data_9EBR
# 
_entry.id   9EBR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EBR         pdb_00009ebr 10.2210/pdb9ebr/pdb 
WWPDB D_1000290129 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-22 ? 
2 'Structure model' 1 1 2025-02-19 ? 
3 'Structure model' 1 2 2025-04-02 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 '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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.journal_volume'          
11 3 'Structure model' '_citation.page_first'              
12 3 'Structure model' '_citation.page_last'               
13 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2025-01-22 
_pdbx_database_PDB_obs_spr.pdb_id           9EBR 
_pdbx_database_PDB_obs_spr.replace_pdb_id   9BUL 
_pdbx_database_PDB_obs_spr.details          ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EBR 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-13 
_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              glasfeld@reed.edu 
_pdbx_contact_author.name_first         Arthur 
_pdbx_contact_author.name_last          Glasfeld 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0680-0263 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Glasfeld, A.'  1 0000-0003-0680-0263 
'Cheng, D.W.C.' 2 0000-0003-1545-0269 
'Li, Y.'        3 0000-0001-6593-1453 
# 
_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                   GW 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Inorg.Chem. 
_citation.journal_id_ASTM           JJBCFA 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1432-1327 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            30 
_citation.language                  ? 
_citation.page_first                169 
_citation.page_last                 179 
_citation.title                     
'The activation of the metal-containing regulatory protein NiaR from Thermotoga maritima by its effector, nicotinic acid.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1007/s00775-025-02096-y 
_citation.pdbx_database_id_PubMed   39899144 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cheng, W.C.D.'     1 ? 
primary 'Li, Y.'            2 ? 
primary 'Nakashima, M.'     3 ? 
primary 'Moenne-Loccoz, P.' 4 ? 
primary 'Rush, K.W.'        5 ? 
primary 'Glasfeld, A.'      6 ? 
# 
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 'Probable transcription repressor NiaR' 19583.803 1 ? ? ? ? 
2 non-polymer syn 'FE (II) ION'                           55.845    1 ? ? ? ? 
3 non-polymer syn 'NICOTINIC ACID'                        123.109   1 ? ? ? ? 
4 non-polymer syn PROLINE                                 115.130   1 ? ? ? ? 
5 water       nat water                                   18.015    9 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MHMKTVRQERLKSIVRILERSKEPVSGAQLAEELSVSRQVIVQDIAYLRSLGYNIVATPRGYVLAGGKSGVSRLVAVKHA
PEEIKEELLCVVRNGGRIVDVIVEHPVYGEIRGIIDVSSEEEVLKFVNLMEMAKTEPLLTLSGGVHLHTIEAPDEETMER
IMRELKKKGFLIEEG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHMKTVRQERLKSIVRILERSKEPVSGAQLAEELSVSRQVIVQDIAYLRSLGYNIVATPRGYVLAGGKSGVSRLVAVKHA
PEEIKEELLCVVRNGGRIVDVIVEHPVYGEIRGIIDVSSEEEVLKFVNLMEMAKTEPLLTLSGGVHLHTIEAPDEETMER
IMRELKKKGFLIEEG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FE (II) ION'    FE2 
3 'NICOTINIC ACID' NIO 
4 PROLINE          PRO 
5 water            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   MET n 
1 4   LYS n 
1 5   THR n 
1 6   VAL n 
1 7   ARG n 
1 8   GLN n 
1 9   GLU n 
1 10  ARG n 
1 11  LEU n 
1 12  LYS n 
1 13  SER n 
1 14  ILE n 
1 15  VAL n 
1 16  ARG n 
1 17  ILE n 
1 18  LEU n 
1 19  GLU n 
1 20  ARG n 
1 21  SER n 
1 22  LYS n 
1 23  GLU n 
1 24  PRO n 
1 25  VAL n 
1 26  SER n 
1 27  GLY n 
1 28  ALA n 
1 29  GLN n 
1 30  LEU n 
1 31  ALA n 
1 32  GLU n 
1 33  GLU n 
1 34  LEU n 
1 35  SER n 
1 36  VAL n 
1 37  SER n 
1 38  ARG n 
1 39  GLN n 
1 40  VAL n 
1 41  ILE n 
1 42  VAL n 
1 43  GLN n 
1 44  ASP n 
1 45  ILE n 
1 46  ALA n 
1 47  TYR n 
1 48  LEU n 
1 49  ARG n 
1 50  SER n 
1 51  LEU n 
1 52  GLY n 
1 53  TYR n 
1 54  ASN n 
1 55  ILE n 
1 56  VAL n 
1 57  ALA n 
1 58  THR n 
1 59  PRO n 
1 60  ARG n 
1 61  GLY n 
1 62  TYR n 
1 63  VAL n 
1 64  LEU n 
1 65  ALA n 
1 66  GLY n 
1 67  GLY n 
1 68  LYS n 
1 69  SER n 
1 70  GLY n 
1 71  VAL n 
1 72  SER n 
1 73  ARG n 
1 74  LEU n 
1 75  VAL n 
1 76  ALA n 
1 77  VAL n 
1 78  LYS n 
1 79  HIS n 
1 80  ALA n 
1 81  PRO n 
1 82  GLU n 
1 83  GLU n 
1 84  ILE n 
1 85  LYS n 
1 86  GLU n 
1 87  GLU n 
1 88  LEU n 
1 89  LEU n 
1 90  CYS n 
1 91  VAL n 
1 92  VAL n 
1 93  ARG n 
1 94  ASN n 
1 95  GLY n 
1 96  GLY n 
1 97  ARG n 
1 98  ILE n 
1 99  VAL n 
1 100 ASP n 
1 101 VAL n 
1 102 ILE n 
1 103 VAL n 
1 104 GLU n 
1 105 HIS n 
1 106 PRO n 
1 107 VAL n 
1 108 TYR n 
1 109 GLY n 
1 110 GLU n 
1 111 ILE n 
1 112 ARG n 
1 113 GLY n 
1 114 ILE n 
1 115 ILE n 
1 116 ASP n 
1 117 VAL n 
1 118 SER n 
1 119 SER n 
1 120 GLU n 
1 121 GLU n 
1 122 GLU n 
1 123 VAL n 
1 124 LEU n 
1 125 LYS n 
1 126 PHE n 
1 127 VAL n 
1 128 ASN n 
1 129 LEU n 
1 130 MET n 
1 131 GLU n 
1 132 MET n 
1 133 ALA n 
1 134 LYS n 
1 135 THR n 
1 136 GLU n 
1 137 PRO n 
1 138 LEU n 
1 139 LEU n 
1 140 THR n 
1 141 LEU n 
1 142 SER n 
1 143 GLY n 
1 144 GLY n 
1 145 VAL n 
1 146 HIS n 
1 147 LEU n 
1 148 HIS n 
1 149 THR n 
1 150 ILE n 
1 151 GLU n 
1 152 ALA n 
1 153 PRO n 
1 154 ASP n 
1 155 GLU n 
1 156 GLU n 
1 157 THR n 
1 158 MET n 
1 159 GLU n 
1 160 ARG n 
1 161 ILE n 
1 162 MET n 
1 163 ARG n 
1 164 GLU n 
1 165 LEU n 
1 166 LYS n 
1 167 LYS n 
1 168 LYS n 
1 169 GLY n 
1 170 PHE n 
1 171 LEU n 
1 172 ILE n 
1 173 GLU n 
1 174 GLU n 
1 175 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   175 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'niaR, TM_1602' 
_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      'Thermotoga maritima' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2336 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE          ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE         ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE       ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'  ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE         ? 'C3 H7 N O2 S'   121.158 
FE2 non-polymer         . 'FE (II) ION'    ? 'Fe 2'           55.845  
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 
NIO non-polymer         . 'NICOTINIC ACID' ? 'C6 H5 N O2'     123.109 
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 
TYR 'L-peptide linking' y TYROSINE         ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE           ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   HIS 2   2   ?   ?   ?   A . n 
A 1 3   MET 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   ARG 7   7   7   ARG ARG A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  VAL 63  63  63  VAL VAL 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  GLY 66  66  66  GLY GLY A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  SER 72  72  72  SER SER 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  VAL 75  75  75  VAL VAL A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  HIS 79  79  79  HIS HIS A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  CYS 90  90  90  CYS CYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  ASN 94  94  94  ASN ASN A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 MET 132 132 132 MET MET A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 HIS 146 146 146 HIS HIS A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 HIS 148 148 148 HIS HIS A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 MET 158 158 158 MET MET A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 ARG 160 160 160 ARG ARG A . n 
A 1 161 ILE 161 161 161 ILE ILE A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 GLU 174 174 ?   ?   ?   A . n 
A 1 175 GLY 175 175 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 FE2 ? ? FE2 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NIO ? ? NIO ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FE2 1 201 1  FE2 FE2 A . 
C 3 NIO 1 202 1  NIO NIO A . 
D 4 PRO 1 203 1  PRO PRO A . 
E 5 HOH 1 301 11 HOH HOH A . 
E 5 HOH 2 302 10 HOH HOH A . 
E 5 HOH 3 303 12 HOH HOH A . 
E 5 HOH 4 304 6  HOH HOH A . 
E 5 HOH 5 305 2  HOH HOH A . 
E 5 HOH 6 306 1  HOH HOH A . 
E 5 HOH 7 307 5  HOH HOH A . 
E 5 HOH 8 308 3  HOH HOH A . 
E 5 HOH 9 309 9  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EBR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     83.243 
_cell.length_a_esd                 ? 
_cell.length_b                     83.243 
_cell.length_b_esd                 ? 
_cell.length_c                     66.838 
_cell.length_c_esd                 ? 
_cell.volume                       401094.211 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9EBR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            
;P 32 2"
;
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EBR 
_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             3.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.97 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 M L-PROLINE, 0.1 M HEPES PH 7.5,     
10% (W/V) PEG 3350, .001 M NICOTINIC ACID
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   .97946 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        .97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          65.89 
_reflns.entry_id                                       9EBR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.30 
_reflns.d_resolution_low                               35.33 
_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                                     12235 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          35.5 
_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                                .032 
_reflns.pdbx_Rpim_I_all                                .014 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.30 
_reflns_shell.d_res_low                                     2.38 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1190 
_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                               10.0 
_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                               .559 
_reflns_shell.pdbx_Rpim_I_all                               .243 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.935 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               86.35 
_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                                 9EBR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.30 
_refine.ls_d_res_low                             35.33 
_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                     12205 
_refine.ls_number_reflns_R_free                  614 
_refine.ls_number_reflns_R_work                  11591 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2197 
_refine.ls_R_factor_R_free                       0.2603 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2174 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.4137 
_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                            0.3279 
_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                       2.30 
_refine_hist.d_res_low                        35.33 
_refine_hist.number_atoms_solvent             9 
_refine_hist.number_atoms_total               1341 
_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        1314 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         18 
_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' ? 0.0079  ? 1353 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9709  ? 1822 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0517  ? 215  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0087  ? 234  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.5491 ? 530  ? f_dihedral_angle_d ? ? 
# 
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' 2.30 2.53  . . 145 2859 99.87  . . . . 0.3463 . . . . . . . . . . . 0.4072 
'X-RAY DIFFRACTION' 2.53 2.90  . . 140 2874 99.97  . . . . 0.2756 . . . . . . . . . . . 0.3055 
'X-RAY DIFFRACTION' 2.90 3.65  . . 167 2865 100.00 . . . . 0.2936 . . . . . . . . . . . 0.3206 
'X-RAY DIFFRACTION' 3.65 35.33 . . 162 2993 99.81  . . . . 0.1704 . . . . . . . . . . . 0.2197 
# 
_struct.entry_id                     9EBR 
_struct.title                        'The structure of NiaR from Thermotoga maritima bound to nicotinic acid' 
_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        9EBR 
_struct_keywords.text            'Corepressor, regulatory protein, metalloprotein, DNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'DNA BINDING 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 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NIAR_THEMA 
_struct_ref.pdbx_db_accession          Q9X1T8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MHMKTVRQERLKSIVRILERSKEPVSGAQLAEELSVSRQVIVQDIAYLRSLGYNIVATPRGYVLAGGKSGVSRLVAVKHA
PEEIKEELLCVVRNGGRIVDVIVEHPVYGEIRGIIDVSSEEEVLKFVNLMEMAKTEPLLTLSGGVHLHTIEAPDEETMER
IMRELKKKGFLIEEG
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EBR 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 175 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9X1T8 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  175 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       175 
# 
_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)' 2610  ? 
1 MORE         -40   ? 
1 'SSA (A^2)'  18980 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z          1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 6_554 -x,-x+y,-z-1/3 -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 -0.8660254038 
0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -22.2793333333 
# 
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 VAL A 6   ? SER A 21  ? VAL A 6   SER A 21  1 ? 16 
HELX_P HELX_P2 AA2 SER A 26  ? SER A 35  ? SER A 26  SER A 35  1 ? 10 
HELX_P HELX_P3 AA3 SER A 37  ? GLY A 52  ? SER A 37  GLY A 52  1 ? 16 
HELX_P HELX_P4 AA4 ALA A 80  ? GLU A 82  ? ALA A 80  GLU A 82  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 83  ? ASN A 94  ? GLU A 83  ASN A 94  1 ? 12 
HELX_P HELX_P6 AA6 SER A 119 ? GLU A 131 ? SER A 119 GLU A 131 1 ? 13 
HELX_P HELX_P7 AA7 PRO A 137 ? LEU A 141 ? PRO A 137 LEU A 141 5 ? 5  
HELX_P HELX_P8 AA8 ASP A 154 ? LYS A 168 ? ASP A 154 LYS A 168 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 79  NE2 ? ? ? 1_555 B FE2 . FE ? ? A HIS 79  A FE2 201 1_555 ? ? ? ? ? ? ? 2.235 ? ? 
metalc2 metalc ? ? A GLU 87  OE1 ? ? ? 1_555 B FE2 . FE ? ? A GLU 87  A FE2 201 1_555 ? ? ? ? ? ? ? 2.174 ? ? 
metalc3 metalc ? ? A GLU 87  OE2 ? ? ? 1_555 B FE2 . FE ? ? A GLU 87  A FE2 201 1_555 ? ? ? ? ? ? ? 2.583 ? ? 
metalc4 metalc ? ? A HIS 146 NE2 ? ? ? 1_555 B FE2 . FE ? ? A HIS 146 A FE2 201 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc5 metalc ? ? A HIS 148 NE2 ? ? ? 1_555 B FE2 . FE ? ? A HIS 148 A FE2 201 1_555 ? ? ? ? ? ? ? 2.263 ? ? 
metalc6 metalc ? ? B FE2 .   FE  ? ? ? 1_555 C NIO . N  ? ? A FE2 201 A NIO 202 1_555 ? ? ? ? ? ? ? 2.391 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 79  ? A HIS 79  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 OE1 ? A GLU 87  ? A GLU 87  ? 1_555 92.9  ? 
2  NE2 ? A HIS 79  ? A HIS 79  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 OE2 ? A GLU 87  ? A GLU 87  ? 1_555 77.8  ? 
3  OE1 ? A GLU 87  ? A GLU 87  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 OE2 ? A GLU 87  ? A GLU 87  ? 1_555 53.5  ? 
4  NE2 ? A HIS 79  ? A HIS 79  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 NE2 ? A HIS 146 ? A HIS 146 ? 1_555 97.4  ? 
5  OE1 ? A GLU 87  ? A GLU 87  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 NE2 ? A HIS 146 ? A HIS 146 ? 1_555 160.3 ? 
6  OE2 ? A GLU 87  ? A GLU 87  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 NE2 ? A HIS 146 ? A HIS 146 ? 1_555 112.6 ? 
7  NE2 ? A HIS 79  ? A HIS 79  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 NE2 ? A HIS 148 ? A HIS 148 ? 1_555 172.8 ? 
8  OE1 ? A GLU 87  ? A GLU 87  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 NE2 ? A HIS 148 ? A HIS 148 ? 1_555 81.4  ? 
9  OE2 ? A GLU 87  ? A GLU 87  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 NE2 ? A HIS 148 ? A HIS 148 ? 1_555 95.3  ? 
10 NE2 ? A HIS 146 ? A HIS 146 ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 NE2 ? A HIS 148 ? A HIS 148 ? 1_555 86.9  ? 
11 NE2 ? A HIS 79  ? A HIS 79  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 N   ? C NIO .   ? A NIO 202 ? 1_555 107.9 ? 
