.195   28.251 20.342 1.00 29.12 ? 431 ASN A O   1 
ATOM   848  C CB  . ASN A 1 108 ? 3.141   27.638 19.838 1.00 23.50 ? 431 ASN A CB  1 
ATOM   849  C CG  . ASN A 1 108 ? 2.260   27.449 18.648 1.00 25.35 ? 431 ASN A CG  1 
ATOM   850  O OD1 . ASN A 1 108 ? 2.739   27.208 17.532 1.00 23.75 ? 431 ASN A OD1 1 
ATOM   851  N ND2 . ASN A 1 108 ? 0.949   27.544 18.863 1.00 26.21 ? 431 ASN A ND2 1 
ATOM   852  N N   . ASN A 1 109 ? 5.490   26.849 21.967 1.00 19.24 ? 432 ASN A N   1 
ATOM   853  C CA  . ASN A 1 109 ? 6.495   27.313 22.911 1.00 22.21 ? 432 ASN A CA  1 
ATOM   854  C C   . ASN A 1 109 ? 7.863   26.695 22.638 1.00 23.65 ? 432 ASN A C   1 
ATOM   855  O O   . ASN A 1 109 ? 8.899   27.313 22.925 1.00 25.41 ? 432 ASN A O   1 
ATOM   856  C CB  . ASN A 1 109 ? 6.036   27.023 24.344 1.00 25.97 ? 432 ASN A CB  1 
ATOM   857  C CG  . ASN A 1 109 ? 4.980   28.004 24.810 1.00 23.88 ? 432 ASN A CG  1 
ATOM   858  O OD1 . ASN A 1 109 ? 4.789   29.046 24.183 1.00 34.79 ? 432 ASN A OD1 1 
ATOM   859  N ND2 . ASN A 1 109 ? 4.303   27.696 25.915 1.00 28.28 ? 432 ASN A ND2 1 
ATOM   860  N N   . GLN A 1 110 ? 7.884   25.487 22.069 1.00 24.95 ? 433 GLN A N   1 
ATOM   861  C CA  . GLN A 1 110 ? 9.136   24.924 21.594 1.00 21.59 ? 433 GLN A CA  1 
ATOM   862  C C   . GLN A 1 110 ? 9.699   25.724 20.431 1.00 22.06 ? 433 GLN A C   1 
ATOM   863  O O   . GLN A 1 110 ? 10.919  25.906 20.344 1.00 29.30 ? 433 GLN A O   1 
ATOM   864  C CB  . GLN A 1 110 ? 8.940   23.470 21.174 1.00 22.94 ? 433 GLN A CB  1 
ATOM   865  C CG  . GLN A 1 110 ? 8.863   22.487 22.338 1.00 23.55 ? 433 GLN A CG  1 
ATOM   866  C CD  . GLN A 1 110 ? 10.195  22.226 23.020 1.00 27.82 ? 433 GLN A CD  1 
ATOM   867  O OE1 . GLN A 1 110 ? 11.151  23.012 22.928 1.00 29.55 ? 433 GLN A OE1 1 
ATOM   868  N NE2 . GLN A 1 110 ? 10.266  21.110 23.731 1.00 38.24 ? 433 GLN A NE2 1 
ATOM   869  N N   . LEU A 1 111 ? 8.846   26.186 19.516 1.00 27.15 ? 434 LEU A N   1 
ATOM   870  C CA  . LEU A 1 111 ? 9.348   27.000 18.415 1.00 24.54 ? 434 LEU A CA  1 
ATOM   871  C C   . LEU A 1 111 ? 10.143  28.183 18.948 1.00 32.36 ? 434 LEU A C   1 
ATOM   872  O O   . LEU A 1 111 ? 11.186  28.551 18.384 1.00 32.29 ? 434 LEU A O   1 
ATOM   873  C CB  . LEU A 1 111 ? 8.184   27.472 17.540 1.00 24.91 ? 434 LEU A CB  1 
ATOM   874  C CG  . LEU A 1 111 ? 7.453   26.376 16.766 1.00 23.05 ? 434 LEU A CG  1 
ATOM   875  C CD1 . LEU A 1 111 ? 6.347   26.946 15.858 1.00 21.81 ? 434 LEU A CD1 1 
ATOM   876  C CD2 . LEU A 1 111 ? 8.464   25.548 15.955 1.00 31.60 ? 434 LEU A CD2 1 
ATOM   877  N N   . ILE A 1 112 ? 9.693   28.736 20.075 1.00 28.40 ? 435 ILE A N   1 
ATOM   878  C CA  . ILE A 1 112 ? 10.350  29.884 20.693 1.00 33.03 ? 435 ILE A CA  1 
ATOM   879  C C   . ILE A 1 112 ? 11.660  29.478 21.355 1.00 33.56 ? 435 ILE A C   1 
ATOM   880  O O   . ILE A 1 112 ? 12.719  30.052 21.068 1.00 33.99 ? 435 ILE A O   1 
ATOM   881  C CB  . ILE A 1 112 ? 9.389   30.541 21.698 1.00 24.92 ? 435 ILE A CB  1 
ATOM   882  C CG1 . ILE A 1 112 ? 8.181   31.145 20.969 1.00 30.57 ? 435 ILE A CG1 1 
ATOM   883  C CG2 . ILE A 1 112 ? 10.139  31.555 22.550 1.00 30.19 ? 435 ILE A CG2 1 
ATOM   884  C CD1 . ILE A 1 112 ? 7.102   31.643 21.905 1.00 31.05 ? 435 ILE A CD1 1 
ATOM   885  N N   . VAL A 1 113 ? 11.616  28.495 22.262 1.00 32.53 ? 436 VAL A N   1 
ATOM   886  C CA  . VAL A 1 113 ? 12.815  28.070 22.982 1.00 30.08 ? 436 VAL A CA  1 
ATOM   887  C C   . VAL A 1 113 ? 13.895  27.588 22.018 1.00 27.26 ? 436 VAL A C   1 
ATOM   888  O O   . VAL A 1 113 ? 15.072  27.925 22.167 1.00 31.53 ? 436 VAL A O   1 
ATOM   889  C CB  . VAL A 1 113 ? 12.476  26.976 24.008 1.00 27.85 ? 436 VAL A CB  1 
ATOM   890  C CG1 . VAL A 1 113 ? 13.729  26.553 24.736 1.00 25.89 ? 436 VAL A CG1 1 
ATOM   891  C CG2 . VAL A 1 113 ? 11.387  27.448 24.963 1.00 28.60 ? 436 VAL A CG2 1 
ATOM   892  N N   . MET A 1 114 ? 13.514  26.756 21.041 1.00 30.11 ? 437 MET A N   1 
ATOM   893  C CA  . MET A 1 114 ? 14.499  26.200 20.115 1.00 36.02 ? 437 MET A CA  1 
ATOM   894  C C   . MET A 1 114 ? 15.005  27.220 19.107 1.00 35.08 ? 437 MET A C   1 
ATOM   895  O O   . MET A 1 114 ? 15.962  26.922 18.385 1.00 35.79 ? 437 MET A O   1 
ATOM   896  C CB  . MET A 1 114 ? 13.909  25.000 19.366 1.00 25.23 ? 437 MET A CB  1 
ATOM   897  C CG  . MET A 1 114 ? 13.731  23.783 20.231 1.00 35.84 ? 437 MET A CG  1 
ATOM   898  S SD  . MET A 1 114 ? 12.861  22.468 19.365 1.00 40.99 ? 437 MET A SD  1 
ATOM   899  C CE  . MET A 1 114 ? 14.193  21.595 18.569 1.00 41.59 ? 437 MET A CE  1 
ATOM   900  N N   . GLY A 1 115 ? 14.402  28.405 19.038 1.00 31.74 ? 438 GLY A N   1 
ATOM   901  C CA  . GLY A 1 115 ? 14.832  29.363 18.042 1.00 33.25 ? 438 GLY A CA  1 
ATOM   902  C C   . GLY A 1 115 ? 14.397  29.025 16.637 1.00 37.21 ? 438 GLY A C   1 
ATOM   903  O O   . GLY A 1 115 ? 14.955  29.573 15.683 1.00 33.99 ? 438 GLY A O   1 
ATOM   904  N N   . TYR A 1 116 ? 13.395  28.145 16.478 1.00 30.01 ? 439 TYR A N   1 
ATOM   905  C CA  . TYR A 1 116 ? 12.957  27.752 15.137 1.00 30.12 ? 439 TYR A CA  1 
ATOM   906  C C   . TYR A 1 116 ? 12.354  28.927 14.394 1.00 29.13 ? 439 TYR A C   1 
ATOM   907  O O   . TYR A 1 116 ? 12.507  29.035 13.171 1.00 29.22 ? 439 TYR A O   1 
ATOM   908  C CB  . TYR A 1 116 ? 11.938  26.615 15.226 1.00 26.57 ? 439 TYR A CB  1 
ATOM   909  C CG  . TYR A 1 116 ? 11.632  25.937 13.919 1.00 21.43 ? 439 TYR A CG  1 
ATOM   910  C CD1 . TYR A 1 116 ? 10.669  26.444 13.054 1.00 24.64 ? 439 TYR A CD1 1 
ATOM   911  C CD2 . TYR A 1 116 ? 12.315  24.782 13.542 1.00 28.13 ? 439 TYR A CD2 1 
ATOM   912  C CE1 . TYR A 1 116 ? 10.374  25.808 11.829 1.00 26.09 ? 439 TYR A CE1 1 
ATOM   913  C CE2 . TYR A 1 116 ? 12.033  24.144 12.338 1.00 31.85 ? 439 TYR A CE2 1 
ATOM   914  C CZ  . TYR A 1 116 ? 11.063  24.660 11.485 1.00 25.33 ? 439 TYR A CZ  1 
ATOM   915  O OH  . TYR A 1 116 ? 10.788  24.031 10.295 1.00 27.31 ? 439 TYR A OH  1 
ATOM   916  N N   . ASN A 1 117 ? 11.688  29.824 15.118 1.00 28.12 ? 440 ASN A N   1 
ATOM   917  C CA  . ASN A 1 117 ? 11.045  30.961 14.474 1.00 31.99 ? 440 ASN A CA  1 
ATOM   918  C C   . ASN A 1 117 ? 12.055  31.871 13.784 1.00 32.48 ? 440 ASN A C   1 
ATOM   919  O O   . ASN A 1 117 ? 11.738  32.470 12.749 1.00 33.41 ? 440 ASN A O   1 
ATOM   920  C CB  . ASN A 1 117 ? 10.218  31.708 15.517 1.00 25.20 ? 440 ASN A CB  1 
ATOM   921  C CG  . ASN A 1 117 ? 8.995   30.899 15.962 1.00 31.72 ? 440 ASN A CG  1 
ATOM   922  O OD1 . ASN A 1 117 ? 8.386   30.183 15.156 1.00 29.40 ? 440 ASN A OD1 1 
ATOM   923  N ND2 . ASN A 1 117 ? 8.635   31.011 17.234 1.00 32.39 ? 440 ASN A ND2 1 
ATOM   924  N N   . ASN A 1 118 ? 13.276  31.971 14.316 1.00 34.54 ? 441 ASN A N   1 
ATOM   925  C CA  . ASN A 1 118 ? 14.308  32.756 13.642 1.00 31.92 ? 441 ASN A CA  1 
ATOM   926  C C   . ASN A 1 118 ? 14.585  32.236 12.238 1.00 33.01 ? 441 ASN A C   1 
ATOM   927  O O   . ASN A 1 118 ? 14.936  33.020 11.350 1.00 33.73 ? 441 ASN A O   1 
ATOM   928  C CB  . ASN A 1 118 ? 15.595  32.759 14.468 1.00 36.60 ? 441 ASN A CB  1 
ATOM   929  C CG  . ASN A 1 118 ? 15.397  33.347 15.849 1.00 49.50 ? 441 ASN A CG  1 
ATOM   930  O OD1 . ASN A 1 118 ? 14.818  34.424 15.995 1.00 52.28 ? 441 ASN A OD1 1 
ATOM   931  N ND2 . ASN A 1 118 ? 15.862  32.637 16.872 1.00 60.64 ? 441 ASN A ND2 1 
ATOM   932  N N   . PHE A 1 119 ? 14.428  30.926 12.012 1.00 29.15 ? 442 PHE A N   1 
ATOM   933  C CA  . PHE A 1 119 ? 14.650  30.380 10.679 1.00 32.13 ? 442 PHE A CA  1 
ATOM   934  C C   . PHE A 1 119 ? 13.523  30.758 9.731  1.00 30.17 ? 442 PHE A C   1 
ATOM   935  O O   . PHE A 1 119 ? 13.769  30.956 8.534  1.00 33.84 ? 442 PHE A O   1 
ATOM   936  C CB  . PHE A 1 119 ? 14.804  28.855 10.739 1.00 33.86 ? 442 PHE A CB  1 
ATOM   937  C CG  . PHE A 1 119 ? 16.116  28.392 11.328 1.00 35.13 ? 442 PHE A CG  1 
ATOM   938  C CD1 . PHE A 1 119 ? 16.274  28.272 12.703 1.00 36.74 ? 442 PHE A CD1 1 
ATOM   939  C CD2 . PHE A 1 119 ? 17.203  28.080 10.502 1.00 35.56 ? 442 PHE A CD2 1 
ATOM   940  C CE1 . PHE A 1 119 ? 17.496  27.850 13.254 1.00 34.78 ? 442 PHE A CE1 1 
ATOM   941  C CE2 . PHE A 1 119 ? 18.421  27.652 11.039 1.00 38.51 ? 442 PHE A CE2 1 
ATOM   942  C CZ  . PHE A 1 119 ? 18.572  27.539 12.414 1.00 35.21 ? 442 PHE A CZ  1 
ATOM   943  N N   . ILE A 1 120 ? 12.287  30.837 10.242 1.00 26.25 ? 443 ILE A N   1 
ATOM   944  C CA  . ILE A 1 120 ? 11.160  31.273 9.423  1.00 34.05 ? 443 ILE A CA  1 
ATOM   945  C C   . ILE A 1 120 ? 11.326  32.739 9.027  1.00 34.42 ? 443 ILE A C   1 
ATOM   946  O O   . ILE A 1 120 ? 11.013  33.132 7.898  1.00 37.73 ? 443 ILE A O   1 
ATOM   947  C CB  . ILE A 1 120 ? 9.838   31.021 10.172 1.00 33.85 ? 443 ILE A CB  1 
ATOM   948  C CG1 . ILE A 1 120 ? 9.657   29.523 10.444 1.00 27.88 ? 443 ILE A CG1 1 
ATOM   949  C CG2 . ILE A 1 120 ? 8.661   31.547 9.372  1.00 39.19 ? 443 ILE A CG2 1 
ATOM   950  C CD1 . ILE A 1 120 ? 8.550   29.191 11.442 1.00 28.00 ? 443 ILE A CD1 1 
ATOM   951  N N   . LEU A 1 121 ? 11.852  33.565 9.934  1.00 39.23 ? 444 LEU A N   1 
ATOM   952  C CA  . LEU A 1 121 ? 12.098  34.964 9.595  1.00 37.09 ? 444 LEU A CA  1 
ATOM   953  C C   . LEU A 1 121 ? 13.184  35.093 8.537  1.00 40.11 ? 444 LEU A C   1 
ATOM   954  O O   . LEU A 1 121 ? 13.057  35.891 7.601  1.00 40.53 ? 444 LEU A O   1 
ATOM   955  C CB  . LEU A 1 121 ? 12.479  35.752 10.848 1.00 43.82 ? 444 LEU A CB  1 
ATOM   956  C CG  . LEU A 1 121 ? 11.344  36.369 11.673 1.00 59.75 ? 444 LEU A CG  1 
ATOM   957  C CD1 . LEU A 1 121 ? 10.286  35.344 12.079 1.00 46.58 ? 444 LEU A CD1 1 
ATOM   958  C CD2 . LEU A 1 121 ? 11.916  37.066 12.900 1.00 59.23 ? 444 LEU A CD2 1 
ATOM   959  N N   . LYS A 1 122 ? 14.267  34.327 8.675  1.00 36.12 ? 445 LYS A N   1 
ATOM   960  C CA  . LYS A 1 122 ? 15.314  34.355 7.664  1.00 33.58 ? 445 LYS A CA  1 
ATOM   961  C C   . LYS A 1 122 ? 14.797  33.856 6.320  1.00 37.34 ? 445 LYS A C   1 
ATOM   962  O O   . LYS A 1 122 ? 15.217  34.354 5.269  1.00 44.53 ? 445 LYS A O   1 
ATOM   963  C CB  . LYS A 1 122 ? 16.505  33.523 8.132  1.00 34.01 ? 445 LYS A CB  1 
ATOM   964  C CG  . LYS A 1 122 ? 17.829  33.933 7.518  1.00 42.68 ? 445 LYS A CG  1 
ATOM   965  N N   . GLU A 1 123 ? 13.885  32.883 6.336  1.00 39.15 ? 446 GLU A N   1 
ATOM   966  C CA  . GLU A 1 123 ? 13.293  32.384 5.104  1.00 39.17 ? 446 GLU A CA  1 
ATOM   967  C C   . GLU A 1 123 ? 12.569  33.494 4.355  1.00 39.84 ? 446 GLU A C   1 
ATOM   968  O O   . GLU A 1 123 ? 12.673  33.588 3.127  1.00 36.53 ? 446 GLU A O   1 
ATOM   969  C CB  . GLU A 1 123 ? 12.339  31.233 5.426  1.00 37.44 ? 446 GLU A CB  1 
ATOM   970  C CG  . GLU A 1 123 ? 11.204  31.066 4.441  1.00 38.42 ? 446 GLU A CG  1 
ATOM   971  C CD  . GLU A 1 123 ? 10.136  30.081 4.916  1.00 41.63 ? 446 GLU A CD  1 
ATOM   972  O OE1 . GLU A 1 123 ? 10.343  29.401 5.939  1.00 30.28 ? 446 GLU A OE1 1 
ATOM   973  O OE2 . GLU A 1 123 ? 9.075   29.986 4.261  1.00 46.36 ? 446 GLU A OE2 1 
ATOM   974  N N   . LYS A 1 124 ? 11.844  34.356 5.082  1.00 40.30 ? 447 LYS A N   1 
ATOM   975  C CA  . LYS A 1 124 ? 11.095  35.434 4.441  1.00 39.72 ? 447 LYS A CA  1 
ATOM   976  C C   . LYS A 1 124 ? 12.029  36.491 3.877  1.00 45.20 ? 447 LYS A C   1 
ATOM   977  O O   . LYS A 1 124 ? 11.818  36.981 2.760  1.00 50.22 ? 447 LYS A O   1 
ATOM   978  C CB  . LYS A 1 124 ? 10.109  36.074 5.425  1.00 37.07 ? 447 LYS A CB  1 
ATOM   979  N N   . LYS A 1 125 ? 13.069  36.853 4.630  1.00 47.44 ? 448 LYS A N   1 
ATOM   980  C CA  . LYS A 1 125 ? 13.996  37.878 4.159  1.00 43.02 ? 448 LYS A CA  1 
ATOM   981  C C   . LYS A 1 125 ? 14.747  37.420 2.919  1.00 45.84 ? 448 LYS A C   1 
ATOM   982  O O   . LYS A 1 125 ? 14.938  38.202 1.983  1.00 49.28 ? 448 LYS A O   1 
ATOM   983  C CB  . LYS A 1 125 ? 14.977  38.258 5.264  1.00 44.35 ? 448 LYS A CB  1 
ATOM   984  C CG  . LYS A 1 125 ? 14.376  39.142 6.355  1.00 50.57 ? 448 LYS A CG  1 
ATOM   985  C CD  . LYS A 1 125 ? 15.466  39.982 7.030  1.00 55.43 ? 448 LYS A CD  1 
ATOM   986  C CE  . LYS A 1 125 ? 14.913  40.907 8.105  1.00 54.96 ? 448 LYS A CE  1 
ATOM   987  N NZ  . LYS A 1 125 ? 14.271  40.135 9.202  1.00 56.61 ? 448 LYS A NZ  1 
ATOM   988  N N   . ILE A 1 126 ? 15.188  36.160 2.893  1.00 43.40 ? 449 ILE A N   1 
ATOM   989  C CA  . ILE A 1 126 ? 15.835  35.636 1.694  1.00 45.81 ? 449 ILE A CA  1 
ATOM   990  C C   . ILE A 1 126 ? 14.904  35.755 0.494  1.00 48.30 ? 449 ILE A C   1 
ATOM   991  O O   . ILE A 1 126 ? 15.316  36.198 -0.586 1.00 43.10 ? 449 ILE A O   1 
ATOM   992  C CB  . ILE A 1 126 ? 16.295  34.184 1.921  1.00 42.93 ? 449 ILE A CB  1 
ATOM   993  C CG1 . ILE A 1 126 ? 17.432  34.170 2.929  1.00 42.97 ? 449 ILE A CG1 1 
ATOM   994  C CG2 . ILE A 1 126 ? 16.771  33.567 0.611  1.00 47.45 ? 449 ILE A CG2 1 
ATOM   995  C CD1 . ILE A 1 126 ? 18.493  35.176 2.582  1.00 52.41 ? 449 ILE A CD1 1 
ATOM   996  N N   . ASN A 1 127 ? 13.625  35.401 0.675  1.00 44.73 ? 450 ASN A N   1 
ATOM   997  C CA  . ASN A 1 127 ? 12.661  35.504 -0.417 1.00 43.73 ? 450 ASN A CA  1 
ATOM   998  C C   . ASN A 1 127 ? 12.520  36.931 -0.925 1.00 54.37 ? 450 ASN A C   1 
ATOM   999  O O   . ASN A 1 127 ? 12.173  37.129 -2.096 1.00 58.48 ? 450 ASN A O   1 
ATOM   1000 C CB  . ASN A 1 127 ? 11.304  34.956 0.027  1.00 46.89 ? 450 ASN A CB  1 
ATOM   1001 C CG  . ASN A 1 127 ? 11.313  33.440 0.175  1.00 51.76 ? 450 ASN A CG  1 
ATOM   1002 O OD1 . ASN A 1 127 ? 12.155  32.750 -0.413 1.00 53.60 ? 450 ASN A OD1 1 
ATOM   1003 N ND2 . ASN A 1 127 ? 10.371  32.913 0.955  1.00 51.65 ? 450 ASN A ND2 1 
ATOM   1004 N N   . ASP A 1 128 ? 12.816  37.924 -0.082 1.00 56.73 ? 451 ASP A N   1 
ATOM   1005 C CA  . ASP A 1 128 ? 12.759  39.320 -0.509 1.00 61.26 ? 451 ASP A CA  1 
ATOM   1006 C C   . ASP A 1 128 ? 14.035  39.743 -1.226 1.00 57.72 ? 451 ASP A C   1 
ATOM   1007 O O   . ASP A 1 128 ? 13.971  40.473 -2.222 1.00 61.74 ? 451 ASP A O   1 
ATOM   1008 C CB  . ASP A 1 128 ? 12.494  40.228 0.695  1.00 63.71 ? 451 ASP A CB  1 
ATOM   1009 C CG  . ASP A 1 128 ? 11.155  39.940 1.364  1.00 82.63 ? 451 ASP A CG  1 
ATOM   1010 O OD1 . ASP A 1 128 ? 10.394  39.085 0.856  1.00 70.69 ? 451 ASP A OD1 1 
ATOM   1011 O OD2 . ASP A 1 128 ? 10.864  40.572 2.403  1.00 75.49 ? 451 ASP A OD2 1 
ATOM   1012 N N   . MET A 1 129 ? 15.202  39.318 -0.731 1.00 56.05 ? 452 MET A N   1 
ATOM   1013 C CA  . MET A 1 129 ? 16.432  39.505 -1.496 1.00 63.23 ? 452 MET A CA  1 
ATOM   1014 C C   . MET A 1 129 ? 16.263  39.007 -2.919 1.00 62.57 ? 452 MET A C   1 
ATOM   1015 O O   . MET A 1 129 ? 16.512  39.737 -3.885 1.00 78.34 ? 452 MET A O   1 
ATOM   1016 C CB  . MET A 1 129 ? 17.595  38.764 -0.843 1.00 59.47 ? 452 MET A CB  1 
ATOM   1017 C CG  . MET A 1 129 ? 18.728  38.451 -1.825 1.00 53.27 ? 452 MET A CG  1 
ATOM   1018 N N   . LEU A 1 130 ? 15.841  37.751 -3.059 1.00 62.14 ? 453 LEU A N   1 
ATOM   1019 C CA  . LEU A 1 130 ? 15.696  37.159 -4.379 1.00 68.12 ? 453 LEU A CA  1 
ATOM   1020 C C   . LEU A 1 130 ? 14.762  37.985 -5.257 1.00 62.26 ? 453 LEU A C   1 
ATOM   1021 O O   . LEU A 1 130 ? 15.036  38.181 -6.448 1.00 63.34 ? 453 LEU A O   1 
ATOM   1022 C CB  . LEU A 1 130 ? 15.205  35.717 -4.236 1.00 51.14 ? 453 LEU A CB  1 
ATOM   1023 C CG  . LEU A 1 130 ? 16.298  34.747 -3.777 1.00 47.87 ? 453 LEU A CG  1 
ATOM   1024 C CD1 . LEU A 1 130 ? 15.709  33.418 -3.328 1.00 51.50 ? 453 LEU A CD1 1 
ATOM   1025 C CD2 . LEU A 1 130 ? 17.309  34.536 -4.893 1.00 52.43 ? 453 LEU A CD2 1 
ATOM   1026 N N   . LYS A 1 131 ? 13.674  38.510 -4.677 1.00 62.59 ? 454 LYS A N   1 
ATOM   1027 C CA  . LYS A 1 131 ? 12.685  39.243 -5.466 1.00 60.71 ? 454 LYS A CA  1 
ATOM   1028 C C   . LYS A 1 131 ? 13.235  40.573 -5.964 1.00 70.59 ? 454 LYS A C   1 
ATOM   1029 O O   . LYS A 1 131 ? 12.848  41.039 -7.043 1.00 73.20 ? 454 LYS A O   1 
ATOM   1030 C CB  . LYS A 1 131 ? 11.413  39.459 -4.642 1.00 58.92 ? 454 LYS A CB  1 
ATOM   1031 N N   . LEU A 1 132 ? 14.135  41.192 -5.203 1.00 67.39 ? 455 LEU A N   1 
ATOM   1032 C CA  . LEU A 1 132 ? 14.837  42.381 -5.669 1.00 72.55 ? 455 LEU A CA  1 
ATOM   1033 C C   . LEU A 1 132 ? 15.833  42.009 -6.759 1.00 76.27 ? 455 LEU A C   1 
ATOM   1034 O O   . LEU A 1 132 ? 15.647  42.370 -7.926 1.00 94.82 ? 455 LEU A O   1 
ATOM   1035 C CB  . LEU A 1 132 ? 15.556  43.069 -4.506 1.00 73.41 ? 455 LEU A CB  1 
ATOM   1036 N N   . VAL A 1 133 ? 16.888  41.288 -6.375 1.00 68.83 ? 456 VAL A N   1 
ATOM   1037 C CA  . VAL A 1 133 ? 17.949  40.826 -7.278 1.00 62.19 ? 456 VAL A CA  1 
ATOM   1038 C C   . VAL A 1 133 ? 17.448  40.337 -8.645 1.00 70.60 ? 456 VAL A C   1 
ATOM   1039 O O   . VAL A 1 133 ? 16.560  39.483 -8.737 1.00 78.24 ? 456 VAL A O   1 
ATOM   1040 C CB  . VAL A 1 133 ? 18.773  39.715 -6.594 1.00 73.72 ? 456 VAL A CB  1 
ATOM   1041 C CG1 . VAL A 1 133 ? 19.624  38.960 -7.615 1.00 78.37 ? 456 VAL A CG1 1 
