data_9CU8
# 
_entry.id   9CU8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9CU8         pdb_00009cu8 10.2210/pdb9cu8/pdb 
WWPDB D_1000286351 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-12-04 
2 'Structure model' 1 1 2024-12-18 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               '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 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CU8 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dabaker@uw.edu 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Baker 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7896-6217 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bera, A.K.' 1 ? 
'Glogl, M.'  2 ? 
'Baker, D.'  3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Science 
_citation.journal_id_ASTM           SCIEAS 
_citation.journal_id_CSD            0038 
_citation.journal_id_ISSN           1095-9203 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            386 
_citation.language                  ? 
_citation.page_first                1154 
_citation.page_last                 1161 
_citation.title                     'Target-conditioned diffusion generates potent TNFR superfamily antagonists and agonists.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/science.adp1779 
_citation.pdbx_database_id_PubMed   39636970 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Glogl, M.'        1  ? 
primary 'Krishnakumar, A.' 2  ? 
primary 'Ragotte, R.J.'    3  ? 
primary 'Goreshnik, I.'    4  ? 
primary 'Coventry, B.'     5  ? 
primary 'Bera, A.K.'       6  ? 
primary 'Kang, A.'         7  ? 
primary 'Joyce, E.'        8  ? 
primary 'Ahn, G.'          9  ? 
primary 'Huang, B.'        10 ? 
primary 'Yang, W.'         11 ? 
primary 'Chen, W.'         12 ? 
primary 'Sanchez, M.G.'    13 ? 
primary 'Koepnick, B.'     14 ? 
primary 'Baker, D.'        15 ? 
# 
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 TNFR2_mb1                                              11504.309 1   ? ? ? ? 
2 polymer man 'Tumor necrosis factor receptor superfamily member 1B' 20575.297 1   ? ? ? ? 
3 water   nat water                                                  18.015    186 ? ? ? ? 
# 
_entity_name_com.entity_id   2 
_entity_name_com.name        
'Tumor necrosis factor receptor 2,TNF-R2,Tumor necrosis factor receptor type II,TNF-RII,TNFR-II,p75,p80 TNF-alpha receptor' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;LNPEQVAKIGAAIDAGRKYLDAKIEEAKKTLTLRTAQALLVIRSQYERAVDTLFTDPSAAEKELAATLATIDRLLKEHPE
LAAEIKAFIRSTMAEIRALLAASLAA
;
;LNPEQVAKIGAAIDAGRKYLDAKIEEAKKTLTLRTAQALLVIRSQYERAVDTLFTDPSAAEKELAATLATIDRLLKEHPE
LAAEIKAFIRSTMAEIRALLAASLAA
;
A ? 
2 'polypeptide(L)' no no 
;LPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWVPECLSCGSRCSS
DQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSDVVCKPCAPGTFSNTTSSTDICRPH
QICNVVAIPGNASMDAVCTSTSPTRSMAPG
;
;LPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWVPECLSCGSRCSS
DQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSDVVCKPCAPGTFSNTTSSTDICRPH
QICNVVAIPGNASMDAVCTSTSPTRSMAPG
;
B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LEU n 
1 2   ASN n 
1 3   PRO n 
1 4   GLU n 
1 5   GLN n 
1 6   VAL n 
1 7   ALA n 
1 8   LYS n 
1 9   ILE n 
1 10  GLY n 
1 11  ALA n 
1 12  ALA n 
1 13  ILE n 
1 14  ASP n 
1 15  ALA n 
1 16  GLY n 
1 17  ARG n 
1 18  LYS n 
1 19  TYR n 
1 20  LEU n 
1 21  ASP n 
1 22  ALA n 
1 23  LYS n 
1 24  ILE n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  THR n 
1 31  LEU n 
1 32  THR n 
1 33  LEU n 
1 34  ARG n 
1 35  THR n 
1 36  ALA n 
1 37  GLN n 
1 38  ALA n 
1 39  LEU n 
1 40  LEU n 
1 41  VAL n 
1 42  ILE n 
1 43  ARG n 
1 44  SER n 
1 45  GLN n 
1 46  TYR n 
1 47  GLU n 
1 48  ARG n 
1 49  ALA n 
1 50  VAL n 
1 51  ASP n 
1 52  THR n 
1 53  LEU n 
1 54  PHE n 
1 55  THR n 
1 56  ASP n 
1 57  PRO n 
1 58  SER n 
1 59  ALA n 
1 60  ALA n 
1 61  GLU n 
1 62  LYS n 
1 63  GLU n 
1 64  LEU n 
1 65  ALA n 
1 66  ALA n 
1 67  THR n 
1 68  LEU n 
1 69  ALA n 
1 70  THR n 
1 71  ILE n 
1 72  ASP n 
1 73  ARG n 
1 74  LEU n 
1 75  LEU n 
1 76  LYS n 
1 77  GLU n 
1 78  HIS n 
1 79  PRO n 
1 80  GLU n 
1 81  LEU n 
1 82  ALA n 
1 83  ALA n 
1 84  GLU n 
1 85  ILE n 
1 86  LYS n 
1 87  ALA n 
1 88  PHE n 
1 89  ILE n 
1 90  ARG n 
1 91  SER n 
1 92  THR n 
1 93  MET n 
1 94  ALA n 
1 95  GLU n 
1 96  ILE n 
1 97  ARG n 
1 98  ALA n 
1 99  LEU n 
1 100 LEU n 
1 101 ALA n 
1 102 ALA n 
1 103 SER n 
1 104 LEU n 
1 105 ALA n 
1 106 ALA n 
2 1   LEU n 
2 2   PRO n 
2 3   ALA n 
2 4   GLN n 
2 5   VAL n 
2 6   ALA n 
2 7   PHE n 
2 8   THR n 
2 9   PRO n 
2 10  TYR n 
2 11  ALA n 
2 12  PRO n 
2 13  GLU n 
2 14  PRO n 
2 15  GLY n 
2 16  SER n 
2 17  THR n 
2 18  CYS n 
2 19  ARG n 
2 20  LEU n 
2 21  ARG n 
2 22  GLU n 
2 23  TYR n 
2 24  TYR n 
2 25  ASP n 
2 26  GLN n 
2 27  THR n 
2 28  ALA n 
2 29  GLN n 
2 30  MET n 
2 31  CYS n 
2 32  CYS n 
2 33  SER n 
2 34  LYS n 
2 35  CYS n 
2 36  SER n 
2 37  PRO n 
2 38  GLY n 
2 39  GLN n 
2 40  HIS n 
2 41  ALA n 
2 42  LYS n 
2 43  VAL n 
2 44  PHE n 
2 45  CYS n 
2 46  THR n 
2 47  LYS n 
2 48  THR n 
2 49  SER n 
2 50  ASP n 
2 51  THR n 
2 52  VAL n 
2 53  CYS n 
2 54  ASP n 
2 55  SER n 
2 56  CYS n 
2 57  GLU n 
2 58  ASP n 
2 59  SER n 
2 60  THR n 
2 61  TYR n 
2 62  THR n 
2 63  GLN n 
2 64  LEU n 
2 65  TRP n 
2 66  ASN n 
2 67  TRP n 
2 68  VAL n 
2 69  PRO n 
2 70  GLU n 
2 71  CYS n 
2 72  LEU n 
2 73  SER n 
2 74  CYS n 
2 75  GLY n 
2 76  SER n 
2 77  ARG n 
2 78  CYS n 
2 79  SER n 
2 80  SER n 
2 81  ASP n 
2 82  GLN n 
2 83  VAL n 
2 84  GLU n 
2 85  THR n 
2 86  GLN n 
2 87  ALA n 
2 88  CYS n 
2 89  THR n 
2 90  ARG n 
2 91  GLU n 
2 92  GLN n 
2 93  ASN n 
2 94  ARG n 
2 95  ILE n 
2 96  CYS n 
2 97  THR n 
2 98  CYS n 
2 99  ARG n 
2 100 PRO n 
2 101 GLY n 
2 102 TRP n 
2 103 TYR n 
2 104 CYS n 
2 105 ALA n 
2 106 LEU n 
2 107 SER n 
2 108 LYS n 
2 109 GLN n 
2 110 GLU n 
2 111 GLY n 
2 112 CYS n 
2 113 ARG n 
2 114 LEU n 
2 115 CYS n 
2 116 ALA n 
2 117 PRO n 
2 118 LEU n 
2 119 ARG n 
2 120 LYS n 
2 121 CYS n 
2 122 ARG n 
2 123 PRO n 
2 124 GLY n 
2 125 PHE n 
2 126 GLY n 
2 127 VAL n 
2 128 ALA n 
2 129 ARG n 
2 130 PRO n 
2 131 GLY n 
2 132 THR n 
2 133 GLU n 
2 134 THR n 
2 135 SER n 
2 136 ASP n 
2 137 VAL n 
2 138 VAL n 
2 139 CYS n 
2 140 LYS n 
2 141 PRO n 
2 142 CYS n 
2 143 ALA n 
2 144 PRO n 
2 145 GLY n 
2 146 THR n 
2 147 PHE n 
2 148 SER n 
2 149 ASN n 
2 150 THR n 
2 151 THR n 
2 152 SER n 
2 153 SER n 
2 154 THR n 
2 155 ASP n 
2 156 ILE n 
2 157 CYS n 
2 158 ARG n 
2 159 PRO n 
2 160 HIS n 
2 161 GLN n 
2 162 ILE n 
2 163 CYS n 
2 164 ASN n 
2 165 VAL n 
2 166 VAL n 
2 167 ALA n 
2 168 ILE n 
2 169 PRO n 
2 170 GLY n 
2 171 ASN n 
2 172 ALA n 
2 173 SER n 
2 174 MET n 
2 175 ASP n 
2 176 ALA n 
2 177 VAL n 
2 178 CYS n 
2 179 THR n 
2 180 SER n 
2 181 THR n 
2 182 SER n 
2 183 PRO n 
2 184 THR n 
2 185 ARG n 
2 186 SER n 
2 187 MET n 
2 188 ALA n 
2 189 PRO n 
2 190 GLY n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 106 ?     ? ?                        ? ? ? ? ? ? 'synthetic construct' 32630 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 190 human ? 'TNFRSF1B, TNFBR, TNFR2' ? ? ? ? ? ? 'Homo sapiens'        9606  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
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   LEU 1   1   1   LEU LEU A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   PRO 3   3   3   PRO PRO A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  ARG 43  43  43  ARG ARG A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  HIS 78  78  78  HIS HIS A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  GLU 80  80  80  GLU GLU A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  LYS 86  86  86  LYS LYS A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  MET 93  93  93  MET MET A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
B 2 1   LEU 1   91  91  LEU LEU B . n 
B 2 2   PRO 2   92  92  PRO PRO B . n 
B 2 3   ALA 3   93  93  ALA ALA B . n 
B 2 4   GLN 4   94  94  GLN GLN B . n 
B 2 5   VAL 5   95  95  VAL VAL B . n 
B 2 6   ALA 6   96  96  ALA ALA B . n 
B 2 7   PHE 7   97  97  PHE PHE B . n 
B 2 8   THR 8   98  98  THR THR B . n 
B 2 9   PRO 9   99  99  PRO PRO B . n 
B 2 10  TYR 10  100 100 TYR TYR B . n 
B 2 11  ALA 11  101 101 ALA ALA B . n 
B 2 12  PRO 12  102 102 PRO PRO B . n 
B 2 13  GLU 13  103 103 GLU GLU B . n 
B 2 14  PRO 14  104 104 PRO PRO B . n 
B 2 15  GLY 15  105 105 GLY GLY B . n 
B 2 16  SER 16  106 106 SER SER B . n 
B 2 17  THR 17  107 107 THR THR B . n 
B 2 18  CYS 18  108 108 CYS CYS B . n 
B 2 19  ARG 19  109 109 ARG ARG B . n 
B 2 20  LEU 20  110 110 LEU LEU B . n 
B 2 21  ARG 21  111 111 ARG ARG B . n 
B 2 22  GLU 22  112 112 GLU GLU B . n 
B 2 23  TYR 23  113 113 TYR TYR B . n 
B 2 24  TYR 24  114 114 TYR TYR B . n 
B 2 25  ASP 25  115 115 ASP ASP B . n 
B 2 26  GLN 26  116 116 GLN GLN B . n 
B 2 27  THR 27  117 117 THR THR B . n 
B 2 28  ALA 28  118 118 ALA ALA B . n 
B 2 29  GLN 29  119 119 GLN GLN B . n 
B 2 30  MET 30  120 120 MET MET B . n 
B 2 31  CYS 31  121 121 CYS CYS B . n 
B 2 32  CYS 32  122 122 CYS CYS B . n 
B 2 33  SER 33  123 123 SER SER B . n 
B 2 34  LYS 34  124 124 LYS LYS B . n 
B 2 35  CYS 35  125 125 CYS CYS B . n 
B 2 36  SER 36  126 126 SER SER B . n 
B 2 37  PRO 37  127 127 PRO PRO B . n 
B 2 38  GLY 38  128 128 GLY GLY B . n 
B 2 39  GLN 39  129 129 GLN GLN B . n 
B 2 40  HIS 40  130 130 HIS HIS B . n 
B 2 41  ALA 41  131 131 ALA ALA B . n 
B 2 42  LYS 42  132 132 LYS LYS B . n 
B 2 43  VAL 43  133 133 VAL VAL B . n 
B 2 44  PHE 44  134 134 PHE PHE B . n 
B 2 45  CYS 45  135 135 CYS CYS B . n 
B 2 46  THR 46  136 136 THR THR B . n 
B 2 47  LYS 47  137 137 LYS LYS B . n 
B 2 48  THR 48  138 138 THR THR B . n 
B 2 49  SER 49  139 139 SER SER B . n 
B 2 50  ASP 50  140 140 ASP ASP B . n 
B 2 51  THR 51  141 141 THR THR B . n 
B 2 52  VAL 52  142 142 VAL VAL B . n 
B 2 53  CYS 53  143 143 CYS CYS B . n 
B 2 54  ASP 54  144 144 ASP ASP B . n 
B 2 55  SER 55  145 145 SER SER B . n 
B 2 56  CYS 56  146 146 CYS CYS B . n 
B 2 57  GLU 57  147 147 GLU GLU B . n 
B 2 58  ASP 58  148 148 ASP ASP B . n 
B 2 59  SER 59  149 149 SER SER B . n 
B 2 60  THR 60  150 150 THR THR B . n 
B 2 61  TYR 61  151 151 TYR TYR B . n 
B 2 62  THR 62  152 152 THR THR B . n 
B 2 63  GLN 63  153 153 GLN GLN B . n 
B 2 64  LEU 64  154 154 LEU LEU B . n 
B 2 65  TRP 65  155 155 TRP TRP B . n 
B 2 66  ASN 66  156 156 ASN ASN B . n 
B 2 67  TRP 67  157 157 TRP TRP B . n 
B 2 68  VAL 68  158 158 VAL VAL B . n 
B 2 69  PRO 69  159 159 PRO PRO B . n 
B 2 70  GLU 70  160 160 GLU GLU B . n 
B 2 71  CYS 71  161 161 CYS CYS B . n 
B 2 72  LEU 72  162 162 LEU LEU B . n 
B 2 73  SER 73  163 163 SER SER B . n 
B 2 74  CYS 74  164 164 CYS CYS B . n 
B 2 75  GLY 75  165 165 GLY GLY B . n 
B 2 76  SER 76  166 166 SER SER B . n 
B 2 77  ARG 77  167 167 ARG ARG B . n 
B 2 78  CYS 78  168 168 CYS CYS B . n 
B 2 79  SER 79  169 169 SER SER B . n 
B 2 80  SER 80  170 170 SER SER B . n 
B 2 81  ASP 81  171 171 ASP ASP B . n 
B 2 82  GLN 82  172 172 GLN GLN B . n 
B 2 83  VAL 83  173 173 VAL VAL B . n 
B 2 84  GLU 84  174 174 GLU GLU B . n 
B 2 85  THR 85  175 175 THR THR B . n 
B 2 86  GLN 86  176 176 GLN GLN B . n 
B 2 87  ALA 87  177 177 ALA ALA B . n 
B 2 88  CYS 88  178 178 CYS CYS B . n 
B 2 89  THR 89  179 179 THR THR B . n 
B 2 90  ARG 90  180 180 ARG ARG B . n 
B 2 91  GLU 91  181 181 GLU GLU B . n 
B 2 92  GLN 92  182 182 GLN GLN B . n 
B 2 93  ASN 93  183 183 ASN ASN B . n 
B 2 94  ARG 94  184 184 ARG ARG B . n 
B 2 95  ILE 95  185 185 ILE ILE B . n 
B 2 96  CYS 96  186 186 CYS CYS B . n 
B 2 97  THR 97  187 187 THR THR B . n 
B 2 98  CYS 98  188 188 CYS CYS B . n 
B 2 99  ARG 99  189 189 ARG ARG B . n 
B 2 100 PRO 100 190 190 PRO PRO B . n 
B 2 101 GLY 101 191 191 GLY GLY B . n 
B 2 102 TRP 102 192 192 TRP TRP B . n 
B 2 103 TYR 103 193 193 TYR TYR B . n 
B 2 104 CYS 104 194 194 CYS CYS B . n 
B 2 105 ALA 105 195 195 ALA ALA B . n 
B 2 106 LEU 106 196 196 LEU LEU B . n 
B 2 107 SER 107 197 197 SER SER B . n 
B 2 108 LYS 108 198 198 LYS LYS B . n 
B 2 109 GLN 109 199 199 GLN GLN B . n 
B 2 110 GLU 110 200 200 GLU GLU B . n 
B 2 111 GLY 111 201 201 GLY GLY B . n 
B 2 112 CYS 112 202 202 CYS CYS B . n 
B 2 113 ARG 113 203 203 ARG ARG B . n 
B 2 114 LEU 114 204 204 LEU LEU B . n 
B 2 115 CYS 115 205 205 CYS CYS B . n 
B 2 116 ALA 116 206 206 ALA ALA B . n 
B 2 117 PRO 117 207 207 PRO PRO B . n 
B 2 118 LEU 118 208 208 LEU LEU B . n 
B 2 119 ARG 119 209 209 ARG ARG B . n 
B 2 120 LYS 120 210 210 LYS LYS B . n 
B 2 121 CYS 121 211 211 CYS CYS B . n 
B 2 122 ARG 122 212 212 ARG ARG B . n 
B 2 123 PRO 123 213 213 PRO PRO B . n 
B 2 124 GLY 124 214 214 GLY GLY B . n 
B 2 125 PHE 125 215 215 PHE PHE B . n 
B 2 126 GLY 126 216 216 GLY GLY B . n 
B 2 127 VAL 127 217 217 VAL VAL B . n 
B 2 128 ALA 128 218 218 ALA ALA B . n 
B 2 129 ARG 129 219 219 ARG ARG B . n 
B 2 130 PRO 130 220 220 PRO PRO B . n 
B 2 131 GLY 131 221 221 GLY GLY B . n 
B 2 132 THR 132 222 222 THR THR B . n 
B 2 133 GLU 133 223 223 GLU GLU B . n 
B 2 134 THR 134 224 224 THR THR B . n 
B 2 135 SER 135 225 225 SER SER B . n 
B 2 136 ASP 136 226 226 ASP ASP B . n 
B 2 137 VAL 137 227 227 VAL VAL B . n 
B 2 138 VAL 138 228 228 VAL VAL B . n 
B 2 139 CYS 139 229 229 CYS CYS B . n 
B 2 140 LYS 140 230 230 LYS LYS B . n 
B 2 141 PRO 141 231 231 PRO PRO B . n 
B 2 142 CYS 142 232 232 CYS CYS B . n 
B 2 143 ALA 143 233 233 ALA ALA B . n 
B 2 144 PRO 144 234 234 PRO PRO B . n 
B 2 145 GLY 145 235 235 GLY GLY B . n 
B 2 146 THR 146 236 236 THR THR B . n 
B 2 147 PHE 147 237 237 PHE PHE B . n 
B 2 148 SER 148 238 238 SER SER B . n 
B 2 149 ASN 149 239 239 ASN ASN B . n 
B 2 150 THR 150 240 240 THR THR B . n 
B 2 151 THR 151 241 241 THR THR B . n 
B 2 152 SER 152 242 242 SER SER B . n 
B 2 153 SER 153 243 243 SER SER B . n 
B 2 154 THR 154 244 244 THR THR B . n 
B 2 155 ASP 155 245 245 ASP ASP B . n 
B 2 156 ILE 156 246 246 ILE ILE B . n 
B 2 157 CYS 157 247 247 CYS CYS B . n 
B 2 158 ARG 158 248 248 ARG ARG B . n 
B 2 159 PRO 159 249 249 PRO PRO B . n 
B 2 160 HIS 160 250 250 HIS HIS B . n 
B 2 161 GLN 161 251 251 GLN GLN B . n 
B 2 162 ILE 162 252 252 ILE ILE B . n 
B 2 163 CYS 163 253 253 CYS CYS B . n 
B 2 164 ASN 164 254 254 ASN ASN B . n 
B 2 165 VAL 165 255 255 VAL VAL B . n 
B 2 166 VAL 166 256 256 VAL VAL B . n 
B 2 167 ALA 167 257 257 ALA ALA B . n 
B 2 168 ILE 168 258 258 ILE ILE B . n 
B 2 169 PRO 169 259 259 PRO PRO B . n 
B 2 170 GLY 170 260 260 GLY GLY B . n 
B 2 171 ASN 171 261 261 ASN ASN B . n 
B 2 172 ALA 172 262 262 ALA ALA B . n 
B 2 173 SER 173 263 263 SER SER B . n 
B 2 174 MET 174 264 264 MET MET B . n 
B 2 175 ASP 175 265 265 ASP ASP B . n 
B 2 176 ALA 176 266 266 ALA ALA B . n 
B 2 177 VAL 177 267 267 VAL VAL B . n 
B 2 178 CYS 178 268 268 CYS CYS B . n 
B 2 179 THR 179 269 269 THR THR B . n 
B 2 180 SER 180 270 ?   ?   ?   B . n 
B 2 181 THR 181 271 ?   ?   ?   B . n 
B 2 182 SER 182 272 ?   ?   ?   B . n 
B 2 183 PRO 183 273 ?   ?   ?   B . n 
B 2 184 THR 184 274 ?   ?   ?   B . n 
B 2 185 ARG 185 275 ?   ?   ?   B . n 
B 2 186 SER 186 276 ?   ?   ?   B . n 
B 2 187 MET 187 277 ?   ?   ?   B . n 
B 2 188 ALA 188 278 ?   ?   ?   B . n 
B 2 189 PRO 189 279 ?   ?   ?   B . n 
B 2 190 GLY 190 280 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 HOH 1   201 196 HOH HOH A . 
C 3 HOH 2   202 143 HOH HOH A . 
C 3 HOH 3   203 78  HOH HOH A . 
C 3 HOH 4   204 39  HOH HOH A . 
C 3 HOH 5   205 115 HOH HOH A . 
C 3 HOH 6   206 63  HOH HOH A . 
C 3 HOH 7   207 195 HOH HOH A . 
C 3 HOH 8   208 190 HOH HOH A . 
C 3 HOH 9   209 148 HOH HOH A . 
C 3 HOH 10  210 3   HOH HOH A . 
C 3 HOH 11  211 176 HOH HOH A . 
C 3 HOH 12  212 121 HOH HOH A . 
C 3 HOH 13  213 171 HOH HOH A . 
C 3 HOH 14  214 126 HOH HOH A . 
C 3 HOH 15  215 56  HOH HOH A . 
C 3 HOH 16  216 105 HOH HOH A . 
C 3 HOH 17  217 158 HOH HOH A . 
C 3 HOH 18  218 7   HOH HOH A . 
C 3 HOH 19  219 12  HOH HOH A . 
C 3 HOH 20  220 69  HOH HOH A . 
C 3 HOH 21  221 61  HOH HOH A . 
C 3 HOH 22  222 197 HOH HOH A . 
C 3 HOH 23  223 60  HOH HOH A . 
C 3 HOH 24  224 155 HOH HOH A . 
C 3 HOH 25  225 116 HOH HOH A . 
C 3 HOH 26  226 119 HOH HOH A . 
C 3 HOH 27  227 21  HOH HOH A . 
C 3 HOH 28  228 188 HOH HOH A . 
C 3 HOH 29  229 96  HOH HOH A . 
C 3 HOH 30  230 80  HOH HOH A . 
C 3 HOH 31  231 71  HOH HOH A . 
C 3 HOH 32  232 103 HOH HOH A . 
C 3 HOH 33  233 40  HOH HOH A . 
C 3 HOH 34  234 67  HOH HOH A . 
C 3 HOH 35  235 28  HOH HOH A . 
C 3 HOH 36  236 159 HOH HOH A . 
C 3 HOH 37  237 97  HOH HOH A . 
C 3 HOH 38  238 90  HOH HOH A . 
C 3 HOH 39  239 94  HOH HOH A . 
C 3 HOH 40  240 19  HOH HOH A . 
C 3 HOH 41  241 111 HOH HOH A . 
C 3 HOH 42  242 35  HOH HOH A . 
C 3 HOH 43  243 169 HOH HOH A . 
C 3 HOH 44  244 172 HOH HOH A . 
C 3 HOH 45  245 117 HOH HOH A . 
C 3 HOH 46  246 131 HOH HOH A . 
C 3 HOH 47  247 74  HOH HOH A . 
C 3 HOH 48  248 137 HOH HOH A . 
C 3 HOH 49  249 132 HOH HOH A . 
C 3 HOH 50  250 43  HOH HOH A . 
C 3 HOH 51  251 32  HOH HOH A . 
C 3 HOH 52  252 178 HOH HOH A . 
C 3 HOH 53  253 133 HOH HOH A . 
C 3 HOH 54  254 165 HOH HOH A . 
C 3 HOH 55  255 180 HOH HOH A . 
C 3 HOH 56  256 112 HOH HOH A . 
D 3 HOH 1   301 70  HOH HOH B . 
D 3 HOH 2   302 73  HOH HOH B . 
D 3 HOH 3   303 166 HOH HOH B . 
D 3 HOH 4   304 1   HOH HOH B . 
D 3 HOH 5   305 173 HOH HOH B . 
D 3 HOH 6   306 14  HOH HOH B . 
D 3 HOH 7   307 140 HOH HOH B . 
D 3 HOH 8   308 24  HOH HOH B . 
D 3 HOH 9   309 58  HOH HOH B . 
D 3 HOH 10  310 22  HOH HOH B . 
D 3 HOH 11  311 161 HOH HOH B . 
D 3 HOH 12  312 187 HOH HOH B . 
D 3 HOH 13  313 107 HOH HOH B . 
D 3 HOH 14  314 138 HOH HOH B . 
D 3 HOH 15  315 99  HOH HOH B . 
D 3 HOH 16  316 87  HOH HOH B . 
D 3 HOH 17  317 20  HOH HOH B . 
D 3 HOH 18  318 120 HOH HOH B . 
D 3 HOH 19  319 101 HOH HOH B . 
D 3 HOH 20  320 130 HOH HOH B . 
D 3 HOH 21  321 184 HOH HOH B . 
D 3 HOH 22  322 83  HOH HOH B . 
D 3 HOH 23  323 36  HOH HOH B . 
D 3 HOH 24  324 136 HOH HOH B . 
D 3 HOH 25  325 124 HOH HOH B . 
D 3 HOH 26  326 31  HOH HOH B . 
D 3 HOH 27  327 98  HOH HOH B . 
D 3 HOH 28  328 77  HOH HOH B . 
D 3 HOH 29  329 5   HOH HOH B . 
D 3 HOH 30  330 149 HOH HOH B . 
D 3 HOH 31  331 13  HOH HOH B . 
D 3 HOH 32  332 26  HOH HOH B . 
D 3 HOH 33  333 75  HOH HOH B . 
D 3 HOH 34  334 17  HOH HOH B . 
D 3 HOH 35  335 6   HOH HOH B . 
D 3 HOH 36  336 109 HOH HOH B . 
D 3 HOH 37  337 38  HOH HOH B . 
D 3 HOH 38  338 34  HOH HOH B . 
D 3 HOH 39  339 81  HOH HOH B . 
D 3 HOH 40  340 76  HOH HOH B . 
D 3 HOH 41  341 45  HOH HOH B . 
D 3 HOH 42  342 91  HOH HOH B . 
D 3 HOH 43  343 89  HOH HOH B . 
D 3 HOH 44  344 27  HOH HOH B . 
D 3 HOH 45  345 153 HOH HOH B . 
D 3 HOH 46  346 84  HOH HOH B . 
D 3 HOH 47  347 2   HOH HOH B . 
D 3 HOH 48  348 52  HOH HOH B . 
D 3 HOH 49  349 10  HOH HOH B . 
D 3 HOH 50  350 145 HOH HOH B . 
D 3 HOH 51  351 15  HOH HOH B . 
D 3 HOH 52  352 8   HOH HOH B . 
D 3 HOH 53  353 68  HOH HOH B . 
D 3 HOH 54  354 41  HOH HOH B . 
D 3 HOH 55  355 66  HOH HOH B . 
D 3 HOH 56  356 163 HOH HOH B . 
D 3 HOH 57  357 106 HOH HOH B . 
D 3 HOH 58  358 25  HOH HOH B . 
D 3 HOH 59  359 53  HOH HOH B . 
D 3 HOH 60  360 191 HOH HOH B . 
D 3 HOH 61  361 37  HOH HOH B . 
D 3 HOH 62  362 11  HOH HOH B . 
D 3 HOH 63  363 139 HOH HOH B . 
D 3 HOH 64  364 23  HOH HOH B . 
D 3 HOH 65  365 142 HOH HOH B . 
D 3 HOH 66  366 57  HOH HOH B . 
D 3 HOH 67  367 47  HOH HOH B . 
D 3 HOH 68  368 46  HOH HOH B . 
D 3 HOH 69  369 85  HOH HOH B . 
D 3 HOH 70  370 167 HOH HOH B . 
D 3 HOH 71  371 114 HOH HOH B . 
D 3 HOH 72  372 54  HOH HOH B . 
D 3 HOH 73  373 88  HOH HOH B . 
D 3 HOH 74  374 30  HOH HOH B . 
D 3 HOH 75  375 168 HOH HOH B . 
D 3 HOH 76  376 183 HOH HOH B . 
D 3 HOH 77  377 199 HOH HOH B . 
D 3 HOH 78  378 44  HOH HOH B . 
D 3 HOH 79  379 48  HOH HOH B . 
D 3 HOH 80  380 118 HOH HOH B . 
D 3 HOH 81  381 92  HOH HOH B . 
D 3 HOH 82  382 4   HOH HOH B . 
D 3 HOH 83  383 134 HOH HOH B . 
D 3 HOH 84  384 154 HOH HOH B . 
D 3 HOH 85  385 49  HOH HOH B . 
D 3 HOH 86  386 59  HOH HOH B . 
D 3 HOH 87  387 150 HOH HOH B . 
D 3 HOH 88  388 147 HOH HOH B . 
D 3 HOH 89  389 86  HOH HOH B . 
D 3 HOH 90  390 51  HOH HOH B . 
D 3 HOH 91  391 198 HOH HOH B . 
D 3 HOH 92  392 122 HOH HOH B . 
D 3 HOH 93  393 82  HOH HOH B . 
D 3 HOH 94  394 65  HOH HOH B . 
D 3 HOH 95  395 100 HOH HOH B . 
D 3 HOH 96  396 29  HOH HOH B . 
D 3 HOH 97  397 16  HOH HOH B . 
D 3 HOH 98  398 55  HOH HOH B . 
D 3 HOH 99  399 160 HOH HOH B . 
D 3 HOH 100 400 182 HOH HOH B . 
D 3 HOH 101 401 64  HOH HOH B . 
D 3 HOH 102 402 179 HOH HOH B . 
D 3 HOH 103 403 50  HOH HOH B . 
D 3 HOH 104 404 128 HOH HOH B . 
D 3 HOH 105 405 18  HOH HOH B . 
D 3 HOH 106 406 177 HOH HOH B . 
D 3 HOH 107 407 125 HOH HOH B . 
D 3 HOH 108 408 144 HOH HOH B . 
D 3 HOH 109 409 62  HOH HOH B . 
D 3 HOH 110 410 104 HOH HOH B . 
D 3 HOH 111 411 95  HOH HOH B . 
D 3 HOH 112 412 42  HOH HOH B . 
D 3 HOH 113 413 33  HOH HOH B . 
D 3 HOH 114 414 93  HOH HOH B . 
D 3 HOH 115 415 162 HOH HOH B . 
D 3 HOH 116 416 146 HOH HOH B . 
D 3 HOH 117 417 194 HOH HOH B . 
D 3 HOH 118 418 113 HOH HOH B . 
D 3 HOH 119 419 135 HOH HOH B . 
D 3 HOH 120 420 108 HOH HOH B . 
D 3 HOH 121 421 189 HOH HOH B . 
D 3 HOH 122 422 186 HOH HOH B . 
D 3 HOH 123 423 192 HOH HOH B . 
D 3 HOH 124 424 79  HOH HOH B . 
D 3 HOH 125 425 151 HOH HOH B . 
D 3 HOH 126 426 156 HOH HOH B . 
D 3 HOH 127 427 193 HOH HOH B . 
D 3 HOH 128 428 102 HOH HOH B . 
D 3 HOH 129 429 185 HOH HOH B . 
D 3 HOH 130 430 127 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.21.1_5286: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CU8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     35.071 
_cell.length_a_esd                 ? 
_cell.length_b                     74.621 
_cell.length_b_esd                 ? 
_cell.length_c                     104.973 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CU8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CU8 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.47 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    
'1.0M Imidazole; MES monohydrate (acid) pH 6.5, 0.12 M Monosaccharides, 40% v/v PEG 500 MME; 20% w/v PEG 20000' 
_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 EIGER2 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         2024-07-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97936 
_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                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97936 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          26.97 
_reflns.entry_id                                       9CU8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.96 
_reflns.d_resolution_low                               29.16 
_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                                     20443 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.137 
_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                                    1.96 
_reflns_shell.d_res_low                                     2.01 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.60 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1409 
_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                               10.7 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.880 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.725 
_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                                 9CU8 
_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                            1.96 
_refine.ls_d_res_low                             29.16 
_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                     20386 
_refine.ls_number_reflns_R_free                  1998 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.66 
_refine.ls_percent_reflns_R_free                 9.80 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1869 
_refine.ls_R_factor_R_free                       0.2226 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1830 
_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                          1.36 
_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                 22.59 
_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                            0.22 
_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                       1.96 
_refine_hist.d_res_low                        29.16 
_refine_hist.number_atoms_solvent             187 
_refine_hist.number_atoms_total               2339 
_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        2152 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.799  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.725 ? 838 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 353 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 394 ? 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' 1.96 2.01  . . 134 1229 96.00  . . . . 0.2199 . . . . . . . . . . . 0.2808 
'X-RAY DIFFRACTION' 2.01 2.06  . . 140 1298 100.00 . . . . 0.1970 . . . . . . . . . . . 0.2931 
'X-RAY DIFFRACTION' 2.06 2.13  . . 139 1278 100.00 . . . . 0.1917 . . . . . . . . . . . 0.2291 
'X-RAY DIFFRACTION' 2.13 2.19  . . 142 1311 100.00 . . . . 0.1852 . . . . . . . . . . . 0.2390 
'X-RAY DIFFRACTION' 2.19 2.27  . . 139 1269 100.00 . . . . 0.1780 . . . . . . . . . . . 0.2722 
'X-RAY DIFFRACTION' 2.27 2.36  . . 141 1309 100.00 . . . . 0.1921 . . . . . . . . . . . 0.2595 
'X-RAY DIFFRACTION' 2.36 2.47  . . 143 1315 100.00 . . . . 0.1832 . . . . . . . . . . . 0.2330 
'X-RAY DIFFRACTION' 2.47 2.60  . . 141 1288 100.00 . . . . 0.1880 . . . . . . . . . . . 0.2762 
'X-RAY DIFFRACTION' 2.60 2.76  . . 144 1324 100.00 . . . . 0.1926 . . . . . . . . . . . 0.2190 
'X-RAY DIFFRACTION' 2.76 2.98  . . 143 1314 100.00 . . . . 0.1963 . . . . . . . . . . . 0.2597 
'X-RAY DIFFRACTION' 2.98 3.28  . . 142 1318 100.00 . . . . 0.1878 . . . . . . . . . . . 0.2454 
'X-RAY DIFFRACTION' 3.28 3.75  . . 146 1337 100.00 . . . . 0.1745 . . . . . . . . . . . 0.2023 
'X-RAY DIFFRACTION' 3.75 4.72  . . 147 1355 100.00 . . . . 0.1502 . . . . . . . . . . . 0.1670 
'X-RAY DIFFRACTION' 4.72 29.16 . . 157 1443 100.00 . . . . 0.1986 . . . . . . . . . . . 0.2045 
# 
_struct.entry_id                     9CU8 
_struct.title                        'Crystal Structure of TNFR2 TNFR2_mb1 Complex' 
_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        9CU8 
_struct_keywords.text            'De novo protein, TNFR2, antagonists and agonists, TNFR1' 
_struct_keywords.pdbx_keywords   'DE NOVO PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 9CU8        9CU8   ? 1 ? 1  
2 UNP TNR1B_HUMAN P20333 ? 2 
;LPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWVPECLSCGSRCSS
DQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSDVVCKPCAPGTFSNTTSSTDICRPH
QICNVVAIPGNASMDAVCTSTSPTRSMAPG
;
23 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CU8 A 1 ? 106 ? 9CU8   1  ? 106 ? 1  106 
2 2 9CU8 B 1 ? 190 ? P20333 23 ? 212 ? 91 280 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2140  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  15990 ? 