12 OE1 ? A GLU 87  ? A GLU 87  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 N   ? C NIO .   ? A NIO 202 ? 1_555 95.8  ? 
13 OE2 ? A GLU 87  ? A GLU 87  ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 N   ? C NIO .   ? A NIO 202 ? 1_555 149.3 ? 
14 NE2 ? A HIS 146 ? A HIS 146 ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 N   ? C NIO .   ? A NIO 202 ? 1_555 96.8  ? 
15 NE2 ? A HIS 148 ? A HIS 148 ? 1_555 FE ? B FE2 . ? A FE2 201 ? 1_555 N   ? C NIO .   ? A NIO 202 ? 1_555 77.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
# 
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 ASN A 54  ? THR A 58  ? ASN A 54  THR A 58  
AA1 2 GLY A 61  ? ALA A 65  ? GLY A 61  ALA A 65  
AA2 1 VAL A 71  ? LYS A 78  ? VAL A 71  LYS A 78  
AA2 2 VAL A 145 ? ALA A 152 ? VAL A 145 ALA A 152 
AA2 3 ARG A 97  ? HIS A 105 ? ARG A 97  HIS A 105 
AA2 4 GLY A 109 ? VAL A 117 ? GLY A 109 VAL A 117 
# 
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 ASN A 54  ? N ASN A 54  O ALA A 65  ? O ALA A 65  
AA2 1 2 N ARG A 73  ? N ARG A 73  O ILE A 150 ? O ILE A 150 
AA2 2 3 O LEU A 147 ? O LEU A 147 N ILE A 102 ? N ILE A 102 
AA2 3 4 N HIS A 105 ? N HIS A 105 O GLY A 109 ? O GLY A 109 
# 
_pdbx_entry_details.entry_id                   9EBR 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ILE A 115 ? ? -121.85 -56.18  
2 1 MET A 132 ? ? -76.01  -165.28 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+2/3   
3 -x+y,-x,z+1/3  
4 x-y,-y,-z+1/3  
5 -x,-x+y,-z+2/3 
6 y,x,-z         
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -23.257 -20.269 11.175 0.697556325026 0.5137001308   0.521511627167 0.00856185764708 
0.022714783238  0.0474250077432 9.58252833819 8.24625960367 9.09722005636 -2.65554322806  0.0196986731117 -6.78815181928  
-0.787054542921 0.14233894382    0.664618573538  -0.42781309905  -0.222029224411 -0.526516848543 0.405028157724  -0.337285853823 
0.919524541043  
'X-RAY DIFFRACTION' 2 ? refined -14.064 -18.841 5.198  0.767077766199 0.869801028612 0.853013484516 -0.0488275901602 
0.0497009614657 0.108936858055  9.07449157586 9.87751528934 8.98962516246 -3.54943889136  -3.64101046069  6.17589824204   
0.395503118702  -0.098985339503  -0.399208479455 -0.702199379359 0.856478366143  -1.67937040051  -0.789428007586 -1.06861657917  
0.825706192055  
'X-RAY DIFFRACTION' 3 ? refined 13.013  -33.472 6.624  0.872529441525 0.612375613547 0.699604490667 -0.27403475044   
-0.283449714705 0.0763456574413 6.45667947281 6.32415216176 8.0827879603  -0.482006755722 1.74199074788   -0.356000265711 
0.347671885274  -0.0967016492948 -0.104731719963 -0.994579459764 -0.572631677484 -0.512254491983 1.02216576707   0.447495664751  
-0.098549606826 
'X-RAY DIFFRACTION' 4 ? refined 19.446  -25.603 -6.594 0.651355004702 0.594641132707 0.681184270517 -0.254498859613  
-0.165594628455 0.0489581900079 9.06749041983 2.71613524488 7.52328183824 5.03251034253   -7.5515366247   -3.98972073441  
0.653051579755  0.39214376433    -0.919132376486 0.563111289906  0.403535031291  -0.213276862639 0.174186101086  -0.616085612253 
-0.465604224204 
'X-RAY DIFFRACTION' 5 ? refined 6.121   -38.491 -1.368 0.822551629252 0.69122526407  0.79784252796  -0.345207110007  
-0.247405087897 0.0870835659398 2.44239438908 6.93277583242 6.69909862829 -1.77742552394  0.901535305238  -1.94193250427  
0.511602940723  -0.317153018672  -0.220885171091 -0.351181614783 -1.30500616969  0.270868990281  0.247115965958  1.19412789066   
-0.769346989068 
'X-RAY DIFFRACTION' 6 ? refined 16.417  -31.052 7.135  0.926752644062 0.797318425964 0.777714555883 -0.289488209537  
-0.345406715937 0.0657043090707 9.54075309562 5.67651683681 7.81439013822 -1.74215539549  3.93153295951   0.0734533730192 
-0.081599527531 -0.16715734551   0.0508312720277 -1.16947528722  0.548039924507  -0.96528137976  1.95812852967   0.189765199175  
0.0143025665718 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 6   A 48  '( CHAIN A AND RESID 6:48 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 A 49  A 68  '( CHAIN A AND RESID 49:68 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 3 3 A 69  A 98  '( CHAIN A AND RESID 69:98 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 4 4 A 99  A 112 '( CHAIN A AND RESID 99:112 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 5 5 A 113 A 133 '( CHAIN A AND RESID 113:133 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 6 6 A 134 A 173 '( CHAIN A AND RESID 134:173 )' ? ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A HIS 2   ? A HIS 2   
3 1 Y 1 A MET 3   ? A MET 3   
4 1 Y 1 A LYS 4   ? A LYS 4   
5 1 Y 1 A THR 5   ? A THR 5   
6 1 Y 1 A GLU 174 ? A GLU 174 
7 1 Y 1 A GLY 175 ? A GLY 175 
# 
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  
FE2 FE   FE N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
NIO N    N  Y N 251 
NIO C1   C  Y N 252 
NIO C2   C  Y N 253 
NIO C3   C  Y N 254 
NIO C4   C  Y N 255 
NIO C5   C  Y N 256 
NIO C6   C  N N 257 
NIO O1   O  N N 258 
NIO O2   O  N N 259 
NIO H1   H  N N 260 
NIO H3   H  N N 261 
NIO H4   H  N N 262 
NIO H5   H  N N 263 
NIO HO2  H  N N 264 
PHE N    N  N N 265 
PHE CA   C  N S 266 
PHE C    C  N N 267 
PHE O    O  N N 268 
PHE CB   C  N N 269 
PHE CG   C  Y N 270 
PHE CD1  C  Y N 271 
PHE CD2  C  Y N 272 
PHE CE1  C  Y N 273 
PHE CE2  C  Y N 274 
PHE CZ   C  Y N 275 
PHE OXT  O  N N 276 
PHE H    H  N N 277 
PHE H2   H  N N 278 
PHE HA   H  N N 279 
PHE HB2  H  N N 280 
PHE HB3  H  N N 281 
PHE HD1  H  N N 282 
PHE HD2  H  N N 283 
PHE HE1  H  N N 284 
PHE HE2  H  N N 285 
PHE HZ   H  N N 286 
PHE HXT  H  N N 287 
PRO N    N  N N 288 
PRO CA   C  N S 289 
PRO C    C  N N 290 
PRO O    O  N N 291 
PRO CB   C  N N 292 
PRO CG   C  N N 293 
PRO CD   C  N N 294 
PRO OXT  O  N N 295 
PRO H    H  N N 296 
PRO HA   H  N N 297 
PRO HB2  H  N N 298 
PRO HB3  H  N N 299 
PRO HG2  H  N N 300 
PRO HG3  H  N N 301 
PRO HD2  H  N N 302 
PRO HD3  H  N N 303 
PRO HXT  H  N N 304 
SER N    N  N N 305 
SER CA   C  N S 306 
SER C    C  N N 307 
SER O    O  N N 308 
SER CB   C  N N 309 
SER OG   O  N N 310 
SER OXT  O  N N 311 
SER H    H  N N 312 
SER H2   H  N N 313 
SER HA   H  N N 314 
SER HB2  H  N N 315 
SER HB3  H  N N 316 
SER HG   H  N N 317 
SER HXT  H  N N 318 
THR N    N  N N 319 
THR CA   C  N S 320 
THR C    C  N N 321 
THR O    O  N N 322 
THR CB   C  N R 323 
THR OG1  O  N N 324 
THR CG2  C  N N 325 
THR OXT  O  N N 326 
THR H    H  N N 327 
THR H2   H  N N 328 
THR HA   H  N N 329 
THR HB   H  N N 330 
THR HG1  H  N N 331 
THR HG21 H  N N 332 
THR HG22 H  N N 333 
THR HG23 H  N N 334 
THR HXT  H  N N 335 
TYR N    N  N N 336 
TYR CA   C  N S 337 
TYR C    C  N N 338 
TYR O    O  N N 339 
TYR CB   C  N N 340 
TYR CG   C  Y N 341 
TYR CD1  C  Y N 342 
TYR CD2  C  Y N 343 
TYR CE1  C  Y N 344 
TYR CE2  C  Y N 345 
TYR CZ   C  Y N 346 
TYR OH   O  N N 347 
TYR OXT  O  N N 348 
TYR H    H  N N 349 
TYR H2   H  N N 350 
TYR HA   H  N N 351 
TYR HB2  H  N N 352 
TYR HB3  H  N N 353 
TYR HD1  H  N N 354 
TYR HD2  H  N N 355 
TYR HE1  H  N N 356 
TYR HE2  H  N N 357 
TYR HH   H  N N 358 
TYR HXT  H  N N 359 
VAL N    N  N N 360 
VAL CA   C  N S 361 
VAL C    C  N N 362 
VAL O    O  N N 363 
VAL CB   C  N N 364 
VAL CG1  C  N N 365 
VAL CG2  C  N N 366 
VAL OXT  O  N N 367 
VAL H    H  N N 368 
VAL H2   H  N N 369 
VAL HA   H  N N 370 
VAL HB   H  N N 371 
VAL HG11 H  N N 372 
VAL HG12 H  N N 373 
VAL HG13 H  N N 374 
VAL HG21 H  N N 375 
VAL HG22 H  N N 376 
VAL HG23 H  N N 377 
VAL HXT  H  N N 378 
# 
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 
NIO N   C1   doub Y N 237 
NIO N   C5   sing Y N 238 
NIO C1  C2   sing Y N 239 
NIO C1  H1   sing N N 240 
NIO C2  C3   doub Y N 241 
NIO C2  C6   sing N N 242 
NIO C3  C4   sing Y N 243 
NIO C3  H3   sing N N 244 
NIO C4  C5   doub Y N 245 
NIO C4  H4   sing N N 246 
NIO C5  H5   sing N N 247 
NIO C6  O1   doub N N 248 
NIO C6  O2   sing N N 249 
NIO O2  HO2  sing N N 250 
PHE N   CA   sing N N 251 
PHE N   H    sing N N 252 
PHE N   H2   sing N N 253 
PHE CA  C    sing N N 254 
PHE CA  CB   sing N N 255 
PHE CA  HA   sing N N 256 
PHE C   O    doub N N 257 
PHE C   OXT  sing N N 258 
PHE CB  CG   sing N N 259 
PHE CB  HB2  sing N N 260 
PHE CB  HB3  sing N N 261 
PHE CG  CD1  doub Y N 262 
PHE CG  CD2  sing Y N 263 
PHE CD1 CE1  sing Y N 264 
PHE CD1 HD1  sing N N 265 
PHE CD2 CE2  doub Y N 266 
PHE CD2 HD2  sing N N 267 
PHE CE1 CZ   doub Y N 268 
PHE CE1 HE1  sing N N 269 
PHE CE2 CZ   sing Y N 270 
PHE CE2 HE2  sing N N 271 
PHE CZ  HZ   sing N N 272 
PHE OXT HXT  sing N N 273 
PRO N   CA   sing N N 274 
PRO N   CD   sing N N 275 
PRO N   H    sing N N 276 
PRO CA  C    sing N N 277 
PRO CA  CB   sing N N 278 
PRO CA  HA   sing N N 279 
PRO C   O    doub N N 280 
PRO C   OXT  sing N N 281 
PRO CB  CG   sing N N 282 
PRO CB  HB2  sing N N 283 
PRO CB  HB3  sing N N 284 
PRO CG  CD   sing N N 285 
PRO CG  HG2  sing N N 286 
PRO CG  HG3  sing N N 287 
PRO CD  HD2  sing N N 288 
PRO CD  HD3  sing N N 289 
PRO OXT HXT  sing N N 290 
SER N   CA   sing N N 291 
SER N   H    sing N N 292 
SER N   H2   sing N N 293 
SER CA  C    sing N N 294 
SER CA  CB   sing N N 295 
SER CA  HA   sing N N 296 
SER C   O    doub N N 297 
SER C   OXT  sing N N 298 
SER CB  OG   sing N N 299 
SER CB  HB2  sing N N 300 
SER CB  HB3  sing N N 301 
SER OG  HG   sing N N 302 
SER OXT HXT  sing N N 303 
THR N   CA   sing N N 304 
THR N   H    sing N N 305 
THR N   H2   sing N N 306 
THR CA  C    sing N N 307 
THR CA  CB   sing N N 308 
THR CA  HA   sing N N 309 
THR C   O    doub N N 310 
THR C   OXT  sing N N 311 
THR CB  OG1  sing N N 312 
THR CB  CG2  sing N N 313 
THR CB  HB   sing N N 314 
THR OG1 HG1  sing N N 315 
THR CG2 HG21 sing N N 316 
THR CG2 HG22 sing N N 317 
THR CG2 HG23 sing N N 318 
THR OXT HXT  sing N N 319 
TYR N   CA   sing N N 320 
TYR N   H    sing N N 321 
TYR N   H2   sing N N 322 
TYR CA  C    sing N N 323 
TYR CA  CB   sing N N 324 
TYR CA  HA   sing N N 325 
TYR C   O    doub N N 326 
TYR C   OXT  sing N N 327 
TYR CB  CG   sing N N 328 
TYR CB  HB2  sing N N 329 
TYR CB  HB3  sing N N 330 
TYR CG  CD1  doub Y N 331 
TYR CG  CD2  sing Y N 332 
TYR CD1 CE1  sing Y N 333 
TYR CD1 HD1  sing N N 334 
TYR CD2 CE2  doub Y N 335 
TYR CD2 HD2  sing N N 336 
TYR CE1 CZ   doub Y N 337 
TYR CE1 HE1  sing N N 338 
TYR CE2 CZ   sing Y N 339 
TYR CE2 HE2  sing N N 340 
TYR CZ  OH   sing N N 341 
TYR OH  HH   sing N N 342 
TYR OXT HXT  sing N N 343 
VAL N   CA   sing N N 344 
VAL N   H    sing N N 345 
VAL N   H2   sing N N 346 
VAL CA  C    sing N N 347 
VAL CA  CB   sing N N 348 
VAL CA  HA   sing N N 349 
VAL C   O    doub N N 350 
VAL C   OXT  sing N N 351 
VAL CB  CG1  sing N N 352 
VAL CB  CG2  sing N N 353 
VAL CB  HB   sing N N 354 
VAL CG1 HG11 sing N N 355 
VAL CG1 HG12 sing N N 356 
VAL CG1 HG13 sing N N 357 
VAL CG2 HG21 sing N N 358 
VAL CG2 HG22 sing N N 359 
VAL CG2 HG23 sing N N 360 
VAL OXT HXT  sing N N 361 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1J5Y 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 32 2 1' 
_space_group.name_Hall        
;P 32 2"
;
_space_group.IT_number        154 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EBR 
_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]   0.012013 
_atom_sites.fract_transf_matrix[1][2]   0.006936 
_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]   0.013871 
_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]   0.014962 
_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.
;
? 
FE  ? ? 20.90327 4.99816 ? ? 2.55100  38.46870 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H   ? ? 0.51345  0.48472 ? ? 24.73122 6.32584  ? ? 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.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 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   . VAL A 1 6   ? -25.55519 -15.20468 23.70721  1.000 88.89724  ?  6   VAL A N   1 
ATOM   2    C  CA  . VAL A 1 6   ? -26.38129 -15.77993 22.65009  1.000 95.37541  ?  6   VAL A CA  1 
ATOM   3    C  C   . VAL A 1 6   ? -25.76647 -15.62891 21.28005  1.000 97.90271  ?  6   VAL A C   1 
ATOM   4    O  O   . VAL A 1 6   ? -25.72897 -16.58784 20.50006  1.000 92.24204  ?  6   VAL A O   1 
ATOM   5    C  CB  . VAL A 1 6   ? -27.76441 -15.15435 22.57648  1.000 93.48824  ?  6   VAL A CB  1 
ATOM   6    C  CG1 . VAL A 1 6   ? -28.43895 -15.62024 21.27182  1.000 86.25770  ?  6   VAL A CG1 1 
ATOM   7    C  CG2 . VAL A 1 6   ? -28.58818 -15.51814 23.77769  1.000 84.16277  ?  6   VAL A CG2 1 
ATOM   8    N  N   . ARG A 1 7   ? -25.36727 -14.39638 20.95274  1.000 97.34463  ?  7   ARG A N   1 
ATOM   9    C  CA  . ARG A 1 7   ? -24.64288 -14.18445 19.70690  1.000 95.85768  ?  7   ARG A CA  1 
ATOM   10   C  C   . ARG A 1 7   ? -23.31833 -14.93248 19.72686  1.000 95.03682  ?  7   ARG A C   1 
ATOM   11   O  O   . ARG A 1 7   ? -22.89821 -15.50536 18.71171  1.000 88.63011  ?  7   ARG A O   1 
ATOM   12   C  CB  . ARG A 1 7   ? -24.40439 -12.69446 19.45655  1.000 96.67232  ?  7   ARG A CB  1 
ATOM   13   C  CG  . ARG A 1 7   ? -23.54189 -12.48083 18.21283  1.000 103.79601 ?  7   ARG A CG  1 
ATOM   14   C  CD  . ARG A 1 7   ? -23.06054 -11.05430 17.99325  1.000 103.92331 ?  7   ARG A CD  1 
ATOM   15   N  NE  . ARG A 1 7   ? -23.67595 -10.44521 16.81275  1.000 111.11259 ?  7   ARG A NE  1 
ATOM   16   C  CZ  . ARG A 1 7   ? -23.37296 -10.72728 15.54817  1.000 108.47367 ?  7   ARG A CZ  1 
ATOM   17   N  NH1 . ARG A 1 7   ? -22.46542 -11.63792 15.23920  1.000 100.43974 ?  7   ARG A NH1 1 
ATOM   18   N  NH2 . ARG A 1 7   ? -24.00725 -10.08426 14.56508  1.000 107.85456 ?  7   ARG A NH2 1 
ATOM   19   N  N   . GLN A 1 8   ? -22.65741 -14.95815 20.88562  1.000 103.28439 ?  8   GLN A N   1 
ATOM   20   C  CA  . GLN A 1 8   ? -21.38641 -15.66264 20.99779  1.000 101.54009 ?  8   GLN A CA  1 
ATOM   21   C  C   . GLN A 1 8   ? -21.55924 -17.16597 20.78898  1.000 94.91081  ?  8   GLN A C   1 
ATOM   22   O  O   . GLN A 1 8   ? -20.68583 -17.82036 20.20396  1.000 91.38323  ?  8   GLN A O   1 
ATOM   23   C  CB  . GLN A 1 8   ? -20.74700 -15.36475 22.35279  1.000 107.92600 ?  8   GLN A CB  1 
ATOM   24   C  CG  . GLN A 1 8   ? -19.94468 -14.05843 22.39197  1.000 120.13510 ?  8   GLN A CG  1 
ATOM   25   C  CD  . GLN A 1 8   ? -20.71249 -12.85162 21.85590  1.000 120.97868 ?  8   GLN A CD  1 
ATOM   26   O  OE1 . GLN A 1 8   ? -20.52712 -12.44742 20.70166  1.000 113.52226 ?  8   GLN A OE1 1 
ATOM   27   N  NE2 . GLN A 1 8   ? -21.57021 -12.26609 22.69749  1.000 122.77655 ?  8   GLN A NE2 1 
ATOM   28   N  N   . GLU A 1 9   ? -22.68202 -17.73392 21.24749  1.000 90.51315  ?  9   GLU A N   1 
ATOM   29   C  CA  . GLU A 1 9   ? -22.90464 -19.16723 21.05666  1.000 86.97401  ?  9   GLU A CA  1 
ATOM   30   C  C   . GLU A 1 9   ? -23.24469 -19.49280 19.60051  1.000 82.91690  ?  9   GLU A C   1 
ATOM   31   O  O   . GLU A 1 9   ? -22.83295 -20.53723 19.07455  1.000 72.65538  ?  9   GLU A O   1 
ATOM   32   C  CB  . GLU A 1 9   ? -23.99126 -19.66985 22.01431  1.000 83.25886  ?  9   GLU A CB  1 
ATOM   33   C  CG  . GLU A 1 9   ? -23.44485 -20.08734 23.37449  1.000 92.04735  ?  9   GLU A CG  1 
ATOM   34   C  CD  . GLU A 1 9   ? -22.36262 -21.15449 23.26116  1.000 93.95372  ?  9   GLU A CD  1 
ATOM   35   O  OE1 . GLU A 1 9   ? -22.34444 -21.87215 22.23634  1.000 98.48611  ?  9   GLU A OE1 1 
ATOM   36   O  OE2 . GLU A 1 9   ? -21.52276 -21.26790 24.17783  1.000 101.28005 -1 9   GLU A OE2 1 
ATOM   37   N  N   . ARG A 1 10  ? -23.97190 -18.60586 18.91970  1.000 84.47821  ?  10  ARG A N   1 
ATOM   38   C  CA  . ARG A 1 10  ? -24.15976 -18.80183 17.48900  1.000 76.90083  ?  10  ARG A CA  1 
ATOM   39   C  C   . ARG A 1 10  ? -22.82753 -18.68991 16.74407  1.000 76.80165  ?  10  ARG A C   1 
ATOM   40   O  O   . ARG A 1 10  ? -22.52748 -19.51586 15.87088  1.000 69.54530  ?  10  ARG A O   1 
ATOM   41   C  CB  . ARG A 1 10  ? -25.19537 -17.81456 16.94250  1.000 69.44282  ?  10  ARG A CB  1 
ATOM   42   C  CG  . ARG A 1 10  ? -25.62867 -18.13275 15.50542  1.000 69.31216  ?  10  ARG A CG  1 
ATOM   43   C  CD  . ARG A 1 10  ? -26.80332 -17.28224 15.01824  1.000 64.26765  ?  10  ARG A CD  1 
ATOM   44   N  NE  . ARG A 1 10  ? -26.45682 -15.87031 14.92479  1.000 63.36311  ?  10  ARG A NE  1 
ATOM   45   C  CZ  . ARG A 1 10  ? -26.73847 -14.96182 15.84765  1.000 71.80783  ?  10  ARG A CZ  1 
ATOM   46   N  NH1 . ARG A 1 10  ? -27.39295 -15.27952 16.95223  1.000 83.62185  ?  10  ARG A NH1 1 
ATOM   47   N  NH2 . ARG A 1 10  ? -26.34007 -13.70390 15.66374  1.000 80.95578  ?  10  ARG A NH2 1 