ATOM   1042 C CG2 . VAL A 1 133 ? 19.639  40.305 -5.494 1.00 71.61 ? 456 VAL A CG2 1 
HETATM 1043 O O6  . BU3 B 2 .   ? 18.848  31.415 11.718 1.00 55.32 ? 501 BU3 A O6  1 
HETATM 1044 C C3  . BU3 B 2 .   ? 19.413  31.012 12.957 1.00 58.14 ? 501 BU3 A C3  1 
HETATM 1045 C C4  . BU3 B 2 .   ? 19.164  32.034 14.051 1.00 53.99 ? 501 BU3 A C4  1 
HETATM 1046 C C2  . BU3 B 2 .   ? 20.912  30.698 12.847 1.00 57.90 ? 501 BU3 A C2  1 
HETATM 1047 O O5  . BU3 B 2 .   ? 21.197  29.857 11.743 1.00 85.07 ? 501 BU3 A O5  1 
HETATM 1048 C C1  . BU3 B 2 .   ? 21.454  30.115 14.142 1.00 43.21 ? 501 BU3 A C1  1 
HETATM 1049 C C15 A I5K C 3 .   ? -7.801  8.393  19.948 0.41 47.29 ? 502 I5K A C15 1 
HETATM 1050 C C15 B I5K C 3 .   ? -6.027  7.868  18.110 0.59 46.11 ? 502 I5K A C15 1 
HETATM 1051 C C13 A I5K C 3 .   ? -6.311  6.493  20.202 0.41 49.93 ? 502 I5K A C13 1 
HETATM 1052 C C13 B I5K C 3 .   ? -6.126  6.373  20.029 0.59 49.98 ? 502 I5K A C13 1 
HETATM 1053 N N   A I5K C 3 .   ? -6.570  10.778 17.382 0.41 41.02 ? 502 I5K A N   1 
HETATM 1054 N N   B I5K C 3 .   ? -6.549  10.697 17.289 0.59 41.05 ? 502 I5K A N   1 
HETATM 1055 C C   A I5K C 3 .   ? -7.166  11.866 16.729 0.41 40.11 ? 502 I5K A C   1 
HETATM 1056 C C   B I5K C 3 .   ? -7.191  11.778 16.667 0.59 40.13 ? 502 I5K A C   1 
HETATM 1057 O O   A I5K C 3 .   ? -9.355  13.772 16.060 0.41 32.73 ? 502 I5K A O   1 
HETATM 1058 O O   B I5K C 3 .   ? -9.484  13.744 16.491 0.59 34.34 ? 502 I5K A O   1 
HETATM 1059 C C1  A I5K C 3 .   ? -6.336  12.821 15.963 0.41 37.91 ? 502 I5K A C1  1 
HETATM 1060 C C1  B I5K C 3 .   ? -6.409  12.777 15.912 0.59 37.92 ? 502 I5K A C1  1 
HETATM 1061 C C10 A I5K C 3 .   ? -7.125  8.802  18.794 0.41 45.82 ? 502 I5K A C10 1 
HETATM 1062 C C10 B I5K C 3 .   ? -7.023  8.679  18.664 0.59 45.94 ? 502 I5K A C10 1 
HETATM 1063 C C11 A I5K C 3 .   ? -6.042  8.041  18.342 0.41 46.07 ? 502 I5K A C11 1 
HETATM 1064 C C11 B I5K C 3 .   ? -7.575  8.326  19.900 0.59 47.29 ? 502 I5K A C11 1 
HETATM 1065 C C12 A I5K C 3 .   ? -5.619  6.882  19.039 0.41 48.14 ? 502 I5K A C12 1 
HETATM 1066 C C12 B I5K C 3 .   ? -7.137  7.177  20.600 0.59 49.79 ? 502 I5K A C12 1 
HETATM 1067 C C14 A I5K C 3 .   ? -7.387  7.252  20.636 0.41 49.62 ? 502 I5K A C14 1 
HETATM 1068 C C14 B I5K C 3 .   ? -5.591  6.731  18.797 0.59 48.02 ? 502 I5K A C14 1 
HETATM 1069 C C2  A I5K C 3 .   ? -8.529  11.779 16.983 0.41 40.42 ? 502 I5K A C2  1 
HETATM 1070 C C2  B I5K C 3 .   ? -8.547  11.645 16.931 0.59 40.48 ? 502 I5K A C2  1 
HETATM 1071 C C3  A I5K C 3 .   ? -9.600  12.687 16.513 0.41 37.69 ? 502 I5K A C3  1 
HETATM 1072 C C3  B I5K C 3 .   ? -9.628  12.552 16.477 0.59 37.65 ? 502 I5K A C3  1 
HETATM 1073 C C4  A I5K C 3 .   ? -11.039 12.207 16.561 0.41 40.26 ? 502 I5K A C4  1 
HETATM 1074 C C4  B I5K C 3 .   ? -10.927 11.977 15.908 0.59 44.95 ? 502 I5K A C4  1 
HETATM 1075 C C5  A I5K C 3 .   ? -11.236 10.795 16.083 0.41 43.33 ? 502 I5K A C5  1 
HETATM 1076 C C5  B I5K C 3 .   ? -11.781 11.146 16.831 0.59 41.92 ? 502 I5K A C5  1 
HETATM 1077 C C6  A I5K C 3 .   ? -11.082 9.768  17.179 0.41 46.31 ? 502 I5K A C6  1 
HETATM 1078 C C6  B I5K C 3 .   ? -11.147 9.832  17.182 0.59 46.33 ? 502 I5K A C6  1 
HETATM 1079 C C7  A I5K C 3 .   ? -10.145 10.230 18.272 0.41 44.49 ? 502 I5K A C7  1 
HETATM 1080 C C7  B I5K C 3 .   ? -10.084 9.988  18.230 0.59 44.69 ? 502 I5K A C7  1 
HETATM 1081 C C8  A I5K C 3 .   ? -8.777  10.616 17.804 0.41 42.64 ? 502 I5K A C8  1 
HETATM 1082 C C8  B I5K C 3 .   ? -8.749  10.448 17.731 0.59 42.70 ? 502 I5K A C8  1 
HETATM 1083 C C9  A I5K C 3 .   ? -7.550  10.007 18.044 0.41 43.46 ? 502 I5K A C9  1 
HETATM 1084 C C9  B I5K C 3 .   ? -7.495  9.882  17.944 0.59 43.55 ? 502 I5K A C9  1 
HETATM 1085 N N1  A I5K C 3 .   ? -4.543  6.130  18.599 0.41 46.29 ? 502 I5K A N1  1 
HETATM 1086 N N1  B I5K C 3 .   ? -7.686  6.839  21.830 0.59 50.03 ? 502 I5K A N1  1 
HETATM 1087 O O   . HOH D 4 .   ? -3.318  15.460 3.683  1.00 36.40 ? 601 HOH A O   1 
HETATM 1088 O O   . HOH D 4 .   ? 12.111  16.734 25.263 1.00 55.39 ? 602 HOH A O   1 
HETATM 1089 O O   . HOH D 4 .   ? 3.424   30.152 22.501 1.00 39.09 ? 603 HOH A O   1 
HETATM 1090 O O   . HOH D 4 .   ? 8.671   31.341 1.707  1.00 45.22 ? 604 HOH A O   1 
HETATM 1091 O O   . HOH D 4 .   ? -8.209  15.141 14.007 1.00 28.25 ? 605 HOH A O   1 
HETATM 1092 O O   . HOH D 4 .   ? -17.240 15.629 16.639 1.00 44.79 ? 606 HOH A O   1 
HETATM 1093 O O   . HOH D 4 .   ? -5.101  27.397 17.239 1.00 37.27 ? 607 HOH A O   1 
HETATM 1094 O O   . HOH D 4 .   ? 0.782   19.463 3.572  1.00 44.83 ? 608 HOH A O   1 
HETATM 1095 O O   . HOH D 4 .   ? 4.939   27.723 4.118  1.00 42.23 ? 609 HOH A O   1 
HETATM 1096 O O   . HOH D 4 .   ? 13.313  15.299 20.617 1.00 39.27 ? 610 HOH A O   1 
HETATM 1097 O O   . HOH D 4 .   ? 5.285   6.770  13.415 1.00 54.13 ? 611 HOH A O   1 
HETATM 1098 O O   . HOH D 4 .   ? -4.317  24.064 9.005  1.00 33.71 ? 612 HOH A O   1 
HETATM 1099 O O   . HOH D 4 .   ? -2.742  26.297 21.960 1.00 35.39 ? 613 HOH A O   1 
HETATM 1100 O O   . HOH D 4 .   ? 5.812   30.145 14.551 1.00 39.17 ? 614 HOH A O   1 
HETATM 1101 O O   . HOH D 4 .   ? 0.997   10.354 26.126 1.00 48.91 ? 615 HOH A O   1 
HETATM 1102 O O   . HOH D 4 .   ? -1.325  18.125 2.993  1.00 43.03 ? 616 HOH A O   1 
HETATM 1103 O O   . HOH D 4 .   ? 23.526  30.348 10.553 1.00 54.05 ? 617 HOH A O   1 
HETATM 1104 O O   . HOH D 4 .   ? -0.357  7.165  9.822  1.00 35.19 ? 618 HOH A O   1 
HETATM 1105 O O   . HOH D 4 .   ? 13.721  22.650 23.645 1.00 31.60 ? 619 HOH A O   1 
HETATM 1106 O O   . HOH D 4 .   ? 4.479   15.196 28.563 1.00 47.02 ? 620 HOH A O   1 
HETATM 1107 O O   . HOH D 4 .   ? 12.014  11.112 10.061 1.00 37.52 ? 621 HOH A O   1 
HETATM 1108 O O   . HOH D 4 .   ? 3.599   27.639 8.507  1.00 33.14 ? 622 HOH A O   1 
HETATM 1109 O O   . HOH D 4 .   ? -17.711 15.287 22.202 1.00 40.00 ? 623 HOH A O   1 
HETATM 1110 O O   . HOH D 4 .   ? 2.012   26.245 15.009 1.00 28.84 ? 624 HOH A O   1 
HETATM 1111 O O   . HOH D 4 .   ? 3.486   9.142  19.858 1.00 44.00 ? 625 HOH A O   1 
HETATM 1112 O O   . HOH D 4 .   ? -10.475 22.500 23.924 1.00 35.17 ? 626 HOH A O   1 
HETATM 1113 O O   . HOH D 4 .   ? 2.708   10.520 23.897 1.00 39.39 ? 627 HOH A O   1 
HETATM 1114 O O   . HOH D 4 .   ? 3.937   29.451 16.569 1.00 30.99 ? 628 HOH A O   1 
HETATM 1115 O O   . HOH D 4 .   ? -2.363  7.955  16.530 1.00 33.71 ? 629 HOH A O   1 
HETATM 1116 O O   . HOH D 4 .   ? -4.107  11.212 14.304 1.00 33.85 ? 630 HOH A O   1 
HETATM 1117 O O   . HOH D 4 .   ? 4.334   11.982 4.443  1.00 35.22 ? 631 HOH A O   1 
HETATM 1118 O O   . HOH D 4 .   ? 5.971   30.079 18.334 1.00 29.45 ? 632 HOH A O   1 
HETATM 1119 O O   . HOH D 4 .   ? 5.713   11.737 2.053  1.00 42.88 ? 633 HOH A O   1 
HETATM 1120 O O   . HOH D 4 .   ? -11.259 19.190 6.070  1.00 32.48 ? 634 HOH A O   1 
HETATM 1121 O O   . HOH D 4 .   ? -3.997  13.484 13.393 1.00 31.23 ? 635 HOH A O   1 
HETATM 1122 O O   . HOH D 4 .   ? -0.983  27.659 16.680 1.00 33.73 ? 636 HOH A O   1 
HETATM 1123 O O   . HOH D 4 .   ? -4.745  13.184 27.045 1.00 38.74 ? 637 HOH A O   1 
HETATM 1124 O O   . HOH D 4 .   ? -1.724  24.543 8.435  1.00 25.07 ? 638 HOH A O   1 
HETATM 1125 O O   . HOH D 4 .   ? -8.533  18.800 6.780  1.00 26.35 ? 639 HOH A O   1 
HETATM 1126 O O   . HOH D 4 .   ? 15.115  27.092 3.387  1.00 45.28 ? 640 HOH A O   1 
HETATM 1127 O O   . HOH D 4 .   ? 15.771  29.205 24.565 1.00 44.37 ? 641 HOH A O   1 
HETATM 1128 O O   . HOH D 4 .   ? -2.456  17.276 27.671 1.00 32.33 ? 642 HOH A O   1 
HETATM 1129 O O   . HOH D 4 .   ? -5.656  14.497 10.752 1.00 32.49 ? 643 HOH A O   1 
HETATM 1130 O O   . HOH D 4 .   ? -15.892 15.627 20.019 1.00 37.68 ? 644 HOH A O   1 
HETATM 1131 O O   . HOH D 4 .   ? -5.555  15.826 14.263 1.00 25.10 ? 645 HOH A O   1 
HETATM 1132 O O   . HOH D 4 .   ? 3.532   21.929 4.421  1.00 35.30 ? 646 HOH A O   1 
HETATM 1133 O O   . HOH D 4 .   ? 8.244   15.921 25.021 1.00 34.38 ? 647 HOH A O   1 
HETATM 1134 O O   . HOH D 4 .   ? -9.990  13.195 3.253  1.00 37.29 ? 648 HOH A O   1 
HETATM 1135 O O   . HOH D 4 .   ? -11.785 24.562 15.066 1.00 43.91 ? 649 HOH A O   1 
HETATM 1136 O O   . HOH D 4 .   ? 8.790   20.497 -1.146 1.00 46.05 ? 650 HOH A O   1 
HETATM 1137 O O   . HOH D 4 .   ? 9.397   10.353 20.093 1.00 47.09 ? 651 HOH A O   1 
HETATM 1138 O O   . HOH D 4 .   ? -2.129  23.931 28.236 1.00 40.04 ? 652 HOH A O   1 
HETATM 1139 O O   . HOH D 4 .   ? -14.161 13.406 25.353 1.00 38.27 ? 653 HOH A O   1 
HETATM 1140 O O   . HOH D 4 .   ? -13.739 13.380 20.695 1.00 33.91 ? 654 HOH A O   1 
HETATM 1141 O O   . HOH D 4 .   ? -8.251  21.048 19.838 1.00 26.43 ? 655 HOH A O   1 
HETATM 1142 O O   . HOH D 4 .   ? -1.110  12.744 5.495  1.00 34.68 ? 656 HOH A O   1 
HETATM 1143 O O   . HOH D 4 .   ? -15.144 22.096 17.806 1.00 30.98 ? 657 HOH A O   1 
HETATM 1144 O O   . HOH D 4 .   ? -6.193  24.548 18.228 1.00 39.22 ? 658 HOH A O   1 
HETATM 1145 O O   . HOH D 4 .   ? 19.904  22.639 14.656 1.00 33.61 ? 659 HOH A O   1 
HETATM 1146 O O   . HOH D 4 .   ? -6.616  22.698 26.916 1.00 40.15 ? 660 HOH A O   1 
HETATM 1147 O O   . HOH D 4 .   ? 17.389  15.935 15.244 1.00 37.50 ? 661 HOH A O   1 
HETATM 1148 O O   . HOH D 4 .   ? -6.028  22.078 18.565 1.00 25.15 ? 662 HOH A O   1 
HETATM 1149 O O   . HOH D 4 .   ? 6.080   20.069 1.100  1.00 51.11 ? 663 HOH A O   1 
HETATM 1150 O O   . HOH D 4 .   ? -7.378  25.608 15.642 1.00 43.90 ? 664 HOH A O   1 
HETATM 1151 O O   . HOH D 4 .   ? -17.774 16.056 24.597 1.00 43.63 ? 665 HOH A O   1 
HETATM 1152 O O   . HOH D 4 .   ? 7.342   7.985  9.875  1.00 44.99 ? 666 HOH A O   1 
HETATM 1153 O O   . HOH D 4 .   ? -18.253 21.555 23.522 1.00 47.73 ? 667 HOH A O   1 
HETATM 1154 O O   . HOH D 4 .   ? 17.829  15.965 9.846  1.00 39.00 ? 668 HOH A O   1 
HETATM 1155 O O   . HOH D 4 .   ? 15.292  17.885 -1.166 1.00 45.59 ? 669 HOH A O   1 
HETATM 1156 O O   . HOH D 4 .   ? -10.138 22.678 20.472 1.00 39.01 ? 670 HOH A O   1 
HETATM 1157 O O   . HOH D 4 .   ? -8.494  22.019 9.393  1.00 34.57 ? 671 HOH A O   1 
HETATM 1158 O O   . HOH D 4 .   ? 4.339   20.479 2.238  1.00 45.22 ? 672 HOH A O   1 
HETATM 1159 O O   . HOH D 4 .   ? 23.990  24.367 14.847 1.00 41.84 ? 673 HOH A O   1 
HETATM 1160 O O   . HOH D 4 .   ? 6.041   27.394 1.110  1.00 52.82 ? 674 HOH A O   1 
HETATM 1161 O O   . HOH D 4 .   ? 17.957  30.189 16.320 1.00 49.20 ? 675 HOH A O   1 
HETATM 1162 O O   . HOH D 4 .   ? -12.595 22.468 19.481 1.00 32.75 ? 676 HOH A O   1 
HETATM 1163 O O   . HOH D 4 .   ? 10.142  33.549 18.486 1.00 35.80 ? 677 HOH A O   1 
HETATM 1164 O O   . HOH D 4 .   ? -17.027 23.282 19.922 1.00 37.65 ? 678 HOH A O   1 
HETATM 1165 O O   . HOH D 4 .   ? -11.802 11.318 2.013  1.00 40.01 ? 679 HOH A O   1 
HETATM 1166 O O   . HOH D 4 .   ? 20.694  22.899 1.121  1.00 59.98 ? 680 HOH A O   1 
HETATM 1167 O O   . HOH D 4 .   ? -4.556  6.915  15.171 1.00 47.54 ? 681 HOH A O   1 
HETATM 1168 O O   . HOH D 4 .   ? -0.479  28.317 21.756 1.00 40.67 ? 682 HOH A O   1 
HETATM 1169 O O   . HOH D 4 .   ? -12.638 12.630 23.124 1.00 31.16 ? 683 HOH A O   1 
HETATM 1170 O O   . HOH D 4 .   ? -6.201  23.631 29.094 1.00 45.12 ? 684 HOH A O   1 
HETATM 1171 O O   . HOH D 4 .   ? 20.056  21.030 16.664 1.00 36.03 ? 685 HOH A O   1 
HETATM 1172 O O   . HOH D 4 .   ? 0.561   16.351 2.603  1.00 46.70 ? 686 HOH A O   1 
HETATM 1173 O O   . HOH D 4 .   ? 16.597  28.883 5.079  1.00 48.73 ? 687 HOH A O   1 
HETATM 1174 O O   . HOH D 4 .   ? 17.340  41.029 1.619  1.00 57.46 ? 688 HOH A O   1 
HETATM 1175 O O   . HOH D 4 .   ? 21.819  19.576 16.490 1.00 42.61 ? 689 HOH A O   1 
HETATM 1176 O O   . HOH D 4 .   ? 16.602  13.033 1.490  1.00 50.83 ? 690 HOH A O   1 
HETATM 1177 O O   . HOH D 4 .   ? -5.229  9.874  26.278 1.00 50.02 ? 691 HOH A O   1 
HETATM 1178 O O   . HOH D 4 .   ? 10.201  7.974  8.993  1.00 54.80 ? 692 HOH A O   1 
HETATM 1179 O O   . HOH D 4 .   ? 1.501   27.482 10.357 1.00 30.58 ? 693 HOH A O   1 
HETATM 1180 O O   . HOH D 4 .   ? 5.583   9.196  0.834  1.00 47.34 ? 694 HOH A O   1 
HETATM 1181 O O   . HOH D 4 .   ? 25.512  29.037 11.319 1.00 54.45 ? 695 HOH A O   1 
HETATM 1182 O O   . HOH D 4 .   ? 3.816   9.543  4.509  1.00 42.91 ? 696 HOH A O   1 
HETATM 1183 O O   . HOH D 4 .   ? -10.891 25.007 23.161 1.00 52.43 ? 697 HOH A O   1 
HETATM 1184 O O   . HOH D 4 .   ? -6.964  9.522  24.814 1.00 49.21 ? 698 HOH A O   1 
HETATM 1185 O O   . HOH D 4 .   ? 9.275   5.424  7.661  1.00 64.58 ? 699 HOH A O   1 
HETATM 1186 O O   . HOH D 4 .   ? 5.306   12.760 29.775 1.00 53.42 ? 700 HOH A O   1 
HETATM 1187 O O   . HOH D 4 .   ? 5.274   32.262 19.207 1.00 45.33 ? 701 HOH A O   1 
HETATM 1188 O O   . HOH D 4 .   ? -6.686  4.358  7.357  1.00 51.74 ? 702 HOH A O   1 
HETATM 1189 O O   . HOH D 4 .   ? 18.410  18.767 4.890  1.00 45.81 ? 703 HOH A O   1 
HETATM 1190 O O   . HOH D 4 .   ? 27.982  24.557 3.988  1.00 66.32 ? 704 HOH A O   1 
HETATM 1191 O O   . HOH D 4 .   ? 1.707   28.406 12.840 1.00 28.29 ? 705 HOH A O   1 
HETATM 1192 O O   . HOH D 4 .   ? -2.372  23.989 5.878  1.00 41.73 ? 706 HOH A O   1 
HETATM 1193 O O   . HOH D 4 .   ? -0.641  29.562 13.493 1.00 41.29 ? 707 HOH A O   1 
HETATM 1194 O O   . HOH D 4 .   ? 5.164   29.732 9.694  1.00 32.30 ? 708 HOH A O   1 
HETATM 1195 O O   . HOH D 4 .   ? -18.728 22.205 19.298 1.00 47.48 ? 709 HOH A O   1 
HETATM 1196 O O   . HOH D 4 .   ? 6.982   29.818 0.384  1.00 54.98 ? 710 HOH A O   1 
HETATM 1197 O O   . HOH D 4 .   ? -16.755 14.284 26.454 1.00 45.74 ? 711 HOH A O   1 
HETATM 1198 O O   . HOH D 4 .   ? -1.139  27.012 9.260  1.00 31.98 ? 712 HOH A O   1 
HETATM 1199 O O   . HOH D 4 .   ? -14.617 10.892 19.812 1.00 48.42 ? 713 HOH A O   1 
HETATM 1200 O O   . HOH D 4 .   ? 1.279   13.880 3.544  1.00 46.69 ? 714 HOH A O   1 
HETATM 1201 O O   . HOH D 4 .   ? -3.613  13.295 1.961  1.00 40.75 ? 715 HOH A O   1 
HETATM 1202 O O   . HOH D 4 .   ? 12.681  32.373 25.186 1.00 49.29 ? 716 HOH A O   1 
HETATM 1203 O O   . HOH D 4 .   ? -16.192 13.286 24.220 1.00 51.32 ? 717 HOH A O   1 
HETATM 1204 O O   . HOH D 4 .   ? 22.708  22.225 14.925 1.00 37.48 ? 718 HOH A O   1 
HETATM 1205 O O   . HOH D 4 .   ? -9.098  23.901 26.266 1.00 44.82 ? 719 HOH A O   1 
HETATM 1206 O O   . HOH D 4 .   ? 4.321   30.266 12.336 1.00 34.93 ? 720 HOH A O   1 
HETATM 1207 O O   . HOH D 4 .   ? 19.236  35.903 9.528  1.00 50.44 ? 721 HOH A O   1 
HETATM 1208 O O   . HOH D 4 .   ? -11.596 9.755  23.602 1.00 46.22 ? 722 HOH A O   1 
HETATM 1209 O O   . HOH D 4 .   ? 4.969   32.069 8.536  1.00 46.07 ? 723 HOH A O   1 
HETATM 1210 O O   . HOH D 4 .   ? -3.921  13.946 -0.556 1.00 43.34 ? 724 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A SER A 5   ? 0.4789 1.0397 0.6007 -0.1424 0.0708  0.0621  328 SER A N   
2    N N   B SER A 5   ? 0.4907 0.9933 0.6135 -0.1735 0.0596  0.0628  328 SER A N   
3    C CA  A SER A 5   ? 0.4974 1.0218 0.6168 -0.1481 0.0639  0.0634  328 SER A CA  
4    C CA  B SER A 5   ? 0.4981 1.0166 0.6159 -0.1537 0.0646  0.0650  328 SER A CA  
5    C C   A SER A 5   ? 0.5991 1.0812 0.7029 -0.1359 0.0630  0.0702  328 SER A C   
6    C C   B SER A 5   ? 0.5998 1.0825 0.7037 -0.1367 0.0632  0.0702  328 SER A C   
7    O O   A SER A 5   ? 0.6269 1.0968 0.7321 -0.1224 0.0562  0.0674  328 SER A O   
8    O O   B SER A 5   ? 0.6221 1.0983 0.7289 -0.1208 0.0566  0.0665  328 SER A O   
9    C CB  A SER A 5   ? 0.4937 0.9993 0.6130 -0.1794 0.0653  0.0668  328 SER A CB  
10   C CB  B SER A 5   ? 0.4642 1.0313 0.5958 -0.1339 0.0622  0.0549  328 SER A CB  
11   O OG  A SER A 5   ? 0.4711 0.9424 0.5883 -0.1844 0.0582  0.0662  328 SER A OG  
12   O OG  B SER A 5   ? 0.4445 1.0479 0.5892 -0.1488 0.0621  0.0488  328 SER A OG  
13   N N   . PRO A 6   ? 0.5803 1.0418 0.6687 -0.1398 0.0696  0.0790  329 PRO A N   
14   C CA  . PRO A 6   ? 0.6201 1.0455 0.6929 -0.1265 0.0681  0.0840  329 PRO A CA  
15   C C   . PRO A 6   ? 0.6038 1.0439 0.6800 -0.0984 0.0666  0.0764  329 PRO A C   
16   O O   . PRO A 6   ? 0.4608 0.8762 0.5318 -0.0867 0.0624  0.0767  329 PRO A O   
17   C CB  . PRO A 6   ? 0.6002 1.0104 0.6559 -0.1346 0.0756  0.0939  329 PRO A CB  
18   C CG  . PRO A 6   ? 0.5631 0.9876 0.6249 -0.1576 0.0807  0.0971  329 PRO A CG  
19   C CD  . PRO A 6   ? 0.5201 0.9893 0.6032 -0.1556 0.0782  0.0854  329 PRO A CD  
20   N N   . GLU A 7   ? 0.7424 1.2205 0.8268 -0.0868 0.0705  0.0693  330 GLU A N   
21   C CA  . GLU A 7   ? 0.5998 1.0880 0.6881 -0.0588 0.0699  0.0610  330 GLU A CA  
22   C C   . GLU A 7   ? 0.5716 1.0691 0.6740 -0.0476 0.0625  0.0559  330 GLU A C   
23   O O   . GLU A 7   ? 0.4230 0.9057 0.5251 -0.0275 0.0599  0.0535  330 GLU A O   
24   C CB  . GLU A 7   ? 0.5738 1.0969 0.6653 -0.0490 0.0763  0.0547  330 GLU A CB  
25   N N   . PHE A 8   ? 0.4706 0.9932 0.5849 -0.0598 0.0594  0.0540  331 PHE A N   
26   C CA  . PHE A 8   ? 0.3869 0.9182 0.5120 -0.0514 0.0512  0.0498  331 PHE A CA  