# 
_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   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASN A 2  ? THR A 30  ? ASN A 2  THR A 30  1 ? 29 
HELX_P HELX_P2 AA2 THR A 32 ? ASP A 56  ? THR A 32 ASP A 56  1 ? 25 
HELX_P HELX_P3 AA3 ALA A 59 ? LEU A 75  ? ALA A 59 LEU A 75  1 ? 17 
HELX_P HELX_P4 AA4 HIS A 78 ? ALA A 105 ? HIS A 78 ALA A 105 1 ? 28 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? B CYS 18  SG ? ? ? 1_555 B CYS 31  SG ? ? B CYS 108 B CYS 121 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf2  disulf ? ? B CYS 32  SG ? ? ? 1_555 B CYS 45  SG ? ? B CYS 122 B CYS 135 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf3  disulf ? ? B CYS 35  SG ? ? ? 1_555 B CYS 53  SG ? ? B CYS 125 B CYS 143 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf4  disulf ? ? B CYS 56  SG ? ? ? 1_555 B CYS 71  SG ? ? B CYS 146 B CYS 161 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf5  disulf ? ? B CYS 74  SG ? ? ? 1_555 B CYS 88  SG ? ? B CYS 164 B CYS 178 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf6  disulf ? ? B CYS 78  SG ? ? ? 1_555 B CYS 96  SG ? ? B CYS 168 B CYS 186 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf7  disulf ? ? B CYS 98  SG ? ? ? 1_555 B CYS 115 SG ? ? B CYS 188 B CYS 205 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf8  disulf ? ? B CYS 104 SG ? ? ? 1_555 B CYS 112 SG ? ? B CYS 194 B CYS 202 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
disulf9  disulf ? ? B CYS 121 SG ? ? ? 1_555 B CYS 139 SG ? ? B CYS 211 B CYS 229 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf10 disulf ? ? B CYS 142 SG ? ? ? 1_555 B CYS 157 SG ? ? B CYS 232 B CYS 247 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
disulf11 disulf ? ? B CYS 163 SG ? ? ? 1_555 B CYS 178 SG ? ? B CYS 253 B CYS 268 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  CYS B 18  ? CYS B 31  ? CYS B 108 ? 1_555 CYS B 121 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS B 32  ? CYS B 45  ? CYS B 122 ? 1_555 CYS B 135 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS B 35  ? CYS B 53  ? CYS B 125 ? 1_555 CYS B 143 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS B 56  ? CYS B 71  ? CYS B 146 ? 1_555 CYS B 161 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS B 74  ? CYS B 88  ? CYS B 164 ? 1_555 CYS B 178 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS B 78  ? CYS B 96  ? CYS B 168 ? 1_555 CYS B 186 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS B 98  ? CYS B 115 ? CYS B 188 ? 1_555 CYS B 205 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS B 104 ? CYS B 112 ? CYS B 194 ? 1_555 CYS B 202 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS B 121 ? CYS B 139 ? CYS B 211 ? 1_555 CYS B 229 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS B 142 ? CYS B 157 ? CYS B 232 ? 1_555 CYS B 247 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS B 163 ? CYS B 178 ? CYS B 253 ? 1_555 CYS B 268 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          THR 
_struct_mon_prot_cis.label_seq_id           8 
_struct_mon_prot_cis.label_asym_id          B 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           THR 
_struct_mon_prot_cis.auth_seq_id            98 
_struct_mon_prot_cis.auth_asym_id           B 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    9 
_struct_mon_prot_cis.pdbx_label_asym_id_2   B 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     99 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    B 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.06 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU B 22  ? ASP B 25  ? GLU B 112 ASP B 115 
AA1 2 MET B 30  ? SER B 33  ? MET B 120 SER B 123 
AA2 1 GLN B 39  ? VAL B 43  ? GLN B 129 VAL B 133 
AA2 2 VAL B 52  ? SER B 55  ? VAL B 142 SER B 145 
AA3 1 THR B 60  ? TYR B 61  ? THR B 150 TYR B 151 
AA3 2 LEU B 72  ? SER B 73  ? LEU B 162 SER B 163 
AA4 1 VAL B 83  ? GLN B 86  ? VAL B 173 GLN B 176 
AA4 2 ILE B 95  ? THR B 97  ? ILE B 185 THR B 187 
AA5 1 TRP B 102 ? SER B 107 ? TRP B 192 SER B 197 
AA5 2 CYS B 112 ? PRO B 117 ? CYS B 202 PRO B 207 
AA6 1 PHE B 125 ? ARG B 129 ? PHE B 215 ARG B 219 
AA6 2 VAL B 138 ? PRO B 141 ? VAL B 228 PRO B 231 
AA7 1 THR B 146 ? PHE B 147 ? THR B 236 PHE B 237 
AA7 2 ARG B 158 ? PRO B 159 ? ARG B 248 PRO B 249 
AA8 1 VAL B 166 ? ILE B 168 ? VAL B 256 ILE B 258 
AA8 2 VAL B 177 ? CYS B 178 ? VAL B 267 CYS B 268 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASP B 25  ? N ASP B 115 O MET B 30  ? O MET B 120 
AA2 1 2 N VAL B 43  ? N VAL B 133 O VAL B 52  ? O VAL B 142 
AA3 1 2 N TYR B 61  ? N TYR B 151 O LEU B 72  ? O LEU B 162 
AA4 1 2 N VAL B 83  ? N VAL B 173 O THR B 97  ? O THR B 187 
AA5 1 2 N TYR B 103 ? N TYR B 193 O ALA B 116 ? O ALA B 206 
AA6 1 2 N ALA B 128 ? N ALA B 218 O VAL B 138 ? O VAL B 228 
AA7 1 2 N PHE B 147 ? N PHE B 237 O ARG B 158 ? O ARG B 248 
AA8 1 2 N ILE B 168 ? N ILE B 258 O VAL B 177 ? O VAL B 267 
# 
_pdbx_entry_details.entry_id                   9CU8 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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   B GLU 103 ? ? OG B SER 106 ? ? 2.13 
2 1 ND2 B ASN 261 ? ? O  B HOH 301 ? ? 2.17 
3 1 O   A HOH 207 ? ? O  A HOH 246 ? ? 2.17 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     56 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -155.02 
_pdbx_validate_torsion.psi             82.52 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 B SER 270 ? B SER 180 
2  1 Y 1 B THR 271 ? B THR 181 
3  1 Y 1 B SER 272 ? B SER 182 
4  1 Y 1 B PRO 273 ? B PRO 183 
5  1 Y 1 B THR 274 ? B THR 184 
6  1 Y 1 B ARG 275 ? B ARG 185 
7  1 Y 1 B SER 276 ? B SER 186 
8  1 Y 1 B MET 277 ? B MET 187 
9  1 Y 1 B ALA 278 ? B ALA 188 
10 1 Y 1 B PRO 279 ? B PRO 189 
11 1 Y 1 B GLY 280 ? B GLY 190 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Howard Hughes Medical Institute (HHMI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'de novo design model' 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CU8 
_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]   0.028514 
_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]   0.013401 
_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]   0.009526 
_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   . LEU A 1 1   ? 2.434   25.099  -11.910 1.00 42.91 ? 1   LEU A N   1 
ATOM   2    C CA  . LEU A 1 1   ? 2.679   24.424  -13.181 1.00 37.49 ? 1   LEU A CA  1 
ATOM   3    C C   . LEU A 1 1   ? 1.790   24.967  -14.306 1.00 40.24 ? 1   LEU A C   1 
ATOM   4    O O   . LEU A 1 1   ? 0.560   24.947  -14.207 1.00 42.73 ? 1   LEU A O   1 
ATOM   5    C CB  . LEU A 1 1   ? 2.460   22.909  -13.027 1.00 39.82 ? 1   LEU A CB  1 
ATOM   6    C CG  . LEU A 1 1   ? 3.364   22.138  -12.052 1.00 38.62 ? 1   LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 1   ? 2.931   20.683  -11.922 1.00 42.04 ? 1   LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 1   ? 4.820   22.203  -12.485 1.00 39.26 ? 1   LEU A CD2 1 
ATOM   9    N N   . ASN A 1 2   ? 2.407   25.450  -15.377 1.00 38.18 ? 2   ASN A N   1 
ATOM   10   C CA  . ASN A 1 2   ? 1.668   25.864  -16.562 1.00 38.16 ? 2   ASN A CA  1 
ATOM   11   C C   . ASN A 1 2   ? 1.472   24.671  -17.491 1.00 38.95 ? 2   ASN A C   1 
ATOM   12   O O   . ASN A 1 2   ? 2.093   23.620  -17.314 1.00 37.19 ? 2   ASN A O   1 
ATOM   13   C CB  . ASN A 1 2   ? 2.395   27.025  -17.245 1.00 40.55 ? 2   ASN A CB  1 
ATOM   14   C CG  . ASN A 1 2   ? 3.784   26.655  -17.759 1.00 43.02 ? 2   ASN A CG  1 
ATOM   15   O OD1 . ASN A 1 2   ? 4.008   25.558  -18.269 1.00 41.58 ? 2   ASN A OD1 1 
ATOM   16   N ND2 . ASN A 1 2   ? 4.721   27.597  -17.649 1.00 40.61 ? 2   ASN A ND2 1 
ATOM   17   N N   . PRO A 1 3   ? 0.587   24.784  -18.488 1.00 40.23 ? 3   PRO A N   1 
ATOM   18   C CA  . PRO A 1 3   ? 0.312   23.613  -19.344 1.00 34.64 ? 3   PRO A CA  1 
ATOM   19   C C   . PRO A 1 3   ? 1.537   23.024  -20.029 1.00 36.25 ? 3   PRO A C   1 
ATOM   20   O O   . PRO A 1 3   ? 1.556   21.811  -20.280 1.00 26.53 ? 3   PRO A O   1 
ATOM   21   C CB  . PRO A 1 3   ? -0.702  24.157  -20.356 1.00 40.08 ? 3   PRO A CB  1 
ATOM   22   C CG  . PRO A 1 3   ? -1.462  25.192  -19.557 1.00 41.29 ? 3   PRO A CG  1 
ATOM   23   C CD  . PRO A 1 3   ? -0.408  25.857  -18.698 1.00 40.20 ? 3   PRO A CD  1 
ATOM   24   N N   . GLU A 1 4   ? 2.566   23.821  -20.333 1.00 26.62 ? 4   GLU A N   1 
ATOM   25   C CA  . GLU A 1 4   ? 3.751   23.233  -20.954 1.00 34.40 ? 4   GLU A CA  1 
ATOM   26   C C   . GLU A 1 4   ? 4.486   22.327  -19.979 1.00 31.03 ? 4   GLU A C   1 
ATOM   27   O O   . GLU A 1 4   ? 4.884   21.212  -20.334 1.00 32.22 ? 4   GLU A O   1 
ATOM   28   C CB  . GLU A 1 4   ? 4.705   24.310  -21.468 1.00 35.04 ? 4   GLU A CB  1 
ATOM   29   C CG  . GLU A 1 4   ? 5.541   23.832  -22.645 1.00 43.98 ? 4   GLU A CG  1 
ATOM   30   C CD  . GLU A 1 4   ? 6.878   24.544  -22.774 1.00 65.39 ? 4   GLU A CD  1 
ATOM   31   O OE1 . GLU A 1 4   ? 7.921   23.849  -22.819 1.00 65.95 ? 4   GLU A OE1 1 
ATOM   32   O OE2 . GLU A 1 4   ? 6.883   25.797  -22.832 1.00 66.83 ? 4   GLU A OE2 1 
ATOM   33   N N   . GLN A 1 5   ? 4.688   22.803  -18.750 1.00 28.74 ? 5   GLN A N   1 
ATOM   34   C CA  . GLN A 1 5   ? 5.389   22.014  -17.746 1.00 31.16 ? 5   GLN A CA  1 
ATOM   35   C C   . GLN A 1 5   ? 4.632   20.729  -17.429 1.00 27.96 ? 5   GLN A C   1 
ATOM   36   O O   . GLN A 1 5   ? 5.236   19.653  -17.318 1.00 23.68 ? 5   GLN A O   1 
ATOM   37   C CB  . GLN A 1 5   ? 5.589   22.858  -16.487 1.00 31.24 ? 5   GLN A CB  1 
ATOM   38   C CG  . GLN A 1 5   ? 6.372   24.136  -16.758 1.00 40.45 ? 5   GLN A CG  1 
ATOM   39   C CD  . GLN A 1 5   ? 6.151   25.229  -15.715 1.00 44.18 ? 5   GLN A CD  1 
ATOM   40   O OE1 . GLN A 1 5   ? 5.059   25.377  -15.162 1.00 45.85 ? 5   GLN A OE1 1 
ATOM   41   N NE2 . GLN A 1 5   ? 7.197   26.005  -15.450 1.00 51.00 ? 5   GLN A NE2 1 
ATOM   42   N N   . VAL A 1 6   ? 3.308   20.824  -17.279 1.00 27.72 ? 6   VAL A N   1 
ATOM   43   C CA  . VAL A 1 6   ? 2.508   19.641  -16.972 1.00 22.94 ? 6   VAL A CA  1 
ATOM   44   C C   . VAL A 1 6   ? 2.646   18.615  -18.081 1.00 27.33 ? 6   VAL A C   1 
ATOM   45   O O   . VAL A 1 6   ? 2.790   17.412  -17.821 1.00 24.56 ? 6   VAL A O   1 
ATOM   46   C CB  . VAL A 1 6   ? 1.036   20.035  -16.734 1.00 29.92 ? 6   VAL A CB  1 
ATOM   47   C CG1 . VAL A 1 6   ? 0.115   18.809  -16.715 1.00 26.26 ? 6   VAL A CG1 1 
ATOM   48   C CG2 . VAL A 1 6   ? 0.907   20.798  -15.434 1.00 29.91 ? 6   VAL A CG2 1 
ATOM   49   N N   . ALA A 1 7   ? 2.636   19.074  -19.338 1.00 22.56 ? 7   ALA A N   1 
ATOM   50   C CA  . ALA A 1 7   ? 2.767   18.150  -20.461 1.00 24.89 ? 7   ALA A CA  1 
ATOM   51   C C   . ALA A 1 7   ? 4.123   17.451  -20.452 1.00 25.22 ? 7   ALA A C   1 
ATOM   52   O O   . ALA A 1 7   ? 4.207   16.243  -20.713 1.00 27.63 ? 7   ALA A O   1 
ATOM   53   C CB  . ALA A 1 7   ? 2.550   18.891  -21.778 1.00 33.08 ? 7   ALA A CB  1 
ATOM   54   N N   . LYS A 1 8   ? 5.198   18.189  -20.157 1.00 26.05 ? 8   LYS A N   1 
ATOM   55   C CA  . LYS A 1 8   ? 6.518   17.563  -20.064 1.00 25.63 ? 8   LYS A CA  1 
ATOM   56   C C   . LYS A 1 8   ? 6.592   16.577  -18.902 1.00 24.02 ? 8   LYS A C   1 
ATOM   57   O O   . LYS A 1 8   ? 7.208   15.507  -19.018 1.00 21.96 ? 8   LYS A O   1 
ATOM   58   C CB  . LYS A 1 8   ? 7.597   18.629  -19.907 1.00 30.83 ? 8   LYS A CB  1 
ATOM   59   C CG  . LYS A 1 8   ? 8.279   19.022  -21.200 1.00 34.88 ? 8   LYS A CG  1 
ATOM   60   C CD  . LYS A 1 8   ? 9.297   20.124  -20.930 1.00 48.77 ? 8   LYS A CD  1 
ATOM   61   C CE  . LYS A 1 8   ? 9.943   20.612  -22.218 1.00 61.36 ? 8   LYS A CE  1 
ATOM   62   N NZ  . LYS A 1 8   ? 10.608  19.491  -22.947 1.00 67.67 ? 8   LYS A NZ  1 
ATOM   63   N N   . ILE A 1 9   ? 6.001   16.937  -17.763 1.00 23.88 ? 9   ILE A N   1 
ATOM   64   C CA  . ILE A 1 9   ? 5.973   16.028  -16.619 1.00 24.49 ? 9   ILE A CA  1 
ATOM   65   C C   . ILE A 1 9   ? 5.162   14.777  -16.950 1.00 21.65 ? 9   ILE A C   1 
ATOM   66   O O   . ILE A 1 9   ? 5.590   13.648  -16.682 1.00 21.70 ? 9   ILE A O   1 
ATOM   67   C CB  . ILE A 1 9   ? 5.428   16.758  -15.381 1.00 25.51 ? 9   ILE A CB  1 
ATOM   68   C CG1 . ILE A 1 9   ? 6.430   17.840  -14.963 1.00 23.51 ? 9   ILE A CG1 1 
ATOM   69   C CG2 . ILE A 1 9   ? 5.158   15.758  -14.253 1.00 21.99 ? 9   ILE A CG2 1 
ATOM   70   C CD1 . ILE A 1 9   ? 5.882   18.881  -13.965 1.00 28.30 ? 9   ILE A CD1 1 
ATOM   71   N N   . GLY A 1 10  ? 3.984   14.955  -17.545 1.00 22.29 ? 10  GLY A N   1 
ATOM   72   C CA  . GLY A 1 10  ? 3.174   13.795  -17.909 1.00 23.22 ? 10  GLY A CA  1 
ATOM   73   C C   . GLY A 1 10  ? 3.876   12.875  -18.895 1.00 27.57 ? 10  GLY A C   1 
ATOM   74   O O   . GLY A 1 10  ? 3.771   11.646  -18.803 1.00 21.75 ? 10  GLY A O   1 
ATOM   75   N N   . ALA A 1 11  ? 4.610   13.455  -19.848 1.00 24.13 ? 11  ALA A N   1 
ATOM   76   C CA  . ALA A 1 11  ? 5.305   12.647  -20.849 1.00 27.14 ? 11  ALA A CA  1 
ATOM   77   C C   . ALA A 1 11  ? 6.375   11.767  -20.207 1.00 25.54 ? 11  ALA A C   1 
ATOM   78   O O   . ALA A 1 11  ? 6.579   10.621  -20.622 1.00 22.38 ? 11  ALA A O   1 
ATOM   79   C CB  . ALA A 1 11  ? 5.921   13.557  -21.918 1.00 27.65 ? 11  ALA A CB  1 
ATOM   80   N N   . ALA A 1 12  ? 7.069   12.293  -19.191 1.00 24.90 ? 12  ALA A N   1 
ATOM   81   C CA  . ALA A 1 12  ? 8.062   11.508  -18.465 1.00 28.59 ? 12  ALA A CA  1 
ATOM   82   C C   . ALA A 1 12  ? 7.408   10.370  -17.690 1.00 23.06 ? 12  ALA A C   1 
ATOM   83   O O   . ALA A 1 12  ? 7.911   9.237   -17.691 1.00 24.56 ? 12  ALA A O   1 
ATOM   84   C CB  . ALA A 1 12  ? 8.843   12.411  -17.511 1.00 21.03 ? 12  ALA A CB  1 
ATOM   85   N N   . ILE A 1 13  ? 6.287   10.651  -17.017 1.00 22.68 ? 13  ILE A N   1 
ATOM   86   C CA  . ILE A 1 13  ? 5.595   9.593   -16.279 1.00 20.33 ? 13  ILE A CA  1 
ATOM   87   C C   . ILE A 1 13  ? 5.140   8.492   -17.230 1.00 22.98 ? 13  ILE A C   1 
ATOM   88   O O   . ILE A 1 13  ? 5.293   7.298   -16.946 1.00 22.84 ? 13  ILE A O   1 
ATOM   89   C CB  . ILE A 1 13  ? 4.409   10.173  -15.485 1.00 22.75 ? 13  ILE A CB  1 
ATOM   90   C CG1 . ILE A 1 13  ? 4.907   11.172  -14.440 1.00 17.92 ? 13  ILE A CG1 1 
ATOM   91   C CG2 . ILE A 1 13  ? 3.629   9.037   -14.812 1.00 23.73 ? 13  ILE A CG2 1 
ATOM   92   C CD1 . ILE A 1 13  ? 3.788   12.064  -13.856 1.00 18.00 ? 13  ILE A CD1 1 
ATOM   93   N N   . ASP A 1 14  ? 4.548   8.878   -18.365 1.00 23.41 ? 14  ASP A N   1 
ATOM   94   C CA  . ASP A 1 14  ? 4.091   7.883   -19.335 1.00 21.16 ? 14  ASP A CA  1 
ATOM   95   C C   . ASP A 1 14  ? 5.250   7.044   -19.858 1.00 24.65 ? 14  ASP A C   1 
ATOM   96   O O   . ASP A 1 14  ? 5.090   5.840   -20.117 1.00 25.31 ? 14  ASP A O   1 
ATOM   97   C CB  . ASP A 1 14  ? 3.378   8.555   -20.511 1.00 20.31 ? 14  ASP A CB  1 
ATOM   98   C CG  . ASP A 1 14  ? 2.111   9.283   -20.098 1.00 33.22 ? 14  ASP A CG  1 
ATOM   99   O OD1 . ASP A 1 14  ? 1.554   8.966   -19.021 1.00 31.33 ? 14  ASP A OD1 1 
ATOM   100  O OD2 . ASP A 1 14  ? 1.669   10.178  -20.858 1.00 32.17 ? 14  ASP A OD2 1 
ATOM   101  N N   . ALA A 1 15  ? 6.419   7.662   -20.047 1.00 23.94 ? 15  ALA A N   1 
ATOM   102  C CA  . ALA A 1 15  ? 7.564   6.901   -20.532 1.00 27.22 ? 15  ALA A CA  1 
ATOM   103  C C   . ALA A 1 15  ? 7.912   5.767   -19.574 1.00 25.50 ? 15  ALA A C   1 
ATOM   104  O O   . ALA A 1 15  ? 8.175   4.643   -20.009 1.00 26.85 ? 15  ALA A O   1 
ATOM   105  C CB  . ALA A 1 15  ? 8.767   7.817   -20.748 1.00 25.87 ? 15  ALA A CB  1 
ATOM   106  N N   . GLY A 1 16  ? 7.903   6.040   -18.266 1.00 25.22 ? 16  GLY A N   1 
ATOM   107  C CA  . GLY A 1 16  ? 8.205   4.994   -17.305 1.00 22.67 ? 16  GLY A CA  1 
ATOM   108  C C   . GLY A 1 16  ? 7.135   3.921   -17.268 1.00 25.93 ? 16  GLY A C   1 
ATOM   109  O O   . GLY A 1 16  ? 7.439   2.725   -17.229 1.00 21.74 ? 16  GLY A O   1 
ATOM   110  N N   . ARG A 1 17  ? 5.868   4.334   -17.281 1.00 21.20 ? 17  ARG A N   1 
ATOM   111  C CA  . ARG A 1 17  ? 4.773   3.375   -17.315 1.00 19.15 ? 17  ARG A CA  1 
ATOM   112  C C   . ARG A 1 17  ? 4.822   2.520   -18.576 1.00 22.52 ? 17  ARG A C   1 
ATOM   113  O O   . ARG A 1 17  ? 4.604   1.302   -18.525 1.00 22.41 ? 17  ARG A O   1 
ATOM   114  C CB  . ARG A 1 17  ? 3.447   4.131   -17.226 1.00 23.80 ? 17  ARG A CB  1 
ATOM   115  C CG  . ARG A 1 17  ? 2.218   3.294   -17.490 1.00 26.94 ? 17  ARG A CG  1 
ATOM   116  C CD  . ARG A 1 17  ? 2.066   2.221   -16.447 1.00 26.16 ? 17  ARG A CD  1 
ATOM   117  N NE  . ARG A 1 17  ? 0.889   1.394   -16.697 1.00 31.10 ? 17  ARG A NE  1 
ATOM   118  C CZ  . ARG A 1 17  ? -0.216  1.407   -15.964 1.00 37.28 ? 17  ARG A CZ  1 
ATOM   119  N NH1 . ARG A 1 17  ? -0.346  2.214   -14.922 1.00 31.96 ? 17  ARG A NH1 1 
ATOM   120  N NH2 . ARG A 1 17  ? -1.210  0.571   -16.271 1.00 32.89 ? 17  ARG A NH2 1 
ATOM   121  N N   . LYS A 1 18  ? 5.101   3.140   -19.721 1.00 23.33 ? 18  LYS A N   1 
ATOM   122  C CA  . LYS A 1 18  ? 5.076   2.403   -20.979 1.00 26.38 ? 18  LYS A CA  1 
ATOM   123  C C   . LYS A 1 18  ? 6.259   1.455   -21.081 1.00 26.23 ? 18  LYS A C   1 
ATOM   124  O O   . LYS A 1 18  ? 6.135   0.360   -21.648 1.00 27.69 ? 18  LYS A O   1 
ATOM   125  C CB  . LYS A 1 18  ? 5.064   3.374   -22.161 1.00 27.29 ? 18  LYS A CB  1 
ATOM   126  C CG  . LYS A 1 18  ? 3.715   3.996   -22.449 1.00 30.52 ? 18  LYS A CG  1 
ATOM   127  C CD  . LYS A 1 18  ? 3.882   5.192   -23.396 1.00 39.23 ? 18  LYS A CD  1 
ATOM   128  C CE  . LYS A 1 18  ? 2.599   5.465   -24.145 1.00 42.73 ? 18  LYS A CE  1 
ATOM   129  N NZ  . LYS A 1 18  ? 1.946   4.179   -24.528 1.00 45.76 ? 18  LYS A NZ  1 
ATOM   130  N N   . TYR A 1 19  ? 7.423   1.866   -20.569 1.00 23.02 ? 19  TYR A N   1 
ATOM   131  C CA  . TYR A 1 19  ? 8.558   0.950   -20.490 1.00 22.87 ? 19  TYR A CA  1 
ATOM   132  C C   . TYR A 1 19  ? 8.206   -0.276  -19.650 1.00 25.19 ? 19  TYR A C   1 
ATOM   133  O O   . TYR A 1 19  ? 8.445   -1.420  -20.060 1.00 22.34 ? 19  TYR A O   1 
ATOM   134  C CB  . TYR A 1 19  ? 9.778   1.661   -19.910 1.00 22.86 ? 19  TYR A CB  1 
ATOM   135  C CG  . TYR A 1 19  ? 10.945  0.728   -19.656 1.00 27.05 ? 19  TYR A CG  1 
ATOM   136  C CD1 . TYR A 1 19  ? 11.784  0.337   -20.697 1.00 27.03 ? 19  TYR A CD1 1 
ATOM   137  C CD2 . TYR A 1 19  ? 11.208  0.239   -18.382 1.00 24.02 ? 19  TYR A CD2 1 
ATOM   138  C CE1 . TYR A 1 19  ? 12.852  -0.517  -20.476 1.00 27.52 ? 19  TYR A CE1 1 
ATOM   139  C CE2 . TYR A 1 19  ? 12.278  -0.611  -18.144 1.00 26.06 ? 19  TYR A CE2 1 
ATOM   140  C CZ  . TYR A 1 19  ? 13.095  -0.988  -19.197 1.00 27.29 ? 19  TYR A CZ  1 
ATOM   141  O OH  . TYR A 1 19  ? 14.156  -1.834  -18.974 1.00 28.31 ? 19  TYR A OH  1 
ATOM   142  N N   . LEU A 1 20  ? 7.638   -0.053  -18.461 1.00 21.65 ? 20  LEU A N   1 
ATOM   143  C CA  . LEU A 1 20  ? 7.262   -1.181  -17.616 1.00 21.66 ? 20  LEU A CA  1 
ATOM   144  C C   . LEU A 1 20  ? 6.256   -2.085  -18.311 1.00 23.93 ? 20  LEU A C   1 
ATOM   145  O O   . LEU A 1 20  ? 6.353   -3.316  -18.215 1.00 22.89 ? 20  LEU A O   1 
ATOM   146  C CB  . LEU A 1 20  ? 6.704   -0.690  -16.280 1.00 23.69 ? 20  LEU A CB  1 
ATOM   147  C CG  . LEU A 1 20  ? 7.756   -0.063  -15.370 1.00 22.35 ? 20  LEU A CG  1 
ATOM   148  C CD1 . LEU A 1 20  ? 7.106   0.500   -14.113 1.00 21.93 ? 20  LEU A CD1 1 
ATOM   149  C CD2 . LEU A 1 20  ? 8.812   -1.110  -15.024 1.00 19.84 ? 20  LEU A CD2 1 
ATOM   150  N N   . ASP A 1 21  ? 5.282   -1.502  -19.019 1.00 22.40 ? 21  ASP A N   1 
ATOM   151  C CA  . ASP A 1 21  ? 4.300   -2.337  -19.716 1.00 24.84 ? 21  ASP A CA  1 
ATOM   152  C C   . ASP A 1 21  ? 4.945   -3.145  -20.841 1.00 23.97 ? 21  ASP A C   1 
ATOM   153  O O   . ASP A 1 21  ? 4.519   -4.273  -21.124 1.00 22.96 ? 21  ASP A O   1 
ATOM   154  C CB  . ASP A 1 21  ? 3.159   -1.470  -20.262 1.00 26.71 ? 21  ASP A CB  1 
ATOM   155  C CG  . ASP A 1 21  ? 2.288   -0.886  -19.157 1.00 33.53 ? 21  ASP A CG  1 
ATOM   156  O OD1 . ASP A 1 21  ? 2.348   -1.395  -18.019 1.00 32.12 ? 21  ASP A OD1 1 
ATOM   157  O OD2 . ASP A 1 21  ? 1.538   0.080   -19.423 1.00 38.88 ? 21  ASP A OD2 1 
ATOM   158  N N   . ALA A 1 22  ? 5.962   -2.585  -21.501 1.00 24.44 ? 22  ALA A N   1 
ATOM   159  C CA  . ALA A 1 22  ? 6.661   -3.331  -22.544 1.00 27.96 ? 22  ALA A CA  1 
ATOM   160  C C   . ALA A 1 22  ? 7.490   -4.467  -21.954 1.00 26.04 ? 22  ALA A C   1 
ATOM   161  O O   . ALA A 1 22  ? 7.621   -5.529  -22.571 1.00 27.17 ? 22  ALA A O   1 
ATOM   162  C CB  . ALA A 1 22  ? 7.546   -2.392  -23.361 1.00 24.60 ? 22  ALA A CB  1 
ATOM   163  N N   . LYS A 1 23  ? 8.073   -4.256  -20.772 1.00 22.82 ? 23  LYS A N   1 
ATOM   164  C CA  . LYS A 1 23  ? 8.789   -5.337  -20.103 1.00 23.26 ? 23  LYS A CA  1 
ATOM   165  C C   . LYS A 1 23  ? 7.829   -6.444  -19.680 1.00 27.22 ? 23  LYS A C   1 
ATOM   166  O O   . LYS A 1 23  ? 8.179   -7.632  -19.719 1.00 22.39 ? 23  LYS A O   1 
ATOM   167  C CB  . LYS A 1 23  ? 9.562   -4.790  -18.902 1.00 21.81 ? 23  LYS A CB  1 
ATOM   168  C CG  . LYS A 1 23  ? 10.572  -3.705  -19.283 1.00 24.41 ? 23  LYS A CG  1 
ATOM   169  C CD  . LYS A 1 23  ? 11.561  -4.206  -20.340 1.00 25.90 ? 23  LYS A CD  1 
ATOM   170  C CE  . LYS A 1 23  ? 12.647  -5.054  -19.703 1.00 29.15 ? 23  LYS A CE  1 
ATOM   171  N NZ  . LYS A 1 23  ? 13.616  -5.602  -20.696 1.00 28.80 ? 23  LYS A NZ  1 
ATOM   172  N N   . ILE A 1 24  ? 6.610   -6.072  -19.286 1.00 23.88 ? 24  ILE A N   1 
ATOM   173  C CA  . ILE A 1 24  ? 5.593   -7.073  -18.958 1.00 23.57 ? 24  ILE A CA  1 
ATOM   174  C C   . ILE A 1 24  ? 5.213   -7.871  -20.201 1.00 24.96 ? 24  ILE A C   1 
ATOM   175  O O   . ILE A 1 24  ? 5.151   -9.105  -20.173 1.00 25.00 ? 24  ILE A O   1 
ATOM   176  C CB  . ILE A 1 24  ? 4.363   -6.393  -18.334 1.00 22.18 ? 24  ILE A CB  1 
ATOM   177  C CG1 . ILE A 1 24  ? 4.696   -5.930  -16.910 1.00 27.03 ? 24  ILE A CG1 1 
ATOM   178  C CG2 . ILE A 1 24  ? 3.170   -7.349  -18.339 1.00 27.79 ? 24  ILE A CG2 1 
ATOM   179  C CD1 . ILE A 1 24  ? 3.684   -4.961  -16.324 1.00 23.58 ? 24  ILE A CD1 1 
ATOM   180  N N   . GLU A 1 25  ? 4.941   -7.172  -21.309 1.00 26.29 ? 25  GLU A N   1 
ATOM   181  C CA  . GLU A 1 25  ? 4.595   -7.853  -22.555 1.00 31.75 ? 25  GLU A CA  1 
ATOM   182  C C   . GLU A 1 25  ? 5.726   -8.761  -23.021 1.00 29.60 ? 25  GLU A C   1 
ATOM   183  O O   . GLU A 1 25  ? 5.480   -9.842  -23.569 1.00 32.06 ? 25  GLU A O   1 
ATOM   184  C CB  . GLU A 1 25  ? 4.255   -6.825  -23.636 1.00 35.58 ? 25  GLU A CB  1 
ATOM   185  C CG  . GLU A 1 25  ? 2.920   -6.114  -23.425 1.00 41.90 ? 25  GLU A CG  1 
ATOM   186  C CD  . GLU A 1 25  ? 1.761   -7.095  -23.287 1.00 51.59 ? 25  GLU A CD  1 
ATOM   187  O OE1 . GLU A 1 25  ? 0.966   -6.953  -22.330 1.00 48.57 ? 25  GLU A OE1 1 
ATOM   188  O OE2 . GLU A 1 25  ? 1.659   -8.018  -24.127 1.00 57.58 ? 25  GLU A OE2 1 
ATOM   189  N N   . GLU A 1 26  ? 6.971   -8.330  -22.824 1.00 26.32 ? 26  GLU A N   1 
ATOM   190  C CA  . GLU A 1 26  ? 8.119   -9.156  -23.190 1.00 26.55 ? 26  GLU A CA  1 
ATOM   191  C C   . GLU A 1 26  ? 8.170   -10.425 -22.351 1.00 28.21 ? 26  GLU A C   1 
ATOM   192  O O   . GLU A 1 26  ? 8.418   -11.519 -22.876 1.00 26.00 ? 26  GLU A O   1 
ATOM   193  C CB  . GLU A 1 26  ? 9.410   -8.350  -23.025 1.00 24.88 ? 26  GLU A CB  1 
ATOM   194  C CG  . GLU A 1 26  ? 10.687  -9.172  -23.182 1.00 28.88 ? 26  GLU A CG  1 
ATOM   195  C CD  . GLU A 1 26  ? 11.892  -8.501  -22.539 1.00 36.25 ? 26  GLU A CD  1 
ATOM   196  O OE1 . GLU A 1 26  ? 12.974  -9.124  -22.483 1.00 38.39 ? 26  GLU A OE1 1 
ATOM   197  O OE2 . GLU A 1 26  ? 11.759  -7.346  -22.081 1.00 39.05 ? 26  GLU A OE2 1 
ATOM   198  N N   . ALA A 1 27  ? 7.956   -10.297 -21.039 1.00 26.34 ? 27  ALA A N   1 
ATOM   199  C CA  . ALA A 1 27  ? 7.916   -11.480 -20.186 1.00 22.94 ? 27  ALA A CA  1 
ATOM   200  C C   . ALA A 1 27  ? 6.780   -12.405 -20.589 1.00 29.67 ? 27  ALA A C   1 
ATOM   201  O O   . ALA A 1 27  ? 6.929   -13.634 -20.527 1.00 32.25 ? 27  ALA A O   1 
ATOM   202  C CB  . ALA A 1 27  ? 7.785   -11.079 -18.714 1.00 24.47 ? 27  ALA A CB  1 
ATOM   203  N N   . LYS A 1 28  ? 5.645   -11.837 -21.017 1.00 26.76 ? 28  LYS A N   1 
ATOM   204  C CA  . LYS A 1 28  ? 4.528   -12.661 -21.468 1.00 31.81 ? 28  LYS A CA  1 
ATOM   205  C C   . LYS A 1 28  ? 4.857   -13.381 -22.774 1.00 33.59 ? 28  LYS A C   1 
ATOM   206  O O   . LYS A 1 28  ? 4.556   -14.570 -22.918 1.00 30.32 ? 28  LYS A O   1 
ATOM   207  C CB  . LYS A 1 28  ? 3.269   -11.805 -21.618 1.00 32.94 ? 28  LYS A CB  1 
ATOM   208  C CG  . LYS A 1 28  ? 2.546   -11.594 -20.298 1.00 34.25 ? 28  LYS A CG  1 
ATOM   209  C CD  . LYS A 1 28  ? 1.543   -10.466 -20.363 1.00 41.13 ? 28  LYS A CD  1 
ATOM   210  C CE  . LYS A 1 28  ? 0.403   -10.780 -21.307 1.00 45.17 ? 28  LYS A CE  1 
ATOM   211  N NZ  . LYS A 1 28  ? -0.230  -9.507  -21.789 1.00 55.57 ? 28  LYS A NZ  1 
ATOM   212  N N   . LYS A 1 29  ? 5.481   -12.682 -23.730 1.00 31.18 ? 29  LYS A N   1 
ATOM   213  C CA  . LYS A 1 29  ? 5.806   -13.300 -25.014 1.00 36.63 ? 29  LYS A CA  1 
ATOM   214  C C   . LYS A 1 29  ? 6.836   -14.415 -24.875 1.00 35.92 ? 29  LYS A C   1 
ATOM   215  O O   . LYS A 1 29  ? 6.776   -15.399 -25.619 1.00 38.41 ? 29  LYS A O   1 
ATOM   216  C CB  . LYS A 1 29  ? 6.300   -12.242 -26.003 1.00 31.74 ? 29  LYS A CB  1 
ATOM   217  C CG  . LYS A 1 29  ? 5.171   -11.452 -26.622 1.00 40.67 ? 29  LYS A CG  1 
ATOM   218  C CD  . LYS A 1 29  ? 5.666   -10.272 -27.438 1.00 41.79 ? 29  LYS A CD  1 
ATOM   219  C CE  . LYS A 1 29  ? 4.501   -9.365  -27.793 1.00 50.66 ? 29  LYS A CE  1 
ATOM   220  N NZ  . LYS A 1 29  ? 4.928   -8.217  -28.637 1.00 57.10 ? 29  LYS A NZ  1 
ATOM   221  N N   . THR A 1 30  ? 7.788   -14.280 -23.949 1.00 33.89 ? 30  THR A N   1 
ATOM   222  C CA  . THR A 1 30  ? 8.757   -15.335 -23.668 1.00 34.42 ? 30  THR A CA  1 
ATOM   223  C C   . THR A 1 30  ? 8.249   -16.346 -22.647 1.00 35.71 ? 30  THR A C   1 
ATOM   224  O O   . THR A 1 30  ? 8.990   -17.269 -22.283 1.00 35.01 ? 30  THR A O   1 
ATOM   225  C CB  . THR A 1 30  ? 10.074  -14.734 -23.173 1.00 35.44 ? 30  THR A CB  1 
ATOM   226  O OG1 . THR A 1 30  ? 9.851   -14.076 -21.922 1.00 32.77 ? 30  THR A OG1 1 
ATOM   227  C CG2 . THR A 1 30  ? 10.607  -13.716 -24.172 1.00 33.60 ? 30  THR A CG2 1 
ATOM   228  N N   . LEU A 1 31  ? 7.012   -16.187 -22.171 1.00 34.33 ? 31  LEU A N   1 
ATOM   229  C CA  . LEU A 1 31  ? 6.395   -17.132 -21.245 1.00 32.55 ? 31  LEU A CA  1 
ATOM   230  C C   . LEU A 1 31  ? 7.139   -17.208 -19.912 1.00 32.87 ? 31  LEU A C   1 
ATOM   231  O O   . LEU A 1 31  ? 7.123   -18.241 -19.241 1.00 33.40 ? 31  LEU A O   1 
ATOM   232  C CB  . LEU A 1 31  ? 6.292   -18.525 -21.876 1.00 37.34 ? 31  LEU A CB  1 
ATOM   233  C CG  . LEU A 1 31  ? 5.046   -19.330 -21.544 1.00 40.47 ? 31  LEU A CG  1 
ATOM   234  C CD1 . LEU A 1 31  ? 3.801   -18.650 -22.092 1.00 40.92 ? 31  LEU A CD1 1 
ATOM   235  C CD2 . LEU A 1 31  ? 5.204   -20.700 -22.128 1.00 49.05 ? 31  LEU A CD2 1 
ATOM   236  N N   . THR A 1 32  ? 7.819   -16.134 -19.507 1.00 32.59 ? 32  THR A N   1 
ATOM   237  C CA  . THR A 1 32  ? 8.381   -16.080 -18.157 1.00 32.44 ? 32  THR A CA  1 
ATOM   238  C C   . THR A 1 32  ? 7.353   -15.367 -17.280 1.00 30.11 ? 32  THR A C   1 
ATOM   239  O O   . THR A 1 32  ? 7.474   -14.190 -16.924 1.00 26.30 ? 32  THR A O   1 
ATOM   240  C CB  . THR A 1 32  ? 9.751   -15.409 -18.147 1.00 31.91 ? 32  THR A CB  1 
ATOM   241  O OG1 . THR A 1 32  ? 10.138  -15.140 -16.795 1.00 41.44 ? 32  THR A OG1 1 
ATOM   242  C CG2 . THR A 1 32  ? 9.744   -14.125 -18.928 1.00 30.07 ? 32  THR A CG2 1 
ATOM   243  N N   . LEU A 1 33  ? 6.298   -16.113 -16.948 1.00 28.49 ? 33  LEU A N   1 
ATOM   244  C CA  . LEU A 1 33  ? 5.128   -15.495 -16.336 1.00 28.71 ? 33  LEU A CA  1 
ATOM   245  C C   . LEU A 1 33  ? 5.386   -15.080 -14.891 1.00 23.78 ? 33  LEU A C   1 
ATOM   246  O O   . LEU A 1 33  ? 4.807   -14.098 -14.425 1.00 21.62 ? 33  LEU A O   1 
ATOM   247  C CB  . LEU A 1 33  ? 3.934   -16.442 -16.434 1.00 25.72 ? 33  LEU A CB  1 
ATOM   248  C CG  . LEU A 1 33  ? 3.519   -16.726 -17.885 1.00 29.00 ? 33  LEU A CG  1 
ATOM   249  C CD1 . LEU A 1 33  ? 2.267   -17.612 -17.944 1.00 33.28 ? 33  LEU A CD1 1 
ATOM   250  C CD2 . LEU A 1 33  ? 3.295   -15.430 -18.659 1.00 31.37 ? 33  LEU A CD2 1 
ATOM   251  N N   . ARG A 1 34  ? 6.253   -15.793 -14.173 1.00 24.35 ? 34  ARG A N   1 
ATOM   252  C CA  . ARG A 1 34  ? 6.565   -15.372 -12.811 1.00 28.75 ? 34  ARG A CA  1 
ATOM   253  C C   . ARG A 1 34  ? 7.283   -14.028 -12.804 1.00 25.84 ? 34  ARG A C   1 
ATOM   254  O O   . ARG A 1 34  ? 7.060   -13.215 -11.900 1.00 26.04 ? 34  ARG A O   1 
ATOM   255  C CB  . ARG A 1 34  ? 7.387   -16.454 -12.100 1.00 29.20 ? 34  ARG A CB  1 
ATOM   256  C CG  . ARG A 1 34  ? 6.555   -17.709 -11.798 1.00 24.81 ? 34  ARG A CG  1 
ATOM   257  C CD  . ARG A 1 34  ? 7.371   -18.830 -11.155 1.00 30.25 ? 34  ARG A CD  1 
ATOM   258  N NE  . ARG A 1 34  ? 6.543   -20.008 -10.917 1.00 31.18 ? 34  ARG A NE  1 
ATOM   259  C CZ  . ARG A 1 34  ? 6.933   -21.081 -10.241 1.00 35.17 ? 34  ARG A CZ  1 
ATOM   260  N NH1 . ARG A 1 34  ? 8.144   -21.168 -9.718  1.00 28.02 ? 34  ARG A NH1 1 
ATOM   261  N NH2 . ARG A 1 34  ? 6.083   -22.092 -10.082 1.00 27.36 ? 34  ARG A NH2 1 
ATOM   262  N N   . THR A 1 35  ? 8.097   -13.754 -13.828 1.00 23.57 ? 35  THR A N   1 
ATOM   263  C CA  . THR A 1 35  ? 8.700   -12.428 -13.972 1.00 23.99 ? 35  THR A CA  1 
ATOM   264  C C   . THR A 1 35  ? 7.659   -11.368 -14.337 1.00 23.05 ? 35  THR A C   1 
ATOM   265  O O   . THR A 1 35  ? 7.735   -10.216 -13.872 1.00 22.53 ? 35  THR A O   1 
ATOM   266  C CB  . THR A 1 35  ? 9.801   -12.485 -15.035 1.00 28.18 ? 35  THR A CB  1 
ATOM   267  O OG1 . THR A 1 35  ? 10.772  -13.472 -14.663 1.00 28.85 ? 35  THR A OG1 1 
ATOM   268  C CG2 . THR A 1 35  ? 10.490  -11.142 -15.174 1.00 27.22 ? 35  THR A CG2 1 
ATOM   269  N N   . ALA A 1 36  ? 6.709   -11.718 -15.206 1.00 20.57 ? 36  ALA A N   1 
ATOM   270  C CA  . ALA A 1 36  ? 5.616   -10.805 -15.521 1.00 21.34 ? 36  ALA A CA  1 
ATOM   271  C C   . ALA A 1 36  ? 4.838   -10.428 -14.265 1.00 20.76 ? 36  ALA A C   1 
ATOM   272  O O   . ALA A 1 36  ? 4.416   -9.273  -14.109 1.00 20.13 ? 36  ALA A O   1 
ATOM   273  C CB  . ALA A 1 36  ? 4.678   -11.435 -16.556 1.00 19.38 ? 36  ALA A CB  1 
ATOM   274  N N   . GLN A 1 37  ? 4.632   -11.393 -13.360 1.00 21.53 ? 37  GLN A N   1 
ATOM   275  C CA  . GLN A 1 37  ? 3.929   -11.112 -12.108 1.00 21.29 ? 37  GLN A CA  1 
ATOM   276  C C   . GLN A 1 37  ? 4.731   -10.155 -11.228 1.00 21.42 ? 37  GLN A C   1 