ATOM   48   N  N   . LEU A 1 11  ? -22.00534 -17.69218 17.08807  1.000 77.92494  ?  11  LEU A N   1 
ATOM   49   C  CA  . LEU A 1 11  ? -20.69054 -17.55553 16.45944  1.000 78.32667  ?  11  LEU A CA  1 
ATOM   50   C  C   . LEU A 1 11  ? -19.85565 -18.81824 16.64332  1.000 87.15618  ?  11  LEU A C   1 
ATOM   51   O  O   . LEU A 1 11  ? -19.27584 -19.33988 15.67850  1.000 85.48176  ?  11  LEU A O   1 
ATOM   52   C  CB  . LEU A 1 11  ? -19.94922 -16.34641 17.02837  1.000 80.05127  ?  11  LEU A CB  1 
ATOM   53   C  CG  . LEU A 1 11  ? -20.30230 -14.97090 16.46618  1.000 89.34255  ?  11  LEU A CG  1 
ATOM   54   C  CD1 . LEU A 1 11  ? -19.59325 -13.87727 17.24030  1.000 94.64009  ?  11  LEU A CD1 1 
ATOM   55   C  CD2 . LEU A 1 11  ? -19.94869 -14.89029 14.99738  1.000 83.92565  ?  11  LEU A CD2 1 
ATOM   56   N  N   . LYS A 1 12  ? -19.76964 -19.31960 17.88500  1.000 80.70681  ?  12  LYS A N   1 
ATOM   57   C  CA  . LYS A 1 12  ? -19.02966 -20.55195 18.11962  1.000 81.44636  ?  12  LYS A CA  1 
ATOM   58   C  C   . LYS A 1 12  ? -19.60769 -21.69228 17.29825  1.000 78.66108  ?  12  LYS A C   1 
ATOM   59   O  O   . LYS A 1 12  ? -18.86045 -22.46635 16.69122  1.000 84.58758  ?  12  LYS A O   1 
ATOM   60   C  CB  . LYS A 1 12  ? -19.01906 -20.90997 19.60695  1.000 87.68991  ?  12  LYS A CB  1 
ATOM   61   C  CG  . LYS A 1 12  ? -17.78301 -20.44651 20.36157  1.000 87.26441  ?  12  LYS A CG  1 
ATOM   62   C  CD  . LYS A 1 12  ? -17.90224 -20.80440 21.83562  1.000 93.27088  ?  12  LYS A CD  1 
ATOM   63   C  CE  . LYS A 1 12  ? -16.56531 -20.66002 22.55186  1.000 106.36721 ?  12  LYS A CE  1 
ATOM   64   N  NZ  . LYS A 1 12  ? -16.55187 -21.25418 23.93142  1.000 111.57921 ?  12  LYS A NZ  1 
ATOM   65   N  N   . SER A 1 13  ? -20.93362 -21.80123 17.23564  1.000 76.49460  ?  13  SER A N   1 
ATOM   66   C  CA  . SER A 1 13  ? -21.50640 -22.92855 16.51073  1.000 80.38451  ?  13  SER A CA  1 
ATOM   67   C  C   . SER A 1 13  ? -21.23944 -22.84232 15.00885  1.000 76.29345  ?  13  SER A C   1 
ATOM   68   O  O   . SER A 1 13  ? -21.07436 -23.87851 14.34900  1.000 72.14913  ?  13  SER A O   1 
ATOM   69   C  CB  . SER A 1 13  ? -22.99947 -23.04373 16.79258  1.000 71.33238  ?  13  SER A CB  1 
ATOM   70   O  OG  . SER A 1 13  ? -23.18519 -23.61317 18.06253  1.000 76.89682  ?  13  SER A OG  1 
ATOM   71   N  N   . ILE A 1 14  ? -21.17199 -21.63762 14.44435  1.000 75.45250  ?  14  ILE A N   1 
ATOM   72   C  CA  . ILE A 1 14  ? -20.88617 -21.53831 13.01553  1.000 72.12531  ?  14  ILE A CA  1 
ATOM   73   C  C   . ILE A 1 14  ? -19.51072 -22.12205 12.71403  1.000 78.09431  ?  14  ILE A C   1 
ATOM   74   O  O   . ILE A 1 14  ? -19.35945 -22.98963 11.84426  1.000 76.92105  ?  14  ILE A O   1 
ATOM   75   C  CB  . ILE A 1 14  ? -21.01091 -20.08545 12.53371  1.000 69.33045  ?  14  ILE A CB  1 
ATOM   76   C  CG1 . ILE A 1 14  ? -22.48037 -19.71805 12.39451  1.000 63.48735  ?  14  ILE A CG1 1 
ATOM   77   C  CG2 . ILE A 1 14  ? -20.29333 -19.89367 11.19315  1.000 66.16646  ?  14  ILE A CG2 1 
ATOM   78   C  CD1 . ILE A 1 14  ? -22.73124 -18.25276 12.46205  1.000 66.20711  ?  14  ILE A CD1 1 
ATOM   79   N  N   . VAL A 1 15  ? -18.49236 -21.68297 13.45249  1.000 76.89611  ?  15  VAL A N   1 
ATOM   80   C  CA  . VAL A 1 15  ? -17.15978 -22.26374 13.29267  1.000 82.08390  ?  15  VAL A CA  1 
ATOM   81   C  C   . VAL A 1 15  ? -17.21797 -23.78245 13.43867  1.000 83.59137  ?  15  VAL A C   1 
ATOM   82   O  O   . VAL A 1 15  ? -16.80426 -24.53329 12.54263  1.000 80.81734  ?  15  VAL A O   1 
ATOM   83   C  CB  . VAL A 1 15  ? -16.18725 -21.64122 14.30806  1.000 85.90018  ?  15  VAL A CB  1 
ATOM   84   C  CG1 . VAL A 1 15  ? -14.80228 -22.27113 14.16856  1.000 85.45734  ?  15  VAL A CG1 1 
ATOM   85   C  CG2 . VAL A 1 15  ? -16.14553 -20.12315 14.12315  1.000 84.35297  ?  15  VAL A CG2 1 
ATOM   86   N  N   . ARG A 1 16  ? -17.73562 -24.24850 14.58038  1.000 77.81353  ?  16  ARG A N   1 
ATOM   87   C  CA  . ARG A 1 16  ? -17.85077 -25.67864 14.85348  1.000 83.42824  ?  16  ARG A CA  1 
ATOM   88   C  C   . ARG A 1 16  ? -18.38483 -26.44802 13.64223  1.000 83.49558  ?  16  ARG A C   1 
ATOM   89   O  O   . ARG A 1 16  ? -17.85139 -27.50675 13.28360  1.000 85.29698  ?  16  ARG A O   1 
ATOM   90   C  CB  . ARG A 1 16  ? -18.74937 -25.87738 16.08307  1.000 79.62569  ?  16  ARG A CB  1 
ATOM   91   C  CG  . ARG A 1 16  ? -18.53310 -27.12186 16.89317  1.000 85.54307  ?  16  ARG A CG  1 
ATOM   92   C  CD  . ARG A 1 16  ? -18.90537 -26.84629 18.35859  1.000 86.50349  ?  16  ARG A CD  1 
ATOM   93   N  NE  . ARG A 1 16  ? -20.02413 -25.91325 18.49545  1.000 89.45238  ?  16  ARG A NE  1 
ATOM   94   C  CZ  . ARG A 1 16  ? -20.30551 -25.23464 19.60583  1.000 91.65037  ?  16  ARG A CZ  1 
ATOM   95   N  NH1 . ARG A 1 16  ? -19.53203 -25.31530 20.67922  1.000 92.25609  ?  16  ARG A NH1 1 
ATOM   96   N  NH2 . ARG A 1 16  ? -21.39060 -24.45770 19.64278  1.000 80.82805  ?  16  ARG A NH2 1 
ATOM   97   N  N   . ILE A 1 17  ? -19.42375 -25.92156 12.98503  1.000 79.30616  ?  17  ILE A N   1 
ATOM   98   C  CA  . ILE A 1 17  ? -20.02105 -26.62507 11.84878  1.000 83.15292  ?  17  ILE A CA  1 
ATOM   99   C  C   . ILE A 1 17  ? -19.05109 -26.70270 10.66151  1.000 80.59324  ?  17  ILE A C   1 
ATOM   100  O  O   . ILE A 1 17  ? -19.05391 -27.68658 9.89917   1.000 68.26476  ?  17  ILE A O   1 
ATOM   101  C  CB  . ILE A 1 17  ? -21.34395 -25.93045 11.47713  1.000 80.12979  ?  17  ILE A CB  1 
ATOM   102  C  CG1 . ILE A 1 17  ? -22.29170 -25.95922 12.67622  1.000 82.44712  ?  17  ILE A CG1 1 
ATOM   103  C  CG2 . ILE A 1 17  ? -21.99530 -26.58217 10.26730  1.000 75.63857  ?  17  ILE A CG2 1 
ATOM   104  C  CD1 . ILE A 1 17  ? -23.59451 -25.27205 12.45008  1.000 69.80828  ?  17  ILE A CD1 1 
ATOM   105  N  N   . LEU A 1 18  ? -18.19584 -25.68676 10.50336  1.000 80.30886  ?  18  LEU A N   1 
ATOM   106  C  CA  . LEU A 1 18  ? -17.29433 -25.58641 9.35980   1.000 80.09994  ?  18  LEU A CA  1 
ATOM   107  C  C   . LEU A 1 18  ? -16.04153 -26.44046 9.50909   1.000 82.52017  ?  18  LEU A C   1 
ATOM   108  O  O   . LEU A 1 18  ? -15.40427 -26.76412 8.50372   1.000 85.15075  ?  18  LEU A O   1 
ATOM   109  C  CB  . LEU A 1 18  ? -16.89891 -24.12381 9.13315   1.000 71.60958  ?  18  LEU A CB  1 
ATOM   110  C  CG  . LEU A 1 18  ? -18.10176 -23.20537 8.91461   1.000 74.98759  ?  18  LEU A CG  1 
ATOM   111  C  CD1 . LEU A 1 18  ? -17.67425 -21.76080 8.72078   1.000 68.76499  ?  18  LEU A CD1 1 
ATOM   112  C  CD2 . LEU A 1 18  ? -18.92550 -23.69232 7.73766   1.000 74.67180  ?  18  LEU A CD2 1 
ATOM   113  N  N   . GLU A 1 19  ? -15.67686 -26.82858 10.72351  1.000 78.98195  ?  19  GLU A N   1 
ATOM   114  C  CA  . GLU A 1 19  ? -14.49638 -27.66091 10.88233  1.000 83.59497  ?  19  GLU A CA  1 
ATOM   115  C  C   . GLU A 1 19  ? -14.77704 -29.14064 10.65060  1.000 88.98131  ?  19  GLU A C   1 
ATOM   116  O  O   . GLU A 1 19  ? -13.85846 -29.88971 10.27887  1.000 91.24816  ?  19  GLU A O   1 
ATOM   117  C  CB  . GLU A 1 19  ? -13.90255 -27.46068 12.27817  1.000 88.19946  ?  19  GLU A CB  1 
ATOM   118  C  CG  . GLU A 1 19  ? -13.59948 -26.00893 12.59821  1.000 94.63051  ?  19  GLU A CG  1 
ATOM   119  C  CD  . GLU A 1 19  ? -13.24967 -25.79918 14.06028  1.000 100.40423 ?  19  GLU A CD  1 
ATOM   120  O  OE1 . GLU A 1 19  ? -13.81090 -26.52322 14.92529  1.000 98.76529  ?  19  GLU A OE1 1 
ATOM   121  O  OE2 . GLU A 1 19  ? -12.41151 -24.90761 14.33561  1.000 108.94062 -1 19  GLU A OE2 1 
ATOM   122  N  N   . ARG A 1 20  ? -16.01765 -29.58934 10.87019  1.000 90.00682  ?  20  ARG A N   1 
ATOM   123  C  CA  . ARG A 1 20  ? -16.34543 -31.00182 10.73535  1.000 93.55819  ?  20  ARG A CA  1 
ATOM   124  C  C   . ARG A 1 20  ? -17.09538 -31.32645 9.45202   1.000 92.34453  ?  20  ARG A C   1 
ATOM   125  O  O   . ARG A 1 20  ? -17.11994 -32.49804 9.05064   1.000 95.24200  ?  20  ARG A O   1 
ATOM   126  C  CB  . ARG A 1 20  ? -17.16350 -31.48120 11.94251  1.000 87.97400  ?  20  ARG A CB  1 
ATOM   127  C  CG  . ARG A 1 20  ? -18.47884 -30.76368 12.13375  1.000 87.24161  ?  20  ARG A CG  1 
ATOM   128  C  CD  . ARG A 1 20  ? -19.27315 -31.35975 13.28920  1.000 91.28514  ?  20  ARG A CD  1 
ATOM   129  N  NE  . ARG A 1 20  ? -20.70258 -31.27033 13.02521  1.000 85.92395  ?  20  ARG A NE  1 
ATOM   130  C  CZ  . ARG A 1 20  ? -21.48376 -30.29105 13.44744  1.000 86.61067  ?  20  ARG A CZ  1 
ATOM   131  N  NH1 . ARG A 1 20  ? -21.04409 -29.37853 14.29869  1.000 90.26571  ?  20  ARG A NH1 1 
ATOM   132  N  NH2 . ARG A 1 20  ? -22.72920 -30.20824 12.98204  1.000 84.40638  ?  20  ARG A NH2 1 
ATOM   133  N  N   . SER A 1 21  ? -17.67743 -30.32929 8.78883   1.000 84.17861  ?  21  SER A N   1 
ATOM   134  C  CA  . SER A 1 21  ? -18.48063 -30.57900 7.60256   1.000 87.50626  ?  21  SER A CA  1 
ATOM   135  C  C   . SER A 1 21  ? -17.58211 -30.84416 6.39224   1.000 90.15585  ?  21  SER A C   1 
ATOM   136  O  O   . SER A 1 21  ? -16.63131 -30.09877 6.12420   1.000 84.81816  ?  21  SER A O   1 
ATOM   137  C  CB  . SER A 1 21  ? -19.42195 -29.40214 7.35934   1.000 85.15753  ?  21  SER A CB  1 
ATOM   138  O  OG  . SER A 1 21  ? -20.46229 -29.78287 6.48204   1.000 91.34153  ?  21  SER A OG  1 
ATOM   139  N  N   . LYS A 1 22  ? -17.87204 -31.93555 5.68409   1.000 88.04566  ?  22  LYS A N   1 
ATOM   140  C  CA  . LYS A 1 22  ? -17.02894 -32.44133 4.61421   1.000 86.78361  ?  22  LYS A CA  1 
ATOM   141  C  C   . LYS A 1 22  ? -17.31740 -31.78966 3.26646   1.000 89.85384  ?  22  LYS A C   1 
ATOM   142  O  O   . LYS A 1 22  ? -16.52191 -31.95114 2.33271   1.000 92.38381  ?  22  LYS A O   1 
ATOM   143  C  CB  . LYS A 1 22  ? -17.18606 -33.96773 4.50161   1.000 99.05237  ?  22  LYS A CB  1 
ATOM   144  C  CG  . LYS A 1 22  ? -16.75873 -34.74518 5.75636   1.000 95.02326  ?  22  LYS A CG  1 
ATOM   145  C  CD  . LYS A 1 22  ? -17.02647 -36.22778 5.60196   1.000 101.36554 ?  22  LYS A CD  1 
ATOM   146  C  CE  . LYS A 1 22  ? -16.80150 -37.00367 6.90444   1.000 104.76575 ?  22  LYS A CE  1 
ATOM   147  N  NZ  . LYS A 1 22  ? -15.37856 -37.10990 7.33444   1.000 105.96421 ?  22  LYS A NZ  1 
ATOM   148  N  N   . GLU A 1 23  ? -18.42341 -31.06663 3.15405   1.000 88.85018  ?  23  GLU A N   1 
ATOM   149  C  CA  . GLU A 1 23  ? -18.85195 -30.31949 1.98426   1.000 87.82557  ?  23  GLU A CA  1 
ATOM   150  C  C   . GLU A 1 23  ? -19.04259 -28.85517 2.35868   1.000 82.20303  ?  23  GLU A C   1 
ATOM   151  O  O   . GLU A 1 23  ? -19.23156 -28.53152 3.53620   1.000 74.63371  ?  23  GLU A O   1 
ATOM   152  C  CB  . GLU A 1 23  ? -20.17380 -30.87392 1.42894   1.000 87.91526  ?  23  GLU A CB  1 
ATOM   153  C  CG  . GLU A 1 23  ? -20.07900 -32.31724 0.91210   1.000 105.32229 ?  23  GLU A CG  1 
ATOM   154  C  CD  . GLU A 1 23  ? -21.42710 -32.90381 0.50444   1.000 113.02956 ?  23  GLU A CD  1 
ATOM   155  O  OE1 . GLU A 1 23  ? -22.44341 -32.16227 0.54048   1.000 108.02011 ?  23  GLU A OE1 1 
ATOM   156  O  OE2 . GLU A 1 23  ? -21.45739 -34.10724 0.15197   1.000 115.73346 -1 23  GLU A OE2 1 
ATOM   157  N  N   . PRO A 1 24  ? -18.99818 -27.94474 1.38240   1.000 78.35806  ?  24  PRO A N   1 
ATOM   158  C  CA  . PRO A 1 24  ? -19.31792 -26.53606 1.68754   1.000 77.54395  ?  24  PRO A CA  1 
ATOM   159  C  C   . PRO A 1 24  ? -20.72629 -26.42172 2.27078   1.000 73.34508  ?  24  PRO A C   1 
ATOM   160  O  O   . PRO A 1 24  ? -21.66508 -27.06018 1.79204   1.000 75.78208  ?  24  PRO A O   1 
ATOM   161  C  CB  . PRO A 1 24  ? -19.20411 -25.84090 0.32315   1.000 75.48619  ?  24  PRO A CB  1 
ATOM   162  C  CG  . PRO A 1 24  ? -18.50029 -26.84300 -0.58014  1.000 78.70151  ?  24  PRO A CG  1 
ATOM   163  C  CD  . PRO A 1 24  ? -18.78749 -28.19031 -0.05176  1.000 80.49277  ?  24  PRO A CD  1 
ATOM   164  N  N   . VAL A 1 25  ? -20.88819 -25.60748 3.31405   1.000 71.55457  ?  25  VAL A N   1 
ATOM   165  C  CA  . VAL A 1 25  ? -22.18821 -25.47648 3.97893   1.000 70.87181  ?  25  VAL A CA  1 
ATOM   166  C  C   . VAL A 1 25  ? -22.75857 -24.08400 3.71610   1.000 66.86360  ?  25  VAL A C   1 
ATOM   167  O  O   . VAL A 1 25  ? -22.16798 -23.06817 4.10402   1.000 67.13199  ?  25  VAL A O   1 
ATOM   168  C  CB  . VAL A 1 25  ? -22.08564 -25.78839 5.47843   1.000 74.28244  ?  25  VAL A CB  1 
ATOM   169  C  CG1 . VAL A 1 25  ? -20.69789 -25.44190 5.98156   1.000 78.74389  ?  25  VAL A CG1 1 
ATOM   170  C  CG2 . VAL A 1 25  ? -23.18064 -25.05315 6.26153   1.000 65.39976  ?  25  VAL A CG2 1 
ATOM   171  N  N   . SER A 1 26  ? -23.90982 -24.03794 3.05278   1.000 65.56960  ?  26  SER A N   1 
ATOM   172  C  CA  . SER A 1 26  ? -24.41425 -22.77545 2.54369   1.000 67.77171  ?  26  SER A CA  1 
ATOM   173  C  C   . SER A 1 26  ? -24.95290 -21.92505 3.67382   1.000 65.40431  ?  26  SER A C   1 
ATOM   174  O  O   . SER A 1 26  ? -25.33231 -22.43215 4.73694   1.000 61.96262  ?  26  SER A O   1 
ATOM   175  C  CB  . SER A 1 26  ? -25.51553 -23.00419 1.50413   1.000 74.24960  ?  26  SER A CB  1 
ATOM   176  O  OG  . SER A 1 26  ? -26.68281 -23.52637 2.11081   1.000 73.20747  ?  26  SER A OG  1 
ATOM   177  N  N   . GLY A 1 27  ? -24.97113 -20.60998 3.43018   1.000 67.53454  ?  27  GLY A N   1 
ATOM   178  C  CA  . GLY A 1 27  ? -25.62954 -19.71187 4.35644   1.000 59.36328  ?  27  GLY A CA  1 
ATOM   179  C  C   . GLY A 1 27  ? -27.00680 -20.20533 4.73473   1.000 60.40385  ?  27  GLY A C   1 
ATOM   180  O  O   . GLY A 1 27  ? -27.38475 -20.19217 5.91268   1.000 57.89142  ?  27  GLY A O   1 
ATOM   181  N  N   . ALA A 1 28  ? -27.75877 -20.69112 3.74425   1.000 59.77834  ?  28  ALA A N   1 
ATOM   182  C  CA  . ALA A 1 28  ? -29.10613 -21.18558 3.98979   1.000 63.02689  ?  28  ALA A CA  1 
ATOM   183  C  C   . ALA A 1 28  ? -29.10934 -22.38020 4.93568   1.000 67.15427  ?  28  ALA A C   1 
ATOM   184  O  O   . ALA A 1 28  ? -30.07562 -22.57189 5.68415   1.000 60.27470  ?  28  ALA A O   1 
ATOM   185  C  CB  . ALA A 1 28  ? -29.77419 -21.56931 2.66281   1.000 64.57698  ?  28  ALA A CB  1 
ATOM   186  N  N   . GLN A 1 29  ? -28.06746 -23.21482 4.89036   1.000 66.00386  ?  29  GLN A N   1 
ATOM   187  C  CA  . GLN A 1 29  ? -28.03460 -24.36897 5.78324   1.000 68.81404  ?  29  GLN A CA  1 
ATOM   188  C  C   . GLN A 1 29  ? -27.72404 -23.94056 7.19934   1.000 60.63474  ?  29  GLN A C   1 
ATOM   189  O  O   . GLN A 1 29  ? -28.34839 -24.42362 8.14512   1.000 62.81492  ?  29  GLN A O   1 
ATOM   190  C  CB  . GLN A 1 29  ? -27.01355 -25.39806 5.29363   1.000 66.88002  ?  29  GLN A CB  1 
ATOM   191  C  CG  . GLN A 1 29  ? -27.54749 -26.21409 4.12800   1.000 75.89530  ?  29  GLN A CG  1 
ATOM   192  C  CD  . GLN A 1 29  ? -26.46602 -26.73799 3.17981   1.000 83.61135  ?  29  GLN A CD  1 
ATOM   193  O  OE1 . GLN A 1 29  ? -25.27175 -26.49908 3.37309   1.000 78.04753  ?  29  GLN A OE1 1 
ATOM   194  N  NE2 . GLN A 1 29  ? -26.89284 -27.45331 2.14137   1.000 89.64003  ?  29  GLN A NE2 1 
ATOM   195  N  N   . LEU A 1 30  ? -26.77811 -23.01732 7.34801   1.000 63.21127  ?  30  LEU A N   1 
ATOM   196  C  CA  . LEU A 1 30  ? -26.51479 -22.40855 8.64274   1.000 61.36488  ?  30  LEU A CA  1 
ATOM   197  C  C   . LEU A 1 30  ? -27.77873 -21.79069 9.23490   1.000 59.23019  ?  30  LEU A C   1 
ATOM   198  O  O   . LEU A 1 30  ? -28.04972 -21.93963 10.43078  1.000 60.10526  ?  30  LEU A O   1 
ATOM   199  C  CB  . LEU A 1 30  ? -25.41195 -21.35774 8.49431   1.000 59.70723  ?  30  LEU A CB  1 
ATOM   200  C  CG  . LEU A 1 30  ? -24.10250 -21.97714 7.99985   1.000 64.20454  ?  30  LEU A CG  1 
ATOM   201  C  CD1 . LEU A 1 30  ? -23.07044 -20.91513 7.70678   1.000 68.16198  ?  30  LEU A CD1 1 
ATOM   202  C  CD2 . LEU A 1 30  ? -23.55670 -22.93109 9.03265   1.000 61.97865  ?  30  LEU A CD2 1 
ATOM   203  N  N   . ALA A 1 31  ? -28.58211 -21.11171 8.41281   1.000 62.21495  ?  31  ALA A N   1 
ATOM   204  C  CA  . ALA A 1 31  ? -29.74449 -20.42619 8.96921   1.000 58.84088  ?  31  ALA A CA  1 
ATOM   205  C  C   . ALA A 1 31  ? -30.74651 -21.42936 9.51058   1.000 62.07090  ?  31  ALA A C   1 
ATOM   206  O  O   . ALA A 1 31  ? -31.31753 -21.23039 10.59250  1.000 60.43251  ?  31  ALA A O   1 
ATOM   207  C  CB  . ALA A 1 31  ? -30.40095 -19.53243 7.92399   1.000 61.17408  ?  31  ALA A CB  1 
ATOM   208  N  N   . GLU A 1 32  ? -30.96607 -22.51751 8.77493   1.000 58.55857  ?  32  GLU A N   1 
ATOM   209  C  CA  . GLU A 1 32  ? -31.90304 -23.52481 9.24284   1.000 68.77910  ?  32  GLU A CA  1 
ATOM   210  C  C   . GLU A 1 32  ? -31.36087 -24.22853 10.48144  1.000 62.18536  ?  32  GLU A C   1 