27   C C   . PHE A 8   ? 0.3989 0.8926 0.5186 -0.0533 0.0454  0.0541  331 PHE A C   
28   O O   . PHE A 8   ? 0.3385 0.8263 0.4611 -0.0340 0.0402  0.0524  331 PHE A O   
29   C CB  . PHE A 8   ? 0.3707 0.9327 0.5065 -0.0700 0.0490  0.0464  331 PHE A CB  
30   C CG  . PHE A 8   ? 0.3922 0.9730 0.5380 -0.0592 0.0407  0.0406  331 PHE A CG  
31   C CD1 . PHE A 8   ? 0.3791 0.9956 0.5322 -0.0385 0.0402  0.0354  331 PHE A CD1 
32   C CD2 . PHE A 8   ? 0.3487 0.9119 0.4950 -0.0691 0.0334  0.0404  331 PHE A CD2 
33   C CE1 . PHE A 8   ? 0.3726 1.0063 0.5317 -0.0270 0.0327  0.0315  331 PHE A CE1 
34   C CE2 . PHE A 8   ? 0.2945 0.8767 0.4477 -0.0582 0.0256  0.0350  331 PHE A CE2 
35   C CZ  . PHE A 8   ? 0.3673 0.9848 0.5260 -0.0369 0.0254  0.0313  331 PHE A CZ  
36   N N   . MET A 9   ? 0.4129 0.8788 0.5236 -0.0758 0.0463  0.0605  332 MET A N   
37   C CA  . MET A 9   ? 0.3774 0.8077 0.4822 -0.0783 0.0407  0.0647  332 MET A CA  
38   C C   . MET A 9   ? 0.3310 0.7409 0.4278 -0.0565 0.0419  0.0670  332 MET A C   
39   O O   . MET A 9   ? 0.2628 0.6545 0.3596 -0.0449 0.0352  0.0664  332 MET A O   
40   C CB  . MET A 9   ? 0.4311 0.8299 0.5247 -0.1047 0.0422  0.0721  332 MET A CB  
41   C CG  . MET A 9   ? 0.5190 0.9238 0.6213 -0.1270 0.0385  0.0682  332 MET A CG  
42   S SD  . MET A 9   ? 0.7206 1.0817 0.8075 -0.1556 0.0433  0.0780  332 MET A SD  
43   C CE  . MET A 9   ? 0.5561 0.8691 0.6234 -0.1435 0.0410  0.0876  332 MET A CE  
44   N N   . ASN A 10  ? 0.3219 0.7296 0.4093 -0.0500 0.0493  0.0678  333 ASN A N   
45   C CA  . ASN A 10  ? 0.3015 0.6889 0.3807 -0.0295 0.0509  0.0666  333 ASN A CA  
46   C C   . ASN A 10  ? 0.2704 0.6689 0.3616 -0.0044 0.0480  0.0602  333 ASN A C   
47   O O   . ASN A 10  ? 0.3024 0.6657 0.3866 0.0088  0.0429  0.0596  333 ASN A O   
48   C CB  . ASN A 10  ? 0.3506 0.7418 0.4190 -0.0263 0.0594  0.0650  333 ASN A CB  
49   C CG  . ASN A 10  ? 0.4995 0.8630 0.5484 -0.0427 0.0610  0.0737  333 ASN A CG  
50   O OD1 . ASN A 10  ? 0.3314 0.6632 0.3729 -0.0533 0.0549  0.0803  333 ASN A OD1 
51   N ND2 . ASN A 10  ? 0.6477 1.0172 0.6861 -0.0422 0.0671  0.0726  333 ASN A ND2 
52   N N   . LYS A 11  ? 0.2725 0.7056 0.3755 0.0031  0.0487  0.0549  334 LYS A N   
53   C CA  . LYS A 11  ? 0.2724 0.7119 0.3837 0.0277  0.0452  0.0511  334 LYS A CA  
54   C C   . LYS A 11  ? 0.1894 0.6177 0.3041 0.0273  0.0360  0.0548  334 LYS A C   
55   O O   . LYS A 11  ? 0.2459 0.6544 0.3593 0.0466  0.0334  0.0561  334 LYS A O   
56   C CB  . LYS A 11  ? 0.2153 0.6934 0.3359 0.0335  0.0461  0.0459  334 LYS A CB  
57   C CG  . LYS A 11  ? 0.2295 0.7215 0.3480 0.0399  0.0547  0.0407  334 LYS A CG  
58   C CD  . LYS A 11  ? 0.3275 0.7908 0.4383 0.0594  0.0598  0.0373  334 LYS A CD  
59   C CE  . LYS A 11  ? 0.3580 0.8370 0.4659 0.0645  0.0682  0.0298  334 LYS A CE  
60   N NZ  . LYS A 11  ? 0.5123 0.9972 0.6117 0.0410  0.0720  0.0325  334 LYS A NZ  
61   N N   . GLN A 12  ? 0.2580 0.6957 0.3758 0.0048  0.0311  0.0562  335 GLN A N   
62   C CA  . GLN A 12  ? 0.2567 0.6874 0.3772 0.0036  0.0216  0.0573  335 GLN A CA  
63   C C   . GLN A 12  ? 0.2192 0.6028 0.3275 0.0097  0.0182  0.0615  335 GLN A C   
64   O O   . GLN A 12  ? 0.2250 0.5983 0.3330 0.0275  0.0136  0.0628  335 GLN A O   
65   C CB  . GLN A 12  ? 0.2298 0.6714 0.3538 -0.0247 0.0179  0.0553  335 GLN A CB  
66   C CG  . GLN A 12  ? 0.2939 0.7751 0.4267 -0.0302 0.0180  0.0488  335 GLN A CG  
67   C CD  . GLN A 12  ? 0.3515 0.8377 0.4874 -0.0608 0.0159  0.0455  335 GLN A CD  
68   O OE1 . GLN A 12  ? 0.3570 0.8249 0.4876 -0.0814 0.0208  0.0493  335 GLN A OE1 
69   N NE2 . GLN A 12  ? 0.3188 0.8266 0.4615 -0.0636 0.0092  0.0384  335 GLN A NE2 
70   N N   . TRP A 13  ? 0.2157 0.5631 0.3089 -0.0045 0.0198  0.0637  336 TRP A N   
71   C CA  . TRP A 13  ? 0.2742 0.5737 0.3528 0.0000  0.0148  0.0660  336 TRP A CA  
72   C C   . TRP A 13  ? 0.2392 0.5204 0.3127 0.0216  0.0185  0.0653  336 TRP A C   
73   O O   . TRP A 13  ? 0.2163 0.4671 0.2826 0.0294  0.0142  0.0668  336 TRP A O   
74   C CB  . TRP A 13  ? 0.2361 0.5037 0.2999 -0.0192 0.0144  0.0691  336 TRP A CB  
75   C CG  . TRP A 13  ? 0.2435 0.5055 0.2976 -0.0233 0.0224  0.0713  336 TRP A CG  
76   C CD1 . TRP A 13  ? 0.3082 0.5881 0.3624 -0.0399 0.0285  0.0743  336 TRP A CD1 
77   C CD2 . TRP A 13  ? 0.2252 0.4632 0.2669 -0.0120 0.0250  0.0705  336 TRP A CD2 
78   N NE1 . TRP A 13  ? 0.3428 0.6134 0.3844 -0.0376 0.0347  0.0763  336 TRP A NE1 
79   C CE2 . TRP A 13  ? 0.2683 0.5141 0.3024 -0.0207 0.0322  0.0727  336 TRP A CE2 
80   C CE3 . TRP A 13  ? 0.2651 0.4783 0.3019 0.0035  0.0225  0.0677  336 TRP A CE3 
81   C CZ2 . TRP A 13  ? 0.2768 0.5090 0.2983 -0.0135 0.0359  0.0705  336 TRP A CZ2 
82   C CZ3 . TRP A 13  ? 0.2255 0.4231 0.2512 0.0086  0.0265  0.0649  336 TRP A CZ3 
83   C CH2 . TRP A 13  ? 0.2944 0.5030 0.3125 0.0007  0.0326  0.0655  336 TRP A CH2 
84   N N   . TYR A 14  ? 0.2492 0.5487 0.3270 0.0311  0.0268  0.0623  337 TYR A N   
85   C CA  . TYR A 14  ? 0.2780 0.5604 0.3539 0.0528  0.0306  0.0596  337 TYR A CA  
86   C C   . TYR A 14  ? 0.2378 0.5262 0.3228 0.0710  0.0269  0.0626  337 TYR A C   
87   O O   . TYR A 14  ? 0.2297 0.4860 0.3087 0.0820  0.0258  0.0646  337 TYR A O   
88   C CB  . TYR A 14  ? 0.2473 0.5501 0.3265 0.0611  0.0405  0.0535  337 TYR A CB  
89   C CG  . TYR A 14  ? 0.3250 0.6005 0.3895 0.0578  0.0452  0.0486  337 TYR A CG  
90   C CD1 . TYR A 14  ? 0.2572 0.5322 0.3111 0.0386  0.0457  0.0506  337 TYR A CD1 
91   C CD2 . TYR A 14  ? 0.2706 0.5210 0.3311 0.0738  0.0491  0.0421  337 TYR A CD2 
92   C CE1 . TYR A 14  ? 0.3005 0.5565 0.3399 0.0369  0.0491  0.0461  337 TYR A CE1 
93   C CE2 . TYR A 14  ? 0.3158 0.5461 0.3633 0.0697  0.0527  0.0351  337 TYR A CE2 
94   C CZ  . TYR A 14  ? 0.3447 0.5808 0.3815 0.0520  0.0522  0.0371  337 TYR A CZ  
95   O OH  . TYR A 14  ? 0.3442 0.5665 0.3672 0.0491  0.0551  0.0302  337 TYR A OH  
96   N N   . LEU A 15  ? 0.1718 0.5032 0.2710 0.0737  0.0251  0.0635  338 LEU A N   
97   C CA  . LEU A 15  ? 0.1693 0.5047 0.2717 0.0902  0.0204  0.0671  338 LEU A CA  
98   C C   . LEU A 15  ? 0.2372 0.5508 0.3336 0.0855  0.0121  0.0721  338 LEU A C   
99   O O   . LEU A 15  ? 0.2413 0.5307 0.3304 0.0991  0.0110  0.0760  338 LEU A O   
100  C CB  . LEU A 15  ? 0.2304 0.6060 0.3397 0.0872  0.0179  0.0640  338 LEU A CB  
101  C CG  . LEU A 15  ? 0.2143 0.6099 0.3280 0.0980  0.0251  0.0594  338 LEU A CG  
102  C CD1 . LEU A 15  ? 0.2904 0.7314 0.4121 0.0884  0.0229  0.0555  338 LEU A CD1 
103  C CD2 . LEU A 15  ? 0.2657 0.6422 0.3755 0.1243  0.0276  0.0618  338 LEU A CD2 
104  N N   . LEU A 16  ? 0.1763 0.4881 0.2699 0.0635  0.0070  0.0707  339 LEU A N   
105  C CA  . LEU A 16  ? 0.1774 0.4649 0.2625 0.0587  -0.0008 0.0731  339 LEU A CA  
106  C C   . LEU A 16  ? 0.2528 0.4936 0.3248 0.0652  0.0012  0.0758  339 LEU A C   
107  O O   . LEU A 16  ? 0.1994 0.4259 0.2675 0.0742  -0.0023 0.0803  339 LEU A O   
108  C CB  . LEU A 16  ? 0.2412 0.5265 0.3230 0.0334  -0.0055 0.0692  339 LEU A CB  
109  C CG  . LEU A 16  ? 0.2910 0.6210 0.3862 0.0222  -0.0089 0.0648  339 LEU A CG  
110  C CD1 . LEU A 16  ? 0.2332 0.5483 0.3230 -0.0030 -0.0133 0.0606  339 LEU A CD1 
111  C CD2 . LEU A 16  ? 0.2456 0.5979 0.3450 0.0372  -0.0139 0.0648  339 LEU A CD2 
112  N N   . ALA A 17  ? 0.2091 0.4293 0.2742 0.0597  0.0068  0.0727  340 ALA A N   
113  C CA  . ALA A 17  ? 0.2307 0.4119 0.2850 0.0637  0.0091  0.0728  340 ALA A CA  
114  C C   . ALA A 17  ? 0.2724 0.4444 0.3300 0.0845  0.0138  0.0756  340 ALA A C   
115  O O   . ALA A 17  ? 0.3139 0.4590 0.3656 0.0886  0.0130  0.0790  340 ALA A O   
116  C CB  . ALA A 17  ? 0.2041 0.3747 0.2512 0.0548  0.0143  0.0675  340 ALA A CB  
117  N N   . ASN A 18  ? 0.2603 0.4537 0.3275 0.0981  0.0195  0.0747  341 ASN A N   
118  C CA  . ASN A 18  ? 0.3051 0.4858 0.3752 0.1202  0.0248  0.0788  341 ASN A CA  
119  C C   . ASN A 18  ? 0.3654 0.5413 0.4308 0.1230  0.0193  0.0858  341 ASN A C   
120  O O   . ASN A 18  ? 0.3800 0.5253 0.4387 0.1291  0.0220  0.0896  341 ASN A O   
121  C CB  . ASN A 18  ? 0.3490 0.5523 0.4275 0.1336  0.0314  0.0747  341 ASN A CB  
122  C CG  . ASN A 18  ? 0.4209 0.6092 0.4974 0.1351  0.0404  0.0650  341 ASN A CG  
123  O OD1 . ASN A 18  ? 0.4777 0.6297 0.5491 0.1428  0.0458  0.0627  341 ASN A OD1 
124  N ND2 . ASN A 18  ? 0.3869 0.6015 0.4654 0.1247  0.0422  0.0580  341 ASN A ND2 
125  N N   A GLN A 19  ? 0.2993 0.5059 0.3675 0.1160  0.0126  0.0860  342 GLN A N   
126  N N   B GLN A 19  ? 0.2982 0.5047 0.3663 0.1160  0.0126  0.0860  342 GLN A N   
127  C CA  A GLN A 19  ? 0.3499 0.5556 0.4120 0.1170  0.0081  0.0899  342 GLN A CA  
128  C CA  B GLN A 19  ? 0.3502 0.5554 0.4123 0.1171  0.0082  0.0900  342 GLN A CA  
129  C C   A GLN A 19  ? 0.3563 0.5344 0.4095 0.1077  0.0048  0.0913  342 GLN A C   
130  C C   B GLN A 19  ? 0.3567 0.5341 0.4099 0.1079  0.0050  0.0913  342 GLN A C   
131  O O   A GLN A 19  ? 0.3772 0.5397 0.4238 0.1120  0.0056  0.0954  342 GLN A O   
132  O O   B GLN A 19  ? 0.3780 0.5390 0.4246 0.1123  0.0060  0.0955  342 GLN A O   
133  C CB  A GLN A 19  ? 0.3009 0.5475 0.3687 0.1102  0.0020  0.0868  342 GLN A CB  
134  C CB  B GLN A 19  ? 0.2999 0.5456 0.3674 0.1105  0.0020  0.0869  342 GLN A CB  
135  C CG  A GLN A 19  ? 0.3365 0.6127 0.4108 0.1217  0.0048  0.0862  342 GLN A CG  
136  C CG  B GLN A 19  ? 0.4243 0.6749 0.4857 0.1129  -0.0019 0.0895  342 GLN A CG  
137  C CD  A GLN A 19  ? 0.3376 0.6568 0.4216 0.1095  0.0010  0.0796  342 GLN A CD  
138  C CD  B GLN A 19  ? 0.3661 0.6587 0.4334 0.1064  -0.0077 0.0845  342 GLN A CD  
139  O OE1 A GLN A 19  ? 0.3817 0.7091 0.4673 0.0923  -0.0048 0.0759  342 GLN A OE1 
140  O OE1 B GLN A 19  ? 0.3197 0.6384 0.3962 0.0993  -0.0083 0.0793  342 GLN A OE1 
141  N NE2 A GLN A 19  ? 0.2933 0.6396 0.3839 0.1176  0.0044  0.0775  342 GLN A NE2 
142  N NE2 B GLN A 19  ? 0.3651 0.6665 0.4272 0.1077  -0.0114 0.0851  342 GLN A NE2 
143  N N   . LEU A 20  ? 0.2935 0.4669 0.3463 0.0950  0.0014  0.0883  343 LEU A N   
144  C CA  . LEU A 20  ? 0.3132 0.4627 0.3569 0.0859  -0.0024 0.0880  343 LEU A CA  
145  C C   . LEU A 20  ? 0.3026 0.4176 0.3406 0.0903  0.0035  0.0902  343 LEU A C   
146  O O   . LEU A 20  ? 0.3215 0.4207 0.3532 0.0883  0.0030  0.0914  343 LEU A O   
147  C CB  . LEU A 20  ? 0.3078 0.4616 0.3509 0.0718  -0.0082 0.0851  343 LEU A CB  
148  C CG  . LEU A 20  ? 0.3514 0.4866 0.3849 0.0625  -0.0136 0.0828  343 LEU A CG  
149  C CD1 . LEU A 20  ? 0.3172 0.4568 0.3486 0.0665  -0.0150 0.0821  343 LEU A CD1 
150  C CD2 . LEU A 20  ? 0.3456 0.4895 0.3784 0.0486  -0.0203 0.0795  343 LEU A CD2 
151  N N   . ILE A 21  ? 0.3120 0.4174 0.3531 0.0958  0.0095  0.0898  344 ILE A N   
152  C CA  . ILE A 21  ? 0.3495 0.4216 0.3865 0.0992  0.0158  0.0906  344 ILE A CA  
153  C C   . ILE A 21  ? 0.3875 0.4483 0.4236 0.1087  0.0204  0.0955  344 ILE A C   
154  O O   . ILE A 21  ? 0.3689 0.4048 0.4005 0.1070  0.0236  0.0979  344 ILE A O   
155  C CB  . ILE A 21  ? 0.3081 0.3695 0.3465 0.0992  0.0227  0.0824  344 ILE A CB  
156  C CG1 . ILE A 21  ? 0.2875 0.3150 0.3198 0.0934  0.0272  0.0781  344 ILE A CG1 
157  C CG2 . ILE A 21  ? 0.3649 0.4323 0.4112 0.1164  0.0301  0.0829  344 ILE A CG2 
158  C CD1 . ILE A 21  ? 0.3319 0.3557 0.3566 0.0782  0.0205  0.0760  344 ILE A CD1 
159  N N   . LEU A 22  ? 0.3591 0.4401 0.3991 0.1184  0.0208  0.0978  345 LEU A N   
160  C CA  . LEU A 22  ? 0.3796 0.4519 0.4172 0.1286  0.0246  0.1047  345 LEU A CA  
161  C C   . LEU A 22  ? 0.3402 0.4180 0.3721 0.1223  0.0197  0.1085  345 LEU A C   
162  O O   . LEU A 22  ? 0.3784 0.4383 0.4060 0.1252  0.0235  0.1147  345 LEU A O   
163  C CB  . LEU A 22  ? 0.4344 0.5301 0.4771 0.1421  0.0259  0.1063  345 LEU A CB  
164  C CG  . LEU A 22  ? 0.4970 0.5830 0.5451 0.1530  0.0333  0.1025  345 LEU A CG  
165  C CD1 . LEU A 22  ? 0.4558 0.5712 0.5091 0.1660  0.0334  0.1032  345 LEU A CD1 
166  C CD2 . LEU A 22  ? 0.5159 0.5594 0.5606 0.1591  0.0417  0.1050  345 LEU A CD2 
167  N N   . SER A 23  ? 0.3579 0.4600 0.3898 0.1137  0.0119  0.1043  346 SER A N   
168  C CA  . SER A 23  ? 0.2887 0.3973 0.3153 0.1086  0.0076  0.1054  346 SER A CA  
169  C C   . SER A 23  ? 0.3726 0.4565 0.3941 0.1001  0.0083  0.1049  346 SER A C   
170  O O   . SER A 23  ? 0.3454 0.4266 0.3626 0.1008  0.0091  0.1093  346 SER A O   
171  C CB  . SER A 23  ? 0.3139 0.4499 0.3422 0.1005  -0.0006 0.0989  346 SER A CB  
172  O OG  . SER A 23  ? 0.4500 0.6141 0.4841 0.1074  -0.0012 0.0991  346 SER A OG  
173  N N   . LEU A 24  ? 0.3481 0.4171 0.3699 0.0927  0.0082  0.1000  347 LEU A N   
174  C CA  . LEU A 24  ? 0.3378 0.3863 0.3552 0.0851  0.0090  0.0993  347 LEU A CA  
175  C C   . LEU A 24  ? 0.3654 0.3913 0.3824 0.0911  0.0176  0.1068  347 LEU A C   
176  O O   . LEU A 24  ? 0.4141 0.4320 0.4276 0.0876  0.0189  0.1103  347 LEU A O   
177  C CB  . LEU A 24  ? 0.3245 0.3647 0.3417 0.0774  0.0074  0.0932  347 LEU A CB  
178  C CG  . LEU A 24  ? 0.2733 0.3294 0.2895 0.0696  -0.0007 0.0870  347 LEU A CG  
179  C CD1 . LEU A 24  ? 0.3030 0.3483 0.3162 0.0626  -0.0018 0.0834  347 LEU A CD1 
180  C CD2 . LEU A 24  ? 0.2456 0.3110 0.2578 0.0649  -0.0065 0.0843  347 LEU A CD2 
181  N N   . SER A 25  ? 0.4235 0.4384 0.4444 0.1005  0.0241  0.1092  348 SER A N   
182  C CA  . SER A 25  ? 0.4206 0.4081 0.4411 0.1061  0.0333  0.1159  348 SER A CA  
183  C C   . SER A 25  ? 0.4008 0.3938 0.4178 0.1113  0.0343  0.1257  348 SER A C   
184  O O   . SER A 25  ? 0.5008 0.4720 0.5157 0.1106  0.0406  0.1325  348 SER A O   
185  C CB  . SER A 25  ? 0.4073 0.3827 0.4322 0.1177  0.0400  0.1152  348 SER A CB  
186  O OG  . SER A 25  ? 0.4936 0.4569 0.5214 0.1137  0.0424  0.1065  348 SER A OG  
187  N N   . LYS A 26  ? 0.4102 0.4322 0.4267 0.1162  0.0289  0.1270  349 LYS A N   
188  C CA  . LYS A 26  ? 0.4736 0.5044 0.4865 0.1235  0.0304  0.1371  349 LYS A CA  
189  C C   . LYS A 26  ? 0.5147 0.5643 0.5238 0.1156  0.0246  0.1356  349 LYS A C   
190  O O   . LYS A 26  ? 0.4982 0.5560 0.5038 0.1212  0.0264  0.1443  349 LYS A O   
191  C CB  . LYS A 26  ? 0.4885 0.5401 0.5030 0.1375  0.0302  0.1409  349 LYS A CB  
192  C CG  . LYS A 26  ? 0.5533 0.6398 0.5699 0.1348  0.0218  0.1331  349 LYS A CG  
193  C CD  . LYS A 26  ? 0.6160 0.7267 0.6336 0.1496  0.0223  0.1386  349 LYS A CD  
194  C CE  . LYS A 26  ? 0.8663 1.0123 0.8876 0.1459  0.0147  0.1299  349 LYS A CE  
195  N NZ  . LYS A 26  ? 0.6567 0.8226 0.6749 0.1364  0.0080  0.1252  349 LYS A NZ  
196  N N   . TYR A 27  ? 0.4532 0.5089 0.4624 0.1039  0.0181  0.1251  350 TYR A N   
197  C CA  . TYR A 27  ? 0.4086 0.4776 0.4139 0.0973  0.0135  0.1227  350 TYR A CA  
198  C C   . TYR A 27  ? 0.4658 0.5189 0.4683 0.0949  0.0188  0.1301  350 TYR A C   
199  O O   . TYR A 27  ? 0.4207 0.4485 0.4246 0.0932  0.0248  0.1335  350 TYR A O   
200  C CB  . TYR A 27  ? 0.4806 0.5541 0.4860 0.0863  0.0060  0.1102  350 TYR A CB  
201  C CG  . TYR A 27  ? 0.3547 0.4446 0.3561 0.0819  0.0005  0.1056  350 TYR A CG  
202  C CD1 . TYR A 27  ? 0.4156 0.4986 0.4137 0.0754  -0.0001 0.1034  350 TYR A CD1 
203  C CD2 . TYR A 27  ? 0.4072 0.5213 0.4079 0.0854  -0.0036 0.1036  350 TYR A CD2 
204  C CE1 . TYR A 27  ? 0.4270 0.5252 0.4212 0.0732  -0.0046 0.0988  350 TYR A CE1 
205  C CE2 . TYR A 27  ? 0.3951 0.5235 0.3917 0.0824  -0.0081 0.0986  350 TYR A CE2 
206  C CZ  . TYR A 27  ? 0.4101 0.5297 0.4034 0.0768  -0.0085 0.0960  350 TYR A CZ  
207  O OH  . TYR A 27  ? 0.5096 0.6439 0.4985 0.0754  -0.0127 0.0904  350 TYR A OH  
208  N N   . GLU A 28  ? 0.4777 0.5469 0.4765 0.0944  0.0171  0.1325  351 GLU A N   
209  C CA  . GLU A 28  ? 0.4836 0.5437 0.4800 0.0918  0.0222  0.1407  351 GLU A CA  
210  C C   . GLU A 28  ? 0.5321 0.5736 0.5297 0.0811  0.0228  0.1358  351 GLU A C   
211  O O   . GLU A 28  ? 0.5283 0.5771 0.5258 0.0744  0.0162  0.1247  351 GLU A O   
212  C CB  . GLU A 28  ? 0.6275 0.7137 0.6200 0.0921  0.0188  0.1407  351 GLU A CB  
213  C CG  . GLU A 28  ? 0.8915 0.9746 0.8819 0.0882  0.0233  0.1483  351 GLU A CG  
214  C CD  . GLU A 28  ? 0.7226 0.7885 0.7121 0.0932  0.0330  0.1650  351 GLU A CD  
215  O OE1 . GLU A 28  ? 0.7276 0.7952 0.7164 0.1038  0.0354  0.1723  351 GLU A OE1 
216  O OE2 . GLU A 28  ? 0.7070 0.7569 0.6960 0.0862  0.0387  0.1713  351 GLU A OE2 
217  N N   . GLY A 29  ? 0.4656 0.4820 0.4640 0.0794  0.0313  0.1443  352 GLY A N   
218  C CA  . GLY A 29  ? 0.4118 0.4106 0.4118 0.0687  0.0338  0.1409  352 GLY A CA  
219  C C   . GLY A 29  ? 0.4786 0.4623 0.4822 0.0670  0.0332  0.1326  352 GLY A C   
220  O O   . GLY A 29  ? 0.4278 0.3991 0.4329 0.0580  0.0353  0.1291  352 GLY A O   
221  N N   . GLY A 30  ? 0.4622 0.4492 0.4675 0.0753  0.0312  0.1299  353 GLY A N   
222  C CA  . GLY A 30  ? 0.4027 0.3790 0.4113 0.0746  0.0311  0.1223  353 GLY A CA  
223  C C   . GLY A 30  ? 0.4635 0.4060 0.4751 0.0727  0.0416  0.1245  353 GLY A C   
224  O O   . GLY A 30  ? 0.4856 0.4171 0.4997 0.0681  0.0428  0.1172  353 GLY A O   