ATOM   277  O O   . GLN A 1 37  ? 4.172   -9.218  -10.641 1.00 20.83 ? 37  GLN A O   1 
ATOM   278  C CB  . GLN A 1 37  ? 3.652   -12.425 -11.364 1.00 24.85 ? 37  GLN A CB  1 
ATOM   279  C CG  . GLN A 1 37  ? 2.722   -13.391 -12.098 1.00 26.01 ? 37  GLN A CG  1 
ATOM   280  C CD  . GLN A 1 37  ? 1.256   -12.993 -11.993 1.00 26.12 ? 37  GLN A CD  1 
ATOM   281  O OE1 . GLN A 1 37  ? 0.875   -11.860 -12.289 1.00 29.60 ? 37  GLN A OE1 1 
ATOM   282  N NE2 . GLN A 1 37  ? 0.431   -13.927 -11.560 1.00 27.76 ? 37  GLN A NE2 1 
ATOM   283  N N   . ALA A 1 38  ? 6.048   -10.370 -11.133 1.00 20.21 ? 38  ALA A N   1 
ATOM   284  C CA  . ALA A 1 38  ? 6.894   -9.467  -10.352 1.00 18.85 ? 38  ALA A CA  1 
ATOM   285  C C   . ALA A 1 38  ? 6.863   -8.057  -10.928 1.00 19.86 ? 38  ALA A C   1 
ATOM   286  O O   . ALA A 1 38  ? 6.852   -7.069  -10.187 1.00 19.05 ? 38  ALA A O   1 
ATOM   287  C CB  . ALA A 1 38  ? 8.334   -9.995  -10.305 1.00 19.10 ? 38  ALA A CB  1 
ATOM   288  N N   . LEU A 1 39  ? 6.834   -7.945  -12.253 1.00 19.30 ? 39  LEU A N   1 
ATOM   289  C CA  . LEU A 1 39  ? 6.811   -6.631  -12.887 1.00 18.76 ? 39  LEU A CA  1 
ATOM   290  C C   . LEU A 1 39  ? 5.494   -5.889  -12.639 1.00 20.04 ? 39  LEU A C   1 
ATOM   291  O O   . LEU A 1 39  ? 5.486   -4.657  -12.548 1.00 21.62 ? 39  LEU A O   1 
ATOM   292  C CB  . LEU A 1 39  ? 7.077   -6.805  -14.376 1.00 18.76 ? 39  LEU A CB  1 
ATOM   293  C CG  . LEU A 1 39  ? 8.527   -7.175  -14.710 1.00 24.16 ? 39  LEU A CG  1 
ATOM   294  C CD1 . LEU A 1 39  ? 8.622   -7.624  -16.158 1.00 22.46 ? 39  LEU A CD1 1 
ATOM   295  C CD2 . LEU A 1 39  ? 9.440   -5.964  -14.464 1.00 25.62 ? 39  LEU A CD2 1 
ATOM   296  N N   . LEU A 1 40  ? 4.372   -6.611  -12.543 1.00 19.98 ? 40  LEU A N   1 
ATOM   297  C CA  . LEU A 1 40  ? 3.121   -5.977  -12.132 1.00 19.51 ? 40  LEU A CA  1 
ATOM   298  C C   . LEU A 1 40  ? 3.257   -5.322  -10.768 1.00 19.34 ? 40  LEU A C   1 
ATOM   299  O O   . LEU A 1 40  ? 2.741   -4.216  -10.545 1.00 17.41 ? 40  LEU A O   1 
ATOM   300  C CB  . LEU A 1 40  ? 1.981   -6.998  -12.085 1.00 23.48 ? 40  LEU A CB  1 
ATOM   301  C CG  . LEU A 1 40  ? 1.394   -7.523  -13.386 1.00 32.01 ? 40  LEU A CG  1 
ATOM   302  C CD1 . LEU A 1 40  ? 0.214   -8.419  -13.048 1.00 36.43 ? 40  LEU A CD1 1 
ATOM   303  C CD2 . LEU A 1 40  ? 0.961   -6.380  -14.294 1.00 27.75 ? 40  LEU A CD2 1 
ATOM   304  N N   . VAL A 1 41  ? 3.922   -5.999  -9.828  1.00 16.89 ? 41  VAL A N   1 
ATOM   305  C CA  . VAL A 1 41  ? 4.088   -5.423  -8.495  1.00 14.09 ? 41  VAL A CA  1 
ATOM   306  C C   . VAL A 1 41  ? 4.960   -4.181  -8.565  1.00 18.73 ? 41  VAL A C   1 
ATOM   307  O O   . VAL A 1 41  ? 4.657   -3.149  -7.949  1.00 18.27 ? 41  VAL A O   1 
ATOM   308  C CB  . VAL A 1 41  ? 4.680   -6.455  -7.517  1.00 17.98 ? 41  VAL A CB  1 
ATOM   309  C CG1 . VAL A 1 41  ? 4.755   -5.836  -6.131  1.00 18.70 ? 41  VAL A CG1 1 
ATOM   310  C CG2 . VAL A 1 41  ? 3.833   -7.726  -7.485  1.00 20.53 ? 41  VAL A CG2 1 
ATOM   311  N N   . ILE A 1 42  ? 6.076   -4.274  -9.288  1.00 18.98 ? 42  ILE A N   1 
ATOM   312  C CA  . ILE A 1 42  ? 6.978   -3.134  -9.421  1.00 18.40 ? 42  ILE A CA  1 
ATOM   313  C C   . ILE A 1 42  ? 6.252   -1.961  -10.064 1.00 19.97 ? 42  ILE A C   1 
ATOM   314  O O   . ILE A 1 42  ? 6.415   -0.800  -9.655  1.00 19.02 ? 42  ILE A O   1 
ATOM   315  C CB  . ILE A 1 42  ? 8.219   -3.556  -10.230 1.00 21.11 ? 42  ILE A CB  1 
ATOM   316  C CG1 . ILE A 1 42  ? 9.042   -4.569  -9.420  1.00 18.86 ? 42  ILE A CG1 1 
ATOM   317  C CG2 . ILE A 1 42  ? 9.028   -2.316  -10.681 1.00 21.18 ? 42  ILE A CG2 1 
ATOM   318  C CD1 . ILE A 1 42  ? 9.936   -5.502  -10.251 1.00 19.83 ? 42  ILE A CD1 1 
ATOM   319  N N   . ARG A 1 43  ? 5.420   -2.245  -11.066 1.00 19.49 ? 43  ARG A N   1 
ATOM   320  C CA  . ARG A 1 43  ? 4.655   -1.173  -11.699 1.00 18.72 ? 43  ARG A CA  1 
ATOM   321  C C   . ARG A 1 43  ? 3.742   -0.478  -10.696 1.00 18.60 ? 43  ARG A C   1 
ATOM   322  O O   . ARG A 1 43  ? 3.626   0.749   -10.709 1.00 17.23 ? 43  ARG A O   1 
ATOM   323  C CB  . ARG A 1 43  ? 3.832   -1.709  -12.863 1.00 21.75 ? 43  ARG A CB  1 
ATOM   324  C CG  . ARG A 1 43  ? 3.178   -0.601  -13.691 1.00 20.24 ? 43  ARG A CG  1 
ATOM   325  C CD  . ARG A 1 43  ? 2.377   -1.177  -14.831 1.00 25.65 ? 43  ARG A CD  1 
ATOM   326  N NE  . ARG A 1 43  ? 1.173   -1.845  -14.349 1.00 30.53 ? 43  ARG A NE  1 
ATOM   327  C CZ  . ARG A 1 43  ? 0.343   -2.545  -15.115 1.00 34.28 ? 43  ARG A CZ  1 
ATOM   328  N NH1 . ARG A 1 43  ? 0.580   -2.726  -16.403 1.00 29.27 ? 43  ARG A NH1 1 
ATOM   329  N NH2 . ARG A 1 43  ? -0.755  -3.070  -14.574 1.00 31.64 ? 43  ARG A NH2 1 
ATOM   330  N N   . SER A 1 44  ? 3.103   -1.244  -9.801  1.00 18.29 ? 44  SER A N   1 
ATOM   331  C CA  . SER A 1 44  ? 2.192   -0.625  -8.834  1.00 18.36 ? 44  SER A CA  1 
ATOM   332  C C   . SER A 1 44  ? 2.940   0.299   -7.881  1.00 20.27 ? 44  SER A C   1 
ATOM   333  O O   . SER A 1 44  ? 2.413   1.348   -7.471  1.00 13.84 ? 44  SER A O   1 
ATOM   334  C CB  . SER A 1 44  ? 1.425   -1.694  -8.051  1.00 20.81 ? 44  SER A CB  1 
ATOM   335  O OG  . SER A 1 44  ? 2.279   -2.465  -7.209  1.00 18.47 ? 44  SER A OG  1 
ATOM   336  N N   . GLN A 1 45  ? 4.170   -0.071  -7.510  1.00 17.07 ? 45  GLN A N   1 
ATOM   337  C CA  . GLN A 1 45  ? 4.930   0.778   -6.599  1.00 20.81 ? 45  GLN A CA  1 
ATOM   338  C C   . GLN A 1 45  ? 5.504   2.000   -7.314  1.00 20.68 ? 45  GLN A C   1 
ATOM   339  O O   . GLN A 1 45  ? 5.599   3.079   -6.717  1.00 19.70 ? 45  GLN A O   1 
ATOM   340  C CB  . GLN A 1 45  ? 6.034   -0.033  -5.914  1.00 22.35 ? 45  GLN A CB  1 
ATOM   341  C CG  . GLN A 1 45  ? 6.959   0.815   -5.028  1.00 21.28 ? 45  GLN A CG  1 
ATOM   342  C CD  . GLN A 1 45  ? 6.213   1.582   -3.941  1.00 26.26 ? 45  GLN A CD  1 
ATOM   343  O OE1 . GLN A 1 45  ? 5.134   1.170   -3.503  1.00 23.80 ? 45  GLN A OE1 1 
ATOM   344  N NE2 . GLN A 1 45  ? 6.785   2.711   -3.503  1.00 28.00 ? 45  GLN A NE2 1 
ATOM   345  N N   . TYR A 1 46  ? 5.896   1.849   -8.585  1.00 17.91 ? 46  TYR A N   1 
ATOM   346  C CA  . TYR A 1 46  ? 6.231   3.006   -9.412  1.00 14.97 ? 46  TYR A CA  1 
ATOM   347  C C   . TYR A 1 46  ? 5.088   4.018   -9.431  1.00 19.25 ? 46  TYR A C   1 
ATOM   348  O O   . TYR A 1 46  ? 5.299   5.225   -9.233  1.00 18.24 ? 46  TYR A O   1 
ATOM   349  C CB  . TYR A 1 46  ? 6.575   2.541   -10.829 1.00 18.79 ? 46  TYR A CB  1 
ATOM   350  C CG  . TYR A 1 46  ? 6.665   3.657   -11.853 1.00 18.16 ? 46  TYR A CG  1 
ATOM   351  C CD1 . TYR A 1 46  ? 7.781   4.488   -11.904 1.00 19.80 ? 46  TYR A CD1 1 
ATOM   352  C CD2 . TYR A 1 46  ? 5.631   3.884   -12.759 1.00 18.28 ? 46  TYR A CD2 1 
ATOM   353  C CE1 . TYR A 1 46  ? 7.870   5.516   -12.852 1.00 23.26 ? 46  TYR A CE1 1 
ATOM   354  C CE2 . TYR A 1 46  ? 5.707   4.906   -13.711 1.00 18.82 ? 46  TYR A CE2 1 
ATOM   355  C CZ  . TYR A 1 46  ? 6.833   5.716   -13.748 1.00 21.04 ? 46  TYR A CZ  1 
ATOM   356  O OH  . TYR A 1 46  ? 6.918   6.724   -14.687 1.00 21.11 ? 46  TYR A OH  1 
ATOM   357  N N   . GLU A 1 47  ? 3.857   3.542   -9.649  1.00 16.16 ? 47  GLU A N   1 
ATOM   358  C CA  . GLU A 1 47  ? 2.717   4.456   -9.683  1.00 16.50 ? 47  GLU A CA  1 
ATOM   359  C C   . GLU A 1 47  ? 2.556   5.187   -8.354  1.00 17.85 ? 47  GLU A C   1 
ATOM   360  O O   . GLU A 1 47  ? 2.320   6.401   -8.331  1.00 20.56 ? 47  GLU A O   1 
ATOM   361  C CB  . GLU A 1 47  ? 1.440   3.698   -10.053 1.00 19.33 ? 47  GLU A CB  1 
ATOM   362  C CG  . GLU A 1 47  ? 1.440   3.147   -11.481 1.00 19.51 ? 47  GLU A CG  1 
ATOM   363  C CD  . GLU A 1 47  ? 0.985   4.182   -12.509 1.00 32.62 ? 47  GLU A CD  1 
ATOM   364  O OE1 . GLU A 1 47  ? -0.011  4.905   -12.245 1.00 29.47 ? 47  GLU A OE1 1 
ATOM   365  O OE2 . GLU A 1 47  ? 1.641   4.296   -13.572 1.00 29.73 ? 47  GLU A OE2 1 
ATOM   366  N N   . ARG A 1 48  ? 2.701   4.469   -7.235  1.00 15.40 ? 48  ARG A N   1 
ATOM   367  C CA  . ARG A 1 48  ? 2.611   5.108   -5.924  1.00 14.97 ? 48  ARG A CA  1 
ATOM   368  C C   . ARG A 1 48  ? 3.728   6.126   -5.725  1.00 17.25 ? 48  ARG A C   1 
ATOM   369  O O   . ARG A 1 48  ? 3.500   7.215   -5.189  1.00 18.10 ? 48  ARG A O   1 
ATOM   370  C CB  . ARG A 1 48  ? 2.661   4.051   -4.819  1.00 19.82 ? 48  ARG A CB  1 
ATOM   371  C CG  . ARG A 1 48  ? 2.664   4.635   -3.394  1.00 19.89 ? 48  ARG A CG  1 
ATOM   372  C CD  . ARG A 1 48  ? 2.784   3.507   -2.346  1.00 22.31 ? 48  ARG A CD  1 
ATOM   373  N NE  . ARG A 1 48  ? 2.716   3.996   -0.969  1.00 21.62 ? 48  ARG A NE  1 
ATOM   374  C CZ  . ARG A 1 48  ? 1.626   3.960   -0.217  1.00 28.41 ? 48  ARG A CZ  1 
ATOM   375  N NH1 . ARG A 1 48  ? 0.479   3.487   -0.683  1.00 24.60 ? 48  ARG A NH1 1 
ATOM   376  N NH2 . ARG A 1 48  ? 1.690   4.394   1.042   1.00 30.73 ? 48  ARG A NH2 1 
ATOM   377  N N   . ALA A 1 49  ? 4.949   5.777   -6.128  1.00 17.98 ? 49  ALA A N   1 
ATOM   378  C CA  . ALA A 1 49  ? 6.077   6.693   -5.970  1.00 18.69 ? 49  ALA A CA  1 
ATOM   379  C C   . ALA A 1 49  ? 5.898   7.950   -6.813  1.00 20.03 ? 49  ALA A C   1 
ATOM   380  O O   . ALA A 1 49  ? 6.302   9.047   -6.404  1.00 20.30 ? 49  ALA A O   1 
ATOM   381  C CB  . ALA A 1 49  ? 7.375   5.982   -6.341  1.00 19.04 ? 49  ALA A CB  1 
ATOM   382  N N   . VAL A 1 50  ? 5.314   7.813   -8.004  1.00 16.24 ? 50  VAL A N   1 
ATOM   383  C CA  . VAL A 1 50  ? 5.020   8.996   -8.817  1.00 15.39 ? 50  VAL A CA  1 
ATOM   384  C C   . VAL A 1 50  ? 3.923   9.841   -8.165  1.00 21.03 ? 50  VAL A C   1 
ATOM   385  O O   . VAL A 1 50  ? 4.033   11.074  -8.097  1.00 20.73 ? 50  VAL A O   1 
ATOM   386  C CB  . VAL A 1 50  ? 4.634   8.585   -10.250 1.00 16.85 ? 50  VAL A CB  1 
ATOM   387  C CG1 . VAL A 1 50  ? 4.116   9.801   -11.037 1.00 20.96 ? 50  VAL A CG1 1 
ATOM   388  C CG2 . VAL A 1 50  ? 5.843   7.942   -10.978 1.00 19.68 ? 50  VAL A CG2 1 
ATOM   389  N N   . ASP A 1 51  ? 2.847   9.191   -7.692  1.00 21.10 ? 51  ASP A N   1 
ATOM   390  C CA  . ASP A 1 51  ? 1.768   9.888   -6.985  1.00 19.25 ? 51  ASP A CA  1 
ATOM   391  C C   . ASP A 1 51  ? 2.325   10.814  -5.918  1.00 20.86 ? 51  ASP A C   1 
ATOM   392  O O   . ASP A 1 51  ? 1.878   11.953  -5.760  1.00 18.95 ? 51  ASP A O   1 
ATOM   393  C CB  . ASP A 1 51  ? 0.832   8.907   -6.279  1.00 19.20 ? 51  ASP A CB  1 
ATOM   394  C CG  . ASP A 1 51  ? -0.038  8.077   -7.213  1.00 25.25 ? 51  ASP A CG  1 
ATOM   395  O OD1 . ASP A 1 51  ? -0.140  8.358   -8.428  1.00 22.99 ? 51  ASP A OD1 1 
ATOM   396  O OD2 . ASP A 1 51  ? -0.647  7.111   -6.682  1.00 24.94 ? 51  ASP A OD2 1 
ATOM   397  N N   . THR A 1 52  ? 3.287   10.314  -5.146  1.00 18.24 ? 52  THR A N   1 
ATOM   398  C CA  . THR A 1 52  ? 3.712   11.019  -3.946  1.00 21.30 ? 52  THR A CA  1 
ATOM   399  C C   . THR A 1 52  ? 4.457   12.308  -4.278  1.00 20.80 ? 52  THR A C   1 
ATOM   400  O O   . THR A 1 52  ? 4.466   13.244  -3.469  1.00 23.97 ? 52  THR A O   1 
ATOM   401  C CB  . THR A 1 52  ? 4.577   10.084  -3.096  1.00 24.88 ? 52  THR A CB  1 
ATOM   402  O OG1 . THR A 1 52  ? 3.894   8.827   -2.925  1.00 29.79 ? 52  THR A OG1 1 
ATOM   403  C CG2 . THR A 1 52  ? 4.778   10.670  -1.745  1.00 29.71 ? 52  THR A CG2 1 
ATOM   404  N N   . LEU A 1 53  ? 5.077   12.383  -5.457  1.00 20.59 ? 53  LEU A N   1 
ATOM   405  C CA  . LEU A 1 53  ? 5.685   13.642  -5.897  1.00 22.23 ? 53  LEU A CA  1 
ATOM   406  C C   . LEU A 1 53  ? 4.682   14.788  -5.919  1.00 28.37 ? 53  LEU A C   1 
ATOM   407  O O   . LEU A 1 53  ? 5.068   15.962  -5.788  1.00 24.22 ? 53  LEU A O   1 
ATOM   408  C CB  . LEU A 1 53  ? 6.292   13.475  -7.290  1.00 25.95 ? 53  LEU A CB  1 
ATOM   409  C CG  . LEU A 1 53  ? 7.568   12.640  -7.349  1.00 25.45 ? 53  LEU A CG  1 
ATOM   410  C CD1 . LEU A 1 53  ? 7.993   12.447  -8.787  1.00 27.65 ? 53  LEU A CD1 1 
ATOM   411  C CD2 . LEU A 1 53  ? 8.649   13.346  -6.574  1.00 29.74 ? 53  LEU A CD2 1 
ATOM   412  N N   . PHE A 1 54  ? 3.403   14.475  -6.107  1.00 23.34 ? 54  PHE A N   1 
ATOM   413  C CA  . PHE A 1 54  ? 2.346   15.474  -6.173  1.00 23.03 ? 54  PHE A CA  1 
ATOM   414  C C   . PHE A 1 54  ? 1.489   15.532  -4.920  1.00 29.10 ? 54  PHE A C   1 
ATOM   415  O O   . PHE A 1 54  ? 1.032   16.612  -4.559  1.00 31.27 ? 54  PHE A O   1 
ATOM   416  C CB  . PHE A 1 54  ? 1.453   15.207  -7.399  1.00 22.63 ? 54  PHE A CB  1 
ATOM   417  C CG  . PHE A 1 54  ? 2.240   15.073  -8.667  1.00 24.79 ? 54  PHE A CG  1 
ATOM   418  C CD1 . PHE A 1 54  ? 2.679   16.204  -9.345  1.00 21.46 ? 54  PHE A CD1 1 
ATOM   419  C CD2 . PHE A 1 54  ? 2.617   13.831  -9.138  1.00 21.48 ? 54  PHE A CD2 1 
ATOM   420  C CE1 . PHE A 1 54  ? 3.455   16.092  -10.487 1.00 20.78 ? 54  PHE A CE1 1 
ATOM   421  C CE2 . PHE A 1 54  ? 3.385   13.719  -10.282 1.00 21.73 ? 54  PHE A CE2 1 
ATOM   422  C CZ  . PHE A 1 54  ? 3.809   14.856  -10.951 1.00 23.53 ? 54  PHE A CZ  1 
ATOM   423  N N   . THR A 1 55  ? 1.261   14.405  -4.238  1.00 27.04 ? 55  THR A N   1 
ATOM   424  C CA  . THR A 1 55  ? 0.382   14.424  -3.075  1.00 27.02 ? 55  THR A CA  1 
ATOM   425  C C   . THR A 1 55  ? 1.117   14.703  -1.776  1.00 26.66 ? 55  THR A C   1 
ATOM   426  O O   . THR A 1 55  ? 0.542   15.323  -0.874  1.00 28.72 ? 55  THR A O   1 
ATOM   427  C CB  . THR A 1 55  ? -0.358  13.096  -2.932  1.00 24.76 ? 55  THR A CB  1 
ATOM   428  O OG1 . THR A 1 55  ? 0.607   12.038  -2.851  1.00 25.42 ? 55  THR A OG1 1 
ATOM   429  C CG2 . THR A 1 55  ? -1.277  12.873  -4.132  1.00 26.80 ? 55  THR A CG2 1 
ATOM   430  N N   . ASP A 1 56  ? 2.357   14.233  -1.643  1.00 28.92 ? 56  ASP A N   1 
ATOM   431  C CA  . ASP A 1 56  ? 3.144   14.449  -0.428  1.00 30.23 ? 56  ASP A CA  1 
ATOM   432  C C   . ASP A 1 56  ? 4.628   14.376  -0.765  1.00 27.29 ? 56  ASP A C   1 
ATOM   433  O O   . ASP A 1 56  ? 5.281   13.353  -0.554  1.00 22.96 ? 56  ASP A O   1 
ATOM   434  C CB  . ASP A 1 56  ? 2.785   13.429  0.654   1.00 30.85 ? 56  ASP A CB  1 
ATOM   435  C CG  . ASP A 1 56  ? 3.516   13.681  1.971   1.00 36.35 ? 56  ASP A CG  1 
ATOM   436  O OD1 . ASP A 1 56  ? 4.362   14.610  2.042   1.00 33.13 ? 56  ASP A OD1 1 
ATOM   437  O OD2 . ASP A 1 56  ? 3.246   12.945  2.941   1.00 31.96 ? 56  ASP A OD2 1 
ATOM   438  N N   . PRO A 1 57  ? 5.197   15.481  -1.261  1.00 27.55 ? 57  PRO A N   1 
ATOM   439  C CA  . PRO A 1 57  ? 6.631   15.494  -1.613  1.00 25.15 ? 57  PRO A CA  1 
ATOM   440  C C   . PRO A 1 57  ? 7.566   15.086  -0.484  1.00 25.58 ? 57  PRO A C   1 
ATOM   441  O O   . PRO A 1 57  ? 8.698   14.669  -0.764  1.00 24.76 ? 57  PRO A O   1 
ATOM   442  C CB  . PRO A 1 57  ? 6.871   16.962  -2.017  1.00 27.54 ? 57  PRO A CB  1 
ATOM   443  C CG  . PRO A 1 57  ? 5.527   17.493  -2.401  1.00 29.33 ? 57  PRO A CG  1 
ATOM   444  C CD  . PRO A 1 57  ? 4.534   16.772  -1.532  1.00 28.89 ? 57  PRO A CD  1 
ATOM   445  N N   . SER A 1 58  ? 7.157   15.219  0.778   1.00 23.86 ? 58  SER A N   1 
ATOM   446  C CA  . SER A 1 58  ? 8.052   14.834  1.862   1.00 26.35 ? 58  SER A CA  1 
ATOM   447  C C   . SER A 1 58  ? 8.249   13.325  1.943   1.00 31.27 ? 58  SER A C   1 
ATOM   448  O O   . SER A 1 58  ? 9.160   12.871  2.641   1.00 27.11 ? 58  SER A O   1 
ATOM   449  C CB  . SER A 1 58  ? 7.518   15.368  3.199   1.00 31.41 ? 58  SER A CB  1 
ATOM   450  O OG  . SER A 1 58  ? 6.318   14.714  3.607   1.00 28.75 ? 58  SER A OG  1 
ATOM   451  N N   . ALA A 1 59  ? 7.423   12.546  1.248   1.00 27.36 ? 59  ALA A N   1 
ATOM   452  C CA  . ALA A 1 59  ? 7.522   11.091  1.246   1.00 27.32 ? 59  ALA A CA  1 
ATOM   453  C C   . ALA A 1 59  ? 8.137   10.541  -0.028  1.00 25.10 ? 59  ALA A C   1 
ATOM   454  O O   . ALA A 1 59  ? 8.336   9.329   -0.122  1.00 27.38 ? 59  ALA A O   1 
ATOM   455  C CB  . ALA A 1 59  ? 6.138   10.464  1.451   1.00 26.42 ? 59  ALA A CB  1 
ATOM   456  N N   . ALA A 1 60  ? 8.478   11.401  -0.997  1.00 26.81 ? 60  ALA A N   1 
ATOM   457  C CA  . ALA A 1 60  ? 8.839   10.904  -2.322  1.00 27.55 ? 60  ALA A CA  1 
ATOM   458  C C   . ALA A 1 60  ? 10.109  10.064  -2.286  1.00 31.72 ? 60  ALA A C   1 
ATOM   459  O O   . ALA A 1 60  ? 10.161  8.988   -2.890  1.00 25.32 ? 60  ALA A O   1 
ATOM   460  C CB  . ALA A 1 60  ? 8.999   12.058  -3.304  1.00 27.67 ? 60  ALA A CB  1 
ATOM   461  N N   . GLU A 1 61  ? 11.161  10.555  -1.624  1.00 28.21 ? 61  GLU A N   1 
ATOM   462  C CA  . GLU A 1 61  ? 12.419  9.815   -1.644  1.00 34.97 ? 61  GLU A CA  1 
ATOM   463  C C   . GLU A 1 61  ? 12.269  8.458   -0.966  1.00 28.13 ? 61  GLU A C   1 
ATOM   464  O O   . GLU A 1 61  ? 12.916  7.487   -1.374  1.00 30.16 ? 61  GLU A O   1 
ATOM   465  C CB  . GLU A 1 61  ? 13.537  10.634  -0.990  1.00 39.68 ? 61  GLU A CB  1 
ATOM   466  C CG  . GLU A 1 61  ? 13.802  10.323  0.473   1.00 48.29 ? 61  GLU A CG  1 
ATOM   467  C CD  . GLU A 1 61  ? 14.980  11.108  1.039   1.00 63.48 ? 61  GLU A CD  1 
ATOM   468  O OE1 . GLU A 1 61  ? 15.575  10.653  2.043   1.00 69.82 ? 61  GLU A OE1 1 
ATOM   469  O OE2 . GLU A 1 61  ? 15.314  12.176  0.477   1.00 61.32 ? 61  GLU A OE2 1 
ATOM   470  N N   . LYS A 1 62  ? 11.399  8.362   0.043   1.00 26.46 ? 62  LYS A N   1 
ATOM   471  C CA  . LYS A 1 62  ? 11.166  7.079   0.693   1.00 34.27 ? 62  LYS A CA  1 
ATOM   472  C C   . LYS A 1 62  ? 10.430  6.118   -0.235  1.00 32.12 ? 62  LYS A C   1 
ATOM   473  O O   . LYS A 1 62  ? 10.710  4.910   -0.235  1.00 24.54 ? 62  LYS A O   1 
ATOM   474  C CB  . LYS A 1 62  ? 10.380  7.286   1.986   1.00 33.47 ? 62  LYS A CB  1 
ATOM   475  C CG  . LYS A 1 62  ? 10.791  6.347   3.108   1.00 50.67 ? 62  LYS A CG  1 
ATOM   476  C CD  . LYS A 1 62  ? 10.756  7.046   4.461   1.00 64.02 ? 62  LYS A CD  1 
ATOM   477  C CE  . LYS A 1 62  ? 11.808  8.153   4.554   1.00 59.94 ? 62  LYS A CE  1 
ATOM   478  N NZ  . LYS A 1 62  ? 13.210  7.632   4.626   1.00 57.85 ? 62  LYS A NZ  1 
ATOM   479  N N   . GLU A 1 63  ? 9.468   6.631   -1.021  1.00 27.75 ? 63  GLU A N   1 
ATOM   480  C CA  . GLU A 1 63  ? 8.734   5.755   -1.934  1.00 25.03 ? 63  GLU A CA  1 
ATOM   481  C C   . GLU A 1 63  ? 9.606   5.315   -3.105  1.00 26.30 ? 63  GLU A C   1 
ATOM   482  O O   . GLU A 1 63  ? 9.470   4.183   -3.598  1.00 21.25 ? 63  GLU A O   1 
ATOM   483  C CB  . GLU A 1 63  ? 7.458   6.444   -2.438  1.00 24.78 ? 63  GLU A CB  1 
ATOM   484  C CG  . GLU A 1 63  ? 6.392   6.702   -1.366  1.00 24.39 ? 63  GLU A CG  1 
ATOM   485  C CD  . GLU A 1 63  ? 5.738   5.439   -0.792  1.00 28.78 ? 63  GLU A CD  1 
ATOM   486  O OE1 . GLU A 1 63  ? 6.110   4.310   -1.174  1.00 26.79 ? 63  GLU A OE1 1 
ATOM   487  O OE2 . GLU A 1 63  ? 4.841   5.575   0.068   1.00 29.59 ? 63  GLU A OE2 1 
ATOM   488  N N   . LEU A 1 64  ? 10.509  6.184   -3.564  1.00 25.28 ? 64  LEU A N   1 
ATOM   489  C CA  . LEU A 1 64  ? 11.451  5.770   -4.598  1.00 27.50 ? 64  LEU A CA  1 
ATOM   490  C C   . LEU A 1 64  ? 12.364  4.672   -4.075  1.00 24.54 ? 64  LEU A C   1 
ATOM   491  O O   . LEU A 1 64  ? 12.588  3.659   -4.749  1.00 26.53 ? 64  LEU A O   1 
ATOM   492  C CB  . LEU A 1 64  ? 12.273  6.966   -5.084  1.00 29.51 ? 64  LEU A CB  1 
ATOM   493  C CG  . LEU A 1 64  ? 13.392  6.602   -6.067  1.00 28.68 ? 64  LEU A CG  1 
ATOM   494  C CD1 . LEU A 1 64  ? 12.844  5.917   -7.313  1.00 31.79 ? 64  LEU A CD1 1 
ATOM   495  C CD2 . LEU A 1 64  ? 14.203  7.845   -6.447  1.00 36.29 ? 64  LEU A CD2 1 
ATOM   496  N N   . ALA A 1 65  ? 12.889  4.853   -2.859  1.00 25.27 ? 65  ALA A N   1 
ATOM   497  C CA  . ALA A 1 65  ? 13.731  3.823   -2.253  1.00 26.42 ? 65  ALA A CA  1 
ATOM   498  C C   . ALA A 1 65  ? 12.990  2.491   -2.152  1.00 26.04 ? 65  ALA A C   1 
ATOM   499  O O   . ALA A 1 65  ? 13.568  1.430   -2.420  1.00 25.00 ? 65  ALA A O   1 
ATOM   500  C CB  . ALA A 1 65  ? 14.202  4.275   -0.871  1.00 26.17 ? 65  ALA A CB  1 
ATOM   501  N N   . ALA A 1 66  ? 11.709  2.531   -1.759  1.00 25.16 ? 66  ALA A N   1 
ATOM   502  C CA  . ALA A 1 66  ? 10.902  1.315   -1.659  1.00 23.13 ? 66  ALA A CA  1 
ATOM   503  C C   . ALA A 1 66  ? 10.662  0.672   -3.019  1.00 24.78 ? 66  ALA A C   1 
ATOM   504  O O   . ALA A 1 66  ? 10.519  -0.559  -3.103  1.00 28.00 ? 66  ALA A O   1 
ATOM   505  C CB  . ALA A 1 66  ? 9.560   1.616   -0.993  1.00 25.18 ? 66  ALA A CB  1 
ATOM   506  N N   . THR A 1 67  ? 10.602  1.479   -4.085  1.00 23.94 ? 67  THR A N   1 
ATOM   507  C CA  . THR A 1 67  ? 10.505  0.935   -5.441  1.00 22.67 ? 67  THR A CA  1 
ATOM   508  C C   . THR A 1 67  ? 11.762  0.150   -5.799  1.00 24.15 ? 67  THR A C   1 
ATOM   509  O O   . THR A 1 67  ? 11.690  -1.002  -6.252  1.00 22.78 ? 67  THR A O   1 
ATOM   510  C CB  . THR A 1 67  ? 10.286  2.064   -6.462  1.00 20.40 ? 67  THR A CB  1 
ATOM   511  O OG1 . THR A 1 67  ? 9.222   2.923   -6.031  1.00 24.85 ? 67  THR A OG1 1 
ATOM   512  C CG2 . THR A 1 67  ? 9.939   1.478   -7.824  1.00 20.28 ? 67  THR A CG2 1 
ATOM   513  N N   . LEU A 1 68  ? 12.931  0.769   -5.611  1.00 24.57 ? 68  LEU A N   1 
ATOM   514  C CA  . LEU A 1 68  ? 14.183  0.104   -5.976  1.00 22.90 ? 68  LEU A CA  1 
ATOM   515  C C   . LEU A 1 68  ? 14.417  -1.143  -5.127  1.00 22.41 ? 68  LEU A C   1 
ATOM   516  O O   . LEU A 1 68  ? 14.920  -2.157  -5.622  1.00 29.08 ? 68  LEU A O   1 
ATOM   517  C CB  . LEU A 1 68  ? 15.356  1.088   -5.849  1.00 26.56 ? 68  LEU A CB  1 
ATOM   518  C CG  . LEU A 1 68  ? 15.201  2.375   -6.666  1.00 29.76 ? 68  LEU A CG  1 
ATOM   519  C CD1 . LEU A 1 68  ? 16.321  3.391   -6.387  1.00 32.30 ? 68  LEU A CD1 1 
ATOM   520  C CD2 . LEU A 1 68  ? 15.115  2.074   -8.161  1.00 32.28 ? 68  LEU A CD2 1 
ATOM   521  N N   . ALA A 1 69  ? 14.036  -1.101  -3.851  1.00 22.94 ? 69  ALA A N   1 
ATOM   522  C CA  . ALA A 1 69  ? 14.153  -2.296  -3.017  1.00 25.82 ? 69  ALA A CA  1 
ATOM   523  C C   . ALA A 1 69  ? 13.210  -3.404  -3.483  1.00 26.16 ? 69  ALA A C   1 
ATOM   524  O O   . ALA A 1 69  ? 13.550  -4.592  -3.413  1.00 23.99 ? 69  ALA A O   1 
ATOM   525  C CB  . ALA A 1 69  ? 13.876  -1.942  -1.556  1.00 27.51 ? 69  ALA A CB  1 
ATOM   526  N N   . THR A 1 70  ? 12.013  -3.040  -3.949  1.00 23.60 ? 70  THR A N   1 
ATOM   527  C CA  . THR A 1 70  ? 11.093  -4.042  -4.485  1.00 23.17 ? 70  THR A CA  1 
ATOM   528  C C   . THR A 1 70  ? 11.660  -4.688  -5.742  1.00 23.50 ? 70  THR A C   1 
ATOM   529  O O   . THR A 1 70  ? 11.536  -5.907  -5.935  1.00 23.56 ? 70  THR A O   1 
ATOM   530  C CB  . THR A 1 70  ? 9.727   -3.406  -4.766  1.00 26.78 ? 70  THR A CB  1 
ATOM   531  O OG1 . THR A 1 70  ? 9.184   -2.928  -3.537  1.00 22.13 ? 70  THR A OG1 1 
ATOM   532  C CG2 . THR A 1 70  ? 8.760   -4.424  -5.339  1.00 21.78 ? 70  THR A CG2 1 
ATOM   533  N N   . ILE A 1 71  ? 12.291  -3.890  -6.605  1.00 21.17 ? 71  ILE A N   1 
ATOM   534  C CA  . ILE A 1 71  ? 12.952  -4.444  -7.784  1.00 23.98 ? 71  ILE A CA  1 
ATOM   535  C C   . ILE A 1 71  ? 14.067  -5.396  -7.359  1.00 27.54 ? 71  ILE A C   1 
ATOM   536  O O   . ILE A 1 71  ? 14.149  -6.533  -7.835  1.00 26.27 ? 71  ILE A O   1 
ATOM   537  C CB  . ILE A 1 71  ? 13.489  -3.314  -8.682  1.00 25.87 ? 71  ILE A CB  1 
ATOM   538  C CG1 . ILE A 1 71  ? 12.340  -2.467  -9.242  1.00 25.23 ? 71  ILE A CG1 1 
ATOM   539  C CG2 . ILE A 1 71  ? 14.312  -3.884  -9.833  1.00 27.42 ? 71  ILE A CG2 1 
ATOM   540  C CD1 . ILE A 1 71  ? 12.800  -1.106  -9.747  1.00 23.89 ? 71  ILE A CD1 1 
ATOM   541  N N   . ASP A 1 72  ? 14.929  -4.943  -6.439  1.00 24.92 ? 72  ASP A N   1 
ATOM   542  C CA  . ASP A 1 72  ? 16.012  -5.791  -5.928  1.00 29.17 ? 72  ASP A CA  1 
ATOM   543  C C   . ASP A 1 72  ? 15.485  -7.115  -5.388  1.00 30.15 ? 72  ASP A C   1 
ATOM   544  O O   . ASP A 1 72  ? 16.086  -8.173  -5.608  1.00 31.11 ? 72  ASP A O   1 
ATOM   545  C CB  . ASP A 1 72  ? 16.772  -5.068  -4.810  1.00 30.68 ? 72  ASP A CB  1 
ATOM   546  C CG  . ASP A 1 72  ? 17.622  -3.920  -5.308  1.00 43.72 ? 72  ASP A CG  1 
ATOM   547  O OD1 . ASP A 1 72  ? 18.226  -4.038  -6.396  1.00 47.36 ? 72  ASP A OD1 1 
ATOM   548  O OD2 . ASP A 1 72  ? 17.703  -2.897  -4.586  1.00 52.82 ? 72  ASP A OD2 1 
ATOM   549  N N   . ARG A 1 73  ? 14.372  -7.069  -4.655  1.00 25.39 ? 73  ARG A N   1 
ATOM   550  C CA  . ARG A 1 73  ? 13.851  -8.247  -3.968  1.00 24.58 ? 73  ARG A CA  1 
ATOM   551  C C   . ARG A 1 73  ? 13.174  -9.201  -4.944  1.00 27.62 ? 73  ARG A C   1 
ATOM   552  O O   . ARG A 1 73  ? 13.492  -10.395 -4.991  1.00 24.64 ? 73  ARG A O   1 
ATOM   553  C CB  . ARG A 1 73  ? 12.878  -7.794  -2.876  1.00 27.89 ? 73  ARG A CB  1 
ATOM   554  C CG  . ARG A 1 73  ? 12.247  -8.883  -2.047  1.00 34.25 ? 73  ARG A CG  1 
ATOM   555  C CD  . ARG A 1 73  ? 11.502  -8.273  -0.851  1.00 35.89 ? 73  ARG A CD  1 
ATOM   556  N NE  . ARG A 1 73  ? 10.424  -7.385  -1.272  1.00 33.46 ? 73  ARG A NE  1 
ATOM   557  C CZ  . ARG A 1 73  ? 10.436  -6.061  -1.158  1.00 33.89 ? 73  ARG A CZ  1 
ATOM   558  N NH1 . ARG A 1 73  ? 11.446  -5.419  -0.585  1.00 34.88 ? 73  ARG A NH1 1 
ATOM   559  N NH2 . ARG A 1 73  ? 9.405   -5.362  -1.624  1.00 28.28 ? 73  ARG A NH2 1 
ATOM   560  N N   . LEU A 1 74  ? 12.250  -8.687  -5.753  1.00 24.71 ? 74  LEU A N   1 
ATOM   561  C CA  . LEU A 1 74  ? 11.464  -9.566  -6.610  1.00 24.18 ? 74  LEU A CA  1 
ATOM   562  C C   . LEU A 1 74  ? 12.287  -10.126 -7.761  1.00 21.05 ? 74  LEU A C   1 
ATOM   563  O O   . LEU A 1 74  ? 12.018  -11.239 -8.230  1.00 25.47 ? 74  LEU A O   1 
ATOM   564  C CB  . LEU A 1 74  ? 10.250  -8.811  -7.140  1.00 20.57 ? 74  LEU A CB  1 
ATOM   565  C CG  . LEU A 1 74  ? 9.285   -8.385  -6.029  1.00 22.13 ? 74  LEU A CG  1 
ATOM   566  C CD1 . LEU A 1 74  ? 8.064   -7.737  -6.644  1.00 22.84 ? 74  LEU A CD1 1 
ATOM   567  C CD2 . LEU A 1 74  ? 8.898   -9.575  -5.163  1.00 25.64 ? 74  LEU A CD2 1 
ATOM   568  N N   . LEU A 1 75  ? 13.277  -9.374  -8.237  1.00 20.52 ? 75  LEU A N   1 
ATOM   569  C CA  . LEU A 1 75  ? 14.085  -9.770  -9.385  1.00 22.92 ? 75  LEU A CA  1 
ATOM   570  C C   . LEU A 1 75  ? 15.510  -10.125 -8.963  1.00 29.04 ? 75  LEU A C   1 
ATOM   571  O O   . LEU A 1 75  ? 16.458  -9.973  -9.739  1.00 22.27 ? 75  LEU A O   1 
ATOM   572  C CB  . LEU A 1 75  ? 14.089  -8.664  -10.438 1.00 26.32 ? 75  LEU A CB  1 
ATOM   573  C CG  . LEU A 1 75  ? 12.717  -8.303  -11.024 1.00 25.55 ? 75  LEU A CG  1 
ATOM   574  C CD1 . LEU A 1 75  ? 12.866  -7.256  -12.099 1.00 22.04 ? 75  LEU A CD1 1 
ATOM   575  C CD2 . LEU A 1 75  ? 12.036  -9.547  -11.584 1.00 22.10 ? 75  LEU A CD2 1 
ATOM   576  N N   . LYS A 1 76  ? 15.653  -10.593 -7.720  1.00 27.31 ? 76  LYS A N   1 
ATOM   577  C CA  . LYS A 1 76  ? 16.956  -10.936 -7.158  1.00 28.81 ? 76  LYS A CA  1 
ATOM   578  C C   . LYS A 1 76  ? 17.692  -11.956 -8.022  1.00 30.18 ? 76  LYS A C   1 
ATOM   579  O O   . LYS A 1 76  ? 18.917  -11.889 -8.169  1.00 32.74 ? 76  LYS A O   1 
ATOM   580  C CB  . LYS A 1 76  ? 16.753  -11.450 -5.726  1.00 33.33 ? 76  LYS A CB  1 
ATOM   581  C CG  . LYS A 1 76  ? 17.745  -12.478 -5.228  1.00 42.61 ? 76  LYS A CG  1 
ATOM   582  C CD  . LYS A 1 76  ? 17.916  -12.415 -3.692  1.00 45.27 ? 76  LYS A CD  1 
ATOM   583  C CE  . LYS A 1 76  ? 16.838  -13.171 -2.915  1.00 37.16 ? 76  LYS A CE  1 
ATOM   584  N NZ  . LYS A 1 76  ? 17.095  -13.160 -1.410  1.00 30.57 ? 76  LYS A NZ  1 
ATOM   585  N N   . GLU A 1 77  ? 16.966  -12.883 -8.626  1.00 30.06 ? 77  GLU A N   1 
ATOM   586  C CA  . GLU A 1 77  ? 17.578  -13.935 -9.427  1.00 29.06 ? 77  GLU A CA  1 
ATOM   587  C C   . GLU A 1 77  ? 17.684  -13.578 -10.908 1.00 32.98 ? 77  GLU A C   1 
ATOM   588  O O   . GLU A 1 77  ? 18.071  -14.433 -11.707 1.00 31.82 ? 77  GLU A O   1 
ATOM   589  C CB  . GLU A 1 77  ? 16.797  -15.238 -9.249  1.00 31.20 ? 77  GLU A CB  1 
ATOM   590  C CG  . GLU A 1 77  ? 16.719  -15.708 -7.791  1.00 36.58 ? 77  GLU A CG  1 
ATOM   591  C CD  . GLU A 1 77  ? 18.097  -15.965 -7.169  1.00 39.84 ? 77  GLU A CD  1 
ATOM   592  O OE1 . GLU A 1 77  ? 18.217  -15.897 -5.923  1.00 37.33 ? 77  GLU A OE1 1 
ATOM   593  O OE2 . GLU A 1 77  ? 19.059  -16.240 -7.928  1.00 42.84 ? 77  GLU A OE2 1 
ATOM   594  N N   . HIS A 1 78  ? 17.362  -12.339 -11.293 1.00 29.40 ? 78  HIS A N   1 
ATOM   595  C CA  . HIS A 1 78  ? 17.522  -11.865 -12.670 1.00 25.95 ? 78  HIS A CA  1 
ATOM   596  C C   . HIS A 1 78  ? 18.244  -10.526 -12.636 1.00 30.48 ? 78  HIS A C   1 
ATOM   597  O O   . HIS A 1 78  ? 17.656  -9.473  -12.922 1.00 26.38 ? 78  HIS A O   1 
ATOM   598  C CB  . HIS A 1 78  ? 16.175  -11.737 -13.386 1.00 31.74 ? 78  HIS A CB  1 
ATOM   599  C CG  . HIS A 1 78  ? 15.290  -12.932 -13.228 1.00 38.11 ? 78  HIS A CG  1 
ATOM   600  N ND1 . HIS A 1 78  ? 15.437  -14.074 -13.987 1.00 46.08 ? 78  HIS A ND1 1 
ATOM   601  C CD2 . HIS A 1 78  ? 14.248  -13.166 -12.393 1.00 40.60 ? 78  HIS A CD2 1 
ATOM   602  C CE1 . HIS A 1 78  ? 14.525  -14.962 -13.626 1.00 45.45 ? 78  HIS A CE1 1 
ATOM   603  N NE2 . HIS A 1 78  ? 13.791  -14.435 -12.661 1.00 49.70 ? 78  HIS A NE2 1 
ATOM   604  N N   . PRO A 1 79  ? 19.538  -10.529 -12.307 1.00 29.16 ? 79  PRO A N   1 
ATOM   605  C CA  . PRO A 1 79  ? 20.219  -9.252  -12.050 1.00 26.66 ? 79  PRO A CA  1 
ATOM   606  C C   . PRO A 1 79  ? 20.330  -8.355  -13.273 1.00 29.89 ? 79  PRO A C   1 
ATOM   607  O O   . PRO A 1 79  ? 20.319  -7.123  -13.118 1.00 26.00 ? 79  PRO A O   1 
ATOM   608  C CB  . PRO A 1 79  ? 21.595  -9.692  -11.530 1.00 30.72 ? 79  PRO A CB  1 
ATOM   609  C CG  . PRO A 1 79  ? 21.798  -11.054 -12.092 1.00 29.67 ? 79  PRO A CG  1 
ATOM   610  C CD  . PRO A 1 79  ? 20.442  -11.688 -12.167 1.00 31.12 ? 79  PRO A CD  1 
ATOM   611  N N   . GLU A 1 80  ? 20.433  -8.919  -14.483 1.00 25.44 ? 80  GLU A N   1 
ATOM   612  C CA  . GLU A 1 80  ? 20.482  -8.069  -15.673 1.00 34.40 ? 80  GLU A CA  1 
ATOM   613  C C   . GLU A 1 80  ? 19.186  -7.284  -15.830 1.00 31.36 ? 80  GLU A C   1 
ATOM   614  O O   . GLU A 1 80  ? 19.194  -6.061  -16.030 1.00 28.47 ? 80  GLU A O   1 
ATOM   615  C CB  . GLU A 1 80  ? 20.753  -8.908  -16.925 1.00 38.15 ? 80  GLU A CB  1 
ATOM   616  C CG  . GLU A 1 80  ? 20.486  -8.131  -18.211 1.00 53.19 ? 80  GLU A CG  1 
ATOM   617  C CD  . GLU A 1 80  ? 21.220  -8.687  -19.419 1.00 71.69 ? 80  GLU A CD  1 
ATOM   618  O OE1 . GLU A 1 80  ? 21.866  -9.749  -19.287 1.00 78.36 ? 80  GLU A OE1 1 
ATOM   619  O OE2 . GLU A 1 80  ? 21.154  -8.055  -20.499 1.00 64.58 ? 80  GLU A OE2 1 
ATOM   620  N N   . LEU A 1 81  ? 18.056  -7.985  -15.740 1.00 31.82 ? 81  LEU A N   1 
ATOM   621  C CA  . LEU A 1 81  ? 16.753  -7.337  -15.821 1.00 27.37 ? 81  LEU A CA  1 
ATOM   622  C C   . LEU A 1 81  ? 16.562  -6.342  -14.688 1.00 26.19 ? 81  LEU A C   1 
ATOM   623  O O   . LEU A 1 81  ? 16.079  -5.224  -14.905 1.00 25.13 ? 81  LEU A O   1 
ATOM   624  C CB  . LEU A 1 81  ? 15.658  -8.400  -15.786 1.00 26.85 ? 81  LEU A CB  1 