ATOM   211  O  O   . GLU A 1 32  ? -32.11530 -24.50929 11.41356  1.000 56.15627  ?  32  GLU A O   1 
ATOM   212  C  CB  . GLU A 1 32  ? -32.21680 -24.53734 8.13912   1.000 70.23909  ?  32  GLU A CB  1 
ATOM   213  C  CG  . GLU A 1 32  ? -33.44996 -25.39753 8.47367   1.000 81.12623  ?  32  GLU A CG  1 
ATOM   214  C  CD  . GLU A 1 32  ? -33.51501 -26.72231 7.69663   1.000 95.97147  ?  32  GLU A CD  1 
ATOM   215  O  OE1 . GLU A 1 32  ? -32.46391 -27.38756 7.53742   1.000 96.86012  ?  32  GLU A OE1 1 
ATOM   216  O  OE2 . GLU A 1 32  ? -34.62101 -27.10594 7.24564   1.000 100.35265 -1 32  GLU A OE2 1 
ATOM   217  N  N   . GLU A 1 33  ? -30.04719 -24.44905 10.54239  1.000 58.86547  ?  33  GLU A N   1 
ATOM   218  C  CA  . GLU A 1 33  ? -29.48324 -25.17323 11.67501  1.000 68.12849  ?  33  GLU A CA  1 
ATOM   219  C  C   . GLU A 1 33  ? -29.49972 -24.34591 12.95286  1.000 65.58222  ?  33  GLU A C   1 
ATOM   220  O  O   . GLU A 1 33  ? -29.62614 -24.90266 14.05503  1.000 60.42819  ?  33  GLU A O   1 
ATOM   221  C  CB  . GLU A 1 33  ? -28.06021 -25.60060 11.35611  1.000 69.29948  ?  33  GLU A CB  1 
ATOM   222  C  CG  . GLU A 1 33  ? -27.49283 -26.54555 12.38537  1.000 80.41434  ?  33  GLU A CG  1 
ATOM   223  C  CD  . GLU A 1 33  ? -26.44228 -27.45955 11.77894  1.000 91.26510  ?  33  GLU A CD  1 
ATOM   224  O  OE1 . GLU A 1 33  ? -26.68999 -28.01763 10.68200  1.000 96.77909  ?  33  GLU A OE1 1 
ATOM   225  O  OE2 . GLU A 1 33  ? -25.35959 -27.60723 12.38784  1.000 91.86441  -1 33  GLU A OE2 1 
ATOM   226  N  N   . LEU A 1 34  ? -29.32233 -23.03095 12.83624  1.000 54.88947  ?  34  LEU A N   1 
ATOM   227  C  CA  . LEU A 1 34  ? -29.18988 -22.18665 14.01246  1.000 65.16718  ?  34  LEU A CA  1 
ATOM   228  C  C   . LEU A 1 34  ? -30.42146 -21.31619 14.26491  1.000 65.42402  ?  34  LEU A C   1 
ATOM   229  O  O   . LEU A 1 34  ? -30.36214 -20.41786 15.10229  1.000 63.78168  ?  34  LEU A O   1 
ATOM   230  C  CB  . LEU A 1 34  ? -27.92760 -21.32994 13.88781  1.000 59.54604  ?  34  LEU A CB  1 
ATOM   231  C  CG  . LEU A 1 34  ? -26.72753 -22.23956 13.64046  1.000 65.32633  ?  34  LEU A CG  1 
ATOM   232  C  CD1 . LEU A 1 34  ? -25.50135 -21.54932 13.03590  1.000 55.69350  ?  34  LEU A CD1 1 
ATOM   233  C  CD2 . LEU A 1 34  ? -26.35801 -22.97729 14.92190  1.000 63.82427  ?  34  LEU A CD2 1 
ATOM   234  N  N   . SER A 1 35  ? -31.51631 -21.54322 13.52992  1.000 66.59028  ?  35  SER A N   1 
ATOM   235  C  CA  . SER A 1 35  ? -32.80795 -20.87088 13.73905  1.000 60.84536  ?  35  SER A CA  1 
ATOM   236  C  C   . SER A 1 35  ? -32.70201 -19.33630 13.67976  1.000 59.06328  ?  35  SER A C   1 
ATOM   237  O  O   . SER A 1 35  ? -33.44996 -18.60710 14.32443  1.000 71.12040  ?  35  SER A O   1 
ATOM   238  C  CB  . SER A 1 35  ? -33.44186 -21.34271 15.04337  1.000 68.01864  ?  35  SER A CB  1 
ATOM   239  O  OG  . SER A 1 35  ? -33.12508 -22.70723 15.27256  1.000 75.14563  ?  35  SER A OG  1 
ATOM   240  N  N   . VAL A 1 36  ? -31.79264 -18.83145 12.86116  1.000 63.90445  ?  36  VAL A N   1 
ATOM   241  C  CA  . VAL A 1 36  ? -31.81999 -17.43093 12.47725  1.000 60.62041  ?  36  VAL A CA  1 
ATOM   242  C  C   . VAL A 1 36  ? -31.98331 -17.33208 10.96552  1.000 59.63991  ?  36  VAL A C   1 
ATOM   243  O  O   . VAL A 1 36  ? -31.82228 -18.29831 10.21447  1.000 57.48008  ?  36  VAL A O   1 
ATOM   244  C  CB  . VAL A 1 36  ? -30.57070 -16.63936 12.93875  1.000 60.04121  ?  36  VAL A CB  1 
ATOM   245  C  CG1 . VAL A 1 36  ? -30.45063 -16.64007 14.48292  1.000 58.10718  ?  36  VAL A CG1 1 
ATOM   246  C  CG2 . VAL A 1 36  ? -29.30512 -17.17708 12.29342  1.000 55.38816  ?  36  VAL A CG2 1 
ATOM   247  N  N   . SER A 1 37  ? -32.32532 -16.13020 10.52376  1.000 64.11879  ?  37  SER A N   1 
ATOM   248  C  CA  . SER A 1 37  ? -32.38429 -15.85867 9.10056   1.000 57.33229  ?  37  SER A CA  1 
ATOM   249  C  C   . SER A 1 37  ? -30.99293 -15.99433 8.48641   1.000 59.29763  ?  37  SER A C   1 
ATOM   250  O  O   . SER A 1 37  ? -29.96907 -15.82329 9.16069   1.000 60.22257  ?  37  SER A O   1 
ATOM   251  C  CB  . SER A 1 37  ? -32.93621 -14.45432 8.86689   1.000 59.49691  ?  37  SER A CB  1 
ATOM   252  O  OG  . SER A 1 37  ? -31.93153 -13.47410 9.02463   1.000 55.62593  ?  37  SER A OG  1 
ATOM   253  N  N   . ARG A 1 38  ? -30.95119 -16.28946 7.18423   1.000 48.51076  ?  38  ARG A N   1 
ATOM   254  C  CA  . ARG A 1 38  ? -29.65656 -16.29356 6.52221   1.000 53.08467  ?  38  ARG A CA  1 
ATOM   255  C  C   . ARG A 1 38  ? -29.04378 -14.89270 6.45272   1.000 55.93685  ?  38  ARG A C   1 
ATOM   256  O  O   . ARG A 1 38  ? -27.81136 -14.76124 6.42359   1.000 55.99970  ?  38  ARG A O   1 
ATOM   257  C  CB  . ARG A 1 38  ? -29.77825 -16.89987 5.11310   1.000 60.10351  ?  38  ARG A CB  1 
ATOM   258  C  CG  . ARG A 1 38  ? -28.47674 -16.79104 4.30894   1.000 57.63909  ?  38  ARG A CG  1 
ATOM   259  C  CD  . ARG A 1 38  ? -28.59136 -17.40184 2.93496   1.000 60.07048  ?  38  ARG A CD  1 
ATOM   260  N  NE  . ARG A 1 38  ? -29.59011 -16.71659 2.12102   1.000 65.52019  ?  38  ARG A NE  1 
ATOM   261  C  CZ  . ARG A 1 38  ? -29.37286 -15.60747 1.42401   1.000 64.68455  ?  38  ARG A CZ  1 
ATOM   262  N  NH1 . ARG A 1 38  ? -28.18161 -15.01918 1.40581   1.000 59.74227  ?  38  ARG A NH1 1 
ATOM   263  N  NH2 . ARG A 1 38  ? -30.38118 -15.06272 0.74341   1.000 57.43688  ?  38  ARG A NH2 1 
ATOM   264  N  N   . GLN A 1 39  ? -29.87033 -13.84377 6.43043   1.000 56.31813  ?  39  GLN A N   1 
ATOM   265  C  CA  . GLN A 1 39  ? -29.33738 -12.48737 6.52027   1.000 59.32130  ?  39  GLN A CA  1 
ATOM   266  C  C   . GLN A 1 39  ? -28.52113 -12.29011 7.80321   1.000 55.82384  ?  39  GLN A C   1 
ATOM   267  O  O   . GLN A 1 39  ? -27.49086 -11.60403 7.79931   1.000 57.79473  ?  39  GLN A O   1 
ATOM   268  C  CB  . GLN A 1 39  ? -30.48845 -11.47782 6.43693   1.000 58.36066  ?  39  GLN A CB  1 
ATOM   269  C  CG  . GLN A 1 39  ? -31.14953 -11.38737 5.07448   1.000 54.14319  ?  39  GLN A CG  1 
ATOM   270  C  CD  . GLN A 1 39  ? -31.85964 -12.68203 4.63756   1.000 52.35362  ?  39  GLN A CD  1 
ATOM   271  O  OE1 . GLN A 1 39  ? -32.30980 -13.49650 5.46843   1.000 49.04392  ?  39  GLN A OE1 1 
ATOM   272  N  NE2 . GLN A 1 39  ? -31.97033 -12.85989 3.31845   1.000 48.94254  ?  39  GLN A NE2 1 
ATOM   273  N  N   . VAL A 1 40  ? -28.99189 -12.84810 8.91615   1.000 55.48792  ?  40  VAL A N   1 
ATOM   274  C  CA  . VAL A 1 40  ? -28.21804 -12.84380 10.15307  1.000 56.92836  ?  40  VAL A CA  1 
ATOM   275  C  C   . VAL A 1 40  ? -26.92165 -13.62581 9.97461   1.000 57.90193  ?  40  VAL A C   1 
ATOM   276  O  O   . VAL A 1 40  ? -25.84770 -13.17192 10.38360  1.000 60.50479  ?  40  VAL A O   1 
ATOM   277  C  CB  . VAL A 1 40  ? -29.06530 -13.39823 11.31064  1.000 56.62402  ?  40  VAL A CB  1 
ATOM   278  C  CG1 . VAL A 1 40  ? -28.20075 -13.64683 12.51531  1.000 50.56034  ?  40  VAL A CG1 1 
ATOM   279  C  CG2 . VAL A 1 40  ? -30.17622 -12.42532 11.66092  1.000 58.33364  ?  40  VAL A CG2 1 
ATOM   280  N  N   . ILE A 1 41  ? -26.99930 -14.80667 9.34976   1.000 59.91708  ?  41  ILE A N   1 
ATOM   281  C  CA  . ILE A 1 41  ? -25.79505 -15.58495 9.05860   1.000 57.39439  ?  41  ILE A CA  1 
ATOM   282  C  C   . ILE A 1 41  ? -24.79086 -14.73374 8.29431   1.000 64.81696  ?  41  ILE A C   1 
ATOM   283  O  O   . ILE A 1 41  ? -23.61390 -14.64959 8.67151   1.000 61.78095  ?  41  ILE A O   1 
ATOM   284  C  CB  . ILE A 1 41  ? -26.14815 -16.86724 8.28254   1.000 55.86869  ?  41  ILE A CB  1 
ATOM   285  C  CG1 . ILE A 1 41  ? -26.93390 -17.84131 9.16251   1.000 56.18866  ?  41  ILE A CG1 1 
ATOM   286  C  CG2 . ILE A 1 41  ? -24.89003 -17.56719 7.85275   1.000 60.98001  ?  41  ILE A CG2 1 
ATOM   287  C  CD1 . ILE A 1 41  ? -26.26552 -18.10141 10.50838  1.000 56.88591  ?  41  ILE A CD1 1 
ATOM   288  N  N   . VAL A 1 42  ? -25.25244 -14.06483 7.22295   1.000 58.58945  ?  42  VAL A N   1 
ATOM   289  C  CA  . VAL A 1 42  ? -24.36144 -13.25042 6.39847   1.000 59.42988  ?  42  VAL A CA  1 
ATOM   290  C  C   . VAL A 1 42  ? -23.63162 -12.21641 7.24154   1.000 65.04935  ?  42  VAL A C   1 
ATOM   291  O  O   . VAL A 1 42  ? -22.45183 -11.92760 7.01175   1.000 67.98387  ?  42  VAL A O   1 
ATOM   292  C  CB  . VAL A 1 42  ? -25.14441 -12.57761 5.24980   1.000 66.25091  ?  42  VAL A CB  1 
ATOM   293  C  CG1 . VAL A 1 42  ? -24.36120 -11.41827 4.69623   1.000 56.73201  ?  42  VAL A CG1 1 
ATOM   294  C  CG2 . VAL A 1 42  ? -25.40933 -13.56596 4.12466   1.000 58.76015  ?  42  VAL A CG2 1 
ATOM   295  N  N   . GLN A 1 43  ? -24.31179 -11.62455 8.22103   1.000 67.65513  ?  43  GLN A N   1 
ATOM   296  C  CA  . GLN A 1 43  ? -23.60271 -10.70849 9.10276   1.000 70.48427  ?  43  GLN A CA  1 
ATOM   297  C  C   . GLN A 1 43  ? -22.59459 -11.44360 9.97719   1.000 74.15608  ?  43  GLN A C   1 
ATOM   298  O  O   . GLN A 1 43  ? -21.47283 -10.96273 10.18523  1.000 76.33177  ?  43  GLN A O   1 
ATOM   299  C  CB  . GLN A 1 43  ? -24.59450 -9.94904  9.96318   1.000 75.93327  ?  43  GLN A CB  1 
ATOM   300  C  CG  . GLN A 1 43  ? -25.46253 -9.04932  9.15787   1.000 73.18859  ?  43  GLN A CG  1 
ATOM   301  C  CD  . GLN A 1 43  ? -26.42863 -8.31182  10.02434  1.000 78.61075  ?  43  GLN A CD  1 
ATOM   302  O  OE1 . GLN A 1 43  ? -26.04730 -7.46074  10.83323  1.000 80.34791  ?  43  GLN A OE1 1 
ATOM   303  N  NE2 . GLN A 1 43  ? -27.69772 -8.65637  9.89339   1.000 79.75135  ?  43  GLN A NE2 1 
ATOM   304  N  N   . ASP A 1 44  ? -22.97434 -12.60989 10.49907  1.000 66.24001  ?  44  ASP A N   1 
ATOM   305  C  CA  . ASP A 1 44  ? -22.06408 -13.33004 11.37357  1.000 74.79055  ?  44  ASP A CA  1 
ATOM   306  C  C   . ASP A 1 44  ? -20.80490 -13.75084 10.63012  1.000 76.78666  ?  44  ASP A C   1 
ATOM   307  O  O   . ASP A 1 44  ? -19.71183 -13.75440 11.20920  1.000 76.89533  ?  44  ASP A O   1 
ATOM   308  C  CB  . ASP A 1 44  ? -22.77070 -14.54427 11.99110  1.000 71.67995  ?  44  ASP A CB  1 
ATOM   309  C  CG  . ASP A 1 44  ? -23.91577 -14.14493 12.91440  1.000 72.38007  ?  44  ASP A CG  1 
ATOM   310  O  OD1 . ASP A 1 44  ? -23.89393 -13.01663 13.47848  1.000 80.21234  ?  44  ASP A OD1 1 
ATOM   311  O  OD2 . ASP A 1 44  ? -24.84008 -14.96165 13.07111  1.000 70.30098  -1 44  ASP A OD2 1 
ATOM   312  N  N   . ILE A 1 45  ? -20.92376 -14.08475 9.34672   1.000 73.17287  ?  45  ILE A N   1 
ATOM   313  C  CA  . ILE A 1 45  ? -19.73653 -14.48313 8.60577   1.000 75.23446  ?  45  ILE A CA  1 
ATOM   314  C  C   . ILE A 1 45  ? -18.79100 -13.30238 8.43070   1.000 81.37494  ?  45  ILE A C   1 
ATOM   315  O  O   . ILE A 1 45  ? -17.56672 -13.45098 8.53566   1.000 83.79776  ?  45  ILE A O   1 
ATOM   316  C  CB  . ILE A 1 45  ? -20.12805 -15.09349 7.25695   1.000 75.60747  ?  45  ILE A CB  1 
ATOM   317  C  CG1 . ILE A 1 45  ? -21.08154 -16.26237 7.47449   1.000 71.82444  ?  45  ILE A CG1 1 
ATOM   318  C  CG2 . ILE A 1 45  ? -18.88268 -15.54738 6.52416   1.000 75.41182  ?  45  ILE A CG2 1 
ATOM   319  C  CD1 . ILE A 1 45  ? -20.41394 -17.44227 8.05109   1.000 75.50972  ?  45  ILE A CD1 1 
ATOM   320  N  N   . ALA A 1 46  ? -19.33372 -12.11280 8.16159   1.000 80.03661  ?  46  ALA A N   1 
ATOM   321  C  CA  . ALA A 1 46  ? -18.48413 -10.92953 8.05156   1.000 83.40545  ?  46  ALA A CA  1 
ATOM   322  C  C   . ALA A 1 46  ? -17.83967 -10.56859 9.38580   1.000 89.42377  ?  46  ALA A C   1 
ATOM   323  O  O   . ALA A 1 46  ? -16.72626 -10.02128 9.41353   1.000 92.77695  ?  46  ALA A O   1 
ATOM   324  C  CB  . ALA A 1 46  ? -19.29560 -9.75449  7.51305   1.000 82.57698  ?  46  ALA A CB  1 
ATOM   325  N  N   . TYR A 1 47  ? -18.52490 -10.86062 10.49402  1.000 85.29231  ?  47  TYR A N   1 
ATOM   326  C  CA  . TYR A 1 47  ? -17.97777 -10.56625 11.81349  1.000 90.65762  ?  47  TYR A CA  1 
ATOM   327  C  C   . TYR A 1 47  ? -16.80936 -11.48594 12.12596  1.000 91.91044  ?  47  TYR A C   1 
ATOM   328  O  O   . TYR A 1 47  ? -15.80134 -11.04865 12.69851  1.000 95.53087  ?  47  TYR A O   1 
ATOM   329  C  CB  . TYR A 1 47  ? -19.08303 -10.70013 12.86919  1.000 89.47935  ?  47  TYR A CB  1 
ATOM   330  C  CG  . TYR A 1 47  ? -18.71946 -10.26321 14.28229  1.000 95.78532  ?  47  TYR A CG  1 
ATOM   331  C  CD1 . TYR A 1 47  ? -17.74488 -10.93204 15.01123  1.000 99.49667  ?  47  TYR A CD1 1 
ATOM   332  C  CD2 . TYR A 1 47  ? -19.39303 -9.20982  14.90302  1.000 101.23978 ?  47  TYR A CD2 1 
ATOM   333  C  CE1 . TYR A 1 47  ? -17.41377 -10.54190 16.31064  1.000 104.39100 ?  47  TYR A CE1 1 
ATOM   334  C  CE2 . TYR A 1 47  ? -19.08041 -8.82165  16.19673  1.000 106.32409 ?  47  TYR A CE2 1 
ATOM   335  C  CZ  . TYR A 1 47  ? -18.08533 -9.49110  16.89617  1.000 103.49251 ?  47  TYR A CZ  1 
ATOM   336  O  OH  . TYR A 1 47  ? -17.76233 -9.12003  18.17916  1.000 108.05473 ?  47  TYR A OH  1 
ATOM   337  N  N   . LEU A 1 48  ? -16.93054 -12.76297 11.74699  1.000 90.72182  ?  48  LEU A N   1 
ATOM   338  C  CA  . LEU A 1 48  ? -15.91701 -13.75737 12.07420  1.000 86.73496  ?  48  LEU A CA  1 
ATOM   339  C  C   . LEU A 1 48  ? -14.64595 -13.53908 11.26843  1.000 95.97878  ?  48  LEU A C   1 
ATOM   340  O  O   . LEU A 1 48  ? -13.54073 -13.77166 11.77918  1.000 101.22046 ?  48  LEU A O   1 
ATOM   341  C  CB  . LEU A 1 48  ? -16.47388 -15.16325 11.84105  1.000 81.51044  ?  48  LEU A CB  1 
ATOM   342  C  CG  . LEU A 1 48  ? -17.55217 -15.64454 12.81971  1.000 83.51024  ?  48  LEU A CG  1 
ATOM   343  C  CD1 . LEU A 1 48  ? -18.31407 -16.84424 12.27872  1.000 72.55900  ?  48  LEU A CD1 1 
ATOM   344  C  CD2 . LEU A 1 48  ? -16.93766 -15.98743 14.18063  1.000 89.74033  ?  48  LEU A CD2 1 
ATOM   345  N  N   . ARG A 1 49  ? -14.77595 -13.07081 10.02491  1.000 90.49369  ?  49  ARG A N   1 
ATOM   346  C  CA  . ARG A 1 49  ? -13.59392 -12.82175 9.20940   1.000 93.31320  ?  49  ARG A CA  1 
ATOM   347  C  C   . ARG A 1 49  ? -12.80144 -11.64364 9.75306   1.000 96.11102  ?  49  ARG A C   1 
ATOM   348  O  O   . ARG A 1 49  ? -11.58527 -11.74312 9.94689   1.000 100.09997 ?  49  ARG A O   1 
ATOM   349  C  CB  . ARG A 1 49  ? -13.99028 -12.60574 7.74578   1.000 91.07815  ?  49  ARG A CB  1 
ATOM   350  C  CG  . ARG A 1 49  ? -13.90551 -13.89391 6.91753   1.000 91.96482  ?  49  ARG A CG  1 
ATOM   351  C  CD  . ARG A 1 49  ? -14.28141 -13.68284 5.47076   1.000 90.37615  ?  49  ARG A CD  1 
ATOM   352  N  NE  . ARG A 1 49  ? -15.55262 -12.98345 5.37289   1.000 93.40736  ?  49  ARG A NE  1 
ATOM   353  C  CZ  . ARG A 1 49  ? -16.41505 -13.12180 4.37447   1.000 95.99949  ?  49  ARG A CZ  1 
ATOM   354  N  NH1 . ARG A 1 49  ? -16.18345 -13.95402 3.37071   1.000 99.13124  ?  49  ARG A NH1 1 
ATOM   355  N  NH2 . ARG A 1 49  ? -17.54509 -12.41567 4.39000   1.000 90.02882  ?  49  ARG A NH2 1 
ATOM   356  N  N   . SER A 1 50  ? -13.47626 -10.52371 10.02692  1.000 98.25619  ?  50  SER A N   1 
ATOM   357  C  CA  . SER A 1 50  ? -12.81578 -9.41120  10.69980  1.000 98.28437  ?  50  SER A CA  1 
ATOM   358  C  C   . SER A 1 50  ? -12.13377 -9.84878  11.98644  1.000 101.15614 ?  50  SER A C   1 
ATOM   359  O  O   . SER A 1 50  ? -11.24171 -9.14852  12.47328  1.000 107.20845 ?  50  SER A O   1 
ATOM   360  C  CB  . SER A 1 50  ? -13.82750 -8.31422  11.00970  1.000 99.57757  ?  50  SER A CB  1 
ATOM   361  O  OG  . SER A 1 50  ? -14.87674 -8.82774  11.80908  1.000 99.11155  ?  50  SER A OG  1 
ATOM   362  N  N   . LEU A 1 51  ? -12.53812 -10.98997 12.54817  1.000 102.33731 ?  51  LEU A N   1 
ATOM   363  C  CA  . LEU A 1 51  ? -11.92520 -11.52148 13.75629  1.000 100.14344 ?  51  LEU A CA  1 
ATOM   364  C  C   . LEU A 1 51  ? -10.65901 -12.31704 13.48679  1.000 106.97556 ?  51  LEU A C   1 
ATOM   365  O  O   . LEU A 1 51  ? -9.79412  -12.40022 14.36798  1.000 121.19498 ?  51  LEU A O   1 
ATOM   366  C  CB  . LEU A 1 51  ? -12.91971 -12.40238 14.50586  1.000 95.18813  ?  51  LEU A CB  1 
ATOM   367  C  CG  . LEU A 1 51  ? -13.96010 -11.56347 15.23610  1.000 99.38047  ?  51  LEU A CG  1 
ATOM   368  C  CD1 . LEU A 1 51  ? -14.82093 -12.44399 16.11613  1.000 98.12027  ?  51  LEU A CD1 1 
ATOM   369  C  CD2 . LEU A 1 51  ? -13.26201 -10.47313 16.04139  1.000 101.31332 ?  51  LEU A CD2 1 
ATOM   370  N  N   . GLY A 1 52  ? -10.52228 -12.90357 12.30258  1.000 111.80848 ?  52  GLY A N   1 
ATOM   371  C  CA  . GLY A 1 52  ? -9.31260  -13.63324 11.97932  1.000 113.30001 ?  52  GLY A CA  1 
ATOM   372  C  C   . GLY A 1 52  ? -9.55914  -15.03674 11.46869  1.000 112.43767 ?  52  GLY A C   1 
ATOM   373  O  O   . GLY A 1 52  ? -8.62524  -15.83947 11.36721  1.000 117.37558 ?  52  GLY A O   1 
ATOM   374  N  N   . TYR A 1 53  ? -10.81199 -15.35269 11.15641  1.000 102.98240 ?  53  TYR A N   1 