225  N N   . HIS A 31  ? 0.4747 0.3987 0.4858 0.0753  0.0500  0.1340  354 HIS A N   
226  C CA  . HIS A 31  ? 0.5035 0.3897 0.5176 0.0723  0.0614  0.1339  354 HIS A CA  
227  C C   . HIS A 31  ? 0.4278 0.2988 0.4445 0.0557  0.0655  0.1268  354 HIS A C   
228  O O   . HIS A 31  ? 0.5090 0.3521 0.5300 0.0509  0.0736  0.1187  354 HIS A O   
229  C CB  . HIS A 31  ? 0.4584 0.3268 0.4703 0.0757  0.0695  0.1464  354 HIS A CB  
230  C CG  . HIS A 31  ? 0.4498 0.3266 0.4582 0.0669  0.0698  0.1544  354 HIS A CG  
231  N ND1 . HIS A 31  ? 0.4992 0.4085 0.5035 0.0725  0.0625  0.1600  354 HIS A ND1 
232  C CD2 . HIS A 31  ? 0.4961 0.3550 0.5051 0.0518  0.0774  0.1566  354 HIS A CD2 
233  C CE1 . HIS A 31  ? 0.5229 0.4346 0.5248 0.0632  0.0652  0.1663  354 HIS A CE1 
234  N NE2 . HIS A 31  ? 0.5478 0.4301 0.5525 0.0499  0.0743  0.1650  354 HIS A NE2 
235  N N   . ILE A 32  ? 0.4571 0.3471 0.4720 0.0464  0.0610  0.1280  355 ILE A N   
236  C CA  . ILE A 32  ? 0.5158 0.3954 0.5346 0.0289  0.0661  0.1210  355 ILE A CA  
237  C C   . ILE A 32  ? 0.4674 0.3590 0.4873 0.0252  0.0582  0.1009  355 ILE A C   
238  O O   . ILE A 32  ? 0.4654 0.3566 0.4882 0.0099  0.0592  0.0856  355 ILE A O   
239  C CB  . ILE A 32  ? 0.4903 0.3954 0.5072 0.0188  0.0621  0.1233  355 ILE A CB  
240  C CG1 . ILE A 32  ? 0.5040 0.4445 0.5164 0.0251  0.0475  0.1186  355 ILE A CG1 
241  C CG2 . ILE A 32  ? 0.4899 0.3933 0.5035 0.0212  0.0670  0.1386  355 ILE A CG2 
242  C CD1 . ILE A 32  ? 0.4369 0.4034 0.4476 0.0171  0.0432  0.1173  355 ILE A CD1 
243  N N   . PHE A 33  ? 0.3998 0.3049 0.4175 0.0382  0.0507  0.1009  356 PHE A N   
244  C CA  . PHE A 33  ? 0.4259 0.3411 0.4435 0.0355  0.0448  0.0848  356 PHE A CA  
245  C C   . PHE A 33  ? 0.4562 0.3550 0.4766 0.0443  0.0504  0.0806  356 PHE A C   
246  O O   . PHE A 33  ? 0.4454 0.3536 0.4653 0.0425  0.0469  0.0679  356 PHE A O   
247  C CB  . PHE A 33  ? 0.3331 0.2783 0.3462 0.0402  0.0322  0.0858  356 PHE A CB  
248  C CG  . PHE A 33  ? 0.3979 0.3604 0.4076 0.0351  0.0263  0.0891  356 PHE A CG  
249  C CD1 . PHE A 33  ? 0.3313 0.3029 0.3400 0.0233  0.0232  0.0780  356 PHE A CD1 
250  C CD2 . PHE A 33  ? 0.3750 0.3486 0.3822 0.0436  0.0237  0.1024  356 PHE A CD2 
251  C CE1 . PHE A 33  ? 0.3565 0.3463 0.3626 0.0209  0.0182  0.0803  356 PHE A CE1 
252  C CE2 . PHE A 33  ? 0.4203 0.4116 0.4240 0.0402  0.0188  0.1039  356 PHE A CE2 
253  C CZ  . PHE A 33  ? 0.3449 0.3437 0.3485 0.0293  0.0162  0.0928  356 PHE A CZ  
254  N N   . GLU A 34  ? 0.3813 0.2564 0.4042 0.0549  0.0595  0.0914  357 GLU A N   
255  C CA  . GLU A 34  ? 0.4517 0.3136 0.4775 0.0675  0.0648  0.0881  357 GLU A CA  
256  C C   . GLU A 34  ? 0.4478 0.2935 0.4759 0.0572  0.0703  0.0673  357 GLU A C   
257  O O   . GLU A 34  ? 0.4144 0.2678 0.4431 0.0631  0.0695  0.0571  357 GLU A O   
258  C CB  . GLU A 34  ? 0.4395 0.2819 0.4659 0.0796  0.0720  0.1011  357 GLU A CB  
259  C CG  . GLU A 34  ? 0.4608 0.2931 0.4899 0.0941  0.0768  0.0967  357 GLU A CG  
260  C CD  . GLU A 34  ? 0.5373 0.4052 0.5671 0.1061  0.0680  0.0974  357 GLU A CD  
261  O OE1 . GLU A 34  ? 0.5669 0.4657 0.5942 0.1036  0.0580  0.1029  357 GLU A OE1 
262  O OE2 . GLU A 34  ? 0.5446 0.4104 0.5779 0.1170  0.0716  0.0907  357 GLU A OE2 
263  N N   . LYS A 35  ? 0.4829 0.3087 0.5124 0.0412  0.0765  0.0598  358 LYS A N   
264  C CA  . LYS A 35  ? 0.4968 0.3060 0.5288 0.0301  0.0829  0.0382  358 LYS A CA  
265  C C   . LYS A 35  ? 0.5561 0.3842 0.5873 0.0090  0.0776  0.0251  358 LYS A C   
266  O O   . LYS A 35  ? 0.5642 0.4084 0.5943 0.0031  0.0724  0.0343  358 LYS A O   
267  C CB  . LYS A 35  ? 0.5107 0.2723 0.5468 0.0303  0.0979  0.0391  358 LYS A CB  
268  C CG  . LYS A 35  ? 0.5458 0.2875 0.5826 0.0545  0.1039  0.0482  358 LYS A CG  
269  C CD  . LYS A 35  ? 0.7910 0.4965 0.8281 0.0572  0.1136  0.0588  358 LYS A CD  
270  C CE  . LYS A 35  ? 0.7232 0.3945 0.7628 0.0577  0.1234  0.0418  358 LYS A CE  
271  N NZ  . LYS A 35  ? 0.8936 0.5424 0.9366 0.0323  0.1307  0.0221  358 LYS A NZ  
272  N N   . LEU A 36  ? 0.5603 0.3909 0.5919 -0.0009 0.0787  0.0028  359 LEU A N   
273  C CA  . LEU A 36  ? 0.5162 0.3687 0.5473 -0.0198 0.0737  -0.0106 359 LEU A CA  
274  C C   . LEU A 36  ? 0.6033 0.4375 0.6406 -0.0355 0.0814  -0.0089 359 LEU A C   
275  O O   . LEU A 36  ? 0.5753 0.3706 0.6168 -0.0361 0.0936  -0.0057 359 LEU A O   
276  C CB  . LEU A 36  ? 0.4568 0.3175 0.4866 -0.0269 0.0741  -0.0357 359 LEU A CB  
277  C CG  . LEU A 36  ? 0.5013 0.3894 0.5237 -0.0148 0.0655  -0.0366 359 LEU A CG  
278  C CD1 . LEU A 36  ? 0.4435 0.3401 0.4632 -0.0199 0.0674  -0.0605 359 LEU A CD1 
279  C CD2 . LEU A 36  ? 0.4236 0.3462 0.4402 -0.0148 0.0527  -0.0267 359 LEU A CD2 
280  N N   . VAL A 37  ? 0.6485 0.5109 0.6860 -0.0475 0.0748  -0.0098 360 VAL A N   
281  C CA  . VAL A 37  ? 0.6783 0.5316 0.7222 -0.0636 0.0818  -0.0063 360 VAL A CA  
282  C C   . VAL A 37  ? 0.6809 0.5126 0.7320 -0.0832 0.0923  -0.0279 360 VAL A C   
283  O O   . VAL A 37  ? 0.6837 0.5330 0.7345 -0.0908 0.0886  -0.0504 360 VAL A O   
284  C CB  . VAL A 37  ? 0.6534 0.5489 0.6965 -0.0702 0.0717  -0.0045 360 VAL A CB  
285  C CG1 . VAL A 37  ? 0.7301 0.6232 0.7812 -0.0893 0.0796  -0.0032 360 VAL A CG1 
286  C CG2 . VAL A 37  ? 0.5985 0.5099 0.6347 -0.0516 0.0625  0.0153  360 VAL A CG2 
287  N N   . ASP A 38  ? 0.8057 0.5983 0.8625 -0.0916 0.1060  -0.0212 361 ASP A N   
288  C CA  . ASP A 38  ? 0.9117 0.6808 0.9768 -0.1151 0.1174  -0.0419 361 ASP A CA  
289  C C   . ASP A 38  ? 0.9824 0.7805 1.0542 -0.1380 0.1164  -0.0445 361 ASP A C   
290  O O   . ASP A 38  ? 0.9756 0.7629 1.0502 -0.1431 0.1230  -0.0258 361 ASP A O   
291  C CB  . ASP A 38  ? 0.9067 0.6141 0.9744 -0.1131 0.1339  -0.0327 361 ASP A CB  
292  C CG  . ASP A 38  ? 1.1575 0.8426 1.2297 -0.1280 0.1413  -0.0584 361 ASP A CG  
293  O OD1 . ASP A 38  ? 1.2553 0.9000 1.3261 -0.1201 0.1493  -0.0522 361 ASP A OD1 
294  O OD2 . ASP A 38  ? 1.2951 1.0081 1.3712 -0.1459 0.1373  -0.0847 361 ASP A OD2 
295  N N   . ALA A 39  ? 0.8620 0.7011 0.9363 -0.1509 0.1083  -0.0674 362 ALA A N   
296  C CA  . ALA A 39  ? 0.8610 0.7430 0.9410 -0.1670 0.1035  -0.0692 362 ALA A CA  
297  C C   . ALA A 39  ? 0.8817 0.7416 0.9734 -0.1931 0.1183  -0.0695 362 ALA A C   
298  O O   . ALA A 39  ? 0.7924 0.6729 0.8878 -0.1997 0.1188  -0.0556 362 ALA A O   
299  C CB  . ALA A 39  ? 0.6784 0.6085 0.7585 -0.1744 0.0926  -0.0949 362 ALA A CB  
300  N N   . LYS A 40  ? 0.8267 0.6490 0.9214 -0.2026 0.1280  -0.0830 363 LYS A N   
301  C CA  . LYS A 40  ? 0.8908 0.6985 0.9920 -0.2201 0.1367  -0.0808 363 LYS A CA  
302  C C   . LYS A 40  ? 0.8816 0.6529 0.9792 -0.2096 0.1444  -0.0485 363 LYS A C   
303  O O   . LYS A 40  ? 1.0008 0.7811 1.1029 -0.2215 0.1479  -0.0364 363 LYS A O   
304  C CB  . LYS A 40  ? 0.7229 0.5031 0.8269 -0.2309 0.1433  -0.1043 363 LYS A CB  
305  N N   . LYS A 41  ? 0.9384 0.6734 1.0275 -0.1860 0.1464  -0.0338 364 LYS A N   
306  C CA  . LYS A 41  ? 0.9241 0.6274 1.0076 -0.1726 0.1523  -0.0034 364 LYS A CA  
307  C C   . LYS A 41  ? 1.0149 0.7494 1.0949 -0.1643 0.1469  0.0206  364 LYS A C   
308  O O   . LYS A 41  ? 1.0648 0.7907 1.1421 -0.1632 0.1511  0.0430  364 LYS A O   
309  C CB  . LYS A 41  ? 0.9367 0.6001 1.0122 -0.1472 0.1545  0.0034  364 LYS A CB  
310  N N   . GLN A 42  ? 0.9505 0.7217 1.0295 -0.1582 0.1378  0.0164  365 GLN A N   
311  C CA  . GLN A 42  ? 0.9499 0.7544 1.0257 -0.1504 0.1327  0.0363  365 GLN A CA  
312  C C   . GLN A 42  ? 0.9116 0.7641 0.9958 -0.1721 0.1303  0.0272  365 GLN A C   
313  O O   . GLN A 42  ? 0.9439 0.8364 1.0239 -0.1616 0.1208  0.0379  365 GLN A O   
314  C CB  . GLN A 42  ? 1.0180 0.8446 1.0846 -0.1243 0.1179  0.0382  365 GLN A CB  
315  C CG  . GLN A 42  ? 0.9051 0.7012 0.9631 -0.0987 0.1197  0.0600  365 GLN A CG  
316  C CD  . GLN A 42  ? 1.0600 0.8505 1.1140 -0.0936 0.1251  0.0876  365 GLN A CD  
317  O OE1 . GLN A 42  ? 1.0071 0.7670 1.0553 -0.0824 0.1288  0.0998  365 GLN A OE1 
318  N NE2 . GLN A 42  ? 1.0559 0.8857 1.1101 -0.0985 0.1208  0.0946  365 GLN A NE2 
319  N N   . ASN A 43  ? 0.8458 0.7028 0.9393 -0.1951 0.1331  0.0065  366 ASN A N   
320  C CA  . ASN A 43  ? 0.7953 0.7010 0.8983 -0.2148 0.1304  -0.0027 366 ASN A CA  
321  C C   . ASN A 43  ? 0.9230 0.8861 1.0258 -0.2106 0.1174  -0.0141 366 ASN A C   
322  O O   . ASN A 43  ? 0.9082 0.9179 1.0143 -0.2138 0.1126  -0.0107 366 ASN A O   
323  C CB  . ASN A 43  ? 0.7691 0.6786 0.8729 -0.2174 0.1363  0.0220  366 ASN A CB  
324  N N   . CYS A 44  ? 0.7999 0.7634 0.8959 -0.1955 0.1069  -0.0264 367 CYS A N   
325  C CA  . CYS A 44  ? 0.7060 0.7215 0.7975 -0.1832 0.0896  -0.0364 367 CYS A CA  
326  C C   . CYS A 44  ? 0.6635 0.6878 0.7574 -0.1923 0.0860  -0.0647 367 CYS A C   
327  O O   . CYS A 44  ? 0.6714 0.6875 0.7560 -0.1758 0.0790  -0.0688 367 CYS A O   
328  C CB  . CYS A 44  ? 0.6472 0.6597 0.7248 -0.1522 0.0792  -0.0187 367 CYS A CB  
329  S SG  . CYS A 44  ? 0.8256 0.7804 0.8954 -0.1363 0.0842  -0.0111 367 CYS A SG  
330  N N   . PRO A 45  ? 0.6930 0.7382 0.7994 -0.2195 0.0907  -0.0854 368 PRO A N   
331  C CA  . PRO A 45  ? 0.6120 0.6637 0.7204 -0.2299 0.0887  -0.1144 368 PRO A CA  
332  C C   . PRO A 45  ? 0.6651 0.7669 0.7656 -0.2150 0.0716  -0.1249 368 PRO A C   
333  O O   . PRO A 45  ? 0.7419 0.8445 0.8389 -0.2157 0.0689  -0.1444 368 PRO A O   
334  C CB  . PRO A 45  ? 0.6844 0.7502 0.8015 -0.2506 0.0937  -0.1266 368 PRO A CB  
335  C CG  . PRO A 45  ? 0.6955 0.7951 0.8168 -0.2508 0.0915  -0.1102 368 PRO A CG  
336  C CD  . PRO A 45  ? 0.7193 0.7884 0.8355 -0.2364 0.0954  -0.0826 368 PRO A CD  
337  N N   . ASP A 46  ? 0.6096 0.7522 0.7059 -0.2000 0.0604  -0.1122 369 ASP A N   
338  C CA  . ASP A 46  ? 0.5429 0.7300 0.6300 -0.1830 0.0445  -0.1184 369 ASP A CA  
339  C C   . ASP A 46  ? 0.4305 0.5944 0.5013 -0.1547 0.0374  -0.1027 369 ASP A C   
340  O O   . ASP A 46  ? 0.4345 0.6293 0.4955 -0.1384 0.0248  -0.1026 369 ASP A O   
341  C CB  . ASP A 46  ? 0.4876 0.7296 0.5782 -0.1794 0.0361  -0.1138 369 ASP A CB  
342  C CG  . ASP A 46  ? 0.5420 0.7704 0.6294 -0.1653 0.0371  -0.0876 369 ASP A CG  
343  O OD1 . ASP A 46  ? 0.5708 0.7537 0.6600 -0.1701 0.0484  -0.0750 369 ASP A OD1 
344  O OD2 . ASP A 46  ? 0.5663 0.8297 0.6488 -0.1483 0.0265  -0.0800 369 ASP A OD2 
345  N N   . TYR A 47  ? 0.4400 0.5515 0.5078 -0.1487 0.0455  -0.0891 370 TYR A N   
346  C CA  . TYR A 47  ? 0.3583 0.4532 0.4130 -0.1231 0.0390  -0.0717 370 TYR A CA  
347  C C   . TYR A 47  ? 0.4097 0.5194 0.4541 -0.1125 0.0301  -0.0820 370 TYR A C   
348  O O   . TYR A 47  ? 0.3987 0.5227 0.4324 -0.0937 0.0198  -0.0711 370 TYR A O   
349  C CB  . TYR A 47  ? 0.4420 0.4830 0.4964 -0.1189 0.0496  -0.0585 370 TYR A CB  
350  C CG  . TYR A 47  ? 0.4533 0.4834 0.4963 -0.0943 0.0428  -0.0410 370 TYR A CG  
351  C CD1 . TYR A 47  ? 0.4327 0.4726 0.4721 -0.0819 0.0373  -0.0224 370 TYR A CD1 
352  C CD2 . TYR A 47  ? 0.4677 0.4811 0.5041 -0.0844 0.0421  -0.0449 370 TYR A CD2 
353  C CE1 . TYR A 47  ? 0.4673 0.4988 0.4972 -0.0621 0.0312  -0.0089 370 TYR A CE1 
354  C CE2 . TYR A 47  ? 0.4770 0.4844 0.5046 -0.0647 0.0364  -0.0300 370 TYR A CE2 
355  C CZ  . TYR A 47  ? 0.4450 0.4607 0.4697 -0.0546 0.0308  -0.0125 370 TYR A CZ  
356  O OH  . TYR A 47  ? 0.3866 0.3973 0.4037 -0.0377 0.0253  0.0001  370 TYR A OH  
357  N N   . TYR A 48  ? 0.4611 0.5661 0.5076 -0.1243 0.0346  -0.1027 371 TYR A N   
358  C CA  . TYR A 48  ? 0.4563 0.5747 0.4917 -0.1144 0.0278  -0.1121 371 TYR A CA  
359  C C   . TYR A 48  ? 0.4181 0.5921 0.4505 -0.1169 0.0173  -0.1256 371 TYR A C   
360  O O   . TYR A 48  ? 0.4213 0.6131 0.4425 -0.1077 0.0108  -0.1315 371 TYR A O   
361  C CB  . TYR A 48  ? 0.3672 0.4543 0.4045 -0.1228 0.0378  -0.1286 371 TYR A CB  
362  C CG  . TYR A 48  ? 0.4070 0.4429 0.4443 -0.1127 0.0462  -0.1123 371 TYR A CG  
363  C CD1 . TYR A 48  ? 0.4062 0.4347 0.4331 -0.0916 0.0415  -0.0975 371 TYR A CD1 
364  C CD2 . TYR A 48  ? 0.4960 0.4929 0.5436 -0.1240 0.0589  -0.1102 371 TYR A CD2 
365  C CE1 . TYR A 48  ? 0.4675 0.4562 0.4950 -0.0811 0.0483  -0.0828 371 TYR A CE1 
366  C CE2 . TYR A 48  ? 0.5125 0.4657 0.5591 -0.1117 0.0661  -0.0934 371 TYR A CE2 
367  C CZ  . TYR A 48  ? 0.5036 0.4558 0.5406 -0.0897 0.0602  -0.0805 371 TYR A CZ  
368  O OH  . TYR A 48  ? 0.5605 0.4764 0.5973 -0.0765 0.0665  -0.0645 371 TYR A OH  
369  N N   . ASP A 49  ? 0.3730 0.5777 0.4151 -0.1284 0.0158  -0.1300 372 ASP A N   
370  C CA  . ASP A 49  ? 0.3709 0.6336 0.4095 -0.1240 0.0039  -0.1365 372 ASP A CA  
371  C C   . ASP A 49  ? 0.4064 0.6785 0.4339 -0.0990 -0.0064 -0.1136 372 ASP A C   
372  O O   . ASP A 49  ? 0.4006 0.7103 0.4186 -0.0865 -0.0173 -0.1143 372 ASP A O   
373  C CB  . ASP A 49  ? 0.4728 0.7688 0.5275 -0.1453 0.0065  -0.1501 372 ASP A CB  
374  C CG  . ASP A 49  ? 0.6295 0.9126 0.6932 -0.1689 0.0177  -0.1728 372 ASP A CG  
375  O OD1 . ASP A 49  ? 0.6244 0.9133 0.6808 -0.1666 0.0168  -0.1867 372 ASP A OD1 
376  O OD2 . ASP A 49  ? 0.5389 0.8029 0.6155 -0.1875 0.0285  -0.1745 372 ASP A OD2 
377  N N   . VAL A 50  ? 0.2945 0.5326 0.3224 -0.0912 -0.0030 -0.0940 373 VAL A N   
378  C CA  . VAL A 50  ? 0.3000 0.5393 0.3178 -0.0689 -0.0114 -0.0738 373 VAL A CA  
379  C C   . VAL A 50  ? 0.3543 0.5615 0.3594 -0.0544 -0.0127 -0.0624 373 VAL A C   
380  O O   . VAL A 50  ? 0.3390 0.5569 0.3316 -0.0379 -0.0215 -0.0541 373 VAL A O   
381  C CB  . VAL A 50  ? 0.3608 0.5885 0.3865 -0.0696 -0.0074 -0.0607 373 VAL A CB  
382  C CG1 . VAL A 50  ? 0.3114 0.5341 0.3263 -0.0470 -0.0153 -0.0423 373 VAL A CG1 
383  C CG2 . VAL A 50  ? 0.3808 0.6470 0.4193 -0.0837 -0.0062 -0.0708 373 VAL A CG2 
384  N N   . ILE A 51  ? 0.3034 0.4715 0.3120 -0.0603 -0.0033 -0.0615 374 ILE A N   
385  C CA  . ILE A 51  ? 0.2982 0.4369 0.2978 -0.0481 -0.0028 -0.0506 374 ILE A CA  
386  C C   . ILE A 51  ? 0.3127 0.4549 0.3072 -0.0515 -0.0012 -0.0651 374 ILE A C   
387  O O   . ILE A 51  ? 0.3276 0.4531 0.3291 -0.0634 0.0078  -0.0783 374 ILE A O   
388  C CB  . ILE A 51  ? 0.3238 0.4231 0.3301 -0.0492 0.0062  -0.0403 374 ILE A CB  
389  C CG1 . ILE A 51  ? 0.3537 0.4548 0.3632 -0.0449 0.0043  -0.0261 374 ILE A CG1 
390  C CG2 . ILE A 51  ? 0.3494 0.4249 0.3486 -0.0376 0.0070  -0.0319 374 ILE A CG2 
391  C CD1 . ILE A 51  ? 0.2979 0.4171 0.2975 -0.0292 -0.0070 -0.0163 374 ILE A CD1 
392  N N   . LYS A 52  ? 0.2660 0.4288 0.2474 -0.0403 -0.0094 -0.0626 375 LYS A N   
393  C CA  . LYS A 52  ? 0.3387 0.5124 0.3126 -0.0418 -0.0087 -0.0754 375 LYS A CA  
394  C C   . LYS A 52  ? 0.3445 0.4936 0.3110 -0.0325 -0.0056 -0.0661 375 LYS A C   
395  O O   . LYS A 52  ? 0.3573 0.5150 0.3171 -0.0329 -0.0038 -0.0762 375 LYS A O   
396  C CB  . LYS A 52  ? 0.3143 0.5319 0.2771 -0.0356 -0.0190 -0.0781 375 LYS A CB  
397  C CG  . LYS A 52  ? 0.3265 0.5784 0.2982 -0.0455 -0.0222 -0.0909 375 LYS A CG  
398  C CD  . LYS A 52  ? 0.3692 0.6277 0.3503 -0.0654 -0.0151 -0.1168 375 LYS A CD  
399  C CE  . LYS A 52  ? 0.3549 0.6481 0.3478 -0.0799 -0.0166 -0.1319 375 LYS A CE  
400  N NZ  . LYS A 52  ? 0.3691 0.6689 0.3696 -0.0989 -0.0096 -0.1585 375 LYS A NZ  
401  N N   . ASN A 53  ? 0.3717 0.4943 0.3397 -0.0245 -0.0047 -0.0482 376 ASN A N   
402  C CA  . ASN A 53  ? 0.3441 0.4467 0.3078 -0.0167 -0.0015 -0.0392 376 ASN A CA  
403  C C   . ASN A 53  ? 0.3404 0.4111 0.3150 -0.0164 0.0049  -0.0312 376 ASN A C   
404  O O   . ASN A 53  ? 0.3073 0.3686 0.2811 -0.0085 0.0019  -0.0152 376 ASN A O   
405  C CB  . ASN A 53  ? 0.3435 0.4544 0.2947 -0.0052 -0.0093 -0.0228 376 ASN A CB  
406  C CG  . ASN A 53  ? 0.6505 0.7509 0.5965 0.0000  -0.0059 -0.0158 376 ASN A CG  
407  O OD1 . ASN A 53  ? 0.5731 0.6749 0.5099 0.0069  -0.0104 -0.0020 376 ASN A OD1 
408  N ND2 . ASN A 53  ? 0.4282 0.5181 0.3804 -0.0032 0.0026  -0.0256 376 ASN A ND2 
409  N N   . PRO A 54  ? 0.3045 0.3584 0.2889 -0.0248 0.0138  -0.0424 377 PRO A N   
410  C CA  . PRO A 54  ? 0.3786 0.4030 0.3721 -0.0230 0.0201  -0.0324 377 PRO A CA  
411  C C   . PRO A 54  ? 0.4252 0.4346 0.4175 -0.0114 0.0227  -0.0227 377 PRO A C   
412  O O   . PRO A 54  ? 0.3853 0.4015 0.3724 -0.0079 0.0235  -0.0282 377 PRO A O   
413  C CB  . PRO A 54  ? 0.4261 0.4342 0.4290 -0.0356 0.0300  -0.0480 377 PRO A CB  
414  C CG  . PRO A 54  ? 0.3636 0.3889 0.3619 -0.0413 0.0300  -0.0681 377 PRO A CG  
415  C CD  . PRO A 54  ? 0.4312 0.4919 0.4186 -0.0368 0.0187  -0.0647 377 PRO A CD  
416  N N   . MET A 55  ? 0.3432 0.3361 0.3403 -0.0053 0.0241  -0.0081 378 MET A N   
417  C CA  . MET A 55  ? 0.3259 0.3108 0.3233 0.0063  0.0255  0.0023  378 MET A CA  
418  C C   . MET A 55  ? 0.3737 0.3381 0.3785 0.0111  0.0302  0.0138  378 MET A C   
419  O O   . MET A 55  ? 0.3479 0.3104 0.3547 0.0067  0.0291  0.0192  378 MET A O   
420  C CB  . MET A 55  ? 0.3500 0.3528 0.3399 0.0116  0.0162  0.0124  378 MET A CB  
421  C CG  . MET A 55  ? 0.2467 0.2494 0.2375 0.0204  0.0173  0.0202  378 MET A CG  