ATOM   625  C CG  . LEU A 1 81  ? 14.235  -7.854  -15.742 1.00 24.85 ? 81  LEU A CG  1 
ATOM   626  C CD1 . LEU A 1 81  ? 13.962  -7.079  -17.025 1.00 28.67 ? 81  LEU A CD1 1 
ATOM   627  C CD2 . LEU A 1 81  ? 13.256  -8.998  -15.570 1.00 27.24 ? 81  LEU A CD2 1 
ATOM   628  N N   . ALA A 1 82  ? 16.944  -6.730  -13.471 1.00 23.61 ? 82  ALA A N   1 
ATOM   629  C CA  . ALA A 1 82  ? 16.803  -5.843  -12.319 1.00 22.08 ? 82  ALA A CA  1 
ATOM   630  C C   . ALA A 1 82  ? 17.545  -4.529  -12.529 1.00 27.10 ? 82  ALA A C   1 
ATOM   631  O O   . ALA A 1 82  ? 17.050  -3.462  -12.147 1.00 26.49 ? 82  ALA A O   1 
ATOM   632  C CB  . ALA A 1 82  ? 17.312  -6.548  -11.065 1.00 20.92 ? 82  ALA A CB  1 
ATOM   633  N N   . ALA A 1 83  ? 18.739  -4.592  -13.129 1.00 27.09 ? 83  ALA A N   1 
ATOM   634  C CA  . ALA A 1 83  ? 19.528  -3.392  -13.403 1.00 26.23 ? 83  ALA A CA  1 
ATOM   635  C C   . ALA A 1 83  ? 18.864  -2.506  -14.453 1.00 25.85 ? 83  ALA A C   1 
ATOM   636  O O   . ALA A 1 83  ? 18.885  -1.272  -14.337 1.00 26.17 ? 83  ALA A O   1 
ATOM   637  C CB  . ALA A 1 83  ? 20.934  -3.792  -13.859 1.00 27.42 ? 83  ALA A CB  1 
ATOM   638  N N   . GLU A 1 84  ? 18.276  -3.111  -15.489 1.00 24.96 ? 84  GLU A N   1 
ATOM   639  C CA  . GLU A 1 84  ? 17.595  -2.313  -16.503 1.00 25.56 ? 84  GLU A CA  1 
ATOM   640  C C   . GLU A 1 84  ? 16.414  -1.548  -15.911 1.00 27.43 ? 84  GLU A C   1 
ATOM   641  O O   . GLU A 1 84  ? 16.216  -0.365  -16.213 1.00 28.47 ? 84  GLU A O   1 
ATOM   642  C CB  . GLU A 1 84  ? 17.131  -3.203  -17.649 1.00 30.24 ? 84  GLU A CB  1 
ATOM   643  C CG  . GLU A 1 84  ? 18.261  -3.929  -18.378 1.00 33.83 ? 84  GLU A CG  1 
ATOM   644  C CD  . GLU A 1 84  ? 17.725  -4.995  -19.333 1.00 43.55 ? 84  GLU A CD  1 
ATOM   645  O OE1 . GLU A 1 84  ? 16.952  -5.874  -18.883 1.00 40.62 ? 84  GLU A OE1 1 
ATOM   646  O OE2 . GLU A 1 84  ? 18.054  -4.938  -20.537 1.00 50.85 ? 84  GLU A OE2 1 
ATOM   647  N N   . ILE A 1 85  ? 15.621  -2.197  -15.058 1.00 25.80 ? 85  ILE A N   1 
ATOM   648  C CA  A ILE A 1 85  ? 14.430  -1.527  -14.543 0.48 25.35 ? 85  ILE A CA  1 
ATOM   649  C CA  B ILE A 1 85  ? 14.425  -1.549  -14.522 0.52 25.30 ? 85  ILE A CA  1 
ATOM   650  C C   . ILE A 1 85  ? 14.806  -0.446  -13.540 1.00 24.28 ? 85  ILE A C   1 
ATOM   651  O O   . ILE A 1 85  ? 14.232  0.653   -13.554 1.00 24.11 ? 85  ILE A O   1 
ATOM   652  C CB  A ILE A 1 85  ? 13.460  -2.553  -13.941 0.48 23.00 ? 85  ILE A CB  1 
ATOM   653  C CB  B ILE A 1 85  ? 13.503  -2.592  -13.863 0.52 22.82 ? 85  ILE A CB  1 
ATOM   654  C CG1 A ILE A 1 85  ? 12.955  -3.475  -15.043 0.48 24.89 ? 85  ILE A CG1 1 
ATOM   655  C CG1 B ILE A 1 85  ? 13.243  -3.782  -14.799 0.52 25.07 ? 85  ILE A CG1 1 
ATOM   656  C CG2 A ILE A 1 85  ? 12.299  -1.850  -13.241 0.48 22.61 ? 85  ILE A CG2 1 
ATOM   657  C CG2 B ILE A 1 85  ? 12.206  -1.936  -13.385 0.52 22.66 ? 85  ILE A CG2 1 
ATOM   658  C CD1 A ILE A 1 85  ? 12.741  -4.852  -14.572 0.48 22.66 ? 85  ILE A CD1 1 
ATOM   659  C CD1 B ILE A 1 85  ? 12.435  -3.458  -16.040 0.52 22.51 ? 85  ILE A CD1 1 
ATOM   660  N N   . LYS A 1 86  ? 15.761  -0.726  -12.651 1.00 25.40 ? 86  LYS A N   1 
ATOM   661  C CA  . LYS A 1 86  ? 16.197  0.322   -11.730 1.00 23.89 ? 86  LYS A CA  1 
ATOM   662  C C   . LYS A 1 86  ? 16.731  1.524   -12.486 1.00 27.63 ? 86  LYS A C   1 
ATOM   663  O O   . LYS A 1 86  ? 16.514  2.667   -12.079 1.00 26.19 ? 86  LYS A O   1 
ATOM   664  C CB  . LYS A 1 86  ? 17.268  -0.202  -10.781 1.00 30.13 ? 86  LYS A CB  1 
ATOM   665  C CG  . LYS A 1 86  ? 16.795  -1.272  -9.842  1.00 28.77 ? 86  LYS A CG  1 
ATOM   666  C CD  . LYS A 1 86  ? 17.976  -1.955  -9.182  1.00 39.16 ? 86  LYS A CD  1 
ATOM   667  C CE  . LYS A 1 86  ? 18.528  -1.117  -8.046  1.00 44.46 ? 86  LYS A CE  1 
ATOM   668  N NZ  . LYS A 1 86  ? 19.528  -1.882  -7.242  1.00 51.98 ? 86  LYS A NZ  1 
ATOM   669  N N   . ALA A 1 87  ? 17.445  1.289   -13.590 1.00 27.41 ? 87  ALA A N   1 
ATOM   670  C CA  . ALA A 1 87  ? 18.043  2.411   -14.309 1.00 24.77 ? 87  ALA A CA  1 
ATOM   671  C C   . ALA A 1 87  ? 16.981  3.238   -15.030 1.00 29.03 ? 87  ALA A C   1 
ATOM   672  O O   . ALA A 1 87  ? 17.075  4.471   -15.076 1.00 25.37 ? 87  ALA A O   1 
ATOM   673  C CB  . ALA A 1 87  ? 19.099  1.907   -15.291 1.00 25.92 ? 87  ALA A CB  1 
ATOM   674  N N   . PHE A 1 88  ? 15.967  2.587   -15.607 1.00 24.65 ? 88  PHE A N   1 
ATOM   675  C CA  . PHE A 1 88  ? 14.896  3.351   -16.244 1.00 28.66 ? 88  PHE A CA  1 
ATOM   676  C C   . PHE A 1 88  ? 14.113  4.145   -15.206 1.00 30.34 ? 88  PHE A C   1 
ATOM   677  O O   . PHE A 1 88  ? 13.854  5.342   -15.386 1.00 28.74 ? 88  PHE A O   1 
ATOM   678  C CB  . PHE A 1 88  ? 13.960  2.428   -17.032 1.00 29.36 ? 88  PHE A CB  1 
ATOM   679  C CG  . PHE A 1 88  ? 13.267  3.114   -18.182 1.00 29.05 ? 88  PHE A CG  1 
ATOM   680  C CD1 . PHE A 1 88  ? 12.203  3.974   -17.958 1.00 28.27 ? 88  PHE A CD1 1 
ATOM   681  C CD2 . PHE A 1 88  ? 13.696  2.911   -19.488 1.00 28.14 ? 88  PHE A CD2 1 
ATOM   682  C CE1 . PHE A 1 88  ? 11.577  4.629   -19.019 1.00 32.63 ? 88  PHE A CE1 1 
ATOM   683  C CE2 . PHE A 1 88  ? 13.073  3.561   -20.553 1.00 32.23 ? 88  PHE A CE2 1 
ATOM   684  C CZ  . PHE A 1 88  ? 12.009  4.417   -20.316 1.00 30.98 ? 88  PHE A CZ  1 
ATOM   685  N N   . ILE A 1 89  ? 13.762  3.503   -14.090 1.00 28.12 ? 89  ILE A N   1 
ATOM   686  C CA  . ILE A 1 89  ? 12.977  4.189   -13.066 1.00 25.85 ? 89  ILE A CA  1 
ATOM   687  C C   . ILE A 1 89  ? 13.790  5.303   -12.399 1.00 28.42 ? 89  ILE A C   1 
ATOM   688  O O   . ILE A 1 89  ? 13.264  6.385   -12.124 1.00 25.09 ? 89  ILE A O   1 
ATOM   689  C CB  . ILE A 1 89  ? 12.439  3.163   -12.051 1.00 26.65 ? 89  ILE A CB  1 
ATOM   690  C CG1 . ILE A 1 89  ? 11.360  2.310   -12.718 1.00 23.14 ? 89  ILE A CG1 1 
ATOM   691  C CG2 . ILE A 1 89  ? 11.898  3.860   -10.802 1.00 26.91 ? 89  ILE A CG2 1 
ATOM   692  C CD1 . ILE A 1 89  ? 10.757  1.252   -11.805 1.00 28.89 ? 89  ILE A CD1 1 
ATOM   693  N N   . ARG A 1 90  ? 15.081  5.072   -12.138 1.00 25.43 ? 90  ARG A N   1 
ATOM   694  C CA  . ARG A 1 90  ? 15.906  6.132   -11.561 1.00 30.23 ? 90  ARG A CA  1 
ATOM   695  C C   . ARG A 1 90  ? 15.984  7.335   -12.497 1.00 27.30 ? 90  ARG A C   1 
ATOM   696  O O   . ARG A 1 90  ? 15.803  8.482   -12.074 1.00 30.90 ? 90  ARG A O   1 
ATOM   697  C CB  . ARG A 1 90  ? 17.308  5.603   -11.251 1.00 23.92 ? 90  ARG A CB  1 
ATOM   698  C CG  . ARG A 1 90  ? 17.510  5.188   -9.815  1.00 29.59 ? 90  ARG A CG  1 
ATOM   699  C CD  . ARG A 1 90  ? 18.924  4.638   -9.587  1.00 31.68 ? 90  ARG A CD  1 
ATOM   700  N NE  . ARG A 1 90  ? 19.097  4.158   -8.219  1.00 36.86 ? 90  ARG A NE  1 
ATOM   701  C CZ  . ARG A 1 90  ? 19.784  3.073   -7.890  1.00 38.17 ? 90  ARG A CZ  1 
ATOM   702  N NH1 . ARG A 1 90  ? 20.367  2.324   -8.813  1.00 35.91 ? 90  ARG A NH1 1 
ATOM   703  N NH2 . ARG A 1 90  ? 19.872  2.720   -6.606  1.00 35.64 ? 90  ARG A NH2 1 
ATOM   704  N N   . SER A 1 91  ? 16.241  7.081   -13.781 1.00 28.92 ? 91  SER A N   1 
ATOM   705  C CA  . SER A 1 91  ? 16.358  8.154   -14.763 1.00 32.34 ? 91  SER A CA  1 
ATOM   706  C C   . SER A 1 91  ? 15.035  8.895   -14.939 1.00 32.33 ? 91  SER A C   1 
ATOM   707  O O   . SER A 1 91  ? 15.013  10.127  -15.064 1.00 25.99 ? 91  SER A O   1 
ATOM   708  C CB  . SER A 1 91  ? 16.843  7.561   -16.091 1.00 37.63 ? 91  SER A CB  1 
ATOM   709  O OG  . SER A 1 91  ? 17.043  8.552   -17.081 1.00 47.80 ? 91  SER A OG  1 
ATOM   710  N N   . THR A 1 92  ? 13.921  8.158   -14.944 1.00 26.10 ? 92  THR A N   1 
ATOM   711  C CA  . THR A 1 92  ? 12.605  8.774   -15.071 1.00 26.67 ? 92  THR A CA  1 
ATOM   712  C C   . THR A 1 92  ? 12.298  9.696   -13.894 1.00 27.96 ? 92  THR A C   1 
ATOM   713  O O   . THR A 1 92  ? 11.808  10.820  -14.073 1.00 25.32 ? 92  THR A O   1 
ATOM   714  C CB  . THR A 1 92  ? 11.539  7.681   -15.179 1.00 26.90 ? 92  THR A CB  1 
ATOM   715  O OG1 . THR A 1 92  ? 11.721  6.965   -16.402 1.00 26.61 ? 92  THR A OG1 1 
ATOM   716  C CG2 . THR A 1 92  ? 10.158  8.295   -15.161 1.00 25.25 ? 92  THR A CG2 1 
ATOM   717  N N   . MET A 1 93  ? 12.536  9.218   -12.672 1.00 28.28 ? 93  MET A N   1 
ATOM   718  C CA  . MET A 1 93  ? 12.233  10.030  -11.500 1.00 25.65 ? 93  MET A CA  1 
ATOM   719  C C   . MET A 1 93  ? 13.148  11.241  -11.408 1.00 30.14 ? 93  MET A C   1 
ATOM   720  O O   . MET A 1 93  ? 12.728  12.299  -10.918 1.00 29.38 ? 93  MET A O   1 
ATOM   721  C CB  . MET A 1 93  ? 12.342  9.175   -10.237 1.00 24.51 ? 93  MET A CB  1 
ATOM   722  C CG  . MET A 1 93  ? 11.347  8.023   -10.185 1.00 30.00 ? 93  MET A CG  1 
ATOM   723  S SD  . MET A 1 93  ? 9.621   8.571   -10.173 1.00 36.23 ? 93  MET A SD  1 
ATOM   724  C CE  . MET A 1 93  ? 9.083   8.087   -8.541  1.00 29.47 ? 93  MET A CE  1 
ATOM   725  N N   . ALA A 1 94  ? 14.401  11.104  -11.856 1.00 28.78 ? 94  ALA A N   1 
ATOM   726  C CA  . ALA A 1 94  ? 15.302  12.253  -11.878 1.00 29.71 ? 94  ALA A CA  1 
ATOM   727  C C   . ALA A 1 94  ? 14.759  13.350  -12.784 1.00 28.03 ? 94  ALA A C   1 
ATOM   728  O O   . ALA A 1 94  ? 14.813  14.534  -12.435 1.00 30.82 ? 94  ALA A O   1 
ATOM   729  C CB  . ALA A 1 94  ? 16.701  11.823  -12.327 1.00 25.86 ? 94  ALA A CB  1 
ATOM   730  N N   . GLU A 1 95  ? 14.196  12.969  -13.936 1.00 32.24 ? 95  GLU A N   1 
ATOM   731  C CA  . GLU A 1 95  ? 13.671  13.959  -14.874 1.00 34.62 ? 95  GLU A CA  1 
ATOM   732  C C   . GLU A 1 95  ? 12.423  14.645  -14.329 1.00 33.13 ? 95  GLU A C   1 
ATOM   733  O O   . GLU A 1 95  ? 12.262  15.863  -14.484 1.00 29.35 ? 95  GLU A O   1 
ATOM   734  C CB  . GLU A 1 95  ? 13.369  13.305  -16.223 1.00 33.34 ? 95  GLU A CB  1 
ATOM   735  C CG  . GLU A 1 95  ? 12.838  14.287  -17.263 1.00 46.18 ? 95  GLU A CG  1 
ATOM   736  C CD  . GLU A 1 95  ? 13.731  15.520  -17.417 1.00 54.17 ? 95  GLU A CD  1 
ATOM   737  O OE1 . GLU A 1 95  ? 14.971  15.362  -17.501 1.00 58.66 ? 95  GLU A OE1 1 
ATOM   738  O OE2 . GLU A 1 95  ? 13.192  16.648  -17.441 1.00 55.97 ? 95  GLU A OE2 1 
ATOM   739  N N   . ILE A 1 96  ? 11.525  13.882  -13.699 1.00 28.65 ? 96  ILE A N   1 
ATOM   740  C CA  . ILE A 1 96  ? 10.320  14.476  -13.129 1.00 25.94 ? 96  ILE A CA  1 
ATOM   741  C C   . ILE A 1 96  ? 10.692  15.446  -12.014 1.00 29.72 ? 96  ILE A C   1 
ATOM   742  O O   . ILE A 1 96  ? 10.184  16.574  -11.949 1.00 30.12 ? 96  ILE A O   1 
ATOM   743  C CB  . ILE A 1 96  ? 9.364   13.382  -12.618 1.00 29.12 ? 96  ILE A CB  1 
ATOM   744  C CG1 . ILE A 1 96  ? 8.957   12.435  -13.749 1.00 25.60 ? 96  ILE A CG1 1 
ATOM   745  C CG2 . ILE A 1 96  ? 8.127   14.011  -11.997 1.00 21.62 ? 96  ILE A CG2 1 
ATOM   746  C CD1 . ILE A 1 96  ? 8.191   11.223  -13.253 1.00 27.39 ? 96  ILE A CD1 1 
ATOM   747  N N   . ARG A 1 97  ? 11.575  15.008  -11.110 1.00 27.14 ? 97  ARG A N   1 
ATOM   748  C CA  A ARG A 1 97  ? 12.042  15.880  -10.035 0.45 29.88 ? 97  ARG A CA  1 
ATOM   749  C CA  B ARG A 1 97  ? 12.028  15.885  -10.035 0.55 29.88 ? 97  ARG A CA  1 
ATOM   750  C C   . ARG A 1 97  ? 12.711  17.131  -10.586 1.00 30.92 ? 97  ARG A C   1 
ATOM   751  O O   . ARG A 1 97  ? 12.537  18.229  -10.045 1.00 33.03 ? 97  ARG A O   1 
ATOM   752  C CB  A ARG A 1 97  ? 13.013  15.125  -9.127  0.45 30.67 ? 97  ARG A CB  1 
ATOM   753  C CB  B ARG A 1 97  ? 12.967  15.130  -9.094  0.55 30.67 ? 97  ARG A CB  1 
ATOM   754  C CG  A ARG A 1 97  ? 12.372  14.374  -7.974  0.45 31.25 ? 97  ARG A CG  1 
ATOM   755  C CG  B ARG A 1 97  ? 12.284  14.075  -8.235  0.55 31.00 ? 97  ARG A CG  1 
ATOM   756  C CD  A ARG A 1 97  ? 13.443  13.987  -6.966  0.45 31.53 ? 97  ARG A CD  1 
ATOM   757  C CD  B ARG A 1 97  ? 13.218  13.586  -7.135  0.55 31.71 ? 97  ARG A CD  1 
ATOM   758  N NE  A ARG A 1 97  ? 12.903  13.354  -5.771  0.45 35.56 ? 97  ARG A NE  1 
ATOM   759  N NE  B ARG A 1 97  ? 14.511  13.166  -7.664  0.55 31.87 ? 97  ARG A NE  1 
ATOM   760  C CZ  A ARG A 1 97  ? 12.524  14.005  -4.680  0.45 33.80 ? 97  ARG A CZ  1 
ATOM   761  C CZ  B ARG A 1 97  ? 14.803  11.925  -8.031  0.55 31.72 ? 97  ARG A CZ  1 
ATOM   762  N NH1 A ARG A 1 97  ? 12.566  15.326  -4.612  0.45 39.26 ? 97  ARG A NH1 1 
ATOM   763  N NH1 B ARG A 1 97  ? 13.915  10.951  -7.939  0.55 27.50 ? 97  ARG A NH1 1 
ATOM   764  N NH2 A ARG A 1 97  ? 12.093  13.313  -3.630  0.45 35.57 ? 97  ARG A NH2 1 
ATOM   765  N NH2 B ARG A 1 97  ? 16.017  11.653  -8.501  0.55 23.67 ? 97  ARG A NH2 1 
ATOM   766  N N   . ALA A 1 98  ? 13.485  16.988  -11.666 1.00 29.83 ? 98  ALA A N   1 
ATOM   767  C CA  . ALA A 1 98  ? 14.130  18.157  -12.261 1.00 34.13 ? 98  ALA A CA  1 
ATOM   768  C C   . ALA A 1 98  ? 13.097  19.152  -12.778 1.00 37.06 ? 98  ALA A C   1 
ATOM   769  O O   . ALA A 1 98  ? 13.218  20.362  -12.549 1.00 33.75 ? 98  ALA A O   1 
ATOM   770  C CB  . ALA A 1 98  ? 15.068  17.732  -13.391 1.00 33.05 ? 98  ALA A CB  1 
ATOM   771  N N   . LEU A 1 99  ? 12.070  18.660  -13.477 1.00 29.24 ? 99  LEU A N   1 
ATOM   772  C CA  . LEU A 1 99  ? 11.035  19.553  -13.985 1.00 31.29 ? 99  LEU A CA  1 
ATOM   773  C C   . LEU A 1 99  ? 10.285  20.229  -12.845 1.00 32.92 ? 99  LEU A C   1 
ATOM   774  O O   . LEU A 1 99  ? 9.952   21.420  -12.927 1.00 33.85 ? 99  LEU A O   1 
ATOM   775  C CB  . LEU A 1 99  ? 10.069  18.780  -14.878 1.00 32.59 ? 99  LEU A CB  1 
ATOM   776  C CG  . LEU A 1 99  ? 10.547  18.310  -16.252 1.00 32.54 ? 99  LEU A CG  1 
ATOM   777  C CD1 . LEU A 1 99  ? 9.525   17.325  -16.831 1.00 29.94 ? 99  LEU A CD1 1 
ATOM   778  C CD2 . LEU A 1 99  ? 10.738  19.482  -17.202 1.00 36.00 ? 99  LEU A CD2 1 
ATOM   779  N N   . LEU A 1 100 ? 10.009  19.482  -11.770 1.00 33.50 ? 100 LEU A N   1 
ATOM   780  C CA  . LEU A 1 100 ? 9.304   20.049  -10.626 1.00 33.54 ? 100 LEU A CA  1 
ATOM   781  C C   . LEU A 1 100 ? 10.114  21.161  -9.980  1.00 39.33 ? 100 LEU A C   1 
ATOM   782  O O   . LEU A 1 100 ? 9.605   22.269  -9.758  1.00 37.13 ? 100 LEU A O   1 
ATOM   783  C CB  . LEU A 1 100 ? 8.989   18.955  -9.602  1.00 28.02 ? 100 LEU A CB  1 
ATOM   784  C CG  . LEU A 1 100 ? 7.842   18.029  -9.996  1.00 30.14 ? 100 LEU A CG  1 
ATOM   785  C CD1 . LEU A 1 100 ? 7.630   16.945  -8.939  1.00 27.36 ? 100 LEU A CD1 1 
ATOM   786  C CD2 . LEU A 1 100 ? 6.560   18.845  -10.224 1.00 25.80 ? 100 LEU A CD2 1 
ATOM   787  N N   . ALA A 1 101 ? 11.380  20.877  -9.660  1.00 34.21 ? 101 ALA A N   1 
ATOM   788  C CA  . ALA A 1 101 ? 12.230  21.887  -9.035  1.00 36.71 ? 101 ALA A CA  1 
ATOM   789  C C   . ALA A 1 101 ? 12.335  23.134  -9.900  1.00 41.53 ? 101 ALA A C   1 
ATOM   790  O O   . ALA A 1 101 ? 12.294  24.259  -9.387  1.00 41.74 ? 101 ALA A O   1 
ATOM   791  C CB  . ALA A 1 101 ? 13.622  21.313  -8.763  1.00 33.82 ? 101 ALA A CB  1 
ATOM   792  N N   . ALA A 1 102 ? 12.472  22.956  -11.218 1.00 33.75 ? 102 ALA A N   1 
ATOM   793  C CA  . ALA A 1 102 ? 12.606  24.108  -12.104 1.00 40.99 ? 102 ALA A CA  1 
ATOM   794  C C   . ALA A 1 102 ? 11.340  24.956  -12.122 1.00 49.27 ? 102 ALA A C   1 
ATOM   795  O O   . ALA A 1 102 ? 11.419  26.185  -12.252 1.00 46.77 ? 102 ALA A O   1 
ATOM   796  C CB  . ALA A 1 102 ? 12.961  23.651  -13.516 1.00 34.71 ? 102 ALA A CB  1 
ATOM   797  N N   . SER A 1 103 ? 10.171  24.328  -11.977 1.00 46.55 ? 103 SER A N   1 
ATOM   798  C CA  . SER A 1 103 ? 8.923   25.084  -11.967 1.00 49.80 ? 103 SER A CA  1 
ATOM   799  C C   . SER A 1 103 ? 8.708   25.801  -10.638 1.00 56.15 ? 103 SER A C   1 
ATOM   800  O O   . SER A 1 103 ? 8.219   26.935  -10.617 1.00 60.83 ? 103 SER A O   1 
ATOM   801  C CB  . SER A 1 103 ? 7.751   24.158  -12.277 1.00 43.52 ? 103 SER A CB  1 
ATOM   802  O OG  . SER A 1 103 ? 7.852   23.646  -13.599 1.00 46.98 ? 103 SER A OG  1 
ATOM   803  N N   . LEU A 1 104 ? 9.072   25.162  -9.523  1.00 51.88 ? 104 LEU A N   1 
ATOM   804  C CA  . LEU A 1 104 ? 8.945   25.792  -8.215  1.00 58.46 ? 104 LEU A CA  1 
ATOM   805  C C   . LEU A 1 104 ? 9.939   26.933  -8.023  1.00 65.11 ? 104 LEU A C   1 
ATOM   806  O O   . LEU A 1 104 ? 9.690   27.829  -7.208  1.00 68.16 ? 104 LEU A O   1 
ATOM   807  C CB  . LEU A 1 104 ? 9.125   24.739  -7.117  1.00 65.70 ? 104 LEU A CB  1 
ATOM   808  C CG  . LEU A 1 104 ? 8.833   25.109  -5.660  1.00 75.29 ? 104 LEU A CG  1 
ATOM   809  C CD1 . LEU A 1 104 ? 7.442   25.712  -5.518  1.00 72.65 ? 104 LEU A CD1 1 
ATOM   810  C CD2 . LEU A 1 104 ? 8.980   23.881  -4.764  1.00 66.52 ? 104 LEU A CD2 1 
ATOM   811  N N   . ALA A 1 105 ? 11.052  26.924  -8.756  1.00 63.90 ? 105 ALA A N   1 
ATOM   812  C CA  . ALA A 1 105 ? 12.059  27.973  -8.663  1.00 67.60 ? 105 ALA A CA  1 
ATOM   813  C C   . ALA A 1 105 ? 11.725  29.194  -9.511  1.00 70.49 ? 105 ALA A C   1 
ATOM   814  O O   . ALA A 1 105 ? 12.468  30.182  -9.465  1.00 71.63 ? 105 ALA A O   1 
ATOM   815  C CB  . ALA A 1 105 ? 13.429  27.421  -9.067  1.00 62.59 ? 105 ALA A CB  1 
ATOM   816  N N   . ALA A 1 106 ? 10.640  29.151  -10.280 1.00 70.65 ? 106 ALA A N   1 
ATOM   817  C CA  . ALA A 1 106 ? 10.217  30.286  -11.093 1.00 71.04 ? 106 ALA A CA  1 
ATOM   818  C C   . ALA A 1 106 ? 9.041   31.015  -10.448 1.00 75.36 ? 106 ALA A C   1 
ATOM   819  O O   . ALA A 1 106 ? 7.955   30.451  -10.291 1.00 76.59 ? 106 ALA A O   1 
ATOM   820  C CB  . ALA A 1 106 ? 9.848   29.824  -12.496 1.00 74.03 ? 106 ALA A CB  1 
ATOM   821  N N   . LEU B 2 1   ? -11.071 -33.813 2.466   1.00 29.16 ? 91  LEU B N   1 
ATOM   822  C CA  . LEU B 2 1   ? -11.430 -34.354 1.154   1.00 30.03 ? 91  LEU B CA  1 
ATOM   823  C C   . LEU B 2 1   ? -11.223 -35.865 1.103   1.00 32.96 ? 91  LEU B C   1 
ATOM   824  O O   . LEU B 2 1   ? -10.244 -36.387 1.650   1.00 35.81 ? 91  LEU B O   1 
ATOM   825  C CB  . LEU B 2 1   ? -10.615 -33.693 0.038   1.00 33.07 ? 91  LEU B CB  1 
ATOM   826  C CG  . LEU B 2 1   ? -10.924 -32.229 -0.279  1.00 40.33 ? 91  LEU B CG  1 
ATOM   827  C CD1 . LEU B 2 1   ? -10.031 -31.722 -1.414  1.00 36.98 ? 91  LEU B CD1 1 
ATOM   828  C CD2 . LEU B 2 1   ? -12.398 -32.055 -0.625  1.00 36.12 ? 91  LEU B CD2 1 
ATOM   829  N N   . PRO B 2 2   ? -12.137 -36.570 0.447   1.00 28.38 ? 92  PRO B N   1 
ATOM   830  C CA  . PRO B 2 2   ? -11.969 -38.013 0.253   1.00 29.15 ? 92  PRO B CA  1 
ATOM   831  C C   . PRO B 2 2   ? -10.975 -38.299 -0.866  1.00 33.28 ? 92  PRO B C   1 
ATOM   832  O O   . PRO B 2 2   ? -10.562 -37.407 -1.611  1.00 31.32 ? 92  PRO B O   1 
ATOM   833  C CB  . PRO B 2 2   ? -13.379 -38.485 -0.124  1.00 30.93 ? 92  PRO B CB  1 
ATOM   834  C CG  . PRO B 2 2   ? -13.997 -37.296 -0.783  1.00 35.46 ? 92  PRO B CG  1 
ATOM   835  C CD  . PRO B 2 2   ? -13.421 -36.079 -0.088  1.00 28.30 ? 92  PRO B CD  1 
ATOM   836  N N   . ALA B 2 3   ? -10.605 -39.584 -0.977  1.00 31.31 ? 93  ALA B N   1 
ATOM   837  C CA  . ALA B 2 3   ? -9.692  -40.029 -2.032  1.00 31.12 ? 93  ALA B CA  1 
ATOM   838  C C   . ALA B 2 3   ? -10.215 -39.711 -3.429  1.00 34.76 ? 93  ALA B C   1 
ATOM   839  O O   . ALA B 2 3   ? -9.420  -39.603 -4.372  1.00 43.11 ? 93  ALA B O   1 
ATOM   840  C CB  . ALA B 2 3   ? -9.444  -41.540 -1.916  1.00 33.72 ? 93  ALA B CB  1 
ATOM   841  N N   . GLN B 2 4   ? -11.530 -39.549 -3.575  1.00 31.94 ? 94  GLN B N   1 
ATOM   842  C CA  . GLN B 2 4   ? -12.140 -39.296 -4.876  1.00 44.28 ? 94  GLN B CA  1 
ATOM   843  C C   . GLN B 2 4   ? -11.722 -37.951 -5.480  1.00 42.95 ? 94  GLN B C   1 
ATOM   844  O O   . GLN B 2 4   ? -11.641 -37.829 -6.708  1.00 38.76 ? 94  GLN B O   1 
ATOM   845  C CB  . GLN B 2 4   ? -13.666 -39.366 -4.730  1.00 41.19 ? 94  GLN B CB  1 
ATOM   846  C CG  . GLN B 2 4   ? -14.446 -39.056 -5.988  1.00 49.13 ? 94  GLN B CG  1 
ATOM   847  C CD  . GLN B 2 4   ? -15.940 -39.226 -5.789  1.00 59.74 ? 94  GLN B CD  1 
ATOM   848  O OE1 . GLN B 2 4   ? -16.380 -40.085 -5.021  1.00 58.24 ? 94  GLN B OE1 1 
ATOM   849  N NE2 . GLN B 2 4   ? -16.731 -38.400 -6.476  1.00 53.34 ? 94  GLN B NE2 1 
ATOM   850  N N   . VAL B 2 5   ? -11.454 -36.940 -4.659  1.00 38.09 ? 95  VAL B N   1 
ATOM   851  C CA  . VAL B 2 5   ? -11.342 -35.560 -5.130  1.00 34.30 ? 95  VAL B CA  1 
ATOM   852  C C   . VAL B 2 5   ? -9.871  -35.161 -5.198  1.00 37.35 ? 95  VAL B C   1 
ATOM   853  O O   . VAL B 2 5   ? -9.163  -35.189 -4.183  1.00 36.63 ? 95  VAL B O   1 
ATOM   854  C CB  . VAL B 2 5   ? -12.131 -34.602 -4.225  1.00 41.39 ? 95  VAL B CB  1 
ATOM   855  C CG1 . VAL B 2 5   ? -12.186 -33.212 -4.845  1.00 42.82 ? 95  VAL B CG1 1 
ATOM   856  C CG2 . VAL B 2 5   ? -13.535 -35.150 -3.956  1.00 38.42 ? 95  VAL B CG2 1 
ATOM   857  N N   . ALA B 2 6   ? -9.415  -34.757 -6.384  1.00 34.46 ? 96  ALA B N   1 
ATOM   858  C CA  . ALA B 2 6   ? -8.009  -34.406 -6.569  1.00 42.59 ? 96  ALA B CA  1 
ATOM   859  C C   . ALA B 2 6   ? -7.677  -33.093 -5.868  1.00 38.07 ? 96  ALA B C   1 
ATOM   860  O O   . ALA B 2 6   ? -8.418  -32.112 -5.987  1.00 39.73 ? 96  ALA B O   1 
ATOM   861  C CB  . ALA B 2 6   ? -7.683  -34.293 -8.056  1.00 43.20 ? 96  ALA B CB  1 
ATOM   862  N N   . PHE B 2 7   ? -6.555  -33.072 -5.150  1.00 36.57 ? 97  PHE B N   1 
ATOM   863  C CA  . PHE B 2 7   ? -6.055  -31.871 -4.491  1.00 41.85 ? 97  PHE B CA  1 
ATOM   864  C C   . PHE B 2 7   ? -4.957  -31.220 -5.328  1.00 35.80 ? 97  PHE B C   1 
ATOM   865  O O   . PHE B 2 7   ? -4.233  -31.891 -6.067  1.00 35.51 ? 97  PHE B O   1 
ATOM   866  C CB  . PHE B 2 7   ? -5.523  -32.181 -3.074  1.00 45.06 ? 97  PHE B CB  1 
ATOM   867  C CG  . PHE B 2 7   ? -4.419  -33.247 -3.012  1.00 58.53 ? 97  PHE B CG  1 
ATOM   868  C CD1 . PHE B 2 7   ? -3.231  -33.117 -3.734  1.00 60.48 ? 97  PHE B CD1 1 
ATOM   869  C CD2 . PHE B 2 7   ? -4.551  -34.348 -2.175  1.00 54.43 ? 97  PHE B CD2 1 
ATOM   870  C CE1 . PHE B 2 7   ? -2.236  -34.074 -3.674  1.00 62.17 ? 97  PHE B CE1 1 
ATOM   871  C CE2 . PHE B 2 7   ? -3.546  -35.305 -2.098  1.00 54.54 ? 97  PHE B CE2 1 
ATOM   872  C CZ  . PHE B 2 7   ? -2.390  -35.167 -2.851  1.00 64.05 ? 97  PHE B CZ  1 
ATOM   873  N N   . THR B 2 8   ? -4.830  -29.925 -5.194  1.00 28.57 ? 98  THR B N   1 
ATOM   874  C CA  . THR B 2 8   ? -3.691  -29.258 -5.812  1.00 25.91 ? 98  THR B CA  1 
ATOM   875  C C   . THR B 2 8   ? -2.413  -29.559 -5.024  1.00 32.23 ? 98  THR B C   1 
ATOM   876  O O   . THR B 2 8   ? -2.452  -29.678 -3.799  1.00 37.72 ? 98  THR B O   1 
ATOM   877  C CB  . THR B 2 8   ? -3.921  -27.750 -5.870  1.00 31.52 ? 98  THR B CB  1 
ATOM   878  O OG1 . THR B 2 8   ? -4.351  -27.285 -4.585  1.00 31.67 ? 98  THR B OG1 1 
ATOM   879  C CG2 . THR B 2 8   ? -4.973  -27.416 -6.909  1.00 29.17 ? 98  THR B CG2 1 
ATOM   880  N N   . PRO B 2 9   ? -1.271  -29.687 -5.697  1.00 26.63 ? 99  PRO B N   1 
ATOM   881  C CA  . PRO B 2 9   ? -1.093  -29.571 -7.143  1.00 28.97 ? 99  PRO B CA  1 
ATOM   882  C C   . PRO B 2 9   ? -1.322  -30.913 -7.821  1.00 30.59 ? 99  PRO B C   1 
ATOM   883  O O   . PRO B 2 9   ? -0.984  -31.963 -7.265  1.00 27.45 ? 99  PRO B O   1 
ATOM   884  C CB  . PRO B 2 9   ? 0.359   -29.077 -7.265  1.00 27.33 ? 99  PRO B CB  1 
ATOM   885  C CG  . PRO B 2 9   ? 1.050   -29.727 -6.102  1.00 25.86 ? 99  PRO B CG  1 
ATOM   886  C CD  . PRO B 2 9   ? 0.021   -29.765 -4.990  1.00 28.62 ? 99  PRO B CD  1 
ATOM   887  N N   . TYR B 2 10  ? -1.894  -30.907 -9.025  1.00 25.30 ? 100 TYR B N   1 
ATOM   888  C CA  . TYR B 2 10  ? -2.084  -32.125 -9.800  1.00 30.27 ? 100 TYR B CA  1 
ATOM   889  C C   . TYR B 2 10  ? -1.901  -31.792 -11.272 1.00 34.25 ? 100 TYR B C   1 
ATOM   890  O O   . TYR B 2 10  ? -2.127  -30.658 -11.697 1.00 28.32 ? 100 TYR B O   1 
ATOM   891  C CB  . TYR B 2 10  ? -3.473  -32.745 -9.568  1.00 24.32 ? 100 TYR B CB  1 
ATOM   892  C CG  . TYR B 2 10  ? -4.613  -31.860 -10.027 1.00 33.47 ? 100 TYR B CG  1 
ATOM   893  C CD1 . TYR B 2 10  ? -5.130  -30.874 -9.188  1.00 29.92 ? 100 TYR B CD1 1 
ATOM   894  C CD2 . TYR B 2 10  ? -5.157  -31.989 -11.307 1.00 34.02 ? 100 TYR B CD2 1 
ATOM   895  C CE1 . TYR B 2 10  ? -6.170  -30.058 -9.601  1.00 32.63 ? 100 TYR B CE1 1 
ATOM   896  C CE2 . TYR B 2 10  ? -6.196  -31.173 -11.731 1.00 29.40 ? 100 TYR B CE2 1 
ATOM   897  C CZ  . TYR B 2 10  ? -6.691  -30.206 -10.869 1.00 33.42 ? 100 TYR B CZ  1 
ATOM   898  O OH  . TYR B 2 10  ? -7.722  -29.391 -11.262 1.00 28.79 ? 100 TYR B OH  1 
ATOM   899  N N   . ALA B 2 11  ? -1.492  -32.785 -12.052 1.00 33.16 ? 101 ALA B N   1 
ATOM   900  C CA  . ALA B 2 11  ? -1.404  -32.564 -13.491 1.00 33.92 ? 101 ALA B CA  1 
ATOM   901  C C   . ALA B 2 11  ? -2.776  -32.791 -14.117 1.00 32.09 ? 101 ALA B C   1 
ATOM   902  O O   . ALA B 2 11  ? -3.408  -33.814 -13.848 1.00 30.72 ? 101 ALA B O   1 
ATOM   903  C CB  . ALA B 2 11  ? -0.366  -33.493 -14.124 1.00 35.43 ? 101 ALA B CB  1 
ATOM   904  N N   . PRO B 2 12  ? -3.277  -31.863 -14.930 1.00 34.52 ? 102 PRO B N   1 
ATOM   905  C CA  . PRO B 2 12  ? -4.616  -32.043 -15.500 1.00 39.41 ? 102 PRO B CA  1 
ATOM   906  C C   . PRO B 2 12  ? -4.602  -33.101 -16.596 1.00 42.48 ? 102 PRO B C   1 
ATOM   907  O O   . PRO B 2 12  ? -3.635  -33.226 -17.350 1.00 39.36 ? 102 PRO B O   1 
ATOM   908  C CB  . PRO B 2 12  ? -4.944  -30.657 -16.059 1.00 34.57 ? 102 PRO B CB  1 
ATOM   909  C CG  . PRO B 2 12  ? -3.604  -30.103 -16.445 1.00 36.92 ? 102 PRO B CG  1 
ATOM   910  C CD  . PRO B 2 12  ? -2.623  -30.640 -15.427 1.00 32.70 ? 102 PRO B CD  1 
ATOM   911  N N   . GLU B 2 13  ? -5.681  -33.875 -16.669 1.00 45.33 ? 103 GLU B N   1 
ATOM   912  C CA  . GLU B 2 13  ? -5.791  -34.902 -17.694 1.00 51.46 ? 103 GLU B CA  1 
ATOM   913  C C   . GLU B 2 13  ? -5.910  -34.266 -19.077 1.00 52.56 ? 103 GLU B C   1 
ATOM   914  O O   . GLU B 2 13  ? -6.404  -33.145 -19.209 1.00 52.20 ? 103 GLU B O   1 
ATOM   915  C CB  . GLU B 2 13  ? -7.004  -35.787 -17.441 1.00 56.12 ? 103 GLU B CB  1 
ATOM   916  C CG  . GLU B 2 13  ? -6.778  -36.903 -16.455 1.00 64.52 ? 103 GLU B CG  1 
ATOM   917  C CD  . GLU B 2 13  ? -7.722  -38.060 -16.708 1.00 81.56 ? 103 GLU B CD  1 
ATOM   918  O OE1 . GLU B 2 13  ? -8.010  -38.332 -17.894 1.00 83.66 ? 103 GLU B OE1 1 
ATOM   919  O OE2 . GLU B 2 13  ? -8.185  -38.688 -15.731 1.00 89.26 ? 103 GLU B OE2 1 
ATOM   920  N N   . PRO B 2 14  ? -5.459  -34.956 -20.124 1.00 54.84 ? 104 PRO B N   1 
ATOM   921  C CA  . PRO B 2 14  ? -5.655  -34.433 -21.486 1.00 54.85 ? 104 PRO B CA  1 
ATOM   922  C C   . PRO B 2 14  ? -7.126  -34.134 -21.738 1.00 57.22 ? 104 PRO B C   1 
ATOM   923  O O   . PRO B 2 14  ? -7.996  -34.987 -21.542 1.00 56.04 ? 104 PRO B O   1 
ATOM   924  C CB  . PRO B 2 14  ? -5.138  -35.569 -22.375 1.00 56.25 ? 104 PRO B CB  1 
ATOM   925  C CG  . PRO B 2 14  ? -4.140  -36.278 -21.520 1.00 57.13 ? 104 PRO B CG  1 
ATOM   926  C CD  . PRO B 2 14  ? -4.702  -36.219 -20.124 1.00 56.16 ? 104 PRO B CD  1 
ATOM   927  N N   . GLY B 2 15  ? -7.402  -32.900 -22.146 1.00 58.47 ? 105 GLY B N   1 
ATOM   928  C CA  . GLY B 2 15  ? -8.761  -32.439 -22.323 1.00 55.24 ? 105 GLY B CA  1 
ATOM   929  C C   . GLY B 2 15  ? -9.351  -31.691 -21.147 1.00 62.61 ? 105 GLY B C   1 
ATOM   930  O O   . GLY B 2 15  ? -10.578 -31.565 -21.073 1.00 63.27 ? 105 GLY B O   1 
ATOM   931  N N   . SER B 2 16  ? -8.526  -31.184 -20.237 1.00 62.24 ? 106 SER B N   1 
ATOM   932  C CA  . SER B 2 16  ? -9.003  -30.549 -19.021 1.00 59.29 ? 106 SER B CA  1 
ATOM   933  C C   . SER B 2 16  ? -8.563  -29.094 -18.958 1.00 62.73 ? 106 SER B C   1 
ATOM   934  O O   . SER B 2 16  ? -7.657  -28.658 -19.672 1.00 60.96 ? 106 SER B O   1 
ATOM   935  C CB  . SER B 2 16  ? -8.493  -31.283 -17.779 1.00 59.43 ? 106 SER B CB  1 
ATOM   936  O OG  . SER B 2 16  ? -7.132  -31.604 -17.934 1.00 75.34 ? 106 SER B OG  1 
ATOM   937  N N   . THR B 2 17  ? -9.255  -28.348 -18.106 1.00 58.16 ? 107 THR B N   1 
ATOM   938  C CA  . THR B 2 17  ? -8.784  -27.097 -17.541 1.00 56.76 ? 107 THR B CA  1 
ATOM   939  C C   . THR B 2 17  ? -8.669  -27.296 -16.035 1.00 50.03 ? 107 THR B C   1 
ATOM   940  O O   . THR B 2 17  ? -9.123  -28.304 -15.487 1.00 51.51 ? 107 THR B O   1 
ATOM   941  C CB  . THR B 2 17  ? -9.732  -25.932 -17.866 1.00 54.01 ? 107 THR B CB  1 
ATOM   942  O OG1 . THR B 2 17  ? -9.129  -24.693 -17.469 1.00 62.77 ? 107 THR B OG1 1 
ATOM   943  C CG2 . THR B 2 17  ? -11.056 -26.101 -17.127 1.00 55.67 ? 107 THR B CG2 1 
ATOM   944  N N   . CYS B 2 18  ? -8.041  -26.334 -15.368 1.00 49.15 ? 108 CYS B N   1 
ATOM   945  C CA  . CYS B 2 18  ? -7.983  -26.350 -13.917 1.00 40.34 ? 108 CYS B CA  1 
ATOM   946  C C   . CYS B 2 18  ? -9.311  -25.855 -13.340 1.00 39.33 ? 108 CYS B C   1 
ATOM   947  O O   . CYS B 2 18  ? -10.122 -25.235 -14.031 1.00 39.88 ? 108 CYS B O   1 
ATOM   948  C CB  . CYS B 2 18  ? -6.811  -25.491 -13.425 1.00 30.89 ? 108 CYS B CB  1 
ATOM   949  S SG  . CYS B 2 18  ? -5.156  -26.025 -14.064 1.00 39.73 ? 108 CYS B SG  1 
ATOM   950  N N   . ARG B 2 19  ? -9.524  -26.134 -12.054 1.00 35.05 ? 109 ARG B N   1 
ATOM   951  C CA  . ARG B 2 19  ? -10.742 -25.707 -11.376 1.00 33.81 ? 109 ARG B CA  1 
ATOM   952  C C   . ARG B 2 19  ? -10.803 -24.183 -11.276 1.00 32.33 ? 109 ARG B C   1 
ATOM   953  O O   . ARG B 2 19  ? -9.865  -23.464 -11.637 1.00 33.66 ? 109 ARG B O   1 
ATOM   954  C CB  . ARG B 2 19  ? -10.833 -26.314 -9.980  1.00 29.69 ? 109 ARG B CB  1 
ATOM   955  C CG  . ARG B 2 19  ? -11.050 -27.821 -9.918  1.00 31.08 ? 109 ARG B CG  1 
ATOM   956  C CD  . ARG B 2 19  ? -11.447 -28.201 -8.496  1.00 36.38 ? 109 ARG B CD  1 
ATOM   957  N NE  . ARG B 2 19  ? -11.519 -29.639 -8.268  1.00 44.96 ? 109 ARG B NE  1 
ATOM   958  C CZ  . ARG B 2 19  ? -10.556 -30.357 -7.704  1.00 44.95 ? 109 ARG B CZ  1 
ATOM   959  N NH1 . ARG B 2 19  ? -9.411  -29.804 -7.329  1.00 38.38 ? 109 ARG B NH1 1 
ATOM   960  N NH2 . ARG B 2 19  ? -10.745 -31.663 -7.511  1.00 45.91 ? 109 ARG B NH2 1 
ATOM   961  N N   . LEU B 2 20  ? -11.916 -23.697 -10.717 1.00 31.62 ? 110 LEU B N   1 
ATOM   962  C CA  . LEU B 2 20  ? -12.195 -22.261 -10.691 1.00 32.07 ? 110 LEU B CA  1 
ATOM   963  C C   . LEU B 2 20  ? -11.133 -21.482 -9.917  1.00 30.57 ? 110 LEU B C   1 
ATOM   964  O O   . LEU B 2 20  ? -10.685 -20.414 -10.360 1.00 32.99 ? 110 LEU B O   1 
ATOM   965  C CB  . LEU B 2 20  ? -13.583 -22.021 -10.085 1.00 40.05 ? 110 LEU B CB  1 
ATOM   966  C CG  . LEU B 2 20  ? -13.965 -20.585 -9.721  1.00 37.59 ? 110 LEU B CG  1 
ATOM   967  C CD1 . LEU B 2 20  ? -14.016 -19.696 -10.960 1.00 39.03 ? 110 LEU B CD1 1 
ATOM   968  C CD2 . LEU B 2 20  ? -15.296 -20.557 -8.964  1.00 35.24 ? 110 LEU B CD2 1 
ATOM   969  N N   . ARG B 2 21  ? -10.741 -21.981 -8.742  1.00 31.43 ? 111 ARG B N   1 
ATOM   970  C CA  . ARG B 2 21  ? -9.789  -21.294 -7.874  1.00 25.98 ? 111 ARG B CA  1 
ATOM   971  C C   . ARG B 2 21  ? -8.340  -21.714 -8.135  1.00 22.91 ? 111 ARG B C   1 
ATOM   972  O O   . ARG B 2 21  ? -7.487  -21.551 -7.252  1.00 21.64 ? 111 ARG B O   1 