ATOM   375  C  CA  . TYR A 1 53  ? -11.13296 -16.62044 10.52017  1.000 104.03373 ?  53  TYR A CA  1 
ATOM   376  C  C   . TYR A 1 53  ? -11.18328 -16.43531 9.00610   1.000 101.05374 ?  53  TYR A C   1 
ATOM   377  O  O   . TYR A 1 53  ? -11.54783 -15.36977 8.50158   1.000 101.20092 ?  53  TYR A O   1 
ATOM   378  C  CB  . TYR A 1 53  ? -12.45780 -17.18042 11.04490  1.000 94.39980  ?  53  TYR A CB  1 
ATOM   379  C  CG  . TYR A 1 53  ? -12.42472 -17.56911 12.51017  1.000 95.64890  ?  53  TYR A CG  1 
ATOM   380  C  CD1 . TYR A 1 53  ? -12.46189 -16.60245 13.51222  1.000 98.82654  ?  53  TYR A CD1 1 
ATOM   381  C  CD2 . TYR A 1 53  ? -12.36151 -18.90321 12.89196  1.000 94.27329  ?  53  TYR A CD2 1 
ATOM   382  C  CE1 . TYR A 1 53  ? -12.42657 -16.95990 14.86159  1.000 101.30727 ?  53  TYR A CE1 1 
ATOM   383  C  CE2 . TYR A 1 53  ? -12.32750 -19.27046 14.23405  1.000 95.82049  ?  53  TYR A CE2 1 
ATOM   384  C  CZ  . TYR A 1 53  ? -12.36133 -18.29770 15.21610  1.000 100.71614 ?  53  TYR A CZ  1 
ATOM   385  O  OH  . TYR A 1 53  ? -12.32407 -18.66590 16.55192  1.000 109.68412 ?  53  TYR A OH  1 
ATOM   386  N  N   . ASN A 1 54  ? -10.77767 -17.47401 8.28342   1.000 95.89977  ?  54  ASN A N   1 
ATOM   387  C  CA  . ASN A 1 54  ? -10.68966 -17.43066 6.82637   1.000 93.64547  ?  54  ASN A CA  1 
ATOM   388  C  C   . ASN A 1 54  ? -11.83263 -18.27506 6.25975   1.000 92.61917  ?  54  ASN A C   1 
ATOM   389  O  O   . ASN A 1 54  ? -11.66340 -19.45810 5.95332   1.000 90.25190  ?  54  ASN A O   1 
ATOM   390  C  CB  . ASN A 1 54  ? -9.32195  -17.91866 6.34232   1.000 97.11304  ?  54  ASN A CB  1 
ATOM   391  C  CG  . ASN A 1 54  ? -9.09161  -17.64605 4.85410   1.000 97.56974  ?  54  ASN A CG  1 
ATOM   392  O  OD1 . ASN A 1 54  ? -9.71500  -16.75743 4.26284   1.000 93.07427  ?  54  ASN A OD1 1 
ATOM   393  N  ND2 . ASN A 1 54  ? -8.18507  -18.41134 4.24682   1.000 98.62226  ?  54  ASN A ND2 1 
ATOM   394  N  N   . ILE A 1 55  ? -13.00320 -17.65586 6.13121   1.000 91.17889  ?  55  ILE A N   1 
ATOM   395  C  CA  . ILE A 1 55  ? -14.16363 -18.27283 5.50848   1.000 86.40537  ?  55  ILE A CA  1 
ATOM   396  C  C   . ILE A 1 55  ? -14.34037 -17.63494 4.14202   1.000 92.26135  ?  55  ILE A C   1 
ATOM   397  O  O   . ILE A 1 55  ? -14.48588 -16.40989 4.03141   1.000 93.72806  ?  55  ILE A O   1 
ATOM   398  C  CB  . ILE A 1 55  ? -15.42783 -18.10327 6.36031   1.000 83.00671  ?  55  ILE A CB  1 
ATOM   399  C  CG1 . ILE A 1 55  ? -15.17021 -18.58678 7.78550   1.000 83.61371  ?  55  ILE A CG1 1 
ATOM   400  C  CG2 . ILE A 1 55  ? -16.59222 -18.85228 5.72594   1.000 78.13831  ?  55  ILE A CG2 1 
ATOM   401  C  CD1 . ILE A 1 55  ? -16.42494 -18.70076 8.63547   1.000 77.87225  ?  55  ILE A CD1 1 
ATOM   402  N  N   . VAL A 1 56  ? -14.31451 -18.46074 3.10311   1.000 91.03839  ?  56  VAL A N   1 
ATOM   403  C  CA  . VAL A 1 56  ? -14.54648 -18.01881 1.73710   1.000 86.42439  ?  56  VAL A CA  1 
ATOM   404  C  C   . VAL A 1 56  ? -15.87335 -18.59351 1.27510   1.000 81.13247  ?  56  VAL A C   1 
ATOM   405  O  O   . VAL A 1 56  ? -16.22243 -19.73605 1.60403   1.000 77.87326  ?  56  VAL A O   1 
ATOM   406  C  CB  . VAL A 1 56  ? -13.40117 -18.44247 0.80187   1.000 89.87466  ?  56  VAL A CB  1 
ATOM   407  C  CG1 . VAL A 1 56  ? -12.07344 -17.92718 1.34486   1.000 91.20026  ?  56  VAL A CG1 1 
ATOM   408  C  CG2 . VAL A 1 56  ? -13.38683 -19.95117 0.64135   1.000 87.29216  ?  56  VAL A CG2 1 
ATOM   409  N  N   . ALA A 1 57  ? -16.62865 -17.79066 0.54377   1.000 79.95324  ?  57  ALA A N   1 
ATOM   410  C  CA  . ALA A 1 57  ? -17.87790 -18.26351 -0.01271  1.000 78.75557  ?  57  ALA A CA  1 
ATOM   411  C  C   . ALA A 1 57  ? -17.60848 -18.91808 -1.35842  1.000 81.78072  ?  57  ALA A C   1 
ATOM   412  O  O   . ALA A 1 57  ? -16.79306 -18.43250 -2.14553  1.000 90.49117  ?  57  ALA A O   1 
ATOM   413  C  CB  . ALA A 1 57  ? -18.87481 -17.11778 -0.15712  1.000 82.37274  ?  57  ALA A CB  1 
ATOM   414  N  N   . THR A 1 58  ? -18.27872 -20.03413 -1.60700  1.000 81.70114  ?  58  THR A N   1 
ATOM   415  C  CA  . THR A 1 58  ? -18.13144 -20.75458 -2.86442  1.000 82.08865  ?  58  THR A CA  1 
ATOM   416  C  C   . THR A 1 58  ? -19.52558 -20.96000 -3.43662  1.000 82.11273  ?  58  THR A C   1 
ATOM   417  O  O   . THR A 1 58  ? -20.51583 -20.75069 -2.72549  1.000 83.99137  ?  58  THR A O   1 
ATOM   418  C  CB  . THR A 1 58  ? -17.39788 -22.08832 -2.64859  1.000 81.07695  ?  58  THR A CB  1 
ATOM   419  O  OG1 . THR A 1 58  ? -18.32956 -23.13080 -2.31104  1.000 76.07430  ?  58  THR A OG1 1 
ATOM   420  C  CG2 . THR A 1 58  ? -16.37270 -21.93841 -1.52524  1.000 76.53674  ?  58  THR A CG2 1 
ATOM   421  N  N   . PRO A 1 59  ? -19.65617 -21.36735 -4.69550  1.000 80.29656  ?  59  PRO A N   1 
ATOM   422  C  CA  . PRO A 1 59  ? -21.00528 -21.58015 -5.24778  1.000 83.51964  ?  59  PRO A CA  1 
ATOM   423  C  C   . PRO A 1 59  ? -21.86784 -22.53947 -4.42737  1.000 84.46727  ?  59  PRO A C   1 
ATOM   424  O  O   . PRO A 1 59  ? -23.09560 -22.36567 -4.37913  1.000 87.73872  ?  59  PRO A O   1 
ATOM   425  C  CB  . PRO A 1 59  ? -20.71856 -22.12745 -6.65467  1.000 90.39276  ?  59  PRO A CB  1 
ATOM   426  C  CG  . PRO A 1 59  ? -19.30607 -21.67046 -6.97662  1.000 84.90154  ?  59  PRO A CG  1 
ATOM   427  C  CD  . PRO A 1 59  ? -18.59335 -21.70012 -5.66128  1.000 82.52997  ?  59  PRO A CD  1 
ATOM   428  N  N   . ARG A 1 60  ? -21.26673 -23.53267 -3.76607  1.000 83.00067  ?  60  ARG A N   1 
ATOM   429  C  CA  . ARG A 1 60  ? -22.00036 -24.51905 -2.97898  1.000 80.42353  ?  60  ARG A CA  1 
ATOM   430  C  C   . ARG A 1 60  ? -22.13120 -24.16861 -1.50589  1.000 80.67771  ?  60  ARG A C   1 
ATOM   431  O  O   . ARG A 1 60  ? -22.87570 -24.85192 -0.79706  1.000 80.85755  ?  60  ARG A O   1 
ATOM   432  C  CB  . ARG A 1 60  ? -21.33261 -25.88582 -3.08806  1.000 81.79702  ?  60  ARG A CB  1 
ATOM   433  C  CG  . ARG A 1 60  ? -20.84271 -26.20316 -4.45804  1.000 83.67804  ?  60  ARG A CG  1 
ATOM   434  C  CD  . ARG A 1 60  ? -21.19641 -27.61293 -4.80639  1.000 86.83257  ?  60  ARG A CD  1 
ATOM   435  N  NE  . ARG A 1 60  ? -21.56928 -27.67380 -6.21132  1.000 96.59594  ?  60  ARG A NE  1 
ATOM   436  C  CZ  . ARG A 1 60  ? -20.71572 -27.55276 -7.21876  1.000 93.76061  ?  60  ARG A CZ  1 
ATOM   437  N  NH1 . ARG A 1 60  ? -19.41210 -27.43007 -7.01134  1.000 90.56281  ?  60  ARG A NH1 1 
ATOM   438  N  NH2 . ARG A 1 60  ? -21.18168 -27.54265 -8.46363  1.000 89.19129  ?  60  ARG A NH2 1 
ATOM   439  N  N   . GLY A 1 61  ? -21.41079 -23.16106 -1.01434  1.000 81.00503  ?  61  GLY A N   1 
ATOM   440  C  CA  . GLY A 1 61  ? -21.50644 -22.75326 0.37358   1.000 70.12420  ?  61  GLY A CA  1 
ATOM   441  C  C   . GLY A 1 61  ? -20.17192 -22.30116 0.91430   1.000 73.81612  ?  61  GLY A C   1 
ATOM   442  O  O   . GLY A 1 61  ? -19.19320 -22.19072 0.17847   1.000 80.87012  ?  61  GLY A O   1 
ATOM   443  N  N   . TYR A 1 62  ? -20.13072 -22.04492 2.22358   1.000 68.96186  ?  62  TYR A N   1 
ATOM   444  C  CA  . TYR A 1 62  ? -18.91816 -21.55063 2.86074   1.000 72.19395  ?  62  TYR A CA  1 
ATOM   445  C  C   . TYR A 1 62  ? -17.98020 -22.69630 3.20562   1.000 73.51288  ?  62  TYR A C   1 
ATOM   446  O  O   . TYR A 1 62  ? -18.41282 -23.80977 3.52098   1.000 74.04467  ?  62  TYR A O   1 
ATOM   447  C  CB  . TYR A 1 62  ? -19.23145 -20.77690 4.14690   1.000 70.78263  ?  62  TYR A CB  1 
ATOM   448  C  CG  . TYR A 1 62  ? -20.11815 -19.56508 3.96868   1.000 74.71452  ?  62  TYR A CG  1 
ATOM   449  C  CD1 . TYR A 1 62  ? -19.61837 -18.37395 3.44584   1.000 75.60280  ?  62  TYR A CD1 1 
ATOM   450  C  CD2 . TYR A 1 62  ? -21.45088 -19.60141 4.35191   1.000 70.35843  ?  62  TYR A CD2 1 
ATOM   451  C  CE1 . TYR A 1 62  ? -20.43879 -17.25674 3.28770   1.000 72.37994  ?  62  TYR A CE1 1 
ATOM   452  C  CE2 . TYR A 1 62  ? -22.27425 -18.49646 4.19922   1.000 73.40157  ?  62  TYR A CE2 1 
ATOM   453  C  CZ  . TYR A 1 62  ? -21.76788 -17.32781 3.66963   1.000 72.81703  ?  62  TYR A CZ  1 
ATOM   454  O  OH  . TYR A 1 62  ? -22.59710 -16.23759 3.52938   1.000 77.15758  ?  62  TYR A OH  1 
ATOM   455  N  N   . VAL A 1 63  ? -16.67934 -22.40404 3.16714   1.000 70.21272  ?  63  VAL A N   1 
ATOM   456  C  CA  . VAL A 1 63  ? -15.66412 -23.32193 3.65798   1.000 73.12452  ?  63  VAL A CA  1 
ATOM   457  C  C   . VAL A 1 63  ? -14.65152 -22.54247 4.48779   1.000 80.79995  ?  63  VAL A C   1 
ATOM   458  O  O   . VAL A 1 63  ? -14.28093 -21.40526 4.17207   1.000 78.99999  ?  63  VAL A O   1 
ATOM   459  C  CB  . VAL A 1 63  ? -14.95896 -24.09677 2.52420   1.000 75.64221  ?  63  VAL A CB  1 
ATOM   460  C  CG1 . VAL A 1 63  ? -15.98826 -24.74493 1.60680   1.000 72.02263  ?  63  VAL A CG1 1 
ATOM   461  C  CG2 . VAL A 1 63  ? -14.03116 -23.17567 1.76421   1.000 79.26047  ?  63  VAL A CG2 1 
ATOM   462  N  N   . LEU A 1 64  ? -14.22312 -23.16604 5.57209   1.000 76.82263  ?  64  LEU A N   1 
ATOM   463  C  CA  . LEU A 1 64  ? -13.22512 -22.60178 6.46387   1.000 81.22007  ?  64  LEU A CA  1 
ATOM   464  C  C   . LEU A 1 64  ? -11.84375 -23.02853 5.98110   1.000 85.61388  ?  64  LEU A C   1 
ATOM   465  O  O   . LEU A 1 64  ? -11.57549 -24.22861 5.86870   1.000 86.34330  ?  64  LEU A O   1 
ATOM   466  C  CB  . LEU A 1 64  ? -13.47424 -23.07930 7.89395   1.000 79.65522  ?  64  LEU A CB  1 
ATOM   467  C  CG  . LEU A 1 64  ? -12.48513 -22.51244 8.89772   1.000 84.12882  ?  64  LEU A CG  1 
ATOM   468  C  CD1 . LEU A 1 64  ? -12.61981 -21.00132 8.90630   1.000 86.77894  ?  64  LEU A CD1 1 
ATOM   469  C  CD2 . LEU A 1 64  ? -12.74069 -23.11075 10.27191  1.000 88.45289  ?  64  LEU A CD2 1 
ATOM   470  N  N   . ALA A 1 65  ? -10.96485 -22.05684 5.72255   1.000 92.40032  ?  65  ALA A N   1 
ATOM   471  C  CA  . ALA A 1 65  ? -9.63800  -22.30893 5.16965   1.000 89.39716  ?  65  ALA A CA  1 
ATOM   472  C  C   . ALA A 1 65  ? -8.53551  -22.02168 6.18573   1.000 99.13860  ?  65  ALA A C   1 
ATOM   473  O  O   . ALA A 1 65  ? -8.73883  -21.32697 7.18597   1.000 102.06522 ?  65  ALA A O   1 
ATOM   474  C  CB  . ALA A 1 65  ? -9.40800  -21.46786 3.91161   1.000 91.78034  ?  65  ALA A CB  1 
ATOM   475  N  N   . GLY A 1 66  ? -7.34112  -22.53866 5.88959   1.000 106.01498 ?  66  GLY A N   1 
ATOM   476  C  CA  . GLY A 1 66  ? -6.25400  -22.58007 6.85211   1.000 115.55159 ?  66  GLY A CA  1 
ATOM   477  C  C   . GLY A 1 66  ? -5.53676  -21.27475 7.12930   1.000 124.90892 ?  66  GLY A C   1 
ATOM   478  O  O   . GLY A 1 66  ? -6.00553  -20.44399 7.91448   1.000 126.68367 ?  66  GLY A O   1 
ATOM   479  N  N   . GLY A 1 67  ? -4.37606  -21.09833 6.51159   1.000 133.00015 ?  67  GLY A N   1 
ATOM   480  C  CA  . GLY A 1 67  ? -3.61182  -19.89638 6.75595   1.000 142.14914 ?  67  GLY A CA  1 
ATOM   481  C  C   . GLY A 1 67  ? -3.17032  -19.78332 8.20844   1.000 148.61945 ?  67  GLY A C   1 
ATOM   482  O  O   . GLY A 1 67  ? -3.14795  -20.75690 8.96864   1.000 150.49281 ?  67  GLY A O   1 
ATOM   483  N  N   . LYS A 1 68  ? -2.82069  -18.54997 8.58852   1.000 149.84366 ?  68  LYS A N   1 
ATOM   484  C  CA  . LYS A 1 68  ? -2.30073  -18.24218 9.92386   1.000 142.65623 ?  68  LYS A CA  1 
ATOM   485  C  C   . LYS A 1 68  ? -0.89848  -18.81590 10.11423  1.000 140.62722 ?  68  LYS A C   1 
ATOM   486  O  O   . LYS A 1 68  ? -0.52921  -19.23225 11.21191  1.000 144.45001 ?  68  LYS A O   1 
ATOM   487  C  CB  . LYS A 1 68  ? -3.24545  -18.73853 11.02638  1.000 142.88205 ?  68  LYS A CB  1 
ATOM   488  C  CG  . LYS A 1 68  ? -4.36031  -17.76321 11.39333  1.000 138.78535 ?  68  LYS A CG  1 
ATOM   489  C  CD  . LYS A 1 68  ? -5.39694  -18.39602 12.32115  1.000 137.26683 ?  68  LYS A CD  1 
ATOM   490  C  CE  . LYS A 1 68  ? -6.47750  -17.38817 12.73211  1.000 128.39280 ?  68  LYS A CE  1 
ATOM   491  N  NZ  . LYS A 1 68  ? -7.63964  -17.98818 13.47754  1.000 114.68198 ?  68  LYS A NZ  1 
ATOM   492  N  N   . SER A 1 69  ? -0.10839  -18.82162 9.04094   1.000 139.49499 ?  69  SER A N   1 
ATOM   493  C  CA  . SER A 1 69  ? 1.20276   -19.45989 9.05034   1.000 138.17094 ?  69  SER A CA  1 
ATOM   494  C  C   . SER A 1 69  ? 2.05947   -18.96914 10.21754  1.000 133.76105 ?  69  SER A C   1 
ATOM   495  O  O   . SER A 1 69  ? 1.72908   -17.97571 10.88062  1.000 132.96610 ?  69  SER A O   1 
ATOM   496  C  CB  . SER A 1 69  ? 1.91880   -19.22039 7.71243   1.000 134.63277 ?  69  SER A CB  1 
ATOM   497  O  OG  . SER A 1 69  ? 2.80835   -20.28126 7.38958   1.000 122.01865 ?  69  SER A OG  1 
ATOM   498  N  N   . GLY A 1 70  ? 3.15280   -19.68351 10.48376  1.000 128.63702 ?  70  GLY A N   1 
ATOM   499  C  CA  . GLY A 1 70  ? 4.09081   -19.32271 11.52833  1.000 125.31979 ?  70  GLY A CA  1 
ATOM   500  C  C   . GLY A 1 70  ? 5.51257   -19.13043 11.02614  1.000 120.50506 ?  70  GLY A C   1 
ATOM   501  O  O   . GLY A 1 70  ? 5.77379   -18.23577 10.21619  1.000 118.61234 ?  70  GLY A O   1 
ATOM   502  N  N   . VAL A 1 71  ? 6.44080   -19.97043 11.48637  1.000 116.60660 ?  71  VAL A N   1 
ATOM   503  C  CA  . VAL A 1 71  ? 7.86601   -19.79221 11.22499  1.000 113.26920 ?  71  VAL A CA  1 
ATOM   504  C  C   . VAL A 1 71  ? 8.32206   -20.76992 10.14732  1.000 110.15720 ?  71  VAL A C   1 
ATOM   505  O  O   . VAL A 1 71  ? 7.76660   -21.86580 9.98293   1.000 107.08947 ?  71  VAL A O   1 
ATOM   506  C  CB  . VAL A 1 71  ? 8.70510   -19.96809 12.51277  1.000 121.57372 ?  71  VAL A CB  1 
ATOM   507  C  CG1 . VAL A 1 71  ? 8.53253   -21.36807 13.07535  1.000 117.87561 ?  71  VAL A CG1 1 
ATOM   508  C  CG2 . VAL A 1 71  ? 10.18137  -19.66754 12.25071  1.000 119.31716 ?  71  VAL A CG2 1 
ATOM   509  N  N   . SER A 1 72  ? 9.35100   -20.35981 9.40600   1.000 103.89407 ?  72  SER A N   1 
ATOM   510  C  CA  . SER A 1 72  ? 9.99760   -21.20351 8.41204   1.000 100.79313 ?  72  SER A CA  1 
ATOM   511  C  C   . SER A 1 72  ? 11.50249  -21.00138 8.50209   1.000 98.22578  ?  72  SER A C   1 
ATOM   512  O  O   . SER A 1 72  ? 11.96856  -19.88566 8.75241   1.000 98.32524  ?  72  SER A O   1 
ATOM   513  C  CB  . SER A 1 72  ? 9.51610   -20.87911 6.99252   1.000 95.58989  ?  72  SER A CB  1 
ATOM   514  O  OG  . SER A 1 72  ? 9.90004   -19.56563 6.63588   1.000 99.18344  ?  72  SER A OG  1 
ATOM   515  N  N   . ARG A 1 73  ? 12.25998  -22.08038 8.30079   1.000 94.59668  ?  73  ARG A N   1 
ATOM   516  C  CA  . ARG A 1 73  ? 13.71085  -22.00480 8.27695   1.000 87.72403  ?  73  ARG A CA  1 
ATOM   517  C  C   . ARG A 1 73  ? 14.27540  -22.74358 7.07498   1.000 84.49804  ?  73  ARG A C   1 
ATOM   518  O  O   . ARG A 1 73  ? 13.69683  -23.71395 6.59153   1.000 78.84670  ?  73  ARG A O   1 
ATOM   519  C  CB  . ARG A 1 73  ? 14.33840  -22.59532 9.52971   1.000 91.13665  ?  73  ARG A CB  1 
ATOM   520  C  CG  . ARG A 1 73  ? 15.85319  -22.58390 9.46577   1.000 92.56646  ?  73  ARG A CG  1 
ATOM   521  C  CD  . ARG A 1 73  ? 16.44704  -23.22055 10.67370  1.000 98.56242  ?  73  ARG A CD  1 
ATOM   522  N  NE  . ARG A 1 73  ? 15.98254  -22.56611 11.88654  1.000 101.68002 ?  73  ARG A NE  1 
ATOM   523  C  CZ  . ARG A 1 73  ? 16.57541  -22.70577 13.05951  1.000 100.88980 ?  73  ARG A CZ  1 
ATOM   524  N  NH1 . ARG A 1 73  ? 17.65891  -23.45373 13.19343  1.000 95.56214  ?  73  ARG A NH1 1 
ATOM   525  N  NH2 . ARG A 1 73  ? 16.07024  -22.08106 14.11959  1.000 105.50050 ?  73  ARG A NH2 1 
ATOM   526  N  N   . LEU A 1 74  ? 15.42976  -22.27979 6.61050   1.000 84.90179  ?  74  LEU A N   1 
ATOM   527  C  CA  . LEU A 1 74  ? 16.24817  -23.03513 5.67528   1.000 81.30669  ?  74  LEU A CA  1 
ATOM   528  C  C   . LEU A 1 74  ? 17.20211  -23.92606 6.46314   1.000 81.29388  ?  74  LEU A C   1 
ATOM   529  O  O   . LEU A 1 74  ? 17.90106  -23.45014 7.36180   1.000 85.58724  ?  74  LEU A O   1 
ATOM   530  C  CB  . LEU A 1 74  ? 17.03311  -22.09228 4.76292   1.000 81.93896  ?  74  LEU A CB  1 
ATOM   531  C  CG  . LEU A 1 74  ? 17.75510  -22.80041 3.61929   1.000 82.40380  ?  74  LEU A CG  1 
ATOM   532  C  CD1 . LEU A 1 74  ? 16.73850  -23.52053 2.76372   1.000 76.88396  ?  74  LEU A CD1 1 
ATOM   533  C  CD2 . LEU A 1 74  ? 18.55828  -21.81137 2.79244   1.000 84.00655  ?  74  LEU A CD2 1 
ATOM   534  N  N   . VAL A 1 75  ? 17.20812  -25.22132 6.14785   1.000 87.63802  ?  75  VAL A N   1 
ATOM   535  C  CA  . VAL A 1 75  ? 18.04571  -26.19568 6.83605   1.000 77.58749  ?  75  VAL A CA  1 
ATOM   536  C  C   . VAL A 1 75  ? 18.99353  -26.82626 5.82879   1.000 73.46046  ?  75  VAL A C   1 
ATOM   537  O  O   . VAL A 1 75  ? 18.58549  -27.20514 4.72462   1.000 77.54433  ?  75  VAL A O   1 
ATOM   538  C  CB  . VAL A 1 75  ? 17.20219  -27.27641 7.53835   1.000 78.40048  ?  75  VAL A CB  1 