422  S SD  . MET A 55  ? 0.3429 0.3482 0.3334 0.0224  0.0250  0.0078  378 MET A SD  
423  C CE  . MET A 55  ? 0.2964 0.3251 0.2741 0.0156  0.0194  0.0007  378 MET A CE  
424  N N   . SER A 56  ? 0.3782 0.3301 0.3867 0.0211  0.0358  0.0180  379 SER A N   
425  C CA  . SER A 56  ? 0.3866 0.3208 0.4007 0.0294  0.0405  0.0312  379 SER A CA  
426  C C   . SER A 56  ? 0.3742 0.3147 0.3898 0.0439  0.0401  0.0392  379 SER A C   
427  O O   . SER A 56  ? 0.3523 0.3061 0.3662 0.0459  0.0390  0.0326  379 SER A O   
428  C CB  . SER A 56  ? 0.3922 0.2957 0.4118 0.0263  0.0522  0.0256  379 SER A CB  
429  O OG  . SER A 56  ? 0.4263 0.3194 0.4476 0.0327  0.0588  0.0152  379 SER A OG  
430  N N   . PHE A 57  ? 0.3394 0.2738 0.3584 0.0541  0.0415  0.0539  380 PHE A N   
431  C CA  . PHE A 57  ? 0.3317 0.2772 0.3538 0.0687  0.0411  0.0613  380 PHE A CA  
432  C C   . PHE A 57  ? 0.3846 0.3201 0.4104 0.0762  0.0495  0.0518  380 PHE A C   
433  O O   . PHE A 57  ? 0.3873 0.3425 0.4148 0.0831  0.0482  0.0500  380 PHE A O   
434  C CB  . PHE A 57  ? 0.3662 0.3082 0.3907 0.0801  0.0418  0.0784  380 PHE A CB  
435  C CG  . PHE A 57  ? 0.3779 0.3356 0.3985 0.0750  0.0331  0.0865  380 PHE A CG  
436  C CD1 . PHE A 57  ? 0.3584 0.3347 0.3748 0.0653  0.0241  0.0802  380 PHE A CD1 
437  C CD2 . PHE A 57  ? 0.3150 0.2698 0.3348 0.0796  0.0338  0.0986  380 PHE A CD2 
438  C CE1 . PHE A 57  ? 0.2942 0.2828 0.3068 0.0622  0.0165  0.0856  380 PHE A CE1 
439  C CE2 . PHE A 57  ? 0.3481 0.3215 0.3637 0.0728  0.0256  0.0997  380 PHE A CE2 
440  C CZ  . PHE A 57  ? 0.3189 0.3072 0.3313 0.0656  0.0172  0.0938  380 PHE A CZ  
441  N N   . SER A 58  ? 0.4295 0.3349 0.4568 0.0743  0.0589  0.0446  381 SER A N   
442  C CA  . SER A 58  ? 0.4684 0.3614 0.4990 0.0833  0.0677  0.0338  381 SER A CA  
443  C C   . SER A 58  ? 0.4682 0.3811 0.4953 0.0754  0.0655  0.0163  381 SER A C   
444  O O   . SER A 58  ? 0.4117 0.3338 0.4408 0.0857  0.0693  0.0101  381 SER A O   
445  C CB  . SER A 58  ? 0.4648 0.3155 0.4977 0.0818  0.0790  0.0289  381 SER A CB  
446  O OG  . SER A 58  ? 0.6319 0.4757 0.6623 0.0612  0.0783  0.0191  381 SER A OG  
447  N N   . CYS A 59  ? 0.4327 0.3557 0.4539 0.0588  0.0597  0.0091  382 CYS A N   
448  C CA  . CYS A 59  ? 0.4554 0.4017 0.4708 0.0524  0.0568  -0.0040 382 CYS A CA  
449  C C   . CYS A 59  ? 0.4149 0.3903 0.4293 0.0589  0.0515  0.0049  382 CYS A C   
450  O O   . CYS A 59  ? 0.4329 0.4246 0.4459 0.0619  0.0540  -0.0031 382 CYS A O   
451  C CB  . CYS A 59  ? 0.3933 0.3493 0.4020 0.0363  0.0500  -0.0091 382 CYS A CB  
452  S SG  . CYS A 59  ? 0.4949 0.4266 0.5061 0.0228  0.0549  -0.0209 382 CYS A SG  
453  N N   . ILE A 60  ? 0.3703 0.3540 0.3854 0.0598  0.0444  0.0205  383 ILE A N   
454  C CA  . ILE A 60  ? 0.3753 0.3857 0.3906 0.0626  0.0392  0.0285  383 ILE A CA  
455  C C   . ILE A 60  ? 0.3674 0.3857 0.3912 0.0776  0.0450  0.0303  383 ILE A C   
456  O O   . ILE A 60  ? 0.3092 0.3521 0.3339 0.0789  0.0455  0.0282  383 ILE A O   
457  C CB  . ILE A 60  ? 0.3800 0.3946 0.3943 0.0591  0.0305  0.0415  383 ILE A CB  
458  C CG1 . ILE A 60  ? 0.2807 0.2917 0.2863 0.0465  0.0249  0.0384  383 ILE A CG1 
459  C CG2 . ILE A 60  ? 0.3008 0.3405 0.3171 0.0602  0.0257  0.0488  383 ILE A CG2 
460  C CD1 . ILE A 60  ? 0.2247 0.2386 0.2281 0.0436  0.0165  0.0484  383 ILE A CD1 
461  N N   . LYS A 61  ? 0.3934 0.3919 0.4232 0.0897  0.0502  0.0346  384 LYS A N   
462  C CA  . LYS A 61  ? 0.3825 0.3887 0.4204 0.1078  0.0561  0.0365  384 LYS A CA  
463  C C   . LYS A 61  ? 0.4109 0.4196 0.4487 0.1109  0.0637  0.0203  384 LYS A C   
464  O O   . LYS A 61  ? 0.3396 0.3727 0.3828 0.1216  0.0664  0.0191  384 LYS A O   
465  C CB  . LYS A 61  ? 0.4394 0.4181 0.4815 0.1219  0.0613  0.0455  384 LYS A CB  
466  C CG  . LYS A 61  ? 0.4309 0.4165 0.4735 0.1238  0.0543  0.0631  384 LYS A CG  
467  C CD  . LYS A 61  ? 0.4568 0.4122 0.5010 0.1371  0.0607  0.0739  384 LYS A CD  
468  C CE  . LYS A 61  ? 0.5140 0.4815 0.5548 0.1338  0.0525  0.0881  384 LYS A CE  
469  N NZ  . LYS A 61  ? 0.3978 0.3377 0.4351 0.1361  0.0573  0.0952  384 LYS A NZ  
470  N N   . THR A 62  ? 0.4235 0.4110 0.4557 0.1016  0.0675  0.0064  385 THR A N   
471  C CA  . THR A 62  ? 0.4579 0.4491 0.4886 0.1041  0.0748  -0.0119 385 THR A CA  
472  C C   . THR A 62  ? 0.4189 0.4490 0.4444 0.0961  0.0707  -0.0149 385 THR A C   
473  O O   . THR A 62  ? 0.3941 0.4450 0.4218 0.1044  0.0760  -0.0222 385 THR A O   
474  C CB  . THR A 62  ? 0.4493 0.4106 0.4754 0.0940  0.0792  -0.0277 385 THR A CB  
475  O OG1 . THR A 62  ? 0.5138 0.4359 0.5457 0.1037  0.0869  -0.0262 385 THR A OG1 
476  C CG2 . THR A 62  ? 0.4853 0.4586 0.5068 0.0920  0.0844  -0.0494 385 THR A CG2 
477  N N   . LYS A 63  ? 0.3578 0.3983 0.3761 0.0808  0.0619  -0.0084 386 LYS A N   
478  C CA  . LYS A 63  ? 0.3805 0.4540 0.3927 0.0729  0.0586  -0.0073 386 LYS A CA  
479  C C   . LYS A 63  ? 0.3767 0.4770 0.3970 0.0797  0.0582  0.0036  386 LYS A C   
480  O O   . LYS A 63  ? 0.3482 0.4773 0.3673 0.0785  0.0611  0.0008  386 LYS A O   
481  C CB  . LYS A 63  ? 0.3224 0.3960 0.3248 0.0577  0.0495  -0.0005 386 LYS A CB  
482  C CG  . LYS A 63  ? 0.3593 0.4180 0.3538 0.0497  0.0492  -0.0126 386 LYS A CG  
483  C CD  . LYS A 63  ? 0.4056 0.4639 0.3922 0.0387  0.0400  -0.0046 386 LYS A CD  
484  C CE  . LYS A 63  ? 0.4202 0.5025 0.3953 0.0321  0.0361  -0.0004 386 LYS A CE  
485  N NZ  . LYS A 63  ? 0.3391 0.4184 0.3047 0.0243  0.0283  0.0025  386 LYS A NZ  
486  N N   . LEU A 64  ? 0.2941 0.3893 0.3224 0.0859  0.0546  0.0158  387 LEU A N   
487  C CA  . LEU A 64  ? 0.3163 0.4415 0.3545 0.0930  0.0542  0.0238  387 LEU A CA  
488  C C   . LEU A 64  ? 0.3623 0.5001 0.4084 0.1102  0.0635  0.0155  387 LEU A C   
489  O O   . LEU A 64  ? 0.3733 0.5469 0.4240 0.1112  0.0659  0.0145  387 LEU A O   
490  C CB  . LEU A 64  ? 0.2263 0.3460 0.2708 0.0982  0.0485  0.0367  387 LEU A CB  
491  C CG  . LEU A 64  ? 0.2821 0.4020 0.3215 0.0828  0.0387  0.0453  387 LEU A CG  
492  C CD1 . LEU A 64  ? 0.3134 0.4234 0.3566 0.0893  0.0338  0.0554  387 LEU A CD1 
493  C CD2 . LEU A 64  ? 0.3395 0.4938 0.3818 0.0736  0.0364  0.0482  387 LEU A CD2 
494  N N   . LYS A 65  ? 0.3795 0.4876 0.4274 0.1239  0.0696  0.0092  388 LYS A N   
495  C CA  . LYS A 65  ? 0.3470 0.4618 0.4019 0.1434  0.0792  0.0000  388 LYS A CA  
496  C C   . LYS A 65  ? 0.4501 0.5858 0.4999 0.1385  0.0847  -0.0157 388 LYS A C   
497  O O   . LYS A 65  ? 0.4418 0.6055 0.4983 0.1514  0.0908  -0.0210 388 LYS A O   
498  C CB  . LYS A 65  ? 0.4616 0.5306 0.5172 0.1567  0.0856  -0.0044 388 LYS A CB  
499  C CG  . LYS A 65  ? 0.5087 0.5770 0.5716 0.1813  0.0960  -0.0130 388 LYS A CG  
500  C CD  . LYS A 65  ? 0.6431 0.6570 0.7052 0.1922  0.1036  -0.0177 388 LYS A CD  
501  N N   . LYS A 66  ? 0.3764 0.5033 0.4140 0.1211  0.0826  -0.0230 389 LYS A N   
502  C CA  . LYS A 66  ? 0.3442 0.4925 0.3741 0.1162  0.0875  -0.0376 389 LYS A CA  
503  C C   . LYS A 66  ? 0.3438 0.5317 0.3694 0.1025  0.0836  -0.0284 389 LYS A C   
504  O O   . LYS A 66  ? 0.3459 0.5564 0.3633 0.0973  0.0875  -0.0372 389 LYS A O   
505  C CB  . LYS A 66  ? 0.4125 0.5344 0.4309 0.1059  0.0877  -0.0516 389 LYS A CB  
506  C CG  . LYS A 66  ? 0.4819 0.5631 0.5045 0.1169  0.0944  -0.0645 389 LYS A CG  
507  C CD  . LYS A 66  ? 0.5286 0.5936 0.5412 0.1058  0.0965  -0.0847 389 LYS A CD  
508  C CE  . LYS A 66  ? 0.5670 0.5875 0.5849 0.1148  0.1047  -0.0985 389 LYS A CE  
509  N NZ  . LYS A 66  ? 0.7530 0.7710 0.7649 0.1127  0.1119  -0.1268 389 LYS A NZ  
510  N N   . GLY A 67  ? 0.2983 0.4955 0.3288 0.0962  0.0766  -0.0112 390 GLY A N   
511  C CA  . GLY A 67  ? 0.2895 0.5185 0.3159 0.0811  0.0741  -0.0023 390 GLY A CA  
512  C C   . GLY A 67  ? 0.3403 0.5602 0.3498 0.0646  0.0702  -0.0016 390 GLY A C   
513  O O   . GLY A 67  ? 0.4203 0.6659 0.4217 0.0554  0.0726  0.0004  390 GLY A O   
514  N N   . GLN A 68  ? 0.3534 0.5395 0.3569 0.0612  0.0645  -0.0021 391 GLN A N   
515  C CA  . GLN A 68  ? 0.3447 0.5249 0.3323 0.0491  0.0607  -0.0031 391 GLN A CA  
516  C C   . GLN A 68  ? 0.3899 0.5646 0.3719 0.0366  0.0520  0.0135  391 GLN A C   
517  O O   . GLN A 68  ? 0.4451 0.6138 0.4136 0.0288  0.0479  0.0150  391 GLN A O   
518  C CB  . GLN A 68  ? 0.2915 0.4433 0.2758 0.0517  0.0604  -0.0164 391 GLN A CB  
519  C CG  . GLN A 68  ? 0.4159 0.5727 0.4006 0.0606  0.0696  -0.0364 391 GLN A CG  
520  C CD  . GLN A 68  ? 0.4281 0.5551 0.4115 0.0606  0.0704  -0.0514 391 GLN A CD  
521  O OE1 . GLN A 68  ? 0.4335 0.5318 0.4230 0.0609  0.0674  -0.0465 391 GLN A OE1 
522  N NE2 . GLN A 68  ? 0.4559 0.5915 0.4311 0.0591  0.0748  -0.0706 391 GLN A NE2 
523  N N   . TYR A 69  ? 0.2925 0.4705 0.2843 0.0353  0.0491  0.0250  392 TYR A N   
524  C CA  . TYR A 69  ? 0.3309 0.5042 0.3177 0.0229  0.0420  0.0391  392 TYR A CA  
525  C C   . TYR A 69  ? 0.3831 0.5846 0.3694 0.0135  0.0459  0.0468  392 TYR A C   
526  O O   . TYR A 69  ? 0.3248 0.5503 0.3241 0.0166  0.0504  0.0460  392 TYR A O   
527  C CB  . TYR A 69  ? 0.2819 0.4408 0.2789 0.0250  0.0358  0.0451  392 TYR A CB  
528  C CG  . TYR A 69  ? 0.2831 0.4135 0.2790 0.0310  0.0320  0.0411  392 TYR A CG  
529  C CD1 . TYR A 69  ? 0.2938 0.4074 0.2776 0.0252  0.0272  0.0413  392 TYR A CD1 
530  C CD2 . TYR A 69  ? 0.2406 0.3627 0.2476 0.0428  0.0336  0.0383  392 TYR A CD2 
531  C CE1 . TYR A 69  ? 0.2768 0.3684 0.2611 0.0288  0.0243  0.0373  392 TYR A CE1 
532  C CE2 . TYR A 69  ? 0.3020 0.3980 0.3081 0.0463  0.0314  0.0362  392 TYR A CE2 
533  C CZ  . TYR A 69  ? 0.2992 0.3813 0.2947 0.0382  0.0270  0.0350  392 TYR A CZ  
534  O OH  . TYR A 69  ? 0.2676 0.3280 0.2636 0.0398  0.0256  0.0325  392 TYR A OH  
535  N N   . ALA A 70  ? 0.2911 0.4908 0.2627 0.0022  0.0445  0.0550  393 ALA A N   
536  C CA  . ALA A 70  ? 0.3769 0.5998 0.3460 -0.0096 0.0493  0.0647  393 ALA A CA  
537  C C   . ALA A 70  ? 0.4033 0.6164 0.3767 -0.0223 0.0447  0.0770  393 ALA A C   
538  O O   . ALA A 70  ? 0.3030 0.5384 0.2834 -0.0328 0.0494  0.0825  393 ALA A O   
539  C CB  . ALA A 70  ? 0.3981 0.6244 0.3468 -0.0147 0.0517  0.0694  393 ALA A CB  
540  N N   . TYR A 71  ? 0.3378 0.5197 0.3077 -0.0222 0.0361  0.0799  394 TYR A N   
541  C CA  . TYR A 71  ? 0.3659 0.5329 0.3378 -0.0336 0.0311  0.0888  394 TYR A CA  
542  C C   . TYR A 71  ? 0.3275 0.4797 0.3096 -0.0261 0.0235  0.0836  394 TYR A C   
543  O O   . TYR A 71  ? 0.2796 0.4208 0.2608 -0.0139 0.0211  0.0769  394 TYR A O   
544  C CB  . TYR A 71  ? 0.3744 0.5155 0.3276 -0.0407 0.0281  0.0998  394 TYR A CB  
545  C CG  . TYR A 71  ? 0.5287 0.6823 0.4680 -0.0475 0.0353  0.1086  394 TYR A CG  
546  C CD1 . TYR A 71  ? 0.5480 0.7060 0.4730 -0.0388 0.0366  0.1064  394 TYR A CD1 
547  C CD2 . TYR A 71  ? 0.5708 0.7327 0.5116 -0.0632 0.0409  0.1182  394 TYR A CD2 
548  C CE1 . TYR A 71  ? 0.5815 0.7494 0.4955 -0.0423 0.0415  0.1114  394 TYR A CE1 
549  C CE2 . TYR A 71  ? 0.6663 0.8338 0.5965 -0.0667 0.0463  0.1231  394 TYR A CE2 
550  C CZ  . TYR A 71  ? 0.7057 0.8766 0.6222 -0.0555 0.0464  0.1203  394 TYR A CZ  
551  O OH  . TYR A 71  ? 0.7945 0.9738 0.6998 -0.0582 0.0515  0.1259  394 TYR A OH  
552  N N   . PRO A 72  ? 0.2954 0.4483 0.2866 -0.0345 0.0202  0.0861  395 PRO A N   
553  C CA  . PRO A 72  ? 0.3290 0.4710 0.3279 -0.0274 0.0128  0.0819  395 PRO A CA  
554  C C   . PRO A 72  ? 0.3363 0.4460 0.3234 -0.0218 0.0063  0.0824  395 PRO A C   
555  O O   . PRO A 72  ? 0.3066 0.4106 0.2981 -0.0111 0.0028  0.0778  395 PRO A O   
556  C CB  . PRO A 72  ? 0.2632 0.4123 0.2702 -0.0417 0.0104  0.0840  395 PRO A CB  
557  C CG  . PRO A 72  ? 0.2939 0.4689 0.3052 -0.0532 0.0182  0.0869  395 PRO A CG  
558  C CD  . PRO A 72  ? 0.3357 0.5064 0.3329 -0.0512 0.0241  0.0912  395 PRO A CD  
559  N N   . SER A 73  ? 0.3257 0.4158 0.2976 -0.0279 0.0052  0.0888  396 SER A N   
560  C CA  . SER A 73  ? 0.3279 0.3921 0.2891 -0.0214 -0.0011 0.0892  396 SER A CA  
561  C C   . SER A 73  ? 0.3154 0.3817 0.2738 -0.0097 -0.0004 0.0829  396 SER A C   
562  O O   . SER A 73  ? 0.3217 0.3742 0.2772 -0.0031 -0.0055 0.0803  396 SER A O   
563  C CB  . SER A 73  ? 0.3420 0.3876 0.2870 -0.0281 -0.0016 0.0989  396 SER A CB  
564  O OG  . SER A 73  ? 0.3743 0.4330 0.3107 -0.0288 0.0046  0.1027  396 SER A OG  
565  N N   . GLU A 74  ? 0.3207 0.4050 0.2799 -0.0080 0.0063  0.0796  397 GLU A N   
566  C CA  . GLU A 74  ? 0.2899 0.3751 0.2464 0.0007  0.0078  0.0711  397 GLU A CA  
567  C C   . GLU A 74  ? 0.2803 0.3608 0.2489 0.0089  0.0069  0.0641  397 GLU A C   
568  O O   . GLU A 74  ? 0.2964 0.3666 0.2629 0.0136  0.0054  0.0586  397 GLU A O   
569  C CB  . GLU A 74  ? 0.3083 0.4146 0.2628 0.0008  0.0157  0.0668  397 GLU A CB  
570  C CG  . GLU A 74  ? 0.3107 0.4225 0.2491 -0.0054 0.0172  0.0744  397 GLU A CG  
571  C CD  . GLU A 74  ? 0.4102 0.5487 0.3473 -0.0059 0.0259  0.0705  397 GLU A CD  
572  O OE1 . GLU A 74  ? 0.3991 0.5499 0.3487 -0.0002 0.0306  0.0605  397 GLU A OE1 
573  O OE2 . GLU A 74  ? 0.5197 0.6673 0.4426 -0.0107 0.0283  0.0779  397 GLU A OE2 
574  N N   . PHE A 75  ? 0.2629 0.3524 0.2443 0.0103  0.0082  0.0651  398 PHE A N   
575  C CA  . PHE A 75  ? 0.2574 0.3418 0.2487 0.0196  0.0075  0.0620  398 PHE A CA  
576  C C   . PHE A 75  ? 0.3101 0.3775 0.2983 0.0193  0.0001  0.0649  398 PHE A C   
577  O O   . PHE A 75  ? 0.2445 0.3010 0.2336 0.0251  -0.0002 0.0621  398 PHE A O   
578  C CB  . PHE A 75  ? 0.2398 0.3436 0.2444 0.0228  0.0096  0.0638  398 PHE A CB  
579  C CG  . PHE A 75  ? 0.2517 0.3520 0.2648 0.0326  0.0073  0.0650  398 PHE A CG  
580  C CD1 . PHE A 75  ? 0.2403 0.3345 0.2581 0.0448  0.0125  0.0619  398 PHE A CD1 
581  C CD2 . PHE A 75  ? 0.2284 0.3310 0.2439 0.0299  0.0005  0.0694  398 PHE A CD2 
582  C CE1 . PHE A 75  ? 0.2273 0.3175 0.2512 0.0548  0.0114  0.0661  398 PHE A CE1 
583  C CE2 . PHE A 75  ? 0.2980 0.4017 0.3196 0.0399  -0.0014 0.0718  398 PHE A CE2 
584  C CZ  . PHE A 75  ? 0.2130 0.3104 0.2385 0.0528  0.0042  0.0718  398 PHE A CZ  
585  N N   . VAL A 76  ? 0.2628 0.3275 0.2474 0.0121  -0.0052 0.0700  399 VAL A N   
586  C CA  . VAL A 76  ? 0.2183 0.2686 0.1994 0.0131  -0.0122 0.0713  399 VAL A CA  
587  C C   . VAL A 76  ? 0.2933 0.3310 0.2644 0.0153  -0.0139 0.0694  399 VAL A C   
588  O O   . VAL A 76  ? 0.2973 0.3285 0.2691 0.0200  -0.0165 0.0675  399 VAL A O   
589  C CB  . VAL A 76  ? 0.3187 0.3654 0.2973 0.0046  -0.0168 0.0749  399 VAL A CB  
590  C CG1 . VAL A 76  ? 0.2963 0.3262 0.2684 0.0069  -0.0237 0.0745  399 VAL A CG1 
591  C CG2 . VAL A 76  ? 0.2133 0.2786 0.2043 0.0017  -0.0164 0.0743  399 VAL A CG2 
592  N N   . LYS A 77  ? 0.3050 0.3432 0.2666 0.0120  -0.0121 0.0700  400 LYS A N   
593  C CA  . LYS A 77  ? 0.3215 0.3549 0.2737 0.0147  -0.0142 0.0674  400 LYS A CA  
594  C C   . LYS A 77  ? 0.2968 0.3328 0.2553 0.0185  -0.0110 0.0589  400 LYS A C   
595  O O   . LYS A 77  ? 0.3353 0.3678 0.2921 0.0204  -0.0141 0.0559  400 LYS A O   
596  C CB  . LYS A 77  ? 0.3527 0.3921 0.2932 0.0116  -0.0121 0.0701  400 LYS A CB  
597  C CG  . LYS A 77  ? 0.4632 0.5016 0.3916 0.0152  -0.0164 0.0698  400 LYS A CG  
598  C CD  . LYS A 77  ? 0.5870 0.6345 0.5019 0.0136  -0.0142 0.0747  400 LYS A CD  
599  C CE  . LYS A 77  ? 0.6165 0.6827 0.5337 0.0123  -0.0076 0.0653  400 LYS A CE  
600  N N   . ASP A 78  ? 0.2774 0.3192 0.2441 0.0197  -0.0044 0.0547  401 ASP A N   
601  C CA  . ASP A 78  ? 0.2726 0.3098 0.2452 0.0226  -0.0002 0.0466  401 ASP A CA  
602  C C   . ASP A 78  ? 0.3031 0.3309 0.2829 0.0261  -0.0018 0.0501  401 ASP A C   
603  O O   . ASP A 78  ? 0.2887 0.3100 0.2698 0.0254  -0.0011 0.0461  401 ASP A O   
604  C CB  . ASP A 78  ? 0.2418 0.2838 0.2205 0.0254  0.0080  0.0409  401 ASP A CB  
605  C CG  . ASP A 78  ? 0.3094 0.3602 0.2807 0.0225  0.0115  0.0312  401 ASP A CG  
606  O OD1 . ASP A 78  ? 0.3014 0.3566 0.2628 0.0185  0.0074  0.0294  401 ASP A OD1 
607  O OD2 . ASP A 78  ? 0.3230 0.3789 0.2983 0.0255  0.0185  0.0244  401 ASP A OD2 
608  N N   . VAL A 79  ? 0.2716 0.3015 0.2563 0.0289  -0.0038 0.0573  402 VAL A N   
609  C CA  . VAL A 79  ? 0.2775 0.3027 0.2671 0.0331  -0.0057 0.0615  402 VAL A CA  
610  C C   . VAL A 79  ? 0.2560 0.2780 0.2390 0.0307  -0.0120 0.0617  402 VAL A C   
611  O O   . VAL A 79  ? 0.2686 0.2868 0.2534 0.0318  -0.0113 0.0613  402 VAL A O   
612  C CB  . VAL A 79  ? 0.2655 0.3001 0.2608 0.0369  -0.0076 0.0677  402 VAL A CB  
613  C CG1 . VAL A 79  ? 0.2367 0.2700 0.2345 0.0420  -0.0099 0.0725  402 VAL A CG1 
614  C CG2 . VAL A 79  ? 0.2510 0.2933 0.2542 0.0423  -0.0011 0.0676  402 VAL A CG2 
615  N N   . GLN A 80  ? 0.2736 0.2968 0.2488 0.0278  -0.0175 0.0627  403 GLN A N   
616  C CA  . GLN A 80  ? 0.2554 0.2759 0.2241 0.0286  -0.0235 0.0625  403 GLN A CA  
617  C C   . GLN A 80  ? 0.2885 0.3114 0.2554 0.0277  -0.0220 0.0569  403 GLN A C   
618  O O   . GLN A 80  ? 0.3026 0.3281 0.2692 0.0294  -0.0248 0.0558  403 GLN A O   