ATOM   973  C CB  . ARG B 2 21  ? -10.134 -21.539 -6.405  1.00 24.88 ? 111 ARG B CB  1 
ATOM   974  C CG  . ARG B 2 21  ? -11.598 -21.306 -6.032  1.00 28.58 ? 111 ARG B CG  1 
ATOM   975  C CD  . ARG B 2 21  ? -12.060 -19.905 -6.400  1.00 25.05 ? 111 ARG B CD  1 
ATOM   976  N NE  . ARG B 2 21  ? -13.387 -19.624 -5.856  1.00 26.60 ? 111 ARG B NE  1 
ATOM   977  C CZ  . ARG B 2 21  ? -14.100 -18.546 -6.153  1.00 30.07 ? 111 ARG B CZ  1 
ATOM   978  N NH1 . ARG B 2 21  ? -13.673 -17.655 -7.038  1.00 22.05 ? 111 ARG B NH1 1 
ATOM   979  N NH2 . ARG B 2 21  ? -15.266 -18.352 -5.541  1.00 24.00 ? 111 ARG B NH2 1 
ATOM   980  N N   . GLU B 2 22  ? -8.053  -22.247 -9.317  1.00 21.55 ? 112 GLU B N   1 
ATOM   981  C CA  . GLU B 2 22  ? -6.752  -22.806 -9.659  1.00 20.65 ? 112 GLU B CA  1 
ATOM   982  C C   . GLU B 2 22  ? -6.257  -22.136 -10.927 1.00 28.10 ? 112 GLU B C   1 
ATOM   983  O O   . GLU B 2 22  ? -7.030  -21.531 -11.672 1.00 26.20 ? 112 GLU B O   1 
ATOM   984  C CB  . GLU B 2 22  ? -6.825  -24.337 -9.867  1.00 21.39 ? 112 GLU B CB  1 
ATOM   985  C CG  . GLU B 2 22  ? -7.381  -25.090 -8.671  1.00 24.11 ? 112 GLU B CG  1 
ATOM   986  C CD  . GLU B 2 22  ? -7.639  -26.576 -8.957  1.00 30.58 ? 112 GLU B CD  1 
ATOM   987  O OE1 . GLU B 2 22  ? -7.530  -27.000 -10.124 1.00 26.24 ? 112 GLU B OE1 1 
ATOM   988  O OE2 . GLU B 2 22  ? -7.947  -27.319 -8.008  1.00 25.78 ? 112 GLU B OE2 1 
ATOM   989  N N   . TYR B 2 23  ? -4.951  -22.239 -11.165 1.00 22.55 ? 113 TYR B N   1 
ATOM   990  C CA  . TYR B 2 23  ? -4.366  -21.793 -12.417 1.00 23.12 ? 113 TYR B CA  1 
ATOM   991  C C   . TYR B 2 23  ? -3.353  -22.848 -12.827 1.00 25.98 ? 113 TYR B C   1 
ATOM   992  O O   . TYR B 2 23  ? -2.897  -23.635 -11.999 1.00 20.91 ? 113 TYR B O   1 
ATOM   993  C CB  . TYR B 2 23  ? -3.710  -20.405 -12.290 1.00 24.58 ? 113 TYR B CB  1 
ATOM   994  C CG  . TYR B 2 23  ? -2.363  -20.433 -11.609 1.00 21.95 ? 113 TYR B CG  1 
ATOM   995  C CD1 . TYR B 2 23  ? -2.266  -20.530 -10.232 1.00 18.00 ? 113 TYR B CD1 1 
ATOM   996  C CD2 . TYR B 2 23  ? -1.186  -20.396 -12.352 1.00 21.53 ? 113 TYR B CD2 1 
ATOM   997  C CE1 . TYR B 2 23  ? -1.036  -20.577 -9.605  1.00 20.94 ? 113 TYR B CE1 1 
ATOM   998  C CE2 . TYR B 2 23  ? 0.046   -20.439 -11.737 1.00 22.66 ? 113 TYR B CE2 1 
ATOM   999  C CZ  . TYR B 2 23  ? 0.115   -20.530 -10.363 1.00 23.58 ? 113 TYR B CZ  1 
ATOM   1000 O OH  . TYR B 2 23  ? 1.338   -20.584 -9.741  1.00 25.18 ? 113 TYR B OH  1 
ATOM   1001 N N   . TYR B 2 24  ? -3.019  -22.883 -14.113 1.00 20.97 ? 114 TYR B N   1 
ATOM   1002 C CA  . TYR B 2 24  ? -2.043  -23.848 -14.610 1.00 25.60 ? 114 TYR B CA  1 
ATOM   1003 C C   . TYR B 2 24  ? -0.663  -23.207 -14.541 1.00 28.00 ? 114 TYR B C   1 
ATOM   1004 O O   . TYR B 2 24  ? -0.387  -22.227 -15.242 1.00 29.45 ? 114 TYR B O   1 
ATOM   1005 C CB  . TYR B 2 24  ? -2.371  -24.305 -16.029 1.00 31.71 ? 114 TYR B CB  1 
ATOM   1006 C CG  . TYR B 2 24  ? -1.413  -25.371 -16.508 1.00 29.41 ? 114 TYR B CG  1 
ATOM   1007 C CD1 . TYR B 2 24  ? -1.591  -26.698 -16.152 1.00 31.82 ? 114 TYR B CD1 1 
ATOM   1008 C CD2 . TYR B 2 24  ? -0.315  -25.040 -17.286 1.00 33.75 ? 114 TYR B CD2 1 
ATOM   1009 C CE1 . TYR B 2 24  ? -0.704  -27.679 -16.574 1.00 37.45 ? 114 TYR B CE1 1 
ATOM   1010 C CE2 . TYR B 2 24  ? 0.578   -26.006 -17.714 1.00 37.86 ? 114 TYR B CE2 1 
ATOM   1011 C CZ  . TYR B 2 24  ? 0.381   -27.320 -17.355 1.00 35.66 ? 114 TYR B CZ  1 
ATOM   1012 O OH  . TYR B 2 24  ? 1.267   -28.283 -17.779 1.00 42.82 ? 114 TYR B OH  1 
ATOM   1013 N N   . ASP B 2 25  ? 0.193   -23.731 -13.671 1.00 24.44 ? 115 ASP B N   1 
ATOM   1014 C CA  . ASP B 2 25  ? 1.524   -23.173 -13.490 1.00 26.87 ? 115 ASP B CA  1 
ATOM   1015 C C   . ASP B 2 25  ? 2.491   -23.861 -14.450 1.00 29.52 ? 115 ASP B C   1 
ATOM   1016 O O   . ASP B 2 25  ? 2.689   -25.078 -14.367 1.00 25.99 ? 115 ASP B O   1 
ATOM   1017 C CB  . ASP B 2 25  ? 1.988   -23.326 -12.040 1.00 27.08 ? 115 ASP B CB  1 
ATOM   1018 C CG  . ASP B 2 25  ? 3.342   -22.682 -11.804 1.00 31.09 ? 115 ASP B CG  1 
ATOM   1019 O OD1 . ASP B 2 25  ? 4.363   -23.274 -12.215 1.00 29.94 ? 115 ASP B OD1 1 
ATOM   1020 O OD2 . ASP B 2 25  ? 3.393   -21.566 -11.242 1.00 25.24 ? 115 ASP B OD2 1 
ATOM   1021 N N   . GLN B 2 26  ? 3.114   -23.069 -15.331 1.00 29.19 ? 116 GLN B N   1 
ATOM   1022 C CA  . GLN B 2 26  ? 3.977   -23.605 -16.387 1.00 34.39 ? 116 GLN B CA  1 
ATOM   1023 C C   . GLN B 2 26  ? 5.286   -24.177 -15.851 1.00 33.84 ? 116 GLN B C   1 
ATOM   1024 O O   . GLN B 2 26  ? 5.905   -25.022 -16.507 1.00 33.30 ? 116 GLN B O   1 
ATOM   1025 C CB  . GLN B 2 26  ? 4.296   -22.514 -17.413 1.00 34.21 ? 116 GLN B CB  1 
ATOM   1026 C CG  . GLN B 2 26  ? 3.119   -22.041 -18.240 1.00 38.57 ? 116 GLN B CG  1 
ATOM   1027 C CD  . GLN B 2 26  ? 2.676   -23.065 -19.275 1.00 45.36 ? 116 GLN B CD  1 
ATOM   1028 O OE1 . GLN B 2 26  ? 3.298   -24.121 -19.441 1.00 45.17 ? 116 GLN B OE1 1 
ATOM   1029 N NE2 . GLN B 2 26  ? 1.594   -22.754 -19.976 1.00 45.28 ? 116 GLN B NE2 1 
ATOM   1030 N N   . THR B 2 27  ? 5.754   -23.706 -14.698 1.00 31.60 ? 117 THR B N   1 
ATOM   1031 C CA  . THR B 2 27  ? 7.006   -24.227 -14.154 1.00 28.96 ? 117 THR B CA  1 
ATOM   1032 C C   . THR B 2 27  ? 6.802   -25.611 -13.553 1.00 39.53 ? 117 THR B C   1 
ATOM   1033 O O   . THR B 2 27  ? 7.570   -26.546 -13.828 1.00 35.72 ? 117 THR B O   1 
ATOM   1034 C CB  . THR B 2 27  ? 7.566   -23.254 -13.114 1.00 35.88 ? 117 THR B CB  1 
ATOM   1035 O OG1 . THR B 2 27  ? 7.805   -21.986 -13.738 1.00 33.87 ? 117 THR B OG1 1 
ATOM   1036 C CG2 . THR B 2 27  ? 8.869   -23.776 -12.529 1.00 35.76 ? 117 THR B CG2 1 
ATOM   1037 N N   . ALA B 2 28  ? 5.757   -25.766 -12.738 1.00 32.79 ? 118 ALA B N   1 
ATOM   1038 C CA  . ALA B 2 28  ? 5.424   -27.077 -12.203 1.00 34.92 ? 118 ALA B CA  1 
ATOM   1039 C C   . ALA B 2 28  ? 4.741   -27.968 -13.226 1.00 32.96 ? 118 ALA B C   1 
ATOM   1040 O O   . ALA B 2 28  ? 4.740   -29.189 -13.049 1.00 32.07 ? 118 ALA B O   1 
ATOM   1041 C CB  . ALA B 2 28  ? 4.516   -26.937 -10.977 1.00 30.34 ? 118 ALA B CB  1 
ATOM   1042 N N   . GLN B 2 29  ? 4.166   -27.385 -14.279 1.00 30.24 ? 119 GLN B N   1 
ATOM   1043 C CA  . GLN B 2 29  ? 3.278   -28.097 -15.196 1.00 33.18 ? 119 GLN B CA  1 
ATOM   1044 C C   . GLN B 2 29  ? 2.157   -28.792 -14.428 1.00 35.54 ? 119 GLN B C   1 
ATOM   1045 O O   . GLN B 2 29  ? 1.865   -29.974 -14.632 1.00 27.05 ? 119 GLN B O   1 
ATOM   1046 C CB  . GLN B 2 29  ? 4.048   -29.099 -16.050 1.00 37.83 ? 119 GLN B CB  1 
ATOM   1047 C CG  . GLN B 2 29  ? 5.193   -28.509 -16.830 1.00 39.29 ? 119 GLN B CG  1 
ATOM   1048 C CD  . GLN B 2 29  ? 5.693   -29.482 -17.879 1.00 52.11 ? 119 GLN B CD  1 
ATOM   1049 O OE1 . GLN B 2 29  ? 6.646   -30.226 -17.647 1.00 46.98 ? 119 GLN B OE1 1 
ATOM   1050 N NE2 . GLN B 2 29  ? 5.031   -29.499 -19.034 1.00 54.92 ? 119 GLN B NE2 1 
ATOM   1051 N N   . MET B 2 30  ? 1.546   -28.048 -13.506 1.00 23.90 ? 120 MET B N   1 
ATOM   1052 C CA  . MET B 2 30  ? 0.480   -28.567 -12.663 1.00 28.81 ? 120 MET B CA  1 
ATOM   1053 C C   . MET B 2 30  ? -0.601  -27.516 -12.482 1.00 25.08 ? 120 MET B C   1 
ATOM   1054 O O   . MET B 2 30  ? -0.333  -26.315 -12.532 1.00 24.22 ? 120 MET B O   1 
ATOM   1055 C CB  . MET B 2 30  ? 1.005   -28.939 -11.283 1.00 27.82 ? 120 MET B CB  1 
ATOM   1056 C CG  . MET B 2 30  ? 2.236   -29.769 -11.354 1.00 38.82 ? 120 MET B CG  1 
ATOM   1057 S SD  . MET B 2 30  ? 1.719   -31.451 -11.299 1.00 36.85 ? 120 MET B SD  1 
ATOM   1058 C CE  . MET B 2 30  ? 1.529   -31.539 -9.544  1.00 25.59 ? 120 MET B CE  1 
ATOM   1059 N N   . CYS B 2 31  ? -1.813  -27.985 -12.195 1.00 22.35 ? 121 CYS B N   1 
ATOM   1060 C CA  . CYS B 2 31  ? -2.826  -27.102 -11.624 1.00 24.91 ? 121 CYS B CA  1 
ATOM   1061 C C   . CYS B 2 31  ? -2.474  -26.797 -10.168 1.00 24.30 ? 121 CYS B C   1 
ATOM   1062 O O   . CYS B 2 31  ? -2.199  -27.712 -9.384  1.00 24.56 ? 121 CYS B O   1 
ATOM   1063 C CB  . CYS B 2 31  ? -4.212  -27.738 -11.703 1.00 24.47 ? 121 CYS B CB  1 
ATOM   1064 S SG  . CYS B 2 31  ? -4.872  -27.930 -13.370 1.00 31.78 ? 121 CYS B SG  1 
ATOM   1065 N N   . CYS B 2 32  ? -2.494  -25.509 -9.812  1.00 21.17 ? 122 CYS B N   1 
ATOM   1066 C CA  . CYS B 2 32  ? -2.095  -25.006 -8.499  1.00 19.17 ? 122 CYS B CA  1 
ATOM   1067 C C   . CYS B 2 32  ? -3.143  -24.016 -7.997  1.00 20.23 ? 122 CYS B C   1 
ATOM   1068 O O   . CYS B 2 32  ? -3.851  -23.406 -8.792  1.00 20.60 ? 122 CYS B O   1 
ATOM   1069 C CB  . CYS B 2 32  ? -0.719  -24.301 -8.571  1.00 21.77 ? 122 CYS B CB  1 
ATOM   1070 S SG  . CYS B 2 32  ? 0.585   -25.461 -9.031  1.00 34.46 ? 122 CYS B SG  1 
ATOM   1071 N N   . SER B 2 33  ? -3.230  -23.842 -6.676  1.00 21.02 ? 123 SER B N   1 
ATOM   1072 C CA  . SER B 2 33  ? -4.211  -22.913 -6.116  1.00 21.59 ? 123 SER B CA  1 
ATOM   1073 C C   . SER B 2 33  ? -3.842  -21.460 -6.414  1.00 18.10 ? 123 SER B C   1 
ATOM   1074 O O   . SER B 2 33  ? -2.680  -21.059 -6.309  1.00 15.20 ? 123 SER B O   1 
ATOM   1075 C CB  . SER B 2 33  ? -4.321  -23.096 -4.595  1.00 26.27 ? 123 SER B CB  1 
ATOM   1076 O OG  . SER B 2 33  ? -4.818  -24.371 -4.227  1.00 26.72 ? 123 SER B OG  1 
ATOM   1077 N N   . LYS B 2 34  ? -4.843  -20.668 -6.791  1.00 17.25 ? 124 LYS B N   1 
ATOM   1078 C CA  . LYS B 2 34  ? -4.695  -19.225 -6.732  1.00 16.94 ? 124 LYS B CA  1 
ATOM   1079 C C   . LYS B 2 34  ? -4.941  -18.755 -5.305  1.00 18.30 ? 124 LYS B C   1 
ATOM   1080 O O   . LYS B 2 34  ? -5.512  -19.474 -4.479  1.00 18.70 ? 124 LYS B O   1 
ATOM   1081 C CB  . LYS B 2 34  ? -5.669  -18.524 -7.689  1.00 19.91 ? 124 LYS B CB  1 
ATOM   1082 C CG  . LYS B 2 34  ? -5.353  -18.723 -9.168  1.00 18.69 ? 124 LYS B CG  1 
ATOM   1083 C CD  . LYS B 2 34  ? -6.145  -17.740 -10.040 1.00 24.29 ? 124 LYS B CD  1 
ATOM   1084 C CE  . LYS B 2 34  ? -7.335  -18.381 -10.711 1.00 30.14 ? 124 LYS B CE  1 
ATOM   1085 N NZ  . LYS B 2 34  ? -8.593  -18.244 -9.942  1.00 33.54 ? 124 LYS B NZ  1 
ATOM   1086 N N   . CYS B 2 35  ? -4.491  -17.540 -5.018  1.00 17.72 ? 125 CYS B N   1 
ATOM   1087 C CA  . CYS B 2 35  ? -4.727  -16.898 -3.738  1.00 15.74 ? 125 CYS B CA  1 
ATOM   1088 C C   . CYS B 2 35  ? -5.901  -15.939 -3.875  1.00 17.67 ? 125 CYS B C   1 
ATOM   1089 O O   . CYS B 2 35  ? -6.109  -15.340 -4.933  1.00 18.82 ? 125 CYS B O   1 
ATOM   1090 C CB  . CYS B 2 35  ? -3.483  -16.134 -3.285  1.00 17.61 ? 125 CYS B CB  1 
ATOM   1091 S SG  . CYS B 2 35  ? -2.026  -17.228 -3.138  1.00 20.95 ? 125 CYS B SG  1 
ATOM   1092 N N   . SER B 2 36  ? -6.619  -15.748 -2.790  1.00 16.30 ? 126 SER B N   1 
ATOM   1093 C CA  . SER B 2 36  ? -7.810  -14.917 -2.850  1.00 16.84 ? 126 SER B CA  1 
ATOM   1094 C C   . SER B 2 36  ? -7.451  -13.435 -2.896  1.00 17.52 ? 126 SER B C   1 
ATOM   1095 O O   . SER B 2 36  ? -6.333  -13.040 -2.558  1.00 17.29 ? 126 SER B O   1 
ATOM   1096 C CB  . SER B 2 36  ? -8.700  -15.185 -1.643  1.00 21.19 ? 126 SER B CB  1 
ATOM   1097 O OG  . SER B 2 36  ? -8.039  -14.847 -0.449  1.00 29.95 ? 126 SER B OG  1 
ATOM   1098 N N   . PRO B 2 37  ? -8.395  -12.590 -3.296  1.00 20.63 ? 127 PRO B N   1 
ATOM   1099 C CA  . PRO B 2 37  ? -8.225  -11.148 -3.075  1.00 18.20 ? 127 PRO B CA  1 
ATOM   1100 C C   . PRO B 2 37  ? -7.910  -10.884 -1.610  1.00 16.22 ? 127 PRO B C   1 
ATOM   1101 O O   . PRO B 2 37  ? -8.510  -11.476 -0.715  1.00 18.29 ? 127 PRO B O   1 
ATOM   1102 C CB  . PRO B 2 37  ? -9.587  -10.568 -3.482  1.00 16.53 ? 127 PRO B CB  1 
ATOM   1103 C CG  . PRO B 2 37  ? -10.113 -11.545 -4.486  1.00 19.83 ? 127 PRO B CG  1 
ATOM   1104 C CD  . PRO B 2 37  ? -9.679  -12.898 -3.953  1.00 18.59 ? 127 PRO B CD  1 
ATOM   1105 N N   . GLY B 2 38  ? -6.943  -10.000 -1.361  1.00 15.20 ? 128 GLY B N   1 
ATOM   1106 C CA  . GLY B 2 38  ? -6.459  -9.768  -0.017  1.00 16.78 ? 128 GLY B CA  1 
ATOM   1107 C C   . GLY B 2 38  ? -5.284  -10.634 0.393   1.00 20.14 ? 128 GLY B C   1 
ATOM   1108 O O   . GLY B 2 38  ? -4.703  -10.397 1.459   1.00 17.00 ? 128 GLY B O   1 
ATOM   1109 N N   . GLN B 2 39  ? -4.917  -11.624 -0.420  1.00 14.75 ? 129 GLN B N   1 
ATOM   1110 C CA  . GLN B 2 39  ? -3.750  -12.463 -0.189  1.00 16.08 ? 129 GLN B CA  1 
ATOM   1111 C C   . GLN B 2 39  ? -2.861  -12.472 -1.432  1.00 19.22 ? 129 GLN B C   1 
ATOM   1112 O O   . GLN B 2 39  ? -3.265  -12.054 -2.520  1.00 17.28 ? 129 GLN B O   1 
ATOM   1113 C CB  . GLN B 2 39  ? -4.179  -13.900 0.152   1.00 19.88 ? 129 GLN B CB  1 
ATOM   1114 C CG  . GLN B 2 39  ? -5.063  -14.028 1.409   1.00 19.68 ? 129 GLN B CG  1 
ATOM   1115 C CD  . GLN B 2 39  ? -5.551  -15.464 1.604   1.00 30.83 ? 129 GLN B CD  1 
ATOM   1116 O OE1 . GLN B 2 39  ? -4.826  -16.412 1.316   1.00 26.73 ? 129 GLN B OE1 1 
ATOM   1117 N NE2 . GLN B 2 39  ? -6.792  -15.625 2.065   1.00 28.01 ? 129 GLN B NE2 1 
ATOM   1118 N N   . HIS B 2 40  ? -1.647  -13.008 -1.285  1.00 16.79 ? 130 HIS B N   1 
ATOM   1119 C CA  . HIS B 2 40  ? -0.754  -13.189 -2.426  1.00 18.64 ? 130 HIS B CA  1 
ATOM   1120 C C   . HIS B 2 40  ? -0.017  -14.522 -2.297  1.00 18.20 ? 130 HIS B C   1 
ATOM   1121 O O   . HIS B 2 40  ? -0.041  -15.176 -1.245  1.00 17.62 ? 130 HIS B O   1 
ATOM   1122 C CB  . HIS B 2 40  ? 0.252   -12.038 -2.519  1.00 16.69 ? 130 HIS B CB  1 
ATOM   1123 C CG  . HIS B 2 40  ? 1.247   -12.047 -1.403  1.00 20.96 ? 130 HIS B CG  1 
ATOM   1124 N ND1 . HIS B 2 40  ? 2.555   -12.448 -1.576  1.00 21.63 ? 130 HIS B ND1 1 
ATOM   1125 C CD2 . HIS B 2 40  ? 1.113   -11.750 -0.088  1.00 20.08 ? 130 HIS B CD2 1 
ATOM   1126 C CE1 . HIS B 2 40  ? 3.189   -12.380 -0.418  1.00 21.13 ? 130 HIS B CE1 1 
ATOM   1127 N NE2 . HIS B 2 40  ? 2.339   -11.959 0.500   1.00 22.72 ? 130 HIS B NE2 1 
ATOM   1128 N N   . ALA B 2 41  ? 0.665   -14.918 -3.375  1.00 14.40 ? 131 ALA B N   1 
ATOM   1129 C CA  . ALA B 2 41  ? 1.466   -16.145 -3.377  1.00 17.96 ? 131 ALA B CA  1 
ATOM   1130 C C   . ALA B 2 41  ? 2.803   -15.867 -2.692  1.00 19.64 ? 131 ALA B C   1 
ATOM   1131 O O   . ALA B 2 41  ? 3.738   -15.361 -3.312  1.00 18.85 ? 131 ALA B O   1 
ATOM   1132 C CB  . ALA B 2 41  ? 1.669   -16.651 -4.803  1.00 16.95 ? 131 ALA B CB  1 
ATOM   1133 N N   . LYS B 2 42  ? 2.893   -16.169 -1.395  1.00 19.96 ? 132 LYS B N   1 
ATOM   1134 C CA  . LYS B 2 42  ? 4.177   -16.072 -0.706  1.00 20.87 ? 132 LYS B CA  1 
ATOM   1135 C C   . LYS B 2 42  ? 5.181   -17.090 -1.251  1.00 24.88 ? 132 LYS B C   1 
ATOM   1136 O O   . LYS B 2 42  ? 6.380   -16.794 -1.341  1.00 18.67 ? 132 LYS B O   1 
ATOM   1137 C CB  . LYS B 2 42  ? 3.976   -16.269 0.800   1.00 18.49 ? 132 LYS B CB  1 
ATOM   1138 C CG  . LYS B 2 42  ? 5.288   -16.424 1.582   1.00 24.18 ? 132 LYS B CG  1 
ATOM   1139 C CD  . LYS B 2 42  ? 6.043   -15.095 1.657   1.00 27.95 ? 132 LYS B CD  1 
ATOM   1140 C CE  . LYS B 2 42  ? 7.360   -15.243 2.414   1.00 28.38 ? 132 LYS B CE  1 
ATOM   1141 N NZ  . LYS B 2 42  ? 8.108   -13.942 2.413   1.00 37.11 ? 132 LYS B NZ  1 
ATOM   1142 N N   . VAL B 2 43  ? 4.714   -18.299 -1.592  1.00 19.06 ? 133 VAL B N   1 
ATOM   1143 C CA  . VAL B 2 43  ? 5.534   -19.359 -2.185  1.00 22.81 ? 133 VAL B CA  1 
ATOM   1144 C C   . VAL B 2 43  ? 4.783   -19.950 -3.371  1.00 19.50 ? 133 VAL B C   1 
ATOM   1145 O O   . VAL B 2 43  ? 3.615   -20.326 -3.239  1.00 20.43 ? 133 VAL B O   1 
ATOM   1146 C CB  . VAL B 2 43  ? 5.873   -20.480 -1.178  1.00 21.12 ? 133 VAL B CB  1 
ATOM   1147 C CG1 . VAL B 2 43  ? 6.926   -21.402 -1.759  1.00 23.84 ? 133 VAL B CG1 1 
ATOM   1148 C CG2 . VAL B 2 43  ? 6.335   -19.900 0.149   1.00 22.47 ? 133 VAL B CG2 1 
ATOM   1149 N N   . PHE B 2 44  ? 5.445   -20.024 -4.527  1.00 19.13 ? 134 PHE B N   1 
ATOM   1150 C CA  . PHE B 2 44  ? 4.835   -20.654 -5.692  1.00 19.72 ? 134 PHE B CA  1 
ATOM   1151 C C   . PHE B 2 44  ? 4.746   -22.170 -5.499  1.00 23.11 ? 134 PHE B C   1 
ATOM   1152 O O   . PHE B 2 44  ? 5.536   -22.778 -4.773  1.00 20.43 ? 134 PHE B O   1 
ATOM   1153 C CB  . PHE B 2 44  ? 5.637   -20.339 -6.963  1.00 20.52 ? 134 PHE B CB  1 
ATOM   1154 C CG  . PHE B 2 44  ? 5.603   -18.875 -7.379  1.00 26.28 ? 134 PHE B CG  1 
ATOM   1155 C CD1 . PHE B 2 44  ? 4.395   -18.211 -7.564  1.00 23.06 ? 134 PHE B CD1 1 
ATOM   1156 C CD2 . PHE B 2 44  ? 6.785   -18.179 -7.604  1.00 25.05 ? 134 PHE B CD2 1 
ATOM   1157 C CE1 . PHE B 2 44  ? 4.371   -16.875 -7.959  1.00 22.66 ? 134 PHE B CE1 1 
ATOM   1158 C CE2 . PHE B 2 44  ? 6.767   -16.833 -7.995  1.00 24.39 ? 134 PHE B CE2 1 
ATOM   1159 C CZ  . PHE B 2 44  ? 5.560   -16.185 -8.175  1.00 23.81 ? 134 PHE B CZ  1 
ATOM   1160 N N   . CYS B 2 45  ? 3.772   -22.787 -6.164  1.00 22.09 ? 135 CYS B N   1 
ATOM   1161 C CA  . CYS B 2 45  ? 3.641   -24.237 -6.083  1.00 24.27 ? 135 CYS B CA  1 
ATOM   1162 C C   . CYS B 2 45  ? 4.772   -24.928 -6.830  1.00 24.84 ? 135 CYS B C   1 
ATOM   1163 O O   . CYS B 2 45  ? 5.353   -24.377 -7.770  1.00 21.59 ? 135 CYS B O   1 
ATOM   1164 C CB  . CYS B 2 45  ? 2.323   -24.699 -6.682  1.00 17.92 ? 135 CYS B CB  1 
ATOM   1165 S SG  . CYS B 2 45  ? 2.251   -24.438 -8.481  1.00 24.61 ? 135 CYS B SG  1 
ATOM   1166 N N   . THR B 2 46  ? 5.062   -26.157 -6.412  1.00 24.07 ? 136 THR B N   1 
ATOM   1167 C CA  . THR B 2 46  ? 5.970   -27.070 -7.096  1.00 24.71 ? 136 THR B CA  1 
ATOM   1168 C C   . THR B 2 46  ? 5.182   -28.316 -7.502  1.00 26.85 ? 136 THR B C   1 
ATOM   1169 O O   . THR B 2 46  ? 3.953   -28.364 -7.385  1.00 22.03 ? 136 THR B O   1 
ATOM   1170 C CB  . THR B 2 46  ? 7.150   -27.432 -6.198  1.00 22.65 ? 136 THR B CB  1 
ATOM   1171 O OG1 . THR B 2 46  ? 6.673   -28.257 -5.132  1.00 26.82 ? 136 THR B OG1 1 
ATOM   1172 C CG2 . THR B 2 46  ? 7.780   -26.173 -5.617  1.00 28.47 ? 136 THR B CG2 1 
ATOM   1173 N N   . LYS B 2 47  ? 5.895   -29.347 -7.963  1.00 24.92 ? 137 LYS B N   1 
ATOM   1174 C CA  . LYS B 2 47  ? 5.201   -30.582 -8.312  1.00 26.83 ? 137 LYS B CA  1 
ATOM   1175 C C   . LYS B 2 47  ? 4.647   -31.312 -7.093  1.00 23.90 ? 137 LYS B C   1 
ATOM   1176 O O   . LYS B 2 47  ? 3.763   -32.168 -7.243  1.00 24.42 ? 137 LYS B O   1 
ATOM   1177 C CB  . LYS B 2 47  ? 6.127   -31.505 -9.105  1.00 27.81 ? 137 LYS B CB  1 
ATOM   1178 C CG  . LYS B 2 47  ? 6.471   -30.976 -10.501 1.00 33.87 ? 137 LYS B CG  1 
ATOM   1179 C CD  . LYS B 2 47  ? 7.305   -31.981 -11.305 1.00 39.29 ? 137 LYS B CD  1 
ATOM   1180 C CE  . LYS B 2 47  ? 7.511   -31.510 -12.743 1.00 41.85 ? 137 LYS B CE  1 
ATOM   1181 N NZ  . LYS B 2 47  ? 6.219   -31.405 -13.503 1.00 42.18 ? 137 LYS B NZ  1 
ATOM   1182 N N   . THR B 2 48  ? 5.115   -30.994 -5.887  1.00 19.31 ? 138 THR B N   1 
ATOM   1183 C CA  . THR B 2 48  ? 4.650   -31.708 -4.712  1.00 25.29 ? 138 THR B CA  1 
ATOM   1184 C C   . THR B 2 48  ? 4.044   -30.838 -3.619  1.00 28.00 ? 138 THR B C   1 
ATOM   1185 O O   . THR B 2 48  ? 3.465   -31.395 -2.678  1.00 32.25 ? 138 THR B O   1 
ATOM   1186 C CB  . THR B 2 48  ? 5.793   -32.544 -4.109  1.00 27.69 ? 138 THR B CB  1 
ATOM   1187 O OG1 . THR B 2 48  ? 6.977   -31.741 -4.021  1.00 28.59 ? 138 THR B OG1 1 
ATOM   1188 C CG2 . THR B 2 48  ? 6.063   -33.773 -4.981  1.00 26.40 ? 138 THR B CG2 1 
ATOM   1189 N N   . SER B 2 49  ? 4.138   -29.507 -3.707  1.00 28.33 ? 139 SER B N   1 
ATOM   1190 C CA  A SER B 2 49  ? 3.545   -28.621 -2.713  0.36 26.56 ? 139 SER B CA  1 
ATOM   1191 C CA  B SER B 2 49  ? 3.549   -28.617 -2.713  0.20 26.47 ? 139 SER B CA  1 
ATOM   1192 C CA  C SER B 2 49  ? 3.557   -28.612 -2.713  0.44 26.31 ? 139 SER B CA  1 
ATOM   1193 C C   . SER B 2 49  ? 2.726   -27.543 -3.412  1.00 23.41 ? 139 SER B C   1 
ATOM   1194 O O   . SER B 2 49  ? 3.094   -27.069 -4.486  1.00 21.62 ? 139 SER B O   1 
ATOM   1195 C CB  A SER B 2 49  ? 4.619   -27.977 -1.816  0.36 26.73 ? 139 SER B CB  1 
ATOM   1196 C CB  B SER B 2 49  ? 4.629   -27.966 -1.833  0.20 26.85 ? 139 SER B CB  1 
ATOM   1197 C CB  C SER B 2 49  ? 4.647   -27.951 -1.854  0.44 26.59 ? 139 SER B CB  1 
ATOM   1198 O OG  A SER B 2 49  ? 5.535   -27.202 -2.569  0.36 25.95 ? 139 SER B OG  1 
ATOM   1199 O OG  B SER B 2 49  ? 5.512   -27.167 -2.600  0.20 25.76 ? 139 SER B OG  1 
ATOM   1200 O OG  C SER B 2 49  ? 4.077   -27.128 -0.855  0.44 25.07 ? 139 SER B OG  1 
ATOM   1201 N N   . ASP B 2 50  ? 1.605   -27.173 -2.794  1.00 23.21 ? 140 ASP B N   1 
ATOM   1202 C CA  . ASP B 2 50  ? 0.697   -26.170 -3.342  1.00 22.80 ? 140 ASP B CA  1 
ATOM   1203 C C   . ASP B 2 50  ? 1.205   -24.762 -3.035  1.00 21.81 ? 140 ASP B C   1 
ATOM   1204 O O   . ASP B 2 50  ? 2.102   -24.563 -2.210  1.00 20.94 ? 140 ASP B O   1 
ATOM   1205 C CB  . ASP B 2 50  ? -0.706  -26.356 -2.764  1.00 24.20 ? 140 ASP B CB  1 
ATOM   1206 C CG  . ASP B 2 50  ? -1.800  -25.806 -3.665  1.00 24.09 ? 140 ASP B CG  1 
ATOM   1207 O OD1 . ASP B 2 50  ? -1.505  -25.372 -4.802  1.00 21.38 ? 140 ASP B OD1 1 
ATOM   1208 O OD2 . ASP B 2 50  ? -2.969  -25.825 -3.230  1.00 24.89 ? 140 ASP B OD2 1 
ATOM   1209 N N   . THR B 2 51  ? 0.632   -23.782 -3.742  1.00 18.71 ? 141 THR B N   1 
ATOM   1210 C CA  . THR B 2 51  ? 0.838   -22.367 -3.436  1.00 18.80 ? 141 THR B CA  1 
ATOM   1211 C C   . THR B 2 51  ? 0.685   -22.121 -1.941  1.00 18.74 ? 141 THR B C   1 
ATOM   1212 O O   . THR B 2 51  ? -0.188  -22.705 -1.293  1.00 19.32 ? 141 THR B O   1 
ATOM   1213 C CB  . THR B 2 51  ? -0.194  -21.510 -4.184  1.00 17.87 ? 141 THR B CB  1 
ATOM   1214 O OG1 . THR B 2 51  ? -0.312  -21.935 -5.548  1.00 16.18 ? 141 THR B OG1 1 
ATOM   1215 C CG2 . THR B 2 51  ? 0.179   -20.001 -4.140  1.00 17.35 ? 141 THR B CG2 1 
ATOM   1216 N N   . VAL B 2 52  ? 1.544   -21.273 -1.387  1.00 15.02 ? 142 VAL B N   1 
ATOM   1217 C CA  . VAL B 2 52  ? 1.359   -20.757 -0.030  1.00 18.48 ? 142 VAL B CA  1 
ATOM   1218 C C   . VAL B 2 52  ? 0.845   -19.325 -0.147  1.00 19.12 ? 142 VAL B C   1 
ATOM   1219 O O   . VAL B 2 52  ? 1.532   -18.462 -0.703  1.00 17.47 ? 142 VAL B O   1 
ATOM   1220 C CB  . VAL B 2 52  ? 2.659   -20.808 0.787   1.00 20.37 ? 142 VAL B CB  1 
ATOM   1221 C CG1 . VAL B 2 52  ? 2.453   -20.158 2.172   1.00 20.98 ? 142 VAL B CG1 1 
ATOM   1222 C CG2 . VAL B 2 52  ? 3.155   -22.260 0.936   1.00 23.89 ? 142 VAL B CG2 1 
ATOM   1223 N N   . CYS B 2 53  ? -0.363  -19.075 0.360   1.00 14.71 ? 143 CYS B N   1 
ATOM   1224 C CA  . CYS B 2 53  ? -1.001  -17.767 0.278   1.00 19.98 ? 143 CYS B CA  1 
ATOM   1225 C C   . CYS B 2 53  ? -0.948  -17.074 1.635   1.00 22.86 ? 143 CYS B C   1 
ATOM   1226 O O   . CYS B 2 53  ? -1.382  -17.649 2.641   1.00 22.52 ? 143 CYS B O   1 
ATOM   1227 C CB  . CYS B 2 53  ? -2.456  -17.909 -0.187  1.00 18.83 ? 143 CYS B CB  1 
ATOM   1228 S SG  . CYS B 2 53  ? -2.657  -18.654 -1.823  1.00 22.69 ? 143 CYS B SG  1 
ATOM   1229 N N   . ASP B 2 54  ? -0.431  -15.839 1.661   1.00 17.34 ? 144 ASP B N   1 
ATOM   1230 C CA  . ASP B 2 54  ? -0.369  -15.026 2.869   1.00 21.69 ? 144 ASP B CA  1 
ATOM   1231 C C   . ASP B 2 54  ? -1.125  -13.715 2.677   1.00 20.85 ? 144 ASP B C   1 
ATOM   1232 O O   . ASP B 2 54  ? -1.293  -13.226 1.562   1.00 19.87 ? 144 ASP B O   1 
ATOM   1233 C CB  . ASP B 2 54  ? 1.079   -14.720 3.268   1.00 22.51 ? 144 ASP B CB  1 
ATOM   1234 C CG  . ASP B 2 54  ? 1.804   -15.945 3.784   1.00 26.40 ? 144 ASP B CG  1 
ATOM   1235 O OD1 . ASP B 2 54  ? 1.162   -17.014 3.895   1.00 29.65 ? 144 ASP B OD1 1 
ATOM   1236 O OD2 . ASP B 2 54  ? 3.013   -15.849 4.072   1.00 27.89 ? 144 ASP B OD2 1 
ATOM   1237 N N   . SER B 2 55  ? -1.549  -13.131 3.790   1.00 19.07 ? 145 SER B N   1 
ATOM   1238 C CA  . SER B 2 55  ? -2.345  -11.909 3.743   1.00 21.18 ? 145 SER B CA  1 
ATOM   1239 C C   . SER B 2 55  ? -1.523  -10.712 3.287   1.00 21.14 ? 145 SER B C   1 
ATOM   1240 O O   . SER B 2 55  ? -0.338  -10.593 3.610   1.00 20.04 ? 145 SER B O   1 
ATOM   1241 C CB  . SER B 2 55  ? -2.944  -11.630 5.121   1.00 19.06 ? 145 SER B CB  1 
ATOM   1242 O OG  . SER B 2 55  ? -3.951  -12.584 5.402   1.00 32.78 ? 145 SER B OG  1 
ATOM   1243 N N   . CYS B 2 56  ? -2.161  -9.813  2.534   1.00 18.09 ? 146 CYS B N   1 
ATOM   1244 C CA  . CYS B 2 56  ? -1.550  -8.524  2.227   1.00 20.78 ? 146 CYS B CA  1 
ATOM   1245 C C   . CYS B 2 56  ? -1.388  -7.677  3.488   1.00 27.34 ? 146 CYS B C   1 
ATOM   1246 O O   . CYS B 2 56  ? -2.221  -7.702  4.399   1.00 23.66 ? 146 CYS B O   1 
ATOM   1247 C CB  . CYS B 2 56  ? -2.402  -7.742  1.217   1.00 20.27 ? 146 CYS B CB  1 
ATOM   1248 S SG  . CYS B 2 56  ? -2.560  -8.504  -0.386  1.00 21.19 ? 146 CYS B SG  1 
ATOM   1249 N N   . GLU B 2 57  ? -0.307  -6.907  3.520   1.00 27.70 ? 147 GLU B N   1 
ATOM   1250 C CA  . GLU B 2 57  ? -0.054  -5.928  4.567   1.00 34.88 ? 147 GLU B CA  1 
ATOM   1251 C C   . GLU B 2 57  ? -0.766  -4.607  4.251   1.00 32.24 ? 147 GLU B C   1 
ATOM   1252 O O   . GLU B 2 57  ? -1.074  -4.296  3.098   1.00 25.47 ? 147 GLU B O   1 
ATOM   1253 C CB  . GLU B 2 57  ? 1.456   -5.707  4.712   1.00 38.46 ? 147 GLU B CB  1 
ATOM   1254 C CG  . GLU B 2 57  ? 1.879   -4.855  5.892   1.00 56.38 ? 147 GLU B CG  1 
ATOM   1255 C CD  . GLU B 2 57  ? 2.175   -5.683  7.127   1.00 72.37 ? 147 GLU B CD  1 
ATOM   1256 O OE1 . GLU B 2 57  ? 2.784   -6.771  6.987   1.00 57.73 ? 147 GLU B OE1 1 
ATOM   1257 O OE2 . GLU B 2 57  ? 1.792   -5.244  8.235   1.00 92.64 ? 147 GLU B OE2 1 
ATOM   1258 N N   . ASP B 2 58  ? -1.033  -3.834  5.305   1.00 29.94 ? 148 ASP B N   1 
ATOM   1259 C CA  . ASP B 2 58  ? -1.692  -2.540  5.164   1.00 34.02 ? 148 ASP B CA  1 
ATOM   1260 C C   . ASP B 2 58  ? -0.969  -1.668  4.134   1.00 28.13 ? 148 ASP B C   1 
ATOM   1261 O O   . ASP B 2 58  ? 0.263   -1.650  4.069   1.00 27.74 ? 148 ASP B O   1 
ATOM   1262 C CB  . ASP B 2 58  ? -1.744  -1.858  6.537   1.00 37.15 ? 148 ASP B CB  1 
ATOM   1263 C CG  . ASP B 2 58  ? -2.425  -0.507  6.502   1.00 49.20 ? 148 ASP B CG  1 
ATOM   1264 O OD1 . ASP B 2 58  ? -3.647  -0.453  6.215   1.00 48.79 ? 148 ASP B OD1 1 
ATOM   1265 O OD2 . ASP B 2 58  ? -1.736  0.503   6.781   1.00 51.38 ? 148 ASP B OD2 1 
ATOM   1266 N N   . SER B 2 59  ? -1.759  -0.980  3.301   1.00 23.08 ? 149 SER B N   1 
ATOM   1267 C CA  . SER B 2 59  ? -1.361  -0.114  2.169   1.00 25.56 ? 149 SER B CA  1 
ATOM   1268 C C   . SER B 2 59  ? -0.969  -0.910  0.927   1.00 25.20 ? 149 SER B C   1 
ATOM   1269 O O   . SER B 2 59  ? -0.434  -0.322  -0.035  1.00 21.40 ? 149 SER B O   1 
ATOM   1270 C CB  . SER B 2 59  ? -0.220  0.853   2.506   1.00 30.00 ? 149 SER B CB  1 
ATOM   1271 O OG  . SER B 2 59  ? 1.010   0.156   2.661   1.00 36.28 ? 149 SER B OG  1 
ATOM   1272 N N   . THR B 2 60  ? -1.202  -2.218  0.910   1.00 22.21 ? 150 THR B N   1 
ATOM   1273 C CA  . THR B 2 60  ? -1.049  -3.054  -0.277  1.00 19.37 ? 150 THR B CA  1 
ATOM   1274 C C   . THR B 2 60  ? -2.358  -3.803  -0.501  1.00 20.92 ? 150 THR B C   1 
ATOM   1275 O O   . THR B 2 60  ? -3.197  -3.884  0.399   1.00 20.40 ? 150 THR B O   1 
ATOM   1276 C CB  . THR B 2 60  ? 0.111   -4.055  -0.133  1.00 21.41 ? 150 THR B CB  1 
ATOM   1277 O OG1 . THR B 2 60  ? -0.240  -5.073  0.817   1.00 20.08 ? 150 THR B OG1 1 
ATOM   1278 C CG2 . THR B 2 60  ? 1.379   -3.344  0.322   1.00 23.23 ? 150 THR B CG2 1 
ATOM   1279 N N   . TYR B 2 61  ? -2.525  -4.387  -1.692  1.00 15.48 ? 151 TYR B N   1 
ATOM   1280 C CA  . TYR B 2 61  ? -3.806  -4.995  -2.025  1.00 18.78 ? 151 TYR B CA  1 
ATOM   1281 C C   . TYR B 2 61  ? -3.631  -6.012  -3.150  1.00 17.34 ? 151 TYR B C   1 
ATOM   1282 O O   . TYR B 2 61  ? -2.645  -5.988  -3.886  1.00 18.53 ? 151 TYR B O   1 
ATOM   1283 C CB  . TYR B 2 61  ? -4.832  -3.925  -2.437  1.00 16.76 ? 151 TYR B CB  1 
ATOM   1284 C CG  . TYR B 2 61  ? -4.586  -3.390  -3.835  1.00 17.82 ? 151 TYR B CG  1 
ATOM   1285 C CD1 . TYR B 2 61  ? -3.643  -2.400  -4.056  1.00 17.33 ? 151 TYR B CD1 1 
ATOM   1286 C CD2 . TYR B 2 61  ? -5.268  -3.905  -4.934  1.00 18.69 ? 151 TYR B CD2 1 
ATOM   1287 C CE1 . TYR B 2 61  ? -3.392  -1.924  -5.333  1.00 20.33 ? 151 TYR B CE1 1 
ATOM   1288 C CE2 . TYR B 2 61  ? -5.015  -3.448  -6.214  1.00 24.76 ? 151 TYR B CE2 1 
ATOM   1289 C CZ  . TYR B 2 61  ? -4.086  -2.441  -6.401  1.00 23.71 ? 151 TYR B CZ  1 
ATOM   1290 O OH  . TYR B 2 61  ? -3.841  -1.966  -7.665  1.00 23.34 ? 151 TYR B OH  1 
ATOM   1291 N N   . THR B 2 62  ? -4.617  -6.902  -3.279  1.00 16.84 ? 152 THR B N   1 
ATOM   1292 C CA  . THR B 2 62  ? -4.802  -7.676  -4.505  1.00 15.36 ? 152 THR B CA  1 
ATOM   1293 C C   . THR B 2 62  ? -6.295  -7.725  -4.769  1.00 19.27 ? 152 THR B C   1 
ATOM   1294 O O   . THR B 2 62  ? -7.063  -8.043  -3.864  1.00 16.21 ? 152 THR B O   1 
ATOM   1295 C CB  . THR B 2 62  ? -4.235  -9.107  -4.410  1.00 16.05 ? 152 THR B CB  1 
ATOM   1296 O OG1 . THR B 2 62  ? -4.782  -9.784  -3.271  1.00 16.21 ? 152 THR B OG1 1 
ATOM   1297 C CG2 . THR B 2 62  ? -2.704  -9.092  -4.307  1.00 15.55 ? 152 THR B CG2 1 
ATOM   1298 N N   . GLN B 2 63  ? -6.707  -7.387  -5.985  1.00 16.74 ? 153 GLN B N   1 
ATOM   1299 C CA  . GLN B 2 63  ? -8.125  -7.220  -6.263  1.00 23.66 ? 153 GLN B CA  1 
ATOM   1300 C C   . GLN B 2 63  ? -8.762  -8.482  -6.818  1.00 25.03 ? 153 GLN B C   1 
ATOM   1301 O O   . GLN B 2 63  ? -9.985  -8.648  -6.708  1.00 23.70 ? 153 GLN B O   1 
ATOM   1302 C CB  . GLN B 2 63  ? -8.335  -6.053  -7.241  1.00 24.00 ? 153 GLN B CB  1 
ATOM   1303 C CG  . GLN B 2 63  ? -9.360  -5.042  -6.758  1.00 35.88 ? 153 GLN B CG  1 
ATOM   1304 C CD  . GLN B 2 63  ? -9.369  -3.741  -7.571  1.00 58.97 ? 153 GLN B CD  1 
ATOM   1305 O OE1 . GLN B 2 63  ? -8.843  -2.689  -7.139  1.00 37.87 ? 153 GLN B OE1 1 
ATOM   1306 N NE2 . GLN B 2 63  ? -9.981  -3.805  -8.751  1.00 58.67 ? 153 GLN B NE2 1 
ATOM   1307 N N   . LEU B 2 64  ? -7.959  -9.372  -7.386  1.00 22.73 ? 154 LEU B N   1 
ATOM   1308 C CA  . LEU B 2 64  ? -8.422  -10.564 -8.062  1.00 20.42 ? 154 LEU B CA  1 
ATOM   1309 C C   . LEU B 2 64  ? -7.801  -11.787 -7.403  1.00 21.56 ? 154 LEU B C   1 
ATOM   1310 O O   . LEU B 2 64  ? -6.789  -11.691 -6.698  1.00 17.61 ? 154 LEU B O   1 
ATOM   1311 C CB  . LEU B 2 64  ? -8.051  -10.515 -9.555  1.00 20.70 ? 154 LEU B CB  1 
ATOM   1312 C CG  . LEU B 2 64  ? -8.623  -9.349  -10.373 1.00 29.27 ? 154 LEU B CG  1 
ATOM   1313 C CD1 . LEU B 2 64  ? -8.110  -9.333  -11.811 1.00 28.66 ? 154 LEU B CD1 1 
ATOM   1314 C CD2 . LEU B 2 64  ? -10.134 -9.409  -10.359 1.00 27.88 ? 154 LEU B CD2 1 
ATOM   1315 N N   . TRP B 2 65  ? -8.438  -12.940 -7.615  1.00 18.26 ? 155 TRP B N   1 
ATOM   1316 C CA  . TRP B 2 65  ? -7.754  -14.213 -7.403  1.00 19.01 ? 155 TRP B CA  1 
ATOM   1317 C C   . TRP B 2 65  ? -6.462  -14.217 -8.223  1.00 19.67 ? 155 TRP B C   1 
ATOM   1318 O O   . TRP B 2 65  ? -6.459  -13.837 -9.398  1.00 18.35 ? 155 TRP B O   1 
ATOM   1319 C CB  . TRP B 2 65  ? -8.676  -15.377 -7.792  1.00 19.00 ? 155 TRP B CB  1 
ATOM   1320 C CG  . TRP B 2 65  ? -9.763  -15.628 -6.741  1.00 19.96 ? 155 TRP B CG  1 