ATOM   539  C  CG1 . VAL A 1 75  ? 18.11216  -28.21914 8.30682   1.000 83.28127  ?  75  VAL A CG1 1 
ATOM   540  C  CG2 . VAL A 1 75  ? 16.18921  -26.62881 8.44911   1.000 79.98732  ?  75  VAL A CG2 1 
ATOM   541  N  N   . ALA A 1 76  ? 20.25115  -26.95867 6.22305   1.000 74.38890  ?  76  ALA A N   1 
ATOM   542  C  CA  . ALA A 1 76  ? 21.27499  -27.60164 5.41194   1.000 80.06533  ?  76  ALA A CA  1 
ATOM   543  C  C   . ALA A 1 76  ? 21.45509  -29.04619 5.86926   1.000 77.93013  ?  76  ALA A C   1 
ATOM   544  O  O   . ALA A 1 76  ? 21.63051  -29.30991 7.06320   1.000 83.36465  ?  76  ALA A O   1 
ATOM   545  C  CB  . ALA A 1 76  ? 22.59846  -26.84138 5.51659   1.000 84.72466  ?  76  ALA A CB  1 
ATOM   546  N  N   . VAL A 1 77  ? 21.41206  -29.98222 4.92284   1.000 79.27941  ?  77  VAL A N   1 
ATOM   547  C  CA  . VAL A 1 77  ? 21.47976  -31.40097 5.23960   1.000 80.83989  ?  77  VAL A CA  1 
ATOM   548  C  C   . VAL A 1 77  ? 22.24806  -32.11999 4.14236   1.000 76.12952  ?  77  VAL A C   1 
ATOM   549  O  O   . VAL A 1 77  ? 22.56314  -31.55986 3.09556   1.000 75.03809  ?  77  VAL A O   1 
ATOM   550  C  CB  . VAL A 1 77  ? 20.08436  -32.03169 5.40992   1.000 75.54336  ?  77  VAL A CB  1 
ATOM   551  C  CG1 . VAL A 1 77  ? 19.30896  -31.31478 6.51015   1.000 71.86658  ?  77  VAL A CG1 1 
ATOM   552  C  CG2 . VAL A 1 77  ? 19.33562  -32.02225 4.06763   1.000 71.75255  ?  77  VAL A CG2 1 
ATOM   553  N  N   . LYS A 1 78  ? 22.55420  -33.38044 4.41052   1.000 76.80255  ?  78  LYS A N   1 
ATOM   554  C  CA  . LYS A 1 78  ? 23.14667  -34.27523 3.43242   1.000 77.27844  ?  78  LYS A CA  1 
ATOM   555  C  C   . LYS A 1 78  ? 22.67888  -35.67949 3.76034   1.000 78.46281  ?  78  LYS A C   1 
ATOM   556  O  O   . LYS A 1 78  ? 22.65063  -36.06782 4.93263   1.000 75.25293  ?  78  LYS A O   1 
ATOM   557  C  CB  . LYS A 1 78  ? 24.68408  -34.21766 3.43536   1.000 81.80376  ?  78  LYS A CB  1 
ATOM   558  C  CG  . LYS A 1 78  ? 25.34582  -35.38352 2.70320   1.000 82.85221  ?  78  LYS A CG  1 
ATOM   559  C  CD  . LYS A 1 78  ? 26.87504  -35.34441 2.73980   1.000 82.81575  ?  78  LYS A CD  1 
ATOM   560  C  CE  . LYS A 1 78  ? 27.43021  -36.71769 2.35718   1.000 86.64796  ?  78  LYS A CE  1 
ATOM   561  N  NZ  . LYS A 1 78  ? 28.89751  -36.75808 2.14757   1.000 94.44504  ?  78  LYS A NZ  1 
ATOM   562  N  N   . HIS A 1 79  ? 22.30930  -36.43064 2.72671   1.000 79.23740  ?  79  HIS A N   1 
ATOM   563  C  CA  . HIS A 1 79  ? 21.97907  -37.83660 2.89104   1.000 75.23584  ?  79  HIS A CA  1 
ATOM   564  C  C   . HIS A 1 79  ? 21.78650  -38.44329 1.50560   1.000 83.41069  ?  79  HIS A C   1 
ATOM   565  O  O   . HIS A 1 79  ? 21.66710  -37.73397 0.50431   1.000 83.48910  ?  79  HIS A O   1 
ATOM   566  C  CB  . HIS A 1 79  ? 20.73313  -38.01118 3.73255   1.000 76.04579  ?  79  HIS A CB  1 
ATOM   567  C  CG  . HIS A 1 79  ? 19.54133  -37.33992 3.15358   1.000 78.76793  ?  79  HIS A CG  1 
ATOM   568  N  ND1 . HIS A 1 79  ? 18.94909  -37.75915 1.97644   1.000 81.53865  ?  79  HIS A ND1 1 
ATOM   569  C  CD2 . HIS A 1 79  ? 18.83952  -36.26473 3.56821   1.000 73.77815  ?  79  HIS A CD2 1 
ATOM   570  C  CE1 . HIS A 1 79  ? 17.92550  -36.97505 1.69909   1.000 74.25085  ?  79  HIS A CE1 1 
ATOM   571  N  NE2 . HIS A 1 79  ? 17.83790  -36.06253 2.64738   1.000 73.80653  ?  79  HIS A NE2 1 
ATOM   572  N  N   . ALA A 1 80  ? 21.73514  -39.76265 1.46261   1.000 84.24115  ?  80  ALA A N   1 
ATOM   573  C  CA  . ALA A 1 80  ? 21.66822  -40.46276 0.19545   1.000 93.35436  ?  80  ALA A CA  1 
ATOM   574  C  C   . ALA A 1 80  ? 20.22850  -40.52973 -0.30411  1.000 89.31731  ?  80  ALA A C   1 
ATOM   575  O  O   . ALA A 1 80  ? 19.28069  -40.16409 0.39710   1.000 86.20907  ?  80  ALA A O   1 
ATOM   576  C  CB  . ALA A 1 80  ? 22.26882  -41.85748 0.35104   1.000 105.59820 ?  80  ALA A CB  1 
ATOM   577  N  N   . PRO A 1 81  ? 20.02760  -41.00313 -1.53135  1.000 90.40468  ?  81  PRO A N   1 
ATOM   578  C  CA  . PRO A 1 81  ? 18.64921  -41.11672 -2.03740  1.000 94.02676  ?  81  PRO A CA  1 
ATOM   579  C  C   . PRO A 1 81  ? 17.76378  -41.99181 -1.16517  1.000 88.57478  ?  81  PRO A C   1 
ATOM   580  O  O   . PRO A 1 81  ? 16.58279  -41.68002 -0.98711  1.000 87.58743  ?  81  PRO A O   1 
ATOM   581  C  CB  . PRO A 1 81  ? 18.83936  -41.71173 -3.44231  1.000 89.97743  ?  81  PRO A CB  1 
ATOM   582  C  CG  . PRO A 1 81  ? 20.26140  -41.38186 -3.80974  1.000 91.66946  ?  81  PRO A CG  1 
ATOM   583  C  CD  . PRO A 1 81  ? 21.02817  -41.43768 -2.51964  1.000 93.07510  ?  81  PRO A CD  1 
ATOM   584  N  N   . GLU A 1 82  ? 18.30139  -43.07516 -0.60339  1.000 90.45316  ?  82  GLU A N   1 
ATOM   585  C  CA  . GLU A 1 82  ? 17.48341  -43.98645 0.19193   1.000 89.22001  ?  82  GLU A CA  1 
ATOM   586  C  C   . GLU A 1 82  ? 17.11602  -43.42659 1.56360   1.000 87.86112  ?  82  GLU A C   1 
ATOM   587  O  O   . GLU A 1 82  ? 16.27279  -44.00990 2.24975   1.000 90.03761  ?  82  GLU A O   1 
ATOM   588  C  CB  . GLU A 1 82  ? 18.19999  -45.32883 0.36432   1.000 92.57514  ?  82  GLU A CB  1 
ATOM   589  C  CG  . GLU A 1 82  ? 18.62179  -45.99760 -0.93355  1.000 101.29313 ?  82  GLU A CG  1 
ATOM   590  C  CD  . GLU A 1 82  ? 19.99887  -45.55376 -1.39879  1.000 103.47336 ?  82  GLU A CD  1 
ATOM   591  O  OE1 . GLU A 1 82  ? 20.40935  -44.41993 -1.05909  1.000 97.12481  ?  82  GLU A OE1 1 
ATOM   592  O  OE2 . GLU A 1 82  ? 20.66920  -46.35084 -2.09557  1.000 114.30981 ?  82  GLU A OE2 1 
ATOM   593  N  N   . GLU A 1 83  ? 17.70580  -42.31951 1.98776   1.000 87.31981  ?  83  GLU A N   1 
ATOM   594  C  CA  . GLU A 1 83  ? 17.39563  -41.76539 3.29520   1.000 88.67543  ?  83  GLU A CA  1 
ATOM   595  C  C   . GLU A 1 83  ? 16.30805  -40.69804 3.23489   1.000 86.01047  ?  83  GLU A C   1 
ATOM   596  O  O   . GLU A 1 83  ? 16.11768  -39.96455 4.21692   1.000 75.01667  ?  83  GLU A O   1 
ATOM   597  C  CB  . GLU A 1 83  ? 18.66826  -41.20082 3.93264   1.000 89.94001  ?  83  GLU A CB  1 
ATOM   598  C  CG  . GLU A 1 83  ? 19.94002  -41.96681 3.53393   1.000 91.53803  ?  83  GLU A CG  1 
ATOM   599  C  CD  . GLU A 1 83  ? 21.08490  -41.82578 4.52664   1.000 94.23236  ?  83  GLU A CD  1 
ATOM   600  O  OE1 . GLU A 1 83  ? 21.10518  -42.57337 5.52104   1.000 92.18229  ?  83  GLU A OE1 1 
ATOM   601  O  OE2 . GLU A 1 83  ? 21.97575  -40.97691 4.31082   1.000 95.78638  ?  83  GLU A OE2 1 
ATOM   602  N  N   . ILE A 1 84  ? 15.59662  -40.58344 2.10401   1.000 69.49223  ?  84  ILE A N   1 
ATOM   603  C  CA  . ILE A 1 84  ? 14.60524  -39.52110 1.99088   1.000 75.79943  ?  84  ILE A CA  1 
ATOM   604  C  C   . ILE A 1 84  ? 13.44148  -39.77518 2.94396   1.000 73.42863  ?  84  ILE A C   1 
ATOM   605  O  O   . ILE A 1 84  ? 12.96022  -38.85066 3.61302   1.000 72.49023  ?  84  ILE A O   1 
ATOM   606  C  CB  . ILE A 1 84  ? 14.13053  -39.36177 0.52948   1.000 79.68283  ?  84  ILE A CB  1 
ATOM   607  C  CG1 . ILE A 1 84  ? 15.23342  -38.70773 -0.30669  1.000 78.00691  ?  84  ILE A CG1 1 
ATOM   608  C  CG2 . ILE A 1 84  ? 12.84297  -38.52712 0.44864   1.000 64.95228  ?  84  ILE A CG2 1 
ATOM   609  C  CD1 . ILE A 1 84  ? 14.96322  -38.69435 -1.77899  1.000 73.83759  ?  84  ILE A CD1 1 
ATOM   610  N  N   . LYS A 1 85  ? 12.98256  -41.02653 3.03466   1.000 75.40463  ?  85  LYS A N   1 
ATOM   611  C  CA  . LYS A 1 85  ? 11.84371  -41.34647 3.89786   1.000 83.24645  ?  85  LYS A CA  1 
ATOM   612  C  C   . LYS A 1 85  ? 12.15268  -41.04986 5.36601   1.000 80.03356  ?  85  LYS A C   1 
ATOM   613  O  O   . LYS A 1 85  ? 11.35471  -40.40823 6.06103   1.000 75.25238  ?  85  LYS A O   1 
ATOM   614  C  CB  . LYS A 1 85  ? 11.42478  -42.80729 3.73328   1.000 71.72972  ?  85  LYS A CB  1 
ATOM   615  C  CG  . LYS A 1 85  ? 10.00874  -43.05592 4.23656   1.000 73.39654  ?  85  LYS A CG  1 
ATOM   616  C  CD  . LYS A 1 85  ? 9.75340   -44.52266 4.57799   1.000 95.21236  ?  85  LYS A CD  1 
ATOM   617  C  CE  . LYS A 1 85  ? 9.47001   -45.38322 3.33339   1.000 96.52476  ?  85  LYS A CE  1 
ATOM   618  N  NZ  . LYS A 1 85  ? 9.04055   -46.77264 3.69258   1.000 93.77795  ?  85  LYS A NZ  1 
ATOM   619  N  N   . GLU A 1 86  ? 13.31006  -41.50313 5.85897   1.000 78.28201  ?  86  GLU A N   1 
ATOM   620  C  CA  . GLU A 1 86  ? 13.65619  -41.24659 7.25986   1.000 85.08474  ?  86  GLU A CA  1 
ATOM   621  C  C   . GLU A 1 86  ? 13.58830  -39.75559 7.55828   1.000 79.96684  ?  86  GLU A C   1 
ATOM   622  O  O   . GLU A 1 86  ? 13.01869  -39.33361 8.57554   1.000 77.40889  ?  86  GLU A O   1 
ATOM   623  C  CB  . GLU A 1 86  ? 15.05738  -41.79310 7.59664   1.000 86.76991  ?  86  GLU A CB  1 
ATOM   624  C  CG  . GLU A 1 86  ? 15.52403  -42.94532 6.69103   1.000 100.23575 ?  86  GLU A CG  1 
ATOM   625  C  CD  . GLU A 1 86  ? 16.79254  -43.65409 7.17907   1.000 105.30722 ?  86  GLU A CD  1 
ATOM   626  O  OE1 . GLU A 1 86  ? 17.57358  -43.01608 7.95361   1.000 90.76334  ?  86  GLU A OE1 1 
ATOM   627  O  OE2 . GLU A 1 86  ? 16.97634  -44.85013 6.77751   1.000 98.84389  ?  86  GLU A OE2 1 
ATOM   628  N  N   . GLU A 1 87  ? 14.16388  -38.94381 6.66029   1.000 76.44405  ?  87  GLU A N   1 
ATOM   629  C  CA  . GLU A 1 87  ? 14.22326  -37.50368 6.87132   1.000 72.79115  ?  87  GLU A CA  1 
ATOM   630  C  C   . GLU A 1 87  ? 12.83301  -36.88050 6.85202   1.000 75.24914  ?  87  GLU A C   1 
ATOM   631  O  O   . GLU A 1 87  ? 12.46016  -36.14470 7.77216   1.000 81.20675  ?  87  GLU A O   1 
ATOM   632  C  CB  . GLU A 1 87  ? 15.11673  -36.85686 5.81731   1.000 76.50107  ?  87  GLU A CB  1 
ATOM   633  C  CG  . GLU A 1 87  ? 15.21487  -35.34846 5.95324   1.000 69.44168  ?  87  GLU A CG  1 
ATOM   634  C  CD  . GLU A 1 87  ? 15.77739  -34.67176 4.70359   1.000 77.40199  ?  87  GLU A CD  1 
ATOM   635  O  OE1 . GLU A 1 87  ? 15.11611  -34.73468 3.66820   1.000 63.18627  ?  87  GLU A OE1 1 
ATOM   636  O  OE2 . GLU A 1 87  ? 16.88855  -34.07789 4.73995   1.000 78.79662  ?  87  GLU A OE2 1 
ATOM   637  N  N   . LEU A 1 88  ? 12.04288  -37.17252 5.82033   1.000 70.42930  ?  88  LEU A N   1 
ATOM   638  C  CA  . LEU A 1 88  ? 10.71131  -36.57547 5.72627   1.000 80.41975  ?  88  LEU A CA  1 
ATOM   639  C  C   . LEU A 1 88  ? 9.84065   -36.98550 6.91466   1.000 79.57916  ?  88  LEU A C   1 
ATOM   640  O  O   . LEU A 1 88  ? 9.24724   -36.13372 7.58627   1.000 83.06577  ?  88  LEU A O   1 
ATOM   641  C  CB  . LEU A 1 88  ? 10.04683  -36.95052 4.38583   1.000 75.16673  ?  88  LEU A CB  1 
ATOM   642  C  CG  . LEU A 1 88  ? 10.69642  -36.40703 3.09503   1.000 65.50130  ?  88  LEU A CG  1 
ATOM   643  C  CD1 . LEU A 1 88  ? 9.87174   -36.72474 1.83692   1.000 59.64740  ?  88  LEU A CD1 1 
ATOM   644  C  CD2 . LEU A 1 88  ? 10.95687  -34.90979 3.19077   1.000 59.11712  ?  88  LEU A CD2 1 
ATOM   645  N  N   . LEU A 1 89  ? 9.76025   -38.28865 7.20115   1.000 87.40443  ?  89  LEU A N   1 
ATOM   646  C  CA  . LEU A 1 89  ? 8.97934   -38.73552 8.35422   1.000 90.06252  ?  89  LEU A CA  1 
ATOM   647  C  C   . LEU A 1 89  ? 9.46985   -38.08041 9.63906   1.000 91.41126  ?  89  LEU A C   1 
ATOM   648  O  O   . LEU A 1 89  ? 8.67930   -37.80177 10.55077  1.000 92.53478  ?  89  LEU A O   1 
ATOM   649  C  CB  . LEU A 1 89  ? 9.04683   -40.25776 8.48189   1.000 96.05179  ?  89  LEU A CB  1 
ATOM   650  C  CG  . LEU A 1 89  ? 8.12393   -41.08571 7.58845   1.000 96.89513  ?  89  LEU A CG  1 
ATOM   651  C  CD1 . LEU A 1 89  ? 8.40495   -42.58075 7.77677   1.000 96.47059  ?  89  LEU A CD1 1 
ATOM   652  C  CD2 . LEU A 1 89  ? 6.67586   -40.76654 7.91758   1.000 99.07828  ?  89  LEU A CD2 1 
ATOM   653  N  N   . CYS A 1 90  ? 10.77175  -37.82794 9.71851   1.000 86.65539  ?  90  CYS A N   1 
ATOM   654  C  CA  . CYS A 1 90  ? 11.34444  -37.13722 10.86216  1.000 87.77385  ?  90  CYS A CA  1 
ATOM   655  C  C   . CYS A 1 90  ? 10.72950  -35.74984 11.03564  1.000 87.78384  ?  90  CYS A C   1 
ATOM   656  O  O   . CYS A 1 90  ? 10.30420  -35.37356 12.13292  1.000 86.19240  ?  90  CYS A O   1 
ATOM   657  C  CB  . CYS A 1 90  ? 12.85613  -37.06250 10.66324  1.000 88.00123  ?  90  CYS A CB  1 
ATOM   658  S  SG  . CYS A 1 90  ? 13.73656  -36.33913 11.99123  1.000 97.06765  ?  90  CYS A SG  1 
ATOM   659  N  N   . VAL A 1 91  ? 10.66456  -34.97629 9.95365   1.000 86.60050  ?  91  VAL A N   1 
ATOM   660  C  CA  . VAL A 1 91  ? 10.19728  -33.59582 10.05059  1.000 85.48952  ?  91  VAL A CA  1 
ATOM   661  C  C   . VAL A 1 91  ? 8.71434   -33.55404 10.36964  1.000 87.34509  ?  91  VAL A C   1 
ATOM   662  O  O   . VAL A 1 91  ? 8.26062   -32.78554 11.22507  1.000 88.22063  ?  91  VAL A O   1 
ATOM   663  C  CB  . VAL A 1 91  ? 10.48986  -32.84197 8.74401   1.000 75.12410  ?  91  VAL A CB  1 
ATOM   664  C  CG1 . VAL A 1 91  ? 9.68847   -31.55065 8.68859   1.000 79.62275  ?  91  VAL A CG1 1 
ATOM   665  C  CG2 . VAL A 1 91  ? 11.96928  -32.58045 8.61131   1.000 71.77753  ?  91  VAL A CG2 1 
ATOM   666  N  N   . VAL A 1 92  ? 7.93309   -34.35534 9.65534   1.000 83.52527  ?  92  VAL A N   1 
ATOM   667  C  CA  . VAL A 1 92  ? 6.48962   -34.27202 9.79005   1.000 83.70290  ?  92  VAL A CA  1 
ATOM   668  C  C   . VAL A 1 92  ? 6.05720   -34.77661 11.15910  1.000 92.11097  ?  92  VAL A C   1 
ATOM   669  O  O   . VAL A 1 92  ? 5.17189   -34.18981 11.79275  1.000 92.91521  ?  92  VAL A O   1 
ATOM   670  C  CB  . VAL A 1 92  ? 5.82248   -35.04138 8.63723   1.000 87.14832  ?  92  VAL A CB  1 
ATOM   671  C  CG1 . VAL A 1 92  ? 6.05812   -36.54220 8.79419   1.000 91.33216  ?  92  VAL A CG1 1 
ATOM   672  C  CG2 . VAL A 1 92  ? 4.34834   -34.71971 8.54718   1.000 88.32982  ?  92  VAL A CG2 1 
ATOM   673  N  N   . ARG A 1 93  ? 6.69661   -35.85218 11.65210  1.000 91.51248  ?  93  ARG A N   1 
ATOM   674  C  CA  . ARG A 1 93  ? 6.36317   -36.40163 12.96603  1.000 99.17352  ?  93  ARG A CA  1 
ATOM   675  C  C   . ARG A 1 93  ? 6.64831   -35.41403 14.08564  1.000 95.82406  ?  93  ARG A C   1 
ATOM   676  O  O   . ARG A 1 93  ? 6.07171   -35.53718 15.16610  1.000 93.19921  ?  93  ARG A O   1 
ATOM   677  C  CB  . ARG A 1 93  ? 7.11422   -37.71767 13.21773  1.000 90.84739  ?  93  ARG A CB  1 
ATOM   678  C  CG  . ARG A 1 93  ? 6.52690   -38.85335 12.42506  1.000 96.76593  ?  93  ARG A CG  1 
ATOM   679  C  CD  . ARG A 1 93  ? 7.31957   -40.14110 12.48320  1.000 105.32604 ?  93  ARG A CD  1 
ATOM   680  N  NE  . ARG A 1 93  ? 6.53074   -41.21883 11.89106  1.000 103.92430 ?  93  ARG A NE  1 
ATOM   681  C  CZ  . ARG A 1 93  ? 6.95752   -42.45725 11.67671  1.000 101.97603 ?  93  ARG A CZ  1 
ATOM   682  N  NH1 . ARG A 1 93  ? 8.20161   -42.81938 11.95004  1.000 97.61014  ?  93  ARG A NH1 1 
ATOM   683  N  NH2 . ARG A 1 93  ? 6.11377   -43.35370 11.16952  1.000 98.90055  ?  93  ARG A NH2 1 
ATOM   684  N  N   . ASN A 1 94  ? 7.49916   -34.42194 13.84893  1.000 95.15613  ?  94  ASN A N   1 
ATOM   685  C  CA  . ASN A 1 94  ? 7.67304   -33.33545 14.79658  1.000 95.74130  ?  94  ASN A CA  1 
ATOM   686  C  C   . ASN A 1 94  ? 6.90281   -32.08834 14.37537  1.000 96.16543  ?  94  ASN A C   1 
ATOM   687  O  O   . ASN A 1 94  ? 7.27317   -30.97038 14.75704  1.000 96.02030  ?  94  ASN A O   1 
ATOM   688  C  CB  . ASN A 1 94  ? 9.16072   -33.04644 14.99285  1.000 96.93976  ?  94  ASN A CB  1 
ATOM   689  C  CG  . ASN A 1 94  ? 9.84640   -34.11107 15.85093  1.000 103.27247 ?  94  ASN A CG  1 
ATOM   690  O  OD1 . ASN A 1 94  ? 10.57094  -34.97532 15.34425  1.000 95.00461  ?  94  ASN A OD1 1 
ATOM   691  N  ND2 . ASN A 1 94  ? 9.60653   -34.05468 17.16163  1.000 109.43121 ?  94  ASN A ND2 1 
ATOM   692  N  N   . GLY A 1 95  ? 5.83521   -32.26572 13.60118  1.000 92.10787  ?  95  GLY A N   1 
ATOM   693  C  CA  . GLY A 1 95  ? 4.93874   -31.17318 13.27395  1.000 89.72392  ?  95  GLY A CA  1 
ATOM   694  C  C   . GLY A 1 95  ? 5.54358   -30.09473 12.40446  1.000 92.70563  ?  95  GLY A C   1 
ATOM   695  O  O   . GLY A 1 95  ? 5.23100   -28.90952 12.58400  1.000 94.30528  ?  95  GLY A O   1 
ATOM   696  N  N   . GLY A 1 96  ? 6.42330   -30.47103 11.47942  1.000 88.17263  ?  96  GLY A N   1 
ATOM   697  C  CA  . GLY A 1 96  ? 6.89390   -29.57772 10.44936  1.000 88.26347  ?  96  GLY A CA  1 
ATOM   698  C  C   . GLY A 1 96  ? 6.29535   -29.96722 9.10847   1.000 82.97253  ?  96  GLY A C   1 
ATOM   699  O  O   . GLY A 1 96  ? 5.62071   -30.98361 8.97644   1.000 83.75601  ?  96  GLY A O   1 
ATOM   700  N  N   . ARG A 1 97  ? 6.54765   -29.11581 8.11306   1.000 79.46076  ?  97  ARG A N   1 
ATOM   701  C  CA  . ARG A 1 97  ? 6.16218   -29.36717 6.72397   1.000 77.26000  ?  97  ARG A CA  1 
ATOM   702  C  C   . ARG A 1 97  ? 7.40321   -29.17466 5.87408   1.000 75.84026  ?  97  ARG A C   1 