619  C CB  . GLN A 80  ? 0.2971 0.3119 0.2570 0.0262  -0.0278 0.0633  403 GLN A CB  
620  C CG  . GLN A 80  ? 0.2905 0.2974 0.2450 0.0284  -0.0330 0.0587  403 GLN A CG  
621  C CD  . GLN A 80  ? 0.3986 0.4054 0.3589 0.0302  -0.0346 0.0557  403 GLN A CD  
622  O OE1 . GLN A 80  ? 0.3604 0.3689 0.3251 0.0296  -0.0342 0.0571  403 GLN A OE1 
623  N NE2 . GLN A 80  ? 0.3504 0.3600 0.3109 0.0325  -0.0364 0.0521  403 GLN A NE2 
624  N N   . LEU A 81  ? 0.3049 0.3305 0.2711 0.0245  -0.0176 0.0519  404 LEU A N   
625  C CA  . LEU A 81  ? 0.2714 0.3031 0.2368 0.0215  -0.0161 0.0436  404 LEU A CA  
626  C C   . LEU A 81  ? 0.2590 0.2864 0.2338 0.0195  -0.0117 0.0410  404 LEU A C   
627  O O   . LEU A 81  ? 0.2877 0.3222 0.2632 0.0164  -0.0127 0.0364  404 LEU A O   
628  C CB  . LEU A 81  ? 0.2425 0.2790 0.2055 0.0183  -0.0115 0.0369  404 LEU A CB  
629  C CG  . LEU A 81  ? 0.2787 0.3235 0.2422 0.0131  -0.0089 0.0245  404 LEU A CG  
630  C CD1 . LEU A 81  ? 0.2610 0.3211 0.2169 0.0139  -0.0162 0.0235  404 LEU A CD1 
631  C CD2 . LEU A 81  ? 0.2847 0.3347 0.2457 0.0109  -0.0037 0.0163  404 LEU A CD2 
632  N N   . ILE A 82  ? 0.3036 0.3209 0.2857 0.0216  -0.0064 0.0449  405 ILE A N   
633  C CA  . ILE A 82  ? 0.2629 0.2728 0.2523 0.0205  -0.0015 0.0465  405 ILE A CA  
634  C C   . ILE A 82  ? 0.2781 0.2957 0.2659 0.0218  -0.0068 0.0511  405 ILE A C   
635  O O   . ILE A 82  ? 0.2972 0.3180 0.2881 0.0170  -0.0045 0.0487  405 ILE A O   
636  C CB  . ILE A 82  ? 0.2482 0.2473 0.2437 0.0267  0.0040  0.0535  405 ILE A CB  
637  C CG1 . ILE A 82  ? 0.2971 0.2906 0.2944 0.0276  0.0097  0.0476  405 ILE A CG1 
638  C CG2 . ILE A 82  ? 0.2447 0.2333 0.2457 0.0261  0.0101  0.0581  405 ILE A CG2 
639  C CD1 . ILE A 82  ? 0.3126 0.2972 0.3166 0.0367  0.0156  0.0545  405 ILE A CD1 
640  N N   . PHE A 83  ? 0.2588 0.2807 0.2422 0.0275  -0.0135 0.0567  406 PHE A N   
641  C CA  . PHE A 83  ? 0.2345 0.2641 0.2163 0.0305  -0.0181 0.0596  406 PHE A CA  
642  C C   . PHE A 83  ? 0.3045 0.3450 0.2817 0.0294  -0.0227 0.0536  406 PHE A C   
643  O O   . PHE A 83  ? 0.2824 0.3333 0.2608 0.0300  -0.0237 0.0532  406 PHE A O   
644  C CB  . PHE A 83  ? 0.2625 0.2907 0.2417 0.0348  -0.0230 0.0613  406 PHE A CB  
645  C CG  . PHE A 83  ? 0.2643 0.2890 0.2488 0.0362  -0.0193 0.0650  406 PHE A CG  
646  C CD1 . PHE A 83  ? 0.3551 0.3790 0.3389 0.0356  -0.0219 0.0628  406 PHE A CD1 
647  C CD2 . PHE A 83  ? 0.2732 0.2962 0.2633 0.0388  -0.0129 0.0719  406 PHE A CD2 
648  C CE1 . PHE A 83  ? 0.3030 0.3309 0.2925 0.0382  -0.0192 0.0661  406 PHE A CE1 
649  C CE2 . PHE A 83  ? 0.3245 0.3465 0.3189 0.0424  -0.0098 0.0747  406 PHE A CE2 
650  C CZ  . PHE A 83  ? 0.2889 0.3165 0.2834 0.0425  -0.0134 0.0714  406 PHE A CZ  
651  N N   . ASP A 84  ? 0.3126 0.3541 0.2839 0.0288  -0.0255 0.0496  407 ASP A N   
652  C CA  . ASP A 84  ? 0.2475 0.3031 0.2140 0.0300  -0.0301 0.0445  407 ASP A CA  
653  C C   . ASP A 84  ? 0.2724 0.3402 0.2456 0.0218  -0.0254 0.0366  407 ASP A C   
654  O O   . ASP A 84  ? 0.2669 0.3528 0.2409 0.0223  -0.0282 0.0329  407 ASP A O   
655  C CB  . ASP A 84  ? 0.2964 0.3510 0.2531 0.0324  -0.0338 0.0445  407 ASP A CB  
656  C CG  . ASP A 84  ? 0.3619 0.3985 0.3142 0.0354  -0.0367 0.0481  407 ASP A CG  
657  O OD1 . ASP A 84  ? 0.3993 0.4286 0.3554 0.0362  -0.0378 0.0475  407 ASP A OD1 
658  O OD2 . ASP A 84  ? 0.4023 0.4324 0.3481 0.0348  -0.0374 0.0500  407 ASP A OD2 
659  N N   . ASN A 85  ? 0.2610 0.3204 0.2396 0.0138  -0.0181 0.0325  408 ASN A N   
660  C CA  . ASN A 85  ? 0.2520 0.3191 0.2384 0.0030  -0.0125 0.0232  408 ASN A CA  
661  C C   . ASN A 85  ? 0.2604 0.3278 0.2540 0.0002  -0.0087 0.0280  408 ASN A C   
662  O O   . ASN A 85  ? 0.2650 0.3496 0.2637 -0.0072 -0.0075 0.0221  408 ASN A O   
663  C CB  . ASN A 85  ? 0.2337 0.2856 0.2243 -0.0042 -0.0042 0.0169  408 ASN A CB  
664  C CG  . ASN A 85  ? 0.2695 0.3291 0.2531 -0.0040 -0.0067 0.0090  408 ASN A CG  
665  O OD1 . ASN A 85  ? 0.3346 0.4134 0.3105 -0.0004 -0.0140 0.0074  408 ASN A OD1 
666  N ND2 . ASN A 85  ? 0.2746 0.3204 0.2601 -0.0063 -0.0002 0.0044  408 ASN A ND2 
667  N N   . CYS A 86  ? 0.2348 0.2872 0.2290 0.0057  -0.0067 0.0389  409 CYS A N   
668  C CA  . CYS A 86  ? 0.2571 0.3116 0.2559 0.0046  -0.0030 0.0460  409 CYS A CA  
669  C C   . CYS A 86  ? 0.2649 0.3443 0.2614 0.0083  -0.0095 0.0447  409 CYS A C   
670  O O   . CYS A 86  ? 0.2486 0.3423 0.2509 0.0014  -0.0056 0.0433  409 CYS A O   
671  C CB  . CYS A 86  ? 0.2332 0.2737 0.2307 0.0132  -0.0018 0.0580  409 CYS A CB  
672  S SG  . CYS A 86  ? 0.2725 0.3179 0.2729 0.0136  0.0032  0.0692  409 CYS A SG  
673  N N   . SER A 87  ? 0.2649 0.3491 0.2532 0.0194  -0.0186 0.0452  410 SER A N   
674  C CA  . SER A 87  ? 0.3223 0.4275 0.3077 0.0264  -0.0247 0.0437  410 SER A CA  
675  C C   . SER A 87  ? 0.2754 0.4040 0.2623 0.0234  -0.0271 0.0342  410 SER A C   
676  O O   . SER A 87  ? 0.3097 0.4626 0.2990 0.0257  -0.0287 0.0316  410 SER A O   
677  C CB  . SER A 87  ? 0.3392 0.4356 0.3155 0.0388  -0.0325 0.0458  410 SER A CB  
678  O OG  . SER A 87  ? 0.4102 0.4974 0.3811 0.0399  -0.0358 0.0412  410 SER A OG  
679  N N   . LEU A 88  ? 0.2567 0.3831 0.2422 0.0189  -0.0274 0.0282  411 LEU A N   
680  C CA  . LEU A 88  ? 0.2839 0.4381 0.2715 0.0149  -0.0296 0.0180  411 LEU A CA  
681  C C   . LEU A 88  ? 0.2722 0.4416 0.2725 -0.0006 -0.0219 0.0121  411 LEU A C   
682  O O   . LEU A 88  ? 0.2848 0.4855 0.2896 -0.0011 -0.0237 0.0075  411 LEU A O   
683  C CB  . LEU A 88  ? 0.2386 0.3887 0.2212 0.0126  -0.0309 0.0126  411 LEU A CB  
684  C CG  . LEU A 88  ? 0.2406 0.4229 0.2261 0.0059  -0.0324 -0.0002 411 LEU A CG  
685  C CD1 . LEU A 88  ? 0.2503 0.4653 0.2334 0.0174  -0.0404 -0.0010 411 LEU A CD1 
686  C CD2 . LEU A 88  ? 0.2449 0.4260 0.2228 0.0054  -0.0340 -0.0054 411 LEU A CD2 
687  N N   . TYR A 89  ? 0.2518 0.3988 0.2584 -0.0130 -0.0124 0.0128  412 TYR A N   
688  C CA  . TYR A 89  ? 0.2674 0.4231 0.2860 -0.0313 -0.0035 0.0059  412 TYR A CA  
689  C C   . TYR A 89  ? 0.3294 0.4930 0.3535 -0.0336 0.0012  0.0145  412 TYR A C   
690  O O   . TYR A 89  ? 0.3147 0.5032 0.3480 -0.0460 0.0053  0.0084  412 TYR A O   
691  C CB  . TYR A 89  ? 0.2793 0.4028 0.3018 -0.0427 0.0060  0.0035  412 TYR A CB  
692  C CG  . TYR A 89  ? 0.3327 0.4585 0.3676 -0.0641 0.0165  -0.0050 412 TYR A CG  
693  C CD1 . TYR A 89  ? 0.3843 0.5335 0.4247 -0.0774 0.0160  -0.0232 412 TYR A CD1 
694  C CD2 . TYR A 89  ? 0.3642 0.4699 0.4049 -0.0716 0.0271  0.0055  412 TYR A CD2 
695  C CE1 . TYR A 89  ? 0.3793 0.5302 0.4323 -0.1002 0.0262  -0.0329 412 TYR A CE1 
696  C CE2 . TYR A 89  ? 0.4420 0.5457 0.4941 -0.0932 0.0380  -0.0012 412 TYR A CE2 
697  C CZ  . TYR A 89  ? 0.4473 0.5727 0.5062 -0.1087 0.0376  -0.0214 412 TYR A CZ  
698  O OH  . TYR A 89  ? 0.5156 0.6382 0.5870 -0.1333 0.0492  -0.0298 412 TYR A OH  
699  N N   . ASN A 90  ? 0.2646 0.4113 0.2833 -0.0226 0.0011  0.0279  413 ASN A N   
700  C CA  . ASN A 90  ? 0.2346 0.3876 0.2566 -0.0243 0.0067  0.0378  413 ASN A CA  
701  C C   . ASN A 90  ? 0.3048 0.4865 0.3218 -0.0101 -0.0018 0.0385  413 ASN A C   
702  O O   . ASN A 90  ? 0.2850 0.4627 0.2929 0.0053  -0.0112 0.0383  413 ASN A O   
703  C CB  . ASN A 90  ? 0.2706 0.3912 0.2893 -0.0202 0.0122  0.0519  413 ASN A CB  
704  C CG  . ASN A 90  ? 0.2397 0.3283 0.2628 -0.0308 0.0211  0.0512  413 ASN A CG  
705  O OD1 . ASN A 90  ? 0.2987 0.3791 0.3295 -0.0455 0.0320  0.0525  413 ASN A OD1 
706  N ND2 . ASN A 90  ? 0.2575 0.3276 0.2759 -0.0238 0.0173  0.0486  413 ASN A ND2 
707  N N   . THR A 91  ? 0.2834 0.4930 0.3064 -0.0155 0.0023  0.0392  414 THR A N   
708  C CA  . THR A 91  ? 0.2283 0.4672 0.2470 -0.0007 -0.0047 0.0386  414 THR A CA  
709  C C   . THR A 91  ? 0.2291 0.4509 0.2381 0.0135  -0.0073 0.0486  414 THR A C   
710  O O   . THR A 91  ? 0.2677 0.4657 0.2757 0.0098  -0.0013 0.0591  414 THR A O   
711  C CB  . THR A 91  ? 0.2963 0.5728 0.3245 -0.0104 0.0018  0.0376  414 THR A CB  
712  O OG1 . THR A 91  ? 0.3588 0.6207 0.3911 -0.0243 0.0143  0.0493  414 THR A OG1 
713  C CG2 . THR A 91  ? 0.3577 0.6617 0.3960 -0.0227 0.0020  0.0243  414 THR A CG2 
714  N N   . SER A 92  ? 0.3230 0.5583 0.3247 0.0307  -0.0166 0.0445  415 SER A N   
715  C CA  . SER A 92  ? 0.3249 0.5419 0.3172 0.0432  -0.0201 0.0491  415 SER A CA  
716  C C   . SER A 92  ? 0.2569 0.4832 0.2490 0.0414  -0.0137 0.0600  415 SER A C   
717  O O   . SER A 92  ? 0.3074 0.5134 0.2945 0.0462  -0.0134 0.0644  415 SER A O   
718  C CB  . SER A 92  ? 0.3374 0.5456 0.3242 0.0550  -0.0231 0.0360  415 SER A CB  
719  O OG  . SER A 92  ? 0.4714 0.7126 0.4611 0.0581  -0.0211 0.0307  415 SER A OG  
720  N N   . ASN A 93  ? 0.2458 0.4989 0.2447 0.0326  -0.0060 0.0624  416 ASN A N   
721  C CA  . ASN A 93  ? 0.2014 0.4635 0.1984 0.0311  0.0016  0.0746  416 ASN A CA  
722  C C   . ASN A 93  ? 0.2837 0.5245 0.2859 0.0150  0.0138  0.0880  416 ASN A C   
723  O O   . ASN A 93  ? 0.2244 0.4726 0.2249 0.0124  0.0220  0.1013  416 ASN A O   
724  C CB  . ASN A 93  ? 0.2493 0.5561 0.2488 0.0327  0.0038  0.0713  416 ASN A CB  
725  C CG  . ASN A 93  ? 0.2656 0.5945 0.2782 0.0160  0.0104  0.0667  416 ASN A CG  
726  O OD1 . ASN A 93  ? 0.2664 0.5754 0.2860 0.0013  0.0144  0.0661  416 ASN A OD1 
727  N ND2 . ASN A 93  ? 0.2994 0.6730 0.3158 0.0180  0.0116  0.0618  416 ASN A ND2 
728  N N   . SER A 94  ? 0.2585 0.4717 0.2658 0.0056  0.0155  0.0854  417 SER A N   
729  C CA  . SER A 94  ? 0.2563 0.4422 0.2683 -0.0084 0.0274  0.0964  417 SER A CA  
730  C C   . SER A 94  ? 0.2074 0.3645 0.2119 0.0017  0.0275  0.1088  417 SER A C   
731  O O   . SER A 94  ? 0.2504 0.4016 0.2487 0.0148  0.0176  0.1045  417 SER A O   
732  C CB  . SER A 94  ? 0.2215 0.3909 0.2417 -0.0217 0.0290  0.0854  417 SER A CB  
733  O OG  . SER A 94  ? 0.2486 0.3982 0.2640 -0.0121 0.0202  0.0789  417 SER A OG  
734  N N   . VAL A 95  ? 0.2575 0.3967 0.2630 -0.0048 0.0393  0.1247  418 VAL A N   
735  C CA  . VAL A 95  ? 0.3346 0.4489 0.3338 0.0061  0.0402  0.1377  418 VAL A CA  
736  C C   . VAL A 95  ? 0.2960 0.3859 0.2963 0.0102  0.0338  0.1280  418 VAL A C   
737  O O   . VAL A 95  ? 0.2745 0.3623 0.2689 0.0238  0.0261  0.1291  418 VAL A O   
738  C CB  . VAL A 95  ? 0.3114 0.4026 0.3123 -0.0017 0.0548  0.1551  418 VAL A CB  
739  C CG1 . VAL A 95  ? 0.3955 0.4592 0.3924 0.0119  0.0528  0.1599  418 VAL A CG1 
740  C CG2 . VAL A 95  ? 0.2879 0.4028 0.2868 -0.0042 0.0593  0.1620  418 VAL A CG2 
741  N N   . VAL A 96  ? 0.2383 0.3129 0.2462 -0.0025 0.0369  0.1174  419 VAL A N   
742  C CA  . VAL A 96  ? 0.2379 0.2913 0.2464 0.0006  0.0325  0.1087  419 VAL A CA  
743  C C   . VAL A 96  ? 0.3128 0.3827 0.3159 0.0113  0.0186  0.0986  419 VAL A C   
744  O O   . VAL A 96  ? 0.2783 0.3375 0.2777 0.0206  0.0135  0.0991  419 VAL A O   
745  C CB  . VAL A 96  ? 0.3010 0.3406 0.3178 -0.0157 0.0384  0.0969  419 VAL A CB  
746  C CG1 . VAL A 96  ? 0.3254 0.3510 0.3412 -0.0116 0.0327  0.0861  419 VAL A CG1 
747  C CG2 . VAL A 96  ? 0.3651 0.3772 0.3868 -0.0263 0.0534  0.1071  419 VAL A CG2 
748  N N   . ALA A 97  ? 0.2731 0.3695 0.2757 0.0104  0.0128  0.0899  420 ALA A N   
749  C CA  . ALA A 97  ? 0.2583 0.3636 0.2548 0.0213  0.0006  0.0813  420 ALA A CA  
750  C C   . ALA A 97  ? 0.2751 0.3832 0.2645 0.0341  -0.0042 0.0882  420 ALA A C   
751  O O   . ALA A 97  ? 0.2517 0.3492 0.2380 0.0399  -0.0106 0.0826  420 ALA A O   
752  C CB  . ALA A 97  ? 0.2263 0.3589 0.2231 0.0213  -0.0044 0.0713  420 ALA A CB  
753  N N   . ILE A 98  ? 0.2394 0.3615 0.2271 0.0366  -0.0002 0.0976  421 ILE A N   
754  C CA  . ILE A 98  ? 0.2328 0.3559 0.2180 0.0447  -0.0030 0.0939  421 ILE A CA  
755  C C   . ILE A 98  ? 0.2756 0.3768 0.2623 0.0460  -0.0018 0.0962  421 ILE A C   
756  O O   . ILE A 98  ? 0.3491 0.4454 0.3339 0.0490  -0.0071 0.0866  421 ILE A O   
757  C CB  . ILE A 98  ? 0.2637 0.4076 0.2482 0.0463  0.0023  0.1025  421 ILE A CB  
758  C CG1 . ILE A 98  ? 0.2428 0.4149 0.2261 0.0468  0.0003  0.0964  421 ILE A CG1 
759  C CG2 . ILE A 98  ? 0.2787 0.4245 0.2610 0.0534  0.0004  0.0986  421 ILE A CG2 
760  C CD1 . ILE A 98  ? 0.2182 0.4149 0.2015 0.0451  0.0078  0.1079  421 ILE A CD1 
761  N N   . THR A 99  ? 0.2749 0.3617 0.2646 0.0430  0.0063  0.1089  422 THR A N   
762  C CA  . THR A 99  ? 0.2572 0.3254 0.2489 0.0461  0.0079  0.1101  422 THR A CA  
763  C C   . THR A 99  ? 0.3361 0.3947 0.3281 0.0455  0.0017  0.0991  422 THR A C   
764  O O   . THR A 99  ? 0.2875 0.3441 0.2794 0.0488  -0.0015 0.0939  422 THR A O   
765  C CB  . THR A 99  ? 0.3357 0.3828 0.3308 0.0427  0.0189  0.1231  422 THR A CB  
766  O OG1 . THR A 99  ? 0.3309 0.3846 0.3250 0.0418  0.0255  0.1340  422 THR A OG1 
767  C CG2 . THR A 99  ? 0.3362 0.3674 0.3331 0.0488  0.0204  0.1234  422 THR A CG2 
768  N N   . GLY A 100 ? 0.2364 0.2919 0.2286 0.0407  0.0003  0.0967  423 GLY A N   
769  C CA  . GLY A 100 ? 0.2537 0.3015 0.2452 0.0403  -0.0051 0.0874  423 GLY A CA  
770  C C   . GLY A 100 ? 0.3123 0.3657 0.2997 0.0420  -0.0133 0.0753  423 GLY A C   
771  O O   . GLY A 100 ? 0.2927 0.3387 0.2797 0.0420  -0.0162 0.0706  423 GLY A O   
772  N N   . LYS A 101 ? 0.3159 0.3816 0.3005 0.0432  -0.0163 0.0712  424 LYS A N   
773  C CA  . LYS A 101 ? 0.2691 0.3348 0.2497 0.0448  -0.0227 0.0612  424 LYS A CA  
774  C C   . LYS A 101 ? 0.2943 0.3616 0.2755 0.0467  -0.0229 0.0622  424 LYS A C   
775  O O   . LYS A 101 ? 0.2880 0.3506 0.2680 0.0460  -0.0279 0.0569  424 LYS A O   
776  C CB  . LYS A 101 ? 0.3405 0.4198 0.3184 0.0475  -0.0243 0.0572  424 LYS A CB  
777  C CG  . LYS A 101 ? 0.4612 0.5359 0.4349 0.0495  -0.0311 0.0472  424 LYS A CG  
778  C CD  . LYS A 101 ? 0.5293 0.5923 0.5016 0.0478  -0.0345 0.0435  424 LYS A CD  
779  C CE  . LYS A 101 ? 0.6970 0.7707 0.6710 0.0477  -0.0317 0.0451  424 LYS A CE  
780  N NZ  . LYS A 101 ? 0.6772 0.7458 0.6486 0.0486  -0.0355 0.0401  424 LYS A NZ  
781  N N   . ASN A 102 ? 0.2856 0.3617 0.2687 0.0494  -0.0176 0.0704  425 ASN A N   
782  C CA  . ASN A 102 ? 0.2453 0.3283 0.2289 0.0528  -0.0178 0.0719  425 ASN A CA  
783  C C   . ASN A 102 ? 0.3292 0.4034 0.3162 0.0522  -0.0179 0.0726  425 ASN A C   
784  O O   . ASN A 102 ? 0.2383 0.3188 0.2255 0.0531  -0.0218 0.0691  425 ASN A O   
785  C CB  . ASN A 102 ? 0.2350 0.3290 0.2194 0.0571  -0.0112 0.0827  425 ASN A CB  
786  C CG  . ASN A 102 ? 0.3223 0.4330 0.3033 0.0589  -0.0110 0.0822  425 ASN A CG  
787  O OD1 . ASN A 102 ? 0.3678 0.4826 0.3452 0.0585  -0.0164 0.0720  425 ASN A OD1 
788  N ND2 . ASN A 102 ? 0.2944 0.4148 0.2762 0.0618  -0.0045 0.0939  425 ASN A ND2 
789  N N   A ILE A 103 ? 0.2579 0.3199 0.2480 0.0510  -0.0135 0.0773  426 ILE A N   
790  N N   B ILE A 103 ? 0.2545 0.3167 0.2446 0.0511  -0.0133 0.0776  426 ILE A N   
791  C CA  A ILE A 103 ? 0.2462 0.3028 0.2398 0.0520  -0.0128 0.0781  426 ILE A CA  
792  C CA  B ILE A 103 ? 0.2470 0.3031 0.2406 0.0519  -0.0126 0.0782  426 ILE A CA  
793  C C   A ILE A 103 ? 0.2408 0.2925 0.2332 0.0474  -0.0183 0.0703  426 ILE A C   
794  C C   B ILE A 103 ? 0.2419 0.2944 0.2340 0.0475  -0.0186 0.0700  426 ILE A C   
795  O O   A ILE A 103 ? 0.2504 0.3049 0.2455 0.0479  -0.0194 0.0700  426 ILE A O   
796  O O   B ILE A 103 ? 0.2563 0.3134 0.2508 0.0481  -0.0204 0.0693  426 ILE A O   
797  C CB  A ILE A 103 ? 0.2865 0.3307 0.2838 0.0540  -0.0052 0.0862  426 ILE A CB  
798  C CB  B ILE A 103 ? 0.2878 0.3302 0.2848 0.0529  -0.0055 0.0854  426 ILE A CB  
799  C CG1 A ILE A 103 ? 0.3062 0.3491 0.3077 0.0584  -0.0034 0.0878  426 ILE A CG1 
800  C CG1 B ILE A 103 ? 0.2966 0.3388 0.2948 0.0578  0.0013  0.0959  426 ILE A CG1 
801  C CG2 A ILE A 103 ? 0.2488 0.2820 0.2454 0.0490  -0.0045 0.0848  426 ILE A CG2 
802  C CG2 B ILE A 103 ? 0.2928 0.3305 0.2935 0.0551  -0.0044 0.0851  426 ILE A CG2 
803  C CD1 A ILE A 103 ? 0.3170 0.3436 0.3219 0.0625  0.0049  0.0951  426 ILE A CD1 
804  C CD1 B ILE A 103 ? 0.4071 0.4293 0.4085 0.0588  0.0096  0.1035  426 ILE A CD1 
805  N N   . GLU A 104 ? 0.2400 0.2864 0.2283 0.0437  -0.0216 0.0652  427 GLU A N   
806  C CA  . GLU A 104 ? 0.2363 0.2770 0.2215 0.0404  -0.0271 0.0594  427 GLU A CA  
807  C C   . GLU A 104 ? 0.2471 0.2951 0.2311 0.0408  -0.0328 0.0561  427 GLU A C   
808  O O   . GLU A 104 ? 0.2616 0.3104 0.2463 0.0390  -0.0355 0.0561  427 GLU A O   
809  C CB  . GLU A 104 ? 0.2823 0.3174 0.2627 0.0388  -0.0296 0.0555  427 GLU A CB  
810  C CG  . GLU A 104 ? 0.2363 0.2629 0.2116 0.0368  -0.0352 0.0515  427 GLU A CG  
811  C CD  . GLU A 104 ? 0.3848 0.4085 0.3560 0.0375  -0.0380 0.0480  427 GLU A CD  
812  O OE1 . GLU A 104 ? 0.4331 0.4641 0.4045 0.0400  -0.0386 0.0459  427 GLU A OE1 
813  O OE2 . GLU A 104 ? 0.3705 0.3876 0.3380 0.0363  -0.0393 0.0478  427 GLU A OE2 
814  N N   . THR A 105 ? 0.2910 0.3473 0.2733 0.0431  -0.0347 0.0540  428 THR A N   
815  C CA  . THR A 105 ? 0.2852 0.3527 0.2665 0.0440  -0.0405 0.0504  428 THR A CA  