ATOM   1321 C CD1 . TRP B 2 65  ? -10.965 -14.988 -6.617  1.00 23.24 ? 155 TRP B CD1 1 
ATOM   1322 C CD2 . TRP B 2 65  ? -9.704  -16.577 -5.658  1.00 22.21 ? 155 TRP B CD2 1 
ATOM   1323 N NE1 . TRP B 2 65  ? -11.660 -15.491 -5.529  1.00 19.22 ? 155 TRP B NE1 1 
ATOM   1324 C CE2 . TRP B 2 65  ? -10.909 -16.468 -4.931  1.00 17.78 ? 155 TRP B CE2 1 
ATOM   1325 C CE3 . TRP B 2 65  ? -8.749  -17.514 -5.241  1.00 17.05 ? 155 TRP B CE3 1 
ATOM   1326 C CZ2 . TRP B 2 65  ? -11.181 -17.258 -3.813  1.00 20.35 ? 155 TRP B CZ2 1 
ATOM   1327 C CZ3 . TRP B 2 65  ? -9.020  -18.294 -4.127  1.00 18.82 ? 155 TRP B CZ3 1 
ATOM   1328 C CH2 . TRP B 2 65  ? -10.230 -18.159 -3.428  1.00 20.12 ? 155 TRP B CH2 1 
ATOM   1329 N N   . ASN B 2 66  ? -5.349  -14.598 -7.592  1.00 18.64 ? 156 ASN B N   1 
ATOM   1330 C CA  . ASN B 2 66  ? -4.049  -14.209 -8.136  1.00 18.57 ? 156 ASN B CA  1 
ATOM   1331 C C   . ASN B 2 66  ? -2.967  -15.205 -7.738  1.00 20.06 ? 156 ASN B C   1 
ATOM   1332 O O   . ASN B 2 66  ? -3.157  -16.071 -6.877  1.00 19.96 ? 156 ASN B O   1 
ATOM   1333 C CB  . ASN B 2 66  ? -3.652  -12.802 -7.643  1.00 15.06 ? 156 ASN B CB  1 
ATOM   1334 C CG  . ASN B 2 66  ? -3.275  -12.798 -6.146  1.00 19.44 ? 156 ASN B CG  1 
ATOM   1335 O OD1 . ASN B 2 66  ? -2.129  -13.069 -5.781  1.00 20.40 ? 156 ASN B OD1 1 
ATOM   1336 N ND2 . ASN B 2 66  ? -4.248  -12.526 -5.288  1.00 15.59 ? 156 ASN B ND2 1 
ATOM   1337 N N   . TRP B 2 67  ? -1.804  -15.044 -8.361  1.00 15.75 ? 157 TRP B N   1 
ATOM   1338 C CA  . TRP B 2 67  ? -0.587  -15.655 -7.863  1.00 16.88 ? 157 TRP B CA  1 
ATOM   1339 C C   . TRP B 2 67  ? 0.585   -14.681 -8.009  1.00 20.33 ? 157 TRP B C   1 
ATOM   1340 O O   . TRP B 2 67  ? 1.661   -15.043 -8.486  1.00 17.00 ? 157 TRP B O   1 
ATOM   1341 C CB  . TRP B 2 67  ? -0.328  -16.985 -8.570  1.00 16.73 ? 157 TRP B CB  1 
ATOM   1342 C CG  . TRP B 2 67  ? -0.468  -16.971 -10.064 1.00 20.92 ? 157 TRP B CG  1 
ATOM   1343 C CD1 . TRP B 2 67  ? -1.631  -16.907 -10.782 1.00 24.34 ? 157 TRP B CD1 1 
ATOM   1344 C CD2 . TRP B 2 67  ? 0.589   -17.072 -11.024 1.00 24.88 ? 157 TRP B CD2 1 
ATOM   1345 N NE1 . TRP B 2 67  ? -1.356  -16.944 -12.127 1.00 27.48 ? 157 TRP B NE1 1 
ATOM   1346 C CE2 . TRP B 2 67  ? -0.001  -17.044 -12.301 1.00 25.21 ? 157 TRP B CE2 1 
ATOM   1347 C CE3 . TRP B 2 67  ? 1.978   -17.194 -10.926 1.00 24.52 ? 157 TRP B CE3 1 
ATOM   1348 C CZ2 . TRP B 2 67  ? 0.748   -17.131 -13.470 1.00 29.27 ? 157 TRP B CZ2 1 
ATOM   1349 C CZ3 . TRP B 2 67  ? 2.717   -17.267 -12.086 1.00 30.79 ? 157 TRP B CZ3 1 
ATOM   1350 C CH2 . TRP B 2 67  ? 2.102   -17.236 -13.341 1.00 26.99 ? 157 TRP B CH2 1 
ATOM   1351 N N   . VAL B 2 68  ? 0.399   -13.430 -7.575  1.00 18.81 ? 158 VAL B N   1 
ATOM   1352 C CA  . VAL B 2 68  ? 1.507   -12.473 -7.547  1.00 15.37 ? 158 VAL B CA  1 
ATOM   1353 C C   . VAL B 2 68  ? 2.421   -12.743 -6.356  1.00 19.44 ? 158 VAL B C   1 
ATOM   1354 O O   . VAL B 2 68  ? 1.951   -13.139 -5.276  1.00 18.28 ? 158 VAL B O   1 
ATOM   1355 C CB  . VAL B 2 68  ? 1.023   -11.008 -7.526  1.00 20.57 ? 158 VAL B CB  1 
ATOM   1356 C CG1 . VAL B 2 68  ? 0.418   -10.633 -8.875  1.00 18.65 ? 158 VAL B CG1 1 
ATOM   1357 C CG2 . VAL B 2 68  ? 0.056   -10.760 -6.364  1.00 17.34 ? 158 VAL B CG2 1 
ATOM   1358 N N   . PRO B 2 69  ? 3.732   -12.535 -6.512  1.00 18.91 ? 159 PRO B N   1 
ATOM   1359 C CA  . PRO B 2 69  ? 4.680   -12.847 -5.429  1.00 18.41 ? 159 PRO B CA  1 
ATOM   1360 C C   . PRO B 2 69  ? 4.646   -11.878 -4.266  1.00 19.74 ? 159 PRO B C   1 
ATOM   1361 O O   . PRO B 2 69  ? 5.246   -12.186 -3.228  1.00 19.70 ? 159 PRO B O   1 
ATOM   1362 C CB  . PRO B 2 69  ? 6.044   -12.786 -6.134  1.00 19.30 ? 159 PRO B CB  1 
ATOM   1363 C CG  . PRO B 2 69  ? 5.806   -11.824 -7.290  1.00 16.99 ? 159 PRO B CG  1 
ATOM   1364 C CD  . PRO B 2 69  ? 4.414   -12.150 -7.759  1.00 17.39 ? 159 PRO B CD  1 
ATOM   1365 N N   . GLU B 2 70  ? 4.010   -10.716 -4.427  1.00 19.07 ? 160 GLU B N   1 
ATOM   1366 C CA  . GLU B 2 70  ? 3.856   -9.695  -3.403  1.00 21.25 ? 160 GLU B CA  1 
ATOM   1367 C C   . GLU B 2 70  ? 2.576   -8.929  -3.724  1.00 21.78 ? 160 GLU B C   1 
ATOM   1368 O O   . GLU B 2 70  ? 2.168   -8.860  -4.884  1.00 21.28 ? 160 GLU B O   1 
ATOM   1369 C CB  . GLU B 2 70  ? 5.047   -8.721  -3.372  1.00 23.84 ? 160 GLU B CB  1 
ATOM   1370 C CG  . GLU B 2 70  ? 6.126   -9.023  -2.342  1.00 37.59 ? 160 GLU B CG  1 
ATOM   1371 C CD  . GLU B 2 70  ? 7.266   -7.996  -2.343  1.00 33.06 ? 160 GLU B CD  1 
ATOM   1372 O OE1 . GLU B 2 70  ? 7.031   -6.817  -2.695  1.00 34.97 ? 160 GLU B OE1 1 
ATOM   1373 O OE2 . GLU B 2 70  ? 8.409   -8.372  -1.993  1.00 32.62 ? 160 GLU B OE2 1 
ATOM   1374 N N   . CYS B 2 71  ? 1.944   -8.343  -2.716  1.00 18.88 ? 161 CYS B N   1 
ATOM   1375 C CA  . CYS B 2 71  ? 0.748   -7.566  -3.052  1.00 24.33 ? 161 CYS B CA  1 
ATOM   1376 C C   . CYS B 2 71  ? 1.148   -6.251  -3.723  1.00 16.90 ? 161 CYS B C   1 
ATOM   1377 O O   . CYS B 2 71  ? 2.277   -5.768  -3.570  1.00 20.59 ? 161 CYS B O   1 
ATOM   1378 C CB  . CYS B 2 71  ? -0.115  -7.295  -1.811  1.00 19.35 ? 161 CYS B CB  1 
ATOM   1379 S SG  . CYS B 2 71  ? -0.633  -8.829  -0.945  1.00 22.88 ? 161 CYS B SG  1 
ATOM   1380 N N   . LEU B 2 72  ? 0.213   -5.681  -4.490  1.00 18.09 ? 162 LEU B N   1 
ATOM   1381 C CA  . LEU B 2 72  ? 0.459   -4.404  -5.162  1.00 15.20 ? 162 LEU B CA  1 
ATOM   1382 C C   . LEU B 2 72  ? 0.329   -3.248  -4.180  1.00 20.04 ? 162 LEU B C   1 
ATOM   1383 O O   . LEU B 2 72  ? -0.470  -3.292  -3.242  1.00 17.69 ? 162 LEU B O   1 
ATOM   1384 C CB  . LEU B 2 72  ? -0.523  -4.167  -6.317  1.00 20.05 ? 162 LEU B CB  1 
ATOM   1385 C CG  . LEU B 2 72  ? -0.866  -5.242  -7.360  1.00 29.95 ? 162 LEU B CG  1 
ATOM   1386 C CD1 . LEU B 2 72  ? -1.453  -4.602  -8.632  1.00 25.89 ? 162 LEU B CD1 1 
ATOM   1387 C CD2 . LEU B 2 72  ? 0.330   -6.079  -7.689  1.00 25.02 ? 162 LEU B CD2 1 
ATOM   1388 N N   . SER B 2 73  ? 1.099   -2.186  -4.415  1.00 16.83 ? 163 SER B N   1 
ATOM   1389 C CA  . SER B 2 73  ? 0.984   -1.009  -3.567  1.00 18.73 ? 163 SER B CA  1 
ATOM   1390 C C   . SER B 2 73  ? -0.272  -0.233  -3.929  1.00 18.47 ? 163 SER B C   1 
ATOM   1391 O O   . SER B 2 73  ? -0.551  -0.017  -5.113  1.00 16.95 ? 163 SER B O   1 
ATOM   1392 C CB  . SER B 2 73  ? 2.210   -0.111  -3.720  1.00 19.16 ? 163 SER B CB  1 
ATOM   1393 O OG  . SER B 2 73  ? 3.398   -0.866  -3.522  1.00 21.28 ? 163 SER B OG  1 
ATOM   1394 N N   . CYS B 2 74  ? -1.025  0.193   -2.911  1.00 16.04 ? 164 CYS B N   1 
ATOM   1395 C CA  . CYS B 2 74  ? -2.042  1.223   -3.133  1.00 20.09 ? 164 CYS B CA  1 
ATOM   1396 C C   . CYS B 2 74  ? -1.407  2.524   -3.613  1.00 17.60 ? 164 CYS B C   1 
ATOM   1397 O O   . CYS B 2 74  ? -0.256  2.838   -3.287  1.00 17.72 ? 164 CYS B O   1 
ATOM   1398 C CB  . CYS B 2 74  ? -2.826  1.505   -1.855  1.00 19.29 ? 164 CYS B CB  1 
ATOM   1399 S SG  . CYS B 2 74  ? -4.042  0.222   -1.439  1.00 24.15 ? 164 CYS B SG  1 
ATOM   1400 N N   . GLY B 2 75  ? -2.163  3.273   -4.421  1.00 19.04 ? 165 GLY B N   1 
ATOM   1401 C CA  . GLY B 2 75  ? -1.784  4.642   -4.727  1.00 16.95 ? 165 GLY B CA  1 
ATOM   1402 C C   . GLY B 2 75  ? -1.646  5.475   -3.463  1.00 19.76 ? 165 GLY B C   1 
ATOM   1403 O O   . GLY B 2 75  ? -2.172  5.130   -2.404  1.00 19.22 ? 165 GLY B O   1 
ATOM   1404 N N   . SER B 2 76  ? -0.891  6.572   -3.554  1.00 16.66 ? 166 SER B N   1 
ATOM   1405 C CA  A SER B 2 76  ? -0.655  7.362   -2.355  0.37 23.03 ? 166 SER B CA  1 
ATOM   1406 C CA  B SER B 2 76  ? -0.651  7.390   -2.371  0.63 23.26 ? 166 SER B CA  1 
ATOM   1407 C C   . SER B 2 76  ? -1.962  7.969   -1.856  1.00 21.08 ? 166 SER B C   1 
ATOM   1408 O O   . SER B 2 76  ? -2.926  8.134   -2.603  1.00 19.54 ? 166 SER B O   1 
ATOM   1409 C CB  A SER B 2 76  ? 0.376   8.459   -2.618  0.37 21.26 ? 166 SER B CB  1 
ATOM   1410 C CB  B SER B 2 76  ? 0.320   8.529   -2.682  0.63 21.15 ? 166 SER B CB  1 
ATOM   1411 O OG  A SER B 2 76  ? 1.663   7.899   -2.798  0.37 22.28 ? 166 SER B OG  1 
ATOM   1412 O OG  B SER B 2 76  ? -0.310  9.500   -3.503  0.63 23.94 ? 166 SER B OG  1 
ATOM   1413 N N   . ARG B 2 77  ? -1.988  8.284   -0.560  1.00 23.18 ? 167 ARG B N   1 
ATOM   1414 C CA  . ARG B 2 77  ? -3.142  8.965   0.016   1.00 24.20 ? 167 ARG B CA  1 
ATOM   1415 C C   . ARG B 2 77  ? -3.424  10.258  -0.741  1.00 24.72 ? 167 ARG B C   1 
ATOM   1416 O O   . ARG B 2 77  ? -2.501  10.947  -1.182  1.00 23.10 ? 167 ARG B O   1 
ATOM   1417 C CB  . ARG B 2 77  ? -2.894  9.268   1.494   1.00 29.12 ? 167 ARG B CB  1 
ATOM   1418 C CG  . ARG B 2 77  ? -2.855  8.025   2.384   1.00 32.88 ? 167 ARG B CG  1 
ATOM   1419 C CD  . ARG B 2 77  ? -2.888  8.401   3.860   1.00 43.40 ? 167 ARG B CD  1 
ATOM   1420 N NE  . ARG B 2 77  ? -2.452  7.296   4.705   1.00 54.38 ? 167 ARG B NE  1 
ATOM   1421 C CZ  . ARG B 2 77  ? -3.268  6.479   5.356   1.00 66.76 ? 167 ARG B CZ  1 
ATOM   1422 N NH1 . ARG B 2 77  ? -4.582  6.647   5.328   1.00 61.42 ? 167 ARG B NH1 1 
ATOM   1423 N NH2 . ARG B 2 77  ? -2.754  5.466   6.053   1.00 69.73 ? 167 ARG B NH2 1 
ATOM   1424 N N   . CYS B 2 78  ? -4.709  10.592  -0.881  1.00 20.76 ? 168 CYS B N   1 
ATOM   1425 C CA  . CYS B 2 78  ? -5.100  11.758  -1.664  1.00 23.87 ? 168 CYS B CA  1 
ATOM   1426 C C   . CYS B 2 78  ? -4.639  13.032  -0.966  1.00 29.15 ? 168 CYS B C   1 
ATOM   1427 O O   . CYS B 2 78  ? -4.533  13.085  0.261   1.00 26.85 ? 168 CYS B O   1 
ATOM   1428 C CB  . CYS B 2 78  ? -6.622  11.792  -1.866  1.00 19.71 ? 168 CYS B CB  1 
ATOM   1429 S SG  . CYS B 2 78  ? -7.346  10.193  -2.404  1.00 30.99 ? 168 CYS B SG  1 
ATOM   1430 N N   . SER B 2 79  ? -4.337  14.056  -1.759  1.00 20.67 ? 169 SER B N   1 
ATOM   1431 C CA  . SER B 2 79  ? -4.039  15.346  -1.155  1.00 27.45 ? 169 SER B CA  1 
ATOM   1432 C C   . SER B 2 79  ? -5.340  16.075  -0.812  1.00 31.05 ? 169 SER B C   1 
ATOM   1433 O O   . SER B 2 79  ? -6.436  15.658  -1.196  1.00 24.64 ? 169 SER B O   1 
ATOM   1434 C CB  . SER B 2 79  ? -3.165  16.187  -2.091  1.00 29.10 ? 169 SER B CB  1 
ATOM   1435 O OG  . SER B 2 79  ? -3.803  16.421  -3.336  1.00 28.48 ? 169 SER B OG  1 
ATOM   1436 N N   . SER B 2 80  ? -5.212  17.184  -0.071  1.00 26.28 ? 170 SER B N   1 
ATOM   1437 C CA  . SER B 2 80  ? -6.400  17.872  0.428   1.00 31.34 ? 170 SER B CA  1 
ATOM   1438 C C   . SER B 2 80  ? -7.249  18.452  -0.698  1.00 32.63 ? 170 SER B C   1 
ATOM   1439 O O   . SER B 2 80  ? -8.452  18.661  -0.499  1.00 39.78 ? 170 SER B O   1 
ATOM   1440 C CB  . SER B 2 80  ? -6.008  18.977  1.429   1.00 30.79 ? 170 SER B CB  1 
ATOM   1441 O OG  . SER B 2 80  ? -5.057  19.875  0.880   1.00 36.12 ? 170 SER B OG  1 
ATOM   1442 N N   . ASP B 2 81  ? -6.660  18.697  -1.876  1.00 31.80 ? 171 ASP B N   1 
ATOM   1443 C CA  . ASP B 2 81  ? -7.437  19.151  -3.023  1.00 34.72 ? 171 ASP B CA  1 
ATOM   1444 C C   . ASP B 2 81  ? -8.398  18.077  -3.525  1.00 36.51 ? 171 ASP B C   1 
ATOM   1445 O O   . ASP B 2 81  ? -9.432  18.401  -4.124  1.00 34.40 ? 171 ASP B O   1 
ATOM   1446 C CB  . ASP B 2 81  ? -6.511  19.562  -4.164  1.00 34.34 ? 171 ASP B CB  1 
ATOM   1447 C CG  . ASP B 2 81  ? -5.902  20.938  -3.959  1.00 46.06 ? 171 ASP B CG  1 
ATOM   1448 O OD1 . ASP B 2 81  ? -6.450  21.736  -3.157  1.00 42.43 ? 171 ASP B OD1 1 
ATOM   1449 O OD2 . ASP B 2 81  ? -4.874  21.216  -4.612  1.00 47.75 ? 171 ASP B OD2 1 
ATOM   1450 N N   . GLN B 2 82  ? -8.082  16.811  -3.290  1.00 29.09 ? 172 GLN B N   1 
ATOM   1451 C CA  . GLN B 2 82  ? -8.777  15.703  -3.920  1.00 23.04 ? 172 GLN B CA  1 
ATOM   1452 C C   . GLN B 2 82  ? -9.836  15.124  -2.995  1.00 27.72 ? 172 GLN B C   1 
ATOM   1453 O O   . GLN B 2 82  ? -9.913  15.446  -1.810  1.00 28.67 ? 172 GLN B O   1 
ATOM   1454 C CB  . GLN B 2 82  ? -7.775  14.607  -4.320  1.00 20.88 ? 172 GLN B CB  1 
ATOM   1455 C CG  . GLN B 2 82  ? -6.706  15.073  -5.278  1.00 26.56 ? 172 GLN B CG  1 
ATOM   1456 C CD  . GLN B 2 82  ? -5.649  14.010  -5.518  1.00 31.43 ? 172 GLN B CD  1 
ATOM   1457 O OE1 . GLN B 2 82  ? -5.015  13.536  -4.580  1.00 30.50 ? 172 GLN B OE1 1 
ATOM   1458 N NE2 . GLN B 2 82  ? -5.469  13.620  -6.773  1.00 37.86 ? 172 GLN B NE2 1 
ATOM   1459 N N   . VAL B 2 83  ? -10.645 14.230  -3.557  1.00 22.88 ? 173 VAL B N   1 
ATOM   1460 C CA  . VAL B 2 83  ? -11.631 13.461  -2.812  1.00 26.49 ? 173 VAL B CA  1 
ATOM   1461 C C   . VAL B 2 83  ? -11.286 11.990  -2.979  1.00 26.08 ? 173 VAL B C   1 
ATOM   1462 O O   . VAL B 2 83  ? -11.080 11.528  -4.106  1.00 24.34 ? 173 VAL B O   1 
ATOM   1463 C CB  . VAL B 2 83  ? -13.061 13.725  -3.314  1.00 26.57 ? 173 VAL B CB  1 
ATOM   1464 C CG1 . VAL B 2 83  ? -14.055 12.953  -2.477  1.00 32.95 ? 173 VAL B CG1 1 
ATOM   1465 C CG2 . VAL B 2 83  ? -13.371 15.201  -3.297  1.00 33.43 ? 173 VAL B CG2 1 
ATOM   1466 N N   . GLU B 2 84  ? -11.233 11.258  -1.871  1.00 20.78 ? 174 GLU B N   1 
ATOM   1467 C CA  . GLU B 2 84  ? -10.970 9.820   -1.932  1.00 26.63 ? 174 GLU B CA  1 
ATOM   1468 C C   . GLU B 2 84  ? -12.301 9.128   -2.188  1.00 28.21 ? 174 GLU B C   1 
ATOM   1469 O O   . GLU B 2 84  ? -13.128 9.004   -1.284  1.00 36.31 ? 174 GLU B O   1 
ATOM   1470 C CB  . GLU B 2 84  ? -10.321 9.317   -0.648  1.00 25.53 ? 174 GLU B CB  1 
ATOM   1471 C CG  . GLU B 2 84  ? -9.993  7.817   -0.717  1.00 28.29 ? 174 GLU B CG  1 
ATOM   1472 C CD  . GLU B 2 84  ? -9.567  7.242   0.615   1.00 33.11 ? 174 GLU B CD  1 
ATOM   1473 O OE1 . GLU B 2 84  ? -10.457 6.933   1.433   1.00 35.21 ? 174 GLU B OE1 1 
ATOM   1474 O OE2 . GLU B 2 84  ? -8.347  7.087   0.844   1.00 32.43 ? 174 GLU B OE2 1 
ATOM   1475 N N   . THR B 2 85  ? -12.520 8.678   -3.420  1.00 25.08 ? 175 THR B N   1 
ATOM   1476 C CA  . THR B 2 85  ? -13.782 8.037   -3.749  1.00 28.39 ? 175 THR B CA  1 
ATOM   1477 C C   . THR B 2 85  ? -13.747 6.529   -3.555  1.00 30.77 ? 175 THR B C   1 
ATOM   1478 O O   . THR B 2 85  ? -14.798 5.897   -3.620  1.00 28.09 ? 175 THR B O   1 
ATOM   1479 C CB  . THR B 2 85  ? -14.193 8.349   -5.190  1.00 33.05 ? 175 THR B CB  1 
ATOM   1480 O OG1 . THR B 2 85  ? -13.109 8.066   -6.081  1.00 35.82 ? 175 THR B OG1 1 
ATOM   1481 C CG2 . THR B 2 85  ? -14.601 9.809   -5.331  1.00 34.75 ? 175 THR B CG2 1 
ATOM   1482 N N   . GLN B 2 86  ? -12.576 5.943   -3.326  1.00 26.93 ? 176 GLN B N   1 
ATOM   1483 C CA  . GLN B 2 86  ? -12.467 4.537   -2.957  1.00 27.49 ? 176 GLN B CA  1 
ATOM   1484 C C   . GLN B 2 86  ? -11.296 4.377   -2.000  1.00 24.79 ? 176 GLN B C   1 
ATOM   1485 O O   . GLN B 2 86  ? -10.186 4.834   -2.291  1.00 25.52 ? 176 GLN B O   1 
ATOM   1486 C CB  . GLN B 2 86  ? -12.280 3.658   -4.194  1.00 23.11 ? 176 GLN B CB  1 
ATOM   1487 C CG  . GLN B 2 86  ? -12.062 2.185   -3.910  1.00 26.41 ? 176 GLN B CG  1 
ATOM   1488 C CD  . GLN B 2 86  ? -12.249 1.365   -5.165  1.00 26.41 ? 176 GLN B CD  1 
ATOM   1489 O OE1 . GLN B 2 86  ? -13.349 1.295   -5.700  1.00 27.16 ? 176 GLN B OE1 1 
ATOM   1490 N NE2 . GLN B 2 86  ? -11.170 0.773   -5.666  1.00 26.87 ? 176 GLN B NE2 1 
ATOM   1491 N N   . ALA B 2 87  ? -11.547 3.744   -0.859  1.00 25.04 ? 177 ALA B N   1 
ATOM   1492 C CA  . ALA B 2 87  ? -10.497 3.563   0.128   1.00 25.79 ? 177 ALA B CA  1 
ATOM   1493 C C   . ALA B 2 87  ? -9.531  2.452   -0.287  1.00 24.55 ? 177 ALA B C   1 
ATOM   1494 O O   . ALA B 2 87  ? -9.892  1.511   -0.998  1.00 22.78 ? 177 ALA B O   1 
ATOM   1495 C CB  . ALA B 2 87  ? -11.108 3.254   1.498   1.00 22.64 ? 177 ALA B CB  1 
ATOM   1496 N N   . CYS B 2 88  ? -8.286  2.580   0.160   1.00 20.31 ? 178 CYS B N   1 
ATOM   1497 C CA  . CYS B 2 88  ? -7.319  1.490   0.072   1.00 22.14 ? 178 CYS B CA  1 
ATOM   1498 C C   . CYS B 2 88  ? -7.685  0.430   1.106   1.00 23.72 ? 178 CYS B C   1 
ATOM   1499 O O   . CYS B 2 88  ? -7.766  0.734   2.302   1.00 24.26 ? 178 CYS B O   1 
ATOM   1500 C CB  . CYS B 2 88  ? -5.902  2.013   0.324   1.00 22.50 ? 178 CYS B CB  1 
ATOM   1501 S SG  . CYS B 2 88  ? -4.606  0.730   0.462   1.00 28.46 ? 178 CYS B SG  1 
ATOM   1502 N N   . THR B 2 89  ? -7.942  -0.798  0.650   1.00 20.21 ? 179 THR B N   1 
ATOM   1503 C CA  . THR B 2 89  ? -8.101  -1.953  1.531   1.00 18.98 ? 179 THR B CA  1 
ATOM   1504 C C   . THR B 2 89  ? -7.197  -3.060  1.014   1.00 20.46 ? 179 THR B C   1 
ATOM   1505 O O   . THR B 2 89  ? -6.591  -2.936  -0.053  1.00 19.90 ? 179 THR B O   1 
ATOM   1506 C CB  . THR B 2 89  ? -9.553  -2.445  1.582   1.00 20.39 ? 179 THR B CB  1 
ATOM   1507 O OG1 . THR B 2 89  ? -9.850  -3.118  0.358   1.00 23.61 ? 179 THR B OG1 1 
ATOM   1508 C CG2 . THR B 2 89  ? -10.526 -1.264  1.774   1.00 24.95 ? 179 THR B CG2 1 
ATOM   1509 N N   . ARG B 2 90  ? -7.144  -4.179  1.741   1.00 21.37 ? 180 ARG B N   1 
ATOM   1510 C CA  . ARG B 2 90  ? -6.350  -5.308  1.255   1.00 21.58 ? 180 ARG B CA  1 
ATOM   1511 C C   . ARG B 2 90  ? -6.884  -5.894  -0.044  1.00 19.42 ? 180 ARG B C   1 
ATOM   1512 O O   . ARG B 2 90  ? -6.163  -6.662  -0.700  1.00 19.16 ? 180 ARG B O   1 
ATOM   1513 C CB  . ARG B 2 90  ? -6.265  -6.404  2.330   1.00 24.06 ? 180 ARG B CB  1 
ATOM   1514 C CG  . ARG B 2 90  ? -5.893  -5.891  3.730   1.00 32.39 ? 180 ARG B CG  1 
ATOM   1515 C CD  . ARG B 2 90  ? -4.480  -5.300  3.847   1.00 33.63 ? 180 ARG B CD  1 
ATOM   1516 N NE  . ARG B 2 90  ? -4.238  -4.143  2.983   1.00 37.46 ? 180 ARG B NE  1 
ATOM   1517 C CZ  . ARG B 2 90  ? -4.624  -2.895  3.229   1.00 37.16 ? 180 ARG B CZ  1 
ATOM   1518 N NH1 . ARG B 2 90  ? -5.234  -2.561  4.364   1.00 35.42 ? 180 ARG B NH1 1 
ATOM   1519 N NH2 . ARG B 2 90  ? -4.399  -1.956  2.308   1.00 28.96 ? 180 ARG B NH2 1 
ATOM   1520 N N   . GLU B 2 91  ? -8.110  -5.543  -0.442  1.00 18.38 ? 181 GLU B N   1 
ATOM   1521 C CA  . GLU B 2 91  ? -8.729  -6.098  -1.637  1.00 19.02 ? 181 GLU B CA  1 
ATOM   1522 C C   . GLU B 2 91  ? -8.985  -5.072  -2.736  1.00 21.83 ? 181 GLU B C   1 
ATOM   1523 O O   . GLU B 2 91  ? -9.527  -5.445  -3.776  1.00 21.10 ? 181 GLU B O   1 
ATOM   1524 C CB  . GLU B 2 91  ? -10.061 -6.796  -1.287  1.00 22.65 ? 181 GLU B CB  1 
ATOM   1525 C CG  . GLU B 2 91  ? -9.955  -7.938  -0.291  1.00 24.69 ? 181 GLU B CG  1 
ATOM   1526 C CD  . GLU B 2 91  ? -9.943  -7.469  1.164   1.00 28.21 ? 181 GLU B CD  1 
ATOM   1527 O OE1 . GLU B 2 91  ? -10.521 -6.399  1.460   1.00 29.70 ? 181 GLU B OE1 1 
ATOM   1528 O OE2 . GLU B 2 91  ? -9.371  -8.187  2.015   1.00 33.21 ? 181 GLU B OE2 1 
ATOM   1529 N N   . GLN B 2 92  ? -8.635  -3.797  -2.547  1.00 18.90 ? 182 GLN B N   1 
ATOM   1530 C CA  . GLN B 2 92  ? -8.879  -2.815  -3.601  1.00 21.06 ? 182 GLN B CA  1 
ATOM   1531 C C   . GLN B 2 92  ? -7.914  -1.649  -3.448  1.00 20.58 ? 182 GLN B C   1 
ATOM   1532 O O   . GLN B 2 92  ? -7.516  -1.299  -2.332  1.00 18.16 ? 182 GLN B O   1 
ATOM   1533 C CB  . GLN B 2 92  ? -10.323 -2.290  -3.568  1.00 21.78 ? 182 GLN B CB  1 
ATOM   1534 C CG  . GLN B 2 92  ? -10.597 -1.447  -2.346  1.00 21.55 ? 182 GLN B CG  1 
ATOM   1535 C CD  . GLN B 2 92  ? -12.062 -1.081  -2.178  1.00 28.07 ? 182 GLN B CD  1 
ATOM   1536 O OE1 . GLN B 2 92  ? -12.951 -1.744  -2.710  1.00 28.62 ? 182 GLN B OE1 1 
ATOM   1537 N NE2 . GLN B 2 92  ? -12.314 -0.019  -1.420  1.00 22.70 ? 182 GLN B NE2 1 
ATOM   1538 N N   . ASN B 2 93  ? -7.573  -1.044  -4.591  1.00 18.36 ? 183 ASN B N   1 
ATOM   1539 C CA  . ASN B 2 93  ? -6.706  0.127   -4.672  1.00 19.63 ? 183 ASN B CA  1 
ATOM   1540 C C   . ASN B 2 93  ? -7.456  1.391   -4.243  1.00 23.31 ? 183 ASN B C   1 
ATOM   1541 O O   . ASN B 2 93  ? -8.689  1.472   -4.316  1.00 21.19 ? 183 ASN B O   1 
ATOM   1542 C CB  . ASN B 2 93  ? -6.175  0.299   -6.112  1.00 19.96 ? 183 ASN B CB  1 
ATOM   1543 C CG  . ASN B 2 93  ? -5.023  1.328   -6.222  1.00 21.63 ? 183 ASN B CG  1 
ATOM   1544 O OD1 . ASN B 2 93  ? -4.458  1.754   -5.224  1.00 21.83 ? 183 ASN B OD1 1 
ATOM   1545 N ND2 . ASN B 2 93  ? -4.694  1.729   -7.450  1.00 21.63 ? 183 ASN B ND2 1 
ATOM   1546 N N   . ARG B 2 94  ? -6.693  2.376   -3.776  1.00 19.08 ? 184 ARG B N   1 
ATOM   1547 C CA  . ARG B 2 94  ? -7.235  3.704   -3.508  1.00 24.20 ? 184 ARG B CA  1 
ATOM   1548 C C   . ARG B 2 94  ? -7.556  4.426   -4.815  1.00 23.62 ? 184 ARG B C   1 
ATOM   1549 O O   . ARG B 2 94  ? -6.840  4.281   -5.807  1.00 24.64 ? 184 ARG B O   1 
ATOM   1550 C CB  . ARG B 2 94  ? -6.217  4.526   -2.703  1.00 19.46 ? 184 ARG B CB  1 
ATOM   1551 C CG  . ARG B 2 94  ? -6.672  5.917   -2.353  1.00 24.92 ? 184 ARG B CG  1 
ATOM   1552 C CD  . ARG B 2 94  ? -5.681  6.571   -1.418  1.00 25.24 ? 184 ARG B CD  1 
ATOM   1553 N NE  . ARG B 2 94  ? -5.755  6.027   -0.066  1.00 24.81 ? 184 ARG B NE  1 
ATOM   1554 C CZ  . ARG B 2 94  ? -4.763  5.398   0.548   1.00 27.28 ? 184 ARG B CZ  1 
ATOM   1555 N NH1 . ARG B 2 94  ? -3.614  5.147   -0.067  1.00 20.02 ? 184 ARG B NH1 1 
ATOM   1556 N NH2 . ARG B 2 94  ? -4.913  5.043   1.821   1.00 23.27 ? 184 ARG B NH2 1 
ATOM   1557 N N   . ILE B 2 95  ? -8.634  5.212   -4.823  1.00 21.33 ? 185 ILE B N   1 
ATOM   1558 C CA  . ILE B 2 95  ? -8.968  6.037   -5.982  1.00 23.92 ? 185 ILE B CA  1 
ATOM   1559 C C   . ILE B 2 95  ? -9.207  7.466   -5.508  1.00 24.64 ? 185 ILE B C   1 
ATOM   1560 O O   . ILE B 2 95  ? -10.053 7.699   -4.636  1.00 18.96 ? 185 ILE B O   1 
ATOM   1561 C CB  . ILE B 2 95  ? -10.197 5.522   -6.743  1.00 24.24 ? 185 ILE B CB  1 
ATOM   1562 C CG1 . ILE B 2 95  ? -9.951  4.099   -7.264  1.00 28.45 ? 185 ILE B CG1 1 
ATOM   1563 C CG2 . ILE B 2 95  ? -10.521 6.471   -7.898  1.00 26.41 ? 185 ILE B CG2 1 
ATOM   1564 C CD1 . ILE B 2 95  ? -11.160 3.496   -7.943  1.00 26.23 ? 185 ILE B CD1 1 
ATOM   1565 N N   . CYS B 2 96  ? -8.462  8.413   -6.081  1.00 18.14 ? 186 CYS B N   1 
ATOM   1566 C CA  . CYS B 2 96  ? -8.592  9.837   -5.775  1.00 20.99 ? 186 CYS B CA  1 
ATOM   1567 C C   . CYS B 2 96  ? -9.175  10.561  -6.983  1.00 21.92 ? 186 CYS B C   1 
ATOM   1568 O O   . CYS B 2 96  ? -8.785  10.293  -8.123  1.00 23.06 ? 186 CYS B O   1 
ATOM   1569 C CB  . CYS B 2 96  ? -7.232  10.463  -5.419  1.00 20.81 ? 186 CYS B CB  1 
ATOM   1570 S SG  . CYS B 2 96  ? -6.296  9.649   -4.058  1.00 25.16 ? 186 CYS B SG  1 
ATOM   1571 N N   . THR B 2 97  ? -10.092 11.495  -6.734  1.00 24.88 ? 187 THR B N   1 
ATOM   1572 C CA  . THR B 2 97  ? -10.750 12.211  -7.813  1.00 24.12 ? 187 THR B CA  1 
ATOM   1573 C C   . THR B 2 97  ? -10.772 13.696  -7.500  1.00 27.73 ? 187 THR B C   1 
ATOM   1574 O O   . THR B 2 97  ? -10.500 14.129  -6.374  1.00 28.84 ? 187 THR B O   1 
ATOM   1575 C CB  . THR B 2 97  ? -12.179 11.702  -8.055  1.00 28.89 ? 187 THR B CB  1 
ATOM   1576 O OG1 . THR B 2 97  ? -12.966 11.909  -6.882  1.00 28.64 ? 187 THR B OG1 1 
ATOM   1577 C CG2 . THR B 2 97  ? -12.177 10.208  -8.403  1.00 31.05 ? 187 THR B CG2 1 
ATOM   1578 N N   . CYS B 2 98  ? -11.107 14.474  -8.521  1.00 24.59 ? 188 CYS B N   1 
ATOM   1579 C CA  . CYS B 2 98  ? -11.175 15.922  -8.415  1.00 23.19 ? 188 CYS B CA  1 
ATOM   1580 C C   . CYS B 2 98  ? -12.600 16.366  -8.106  1.00 26.70 ? 188 CYS B C   1 
ATOM   1581 O O   . CYS B 2 98  ? -13.567 15.700  -8.481  1.00 27.84 ? 188 CYS B O   1 
ATOM   1582 C CB  . CYS B 2 98  ? -10.693 16.569  -9.713  1.00 22.04 ? 188 CYS B CB  1 
ATOM   1583 S SG  . CYS B 2 98  ? -9.040  16.002  -10.195 1.00 28.32 ? 188 CYS B SG  1 
ATOM   1584 N N   . ARG B 2 99  ? -12.715 17.503  -7.406  1.00 24.85 ? 189 ARG B N   1 
ATOM   1585 C CA  . ARG B 2 99  ? -13.998 18.092  -7.046  1.00 26.99 ? 189 ARG B CA  1 
ATOM   1586 C C   . ARG B 2 99  ? -14.622 18.770  -8.261  1.00 26.76 ? 189 ARG B C   1 
ATOM   1587 O O   . ARG B 2 99  ? -13.921 19.093  -9.225  1.00 27.79 ? 189 ARG B O   1 
ATOM   1588 C CB  . ARG B 2 99  ? -13.803 19.097  -5.906  1.00 28.37 ? 189 ARG B CB  1 
ATOM   1589 C CG  . ARG B 2 99  ? -13.296 18.439  -4.627  1.00 32.71 ? 189 ARG B CG  1 
ATOM   1590 C CD  . ARG B 2 99  ? -12.973 19.412  -3.487  1.00 34.30 ? 189 ARG B CD  1 
ATOM   1591 N NE  . ARG B 2 99  ? -13.332 18.815  -2.202  1.00 37.71 ? 189 ARG B NE  1 
ATOM   1592 C CZ  . ARG B 2 99  ? -12.490 18.231  -1.357  1.00 41.34 ? 189 ARG B CZ  1 
ATOM   1593 N NH1 . ARG B 2 99  ? -11.181 18.220  -1.572  1.00 38.77 ? 189 ARG B NH1 1 
ATOM   1594 N NH2 . ARG B 2 99  ? -12.973 17.636  -0.268  1.00 43.93 ? 189 ARG B NH2 1 
ATOM   1595 N N   . PRO B 2 100 ? -15.948 18.972  -8.260  1.00 32.22 ? 190 PRO B N   1 
ATOM   1596 C CA  . PRO B 2 100 ? -16.556 19.788  -9.319  1.00 27.10 ? 190 PRO B CA  1 
ATOM   1597 C C   . PRO B 2 100 ? -15.897 21.161  -9.364  1.00 24.48 ? 190 PRO B C   1 
ATOM   1598 O O   . PRO B 2 100 ? -15.454 21.695  -8.346  1.00 22.98 ? 190 PRO B O   1 
ATOM   1599 C CB  . PRO B 2 100 ? -18.033 19.874  -8.907  1.00 33.46 ? 190 PRO B CB  1 
ATOM   1600 C CG  . PRO B 2 100 ? -18.267 18.642  -8.076  1.00 30.04 ? 190 PRO B CG  1 
ATOM   1601 C CD  . PRO B 2 100 ? -16.961 18.439  -7.325  1.00 33.65 ? 190 PRO B CD  1 
ATOM   1602 N N   . GLY B 2 101 ? -15.778 21.705  -10.567 1.00 24.41 ? 191 GLY B N   1 
ATOM   1603 C CA  . GLY B 2 101 ? -15.013 22.923  -10.749 1.00 25.74 ? 191 GLY B CA  1 
ATOM   1604 C C   . GLY B 2 101 ? -13.535 22.700  -10.957 1.00 24.33 ? 191 GLY B C   1 
ATOM   1605 O O   . GLY B 2 101 ? -12.792 23.675  -11.118 1.00 26.05 ? 191 GLY B O   1 
ATOM   1606 N N   . TRP B 2 102 ? -13.090 21.448  -10.957 1.00 21.83 ? 192 TRP B N   1 
ATOM   1607 C CA  . TRP B 2 102 ? -11.695 21.082  -11.144 1.00 24.47 ? 192 TRP B CA  1 
ATOM   1608 C C   . TRP B 2 102 ? -11.603 20.024  -12.236 1.00 21.74 ? 192 TRP B C   1 
ATOM   1609 O O   . TRP B 2 102 ? -12.560 19.300  -12.509 1.00 23.46 ? 192 TRP B O   1 
ATOM   1610 C CB  . TRP B 2 102 ? -11.068 20.522  -9.853  1.00 21.34 ? 192 TRP B CB  1 
ATOM   1611 C CG  . TRP B 2 102 ? -10.966 21.503  -8.708  1.00 24.56 ? 192 TRP B CG  1 
ATOM   1612 C CD1 . TRP B 2 102 ? -11.998 22.126  -8.062  1.00 24.23 ? 192 TRP B CD1 1 
ATOM   1613 C CD2 . TRP B 2 102 ? -9.764  21.947  -8.064  1.00 23.36 ? 192 TRP B CD2 1 
ATOM   1614 N NE1 . TRP B 2 102 ? -11.510 22.930  -7.060  1.00 27.50 ? 192 TRP B NE1 1 
ATOM   1615 C CE2 . TRP B 2 102 ? -10.143 22.839  -7.042  1.00 26.65 ? 192 TRP B CE2 1 
ATOM   1616 C CE3 . TRP B 2 102 ? -8.403  21.680  -8.258  1.00 24.48 ? 192 TRP B CE3 1 
ATOM   1617 C CZ2 . TRP B 2 102 ? -9.212  23.470  -6.221  1.00 25.84 ? 192 TRP B CZ2 1 
ATOM   1618 C CZ3 . TRP B 2 102 ? -7.484  22.294  -7.443  1.00 25.62 ? 192 TRP B CZ3 1 
ATOM   1619 C CH2 . TRP B 2 102 ? -7.889  23.184  -6.434  1.00 27.77 ? 192 TRP B CH2 1 
ATOM   1620 N N   . TYR B 2 103 ? -10.437 19.932  -12.861 1.00 21.45 ? 193 TYR B N   1 
ATOM   1621 C CA  . TYR B 2 103 ? -10.168 18.861  -13.804 1.00 24.90 ? 193 TYR B CA  1 
ATOM   1622 C C   . TYR B 2 103 ? -8.904  18.138  -13.368 1.00 24.74 ? 193 TYR B C   1 
ATOM   1623 O O   . TYR B 2 103 ? -8.120  18.644  -12.553 1.00 18.92 ? 193 TYR B O   1 
ATOM   1624 C CB  . TYR B 2 103 ? -10.025 19.378  -15.247 1.00 20.14 ? 193 TYR B CB  1 
ATOM   1625 C CG  . TYR B 2 103 ? -8.769  20.166  -15.500 1.00 25.10 ? 193 TYR B CG  1 
ATOM   1626 C CD1 . TYR B 2 103 ? -8.684  21.509  -15.140 1.00 24.91 ? 193 TYR B CD1 1 
ATOM   1627 C CD2 . TYR B 2 103 ? -7.659  19.573  -16.109 1.00 26.55 ? 193 TYR B CD2 1 
ATOM   1628 C CE1 . TYR B 2 103 ? -7.539  22.233  -15.365 1.00 24.03 ? 193 TYR B CE1 1 
ATOM   1629 C CE2 . TYR B 2 103 ? -6.507  20.298  -16.341 1.00 28.29 ? 193 TYR B CE2 1 
ATOM   1630 C CZ  . TYR B 2 103 ? -6.456  21.626  -15.965 1.00 27.20 ? 193 TYR B CZ  1 
ATOM   1631 O OH  . TYR B 2 103 ? -5.327  22.369  -16.182 1.00 27.46 ? 193 TYR B OH  1 
ATOM   1632 N N   . CYS B 2 104 ? -8.723  16.943  -13.919 1.00 23.38 ? 194 CYS B N   1 
ATOM   1633 C CA  . CYS B 2 104 ? -7.555  16.123  -13.619 1.00 23.21 ? 194 CYS B CA  1 
ATOM   1634 C C   . CYS B 2 104 ? -6.429  16.504  -14.574 1.00 22.15 ? 194 CYS B C   1 
ATOM   1635 O O   . CYS B 2 104 ? -6.490  16.202  -15.773 1.00 21.69 ? 194 CYS B O   1 
ATOM   1636 C CB  . CYS B 2 104 ? -7.886  14.640  -13.730 1.00 24.34 ? 194 CYS B CB  1 
ATOM   1637 S SG  . CYS B 2 104 ? -6.452  13.673  -13.212 1.00 29.53 ? 194 CYS B SG  1 
ATOM   1638 N N   . ALA B 2 105 ? -5.396  17.161  -14.042 1.00 21.62 ? 195 ALA B N   1 
ATOM   1639 C CA  . ALA B 2 105 ? -4.280  17.598  -14.878 1.00 22.11 ? 195 ALA B CA  1 
ATOM   1640 C C   . ALA B 2 105 ? -3.332  16.446  -15.211 1.00 24.58 ? 195 ALA B C   1 
ATOM   1641 O O   . ALA B 2 105 ? -2.814  16.368  -16.333 1.00 20.51 ? 195 ALA B O   1 
ATOM   1642 C CB  . ALA B 2 105 ? -3.512  18.732  -14.190 1.00 25.08 ? 195 ALA B CB  1 
ATOM   1643 N N   . LEU B 2 106 ? -3.061  15.572  -14.242 1.00 20.07 ? 196 LEU B N   1 
ATOM   1644 C CA  . LEU B 2 106 ? -2.290  14.344  -14.462 1.00 22.56 ? 196 LEU B CA  1 
ATOM   1645 C C   . LEU B 2 106 ? -3.184  13.161  -14.101 1.00 22.01 ? 196 LEU B C   1 
ATOM   1646 O O   . LEU B 2 106 ? -3.507  12.945  -12.923 1.00 21.10 ? 196 LEU B O   1 
ATOM   1647 C CB  . LEU B 2 106 ? -0.996  14.335  -13.641 1.00 23.38 ? 196 LEU B CB  1 
ATOM   1648 C CG  . LEU B 2 106 ? 0.032   15.403  -14.015 1.00 22.96 ? 196 LEU B CG  1 
ATOM   1649 C CD1 . LEU B 2 106 ? 1.136   15.464  -12.976 1.00 22.11 ? 196 LEU B CD1 1 
ATOM   1650 C CD2 . LEU B 2 106 ? 0.620   15.122  -15.393 1.00 18.35 ? 196 LEU B CD2 1 
ATOM   1651 N N   . SER B 2 107 ? -3.582  12.390  -15.108 1.00 19.71 ? 197 SER B N   1 
ATOM   1652 C CA  . SER B 2 107 ? -4.557  11.330  -14.912 1.00 22.22 ? 197 SER B CA  1 
ATOM   1653 C C   . SER B 2 107 ? -3.866  9.992   -14.660 1.00 28.92 ? 197 SER B C   1 
ATOM   1654 O O   . SER B 2 107 ? -2.798  9.711   -15.217 1.00 26.08 ? 197 SER B O   1 
ATOM   1655 C CB  . SER B 2 107 ? -5.480  11.246  -16.136 1.00 25.84 ? 197 SER B CB  1 
ATOM   1656 O OG  . SER B 2 107 ? -6.564  10.364  -15.917 1.00 37.81 ? 197 SER B OG  1 
ATOM   1657 N N   . LYS B 2 108 ? -4.474  9.183   -13.794 1.00 22.96 ? 198 LYS B N   1 
ATOM   1658 C CA  . LYS B 2 108 ? -4.098  7.788   -13.605 1.00 23.68 ? 198 LYS B CA  1 
ATOM   1659 C C   . LYS B 2 108 ? -5.074  6.893   -14.351 1.00 30.84 ? 198 LYS B C   1 
ATOM   1660 O O   . LYS B 2 108 ? -6.154  7.324   -14.775 1.00 28.80 ? 198 LYS B O   1 
ATOM   1661 C CB  . LYS B 2 108 ? -4.090  7.421   -12.120 1.00 21.40 ? 198 LYS B CB  1 
ATOM   1662 C CG  . LYS B 2 108 ? -3.193  8.289   -11.269 1.00 23.81 ? 198 LYS B CG  1 
ATOM   1663 C CD  . LYS B 2 108 ? -3.218  7.852   -9.812  1.00 25.31 ? 198 LYS B CD  1 
ATOM   1664 C CE  . LYS B 2 108 ? -2.612  6.455   -9.664  1.00 25.03 ? 198 LYS B CE  1 
ATOM   1665 N NZ  . LYS B 2 108 ? -2.628  6.002   -8.233  1.00 30.15 ? 198 LYS B NZ  1 
ATOM   1666 N N   . GLN B 2 109 ? -4.684  5.620   -14.491 1.00 25.43 ? 199 GLN B N   1 
ATOM   1667 C CA  . GLN B 2 109 ? -5.594  4.623   -15.044 1.00 32.84 ? 199 GLN B CA  1 