ATOM   703  O  O   . ARG A 1 97  ? 8.12065   -28.18224 6.05693   1.000 78.56245  ?  97  ARG A O   1 
ATOM   704  C  CB  . ARG A 1 97  ? 5.03563   -28.42202 6.26277   1.000 80.94813  ?  97  ARG A CB  1 
ATOM   705  C  CG  . ARG A 1 97  ? 4.90875   -28.22940 4.73366   1.000 78.81174  ?  97  ARG A CG  1 
ATOM   706  C  CD  . ARG A 1 97  ? 3.53833   -27.64513 4.31324   1.000 78.31121  ?  97  ARG A CD  1 
ATOM   707  N  NE  . ARG A 1 97  ? 3.20867   -26.41517 5.02540   1.000 88.68682  ?  97  ARG A NE  1 
ATOM   708  C  CZ  . ARG A 1 97  ? 2.21792   -26.28938 5.90300   1.000 103.03277 ?  97  ARG A CZ  1 
ATOM   709  N  NH1 . ARG A 1 97  ? 1.34874   -27.26707 6.10937   1.000 105.75981 ?  97  ARG A NH1 1 
ATOM   710  N  NH2 . ARG A 1 97  ? 2.09835   -25.15455 6.59544   1.000 97.97570  ?  97  ARG A NH2 1 
ATOM   711  N  N   . ILE A 1 98  ? 7.69824   -30.13098 4.99338   1.000 68.75559  ?  98  ILE A N   1 
ATOM   712  C  CA  . ILE A 1 98  ? 8.84764   -29.98799 4.10387   1.000 73.08760  ?  98  ILE A CA  1 
ATOM   713  C  C   . ILE A 1 98  ? 8.36341   -29.26229 2.86443   1.000 69.92187  ?  98  ILE A C   1 
ATOM   714  O  O   . ILE A 1 98  ? 7.71695   -29.86292 2.00511   1.000 66.97458  ?  98  ILE A O   1 
ATOM   715  C  CB  . ILE A 1 98  ? 9.50263   -31.32004 3.72812   1.000 68.16434  ?  98  ILE A CB  1 
ATOM   716  C  CG1 . ILE A 1 98  ? 9.80835   -32.14120 4.96659   1.000 66.93763  ?  98  ILE A CG1 1 
ATOM   717  C  CG2 . ILE A 1 98  ? 10.78649  -31.04006 2.89451   1.000 55.71287  ?  98  ILE A CG2 1 
ATOM   718  C  CD1 . ILE A 1 98  ? 8.59869   -32.89891 5.50869   1.000 74.06967  ?  98  ILE A CD1 1 
ATOM   719  N  N   . VAL A 1 99  ? 8.72267   -27.98417 2.77220   1.000 69.87304  ?  99  VAL A N   1 
ATOM   720  C  CA  . VAL A 1 99  ? 8.26002   -27.11865 1.69423   1.000 69.36826  ?  99  VAL A CA  1 
ATOM   721  C  C   . VAL A 1 99  ? 8.91387   -27.48672 0.37235   1.000 68.54506  ?  99  VAL A C   1 
ATOM   722  O  O   . VAL A 1 99  ? 8.23278   -27.58582 -0.65931  1.000 70.44715  ?  99  VAL A O   1 
ATOM   723  C  CB  . VAL A 1 99  ? 8.52906   -25.64688 2.05349   1.000 70.88762  ?  99  VAL A CB  1 
ATOM   724  C  CG1 . VAL A 1 99  ? 8.05409   -24.72561 0.93645   1.000 67.81685  ?  99  VAL A CG1 1 
ATOM   725  C  CG2 . VAL A 1 99  ? 7.83460   -25.30288 3.34401   1.000 75.08415  ?  99  VAL A CG2 1 
ATOM   726  N  N   . ASP A 1 100 ? 10.23519  -27.64777 0.35414   1.000 66.56318  ?  100 ASP A N   1 
ATOM   727  C  CA  . ASP A 1 100 ? 10.90169  -27.88335 -0.92383  1.000 67.62726  ?  100 ASP A CA  1 
ATOM   728  C  C   . ASP A 1 100 ? 12.31107  -28.40095 -0.68060  1.000 65.64872  ?  100 ASP A C   1 
ATOM   729  O  O   . ASP A 1 100 ? 12.73869  -28.61172 0.45583   1.000 63.01661  ?  100 ASP A O   1 
ATOM   730  C  CB  . ASP A 1 100 ? 10.92659  -26.61844 -1.77843  1.000 68.35591  ?  100 ASP A CB  1 
ATOM   731  C  CG  . ASP A 1 100 ? 11.77652  -25.51646 -1.17446  1.000 69.81073  ?  100 ASP A CG  1 
ATOM   732  O  OD1 . ASP A 1 100 ? 12.61694  -25.79221 -0.29066  1.000 68.20654  ?  100 ASP A OD1 1 
ATOM   733  O  OD2 . ASP A 1 100 ? 11.59179  -24.35529 -1.59444  1.000 74.20496  ?  100 ASP A OD2 1 
ATOM   734  N  N   . VAL A 1 101 ? 13.01913  -28.62973 -1.77519  1.000 59.80620  ?  101 VAL A N   1 
ATOM   735  C  CA  . VAL A 1 101 ? 14.42228  -28.98831 -1.74142  1.000 64.87394  ?  101 VAL A CA  1 
ATOM   736  C  C   . VAL A 1 101 ? 15.13778  -28.05506 -2.69059  1.000 69.08814  ?  101 VAL A C   1 
ATOM   737  O  O   . VAL A 1 101 ? 14.63613  -27.76669 -3.77922  1.000 66.27021  ?  101 VAL A O   1 
ATOM   738  C  CB  . VAL A 1 101 ? 14.67960  -30.44317 -2.15724  1.000 64.09381  ?  101 VAL A CB  1 
ATOM   739  C  CG1 . VAL A 1 101 ? 14.09494  -30.70332 -3.51884  1.000 56.16509  ?  101 VAL A CG1 1 
ATOM   740  C  CG2 . VAL A 1 101 ? 16.18418  -30.68385 -2.18371  1.000 68.67927  ?  101 VAL A CG2 1 
ATOM   741  N  N   . ILE A 1 102 ? 16.31416  -27.59916 -2.28797  1.000 69.49147  ?  102 ILE A N   1 
ATOM   742  C  CA  . ILE A 1 102 ? 17.11122  -26.67035 -3.06457  1.000 69.02361  ?  102 ILE A CA  1 
ATOM   743  C  C   . ILE A 1 102 ? 18.51578  -27.22793 -3.14188  1.000 73.34023  ?  102 ILE A C   1 
ATOM   744  O  O   . ILE A 1 102 ? 19.15991  -27.45321 -2.11124  1.000 70.38297  ?  102 ILE A O   1 
ATOM   745  C  CB  . ILE A 1 102 ? 17.13977  -25.26929 -2.44361  1.000 74.25792  ?  102 ILE A CB  1 
ATOM   746  C  CG1 . ILE A 1 102 ? 15.80607  -24.56675 -2.63549  1.000 68.45731  ?  102 ILE A CG1 1 
ATOM   747  C  CG2 . ILE A 1 102 ? 18.25463  -24.45047 -3.05803  1.000 69.71664  ?  102 ILE A CG2 1 
ATOM   748  C  CD1 . ILE A 1 102 ? 15.77862  -23.24388 -1.96655  1.000 67.57220  ?  102 ILE A CD1 1 
ATOM   749  N  N   . VAL A 1 103 ? 18.98927  -27.45560 -4.34430  1.000 68.78187  ?  103 VAL A N   1 
ATOM   750  C  CA  . VAL A 1 103 ? 20.36575  -27.85208 -4.55461  1.000 71.96092  ?  103 VAL A CA  1 
ATOM   751  C  C   . VAL A 1 103 ? 21.14084  -26.68061 -5.13801  1.000 69.99296  ?  103 VAL A C   1 
ATOM   752  O  O   . VAL A 1 103 ? 20.62473  -25.92542 -5.97269  1.000 73.16866  ?  103 VAL A O   1 
ATOM   753  C  CB  . VAL A 1 103 ? 20.41134  -29.08247 -5.46549  1.000 73.81282  ?  103 VAL A CB  1 
ATOM   754  C  CG1 . VAL A 1 103 ? 21.79742  -29.25098 -6.04402  1.000 79.38607  ?  103 VAL A CG1 1 
ATOM   755  C  CG2 . VAL A 1 103 ? 20.00684  -30.28727 -4.65537  1.000 77.44942  ?  103 VAL A CG2 1 
ATOM   756  N  N   . GLU A 1 104 ? 22.37234  -26.51378 -4.69706  1.000 69.43725  ?  104 GLU A N   1 
ATOM   757  C  CA  A GLU A 1 104 ? 23.24266  -25.45897 -5.21252  0.552 72.22043  ?  104 GLU A CA  1 
ATOM   758  C  CA  B GLU A 1 104 ? 23.25045  -25.46374 -5.19985  0.448 72.31511  ?  104 GLU A CA  1 
ATOM   759  C  C   . GLU A 1 104 ? 24.09874  -26.10303 -6.29624  1.000 67.22260  ?  104 GLU A C   1 
ATOM   760  O  O   . GLU A 1 104 ? 25.10379  -26.75564 -6.01398  1.000 69.69632  ?  104 GLU A O   1 
ATOM   761  C  CB  A GLU A 1 104 ? 24.08157  -24.82303 -4.10247  0.552 72.74954  ?  104 GLU A CB  1 
ATOM   762  C  CB  B GLU A 1 104 ? 24.08949  -24.87018 -4.06499  0.448 72.55819  ?  104 GLU A CB  1 
ATOM   763  C  CG  A GLU A 1 104 ? 23.42175  -23.62704 -3.39551  0.552 73.11813  ?  104 GLU A CG  1 
ATOM   764  C  CG  B GLU A 1 104 ? 23.25428  -24.28483 -2.91223  0.448 72.83479  ?  104 GLU A CG  1 
ATOM   765  C  CD  A GLU A 1 104 ? 23.39308  -22.35433 -4.24374  0.552 75.98368  ?  104 GLU A CD  1 
ATOM   766  C  CD  B GLU A 1 104 ? 24.07775  -23.49687 -1.90733  0.448 76.37675  ?  104 GLU A CD  1 
ATOM   767  O  OE1 A GLU A 1 104 ? 23.38447  -22.45175 -5.49152  0.552 72.54069  ?  104 GLU A OE1 1 
ATOM   768  O  OE1 B GLU A 1 104 ? 25.25151  -23.85237 -1.67350  0.448 80.10908  ?  104 GLU A OE1 1 
ATOM   769  O  OE2 A GLU A 1 104 ? 23.38610  -21.24790 -3.65208  0.552 78.61450  ?  104 GLU A OE2 1 
ATOM   770  O  OE2 B GLU A 1 104 ? 23.55082  -22.50996 -1.35335  0.448 75.73419  ?  104 GLU A OE2 1 
ATOM   771  N  N   . HIS A 1 105 ? 23.68730  -25.94609 -7.51389  1.000 68.91969  ?  105 HIS A N   1 
ATOM   772  C  CA  . HIS A 1 105 ? 24.37637  -26.64244 -8.59175  1.000 70.55510  ?  105 HIS A CA  1 
ATOM   773  C  C   . HIS A 1 105 ? 25.56659  -25.81182 -9.06708  1.000 65.26791  ?  105 HIS A C   1 
ATOM   774  O  O   . HIS A 1 105 ? 25.39982  -24.62899 -9.39754  1.000 65.33204  ?  105 HIS A O   1 
ATOM   775  C  CB  . HIS A 1 105 ? 23.41141  -26.91561 -9.73885  1.000 65.47666  ?  105 HIS A CB  1 
ATOM   776  C  CG  . HIS A 1 105 ? 23.97871  -27.77744 -10.82523 1.000 70.72684  ?  105 HIS A CG  1 
ATOM   777  N  ND1 . HIS A 1 105 ? 24.93678  -27.32346 -11.70919 1.000 76.79034  ?  105 HIS A ND1 1 
ATOM   778  C  CD2 . HIS A 1 105 ? 23.71871  -29.05904 -11.17596 1.000 67.54531  ?  105 HIS A CD2 1 
ATOM   779  C  CE1 . HIS A 1 105 ? 25.23352  -28.29047 -12.56143 1.000 73.06467  ?  105 HIS A CE1 1 
ATOM   780  N  NE2 . HIS A 1 105 ? 24.52160  -29.35554 -12.24717 1.000 69.77472  ?  105 HIS A NE2 1 
ATOM   781  N  N   . PRO A 1 106 ? 26.77392  -26.37888 -9.10314  1.000 65.52584  ?  106 PRO A N   1 
ATOM   782  C  CA  . PRO A 1 106 ? 27.94849  -25.56676 -9.46604  1.000 63.25062  ?  106 PRO A CA  1 
ATOM   783  C  C   . PRO A 1 106 ? 27.81334  -24.86990 -10.81264 1.000 68.61053  ?  106 PRO A C   1 
ATOM   784  O  O   . PRO A 1 106 ? 28.26236  -23.72481 -10.95798 1.000 60.88887  ?  106 PRO A O   1 
ATOM   785  C  CB  . PRO A 1 106 ? 29.09182  -26.59435 -9.47387  1.000 62.68638  ?  106 PRO A CB  1 
ATOM   786  C  CG  . PRO A 1 106 ? 28.57907  -27.76304 -8.70971  1.000 70.03428  ?  106 PRO A CG  1 
ATOM   787  C  CD  . PRO A 1 106 ? 27.10745  -27.80462 -8.97659  1.000 70.62041  ?  106 PRO A CD  1 
ATOM   788  N  N   . VAL A 1 107 ? 27.22106  -25.52928 -11.81051 1.000 69.53750  ?  107 VAL A N   1 
ATOM   789  C  CA  . VAL A 1 107 ? 27.01121  -24.88805 -13.10608 1.000 63.46712  ?  107 VAL A CA  1 
ATOM   790  C  C   . VAL A 1 107 ? 25.77395  -24.00961 -13.07723 1.000 58.85427  ?  107 VAL A C   1 
ATOM   791  O  O   . VAL A 1 107 ? 25.83637  -22.81003 -13.34743 1.000 58.79409  ?  107 VAL A O   1 
ATOM   792  C  CB  . VAL A 1 107 ? 26.89615  -25.94226 -14.21875 1.000 71.06989  ?  107 VAL A CB  1 
ATOM   793  C  CG1 . VAL A 1 107 ? 26.24979  -25.31514 -15.45741 1.000 69.35579  ?  107 VAL A CG1 1 
ATOM   794  C  CG2 . VAL A 1 107 ? 28.25114  -26.51683 -14.55011 1.000 69.29418  ?  107 VAL A CG2 1 
ATOM   795  N  N   . TYR A 1 108 ? 24.63143  -24.59864 -12.75480 1.000 61.11341  ?  108 TYR A N   1 
ATOM   796  C  CA  . TYR A 1 108 ? 23.34366  -23.92917 -12.89868 1.000 64.22489  ?  108 TYR A CA  1 
ATOM   797  C  C   . TYR A 1 108 ? 22.96384  -23.05293 -11.70850 1.000 65.32998  ?  108 TYR A C   1 
ATOM   798  O  O   . TYR A 1 108 ? 21.98677  -22.29523 -11.79343 1.000 58.58273  ?  108 TYR A O   1 
ATOM   799  C  CB  . TYR A 1 108 ? 22.26352  -24.97138 -13.12214 1.000 63.97610  ?  108 TYR A CB  1 
ATOM   800  C  CG  . TYR A 1 108 ? 22.44620  -25.71471 -14.40264 1.000 68.62348  ?  108 TYR A CG  1 
ATOM   801  C  CD1 . TYR A 1 108 ? 22.72958  -25.03289 -15.59521 1.000 63.63726  ?  108 TYR A CD1 1 
ATOM   802  C  CD2 . TYR A 1 108 ? 22.33797  -27.09139 -14.44094 1.000 66.58837  ?  108 TYR A CD2 1 
ATOM   803  C  CE1 . TYR A 1 108 ? 22.87518  -25.72665 -16.78149 1.000 64.32068  ?  108 TYR A CE1 1 
ATOM   804  C  CE2 . TYR A 1 108 ? 22.49038  -27.78050 -15.62660 1.000 59.17219  ?  108 TYR A CE2 1 
ATOM   805  C  CZ  . TYR A 1 108 ? 22.76621  -27.09632 -16.77375 1.000 60.46096  ?  108 TYR A CZ  1 
ATOM   806  O  OH  . TYR A 1 108 ? 22.92766  -27.79958 -17.92919 1.000 70.04321  ?  108 TYR A OH  1 
ATOM   807  N  N   . GLY A 1 109 ? 23.69437  -23.13316 -10.61092 1.000 63.11267  ?  109 GLY A N   1 
ATOM   808  C  CA  . GLY A 1 109 ? 23.27132  -22.40726 -9.43481  1.000 64.24635  ?  109 GLY A CA  1 
ATOM   809  C  C   . GLY A 1 109 ? 22.13584  -23.10739 -8.72223  1.000 69.67861  ?  109 GLY A C   1 
ATOM   810  O  O   . GLY A 1 109 ? 22.13712  -24.33099 -8.54976  1.000 72.24739  ?  109 GLY A O   1 
ATOM   811  N  N   . GLU A 1 110 ? 21.14151  -22.35055 -8.31495  1.000 66.04604  ?  110 GLU A N   1 
ATOM   812  C  CA  . GLU A 1 110 ? 20.21379  -22.83140 -7.30969  1.000 67.02273  ?  110 GLU A CA  1 
ATOM   813  C  C   . GLU A 1 110 ? 18.99346  -23.43066 -7.99397  1.000 74.06258  ?  110 GLU A C   1 
ATOM   814  O  O   . GLU A 1 110 ? 18.27889  -22.74200 -8.73126  1.000 75.72808  ?  110 GLU A O   1 
ATOM   815  C  CB  . GLU A 1 110 ? 19.89141  -21.69190 -6.34919  1.000 72.27473  ?  110 GLU A CB  1 
ATOM   816  C  CG  . GLU A 1 110 ? 18.47417  -21.46647 -6.01941  1.000 80.04085  ?  110 GLU A CG  1 
ATOM   817  C  CD  . GLU A 1 110 ? 18.35405  -20.78638 -4.67462  1.000 78.92896  ?  110 GLU A CD  1 
ATOM   818  O  OE1 . GLU A 1 110 ? 19.40670  -20.40774 -4.11033  1.000 81.54269  ?  110 GLU A OE1 1 
ATOM   819  O  OE2 . GLU A 1 110 ? 17.21841  -20.65481 -4.17124  1.000 88.50136  ?  110 GLU A OE2 1 
ATOM   820  N  N   . ILE A 1 111 ? 18.80159  -24.73457 -7.78590  1.000 73.73756  ?  111 ILE A N   1 
ATOM   821  C  CA  . ILE A 1 111 ? 17.77444  -25.53467 -8.43967  1.000 65.88337  ?  111 ILE A CA  1 
ATOM   822  C  C   . ILE A 1 111 ? 16.80356  -26.03232 -7.37434  1.000 71.96488  ?  111 ILE A C   1 
ATOM   823  O  O   . ILE A 1 111 ? 17.21990  -26.65482 -6.38748  1.000 71.61925  ?  111 ILE A O   1 
ATOM   824  C  CB  . ILE A 1 111 ? 18.38976  -26.72701 -9.18476  1.000 66.98103  ?  111 ILE A CB  1 
ATOM   825  C  CG1 . ILE A 1 111 ? 19.10727  -26.25922 -10.44238 1.000 70.20914  ?  111 ILE A CG1 1 
ATOM   826  C  CG2 . ILE A 1 111 ? 17.30807  -27.79340 -9.46273  1.000 66.19936  ?  111 ILE A CG2 1 
ATOM   827  C  CD1 . ILE A 1 111 ? 19.35279  -27.36827 -11.43033 1.000 71.12798  ?  111 ILE A CD1 1 
ATOM   828  N  N   . ARG A 1 112 ? 15.51660  -25.77854 -7.58043  1.000 65.66250  ?  112 ARG A N   1 
ATOM   829  C  CA  . ARG A 1 112 ? 14.50750  -25.94489 -6.54831  1.000 69.27922  ?  112 ARG A CA  1 
ATOM   830  C  C   . ARG A 1 112 ? 13.48500  -26.99108 -6.97418  1.000 67.76222  ?  112 ARG A C   1 
ATOM   831  O  O   . ARG A 1 112 ? 13.07380  -27.02379 -8.13515  1.000 65.51678  ?  112 ARG A O   1 
ATOM   832  C  CB  . ARG A 1 112 ? 13.79452  -24.61398 -6.25454  1.000 59.68605  ?  112 ARG A CB  1 
ATOM   833  C  CG  . ARG A 1 112 ? 12.79452  -24.71364 -5.11457  1.000 69.76443  ?  112 ARG A CG  1 
ATOM   834  C  CD  . ARG A 1 112 ? 12.17007  -23.37583 -4.80257  1.000 70.18590  ?  112 ARG A CD  1 
ATOM   835  N  NE  . ARG A 1 112 ? 11.06116  -23.48804 -3.86245  1.000 70.07405  ?  112 ARG A NE  1 
ATOM   836  C  CZ  . ARG A 1 112 ? 9.80831   -23.15123 -4.13928  1.000 67.93482  ?  112 ARG A CZ  1 
ATOM   837  N  NH1 . ARG A 1 112 ? 9.46478   -22.68244 -5.32672  1.000 79.18678  ?  112 ARG A NH1 1 
ATOM   838  N  NH2 . ARG A 1 112 ? 8.88159   -23.26073 -3.19137  1.000 75.14020  ?  112 ARG A NH2 1 
ATOM   839  N  N   . GLY A 1 113 ? 13.07724  -27.83564 -6.02451  1.000 63.99119  ?  113 GLY A N   1 
ATOM   840  C  CA  . GLY A 1 113 ? 12.01064  -28.80308 -6.23909  1.000 64.67361  ?  113 GLY A CA  1 
ATOM   841  C  C   . GLY A 1 113 ? 10.93006  -28.66716 -5.18283  1.000 59.12759  ?  113 GLY A C   1 
ATOM   842  O  O   . GLY A 1 113 ? 11.23185  -28.53538 -3.99764  1.000 66.23478  ?  113 GLY A O   1 
ATOM   843  N  N   . ILE A 1 114 ? 9.67546   -28.64829 -5.61479  1.000 59.74376  ?  114 ILE A N   1 
ATOM   844  C  CA  . ILE A 1 114 ? 8.52554   -28.53650 -4.72457  1.000 64.86799  ?  114 ILE A CA  1 
ATOM   845  C  C   . ILE A 1 114 ? 8.30210   -29.88326 -4.05936  1.000 64.45181  ?  114 ILE A C   1 
ATOM   846  O  O   . ILE A 1 114 ? 8.33512   -30.92617 -4.72995  1.000 57.22241  ?  114 ILE A O   1 
ATOM   847  C  CB  . ILE A 1 114 ? 7.26863   -28.11188 -5.50938  1.000 72.59659  ?  114 ILE A CB  1 
ATOM   848  C  CG1 . ILE A 1 114 ? 7.50265   -26.78169 -6.22598  1.000 70.89905  ?  114 ILE A CG1 1 
ATOM   849  C  CG2 . ILE A 1 114 ? 6.04974   -28.05713 -4.59457  1.000 57.20043  ?  114 ILE A CG2 1 
ATOM   850  C  CD1 . ILE A 1 114 ? 7.79125   -25.65267 -5.27327  1.000 69.40525  ?  114 ILE A CD1 1 
ATOM   851  N  N   . ILE A 1 115 ? 8.07553   -29.85966 -2.74369  1.000 63.92293  ?  115 ILE A N   1 
ATOM   852  C  CA  . ILE A 1 115 ? 7.82828   -31.06391 -1.95495  1.000 60.73509  ?  115 ILE A CA  1 
ATOM   853  C  C   . ILE A 1 115 ? 6.47010   -30.94720 -1.26262  1.000 64.40386  ?  115 ILE A C   1 
ATOM   854  O  O   . ILE A 1 115 ? 5.59699   -31.79961 -1.46620  1.000 59.47170  ?  115 ILE A O   1 
ATOM   855  C  CB  . ILE A 1 115 ? 8.97431   -31.30526 -0.95783  1.000 64.37527  ?  115 ILE A CB  1 
ATOM   856  C  CG1 . ILE A 1 115 ? 10.27638  -31.53219 -1.72694  1.000 63.09716  ?  115 ILE A CG1 1 
ATOM   857  C  CG2 . ILE A 1 115 ? 8.69581   -32.48626 -0.06847  1.000 64.36898  ?  115 ILE A CG2 1 
ATOM   858  C  CD1 . ILE A 1 115 ? 11.48415  -31.90197 -0.82859  1.000 52.14888  ?  115 ILE A CD1 1 
ATOM   859  N  N   . ASP A 1 116 ? 6.25574   -29.88651 -0.47357  1.000 56.98459  ?  116 ASP A N   1 
ATOM   860  C  CA  . ASP A 1 116 ? 4.97921   -29.66176 0.23536   1.000 65.77088  ?  116 ASP A CA  1 
ATOM   861  C  C   . ASP A 1 116 ? 4.43221   -30.95507 0.86643   1.000 67.04559  ?  116 ASP A C   1 
ATOM   862  O  O   . ASP A 1 116 ? 3.31319   -31.40033 0.60297   1.000 62.25037  ?  116 ASP A O   1 
ATOM   863  C  CB  . ASP A 1 116 ? 3.91928   -29.03633 -0.69372  1.000 65.82599  ?  116 ASP A CB  1 
ATOM   864  C  CG  . ASP A 1 116 ? 2.57634   -28.82853 0.01585   1.000 70.50421  ?  116 ASP A CG  1 
ATOM   865  O  OD1 . ASP A 1 116 ? 2.58591   -28.40256 1.20460   1.000 70.20373  ?  116 ASP A OD1 1 
ATOM   866  O  OD2 . ASP A 1 116 ? 1.51862   -29.10896 -0.59244  1.000 68.59472  ?  116 ASP A OD2 1 