816  C C   . THR A 105 ? 0.2944 0.3752 0.2813 0.0448  -0.0396 0.0536  428 THR A C   
817  O O   . THR A 105 ? 0.3240 0.4127 0.3121 0.0424  -0.0451 0.0511  428 THR A O   
818  C CB  . THR A 105 ? 0.2861 0.3649 0.2649 0.0477  -0.0407 0.0482  428 THR A CB  
819  O OG1 . THR A 105 ? 0.3433 0.4142 0.3179 0.0478  -0.0419 0.0445  428 THR A OG1 
820  C CG2 . THR A 105 ? 0.3222 0.4172 0.2996 0.0490  -0.0468 0.0428  428 THR A CG2 
821  N N   . TYR A 106 ? 0.2465 0.3325 0.2370 0.0486  -0.0331 0.0597  429 TYR A N   
822  C CA  . TYR A 106 ? 0.2305 0.3311 0.2267 0.0518  -0.0314 0.0637  429 TYR A CA  
823  C C   . TYR A 106 ? 0.2469 0.3454 0.2473 0.0486  -0.0322 0.0641  429 TYR A C   
824  O O   . TYR A 106 ? 0.2237 0.3404 0.2286 0.0474  -0.0358 0.0630  429 TYR A O   
825  C CB  . TYR A 106 ? 0.2347 0.3344 0.2325 0.0580  -0.0235 0.0720  429 TYR A CB  
826  C CG  . TYR A 106 ? 0.2734 0.3864 0.2764 0.0643  -0.0206 0.0775  429 TYR A CG  
827  C CD1 . TYR A 106 ? 0.3607 0.4978 0.3644 0.0683  -0.0230 0.0773  429 TYR A CD1 
828  C CD2 . TYR A 106 ? 0.3632 0.4668 0.3703 0.0674  -0.0153 0.0826  429 TYR A CD2 
829  C CE1 . TYR A 106 ? 0.3421 0.4948 0.3503 0.0757  -0.0203 0.0825  429 TYR A CE1 
830  C CE2 . TYR A 106 ? 0.4260 0.5426 0.4376 0.0755  -0.0123 0.0877  429 TYR A CE2 
831  C CZ  . TYR A 106 ? 0.3987 0.5403 0.4108 0.0797  -0.0149 0.0879  429 TYR A CZ  
832  O OH  . TYR A 106 ? 0.4496 0.6070 0.4658 0.0890  -0.0121 0.0931  429 TYR A OH  
833  N N   . PHE A 107 ? 0.2076 0.2886 0.2074 0.0468  -0.0286 0.0659  430 PHE A N   
834  C CA  . PHE A 107 ? 0.2081 0.2885 0.2109 0.0440  -0.0283 0.0675  430 PHE A CA  
835  C C   . PHE A 107 ? 0.2373 0.3238 0.2387 0.0373  -0.0357 0.0647  430 PHE A C   
836  O O   . PHE A 107 ? 0.2557 0.3605 0.2633 0.0344  -0.0378 0.0668  430 PHE A O   
837  C CB  . PHE A 107 ? 0.1941 0.2556 0.1940 0.0426  -0.0243 0.0684  430 PHE A CB  
838  C CG  . PHE A 107 ? 0.2605 0.3219 0.2617 0.0396  -0.0235 0.0706  430 PHE A CG  
839  C CD1 . PHE A 107 ? 0.2367 0.3097 0.2453 0.0443  -0.0191 0.0753  430 PHE A CD1 
840  C CD2 . PHE A 107 ? 0.2817 0.3325 0.2758 0.0333  -0.0266 0.0690  430 PHE A CD2 
841  C CE1 . PHE A 107 ? 0.2535 0.3296 0.2629 0.0411  -0.0174 0.0768  430 PHE A CE1 
842  C CE2 . PHE A 107 ? 0.2821 0.3341 0.2755 0.0294  -0.0251 0.0724  430 PHE A CE2 
843  C CZ  . PHE A 107 ? 0.2499 0.3140 0.2512 0.0315  -0.0195 0.0736  430 PHE A CZ  
844  N N   . ASN A 108 ? 0.2384 0.3121 0.2320 0.0345  -0.0403 0.0605  431 ASN A N   
845  C CA  . ASN A 108 ? 0.2748 0.3499 0.2655 0.0275  -0.0480 0.0597  431 ASN A CA  
846  C C   . ASN A 108 ? 0.2645 0.3614 0.2608 0.0235  -0.0526 0.0536  431 ASN A C   
847  O O   . ASN A 108 ? 0.3374 0.4329 0.3361 0.0115  -0.0537 0.0484  431 ASN A O   
848  C CB  . ASN A 108 ? 0.2858 0.3409 0.2663 0.0283  -0.0517 0.0554  431 ASN A CB  
849  C CG  . ASN A 108 ? 0.3176 0.3529 0.2926 0.0287  -0.0478 0.0582  431 ASN A CG  
850  O OD1 . ASN A 108 ? 0.2978 0.3303 0.2742 0.0245  -0.0443 0.0628  431 ASN A OD1 
851  N ND2 . ASN A 108 ? 0.3343 0.3583 0.3032 0.0332  -0.0482 0.0534  431 ASN A ND2 
852  N N   . ASN A 109 ? 0.2060 0.3208 0.2042 0.0312  -0.0534 0.0521  432 ASN A N   
853  C CA  . ASN A 109 ? 0.2321 0.3761 0.2358 0.0283  -0.0589 0.0458  432 ASN A CA  
854  C C   . ASN A 109 ? 0.2388 0.4062 0.2536 0.0278  -0.0554 0.0494  432 ASN A C   
855  O O   . ASN A 109 ? 0.2494 0.4443 0.2717 0.0198  -0.0604 0.0430  432 ASN A O   
856  C CB  . ASN A 109 ? 0.2793 0.4284 0.2790 0.0358  -0.0580 0.0417  432 ASN A CB  
857  C CG  . ASN A 109 ? 0.2594 0.3978 0.2501 0.0352  -0.0640 0.0339  432 ASN A CG  
858  O OD1 . ASN A 109 ? 0.4028 0.5292 0.3898 0.0285  -0.0695 0.0289  432 ASN A OD1 
859  N ND2 . ASN A 109 ? 0.3157 0.4563 0.3023 0.0415  -0.0616 0.0322  432 ASN A ND2 
860  N N   . GLN A 110 ? 0.2577 0.4161 0.2744 0.0353  -0.0468 0.0576  433 GLN A N   
861  C CA  . GLN A 110 ? 0.2046 0.3843 0.2314 0.0367  -0.0433 0.0612  433 GLN A CA  
862  C C   . GLN A 110 ? 0.2069 0.3919 0.2392 0.0237  -0.0454 0.0603  433 GLN A C   
863  O O   . GLN A 110 ? 0.2860 0.4987 0.3287 0.0179  -0.0453 0.0573  433 GLN A O   
864  C CB  . GLN A 110 ? 0.2268 0.3918 0.2530 0.0475  -0.0340 0.0687  433 GLN A CB  
865  C CG  . GLN A 110 ? 0.2349 0.4013 0.2585 0.0579  -0.0300 0.0712  433 GLN A CG  
866  C CD  . GLN A 110 ? 0.2763 0.4747 0.3059 0.0636  -0.0300 0.0718  433 GLN A CD  
867  O OE1 . GLN A 110 ? 0.2872 0.5118 0.3237 0.0574  -0.0347 0.0666  433 GLN A OE1 
868  N NE2 . GLN A 110 ? 0.4092 0.6075 0.4361 0.0748  -0.0247 0.0780  433 GLN A NE2 
869  N N   . LEU A 111 ? 0.2856 0.4367 0.3093 0.0168  -0.0433 0.0601  434 LEU A N   
870  C CA  . LEU A 111 ? 0.2550 0.3979 0.2796 0.0017  -0.0407 0.0576  434 LEU A CA  
871  C C   . LEU A 111 ? 0.3477 0.5045 0.3773 -0.0133 -0.0453 0.0484  434 LEU A C   
872  O O   . LEU A 111 ? 0.3393 0.5107 0.3769 -0.0257 -0.0425 0.0467  434 LEU A O   
873  C CB  . LEU A 111 ? 0.2764 0.3819 0.2884 -0.0015 -0.0394 0.0595  434 LEU A CB  
874  C CG  . LEU A 111 ? 0.2580 0.3518 0.2661 0.0088  -0.0342 0.0659  434 LEU A CG  
875  C CD1 . LEU A 111 ? 0.2562 0.3204 0.2519 0.0054  -0.0339 0.0670  434 LEU A CD1 
876  C CD2 . LEU A 111 ? 0.3576 0.4689 0.3741 0.0103  -0.0275 0.0689  434 LEU A CD2 
877  N N   . ILE A 112 ? 0.2992 0.4548 0.3250 -0.0128 -0.0520 0.0411  435 ILE A N   
878  C CA  . ILE A 112 ? 0.3528 0.5193 0.3828 -0.0280 -0.0568 0.0288  435 ILE A CA  
879  C C   . ILE A 112 ? 0.3380 0.5547 0.3824 -0.0283 -0.0587 0.0251  435 ILE A C   
880  O O   . ILE A 112 ? 0.3341 0.5688 0.3885 -0.0446 -0.0577 0.0192  435 ILE A O   
881  C CB  . ILE A 112 ? 0.2585 0.4093 0.2788 -0.0251 -0.0632 0.0202  435 ILE A CB  
882  C CG1 . ILE A 112 ? 0.3504 0.4539 0.3574 -0.0254 -0.0615 0.0228  435 ILE A CG1 
883  C CG2 . ILE A 112 ? 0.3176 0.4859 0.3435 -0.0395 -0.0687 0.0041  435 ILE A CG2 
884  C CD1 . ILE A 112 ? 0.3643 0.4539 0.3616 -0.0181 -0.0670 0.0151  435 ILE A CD1 
885  N N   . VAL A 113 ? 0.3160 0.5582 0.3619 -0.0102 -0.0613 0.0292  436 VAL A N   
886  C CA  . VAL A 113 ? 0.2649 0.5557 0.3224 -0.0062 -0.0631 0.0266  436 VAL A CA  
887  C C   . VAL A 113 ? 0.2184 0.5293 0.2879 -0.0083 -0.0570 0.0318  436 VAL A C   
888  O O   . VAL A 113 ? 0.2587 0.6009 0.3385 -0.0178 -0.0568 0.0242  436 VAL A O   
889  C CB  . VAL A 113 ? 0.2406 0.5278 0.2897 0.0155  -0.0591 0.0325  436 VAL A CB  
890  C CG1 . VAL A 113 ? 0.2017 0.5250 0.2570 0.0207  -0.0573 0.0302  436 VAL A CG1 
891  C CG2 . VAL A 113 ? 0.2594 0.5300 0.2974 0.0175  -0.0637 0.0272  436 VAL A CG2 
892  N N   . MET A 114 ? 0.2616 0.5536 0.3288 0.0013  -0.0507 0.0436  437 MET A N   
893  C CA  . MET A 114 ? 0.3261 0.6385 0.4040 0.0023  -0.0442 0.0479  437 MET A CA  
894  C C   . MET A 114 ? 0.3149 0.6218 0.3964 -0.0214 -0.0406 0.0425  437 MET A C   
895  O O   . MET A 114 ? 0.3120 0.6441 0.4039 -0.0236 -0.0352 0.0442  437 MET A O   
896  C CB  . MET A 114 ? 0.1993 0.4877 0.2717 0.0192  -0.0371 0.0592  437 MET A CB  
897  C CG  . MET A 114 ? 0.3387 0.6189 0.4040 0.0400  -0.0337 0.0637  437 MET A CG  
898  S SD  . MET A 114 ? 0.4181 0.6625 0.4768 0.0542  -0.0253 0.0733  437 MET A SD  
899  C CE  . MET A 114 ? 0.4136 0.6835 0.4831 0.0636  -0.0181 0.0753  437 MET A CE  
900  N N   . GLY A 115 ? 0.2860 0.5609 0.3590 -0.0383 -0.0428 0.0368  438 GLY A N   
901  C CA  . GLY A 115 ? 0.3084 0.5721 0.3828 -0.0607 -0.0380 0.0349  438 GLY A CA  
902  C C   . GLY A 115 ? 0.3702 0.6070 0.4365 -0.0582 -0.0300 0.0453  438 GLY A C   
903  O O   . GLY A 115 ? 0.3286 0.5658 0.3972 -0.0741 -0.0241 0.0469  438 GLY A O   
904  N N   . TYR A 116 ? 0.2895 0.5044 0.3463 -0.0396 -0.0293 0.0520  439 TYR A N   
905  C CA  . TYR A 116 ? 0.3006 0.4943 0.3495 -0.0366 -0.0223 0.0596  439 TYR A CA  
906  C C   . TYR A 116 ? 0.3041 0.4619 0.3407 -0.0517 -0.0212 0.0615  439 TYR A C   
907  O O   . TYR A 116 ? 0.3085 0.4608 0.3411 -0.0579 -0.0146 0.0670  439 TYR A O   
908  C CB  . TYR A 116 ? 0.2635 0.4407 0.3054 -0.0163 -0.0222 0.0639  439 TYR A CB  
909  C CG  . TYR A 116 ? 0.2040 0.3694 0.2406 -0.0112 -0.0150 0.0686  439 TYR A CG  
910  C CD1 . TYR A 116 ? 0.2598 0.3938 0.2825 -0.0164 -0.0139 0.0712  439 TYR A CD1 
911  C CD2 . TYR A 116 ? 0.2789 0.4663 0.3238 0.0003  -0.0092 0.0696  439 TYR A CD2 
912  C CE1 . TYR A 116 ? 0.2820 0.4100 0.2991 -0.0119 -0.0077 0.0737  439 TYR A CE1 
913  C CE2 . TYR A 116 ? 0.3310 0.5086 0.3706 0.0048  -0.0025 0.0709  439 TYR A CE2 
914  C CZ  . TYR A 116 ? 0.2625 0.4120 0.2881 -0.0021 -0.0019 0.0725  439 TYR A CZ  
915  O OH  . TYR A 116 ? 0.2910 0.4357 0.3109 0.0020  0.0042  0.0720  439 TYR A OH  
916  N N   . ASN A 117 ? 0.3016 0.4356 0.3313 -0.0566 -0.0273 0.0572  440 ASN A N   
917  C CA  . ASN A 117 ? 0.3680 0.4631 0.3845 -0.0675 -0.0263 0.0602  440 ASN A CA  
918  C C   . ASN A 117 ? 0.3716 0.4705 0.3922 -0.0897 -0.0207 0.0617  440 ASN A C   
919  O O   . ASN A 117 ? 0.3959 0.4683 0.4052 -0.0966 -0.0160 0.0701  440 ASN A O   
920  C CB  . ASN A 117 ? 0.2921 0.3634 0.3019 -0.0662 -0.0338 0.0532  440 ASN A CB  
921  C CG  . ASN A 117 ? 0.3799 0.4428 0.3827 -0.0457 -0.0376 0.0545  440 ASN A CG  
922  O OD1 . ASN A 117 ? 0.3548 0.4104 0.3519 -0.0361 -0.0342 0.0618  440 ASN A OD1 
923  N ND2 . ASN A 117 ? 0.3870 0.4532 0.3905 -0.0403 -0.0441 0.0466  440 ASN A ND2 
924  N N   . ASN A 118 ? 0.3805 0.5148 0.4170 -0.1012 -0.0208 0.0544  441 ASN A N   
925  C CA  . ASN A 118 ? 0.3421 0.4857 0.3848 -0.1247 -0.0141 0.0558  441 ASN A CA  
926  C C   . ASN A 118 ? 0.3538 0.5066 0.3940 -0.1231 -0.0049 0.0672  441 ASN A C   
927  O O   . ASN A 118 ? 0.3677 0.5099 0.4038 -0.1408 0.0021  0.0740  441 ASN A O   
928  C CB  . ASN A 118 ? 0.3787 0.5702 0.4416 -0.1357 -0.0160 0.0446  441 ASN A CB  
929  C CG  . ASN A 118 ? 0.5428 0.7300 0.6078 -0.1393 -0.0251 0.0311  441 ASN A CG  
930  O OD1 . ASN A 118 ? 0.5951 0.7410 0.6501 -0.1499 -0.0267 0.0279  441 ASN A OD1 
931  N ND2 . ASN A 118 ? 0.6658 0.8957 0.7426 -0.1286 -0.0310 0.0232  441 ASN A ND2 
932  N N   . PHE A 119 ? 0.2983 0.4694 0.3400 -0.1025 -0.0042 0.0693  442 PHE A N   
933  C CA  . PHE A 119 ? 0.3338 0.5149 0.3722 -0.0995 0.0044  0.0772  442 PHE A CA  
934  C C   . PHE A 119 ? 0.3296 0.4694 0.3474 -0.0974 0.0063  0.0866  442 PHE A C   
935  O O   . PHE A 119 ? 0.3776 0.5192 0.3889 -0.1045 0.0140  0.0948  442 PHE A O   
936  C CB  . PHE A 119 ? 0.3439 0.5528 0.3899 -0.0775 0.0050  0.0746  442 PHE A CB  
937  C CG  . PHE A 119 ? 0.3365 0.5953 0.4028 -0.0769 0.0054  0.0684  442 PHE A CG  
938  C CD1 . PHE A 119 ? 0.3492 0.6220 0.4246 -0.0715 -0.0025 0.0616  442 PHE A CD1 
939  C CD2 . PHE A 119 ? 0.3263 0.6226 0.4023 -0.0807 0.0137  0.0693  442 PHE A CD2 
940  C CE1 . PHE A 119 ? 0.3009 0.6254 0.3950 -0.0690 -0.0028 0.0563  442 PHE A CE1 
941  C CE2 . PHE A 119 ? 0.3399 0.6876 0.4357 -0.0782 0.0139  0.0635  442 PHE A CE2 
942  C CZ  . PHE A 119 ? 0.2902 0.6526 0.3951 -0.0721 0.0053  0.0572  442 PHE A CZ  
943  N N   . ILE A 120 ? 0.2944 0.4014 0.3015 -0.0866 -0.0006 0.0857  443 ILE A N   
944  C CA  . ILE A 120 ? 0.4117 0.4826 0.3993 -0.0830 -0.0001 0.0943  443 ILE A CA  
945  C C   . ILE A 120 ? 0.4278 0.4727 0.4071 -0.1019 0.0029  0.1017  443 ILE A C   
946  O O   . ILE A 120 ? 0.4797 0.5091 0.4448 -0.1040 0.0079  0.1133  443 ILE A O   
947  C CB  . ILE A 120 ? 0.4190 0.4672 0.3998 -0.0670 -0.0083 0.0904  443 ILE A CB  
948  C CG1 . ILE A 120 ? 0.3340 0.4034 0.3219 -0.0500 -0.0092 0.0853  443 ILE A CG1 
949  C CG2 . ILE A 120 ? 0.5039 0.5195 0.4654 -0.0622 -0.0087 0.0987  443 ILE A CG2 
950  C CD1 . ILE A 120 ? 0.3412 0.3963 0.3266 -0.0369 -0.0164 0.0807  443 ILE A CD1 
951  N N   . LEU A 121 ? 0.4877 0.5278 0.4752 -0.1162 0.0003  0.0953  444 LEU A N   
952  C CA  . LEU A 121 ? 0.4725 0.4835 0.4533 -0.1367 0.0046  0.1017  444 LEU A CA  
953  C C   . LEU A 121 ? 0.5020 0.5355 0.4866 -0.1537 0.0154  0.1106  444 LEU A C   
954  O O   . LEU A 121 ? 0.5205 0.5282 0.4911 -0.1631 0.0219  0.1244  444 LEU A O   
955  C CB  . LEU A 121 ? 0.5569 0.5605 0.5475 -0.1501 -0.0003 0.0889  444 LEU A CB  
956  C CG  . LEU A 121 ? 0.7760 0.7382 0.7561 -0.1409 -0.0083 0.0833  444 LEU A CG  
957  C CD1 . LEU A 121 ? 0.6085 0.5767 0.5848 -0.1143 -0.0154 0.0805  444 LEU A CD1 
958  C CD2 . LEU A 121 ? 0.7651 0.7287 0.7568 -0.1561 -0.0125 0.0672  444 LEU A CD2 
959  N N   . LYS A 122 ? 0.4288 0.5119 0.4316 -0.1569 0.0178  0.1037  445 LYS A N   
960  C CA  . LYS A 122 ? 0.3854 0.4976 0.3931 -0.1717 0.0286  0.1112  445 LYS A CA  
961  C C   . LYS A 122 ? 0.4390 0.5488 0.4308 -0.1589 0.0341  0.1233  445 LYS A C   
962  O O   . LYS A 122 ? 0.5331 0.6404 0.5184 -0.1654 0.0419  0.1301  445 LYS A O   
963  C CB  . LYS A 122 ? 0.3635 0.5340 0.3947 -0.1724 0.0292  0.1001  445 LYS A CB  
964  C CG  . LYS A 122 ? 0.4607 0.6595 0.5015 -0.1899 0.0380  0.1001  445 LYS A CG  
965  N N   . GLU A 123 ? 0.4648 0.5722 0.4505 -0.1350 0.0287  0.1202  446 GLU A N   
966  C CA  . GLU A 123 ? 0.4704 0.5772 0.4406 -0.1229 0.0328  0.1287  446 GLU A CA  
967  C C   . GLU A 123 ? 0.4997 0.5644 0.4495 -0.1247 0.0341  0.1400  446 GLU A C   
968  O O   . GLU A 123 ? 0.4597 0.5286 0.3997 -0.1228 0.0406  0.1463  446 GLU A O   
969  C CB  . GLU A 123 ? 0.4493 0.5551 0.4180 -0.0987 0.0258  0.1201  446 GLU A CB  
970  C CG  . GLU A 123 ? 0.4741 0.5629 0.4227 -0.0865 0.0257  0.1270  446 GLU A CG  
971  C CD  . GLU A 123 ? 0.5170 0.5996 0.4652 -0.0666 0.0184  0.1175  446 GLU A CD  
972  O OE1 . GLU A 123 ? 0.3651 0.4575 0.3279 -0.0608 0.0145  0.1071  446 GLU A OE1 
973  O OE2 . GLU A 123 ? 0.5863 0.6559 0.5193 -0.0570 0.0166  0.1208  446 GLU A OE2 
974  N N   . LYS A 124 ? 0.5212 0.5456 0.4643 -0.1264 0.0281  0.1417  447 LYS A N   
975  C CA  . LYS A 124 ? 0.5341 0.5166 0.4584 -0.1230 0.0296  0.1516  447 LYS A CA  
976  C C   . LYS A 124 ? 0.6060 0.5808 0.5307 -0.1415 0.0395  0.1589  447 LYS A C   
977  O O   . LYS A 124 ? 0.6788 0.6405 0.5889 -0.1377 0.0460  0.1701  447 LYS A O   
978  C CB  . LYS A 124 ? 0.5161 0.4580 0.4344 -0.1177 0.0210  0.1497  447 LYS A CB  
979  N N   . LYS A 125 ? 0.6255 0.6101 0.5671 -0.1618 0.0410  0.1523  448 LYS A N   
980  C CA  . LYS A 125 ? 0.5707 0.5485 0.5153 -0.1813 0.0509  0.1580  448 LYS A CA  
981  C C   . LYS A 125 ? 0.5946 0.6080 0.5392 -0.1822 0.0601  0.1638  448 LYS A C   
982  O O   . LYS A 125 ? 0.6465 0.6446 0.5814 -0.1880 0.0692  0.1759  448 LYS A O   
983  C CB  . LYS A 125 ? 0.5771 0.5657 0.5423 -0.2030 0.0498  0.1457  448 LYS A CB  
984  C CG  . LYS A 125 ? 0.6713 0.6155 0.6345 -0.2076 0.0432  0.1399  448 LYS A CG  
985  C CD  . LYS A 125 ? 0.7263 0.6730 0.7069 -0.2338 0.0463  0.1296  448 LYS A CD  
986  C CE  . LYS A 125 ? 0.7359 0.6375 0.7147 -0.2390 0.0401  0.1207  448 LYS A CE  
987  N NZ  . LYS A 125 ? 0.7534 0.6639 0.7337 -0.2277 0.0276  0.1090  448 LYS A NZ  
988  N N   . ILE A 126 ? 0.5444 0.6051 0.4996 -0.1756 0.0584  0.1555  449 ILE A N   
989  C CA  . ILE A 126 ? 0.5635 0.6591 0.5179 -0.1736 0.0664  0.1590  449 ILE A CA  
990  C C   . ILE A 126 ? 0.6099 0.6848 0.5405 -0.1595 0.0689  0.1709  449 ILE A C   
991  O O   . ILE A 126 ? 0.5456 0.6238 0.4681 -0.1648 0.0780  0.1808  449 ILE A O   
992  C CB  . ILE A 126 ? 0.5056 0.6509 0.4745 -0.1638 0.0637  0.1467  449 ILE A CB  
993  C CG1 . ILE A 126 ? 0.4887 0.6627 0.4813 -0.1779 0.0629  0.1360  449 ILE A CG1 
994  C CG2 . ILE A 126 ? 0.5533 0.7312 0.5184 -0.1577 0.0711  0.1488  449 ILE A CG2 
995  C CD1 . ILE A 126 ? 0.6051 0.7828 0.6035 -0.1999 0.0712  0.1397  449 ILE A CD1 
996  N N   . ASN A 127 ? 0.5753 0.6299 0.4943 -0.1415 0.0609  0.1701  450 ASN A N   
997  C CA  . ASN A 127 ? 0.5755 0.6141 0.4720 -0.1266 0.0619  0.1793  450 ASN A CA  
998  C C   . ASN A 127 ? 0.7284 0.7277 0.6096 -0.1331 0.0686  0.1948  450 ASN A C   
999  O O   . ASN A 127 ? 0.7879 0.7837 0.6506 -0.1256 0.0733  0.2050  450 ASN A O   
1000 C CB  . ASN A 127 ? 0.6227 0.6470 0.5119 -0.1072 0.0513  0.1738  450 ASN A CB  
1001 C CG  . ASN A 127 ? 0.6683 0.7303 0.5681 -0.0975 0.0473  0.1608  450 ASN A CG  
1002 O OD1 . ASN A 127 ? 0.6768 0.7758 0.5839 -0.1000 0.0529  0.1571  450 ASN A OD1 
1003 N ND2 . ASN A 127 ? 0.6699 0.7221 0.5705 -0.0855 0.0383  0.1538  450 ASN A ND2 
1004 N N   . ASP A 128 ? 0.7655 0.7359 0.6541 -0.1473 0.0698  0.1964  451 ASP A N   
1005 C CA  . ASP A 128 ? 0.8407 0.7700 0.7170 -0.1541 0.0782  0.2115  451 ASP A CA  
1006 C C   . ASP A 128 ? 0.7881 0.7349 0.6702 -0.1736 0.0910  0.2188  451 ASP A C   
1007 O O   . ASP A 128 ? 0.8508 0.7790 0.7162 -0.1735 0.1006  0.2348  451 ASP A O   
1008 C CB  . ASP A 128 ? 0.8830 0.7716 0.7662 -0.1609 0.0744  0.2085  451 ASP A CB  
1009 C CG  . ASP A 128 ? 1.1316 1.0007 1.0074 -0.1403 0.0624  0.2028  451 ASP A CG  
1010 O OD1 . ASP A 128 ? 0.9785 0.8638 0.8434 -0.1213 0.0577  0.2017  451 ASP A OD1 
1011 O OD2 . ASP A 128 ? 1.0494 0.8880 0.9308 -0.1436 0.0576  0.1980  451 ASP A OD2 
1012 N N   . MET A 129 ? 0.7471 0.7304 0.6522 -0.1900 0.0916  0.2077  452 MET A N   
1013 C CA  . MET A 129 ? 0.8266 0.8377 0.7384 -0.2064 0.1031  0.2128  452 MET A CA  