ATOM   1668 C C   . GLN B 2 109 ? -6.940  4.666   -14.335 1.00 31.48 ? 199 GLN B C   1 
ATOM   1669 O O   . GLN B 2 109 ? -7.991  4.656   -14.984 1.00 37.97 ? 199 GLN B O   1 
ATOM   1670 C CB  . GLN B 2 109 ? -4.969  3.225   -14.948 1.00 33.23 ? 199 GLN B CB  1 
ATOM   1671 C CG  . GLN B 2 109 ? -5.806  2.128   -15.607 1.00 38.98 ? 199 GLN B CG  1 
ATOM   1672 C CD  . GLN B 2 109 ? -4.974  0.939   -16.062 1.00 44.64 ? 199 GLN B CD  1 
ATOM   1673 O OE1 . GLN B 2 109 ? -4.060  0.503   -15.367 1.00 42.96 ? 199 GLN B OE1 1 
ATOM   1674 N NE2 . GLN B 2 109 ? -5.280  0.422   -17.246 1.00 49.94 ? 199 GLN B NE2 1 
ATOM   1675 N N   . GLU B 2 110 ? -6.926  4.749   -13.005 1.00 27.35 ? 200 GLU B N   1 
ATOM   1676 C CA  . GLU B 2 110 ? -8.119  5.029   -12.209 1.00 30.70 ? 200 GLU B CA  1 
ATOM   1677 C C   . GLU B 2 110 ? -7.880  6.281   -11.379 1.00 27.33 ? 200 GLU B C   1 
ATOM   1678 O O   . GLU B 2 110 ? -7.005  6.286   -10.507 1.00 30.93 ? 200 GLU B O   1 
ATOM   1679 C CB  . GLU B 2 110 ? -8.455  3.877   -11.262 1.00 34.35 ? 200 GLU B CB  1 
ATOM   1680 C CG  . GLU B 2 110 ? -8.677  2.524   -11.885 1.00 41.95 ? 200 GLU B CG  1 
ATOM   1681 C CD  . GLU B 2 110 ? -9.437  1.620   -10.946 1.00 42.95 ? 200 GLU B CD  1 
ATOM   1682 O OE1 . GLU B 2 110 ? -8.820  1.081   -9.996  1.00 44.82 ? 200 GLU B OE1 1 
ATOM   1683 O OE2 . GLU B 2 110 ? -10.666 1.485   -11.134 1.00 49.67 ? 200 GLU B OE2 1 
ATOM   1684 N N   . GLY B 2 111 ? -8.681  7.317   -11.606 1.00 29.46 ? 201 GLY B N   1 
ATOM   1685 C CA  . GLY B 2 111 ? -8.557  8.504   -10.786 1.00 25.36 ? 201 GLY B CA  1 
ATOM   1686 C C   . GLY B 2 111 ? -7.447  9.434   -11.249 1.00 26.64 ? 201 GLY B C   1 
ATOM   1687 O O   . GLY B 2 111 ? -7.019  9.430   -12.410 1.00 24.89 ? 201 GLY B O   1 
ATOM   1688 N N   . CYS B 2 112 ? -6.959  10.230  -10.298 1.00 26.27 ? 202 CYS B N   1 
ATOM   1689 C CA  . CYS B 2 112 ? -6.202  11.439  -10.589 1.00 22.84 ? 202 CYS B CA  1 
ATOM   1690 C C   . CYS B 2 112 ? -5.046  11.588  -9.612  1.00 23.39 ? 202 CYS B C   1 
ATOM   1691 O O   . CYS B 2 112 ? -5.214  11.330  -8.418  1.00 27.79 ? 202 CYS B O   1 
ATOM   1692 C CB  . CYS B 2 112 ? -7.118  12.666  -10.484 1.00 25.57 ? 202 CYS B CB  1 
ATOM   1693 S SG  . CYS B 2 112 ? -6.387  14.108  -11.198 1.00 33.39 ? 202 CYS B SG  1 
ATOM   1694 N N   . ARG B 2 113 ? -3.875  12.022  -10.102 1.00 18.98 ? 203 ARG B N   1 
ATOM   1695 C CA  . ARG B 2 113 ? -2.771  12.310  -9.189  1.00 21.43 ? 203 ARG B CA  1 
ATOM   1696 C C   . ARG B 2 113 ? -2.483  13.794  -9.048  1.00 23.36 ? 203 ARG B C   1 
ATOM   1697 O O   . ARG B 2 113 ? -1.749  14.179  -8.132  1.00 25.69 ? 203 ARG B O   1 
ATOM   1698 C CB  . ARG B 2 113 ? -1.478  11.572  -9.601  1.00 20.45 ? 203 ARG B CB  1 
ATOM   1699 C CG  . ARG B 2 113 ? -0.935  11.865  -10.986 1.00 17.45 ? 203 ARG B CG  1 
ATOM   1700 C CD  . ARG B 2 113 ? 0.452   11.201  -11.205 1.00 22.83 ? 203 ARG B CD  1 
ATOM   1701 N NE  . ARG B 2 113 ? 0.551   9.829   -10.708 1.00 23.82 ? 203 ARG B NE  1 
ATOM   1702 C CZ  . ARG B 2 113 ? 0.564   8.734   -11.463 1.00 23.34 ? 203 ARG B CZ  1 
ATOM   1703 N NH1 . ARG B 2 113 ? 0.398   8.793   -12.776 1.00 24.63 ? 203 ARG B NH1 1 
ATOM   1704 N NH2 . ARG B 2 113 ? 0.783   7.550   -10.890 1.00 19.70 ? 203 ARG B NH2 1 
ATOM   1705 N N   . LEU B 2 114 ? -3.057  14.636  -9.902  1.00 20.81 ? 204 LEU B N   1 
ATOM   1706 C CA  . LEU B 2 114 ? -2.926  16.079  -9.754  1.00 21.96 ? 204 LEU B CA  1 
ATOM   1707 C C   . LEU B 2 114 ? -4.171  16.739  -10.326 1.00 22.99 ? 204 LEU B C   1 
ATOM   1708 O O   . LEU B 2 114 ? -4.454  16.582  -11.516 1.00 20.64 ? 204 LEU B O   1 
ATOM   1709 C CB  . LEU B 2 114 ? -1.677  16.584  -10.462 1.00 20.56 ? 204 LEU B CB  1 
ATOM   1710 C CG  . LEU B 2 114 ? -1.465  18.100  -10.357 1.00 25.98 ? 204 LEU B CG  1 
ATOM   1711 C CD1 . LEU B 2 114 ? -1.236  18.513  -8.909  1.00 25.32 ? 204 LEU B CD1 1 
ATOM   1712 C CD2 . LEU B 2 114 ? -0.304  18.529  -11.234 1.00 28.39 ? 204 LEU B CD2 1 
ATOM   1713 N N   . CYS B 2 115 ? -4.909  17.458  -9.483  1.00 18.41 ? 205 CYS B N   1 
ATOM   1714 C CA  . CYS B 2 115 ? -6.084  18.213  -9.899  1.00 25.15 ? 205 CYS B CA  1 
ATOM   1715 C C   . CYS B 2 115 ? -5.740  19.690  -10.057 1.00 20.21 ? 205 CYS B C   1 
ATOM   1716 O O   . CYS B 2 115 ? -4.837  20.209  -9.396  1.00 25.46 ? 205 CYS B O   1 
ATOM   1717 C CB  . CYS B 2 115 ? -7.223  18.069  -8.880  1.00 25.94 ? 205 CYS B CB  1 
ATOM   1718 S SG  . CYS B 2 115 ? -7.834  16.395  -8.608  1.00 27.59 ? 205 CYS B SG  1 
ATOM   1719 N N   . ALA B 2 116 ? -6.482  20.375  -10.927 1.00 20.82 ? 206 ALA B N   1 
ATOM   1720 C CA  . ALA B 2 116 ? -6.306  21.808  -11.129 1.00 21.57 ? 206 ALA B CA  1 
ATOM   1721 C C   . ALA B 2 116 ? -7.663  22.471  -11.310 1.00 22.00 ? 206 ALA B C   1 
ATOM   1722 O O   . ALA B 2 116 ? -8.588  21.862  -11.865 1.00 19.54 ? 206 ALA B O   1 
ATOM   1723 C CB  . ALA B 2 116 ? -5.412  22.117  -12.345 1.00 24.69 ? 206 ALA B CB  1 
ATOM   1724 N N   . PRO B 2 117 ? -7.813  23.718  -10.858 1.00 26.56 ? 207 PRO B N   1 
ATOM   1725 C CA  . PRO B 2 117 ? -9.117  24.386  -10.975 1.00 20.57 ? 207 PRO B CA  1 
ATOM   1726 C C   . PRO B 2 117 ? -9.420  24.714  -12.426 1.00 21.06 ? 207 PRO B C   1 
ATOM   1727 O O   . PRO B 2 117 ? -8.525  25.045  -13.206 1.00 22.13 ? 207 PRO B O   1 
ATOM   1728 C CB  . PRO B 2 117 ? -8.948  25.655  -10.128 1.00 24.36 ? 207 PRO B CB  1 
ATOM   1729 C CG  . PRO B 2 117 ? -7.501  25.927  -10.148 1.00 28.49 ? 207 PRO B CG  1 
ATOM   1730 C CD  . PRO B 2 117 ? -6.805  24.584  -10.208 1.00 23.18 ? 207 PRO B CD  1 
ATOM   1731 N N   . LEU B 2 118 ? -10.688 24.585  -12.794 1.00 23.93 ? 208 LEU B N   1 
ATOM   1732 C CA  . LEU B 2 118 ? -11.099 24.965  -14.137 1.00 24.51 ? 208 LEU B CA  1 
ATOM   1733 C C   . LEU B 2 118 ? -10.944 26.472  -14.308 1.00 26.08 ? 208 LEU B C   1 
ATOM   1734 O O   . LEU B 2 118 ? -11.189 27.244  -13.380 1.00 25.23 ? 208 LEU B O   1 
ATOM   1735 C CB  . LEU B 2 118 ? -12.552 24.551  -14.395 1.00 24.62 ? 208 LEU B CB  1 
ATOM   1736 C CG  . LEU B 2 118 ? -12.894 23.078  -14.597 1.00 25.19 ? 208 LEU B CG  1 
ATOM   1737 C CD1 . LEU B 2 118 ? -14.415 22.892  -14.665 1.00 26.83 ? 208 LEU B CD1 1 
ATOM   1738 C CD2 . LEU B 2 118 ? -12.223 22.544  -15.855 1.00 23.20 ? 208 LEU B CD2 1 
ATOM   1739 N N   . ARG B 2 119 ? -10.496 26.882  -15.490 1.00 24.13 ? 209 ARG B N   1 
ATOM   1740 C CA  . ARG B 2 119 ? -10.458 28.298  -15.850 1.00 30.51 ? 209 ARG B CA  1 
ATOM   1741 C C   . ARG B 2 119 ? -11.873 28.869  -15.917 1.00 27.00 ? 209 ARG B C   1 
ATOM   1742 O O   . ARG B 2 119 ? -12.825 28.183  -16.299 1.00 26.08 ? 209 ARG B O   1 
ATOM   1743 C CB  . ARG B 2 119 ? -9.771  28.456  -17.207 1.00 32.32 ? 209 ARG B CB  1 
ATOM   1744 C CG  . ARG B 2 119 ? -9.587  29.873  -17.709 1.00 39.90 ? 209 ARG B CG  1 
ATOM   1745 C CD  . ARG B 2 119 ? -9.090  29.833  -19.153 1.00 44.60 ? 209 ARG B CD  1 
ATOM   1746 N NE  . ARG B 2 119 ? -8.136  28.748  -19.362 1.00 47.07 ? 209 ARG B NE  1 
ATOM   1747 C CZ  . ARG B 2 119 ? -6.826  28.852  -19.169 1.00 54.97 ? 209 ARG B CZ  1 
ATOM   1748 N NH1 . ARG B 2 119 ? -6.272  29.993  -18.782 1.00 58.53 ? 209 ARG B NH1 1 
ATOM   1749 N NH2 . ARG B 2 119 ? -6.052  27.785  -19.368 1.00 52.19 ? 209 ARG B NH2 1 
ATOM   1750 N N   . LYS B 2 120 ? -12.012 30.136  -15.545 1.00 28.38 ? 210 LYS B N   1 
ATOM   1751 C CA  . LYS B 2 120 ? -13.272 30.854  -15.697 1.00 28.85 ? 210 LYS B CA  1 
ATOM   1752 C C   . LYS B 2 120 ? -13.110 31.918  -16.775 1.00 30.55 ? 210 LYS B C   1 
ATOM   1753 O O   . LYS B 2 120 ? -12.159 32.706  -16.733 1.00 29.88 ? 210 LYS B O   1 
ATOM   1754 C CB  . LYS B 2 120 ? -13.711 31.494  -14.377 1.00 32.03 ? 210 LYS B CB  1 
ATOM   1755 C CG  . LYS B 2 120 ? -14.221 30.497  -13.345 1.00 33.03 ? 210 LYS B CG  1 
ATOM   1756 C CD  . LYS B 2 120 ? -14.682 31.202  -12.071 1.00 39.05 ? 210 LYS B CD  1 
ATOM   1757 C CE  . LYS B 2 120 ? -15.356 30.216  -11.126 1.00 48.04 ? 210 LYS B CE  1 
ATOM   1758 N NZ  . LYS B 2 120 ? -16.459 29.472  -11.820 1.00 44.38 ? 210 LYS B NZ  1 
ATOM   1759 N N   . CYS B 2 121 ? -14.019 31.923  -17.750 1.00 27.09 ? 211 CYS B N   1 
ATOM   1760 C CA  . CYS B 2 121 ? -13.976 32.901  -18.833 1.00 26.53 ? 211 CYS B CA  1 
ATOM   1761 C C   . CYS B 2 121 ? -14.594 34.209  -18.346 1.00 26.80 ? 211 CYS B C   1 
ATOM   1762 O O   . CYS B 2 121 ? -15.784 34.254  -18.005 1.00 29.21 ? 211 CYS B O   1 
ATOM   1763 C CB  . CYS B 2 121 ? -14.707 32.367  -20.069 1.00 25.82 ? 211 CYS B CB  1 
ATOM   1764 S SG  . CYS B 2 121 ? -14.216 30.666  -20.609 1.00 29.59 ? 211 CYS B SG  1 
ATOM   1765 N N   . ARG B 2 122 ? -13.780 35.262  -18.296 1.00 26.56 ? 212 ARG B N   1 
ATOM   1766 C CA  . ARG B 2 122 ? -14.174 36.572  -17.770 1.00 29.62 ? 212 ARG B CA  1 
ATOM   1767 C C   . ARG B 2 122 ? -15.197 37.246  -18.689 1.00 29.84 ? 212 ARG B C   1 
ATOM   1768 O O   . ARG B 2 122 ? -15.485 36.747  -19.782 1.00 27.44 ? 212 ARG B O   1 
ATOM   1769 C CB  . ARG B 2 122 ? -12.926 37.440  -17.600 1.00 31.36 ? 212 ARG B CB  1 
ATOM   1770 C CG  . ARG B 2 122 ? -12.045 37.466  -18.837 1.00 42.29 ? 212 ARG B CG  1 
ATOM   1771 C CD  . ARG B 2 122 ? -10.613 37.923  -18.539 1.00 55.74 ? 212 ARG B CD  1 
ATOM   1772 N NE  . ARG B 2 122 ? -10.531 39.377  -18.520 1.00 61.10 ? 212 ARG B NE  1 
ATOM   1773 C CZ  . ARG B 2 122 ? -10.739 40.122  -17.444 1.00 71.17 ? 212 ARG B CZ  1 
ATOM   1774 N NH1 . ARG B 2 122 ? -10.920 39.586  -16.250 1.00 74.29 ? 212 ARG B NH1 1 
ATOM   1775 N NH2 . ARG B 2 122 ? -10.784 41.438  -17.568 1.00 67.73 ? 212 ARG B NH2 1 
ATOM   1776 N N   . PRO B 2 123 ? -15.785 38.374  -18.265 1.00 29.42 ? 213 PRO B N   1 
ATOM   1777 C CA  . PRO B 2 123 ? -16.688 39.104  -19.168 1.00 31.67 ? 213 PRO B CA  1 
ATOM   1778 C C   . PRO B 2 123 ? -15.978 39.479  -20.459 1.00 26.72 ? 213 PRO B C   1 
ATOM   1779 O O   . PRO B 2 123 ? -14.804 39.852  -20.457 1.00 29.33 ? 213 PRO B O   1 
ATOM   1780 C CB  . PRO B 2 123 ? -17.082 40.344  -18.355 1.00 28.77 ? 213 PRO B CB  1 
ATOM   1781 C CG  . PRO B 2 123 ? -16.973 39.885  -16.930 1.00 32.15 ? 213 PRO B CG  1 
ATOM   1782 C CD  . PRO B 2 123 ? -15.750 39.002  -16.928 1.00 32.25 ? 213 PRO B CD  1 
ATOM   1783 N N   . GLY B 2 124 ? -16.696 39.345  -21.570 1.00 27.38 ? 214 GLY B N   1 
ATOM   1784 C CA  . GLY B 2 124 ? -16.112 39.490  -22.881 1.00 27.67 ? 214 GLY B CA  1 
ATOM   1785 C C   . GLY B 2 124 ? -15.605 38.196  -23.472 1.00 30.46 ? 214 GLY B C   1 
ATOM   1786 O O   . GLY B 2 124 ? -15.182 38.185  -24.637 1.00 27.56 ? 214 GLY B O   1 
ATOM   1787 N N   . PHE B 2 125 ? -15.627 37.110  -22.701 1.00 21.63 ? 215 PHE B N   1 
ATOM   1788 C CA  . PHE B 2 125 ? -15.147 35.806  -23.122 1.00 26.61 ? 215 PHE B CA  1 
ATOM   1789 C C   . PHE B 2 125 ? -16.195 34.756  -22.775 1.00 27.78 ? 215 PHE B C   1 
ATOM   1790 O O   . PHE B 2 125 ? -16.849 34.837  -21.727 1.00 24.70 ? 215 PHE B O   1 
ATOM   1791 C CB  . PHE B 2 125 ? -13.810 35.458  -22.445 1.00 29.32 ? 215 PHE B CB  1 
ATOM   1792 C CG  . PHE B 2 125 ? -12.662 36.354  -22.852 1.00 29.74 ? 215 PHE B CG  1 
ATOM   1793 C CD1 . PHE B 2 125 ? -12.479 37.584  -22.256 1.00 32.60 ? 215 PHE B CD1 1 
ATOM   1794 C CD2 . PHE B 2 125 ? -11.760 35.949  -23.823 1.00 29.91 ? 215 PHE B CD2 1 
ATOM   1795 C CE1 . PHE B 2 125 ? -11.426 38.402  -22.623 1.00 36.46 ? 215 PHE B CE1 1 
ATOM   1796 C CE2 . PHE B 2 125 ? -10.707 36.763  -24.194 1.00 29.86 ? 215 PHE B CE2 1 
ATOM   1797 C CZ  . PHE B 2 125 ? -10.542 37.988  -23.596 1.00 31.87 ? 215 PHE B CZ  1 
ATOM   1798 N N   . GLY B 2 126 ? -16.360 33.777  -23.661 1.00 21.99 ? 216 GLY B N   1 
ATOM   1799 C CA  . GLY B 2 126 ? -17.297 32.701  -23.430 1.00 25.21 ? 216 GLY B CA  1 
ATOM   1800 C C   . GLY B 2 126 ? -16.628 31.348  -23.545 1.00 28.20 ? 216 GLY B C   1 
ATOM   1801 O O   . GLY B 2 126 ? -15.517 31.215  -24.069 1.00 23.45 ? 216 GLY B O   1 
ATOM   1802 N N   . VAL B 2 127 ? -17.331 30.325  -23.046 1.00 25.52 ? 217 VAL B N   1 
ATOM   1803 C CA  . VAL B 2 127 ? -16.812 28.963  -23.117 1.00 25.03 ? 217 VAL B CA  1 
ATOM   1804 C C   . VAL B 2 127 ? -16.807 28.508  -24.567 1.00 26.33 ? 217 VAL B C   1 
ATOM   1805 O O   . VAL B 2 127 ? -17.827 28.597  -25.261 1.00 24.91 ? 217 VAL B O   1 
ATOM   1806 C CB  . VAL B 2 127 ? -17.638 28.014  -22.233 1.00 28.95 ? 217 VAL B CB  1 
ATOM   1807 C CG1 . VAL B 2 127 ? -17.220 26.557  -22.461 1.00 26.21 ? 217 VAL B CG1 1 
ATOM   1808 C CG2 . VAL B 2 127 ? -17.458 28.381  -20.773 1.00 26.63 ? 217 VAL B CG2 1 
ATOM   1809 N N   . ALA B 2 128 ? -15.644 28.062  -25.042 1.00 24.05 ? 218 ALA B N   1 
ATOM   1810 C CA  . ALA B 2 128 ? -15.493 27.460  -26.366 1.00 25.51 ? 218 ALA B CA  1 
ATOM   1811 C C   . ALA B 2 128 ? -15.481 25.937  -26.326 1.00 31.12 ? 218 ALA B C   1 
ATOM   1812 O O   . ALA B 2 128 ? -16.111 25.287  -27.167 1.00 31.32 ? 218 ALA B O   1 
ATOM   1813 C CB  . ALA B 2 128 ? -14.207 27.961  -27.034 1.00 25.72 ? 218 ALA B CB  1 
ATOM   1814 N N   . ARG B 2 129 ? -14.761 25.340  -25.381 1.00 30.79 ? 219 ARG B N   1 
ATOM   1815 C CA  . ARG B 2 129 ? -14.906 23.918  -25.108 1.00 31.73 ? 219 ARG B CA  1 
ATOM   1816 C C   . ARG B 2 129 ? -15.120 23.777  -23.608 1.00 26.73 ? 219 ARG B C   1 
ATOM   1817 O O   . ARG B 2 129 ? -14.318 24.307  -22.812 1.00 27.45 ? 219 ARG B O   1 
ATOM   1818 C CB  . ARG B 2 129 ? -13.692 23.086  -25.565 1.00 33.76 ? 219 ARG B CB  1 
ATOM   1819 C CG  . ARG B 2 129 ? -13.920 21.559  -25.461 1.00 38.80 ? 219 ARG B CG  1 
ATOM   1820 C CD  . ARG B 2 129 ? -12.699 20.752  -25.928 1.00 44.76 ? 219 ARG B CD  1 
ATOM   1821 N NE  . ARG B 2 129 ? -11.515 21.034  -25.120 1.00 44.42 ? 219 ARG B NE  1 
ATOM   1822 C CZ  . ARG B 2 129 ? -10.321 20.482  -25.305 1.00 45.50 ? 219 ARG B CZ  1 
ATOM   1823 N NH1 . ARG B 2 129 ? -10.107 19.602  -26.271 1.00 45.56 ? 219 ARG B NH1 1 
ATOM   1824 N NH2 . ARG B 2 129 ? -9.316  20.817  -24.498 1.00 42.27 ? 219 ARG B NH2 1 
ATOM   1825 N N   . PRO B 2 130 ? -16.181 23.102  -23.183 1.00 26.82 ? 220 PRO B N   1 
ATOM   1826 C CA  . PRO B 2 130 ? -16.416 22.910  -21.749 1.00 26.19 ? 220 PRO B CA  1 
ATOM   1827 C C   . PRO B 2 130 ? -15.332 22.042  -21.125 1.00 30.98 ? 220 PRO B C   1 
ATOM   1828 O O   . PRO B 2 130 ? -14.664 21.248  -21.794 1.00 25.21 ? 220 PRO B O   1 
ATOM   1829 C CB  . PRO B 2 130 ? -17.778 22.201  -21.695 1.00 29.55 ? 220 PRO B CB  1 
ATOM   1830 C CG  . PRO B 2 130 ? -18.358 22.345  -23.073 1.00 32.00 ? 220 PRO B CG  1 
ATOM   1831 C CD  . PRO B 2 130 ? -17.195 22.427  -24.008 1.00 29.13 ? 220 PRO B CD  1 
ATOM   1832 N N   . GLY B 2 131 ? -15.170 22.207  -19.816 1.00 23.99 ? 221 GLY B N   1 
ATOM   1833 C CA  . GLY B 2 131 ? -14.293 21.327  -19.071 1.00 29.24 ? 221 GLY B CA  1 
ATOM   1834 C C   . GLY B 2 131 ? -14.805 19.900  -19.065 1.00 30.84 ? 221 GLY B C   1 
ATOM   1835 O O   . GLY B 2 131 ? -15.999 19.635  -19.203 1.00 29.80 ? 221 GLY B O   1 
ATOM   1836 N N   . THR B 2 132 ? -13.872 18.964  -18.932 1.00 26.51 ? 222 THR B N   1 
ATOM   1837 C CA  . THR B 2 132 ? -14.178 17.546  -18.820 1.00 25.28 ? 222 THR B CA  1 
ATOM   1838 C C   . THR B 2 132 ? -13.418 17.023  -17.613 1.00 27.51 ? 222 THR B C   1 
ATOM   1839 O O   . THR B 2 132 ? -12.664 17.760  -16.969 1.00 25.57 ? 222 THR B O   1 
ATOM   1840 C CB  . THR B 2 132 ? -13.797 16.782  -20.096 1.00 31.19 ? 222 THR B CB  1 
ATOM   1841 O OG1 . THR B 2 132 ? -12.376 16.625  -20.147 1.00 33.89 ? 222 THR B OG1 1 
ATOM   1842 C CG2 . THR B 2 132 ? -14.244 17.546  -21.344 1.00 33.08 ? 222 THR B CG2 1 
ATOM   1843 N N   . GLU B 2 133 ? -13.602 15.744  -17.298 1.00 30.02 ? 223 GLU B N   1 
ATOM   1844 C CA  . GLU B 2 133 ? -12.918 15.210  -16.124 1.00 29.42 ? 223 GLU B CA  1 
ATOM   1845 C C   . GLU B 2 133 ? -11.400 15.335  -16.256 1.00 27.66 ? 223 GLU B C   1 
ATOM   1846 O O   . GLU B 2 133 ? -10.709 15.511  -15.247 1.00 28.01 ? 223 GLU B O   1 
ATOM   1847 C CB  . GLU B 2 133 ? -13.344 13.759  -15.867 1.00 33.49 ? 223 GLU B CB  1 
ATOM   1848 C CG  . GLU B 2 133 ? -12.491 12.697  -16.525 1.00 41.40 ? 223 GLU B CG  1 
ATOM   1849 C CD  . GLU B 2 133 ? -12.544 11.364  -15.791 1.00 51.35 ? 223 GLU B CD  1 
ATOM   1850 O OE1 . GLU B 2 133 ? -13.655 10.944  -15.395 1.00 53.12 ? 223 GLU B OE1 1 
ATOM   1851 O OE2 . GLU B 2 133 ? -11.472 10.744  -15.597 1.00 48.99 ? 223 GLU B OE2 1 
ATOM   1852 N N   . THR B 2 134 ? -10.867 15.328  -17.485 1.00 22.74 ? 224 THR B N   1 
ATOM   1853 C CA  . THR B 2 134 ? -9.424  15.410  -17.696 1.00 30.26 ? 224 THR B CA  1 
ATOM   1854 C C   . THR B 2 134 ? -8.973  16.628  -18.504 1.00 29.15 ? 224 THR B C   1 
ATOM   1855 O O   . THR B 2 134 ? -7.807  16.670  -18.919 1.00 31.02 ? 224 THR B O   1 
ATOM   1856 C CB  . THR B 2 134 ? -8.895  14.133  -18.378 1.00 33.48 ? 224 THR B CB  1 
ATOM   1857 O OG1 . THR B 2 134 ? -9.554  13.941  -19.640 1.00 31.27 ? 224 THR B OG1 1 
ATOM   1858 C CG2 . THR B 2 134 ? -9.120  12.919  -17.500 1.00 34.75 ? 224 THR B CG2 1 
ATOM   1859 N N   . SER B 2 135 ? -9.822  17.634  -18.730 1.00 23.98 ? 225 SER B N   1 
ATOM   1860 C CA  . SER B 2 135 ? -9.354  18.754  -19.536 1.00 29.88 ? 225 SER B CA  1 
ATOM   1861 C C   . SER B 2 135 ? -9.986  20.067  -19.093 1.00 28.32 ? 225 SER B C   1 
ATOM   1862 O O   . SER B 2 135 ? -11.165 20.110  -18.730 1.00 26.33 ? 225 SER B O   1 
ATOM   1863 C CB  . SER B 2 135 ? -9.618  18.500  -21.029 1.00 31.66 ? 225 SER B CB  1 
ATOM   1864 O OG  . SER B 2 135 ? -10.984 18.305  -21.297 1.00 30.53 ? 225 SER B OG  1 
ATOM   1865 N N   . ASP B 2 136 ? -9.183  21.135  -19.138 1.00 26.71 ? 226 ASP B N   1 
ATOM   1866 C CA  . ASP B 2 136 ? -9.609  22.463  -18.719 1.00 27.92 ? 226 ASP B CA  1 
ATOM   1867 C C   . ASP B 2 136 ? -10.604 23.058  -19.719 1.00 29.32 ? 226 ASP B C   1 
ATOM   1868 O O   . ASP B 2 136 ? -10.684 22.651  -20.883 1.00 26.53 ? 226 ASP B O   1 
ATOM   1869 C CB  . ASP B 2 136 ? -8.395  23.390  -18.572 1.00 28.30 ? 226 ASP B CB  1 
ATOM   1870 C CG  . ASP B 2 136 ? -8.687  24.635  -17.741 1.00 32.51 ? 226 ASP B CG  1 
ATOM   1871 O OD1 . ASP B 2 136 ? -9.804  24.765  -17.199 1.00 34.53 ? 226 ASP B OD1 1 
ATOM   1872 O OD2 . ASP B 2 136 ? -7.789  25.502  -17.635 1.00 31.37 ? 226 ASP B OD2 1 
ATOM   1873 N N   . VAL B 2 137 ? -11.407 24.001  -19.219 1.00 24.86 ? 227 VAL B N   1 
ATOM   1874 C CA  . VAL B 2 137 ? -12.238 24.832  -20.081 1.00 26.07 ? 227 VAL B CA  1 
ATOM   1875 C C   . VAL B 2 137 ? -11.349 25.574  -21.074 1.00 27.96 ? 227 VAL B C   1 
ATOM   1876 O O   . VAL B 2 137 ? -10.238 26.009  -20.737 1.00 27.99 ? 227 VAL B O   1 
ATOM   1877 C CB  . VAL B 2 137 ? -13.050 25.829  -19.232 1.00 28.69 ? 227 VAL B CB  1 
ATOM   1878 C CG1 . VAL B 2 137 ? -13.739 26.884  -20.118 1.00 27.48 ? 227 VAL B CG1 1 
ATOM   1879 C CG2 . VAL B 2 137 ? -14.070 25.114  -18.359 1.00 24.39 ? 227 VAL B CG2 1 
ATOM   1880 N N   . VAL B 2 138 ? -11.840 25.729  -22.304 1.00 27.64 ? 228 VAL B N   1 
ATOM   1881 C CA  . VAL B 2 138 ? -11.218 26.585  -23.313 1.00 28.67 ? 228 VAL B CA  1 
ATOM   1882 C C   . VAL B 2 138 ? -12.137 27.785  -23.552 1.00 27.56 ? 228 VAL B C   1 
ATOM   1883 O O   . VAL B 2 138 ? -13.332 27.610  -23.822 1.00 26.12 ? 228 VAL B O   1 
ATOM   1884 C CB  . VAL B 2 138 ? -10.964 25.815  -24.624 1.00 31.91 ? 228 VAL B CB  1 
ATOM   1885 C CG1 . VAL B 2 138 ? -10.220 26.694  -25.643 1.00 30.94 ? 228 VAL B CG1 1 
ATOM   1886 C CG2 . VAL B 2 138 ? -10.195 24.506  -24.358 1.00 29.65 ? 228 VAL B CG2 1 
ATOM   1887 N N   . CYS B 2 139 ? -11.590 28.998  -23.445 1.00 26.04 ? 229 CYS B N   1 
ATOM   1888 C CA  . CYS B 2 139 ? -12.361 30.223  -23.658 1.00 30.31 ? 229 CYS B CA  1 
ATOM   1889 C C   . CYS B 2 139 ? -12.138 30.792  -25.058 1.00 32.53 ? 229 CYS B C   1 
ATOM   1890 O O   . CYS B 2 139 ? -11.159 30.470  -25.736 1.00 27.37 ? 229 CYS B O   1 
ATOM   1891 C CB  . CYS B 2 139 ? -11.993 31.299  -22.628 1.00 30.89 ? 229 CYS B CB  1 
ATOM   1892 S SG  . CYS B 2 139 ? -12.199 30.808  -20.905 1.00 38.48 ? 229 CYS B SG  1 
ATOM   1893 N N   . LYS B 2 140 ? -13.050 31.674  -25.471 1.00 29.54 ? 230 LYS B N   1 
ATOM   1894 C CA  . LYS B 2 140 ? -12.871 32.471  -26.681 1.00 24.22 ? 230 LYS B CA  1 
ATOM   1895 C C   . LYS B 2 140 ? -13.419 33.876  -26.461 1.00 27.67 ? 230 LYS B C   1 
ATOM   1896 O O   . LYS B 2 140 ? -14.362 34.065  -25.683 1.00 23.17 ? 230 LYS B O   1 
ATOM   1897 C CB  . LYS B 2 140 ? -13.581 31.833  -27.886 1.00 25.37 ? 230 LYS B CB  1 
ATOM   1898 C CG  . LYS B 2 140 ? -15.084 31.850  -27.768 1.00 30.53 ? 230 LYS B CG  1 
ATOM   1899 C CD  . LYS B 2 140 ? -15.753 31.232  -28.973 1.00 32.96 ? 230 LYS B CD  1 
ATOM   1900 C CE  . LYS B 2 140 ? -17.259 31.210  -28.790 1.00 37.45 ? 230 LYS B CE  1 
ATOM   1901 N NZ  . LYS B 2 140 ? -17.934 30.682  -30.002 1.00 44.30 ? 230 LYS B NZ  1 
ATOM   1902 N N   . PRO B 2 141 ? -12.848 34.877  -27.131 1.00 26.64 ? 231 PRO B N   1 
ATOM   1903 C CA  . PRO B 2 141 ? -13.443 36.220  -27.080 1.00 26.60 ? 231 PRO B CA  1 
ATOM   1904 C C   . PRO B 2 141 ? -14.743 36.246  -27.863 1.00 28.67 ? 231 PRO B C   1 
ATOM   1905 O O   . PRO B 2 141 ? -14.855 35.639  -28.930 1.00 25.52 ? 231 PRO B O   1 
ATOM   1906 C CB  . PRO B 2 141 ? -12.378 37.112  -27.731 1.00 28.05 ? 231 PRO B CB  1 
ATOM   1907 C CG  . PRO B 2 141 ? -11.569 36.169  -28.589 1.00 30.30 ? 231 PRO B CG  1 
ATOM   1908 C CD  . PRO B 2 141 ? -11.586 34.841  -27.898 1.00 26.41 ? 231 PRO B CD  1 
ATOM   1909 N N   . CYS B 2 142 ? -15.736 36.949  -27.326 1.00 24.43 ? 232 CYS B N   1 
ATOM   1910 C CA  . CYS B 2 142 ? -17.025 37.002  -28.002 1.00 24.44 ? 232 CYS B CA  1 
ATOM   1911 C C   . CYS B 2 142 ? -16.923 37.889  -29.242 1.00 27.59 ? 232 CYS B C   1 
ATOM   1912 O O   . CYS B 2 142 ? -16.396 39.001  -29.179 1.00 27.22 ? 232 CYS B O   1 
ATOM   1913 C CB  . CYS B 2 142 ? -18.103 37.516  -27.047 1.00 29.97 ? 232 CYS B CB  1 
ATOM   1914 S SG  . CYS B 2 142 ? -18.340 36.489  -25.557 1.00 30.63 ? 232 CYS B SG  1 
ATOM   1915 N N   . ALA B 2 143 ? -17.404 37.389  -30.369 1.00 23.96 ? 233 ALA B N   1 
ATOM   1916 C CA  . ALA B 2 143 ? -17.392 38.152  -31.610 1.00 28.13 ? 233 ALA B CA  1 
ATOM   1917 C C   . ALA B 2 143 ? -18.539 39.163  -31.623 1.00 29.48 ? 233 ALA B C   1 
ATOM   1918 O O   . ALA B 2 143 ? -19.514 39.006  -30.882 1.00 28.02 ? 233 ALA B O   1 
ATOM   1919 C CB  . ALA B 2 143 ? -17.509 37.202  -32.800 1.00 30.83 ? 233 ALA B CB  1 
ATOM   1920 N N   . PRO B 2 144 ? -18.452 40.207  -32.462 1.00 29.35 ? 234 PRO B N   1 
ATOM   1921 C CA  . PRO B 2 144 ? -19.531 41.205  -32.516 1.00 30.37 ? 234 PRO B CA  1 
ATOM   1922 C C   . PRO B 2 144 ? -20.888 40.554  -32.727 1.00 30.90 ? 234 PRO B C   1 
ATOM   1923 O O   . PRO B 2 144 ? -21.026 39.573  -33.460 1.00 26.24 ? 234 PRO B O   1 
ATOM   1924 C CB  . PRO B 2 144 ? -19.141 42.094  -33.705 1.00 29.42 ? 234 PRO B CB  1 
ATOM   1925 C CG  . PRO B 2 144 ? -17.653 41.980  -33.789 1.00 29.95 ? 234 PRO B CG  1 
ATOM   1926 C CD  . PRO B 2 144 ? -17.315 40.576  -33.330 1.00 29.68 ? 234 PRO B CD  1 
ATOM   1927 N N   . GLY B 2 145 ? -21.904 41.114  -32.072 1.00 24.15 ? 235 GLY B N   1 
ATOM   1928 C CA  . GLY B 2 145 ? -23.215 40.512  -32.063 1.00 26.53 ? 235 GLY B CA  1 
ATOM   1929 C C   . GLY B 2 145 ? -23.478 39.598  -30.887 1.00 28.08 ? 235 GLY B C   1 
ATOM   1930 O O   . GLY B 2 145 ? -24.629 39.186  -30.690 1.00 29.37 ? 235 GLY B O   1 
ATOM   1931 N N   . THR B 2 146 ? -22.454 39.268  -30.102 1.00 24.97 ? 236 THR B N   1 
ATOM   1932 C CA  . THR B 2 146 ? -22.580 38.361  -28.967 1.00 28.12 ? 236 THR B CA  1 
ATOM   1933 C C   . THR B 2 146 ? -21.833 38.944  -27.775 1.00 24.20 ? 236 THR B C   1 
ATOM   1934 O O   . THR B 2 146 ? -21.015 39.863  -27.912 1.00 21.93 ? 236 THR B O   1 
ATOM   1935 C CB  . THR B 2 146 ? -22.044 36.949  -29.283 1.00 26.35 ? 236 THR B CB  1 
ATOM   1936 O OG1 . THR B 2 146 ? -20.608 36.978  -29.333 1.00 27.10 ? 236 THR B OG1 1 
ATOM   1937 C CG2 . THR B 2 146 ? -22.587 36.450  -30.613 1.00 32.10 ? 236 THR B CG2 1 
ATOM   1938 N N   . PHE B 2 147 ? -22.097 38.386  -26.591 1.00 21.96 ? 237 PHE B N   1 
ATOM   1939 C CA  . PHE B 2 147 ? -21.497 38.935  -25.381 1.00 23.67 ? 237 PHE B CA  1 
ATOM   1940 C C   . PHE B 2 147 ? -21.524 37.919  -24.250 1.00 25.99 ? 237 PHE B C   1 
ATOM   1941 O O   . PHE B 2 147 ? -22.262 36.935  -24.283 1.00 25.12 ? 237 PHE B O   1 
ATOM   1942 C CB  . PHE B 2 147 ? -22.218 40.203  -24.925 1.00 26.41 ? 237 PHE B CB  1 
ATOM   1943 C CG  . PHE B 2 147 ? -23.546 39.948  -24.245 1.00 29.12 ? 237 PHE B CG  1 
ATOM   1944 C CD1 . PHE B 2 147 ? -24.662 39.589  -24.981 1.00 28.86 ? 237 PHE B CD1 1 
ATOM   1945 C CD2 . PHE B 2 147 ? -23.685 40.122  -22.871 1.00 28.20 ? 237 PHE B CD2 1 
ATOM   1946 C CE1 . PHE B 2 147 ? -25.889 39.395  -24.363 1.00 28.45 ? 237 PHE B CE1 1 
ATOM   1947 C CE2 . PHE B 2 147 ? -24.911 39.918  -22.245 1.00 30.37 ? 237 PHE B CE2 1 
ATOM   1948 C CZ  . PHE B 2 147 ? -26.010 39.555  -22.991 1.00 31.03 ? 237 PHE B CZ  1 
ATOM   1949 N N   . SER B 2 148 ? -20.711 38.198  -23.236 1.00 27.33 ? 238 SER B N   1 
ATOM   1950 C CA  . SER B 2 148 ? -20.752 37.486  -21.965 1.00 26.55 ? 238 SER B CA  1 
ATOM   1951 C C   . SER B 2 148 ? -20.493 38.511  -20.877 1.00 27.87 ? 238 SER B C   1 
ATOM   1952 O O   . SER B 2 148 ? -19.439 39.155  -20.870 1.00 24.97 ? 238 SER B O   1 
ATOM   1953 C CB  . SER B 2 148 ? -19.713 36.359  -21.896 1.00 28.16 ? 238 SER B CB  1 
ATOM   1954 O OG  . SER B 2 148 ? -19.628 35.840  -20.575 1.00 25.95 ? 238 SER B OG  1 
ATOM   1955 N N   . ASN B 2 149 ? -21.450 38.665  -19.965 1.00 25.61 ? 239 ASN B N   1 
ATOM   1956 C CA  . ASN B 2 149 ? -21.324 39.615  -18.869 1.00 30.36 ? 239 ASN B CA  1 
ATOM   1957 C C   . ASN B 2 149 ? -20.995 38.935  -17.541 1.00 30.54 ? 239 ASN B C   1 
ATOM   1958 O O   . ASN B 2 149 ? -21.215 39.525  -16.478 1.00 32.52 ? 239 ASN B O   1 
ATOM   1959 C CB  . ASN B 2 149 ? -22.603 40.447  -18.751 1.00 26.21 ? 239 ASN B CB  1 
ATOM   1960 C CG  . ASN B 2 149 ? -23.828 39.604  -18.425 1.00 33.80 ? 239 ASN B CG  1 
ATOM   1961 O OD1 . ASN B 2 149 ? -23.906 38.427  -18.794 1.00 31.07 ? 239 ASN B OD1 1 
ATOM   1962 N ND2 . ASN B 2 149 ? -24.803 40.210  -17.733 1.00 33.50 ? 239 ASN B ND2 1 
ATOM   1963 N N   . THR B 2 150 ? -20.472 37.709  -17.573 1.00 30.07 ? 240 THR B N   1 
ATOM   1964 C CA  . THR B 2 150 ? -20.168 36.967  -16.356 1.00 25.54 ? 240 THR B CA  1 
ATOM   1965 C C   . THR B 2 150 ? -18.760 36.385  -16.410 1.00 28.97 ? 240 THR B C   1 
ATOM   1966 O O   . THR B 2 150 ? -18.151 36.260  -17.476 1.00 27.52 ? 240 THR B O   1 
ATOM   1967 C CB  . THR B 2 150 ? -21.178 35.827  -16.107 1.00 29.43 ? 240 THR B CB  1 
ATOM   1968 O OG1 . THR B 2 150 ? -21.207 34.937  -17.236 1.00 29.93 ? 240 THR B OG1 1 
ATOM   1969 C CG2 . THR B 2 150 ? -22.572 36.385  -15.857 1.00 32.17 ? 240 THR B CG2 1 
ATOM   1970 N N   . THR B 2 151 ? -18.251 36.029  -15.226 1.00 27.52 ? 241 THR B N   1 
ATOM   1971 C CA  . THR B 2 151 ? -17.022 35.255  -15.073 1.00 34.17 ? 241 THR B CA  1 
ATOM   1972 C C   . THR B 2 151 ? -17.432 33.821  -14.735 1.00 31.46 ? 241 THR B C   1 
ATOM   1973 O O   . THR B 2 151 ? -17.972 33.559  -13.656 1.00 33.33 ? 241 THR B O   1 
ATOM   1974 C CB  . THR B 2 151 ? -16.128 35.855  -13.988 1.00 32.15 ? 241 THR B CB  1 
ATOM   1975 O OG1 . THR B 2 151 ? -15.748 37.183  -14.367 1.00 30.87 ? 241 THR B OG1 1 
ATOM   1976 C CG2 . THR B 2 151 ? -14.862 35.010  -13.798 1.00 35.09 ? 241 THR B CG2 1 
ATOM   1977 N N   . SER B 2 152 ? -17.209 32.896  -15.661 1.00 25.97 ? 242 SER B N   1 
ATOM   1978 C CA  . SER B 2 152 ? -17.861 31.602  -15.515 1.00 27.21 ? 242 SER B CA  1 
ATOM   1979 C C   . SER B 2 152 ? -17.162 30.536  -16.345 1.00 31.17 ? 242 SER B C   1 
ATOM   1980 O O   . SER B 2 152 ? -16.733 30.802  -17.470 1.00 28.09 ? 242 SER B O   1 
ATOM   1981 C CB  . SER B 2 152 ? -19.329 31.710  -15.937 1.00 26.16 ? 242 SER B CB  1 
ATOM   1982 O OG  . SER B 2 152 ? -19.906 30.442  -16.169 1.00 28.09 ? 242 SER B OG  1 
ATOM   1983 N N   . SER B 2 153 ? -17.091 29.320  -15.794 1.00 28.48 ? 243 SER B N   1 
ATOM   1984 C CA  A SER B 2 153 ? -16.557 28.178  -16.519 0.33 29.51 ? 243 SER B CA  1 
ATOM   1985 C CA  B SER B 2 153 ? -16.569 28.149  -16.489 0.67 29.51 ? 243 SER B CA  1 
ATOM   1986 C C   . SER B 2 153 ? -17.591 27.510  -17.415 1.00 30.22 ? 243 SER B C   1 
ATOM   1987 O O   . SER B 2 153 ? -17.257 26.543  -18.098 1.00 29.03 ? 243 SER B O   1 
ATOM   1988 C CB  A SER B 2 153 ? -15.980 27.148  -15.538 0.33 28.97 ? 243 SER B CB  1 
ATOM   1989 C CB  B SER B 2 153 ? -16.091 27.089  -15.487 0.67 29.00 ? 243 SER B CB  1 
ATOM   1990 O OG  A SER B 2 153 ? -16.987 26.635  -14.683 0.33 29.39 ? 243 SER B OG  1 
ATOM   1991 O OG  B SER B 2 153 ? -14.927 27.488  -14.794 0.67 27.54 ? 243 SER B OG  1 
ATOM   1992 N N   . THR B 2 154 ? -18.832 28.004  -17.445 1.00 28.57 ? 244 THR B N   1 
ATOM   1993 C CA  . THR B 2 154 ? -19.829 27.365  -18.297 1.00 29.19 ? 244 THR B CA  1 
ATOM   1994 C C   . THR B 2 154 ? -20.558 28.342  -19.226 1.00 28.30 ? 244 THR B C   1 
ATOM   1995 O O   . THR B 2 154 ? -20.967 27.936  -20.318 1.00 25.24 ? 244 THR B O   1 
ATOM   1996 C CB  . THR B 2 154 ? -20.832 26.583  -17.434 1.00 32.12 ? 244 THR B CB  1 
ATOM   1997 O OG1 . THR B 2 154 ? -21.473 27.469  -16.507 1.00 34.97 ? 244 THR B OG1 1 
ATOM   1998 C CG2 . THR B 2 154 ? -20.111 25.491  -16.651 1.00 29.04 ? 244 THR B CG2 1 
ATOM   1999 N N   . ASP B 2 155 ? -20.694 29.619  -18.837 1.00 27.20 ? 245 ASP B N   1 
ATOM   2000 C CA  . ASP B 2 155 ? -21.441 30.590  -19.645 1.00 31.92 ? 245 ASP B CA  1 
ATOM   2001 C C   . ASP B 2 155 ? -20.792 30.806  -21.010 1.00 30.67 ? 245 ASP B C   1 
ATOM   2002 O O   . ASP B 2 155 ? -19.582 31.014  -21.106 1.00 28.51 ? 245 ASP B O   1 
ATOM   2003 C CB  . ASP B 2 155 ? -21.545 31.940  -18.919 1.00 26.91 ? 245 ASP B CB  1 
ATOM   2004 C CG  . ASP B 2 155 ? -22.487 31.896  -17.726 1.00 34.85 ? 245 ASP B CG  1 
ATOM   2005 O OD1 . ASP B 2 155 ? -23.374 31.026  -17.697 1.00 32.57 ? 245 ASP B OD1 1 
ATOM   2006 O OD2 . ASP B 2 155 ? -22.340 32.735  -16.818 1.00 35.64 ? 245 ASP B OD2 1 
ATOM   2007 N N   . ILE B 2 156 ? -21.609 30.800  -22.057 1.00 30.11 ? 246 ILE B N   1 
ATOM   2008 C CA  . ILE B 2 156 ? -21.130 30.929  -23.426 1.00 29.60 ? 246 ILE B CA  1 
ATOM   2009 C C   . ILE B 2 156 ? -21.392 32.347  -23.928 1.00 31.62 ? 246 ILE B C   1 
ATOM   2010 O O   . ILE B 2 156 ? -22.086 33.136  -23.295 1.00 31.78 ? 246 ILE B O   1 
ATOM   2011 C CB  . ILE B 2 156 ? -21.785 29.880  -24.355 1.00 31.54 ? 246 ILE B CB  1 
ATOM   2012 C CG1 . ILE B 2 156 ? -23.289 30.139  -24.502 1.00 33.33 ? 246 ILE B CG1 1 
ATOM   2013 C CG2 . ILE B 2 156 ? -21.543 28.463  -23.818 1.00 29.83 ? 246 ILE B CG2 1 
ATOM   2014 C CD1 . ILE B 2 156 ? -24.001 29.089  -25.349 1.00 34.59 ? 246 ILE B CD1 1 
ATOM   2015 N N   . CYS B 2 157 ? -20.810 32.685  -25.079 1.00 29.83 ? 247 CYS B N   1 
ATOM   2016 C CA  . CYS B 2 157 ? -21.101 33.964  -25.718 1.00 31.02 ? 247 CYS B CA  1 
ATOM   2017 C C   . CYS B 2 157 ? -22.503 33.908  -26.301 1.00 30.87 ? 247 CYS B C   1 
ATOM   2018 O O   . CYS B 2 157 ? -22.789 33.053  -27.143 1.00 34.11 ? 247 CYS B O   1 
ATOM   2019 C CB  . CYS B 2 157 ? -20.078 34.262  -26.811 1.00 28.48 ? 247 CYS B CB  1 
ATOM   2020 S SG  . CYS B 2 157 ? -18.382 34.535  -26.219 1.00 33.51 ? 247 CYS B SG  1 
ATOM   2021 N N   . ARG B 2 158 ? -23.383 34.804  -25.854 1.00 29.03 ? 248 ARG B N   1 
ATOM   2022 C CA  . ARG B 2 158 ? -24.774 34.722  -26.278 1.00 32.84 ? 248 ARG B CA  1 
ATOM   2023 C C   . ARG B 2 158 ? -25.146 35.956  -27.103 1.00 30.86 ? 248 ARG B C   1 
ATOM   2024 O O   . ARG B 2 158 ? -24.515 37.008  -26.962 1.00 30.02 ? 248 ARG B O   1 
ATOM   2025 C CB  . ARG B 2 158 ? -25.716 34.582  -25.067 1.00 33.40 ? 248 ARG B CB  1 
ATOM   2026 C CG  . ARG B 2 158 ? -25.679 35.723  -24.042 1.00 36.84 ? 248 ARG B CG  1 
ATOM   2027 C CD  . ARG B 2 158 ? -26.607 35.398  -22.845 1.00 40.82 ? 248 ARG B CD  1 
ATOM   2028 N NE  . ARG B 2 158 ? -26.849 36.533  -21.955 1.00 36.39 ? 248 ARG B NE  1 
ATOM   2029 C CZ  . ARG B 2 158 ? -26.086 36.855  -20.916 1.00 43.29 ? 248 ARG B CZ  1 
ATOM   2030 N NH1 . ARG B 2 158 ? -24.988 36.172  -20.627 1.00 33.80 ? 248 ARG B NH1 1 
ATOM   2031 N NH2 . ARG B 2 158 ? -26.431 37.892  -20.151 1.00 38.88 ? 248 ARG B NH2 1 
ATOM   2032 N N   . PRO B 2 159 ? -26.135 35.849  -27.995 1.00 29.43 ? 249 PRO B N   1 
ATOM   2033 C CA  . PRO B 2 159 ? -26.429 36.967  -28.900 1.00 32.06 ? 249 PRO B CA  1 
ATOM   2034 C C   . PRO B 2 159 ? -26.913 38.210  -28.165 1.00 28.13 ? 249 PRO B C   1 
ATOM   2035 O O   . PRO B 2 159 ? -27.587 38.134  -27.131 1.00 28.93 ? 249 PRO B O   1 
ATOM   2036 C CB  . PRO B 2 159 ? -27.526 36.409  -29.818 1.00 30.81 ? 249 PRO B CB  1 
ATOM   2037 C CG  . PRO B 2 159 ? -28.069 35.208  -29.112 1.00 40.95 ? 249 PRO B CG  1 
ATOM   2038 C CD  . PRO B 2 159 ? -26.931 34.651  -28.318 1.00 36.01 ? 249 PRO B CD  1 
ATOM   2039 N N   . HIS B 2 160 ? -26.538 39.367  -28.711 1.00 32.51 ? 250 HIS B N   1 
ATOM   2040 C CA  . HIS B 2 160 ? -27.182 40.617  -28.325 1.00 30.17 ? 250 HIS B CA  1 
ATOM   2041 C C   . HIS B 2 160 ? -28.667 40.537  -28.633 1.00 24.95 ? 250 HIS B C   1 
ATOM   2042 O O   . HIS B 2 160 ? -29.090 39.845  -29.560 1.00 27.39 ? 250 HIS B O   1 
ATOM   2043 C CB  . HIS B 2 160 ? -26.590 41.807  -29.088 1.00 28.12 ? 250 HIS B CB  1 
ATOM   2044 C CG  . HIS B 2 160 ? -25.190 42.152  -28.701 1.00 24.91 ? 250 HIS B CG  1 
ATOM   2045 N ND1 . HIS B 2 160 ? -24.322 42.787  -29.561 1.00 31.53 ? 250 HIS B ND1 1 
ATOM   2046 C CD2 . HIS B 2 160 ? -24.505 41.960  -27.549 1.00 30.44 ? 250 HIS B CD2 1 
ATOM   2047 C CE1 . HIS B 2 160 ? -23.159 42.969  -28.960 1.00 32.55 ? 250 HIS B CE1 1 
ATOM   2048 N NE2 . HIS B 2 160 ? -23.242 42.477  -27.736 1.00 31.43 ? 250 HIS B NE2 1 
ATOM   2049 N N   . GLN B 2 161 ? -29.468 41.275  -27.869 1.00 27.03 ? 251 GLN B N   1 
ATOM   2050 C CA  . GLN B 2 161 ? -30.861 41.420  -28.262 1.00 34.62 ? 251 GLN B CA  1 
ATOM   2051 C C   . GLN B 2 161 ? -30.944 42.187  -29.574 1.00 30.37 ? 251 GLN B C   1 
ATOM   2052 O O   . GLN B 2 161 ? -30.054 42.968  -29.924 1.00 32.35 ? 251 GLN B O   1 
ATOM   2053 C CB  . GLN B 2 161 ? -31.675 42.133  -27.182 1.00 29.80 ? 251 GLN B CB  1 
ATOM   2054 C CG  . GLN B 2 161 ? -31.159 43.490  -26.779 1.00 30.23 ? 251 GLN B CG  1 
ATOM   2055 C CD  . GLN B 2 161 ? -32.094 44.160  -25.786 1.00 38.15 ? 251 GLN B CD  1 
ATOM   2056 O OE1 . GLN B 2 161 ? -31.820 45.247  -25.285 1.00 43.57 ? 251 GLN B OE1 1 
ATOM   2057 N NE2 . GLN B 2 161 ? -33.208 43.503  -25.497 1.00 40.76 ? 251 GLN B NE2 1 
ATOM   2058 N N   . ILE B 2 162 ? -31.988 41.937  -30.313 1.00 29.43 ? 252 ILE B N   1 
ATOM   2059 C CA  . ILE B 2 162 ? -32.202 42.666  -31.552 1.00 42.91 ? 252 ILE B CA  1 
ATOM   2060 C C   . ILE B 2 162 ? -32.988 43.919  -31.224 1.00 37.15 ? 252 ILE B C   1 
ATOM   2061 O O   . ILE B 2 162 ? -33.842 43.913  -30.328 1.00 39.18 ? 252 ILE B O   1 
ATOM   2062 C CB  . ILE B 2 162 ? -32.928 41.798  -32.598 1.00 50.43 ? 252 ILE B CB  1 
ATOM   2063 C CG1 . ILE B 2 162 ? -34.296 41.326  -32.080 1.00 48.54 ? 252 ILE B CG1 1 
ATOM   2064 C CG2 . ILE B 2 162 ? -32.045 40.622  -33.019 1.00 46.35 ? 252 ILE B CG2 1 
ATOM   2065 C CD1 . ILE B 2 162 ? -35.474 42.257  -32.426 1.00 45.51 ? 252 ILE B CD1 1 
ATOM   2066 N N   . CYS B 2 163 ? -32.674 45.005  -31.918 1.00 31.62 ? 253 CYS B N   1 
ATOM   2067 C CA  . CYS B 2 163 ? -33.558 46.162  -31.909 1.00 34.70 ? 253 CYS B CA  1 
ATOM   2068 C C   . CYS B 2 163 ? -33.114 47.135  -32.980 1.00 30.78 ? 253 CYS B C   1 
ATOM   2069 O O   . CYS B 2 163 ? -31.916 47.269  -33.267 1.00 27.37 ? 253 CYS B O   1 
ATOM   2070 C CB  . CYS B 2 163 ? -33.597 46.868  -30.557 1.00 38.09 ? 253 CYS B CB  1 
ATOM   2071 S SG  . CYS B 2 163 ? -32.068 47.603  -30.011 1.00 51.07 ? 253 CYS B SG  1 
ATOM   2072 N N   . ASN B 2 164 ? -34.104 47.825  -33.549 1.00 27.14 ? 254 ASN B N   1 
ATOM   2073 C CA  . ASN B 2 164 ? -33.842 48.708  -34.676 1.00 23.68 ? 254 ASN B CA  1 
ATOM   2074 C C   . ASN B 2 164 ? -33.150 49.991  -34.233 1.00 26.19 ? 254 ASN B C   1 
ATOM   2075 O O   . ASN B 2 164 ? -32.288 50.516  -34.949 1.00 22.75 ? 254 ASN B O   1 
ATOM   2076 C CB  . ASN B 2 164 ? -35.149 49.014  -35.402 1.00 26.23 ? 254 ASN B CB  1 
ATOM   2077 C CG  . ASN B 2 164 ? -35.513 47.937  -36.413 1.00 28.88 ? 254 ASN B CG  1 
ATOM   2078 O OD1 . ASN B 2 164 ? -35.911 46.822  -36.051 1.00 25.14 ? 254 ASN B OD1 1 
ATOM   2079 N ND2 . ASN B 2 164 ? -35.354 48.262  -37.692 1.00 21.81 ? 254 ASN B ND2 1 
ATOM   2080 N N   . VAL B 2 165 ? -33.498 50.510  -33.058 1.00 24.80 ? 255 VAL B N   1 
ATOM   2081 C CA  . VAL B 2 165 ? -33.029 51.832  -32.636 1.00 25.44 ? 255 VAL B CA  1 
ATOM   2082 C C   . VAL B 2 165 ? -32.162 51.645  -31.398 1.00 29.38 ? 255 VAL B C   1 
ATOM   2083 O O   . VAL B 2 165 ? -32.671 51.466  -30.286 1.00 25.24 ? 255 VAL B O   1 
ATOM   2084 C CB  . VAL B 2 165 ? -34.186 52.799  -32.380 1.00 26.68 ? 255 VAL B CB  1 
ATOM   2085 C CG1 . VAL B 2 165 ? -33.644 54.183  -31.996 1.00 29.70 ? 255 VAL B CG1 1 
ATOM   2086 C CG2 . VAL B 2 165 ? -35.039 52.906  -33.640 1.00 22.91 ? 255 VAL B CG2 1 
ATOM   2087 N N   . VAL B 2 166 ? -30.847 51.689  -31.585 1.00 30.09 ? 256 VAL B N   1 
ATOM   2088 C CA  . VAL B 2 166 ? -29.900 51.357  -30.527 1.00 32.68 ? 256 VAL B CA  1 
ATOM   2089 C C   . VAL B 2 166 ? -29.606 52.615  -29.720 1.00 35.92 ? 256 VAL B C   1 
ATOM   2090 O O   . VAL B 2 166 ? -29.203 53.637  -30.281 1.00 39.67 ? 256 VAL B O   1 
ATOM   2091 C CB  . VAL B 2 166 ? -28.606 50.766  -31.109 1.00 33.71 ? 256 VAL B CB  1 
ATOM   2092 C CG1 . VAL B 2 166 ? -27.644 50.427  -29.998 1.00 32.62 ? 256 VAL B CG1 1 
ATOM   2093 C CG2 . VAL B 2 166 ? -28.910 49.524  -31.947 1.00 32.56 ? 256 VAL B CG2 1 
ATOM   2094 N N   . ALA B 2 167 ? -29.816 52.549  -28.403 1.00 31.68 ? 257 ALA B N   1 
ATOM   2095 C CA  . ALA B 2 167 ? -29.417 53.659  -27.541 1.00 36.41 ? 257 ALA B CA  1 
ATOM   2096 C C   . ALA B 2 167 ? -27.937 53.564  -27.179 1.00 37.75 ? 257 ALA B C   1 
ATOM   2097 O O   . ALA B 2 167 ? -27.198 54.552  -27.270 1.00 31.09 ? 257 ALA B O   1 
ATOM   2098 C CB  . ALA B 2 167 ? -30.281 53.688  -26.277 1.00 37.56 ? 257 ALA B CB  1 
ATOM   2099 N N   . ILE B 2 168 ? -27.497 52.376  -26.761 1.00 34.11 ? 258 ILE B N   1 
ATOM   2100 C CA  . ILE B 2 168 ? -26.101 52.102  -26.456 1.00 31.72 ? 258 ILE B CA  1 
ATOM   2101 C C   . ILE B 2 168 ? -25.782 50.767  -27.119 1.00 35.80 ? 258 ILE B C   1 
ATOM   2102 O O   . ILE B 2 168 ? -26.402 49.753  -26.785 1.00 30.75 ? 258 ILE B O   1 
ATOM   2103 C CB  . ILE B 2 168 ? -25.828 52.006  -24.945 1.00 36.10 ? 258 ILE B CB  1 
ATOM   2104 C CG1 . ILE B 2 168 ? -26.411 53.207  -24.190 1.00 34.74 ? 258 ILE B CG1 1 
ATOM   2105 C CG2 . ILE B 2 168 ? -24.325 51.834  -24.690 1.00 30.93 ? 258 ILE B CG2 1 
ATOM   2106 C CD1 . ILE B 2 168 ? -25.570 54.437  -24.287 1.00 41.14 ? 258 ILE B CD1 1 
ATOM   2107 N N   . PRO B 2 169 ? -24.831 50.705  -28.051 1.00 32.64 ? 259 PRO B N   1 
ATOM   2108 C CA  . PRO B 2 169 ? -24.547 49.427  -28.719 1.00 34.80 ? 259 PRO B CA  1 
ATOM   2109 C C   . PRO B 2 169 ? -23.968 48.395  -27.763 1.00 30.55 ? 259 PRO B C   1 
ATOM   2110 O O   . PRO B 2 169 ? -23.301 48.723  -26.778 1.00 29.87 ? 259 PRO B O   1 
ATOM   2111 C CB  . PRO B 2 169 ? -23.536 49.808  -29.812 1.00 35.11 ? 259 PRO B CB  1 
ATOM   2112 C CG  . PRO B 2 169 ? -22.969 51.105  -29.386 1.00 38.12 ? 259 PRO B CG  1 
ATOM   2113 C CD  . PRO B 2 169 ? -24.042 51.815  -28.610 1.00 35.16 ? 259 PRO B CD  1 
ATOM   2114 N N   . GLY B 2 170 ? -24.263 47.131  -28.050 1.00 29.84 ? 260 GLY B N   1 
ATOM   2115 C CA  . GLY B 2 170 ? -23.660 46.053  -27.296 1.00 31.18 ? 260 GLY B CA  1 
ATOM   2116 C C   . GLY B 2 170 ? -22.205 45.854  -27.667 1.00 33.16 ? 260 GLY B C   1 
ATOM   2117 O O   . GLY B 2 170 ? -21.757 46.203  -28.758 1.00 29.67 ? 260 GLY B O   1 
ATOM   2118 N N   . ASN B 2 171 ? -21.449 45.283  -26.731 1.00 29.96 ? 261 ASN B N   1 
ATOM   2119 C CA  . ASN B 2 171 ? -20.051 44.943  -26.970 1.00 27.82 ? 261 ASN B CA  1 
ATOM   2120 C C   . ASN B 2 171 ? -19.819 43.517  -26.466 1.00 31.80 ? 261 ASN B C   1 
ATOM   2121 O O   . ASN B 2 171 ? -20.753 42.752  -26.190 1.00 24.87 ? 261 ASN B O   1 
ATOM   2122 C CB  . ASN B 2 171 ? -19.110 45.986  -26.338 1.00 30.84 ? 261 ASN B CB  1 
ATOM   2123 C CG  . ASN B 2 171 ? -19.362 46.201  -24.841 1.00 35.44 ? 261 ASN B CG  1 
ATOM   2124 O OD1 . ASN B 2 171 ? -19.939 45.354  -24.164 1.00 33.77 ? 261 ASN B OD1 1 
ATOM   2125 N ND2 . ASN B 2 171 ? -18.919 47.349  -24.324 1.00 33.51 ? 261 ASN B ND2 1 
ATOM   2126 N N   . ALA B 2 172 ? -18.548 43.135  -26.330 1.00 26.40 ? 262 ALA B N   1 
ATOM   2127 C CA  . ALA B 2 172 ? -18.233 41.758  -25.965 1.00 30.56 ? 262 ALA B CA  1 
ATOM   2128 C C   . ALA B 2 172 ? -18.662 41.405  -24.543 1.00 28.21 ? 262 ALA B C   1 
ATOM   2129 O O   . ALA B 2 172 ? -18.829 40.217  -24.241 1.00 25.63 ? 262 ALA B O   1 
ATOM   2130 C CB  . ALA B 2 172 ? -16.737 41.489  -26.138 1.00 26.85 ? 262 ALA B CB  1 
ATOM   2131 N N   . SER B 2 173 ? -18.855 42.393  -23.665 1.00 25.90 ? 263 SER B N   1 
ATOM   2132 C CA  . SER B 2 173 ? -19.224 42.112  -22.283 1.00 27.75 ? 263 SER B CA  1 
ATOM   2133 C C   . SER B 2 173 ? -20.559 42.720  -21.862 1.00 26.98 ? 263 SER B C   1 
ATOM   2134 O O   . SER B 2 173 ? -20.896 42.672  -20.669 1.00 30.34 ? 263 SER B O   1 
ATOM   2135 C CB  . SER B 2 173 ? -18.123 42.583  -21.330 1.00 31.39 ? 263 SER B CB  1 
ATOM   2136 O OG  . SER B 2 173 ? -18.012 43.989  -21.347 1.00 38.92 ? 263 SER B OG  1 
ATOM   2137 N N   . MET B 2 174 ? -21.349 43.259  -22.785 1.00 27.22 ? 264 MET B N   1 
ATOM   2138 C CA  . MET B 2 174 ? -22.658 43.730  -22.351 1.00 29.57 ? 264 MET B CA  1 
ATOM   2139 C C   . MET B 2 174 ? -23.625 43.753  -23.524 1.00 27.28 ? 264 MET B C   1 
ATOM   2140 O O   . MET B 2 174 ? -23.229 43.936  -24.676 1.00 27.36 ? 264 MET B O   1 
ATOM   2141 C CB  . MET B 2 174 ? -22.575 45.124  -21.710 1.00 32.54 ? 264 MET B CB  1 
ATOM   2142 C CG  . MET B 2 174 ? -22.666 46.265  -22.699 1.00 36.04 ? 264 MET B CG  1 
ATOM   2143 S SD  . MET B 2 174 ? -22.835 47.870  -21.893 1.00 67.27 ? 264 MET B SD  1 
ATOM   2144 C CE  . MET B 2 174 ? -21.774 47.636  -20.463 1.00 54.07 ? 264 MET B CE  1 
ATOM   2145 N N   . ASP B 2 175 ? -24.902 43.589  -23.202 1.00 27.97 ? 265 ASP B N   1 
ATOM   2146 C CA  . ASP B 2 175 ? -25.950 43.585  -24.204 1.00 29.38 ? 265 ASP B CA  1 
ATOM   2147 C C   . ASP B 2 175 ? -26.174 44.999  -24.736 1.00 31.84 ? 265 ASP B C   1 
ATOM   2148 O O   . ASP B 2 175 ? -25.846 45.999  -24.086 1.00 28.92 ? 265 ASP B O   1 
ATOM   2149 C CB  . ASP B 2 175 ? -27.238 43.023  -23.605 1.00 24.77 ? 265 ASP B CB  1 
ATOM   2150 C CG  . ASP B 2 175 ? -28.152 42.412  -24.647 1.00 32.87 ? 265 ASP B CG  1 
ATOM   2151 O OD1 . ASP B 2 175 ? -27.879 42.541  -25.866 1.00 29.75 ? 265 ASP B OD1 1 
ATOM   2152 O OD2 . ASP B 2 175 ? -29.153 41.794  -24.239 1.00 30.39 ? 265 ASP B OD2 1 
ATOM   2153 N N   . ALA B 2 176 ? -26.711 45.076  -25.952 1.00 29.87 ? 266 ALA B N   1 
ATOM   2154 C CA  . ALA B 2 176 ? -27.174 46.361  -26.446 1.00 31.19 ? 266 ALA B CA  1 
ATOM   2155 C C   . ALA B 2 176 ? -28.310 46.865  -25.562 1.00 32.37 ? 266 ALA B C   1 
ATOM   2156 O O   . ALA B 2 176 ? -29.072 46.086  -24.987 1.00 33.19 ? 266 ALA B O   1 
ATOM   2157 C CB  . ALA B 2 176 ? -27.634 46.245  -27.900 1.00 29.69 ? 266 ALA B CB  1 
ATOM   2158 N N   . VAL B 2 177 ? -28.361 48.187  -25.404 1.00 28.73 ? 267 VAL B N   1 
ATOM   2159 C CA  . VAL B 2 177 ? -29.479 48.859  -24.689 1.00 34.73 ? 267 VAL B CA  1 
ATOM   2160 C C   . VAL B 2 177 ? -30.369 49.489  -25.763 1.00 32.55 ? 267 VAL B C   1 
ATOM   2161 O O   . VAL B 2 177 ? -29.856 50.303  -26.532 1.00 30.51 ? 267 VAL B O   1 
ATOM   2162 C CB  . VAL B 2 177 ? -28.961 49.918  -23.700 1.00 38.70 ? 267 VAL B CB  1 
ATOM   2163 C CG1 . VAL B 2 177 ? -30.082 50.800  -23.180 1.00 37.69 ? 267 VAL B CG1 1 
ATOM   2164 C CG2 . VAL B 2 177 ? -28.193 49.280  -22.554 1.00 35.95 ? 267 VAL B CG2 1 
ATOM   2165 N N   . CYS B 2 178 ? -31.655 49.161  -25.772 1.00 34.95 ? 268 CYS B N   1 
ATOM   2166 C CA  . CYS B 2 178 ? -32.549 49.609  -26.876 1.00 34.57 ? 268 CYS B CA  1 
ATOM   2167 C C   . CYS B 2 178 ? -33.474 50.773  -26.493 1.00 39.77 ? 268 CYS B C   1 
ATOM   2168 O O   . CYS B 2 178 ? -34.023 50.755  -25.393 1.00 43.18 ? 268 CYS B O   1 
ATOM   2169 C CB  . CYS B 2 178 ? -33.319 48.405  -27.401 1.00 35.35 ? 268 CYS B CB  1 
ATOM   2170 S SG  . CYS B 2 178 ? -32.185 47.142  -28.040 1.00 61.19 ? 268 CYS B SG  1 
ATOM   2171 N N   . THR B 2 179 ? -33.611 51.749  -27.392 1.00 35.02 ? 269 THR B N   1 
ATOM   2172 C CA  . THR B 2 179 ? -34.498 52.918  -27.162 1.00 44.50 ? 269 THR B CA  1 
ATOM   2173 C C   . THR B 2 179 ? -35.969 52.490  -27.237 1.00 46.38 ? 269 THR B C   1 
ATOM   2174 O O   . THR B 2 179 ? -36.537 52.256  -26.164 1.00 55.89 ? 269 THR B O   1 
ATOM   2175 C CB  . THR B 2 179 ? -34.202 54.044  -28.160 1.00 30.00 ? 269 THR B CB  1 
ATOM   2176 O OG1 . THR B 2 179 ? -34.975 53.780  -29.329 1.00 30.00 ? 269 THR B OG1 1 
ATOM   2177 C CG2 . THR B 2 179 ? -32.741 54.137  -28.529 1.00 30.00 ? 269 THR B CG2 1 
HETATM 2178 O O   . HOH C 3 .   ? 21.528  0.356   -8.587  1.00 49.66 ? 201 HOH A O   1 
HETATM 2179 O O   . HOH C 3 .   ? 19.125  8.328   -18.140 1.00 44.45 ? 202 HOH A O   1 
HETATM 2180 O O   . HOH C 3 .   ? 4.331   4.201   2.127   1.00 36.73 ? 203 HOH A O   1 
HETATM 2181 O O   . HOH C 3 .   ? -0.878  -0.441  -18.851 1.00 43.64 ? 204 HOH A O   1 
HETATM 2182 O O   . HOH C 3 .   ? 0.980   12.656  -20.792 1.00 30.36 ? 205 HOH A O   1 
HETATM 2183 O O   . HOH C 3 .   ? 4.621   -0.004  -23.700 1.00 32.32 ? 206 HOH A O   1 
HETATM 2184 O O   . HOH C 3 .   ? 9.348   -16.724 -14.907 1.00 41.50 ? 207 HOH A O   1 
HETATM 2185 O O   . HOH C 3 .   ? 3.533   13.806  5.376   1.00 38.98 ? 208 HOH A O   1 
HETATM 2186 O O   . HOH C 3 .   ? 15.611  21.260  -12.044 1.00 36.92 ? 209 HOH A O   1 
HETATM 2187 O O   . HOH C 3 .   ? -0.112  1.907   -7.090  1.00 24.62 ? 210 HOH A O   1 
HETATM 2188 O O   . HOH C 3 .   ? -0.811  14.925  1.357   1.00 43.07 ? 211 HOH A O   1 
HETATM 2189 O O   . HOH C 3 .   ? -1.568  -10.875 -12.088 1.00 33.36 ? 212 HOH A O   1 
HETATM 2190 O O   . HOH C 3 .   ? 12.118  3.831   1.738   1.00 35.01 ? 213 HOH A O   1 
HETATM 2191 O O   . HOH C 3 .   ? 15.079  -11.469 -1.016  1.00 37.91 ? 214 HOH A O   1 
HETATM 2192 O O   . HOH C 3 .   ? 6.105   9.669   -23.072 1.00 32.00 ? 215 HOH A O   1 
HETATM 2193 O O   . HOH C 3 .   ? 15.972  9.149   -9.447  1.00 31.46 ? 216 HOH A O   1 
HETATM 2194 O O   . HOH C 3 .   ? 7.796   -13.663 -9.365  1.00 38.01 ? 217 HOH A O   1 
HETATM 2195 O O   . HOH C 3 .   ? 15.076  -2.972  -21.219 1.00 29.83 ? 218 HOH A O   1 
HETATM 2196 O O   . HOH C 3 .   ? -2.033  -13.263 -10.719 1.00 21.88 ? 219 HOH A O   1 
HETATM 2197 O O   . HOH C 3 .   ? 2.865   7.373   -0.300  1.00 32.86 ? 220 HOH A O   1 
HETATM 2198 O O   . HOH C 3 .   ? 1.556   10.866  2.606   1.00 39.28 ? 221 HOH A O   1 
HETATM 2199 O O   . HOH C 3 .   ? 10.341  16.362  -5.752  1.00 42.62 ? 222 HOH A O   1 
HETATM 2200 O O   . HOH C 3 .   ? 2.238   14.721  -21.782 1.00 31.19 ? 223 HOH A O   1 
HETATM 2201 O O   . HOH C 3 .   ? 10.766  -8.423  -19.407 1.00 36.22 ? 224 HOH A O   1 
HETATM 2202 O O   . HOH C 3 .   ? 4.682   18.676  -5.842  1.00 36.90 ? 225 HOH A O   1 
HETATM 2203 O O   . HOH C 3 .   ? 0.975   6.651   -14.817 1.00 25.31 ? 226 HOH A O   1 
HETATM 2204 O O   . HOH C 3 .   ? 8.882   9.125   -5.453  1.00 25.59 ? 227 HOH A O   1 
HETATM 2205 O O   . HOH C 3 .   ? 1.843   -4.829  -20.725 1.00 38.24 ? 228 HOH A O   1 
HETATM 2206 O O   . HOH C 3 .   ? 7.635   16.827  -5.167  1.00 34.69 ? 229 HOH A O   1 
HETATM 2207 O O   . HOH C 3 .   ? 9.549   14.857  -20.411 1.00 35.11 ? 230 HOH A O   1 
HETATM 2208 O O   . HOH C 3 .   ? 0.505   -3.078  -11.796 1.00 28.57 ? 231 HOH A O   1 
HETATM 2209 O O   . HOH C 3 .   ? 7.374   -5.359  -25.360 1.00 31.75 ? 232 HOH A O   1 
HETATM 2210 O O   . HOH C 3 .   ? 14.181  -13.134 -8.395  1.00 32.02 ? 233 HOH A O   1 
HETATM 2211 O O   . HOH C 3 .   ? 16.183  -16.645 -4.137  1.00 37.87 ? 234 HOH A O   1 
HETATM 2212 O O   . HOH C 3 .   ? -1.994  3.306   -11.044 1.00 26.60 ? 235 HOH A O   1 
HETATM 2213 O O   . HOH C 3 .   ? 4.964   27.576  -21.720 1.00 48.37 ? 236 HOH A O   1 
HETATM 2214 O O   . HOH C 3 .   ? 18.586  -2.728  -22.320 1.00 33.46 ? 237 HOH A O   1 
HETATM 2215 O O   . HOH C 3 .   ? 11.276  13.179  -0.381  1.00 33.35 ? 238 HOH A O   1 
HETATM 2216 O O   . HOH C 3 .   ? 9.200   4.593   -22.746 1.00 34.48 ? 239 HOH A O   1 
HETATM 2217 O O   . HOH C 3 .   ? 10.832  10.479  1.979   1.00 33.09 ? 240 HOH A O   1 
HETATM 2218 O O   . HOH C 3 .   ? 20.818  -0.081  -12.491 1.00 27.72 ? 241 HOH A O   1 
HETATM 2219 O O   . HOH C 3 .   ? 10.447  -2.373  -0.789  1.00 25.48 ? 242 HOH A O   1 
HETATM 2220 O O   . HOH C 3 .   ? -0.774  20.148  -21.061 1.00 44.40 ? 243 HOH A O   1 
HETATM 2221 O O   . HOH C 3 .   ? 1.564   0.843   -22.327 1.00 40.85 ? 244 HOH A O   1 
HETATM 2222 O O   . HOH C 3 .   ? 21.261  -13.777 -8.278  1.00 39.81 ? 245 HOH A O   1 
HETATM 2223 O O   . HOH C 3 .   ? 7.765   -18.178 -15.230 1.00 34.73 ? 246 HOH A O   1 
HETATM 2224 O O   . HOH C 3 .   ? 9.237   -12.241 -7.611  1.00 28.19 ? 247 HOH A O   1 
HETATM 2225 O O   . HOH C 3 .   ? 20.805  -11.785 -15.364 1.00 39.56 ? 248 HOH A O   1 
HETATM 2226 O O   . HOH C 3 .   ? 18.225  -11.079 -15.984 1.00 34.11 ? 249 HOH A O   1 
HETATM 2227 O O   . HOH C 3 .   ? 11.943  18.208  -6.745  1.00 37.68 ? 250 HOH A O   1 
HETATM 2228 O O   . HOH C 3 .   ? -0.441  -0.748  -11.149 1.00 33.29 ? 251 HOH A O   1 
HETATM 2229 O O   . HOH C 3 .   ? 3.383   -2.678  -24.399 1.00 44.15 ? 252 HOH A O   1 
HETATM 2230 O O   . HOH C 3 .   ? 16.034  -9.282  -0.853  1.00 37.31 ? 253 HOH A O   1 
HETATM 2231 O O   . HOH C 3 .   ? 20.661  -14.216 -14.987 1.00 46.17 ? 254 HOH A O   1 
HETATM 2232 O O   . HOH C 3 .   ? 9.587   -13.449 -5.046  1.00 37.25 ? 255 HOH A O   1 
HETATM 2233 O O   . HOH C 3 .   ? 7.994   19.551  -4.952  1.00 37.77 ? 256 HOH A O   1 
HETATM 2234 O O   . HOH D 3 .   ? -17.460 47.576  -22.731 1.00 47.66 ? 301 HOH B O   1 
HETATM 2235 O O   . HOH D 3 .   ? -18.211 29.052  -13.224 1.00 33.55 ? 302 HOH B O   1 
HETATM 2236 O O   . HOH D 3 .   ? -12.752 6.755   1.248   1.00 37.51 ? 303 HOH B O   1 
HETATM 2237 O O   . HOH D 3 .   ? -17.539 34.957  -19.466 1.00 19.84 ? 304 HOH B O   1 
HETATM 2238 O O   . HOH D 3 .   ? 5.214   -25.539 -19.104 1.00 47.61 ? 305 HOH B O   1 
HETATM 2239 O O   . HOH D 3 .   ? -12.055 21.115  -22.196 1.00 36.48 ? 306 HOH B O   1 
HETATM 2240 O O   . HOH D 3 .   ? -19.511 48.784  -22.390 1.00 51.88 ? 307 HOH B O   1 
HETATM 2241 O O   . HOH D 3 .   ? -8.709  -7.705  4.366   1.00 33.61 ? 308 HOH B O   1 
HETATM 2242 O O   . HOH D 3 .   ? 9.134   -32.950 -4.577  1.00 31.71 ? 309 HOH B O   1 
HETATM 2243 O O   . HOH D 3 .   ? -8.004  4.828   1.946   1.00 27.27 ? 310 HOH B O   1 
HETATM 2244 O O   . HOH D 3 .   ? -3.794  20.188  -6.665  1.00 39.24 ? 311 HOH B O   1 
HETATM 2245 O O   . HOH D 3 .   ? -8.727  10.885  -14.655 1.00 37.36 ? 312 HOH B O   1 
HETATM 2246 O O   . HOH D 3 .   ? -7.378  26.327  -15.100 1.00 34.26 ? 313 HOH B O   1 
HETATM 2247 O O   . HOH D 3 .   ? -2.852  21.755  -16.444 1.00 39.49 ? 314 HOH B O   1 
HETATM 2248 O O   . HOH D 3 .   ? -23.687 33.925  -21.455 1.00 36.37 ? 315 HOH B O   1 
HETATM 2249 O O   . HOH D 3 .   ? -5.692  17.800  -19.847 1.00 39.60 ? 316 HOH B O   1 
HETATM 2250 O O   . HOH D 3 .   ? -22.010 35.398  -19.638 1.00 30.68 ? 317 HOH B O   1 
HETATM 2251 O O   . HOH D 3 .   ? -3.063  8.172   -5.181  1.00 33.15 ? 318 HOH B O   1 
HETATM 2252 O O   . HOH D 3 .   ? -7.399  -24.287 -4.186  1.00 35.07 ? 319 HOH B O   1 
HETATM 2253 O O   . HOH D 3 .   ? -8.333  8.709   -14.675 1.00 34.94 ? 320 HOH B O   1 
HETATM 2254 O O   . HOH D 3 .   ? -11.178 17.984  -23.862 1.00 41.85 ? 321 HOH B O   1 
HETATM 2255 O O   . HOH D 3 .   ? -7.982  -14.558 -11.382 1.00 28.49 ? 322 HOH B O   1 
HETATM 2256 O O   . HOH D 3 .   ? 6.797   -14.070 -2.317  1.00 28.67 ? 323 HOH B O   1 
HETATM 2257 O O   . HOH D 3 .   ? -11.587 15.535  -12.791 1.00 33.42 ? 324 HOH B O   1 
HETATM 2258 O O   . HOH D 3 .   ? -29.618 46.028  -33.360 1.00 32.86 ? 325 HOH B O   1 
HETATM 2259 O O   . HOH D 3 .   ? -4.956  6.075   -6.329  1.00 33.47 ? 326 HOH B O   1 
HETATM 2260 O O   . HOH D 3 .   ? -12.797 26.674  -11.341 1.00 36.50 ? 327 HOH B O   1 
HETATM 2261 O O   . HOH D 3 .   ? -20.668 25.567  -21.499 1.00 32.56 ? 328 HOH B O   1 
HETATM 2262 O O   . HOH D 3 .   ? -1.821  -0.479  -8.573  1.00 24.09 ? 329 HOH B O   1 
HETATM 2263 O O   . HOH D 3 .   ? -7.600  -34.056 -14.819 1.00 49.85 ? 330 HOH B O   1 
HETATM 2264 O O   . HOH D 3 .   ? 4.007   -3.472  -3.536  1.00 29.49 ? 331 HOH B O   1 
HETATM 2265 O O   . HOH D 3 .   ? -2.097  4.929   -14.149 1.00 34.41 ? 332 HOH B O   1 
HETATM 2266 O O   . HOH D 3 .   ? -8.381  21.903  -22.209 1.00 36.86 ? 333 HOH B O   1 
HETATM 2267 O O   . HOH D 3 .   ? 8.243   -22.711 -4.869  1.00 25.12 ? 334 HOH B O   1 
HETATM 2268 O O   . HOH D 3 .   ? -2.150  3.336   -8.157  1.00 25.17 ? 335 HOH B O   1 
HETATM 2269 O O   . HOH D 3 .   ? 3.984   -13.342 4.416   1.00 31.64 ? 336 HOH B O   1 
HETATM 2270 O O   . HOH D 3 .   ? -12.430 -3.956  0.335   1.00 31.30 ? 337 HOH B O   1 
HETATM 2271 O O   . HOH D 3 .   ? -3.517  18.328  -18.077 1.00 30.04 ? 338 HOH B O   1 
HETATM 2272 O O   . HOH D 3 .   ? -6.306  -10.344 3.653   1.00 35.95 ? 339 HOH B O   1 
HETATM 2273 O O   . HOH D 3 .   ? -14.042 2.722   -0.495  1.00 31.73 ? 340 HOH B O   1 
HETATM 2274 O O   . HOH D 3 .   ? -17.218 23.851  -18.494 1.00 31.07 ? 341 HOH B O   1 
HETATM 2275 O O   . HOH D 3 .   ? -29.608 39.326  -25.292 1.00 36.35 ? 342 HOH B O   1 
HETATM 2276 O O   . HOH D 3 .   ? -14.008 40.129  -28.518 1.00 32.79 ? 343 HOH B O   1 
HETATM 2277 O O   . HOH D 3 .   ? -4.292  17.554  -6.831  1.00 28.47 ? 344 HOH B O   1 
HETATM 2278 O O   . HOH D 3 .   ? -7.630  -18.168 2.575   1.00 35.38 ? 345 HOH B O   1 
HETATM 2279 O O   . HOH D 3 .   ? -5.072  24.738  -14.856 1.00 34.29 ? 346 HOH B O   1 
HETATM 2280 O O   . HOH D 3 .   ? 1.832   -21.102 -7.079  1.00 18.55 ? 347 HOH B O   1 
HETATM 2281 O O   . HOH D 3 .   ? -9.259  -11.100 1.881   1.00 29.09 ? 348 HOH B O   1 
HETATM 2282 O O   . HOH D 3 .   ? 0.014   11.323  -0.191  1.00 27.28 ? 349 HOH B O   1 
HETATM 2283 O O   . HOH D 3 .   ? -1.946  7.322   -16.226 1.00 31.00 ? 350 HOH B O   1 
HETATM 2284 O O   . HOH D 3 .   ? -6.382  -17.592 -0.620  1.00 33.07 ? 351 HOH B O   1 
HETATM 2285 O O   . HOH D 3 .   ? -19.312 30.703  -26.263 1.00 25.43 ? 352 HOH B O   1 
HETATM 2286 O O   . HOH D 3 .   ? -19.917 42.003  -29.253 1.00 30.69 ? 353 HOH B O   1 
HETATM 2287 O O   . HOH D 3 .   ? -7.405  -21.639 -4.499  1.00 27.78 ? 354 HOH B O   1 
HETATM 2288 O O   . HOH D 3 .   ? -8.230  -35.925 -1.537  1.00 36.55 ? 355 HOH B O   1 
HETATM 2289 O O   . HOH D 3 .   ? -4.974  -18.888 2.551   1.00 34.30 ? 356 HOH B O   1 
HETATM 2290 O O   . HOH D 3 .   ? -13.908 19.323  -15.047 1.00 32.74 ? 357 HOH B O   1 
HETATM 2291 O O   . HOH D 3 .   ? -14.215 -14.485 -5.088  1.00 30.09 ? 358 HOH B O   1 
HETATM 2292 O O   . HOH D 3 .   ? 4.881   -24.366 -2.426  1.00 30.89 ? 359 HOH B O   1 
HETATM 2293 O O   . HOH D 3 .   ? -11.256 -34.623 -8.489  1.00 42.76 ? 360 HOH B O   1 
HETATM 2294 O O   . HOH D 3 .   ? -6.535  9.225   0.867   1.00 31.18 ? 361 HOH B O   1 
HETATM 2295 O O   . HOH D 3 .   ? -18.174 32.634  -19.298 1.00 26.91 ? 362 HOH B O   1 
HETATM 2296 O O   . HOH D 3 .   ? 1.851   -6.904  1.713   1.00 32.29 ? 363 HOH B O   1 
HETATM 2297 O O   . HOH D 3 .   ? -10.328 18.880  -6.793  1.00 30.01 ? 364 HOH B O   1 
HETATM 2298 O O   . HOH D 3 .   ? -10.664 -0.715  -8.017  1.00 42.97 ? 365 HOH B O   1 
HETATM 2299 O O   . HOH D 3 .   ? 2.000   -25.446 0.478   1.00 28.21 ? 366 HOH B O   1 
HETATM 2300 O O   . HOH D 3 .   ? -13.418 40.185  -25.632 1.00 33.29 ? 367 HOH B O   1 
HETATM 2301 O O   . HOH D 3 .   ? -6.543  7.754   -8.110  1.00 27.16 ? 368 HOH B O   1 
HETATM 2302 O O   . HOH D 3 .   ? -32.637 47.437  -23.651 1.00 38.42 ? 369 HOH B O   1 
HETATM 2303 O O   . HOH D 3 .   ? -29.309 37.569  -22.969 1.00 41.56 ? 370 HOH B O   1 
HETATM 2304 O O   . HOH D 3 .   ? -16.974 20.311  -12.766 1.00 36.39 ? 371 HOH B O   1 
HETATM 2305 O O   . HOH D 3 .   ? -8.769  29.279  -23.012 1.00 33.36 ? 372 HOH B O   1 
HETATM 2306 O O   . HOH D 3 .   ? -3.661  11.143  -5.997  1.00 33.72 ? 373 HOH B O   1 
HETATM 2307 O O   . HOH D 3 .   ? -11.230 -17.726 -8.897  1.00 28.21 ? 374 HOH B O   1 
HETATM 2308 O O   . HOH D 3 .   ? -3.067  -22.450 -1.231  1.00 34.49 ? 375 HOH B O   1 
HETATM 2309 O O   . HOH D 3 .   ? -33.796 39.932  -29.265 1.00 39.76 ? 376 HOH B O   1 
HETATM 2310 O O   . HOH D 3 .   ? -16.155 44.493  -27.235 1.00 39.73 ? 377 HOH B O   1 
HETATM 2311 O O   . HOH D 3 .   ? -4.856  3.843   -11.186 1.00 26.86 ? 378 HOH B O   1 
HETATM 2312 O O   . HOH D 3 .   ? -5.199  14.786  -17.952 1.00 32.67 ? 379 HOH B O   1 
HETATM 2313 O O   . HOH D 3 .   ? -12.269 -10.234 -7.551  1.00 38.19 ? 380 HOH B O   1 
HETATM 2314 O O   . HOH D 3 .   ? -25.702 43.597  -20.395 1.00 29.16 ? 381 HOH B O   1 
HETATM 2315 O O   . HOH D 3 .   ? -1.528  4.156   1.723   1.00 30.55 ? 382 HOH B O   1 
HETATM 2316 O O   . HOH D 3 .   ? -2.203  15.931  -5.832  1.00 34.96 ? 383 HOH B O   1 
HETATM 2317 O O   . HOH D 3 .   ? -2.763  17.355  1.541   1.00 35.67 ? 384 HOH B O   1 
HETATM 2318 O O   . HOH D 3 .   ? -5.265  24.966  -19.045 1.00 38.21 ? 385 HOH B O   1 
HETATM 2319 O O   . HOH D 3 .   ? -6.527  20.667  -20.311 1.00 33.32 ? 386 HOH B O   1 
HETATM 2320 O O   . HOH D 3 .   ? -11.566 19.388  -28.818 1.00 49.40 ? 387 HOH B O   1 
HETATM 2321 O O   . HOH D 3 .   ? -15.603 26.505  -12.079 1.00 40.37 ? 388 HOH B O   1 
HETATM 2322 O O   . HOH D 3 .   ? -9.545  31.220  -14.337 1.00 39.84 ? 389 HOH B O   1 
HETATM 2323 O O   . HOH D 3 .   ? -10.982 -12.809 -9.118  1.00 26.90 ? 390 HOH B O   1 
HETATM 2324 O O   . HOH D 3 .   ? -5.547  -20.537 -1.700  1.00 42.49 ? 391 HOH B O   1 
HETATM 2325 O O   . HOH D 3 .   ? -19.700 36.777  -12.736 1.00 42.49 ? 392 HOH B O   1 
HETATM 2326 O O   . HOH D 3 .   ? 5.998   -16.356 -4.975  1.00 32.44 ? 393 HOH B O   1 
HETATM 2327 O O   . HOH D 3 .   ? -0.806  -14.467 6.353   1.00 33.95 ? 394 HOH B O   1 
HETATM 2328 O O   . HOH D 3 .   ? -29.156 36.052  -25.671 1.00 41.61 ? 395 HOH B O   1 
HETATM 2329 O O   . HOH D 3 .   ? 0.862   -28.290 -0.124  1.00 28.80 ? 396 HOH B O   1 
HETATM 2330 O O   . HOH D 3 .   ? -1.809  -21.263 1.807   1.00 22.71 ? 397 HOH B O   1 
HETATM 2331 O O   . HOH D 3 .   ? -26.865 45.994  -21.260 1.00 31.29 ? 398 HOH B O   1 
HETATM 2332 O O   . HOH D 3 .   ? -20.721 31.131  -28.199 1.00 46.81 ? 399 HOH B O   1 
HETATM 2333 O O   . HOH D 3 .   ? -5.302  -21.611 -15.622 1.00 44.34 ? 400 HOH B O   1 
HETATM 2334 O O   . HOH D 3 .   ? -7.960  -13.117 3.284   1.00 33.57 ? 401 HOH B O   1 
HETATM 2335 O O   . HOH D 3 .   ? -25.649 46.511  -30.677 1.00 36.49 ? 402 HOH B O   1 
HETATM 2336 O O   . HOH D 3 .   ? -11.835 13.321  -11.244 1.00 30.29 ? 403 HOH B O   1 
HETATM 2337 O O   . HOH D 3 .   ? 0.617   7.608   0.909   1.00 32.29 ? 404 HOH B O   1 
HETATM 2338 O O   . HOH D 3 .   ? 8.469   -19.580 -4.779  1.00 26.42 ? 405 HOH B O   1 
HETATM 2339 O O   . HOH D 3 .   ? -12.042 -24.406 -7.351  1.00 39.07 ? 406 HOH B O   1 
HETATM 2340 O O   . HOH D 3 .   ? 8.364   -23.535 -7.662  1.00 36.26 ? 407 HOH B O   1 
HETATM 2341 O O   . HOH D 3 .   ? 8.772   -30.641 -6.360  1.00 34.16 ? 408 HOH B O   1 
HETATM 2342 O O   . HOH D 3 .   ? 2.901   -8.795  0.255   1.00 30.61 ? 409 HOH B O   1 
HETATM 2343 O O   . HOH D 3 .   ? -24.326 43.323  -17.958 1.00 35.28 ? 410 HOH B O   1 
HETATM 2344 O O   . HOH D 3 .   ? -11.114 34.774  -19.977 1.00 34.26 ? 411 HOH B O   1 
HETATM 2345 O O   . HOH D 3 .   ? -4.664  -7.314  -8.441  1.00 36.98 ? 412 HOH B O   1 
HETATM 2346 O O   . HOH D 3 .   ? 4.250   -25.527 1.947   1.00 26.23 ? 413 HOH B O   1 
HETATM 2347 O O   . HOH D 3 .   ? -24.653 31.406  -21.062 1.00 37.12 ? 414 HOH B O   1 
HETATM 2348 O O   . HOH D 3 .   ? -10.521 7.586   -14.334 1.00 39.28 ? 415 HOH B O   1 
HETATM 2349 O O   . HOH D 3 .   ? -11.508 -12.793 -0.263  1.00 31.22 ? 416 HOH B O   1 
HETATM 2350 O O   . HOH D 3 .   ? 7.141   -32.582 -20.042 1.00 45.73 ? 417 HOH B O   1 
HETATM 2351 O O   . HOH D 3 .   ? -9.865  11.635  -11.873 1.00 38.00 ? 418 HOH B O   1 
HETATM 2352 O O   . HOH D 3 .   ? 3.303   -34.605 -0.956  1.00 38.01 ? 419 HOH B O   1 
HETATM 2353 O O   . HOH D 3 .   ? -12.618 -15.570 -9.898  1.00 41.47 ? 420 HOH B O   1 
HETATM 2354 O O   . HOH D 3 .   ? -6.385  -19.799 0.311   1.00 38.83 ? 421 HOH B O   1 
HETATM 2355 O O   . HOH D 3 .   ? -31.458 56.693  -29.269 1.00 47.21 ? 422 HOH B O   1 
HETATM 2356 O O   . HOH D 3 .   ? -13.335 17.519  -24.941 1.00 44.14 ? 423 HOH B O   1 
HETATM 2357 O O   . HOH D 3 .   ? -2.535  20.654  -18.485 1.00 34.38 ? 424 HOH B O   1 
HETATM 2358 O O   . HOH D 3 .   ? -13.948 -12.466 -3.969  1.00 34.68 ? 425 HOH B O   1 
HETATM 2359 O O   . HOH D 3 .   ? -13.092 -32.488 -24.414 1.00 42.09 ? 426 HOH B O   1 
HETATM 2360 O O   . HOH D 3 .   ? 8.848   -15.705 -4.837  1.00 41.49 ? 427 HOH B O   1 
HETATM 2361 O O   . HOH D 3 .   ? -4.235  -21.194 0.927   1.00 37.16 ? 428 HOH B O   1 
HETATM 2362 O O   . HOH D 3 .   ? -40.832 54.635  -26.985 1.00 42.53 ? 429 HOH B O   1 
HETATM 2363 O O   . HOH D 3 .   ? -5.123  -6.437  -10.919 1.00 43.12 ? 430 HOH B O   1 
# 