1014 C C   . MET A 129 ? 0.8170 0.8487 0.7115 -0.1938 0.1081  0.2216  452 MET A C   
1015 O O   . MET A 129 ? 1.0245 1.0454 0.9065 -0.1999 0.1191  0.2368  452 MET A O   
1016 C CB  . MET A 129 ? 0.7539 0.8142 0.6916 -0.2183 0.1008  0.1967  452 MET A CB  
1017 C CG  . MET A 129 ? 0.6584 0.7638 0.6017 -0.2263 0.1104  0.1991  452 MET A CG  
1018 N N   . LEU A 130 ? 0.8020 0.8635 0.6955 -0.1765 0.1003  0.2118  453 LEU A N   
1019 C CA  . LEU A 130 ? 0.8741 0.9607 0.7534 -0.1648 0.1036  0.2161  453 LEU A CA  
1020 C C   . LEU A 130 ? 0.8220 0.8708 0.6728 -0.1559 0.1070  0.2331  453 LEU A C   
1021 O O   . LEU A 130 ? 0.8363 0.8964 0.6738 -0.1570 0.1153  0.2440  453 LEU A O   
1022 C CB  . LEU A 130 ? 0.6477 0.7641 0.5315 -0.1468 0.0939  0.2010  453 LEU A CB  
1023 C CG  . LEU A 130 ? 0.5823 0.7460 0.4905 -0.1520 0.0937  0.1861  453 LEU A CG  
1024 C CD1 . LEU A 130 ? 0.6208 0.8015 0.5344 -0.1343 0.0846  0.1715  453 LEU A CD1 
1025 C CD2 . LEU A 130 ? 0.6266 0.8297 0.5360 -0.1575 0.1033  0.1885  453 LEU A CD2 
1026 N N   . LYS A 131 ? 0.8444 0.8488 0.6848 -0.1466 0.1007  0.2359  454 LYS A N   
1027 C CA  . LYS A 131 ? 0.8423 0.8110 0.6532 -0.1343 0.1026  0.2510  454 LYS A CA  
1028 C C   . LYS A 131 ? 0.9810 0.9195 0.7817 -0.1486 0.1168  0.2699  454 LYS A C   
1029 O O   . LYS A 131 ? 1.0274 0.9521 0.8017 -0.1419 0.1221  0.2848  454 LYS A O   
1030 C CB  . LYS A 131 ? 0.8347 0.7657 0.6383 -0.1194 0.0922  0.2477  454 LYS A CB  
1031 N N   . LEU A 132 ? 0.9369 0.8656 0.7581 -0.1691 0.1228  0.2693  455 LEU A N   
1032 C CA  . LEU A 132 ? 1.0113 0.9165 0.8287 -0.1863 0.1383  0.2863  455 LEU A CA  
1033 C C   . LEU A 132 ? 1.0436 0.9932 0.8612 -0.1960 0.1474  0.2907  455 LEU A C   
1034 O O   . LEU A 132 ? 1.2893 1.2315 1.0820 -0.1912 0.1553  0.3067  455 LEU A O   
1035 C CB  . LEU A 132 ? 1.0186 0.9076 0.8631 -0.2078 0.1405  0.2809  455 LEU A CB  
1036 N N   . VAL A 133 ? 0.9247 0.9216 0.7689 -0.2087 0.1459  0.2763  456 VAL A N   
1037 C CA  . VAL A 133 ? 0.8221 0.8691 0.6716 -0.2176 0.1538  0.2770  456 VAL A CA  
1038 C C   . VAL A 133 ? 0.9309 0.9961 0.7556 -0.2008 0.1547  0.2845  456 VAL A C   
1039 O O   . VAL A 133 ? 1.0270 1.1020 0.8438 -0.1805 0.1437  0.2759  456 VAL A O   
1040 C CB  . VAL A 133 ? 0.9412 1.0409 0.8191 -0.2219 0.1466  0.2553  456 VAL A CB  
1041 C CG1 . VAL A 133 ? 0.9804 1.1367 0.8608 -0.2224 0.1520  0.2532  456 VAL A CG1 
1042 C CG2 . VAL A 133 ? 0.9079 1.0023 0.8108 -0.2446 0.1483  0.2490  456 VAL A CG2 
1043 O O6  . BU3 B .   ? 0.5645 0.8771 0.6604 -0.1512 0.0105  0.0581  501 BU3 A O6  
1044 C C3  . BU3 B .   ? 0.5820 0.9333 0.6938 -0.1444 0.0030  0.0469  501 BU3 A C3  
1045 C C4  . BU3 B .   ? 0.5357 0.8684 0.6471 -0.1590 -0.0049 0.0370  501 BU3 A C4  
1046 C C2  . BU3 B .   ? 0.5570 0.9599 0.6830 -0.1453 0.0069  0.0410  501 BU3 A C2  
1047 O O5  . BU3 B .   ? 0.8973 1.3135 1.0216 -0.1325 0.0148  0.0481  501 BU3 A O5  
1048 C C1  . BU3 B .   ? 0.3559 0.7938 0.4919 -0.1298 -0.0014 0.0308  501 BU3 A C1  
1049 C C15 A I5K C .   ? 0.6319 0.4997 0.6652 -0.0379 0.0912  0.1121  502 I5K A C15 
1050 C C15 B I5K C .   ? 0.6297 0.4582 0.6640 -0.0239 0.0911  0.0929  502 I5K A C15 
1051 C C13 A I5K C .   ? 0.6883 0.4906 0.7181 -0.0221 0.1045  0.1257  502 I5K A C13 
1052 C C13 B I5K C .   ? 0.6908 0.4874 0.7209 -0.0205 0.1051  0.1239  502 I5K A C13 
1053 N N   A I5K C .   ? 0.5396 0.4517 0.5674 -0.0209 0.0609  0.0739  502 I5K A N   
1054 N N   B I5K C .   ? 0.5405 0.4504 0.5688 -0.0215 0.0616  0.0728  502 I5K A N   
1055 C C   A I5K C .   ? 0.5181 0.4616 0.5442 -0.0247 0.0501  0.0609  502 I5K A C   
1056 C C   B I5K C .   ? 0.5188 0.4606 0.5454 -0.0257 0.0508  0.0600  502 I5K A C   
1057 O O   A I5K C .   ? 0.4020 0.4147 0.4267 -0.0357 0.0324  0.0410  502 I5K A O   
1058 O O   B I5K C .   ? 0.4218 0.4359 0.4469 -0.0356 0.0334  0.0453  502 I5K A O   
1059 C C1  A I5K C .   ? 0.4885 0.4428 0.5092 -0.0139 0.0402  0.0551  502 I5K A C1  
1060 C C1  B I5K C .   ? 0.4884 0.4426 0.5095 -0.0150 0.0405  0.0541  502 I5K A C1  
1061 C C10 A I5K C .   ? 0.6132 0.4816 0.6463 -0.0318 0.0837  0.0959  502 I5K A C10 
1062 C C10 B I5K C .   ? 0.6162 0.4796 0.6497 -0.0317 0.0846  0.0947  502 I5K A C10 
1063 C C11 A I5K C .   ? 0.6277 0.4619 0.6609 -0.0221 0.0896  0.0963  502 I5K A C11 
1064 C C11 B I5K C .   ? 0.6338 0.4967 0.6665 -0.0351 0.0915  0.1128  502 I5K A C11 
1065 C C12 A I5K C .   ? 0.6661 0.4642 0.6987 -0.0164 0.1015  0.1124  502 I5K A C12 
1066 C C12 B I5K C .   ? 0.6773 0.5066 0.7078 -0.0302 0.1019  0.1283  502 I5K A C12 
1067 C C14 A I5K C .   ? 0.6735 0.5071 0.7049 -0.0337 0.1023  0.1280  502 I5K A C14 
1068 C C14 B I5K C .   ? 0.6663 0.4581 0.7000 -0.0180 0.1030  0.1090  502 I5K A C14 
1069 C C2  A I5K C .   ? 0.5152 0.4748 0.5457 -0.0392 0.0520  0.0572  502 I5K A C2  
1070 C C2  B I5K C .   ? 0.5167 0.4735 0.5478 -0.0406 0.0532  0.0565  502 I5K A C2  
1071 C C3  A I5K C .   ? 0.4686 0.4642 0.4992 -0.0454 0.0431  0.0450  502 I5K A C3  
1072 C C3  B I5K C .   ? 0.4686 0.4620 0.5000 -0.0470 0.0444  0.0444  502 I5K A C3  
1073 C C4  A I5K C .   ? 0.4931 0.5048 0.5320 -0.0645 0.0484  0.0374  502 I5K A C4  
1074 C C4  B I5K C .   ? 0.5541 0.5598 0.5942 -0.0680 0.0491  0.0293  502 I5K A C4  
1075 C C5  A I5K C .   ? 0.5382 0.5227 0.5855 -0.0826 0.0613  0.0290  502 I5K A C5  
1076 C C5  B I5K C .   ? 0.5142 0.5170 0.5616 -0.0826 0.0599  0.0365  502 I5K A C5  
1077 C C6  A I5K C .   ? 0.5852 0.5392 0.6351 -0.0864 0.0745  0.0463  502 I5K A C6  
1078 C C6  B I5K C .   ? 0.5845 0.5414 0.6344 -0.0866 0.0739  0.0459  502 I5K A C6  
1079 C C7  A I5K C .   ? 0.5667 0.5156 0.6079 -0.0652 0.0714  0.0680  502 I5K A C7  
1080 C C7  B I5K C .   ? 0.5715 0.5130 0.6135 -0.0667 0.0738  0.0681  502 I5K A C7  
1081 C C8  A I5K C .   ? 0.5496 0.4859 0.5845 -0.0470 0.0651  0.0684  502 I5K A C8  
1082 C C8  B I5K C .   ? 0.5517 0.4834 0.5873 -0.0482 0.0666  0.0677  502 I5K A C8  
1083 C C9  A I5K C .   ? 0.5715 0.4762 0.6038 -0.0344 0.0705  0.0795  502 I5K A C9  
1084 C C9  B I5K C .   ? 0.5737 0.4743 0.6065 -0.0349 0.0715  0.0786  502 I5K A C9  
1085 N N1  A I5K C .   ? 0.6519 0.4234 0.6835 -0.0037 0.1043  0.1092  502 I5K A N1  
1086 N N1  B I5K C .   ? 0.6795 0.5159 0.7056 -0.0330 0.1045  0.1426  502 I5K A N1  
1087 O O   . HOH D .   ? 0.4505 0.5144 0.4182 -0.0106 0.0176  -0.0471 601 HOH A O   
1088 O O   . HOH D .   ? 0.6222 0.8356 0.6468 0.1245  -0.0040 0.1094  602 HOH A O   
1089 O O   . HOH D .   ? 0.4812 0.5476 0.4564 0.0228  -0.0671 0.0286  603 HOH A O   
1090 O O   . HOH D .   ? 0.5877 0.6421 0.4884 -0.0594 0.0253  0.1389  604 HOH A O   
1091 O O   . HOH D .   ? 0.3462 0.3675 0.3596 -0.0224 0.0179  0.0264  605 HOH A O   
1092 O O   . HOH D .   ? 0.4716 0.7044 0.5257 -0.0754 0.0179  0.0011  606 HOH A O   
1093 O O   . HOH D .   ? 0.4797 0.4951 0.4412 0.0410  -0.0452 0.0439  607 HOH A O   
1094 O O   . HOH D .   ? 0.5595 0.6386 0.5053 0.0138  0.0096  0.0113  608 HOH A O   
1095 O O   . HOH D .   ? 0.5458 0.5987 0.4600 -0.0119 0.0004  0.1005  609 HOH A O   
1096 O O   . HOH D .   ? 0.4222 0.6033 0.4665 0.1349  0.0091  0.1055  610 HOH A O   
1097 O O   . HOH D .   ? 0.7342 0.5493 0.7731 0.1227  0.0903  0.0646  611 HOH A O   
1098 O O   . HOH D .   ? 0.4318 0.4785 0.3704 0.0301  -0.0320 0.0495  612 HOH A O   
1099 O O   . HOH D .   ? 0.4433 0.4866 0.4148 0.0437  -0.0430 0.0433  613 HOH A O   
1100 O O   . HOH D .   ? 0.5013 0.5117 0.4752 -0.0178 -0.0369 0.0677  614 HOH A O   
1101 O O   . HOH D .   ? 0.6254 0.6089 0.6242 0.0959  0.0457  0.1639  615 HOH A O   
1102 O O   . HOH D .   ? 0.5344 0.6200 0.4806 0.0063  0.0091  -0.0144 616 HOH A O   
1103 O O   . HOH D .   ? 0.4831 0.9521 0.6184 -0.1536 0.0269  0.0437  617 HOH A O   
1104 O O   . HOH D .   ? 0.4994 0.3059 0.5317 0.0195  0.0891  -0.0164 618 HOH A O   
1105 O O   . HOH D .   ? 0.2868 0.5775 0.3362 0.0649  -0.0344 0.0645  619 HOH A O   
1106 O O   . HOH D .   ? 0.5564 0.6781 0.5521 0.1066  0.0106  0.1326  620 HOH A O   
1107 O O   . HOH D .   ? 0.4361 0.4927 0.4967 0.1572  0.0673  0.0414  621 HOH A O   
1108 O O   . HOH D .   ? 0.4347 0.4496 0.3748 -0.0003 -0.0182 0.0861  622 HOH A O   
1109 O O   . HOH D .   ? 0.4062 0.6562 0.4572 -0.0674 0.0410  0.0586  623 HOH A O   
1110 O O   . HOH D .   ? 0.3692 0.3867 0.3398 0.0232  -0.0347 0.0661  624 HOH A O   
1111 O O   . HOH D .   ? 0.5825 0.4878 0.6014 0.1035  0.0566  0.1272  625 HOH A O   
1112 O O   . HOH D .   ? 0.4041 0.5477 0.3847 0.0504  -0.0191 0.0581  626 HOH A O   
1113 O O   . HOH D .   ? 0.5060 0.4780 0.5126 0.1015  0.0426  0.1473  627 HOH A O   
1114 O O   . HOH D .   ? 0.3982 0.4097 0.3695 0.0047  -0.0460 0.0599  628 HOH A O   
1115 O O   . HOH D .   ? 0.4808 0.2894 0.5105 0.0229  0.0844  0.0852  629 HOH A O   
1116 O O   . HOH D .   ? 0.4530 0.3563 0.4767 -0.0037 0.0528  0.0439  630 HOH A O   
1117 O O   . HOH D .   ? 0.4468 0.4422 0.4490 0.0489  0.0611  -0.0398 631 HOH A O   
1118 O O   . HOH D .   ? 0.3620 0.4074 0.3497 -0.0084 -0.0508 0.0478  632 HOH A O   
1119 O O   . HOH D .   ? 0.5330 0.5686 0.5275 0.0563  0.0703  -0.0651 633 HOH A O   
1120 O O   . HOH D .   ? 0.3602 0.5469 0.3268 -0.0120 -0.0277 -0.0329 634 HOH A O   
1121 O O   . HOH D .   ? 0.4073 0.3584 0.4210 0.0012  0.0329  0.0366  635 HOH A O   
1122 O O   . HOH D .   ? 0.4419 0.4403 0.3994 0.0333  -0.0455 0.0528  636 HOH A O   
1123 O O   . HOH D .   ? 0.4810 0.5170 0.4739 0.0526  0.0377  0.1547  637 HOH A O   
1124 O O   . HOH D .   ? 0.3279 0.3600 0.2648 0.0248  -0.0259 0.0594  638 HOH A O   
1125 O O   . HOH D .   ? 0.3051 0.4241 0.2719 -0.0083 -0.0168 -0.0164 639 HOH A O   
1126 O O   . HOH D .   ? 0.4880 0.7420 0.4906 -0.0686 0.0492  0.0971  640 HOH A O   
1127 O O   . HOH D .   ? 0.4096 0.7872 0.4888 -0.0287 -0.0671 -0.0023 641 HOH A O   
1128 O O   . HOH D .   ? 0.3814 0.4773 0.3698 0.0660  0.0066  0.1146  642 HOH A O   
1129 O O   . HOH D .   ? 0.4111 0.4061 0.4172 -0.0167 0.0220  0.0036  643 HOH A O   
1130 O O   . HOH D .   ? 0.3989 0.5918 0.4410 -0.0556 0.0283  0.0454  644 HOH A O   
1131 O O   . HOH D .   ? 0.3166 0.3150 0.3219 0.0013  0.0142  0.0424  645 HOH A O   
1132 O O   . HOH D .   ? 0.4384 0.5181 0.3848 0.0133  0.0080  0.0460  646 HOH A O   
1133 O O   . HOH D .   ? 0.3876 0.5178 0.4008 0.1096  0.0035  0.1142  647 HOH A O   
1134 O O   . HOH D .   ? 0.4271 0.5676 0.4221 -0.0751 0.0131  -0.1176 648 HOH A O   
1135 O O   . HOH D .   ? 0.5276 0.6442 0.4967 0.0478  -0.0405 0.0284  649 HOH A O   
1136 O O   . HOH D .   ? 0.5341 0.7431 0.4724 0.0142  0.0508  0.0247  650 HOH A O   
1137 O O   . HOH D .   ? 0.5815 0.5971 0.6104 0.1508  0.0407  0.1260  651 HOH A O   
1138 O O   . HOH D .   ? 0.4751 0.5987 0.4476 0.0609  -0.0290 0.0551  652 HOH A O   
1139 O O   . HOH D .   ? 0.4290 0.5718 0.4534 -0.0460 0.0636  0.1271  653 HOH A O   
1140 O O   . HOH D .   ? 0.3829 0.4829 0.4226 -0.0634 0.0498  0.0722  654 HOH A O   
1141 O O   . HOH D .   ? 0.3107 0.3984 0.2950 0.0367  -0.0202 0.0652  655 HOH A O   
1142 O O   . HOH D .   ? 0.4459 0.4313 0.4404 0.0011  0.0418  -0.0440 656 HOH A O   
1143 O O   . HOH D .   ? 0.3191 0.5412 0.3168 0.0317  -0.0309 0.0247  657 HOH A O   
1144 O O   . HOH D .   ? 0.4924 0.5345 0.4632 0.0407  -0.0354 0.0456  658 HOH A O   
1145 O O   . HOH D .   ? 0.2426 0.6713 0.3630 0.0305  0.0012  0.0565  659 HOH A O   
1146 O O   . HOH D .   ? 0.4755 0.5999 0.4501 0.0573  -0.0181 0.0632  660 HOH A O   
1147 O O   . HOH D .   ? 0.3527 0.6331 0.4391 0.1398  0.0204  0.0795  661 HOH A O   
1148 O O   . HOH D .   ? 0.3076 0.3609 0.2870 0.0380  -0.0252 0.0585  662 HOH A O   
1149 O O   . HOH D .   ? 0.6190 0.7594 0.5634 0.0172  0.0329  0.0218  663 HOH A O   
1150 O O   . HOH D .   ? 0.5549 0.5960 0.5169 0.0424  -0.0406 0.0413  664 HOH A O   
1151 O O   . HOH D .   ? 0.4461 0.7265 0.4853 -0.0468 0.0420  0.0797  665 HOH A O   
1152 O O   . HOH D .   ? 0.5936 0.4800 0.6357 0.1285  0.0870  0.0192  666 HOH A O   
1153 O O   . HOH D .   ? 0.4866 0.8265 0.5004 0.0328  -0.0106 0.0376  667 HOH A O   
1154 O O   . HOH D .   ? 0.3584 0.6661 0.4573 0.1289  0.0475  0.0509  668 HOH A O   
1155 O O   . HOH D .   ? 0.4636 0.7999 0.4686 0.0519  0.0888  0.0004  669 HOH A O   
1156 O O   . HOH D .   ? 0.4623 0.5768 0.4430 0.0441  -0.0267 0.0507  670 HOH A O   
1157 O O   . HOH D .   ? 0.4188 0.5203 0.3744 0.0219  -0.0331 0.0218  671 HOH A O   
1158 O O   . HOH D .   ? 0.5549 0.6658 0.4973 0.0153  0.0214  0.0266  672 HOH A O   
1159 O O   . HOH D .   ? 0.2979 0.8485 0.4433 -0.0083 0.0011  0.0353  673 HOH A O   
1160 O O   . HOH D .   ? 0.6702 0.7695 0.5670 -0.0176 0.0160  0.1056  674 HOH A O   
1161 O O   . HOH D .   ? 0.4734 0.8152 0.5809 -0.1041 -0.0234 0.0309  675 HOH A O   
1162 O O   . HOH D .   ? 0.3652 0.5276 0.3517 0.0411  -0.0288 0.0421  676 HOH A O   
1163 O O   . HOH D .   ? 0.4269 0.4934 0.4400 -0.0783 -0.0500 0.0225  677 HOH A O   
1164 O O   . HOH D .   ? 0.3909 0.6503 0.3891 0.0476  -0.0266 0.0194  678 HOH A O   
1165 O O   . HOH D .   ? 0.4448 0.6198 0.4557 -0.1148 0.0202  -0.1715 679 HOH A O   
1166 O O   . HOH D .   ? 0.5903 1.0395 0.6493 -0.0208 0.0784  0.0533  680 HOH A O   
1167 O O   . HOH D .   ? 0.6599 0.4476 0.6988 -0.0203 0.0956  0.0518  681 HOH A O   
1168 O O   . HOH D .   ? 0.5130 0.5526 0.4795 0.0421  -0.0555 0.0414  682 HOH A O   
1169 O O   . HOH D .   ? 0.3605 0.4340 0.3894 -0.0493 0.0622  0.1124  683 HOH A O   
1170 O O   . HOH D .   ? 0.5319 0.6824 0.5001 0.0659  -0.0199 0.0570  684 HOH A O   
1171 O O   . HOH D .   ? 0.2786 0.7011 0.3893 0.0678  -0.0041 0.0611  685 HOH A O   
1172 O O   . HOH D .   ? 0.5812 0.6533 0.5397 0.0109  0.0255  -0.0292 686 HOH A O   
1173 O O   . HOH D .   ? 0.5195 0.7855 0.5465 -0.1029 0.0455  0.1003  687 HOH A O   
1174 O O   . HOH D .   ? 0.7524 0.7241 0.7067 -0.2476 0.0947  0.1888  688 HOH A O   
1175 O O   . HOH D .   ? 0.3482 0.8073 0.4635 0.0942  0.0021  0.0610  689 HOH A O   
1176 O O   . HOH D .   ? 0.5306 0.8149 0.5856 0.1371  0.0998  -0.0317 690 HOH A O   
1177 O O   . HOH D .   ? 0.6495 0.6053 0.6457 0.0377  0.0656  0.1752  691 HOH A O   
1178 O O   . HOH D .   ? 0.6960 0.6375 0.7487 0.1643  0.0913  0.0141  692 HOH A O   
1179 O O   . HOH D .   ? 0.4070 0.4067 0.3484 0.0140  -0.0288 0.0772  693 HOH A O   
1180 O O   . HOH D .   ? 0.5999 0.6004 0.5982 0.0629  0.0890  -0.1103 694 HOH A O   
1181 O O   . HOH D .   ? 0.4532 1.0075 0.6082 -0.1294 0.0236  0.0305  695 HOH A O   
1182 O O   . HOH D .   ? 0.5600 0.4988 0.5717 0.0517  0.0771  -0.0625 696 HOH A O   
1183 O O   . HOH D .   ? 0.6309 0.7569 0.6041 0.0598  -0.0294 0.0364  697 HOH A O   
1184 O O   . HOH D .   ? 0.6434 0.5781 0.6483 0.0079  0.0763  0.1666  698 HOH A O   
1185 O O   . HOH D .   ? 0.8495 0.7045 0.8997 0.1678  0.1144  -0.0210 699 HOH A O   
1186 O O   . HOH D .   ? 0.6395 0.7578 0.6324 0.1315  0.0244  0.1619  700 HOH A O   
1187 O O   . HOH D .   ? 0.5789 0.5887 0.5548 -0.0160 -0.0587 0.0330  701 HOH A O   
1188 O O   . HOH D .   ? 0.7078 0.4958 0.7623 -0.1028 0.1097  -0.1179 702 HOH A O   
1189 O O   . HOH D .   ? 0.4279 0.8036 0.5089 0.0635  0.0668  0.0361  703 HOH A O   
1190 O O   . HOH D .   ? 0.5753 1.2288 0.7157 -0.0578 0.0701  0.0392  704 HOH A O   
1191 O O   . HOH D .   ? 0.3784 0.3686 0.3279 0.0148  -0.0371 0.0742  705 HOH A O   
1192 O O   . HOH D .   ? 0.5345 0.5936 0.4573 0.0232  -0.0229 0.0509  706 HOH A O   
1193 O O   . HOH D .   ? 0.5538 0.5250 0.4900 0.0303  -0.0427 0.0660  707 HOH A O   
1194 O O   . HOH D .   ? 0.4281 0.4257 0.3736 -0.0187 -0.0204 0.0918  708 HOH A O   
1195 O O   . HOH D .   ? 0.4903 0.8097 0.5040 0.0313  -0.0238 0.0112  709 HOH A O   
1196 O O   . HOH D .   ? 0.7098 0.7841 0.5952 -0.0342 0.0212  0.1279  710 HOH A O   
1197 O O   . HOH D .   ? 0.4894 0.7273 0.5213 -0.0555 0.0644  0.1189  711 HOH A O   
1198 O O   . HOH D .   ? 0.4277 0.4302 0.3573 0.0248  -0.0320 0.0681  712 HOH A O   
1199 O O   . HOH D .   ? 0.5722 0.6359 0.6316 -0.1075 0.0742  0.0616  713 HOH A O   
1200 O O   . HOH D .   ? 0.5887 0.6161 0.5692 0.0169  0.0415  -0.0439 714 HOH A O   
1201 O O   . HOH D .   ? 0.5036 0.5693 0.4753 -0.0246 0.0306  -0.0916 715 HOH A O   
1202 O O   . HOH D .   ? 0.5137 0.7938 0.5653 -0.0601 -0.0837 -0.0325 716 HOH A O   
1203 O O   . HOH D .   ? 0.5752 0.7565 0.6183 -0.0742 0.0660  0.1020  717 HOH A O   
1204 O O   . HOH D .   ? 0.2620 0.7673 0.3948 0.0377  0.0032  0.0474  718 HOH A O   
1205 O O   . HOH D .   ? 0.5305 0.6697 0.5029 0.0603  -0.0216 0.0501  719 HOH A O   
1206 O O   . HOH D .   ? 0.4643 0.4464 0.4165 -0.0111 -0.0328 0.0799  720 HOH A O   
1207 O O   . HOH D .   ? 0.5501 0.7493 0.6171 -0.2333 0.0324  0.0765  721 HOH A O   
1208 O O   . HOH D .   ? 0.5798 0.5652 0.6112 -0.0619 0.0923  0.1423  722 HOH A O   
1209 O O   . HOH D .   ? 0.6244 0.5800 0.5460 -0.0300 -0.0188 0.1088  723 HOH A O   
1210 O O   . HOH D .   ? 0.5229 0.6519 0.4720 -0.0260 0.0243  -0.1123 724 HOH A O   
# 