ATOM   867  N  N   . VAL A 1 117 ? 5.23934   -31.55053 1.73024   1.000 69.28044  ?  117 VAL A N   1 
ATOM   868  C  CA  . VAL A 1 117 ? 4.87597   -32.79132 2.39511   1.000 75.12610  ?  117 VAL A CA  1 
ATOM   869  C  C   . VAL A 1 117 ? 4.62974   -32.47437 3.86061   1.000 76.60231  ?  117 VAL A C   1 
ATOM   870  O  O   . VAL A 1 117 ? 5.55734   -32.09352 4.57814   1.000 76.64711  ?  117 VAL A O   1 
ATOM   871  C  CB  . VAL A 1 117 ? 5.96385   -33.85398 2.23315   1.000 70.84510  ?  117 VAL A CB  1 
ATOM   872  C  CG1 . VAL A 1 117 ? 5.91675   -34.81547 3.39009   1.000 68.46719  ?  117 VAL A CG1 1 
ATOM   873  C  CG2 . VAL A 1 117 ? 5.77899   -34.56951 0.90823   1.000 64.00630  ?  117 VAL A CG2 1 
ATOM   874  N  N   . SER A 1 118 ? 3.38707   -32.65420 4.31932   1.000 79.60961  ?  118 SER A N   1 
ATOM   875  C  CA  . SER A 1 118 ? 2.98536   -32.23490 5.65618   1.000 79.23284  ?  118 SER A CA  1 
ATOM   876  C  C   . SER A 1 118 ? 2.44617   -33.35777 6.52723   1.000 79.84665  ?  118 SER A C   1 
ATOM   877  O  O   . SER A 1 118 ? 2.15159   -33.11167 7.69684   1.000 81.69827  ?  118 SER A O   1 
ATOM   878  C  CB  . SER A 1 118 ? 1.91649   -31.13054 5.56995   1.000 85.87680  ?  118 SER A CB  1 
ATOM   879  O  OG  . SER A 1 118 ? 0.65897   -31.68016 5.20756   1.000 91.43010  ?  118 SER A OG  1 
ATOM   880  N  N   . SER A 1 119 ? 2.31275   -34.57058 6.00294   1.000 81.10053  ?  119 SER A N   1 
ATOM   881  C  CA  . SER A 1 119 ? 1.68282   -35.67396 6.70545   1.000 84.68502  ?  119 SER A CA  1 
ATOM   882  C  C   . SER A 1 119 ? 2.38086   -36.96396 6.30533   1.000 82.50479  ?  119 SER A C   1 
ATOM   883  O  O   . SER A 1 119 ? 3.19027   -36.99677 5.37568   1.000 80.12225  ?  119 SER A O   1 
ATOM   884  C  CB  . SER A 1 119 ? 0.18272   -35.75799 6.39074   1.000 80.77263  ?  119 SER A CB  1 
ATOM   885  O  OG  . SER A 1 119 ? -0.03370  -35.71489 4.99279   1.000 82.63246  ?  119 SER A OG  1 
ATOM   886  N  N   . GLU A 1 120 ? 2.06848   -38.03794 7.02314   1.000 75.94370  ?  120 GLU A N   1 
ATOM   887  C  CA  . GLU A 1 120 ? 2.70201   -39.31286 6.72188   1.000 84.86176  ?  120 GLU A CA  1 
ATOM   888  C  C   . GLU A 1 120 ? 2.27416   -39.81075 5.35455   1.000 81.67291  ?  120 GLU A C   1 
ATOM   889  O  O   . GLU A 1 120 ? 3.10640   -40.18779 4.52251   1.000 86.37617  ?  120 GLU A O   1 
ATOM   890  C  CB  . GLU A 1 120 ? 2.34926   -40.34677 7.78940   1.000 90.67472  ?  120 GLU A CB  1 
ATOM   891  C  CG  . GLU A 1 120 ? 2.66923   -39.90084 9.19053   1.000 91.79812  ?  120 GLU A CG  1 
ATOM   892  C  CD  . GLU A 1 120 ? 2.96881   -41.06637 10.09758  1.000 101.26581 ?  120 GLU A CD  1 
ATOM   893  O  OE1 . GLU A 1 120 ? 2.40634   -42.16390 9.87363   1.000 107.40835 ?  120 GLU A OE1 1 
ATOM   894  O  OE2 . GLU A 1 120 ? 3.77703   -40.88421 11.02998  1.000 105.56187 ?  120 GLU A OE2 1 
ATOM   895  N  N   . GLU A 1 121 ? 0.96730   -39.83320 5.11296   1.000 83.26083  ?  121 GLU A N   1 
ATOM   896  C  CA  . GLU A 1 121 ? 0.46305   -40.28895 3.82804   1.000 87.50368  ?  121 GLU A CA  1 
ATOM   897  C  C   . GLU A 1 121 ? 1.20151   -39.58980 2.69762   1.000 82.09968  ?  121 GLU A C   1 
ATOM   898  O  O   . GLU A 1 121 ? 1.65497   -40.23418 1.74437   1.000 85.01122  ?  121 GLU A O   1 
ATOM   899  C  CB  . GLU A 1 121 ? -1.05070  -40.04755 3.76432   1.000 93.63094  ?  121 GLU A CB  1 
ATOM   900  C  CG  . GLU A 1 121 ? -1.72697  -40.43687 2.46364   1.000 99.09227  ?  121 GLU A CG  1 
ATOM   901  C  CD  . GLU A 1 121 ? -1.51593  -41.89090 2.08908   1.000 106.67783 ?  121 GLU A CD  1 
ATOM   902  O  OE1 . GLU A 1 121 ? -1.77031  -42.77656 2.93906   1.000 111.34360 ?  121 GLU A OE1 1 
ATOM   903  O  OE2 . GLU A 1 121 ? -1.10019  -42.14304 0.93314   1.000 107.85061 ?  121 GLU A OE2 1 
ATOM   904  N  N   . GLU A 1 122 ? 1.39246   -38.27497 2.82313   1.000 83.51259  ?  122 GLU A N   1 
ATOM   905  C  CA  . GLU A 1 122 ? 2.09152   -37.52544 1.78543   1.000 79.32306  ?  122 GLU A CA  1 
ATOM   906  C  C   . GLU A 1 122 ? 3.56378   -37.91313 1.69522   1.000 76.68700  ?  122 GLU A C   1 
ATOM   907  O  O   . GLU A 1 122 ? 4.14362   -37.85778 0.60501   1.000 73.71024  ?  122 GLU A O   1 
ATOM   908  C  CB  . GLU A 1 122 ? 1.95088   -36.02577 2.03780   1.000 77.16074  ?  122 GLU A CB  1 
ATOM   909  C  CG  . GLU A 1 122 ? 0.53865   -35.51273 1.87315   1.000 67.27462  ?  122 GLU A CG  1 
ATOM   910  C  CD  . GLU A 1 122 ? 0.45284   -34.00995 2.05629   1.000 79.19640  ?  122 GLU A CD  1 
ATOM   911  O  OE1 . GLU A 1 122 ? 1.42227   -33.39552 2.58067   1.000 79.75542  ?  122 GLU A OE1 1 
ATOM   912  O  OE2 . GLU A 1 122 ? -0.58129  -33.43426 1.65480   1.000 81.57149  ?  122 GLU A OE2 1 
ATOM   913  N  N   . VAL A 1 123 ? 4.18968   -38.29567 2.81598   1.000 77.55803  ?  123 VAL A N   1 
ATOM   914  C  CA  . VAL A 1 123 ? 5.56999   -38.78475 2.75530   1.000 80.86058  ?  123 VAL A CA  1 
ATOM   915  C  C   . VAL A 1 123 ? 5.64293   -40.06006 1.92625   1.000 77.12524  ?  123 VAL A C   1 
ATOM   916  O  O   . VAL A 1 123 ? 6.56981   -40.24985 1.12728   1.000 76.25976  ?  123 VAL A O   1 
ATOM   917  C  CB  . VAL A 1 123 ? 6.15059   -39.01342 4.16722   1.000 79.90312  ?  123 VAL A CB  1 
ATOM   918  C  CG1 . VAL A 1 123 ? 7.43516   -39.83637 4.07586   1.000 71.95547  ?  123 VAL A CG1 1 
ATOM   919  C  CG2 . VAL A 1 123 ? 6.40251   -37.68849 4.88031   1.000 71.82476  ?  123 VAL A CG2 1 
ATOM   920  N  N   . LEU A 1 124 ? 4.66547   -40.94658 2.09636   1.000 76.92224  ?  124 LEU A N   1 
ATOM   921  C  CA  . LEU A 1 124 ? 4.69160   -42.23163 1.41150   1.000 79.20342  ?  124 LEU A CA  1 
ATOM   922  C  C   . LEU A 1 124 ? 4.31235   -42.08746 -0.05935  1.000 81.35845  ?  124 LEU A C   1 
ATOM   923  O  O   . LEU A 1 124 ? 4.91514   -42.73194 -0.92698  1.000 78.94841  ?  124 LEU A O   1 
ATOM   924  C  CB  . LEU A 1 124 ? 3.76314   -43.21220 2.11934   1.000 83.54761  ?  124 LEU A CB  1 
ATOM   925  C  CG  . LEU A 1 124 ? 4.17812   -43.84685 3.45958   1.000 95.94588  ?  124 LEU A CG  1 
ATOM   926  C  CD1 . LEU A 1 124 ? 5.40051   -44.76451 3.31733   1.000 99.32836  ?  124 LEU A CD1 1 
ATOM   927  C  CD2 . LEU A 1 124 ? 4.42087   -42.80399 4.54311   1.000 81.39718  ?  124 LEU A CD2 1 
ATOM   928  N  N   . LYS A 1 125 ? 3.30813   -41.26495 -0.36334  1.000 80.16666  ?  125 LYS A N   1 
ATOM   929  C  CA  . LYS A 1 125 ? 3.03480   -40.96262 -1.76039  1.000 80.23272  ?  125 LYS A CA  1 
ATOM   930  C  C   . LYS A 1 125 ? 4.31053   -40.49558 -2.44686  1.000 72.92835  ?  125 LYS A C   1 
ATOM   931  O  O   . LYS A 1 125 ? 4.65979   -40.97813 -3.53047  1.000 69.40614  ?  125 LYS A O   1 
ATOM   932  C  CB  . LYS A 1 125 ? 1.93236   -39.90549 -1.86243  1.000 71.92490  ?  125 LYS A CB  1 
ATOM   933  C  CG  . LYS A 1 125 ? 1.05168   -40.04402 -3.08294  1.000 85.93467  ?  125 LYS A CG  1 
ATOM   934  C  CD  . LYS A 1 125 ? 0.38576   -41.42052 -3.13510  1.000 86.84583  ?  125 LYS A CD  1 
ATOM   935  C  CE  . LYS A 1 125 ? 0.24212   -41.87457 -4.57981  1.000 86.20491  ?  125 LYS A CE  1 
ATOM   936  N  NZ  . LYS A 1 125 ? 1.44602   -41.37081 -5.33296  1.000 88.58902  ?  125 LYS A NZ  1 
ATOM   937  N  N   . PHE A 1 126 ? 5.06473   -39.62899 -1.77023  1.000 71.48480  ?  126 PHE A N   1 
ATOM   938  C  CA  . PHE A 1 126 ? 6.24520   -38.99462 -2.35452  1.000 66.95879  ?  126 PHE A CA  1 
ATOM   939  C  C   . PHE A 1 126 ? 7.38757   -39.98922 -2.52496  1.000 68.36317  ?  126 PHE A C   1 
ATOM   940  O  O   . PHE A 1 126 ? 8.06414   -39.99916 -3.56084  1.000 64.79756  ?  126 PHE A O   1 
ATOM   941  C  CB  . PHE A 1 126 ? 6.67019   -37.81418 -1.47594  1.000 62.78980  ?  126 PHE A CB  1 
ATOM   942  C  CG  . PHE A 1 126 ? 7.86559   -37.05379 -1.99081  1.000 63.25086  ?  126 PHE A CG  1 
ATOM   943  C  CD1 . PHE A 1 126 ? 9.15403   -37.48663 -1.72396  1.000 56.61891  ?  126 PHE A CD1 1 
ATOM   944  C  CD2 . PHE A 1 126 ? 7.70067   -35.90998 -2.74401  1.000 62.14929  ?  126 PHE A CD2 1 
ATOM   945  C  CE1 . PHE A 1 126 ? 10.24211  -36.80248 -2.21625  1.000 60.80515  ?  126 PHE A CE1 1 
ATOM   946  C  CE2 . PHE A 1 126 ? 8.80580   -35.20796 -3.22303  1.000 62.38805  ?  126 PHE A CE2 1 
ATOM   947  C  CZ  . PHE A 1 126 ? 10.06838  -35.65228 -2.95467  1.000 60.83368  ?  126 PHE A CZ  1 
ATOM   948  N  N   . VAL A 1 127 ? 7.63727   -40.82253 -1.50944  1.000 73.75950  ?  127 VAL A N   1 
ATOM   949  C  CA  . VAL A 1 127 ? 8.75621   -41.75213 -1.60226  1.000 73.77811  ?  127 VAL A CA  1 
ATOM   950  C  C   . VAL A 1 127 ? 8.47459   -42.77025 -2.69216  1.000 77.55040  ?  127 VAL A C   1 
ATOM   951  O  O   . VAL A 1 127 ? 9.35303   -43.09692 -3.49819  1.000 81.45471  ?  127 VAL A O   1 
ATOM   952  C  CB  . VAL A 1 127 ? 9.04558   -42.39851 -0.22829  1.000 77.17442  ?  127 VAL A CB  1 
ATOM   953  C  CG1 . VAL A 1 127 ? 10.03578  -43.55839 -0.35610  1.000 72.13989  ?  127 VAL A CG1 1 
ATOM   954  C  CG2 . VAL A 1 127 ? 9.60804   -41.34121 0.71840   1.000 72.84502  ?  127 VAL A CG2 1 
ATOM   955  N  N   . ASN A 1 128 ? 7.22009   -43.21998 -2.78719  1.000 79.86167  ?  128 ASN A N   1 
ATOM   956  C  CA  . ASN A 1 128 ? 6.81586   -44.12076 -3.86420  1.000 78.74313  ?  128 ASN A CA  1 
ATOM   957  C  C   . ASN A 1 128 ? 7.13658   -43.54849 -5.23507  1.000 80.76308  ?  128 ASN A C   1 
ATOM   958  O  O   . ASN A 1 128 ? 7.75425   -44.22112 -6.06835  1.000 80.84301  ?  128 ASN A O   1 
ATOM   959  C  CB  . ASN A 1 128 ? 5.32827   -44.42076 -3.76367  1.000 88.82506  ?  128 ASN A CB  1 
ATOM   960  C  CG  . ASN A 1 128 ? 5.01646   -45.36327 -2.64985  1.000 97.29006  ?  128 ASN A CG  1 
ATOM   961  O  OD1 . ASN A 1 128 ? 5.92062   -45.99325 -2.08967  1.000 104.07376 ?  128 ASN A OD1 1 
ATOM   962  N  ND2 . ASN A 1 128 ? 3.73095   -45.48233 -2.31046  1.000 102.47388 ?  128 ASN A ND2 1 
ATOM   963  N  N   . LEU A 1 129 ? 6.67871   -42.32611 -5.50835  1.000 74.66987  ?  129 LEU A N   1 
ATOM   964  C  CA  . LEU A 1 129 ? 6.97252   -41.70129 -6.79577  1.000 78.72425  ?  129 LEU A CA  1 
ATOM   965  C  C   . LEU A 1 129 ? 8.46529   -41.70240 -7.06056  1.000 82.36698  ?  129 LEU A C   1 
ATOM   966  O  O   . LEU A 1 129 ? 8.92145   -42.14647 -8.11854  1.000 85.87187  ?  129 LEU A O   1 
ATOM   967  C  CB  . LEU A 1 129 ? 6.43266   -40.27078 -6.83409  1.000 64.42322  ?  129 LEU A CB  1 
ATOM   968  C  CG  . LEU A 1 129 ? 6.08666   -39.76230 -8.23086  1.000 78.33125  ?  129 LEU A CG  1 
ATOM   969  C  CD1 . LEU A 1 129 ? 5.39535   -40.83963 -9.08230  1.000 70.25763  ?  129 LEU A CD1 1 
ATOM   970  C  CD2 . LEU A 1 129 ? 5.19959   -38.54124 -8.10350  1.000 69.95071  ?  129 LEU A CD2 1 
ATOM   971  N  N   . MET A 1 130 ? 9.23960   -41.23191 -6.08103  1.000 80.52680  ?  130 MET A N   1 
ATOM   972  C  CA  . MET A 1 130 ? 10.67857  -41.08389 -6.24670  1.000 80.80614  ?  130 MET A CA  1 
ATOM   973  C  C   . MET A 1 130 ? 11.36473  -42.43322 -6.43179  1.000 82.85388  ?  130 MET A C   1 
ATOM   974  O  O   . MET A 1 130 ? 12.32582  -42.55045 -7.20125  1.000 81.64139  ?  130 MET A O   1 
ATOM   975  C  CB  . MET A 1 130 ? 11.24942  -40.34238 -5.03485  1.000 79.91054  ?  130 MET A CB  1 
ATOM   976  C  CG  . MET A 1 130 ? 12.65124  -39.78663 -5.21711  1.000 70.72168  ?  130 MET A CG  1 
ATOM   977  S  SD  . MET A 1 130 ? 12.71346  -38.43258 -6.41630  1.000 71.58530  ?  130 MET A SD  1 
ATOM   978  C  CE  . MET A 1 130 ? 12.37864  -36.97301 -5.39193  1.000 59.28510  ?  130 MET A CE  1 
ATOM   979  N  N   . GLU A 1 131 ? 10.89247  -43.45381 -5.75572  1.000 80.52213  ?  131 GLU A N   1 
ATOM   980  C  CA  . GLU A 1 131 ? 11.59080  -44.71672 -5.95711  1.000 87.64091  ?  131 GLU A CA  1 
ATOM   981  C  C   . GLU A 1 131 ? 11.31959  -45.33469 -7.26650  1.000 93.03683  ?  131 GLU A C   1 
ATOM   982  O  O   . GLU A 1 131 ? 11.76990  -46.48346 -7.36138  1.000 88.85608  ?  131 GLU A O   1 
ATOM   983  C  CB  . GLU A 1 131 ? 11.22955  -45.71451 -4.85705  1.000 91.19969  ?  131 GLU A CB  1 
ATOM   984  C  CG  . GLU A 1 131 ? 12.10246  -45.58406 -3.62160  1.000 93.23150  ?  131 GLU A CG  1 
ATOM   985  C  CD  . GLU A 1 131 ? 11.47116  -46.23575 -2.41553  1.000 102.56872 ?  131 GLU A CD  1 
ATOM   986  O  OE1 . GLU A 1 131 ? 10.31061  -46.68180 -2.55331  1.000 94.13933  ?  131 GLU A OE1 1 
ATOM   987  O  OE2 . GLU A 1 131 ? 12.12725  -46.29663 -1.34122  1.000 116.91368 ?  131 GLU A OE2 1 
ATOM   988  N  N   . MET A 1 132 ? 10.64942  -44.70607 -8.23512  1.000 100.26632 ?  132 MET A N   1 
ATOM   989  C  CA  . MET A 1 132 ? 10.33381  -45.36790 -9.50053  1.000 103.71422 ?  132 MET A CA  1 
ATOM   990  C  C   . MET A 1 132 ? 11.58956  -45.43427 -10.37404 1.000 108.36630 ?  132 MET A C   1 
ATOM   991  O  O   . MET A 1 132 ? 12.72024  -45.20319 -9.92664  1.000 105.74173 ?  132 MET A O   1 
ATOM   992  C  CB  . MET A 1 132 ? 9.21187   -44.65235 -10.26194 1.000 100.83438 ?  132 MET A CB  1 
ATOM   993  C  CG  . MET A 1 132 ? 7.89946   -44.41645 -9.53626  1.000 100.94760 ?  132 MET A CG  1 
ATOM   994  S  SD  . MET A 1 132 ? 6.99716   -45.90577 -9.10414  1.000 112.21066 ?  132 MET A SD  1 
ATOM   995  C  CE  . MET A 1 132 ? 5.30081   -45.33429 -9.30985  1.000 104.18064 ?  132 MET A CE  1 
ATOM   996  N  N   . ALA A 1 133 ? 11.37202  -45.73091 -11.65770 1.000 108.79227 ?  133 ALA A N   1 
ATOM   997  C  CA  . ALA A 1 133 ? 12.40696  -45.74088 -12.67695 1.000 104.36390 ?  133 ALA A CA  1 
ATOM   998  C  C   . ALA A 1 133 ? 12.59529  -44.35206 -13.28335 1.000 105.69006 ?  133 ALA A C   1 
ATOM   999  O  O   . ALA A 1 133 ? 11.65583  -43.55715 -13.40327 1.000 100.80232 ?  133 ALA A O   1 
ATOM   1000 C  CB  . ALA A 1 133 ? 12.05419  -46.74044 -13.77801 1.000 109.41397 ?  133 ALA A CB  1 
ATOM   1001 N  N   . LYS A 1 134 ? 13.83600  -44.07044 -13.66625 1.000 110.38277 ?  134 LYS A N   1 
ATOM   1002 C  CA  . LYS A 1 134 ? 14.18673  -42.82564 -14.34645 1.000 110.67381 ?  134 LYS A CA  1 
ATOM   1003 C  C   . LYS A 1 134 ? 13.65727  -41.60546 -13.59526 1.000 106.64043 ?  134 LYS A C   1 
ATOM   1004 O  O   . LYS A 1 134 ? 13.33372  -40.57464 -14.19518 1.000 104.88684 ?  134 LYS A O   1 
ATOM   1005 C  CB  . LYS A 1 134 ? 13.70226  -42.83556 -15.80423 1.000 111.36971 ?  134 LYS A CB  1 
ATOM   1006 C  CG  . LYS A 1 134 ? 14.38987  -43.89098 -16.67666 1.000 113.17711 ?  134 LYS A CG  1 
ATOM   1007 C  CD  . LYS A 1 134 ? 15.91082  -43.87555 -16.46989 1.000 117.92137 ?  134 LYS A CD  1 
ATOM   1008 C  CE  . LYS A 1 134 ? 16.49552  -45.28926 -16.40781 1.000 123.00164 ?  134 LYS A CE  1 
ATOM   1009 N  NZ  . LYS A 1 134 ? 17.94961  -45.32333 -16.04795 1.000 125.35815 ?  134 LYS A NZ  1 
ATOM   1010 N  N   . THR A 1 135 ? 13.55797  -41.72004 -12.27287 1.000 96.75800  ?  135 THR A N   1 
ATOM   1011 C  CA  . THR A 1 135 ? 13.28049  -40.57936 -11.41321 1.000 90.55014  ?  135 THR A CA  1 
ATOM   1012 C  C   . THR A 1 135 ? 14.31243  -40.59047 -10.29376 1.000 86.16624  ?  135 THR A C   1 
ATOM   1013 O  O   . THR A 1 135 ? 14.43179  -41.57932 -9.56181  1.000 84.29452  ?  135 THR A O   1 
ATOM   1014 C  CB  . THR A 1 135 ? 11.84363  -40.61856 -10.87114 1.000 92.89707  ?  135 THR A CB  1 
ATOM   1015 O  OG1 . THR A 1 135 ? 11.82519  -41.22845 -9.58110  1.000 95.50647  ?  135 THR A OG1 1 
ATOM   1016 C  CG2 . THR A 1 135 ? 10.91192  -41.40560 -11.81682 1.000 91.45132  ?  135 THR A CG2 1 
ATOM   1017 N  N   . GLU A 1 136 ? 15.07638  -39.50506 -10.18654 1.000 80.35041  ?  136 GLU A N   1 
ATOM   1018 C  CA  . GLU A 1 136 ? 16.19341  -39.35986 -9.26614  1.000 78.20060  ?  136 GLU A CA  1 
ATOM   1019 C  C   . GLU A 1 136 ? 16.05591  -38.07565 -8.46612  1.000 74.62418  ?  136 GLU A C   1 
ATOM   1020 O  O   . GLU A 1 136 ? 15.66906  -37.04322 -9.02101  1.000 73.53941  ?  136 GLU A O   1 
ATOM   1021 C  CB  . GLU A 1 136 ? 17.50881  -39.33433 -10.03818 1.000 79.47247  ?  136 GLU A CB  1 
ATOM   1022 C  CG  . GLU A 1 136 ? 17.61200  -40.47602 -10.98962 1.000 88.56984  ?  136 GLU A CG  1 
ATOM   1023 C  CD  . GLU A 1 136 ? 17.77629  -41.78358 -10.25421 1.000 91.77618  ?  136 GLU A CD  1 
ATOM   1024 O  OE1 . GLU A 1 136 ? 18.42864  -41.76214 -9.18838  1.000 73.72791  ?  136 GLU A OE1 1 
ATOM   1025 O  OE2 . GLU A 1 136 ? 17.24087  -42.81198 -10.73099 1.000 96.48580  ?  136 GLU A OE2 1 
ATOM   1026 N  N   . PRO A 1 137 ? 16.38720  -38.08931 -7.17951  1.000 74.90723  ?  137 PRO A N   1 
ATOM   1027 C  CA  . PRO A 1 137 ? 16.23104  -36.87859 -6.36491  1.000 69.58116  ?  137 PRO A CA  1 
ATOM   1028 C  C   . PRO A 1 137 ? 17.27186  -35.82811 -6.72688  1.000 70.78639  ?  137 PRO A C   1 
ATOM   1029 O  O   . PRO A 1 137 ? 18.33975  -36.12870 -7.25862  1.000 67.80161  ?  137 PRO A O   1 
ATOM   1030 C  CB  . PRO A 1 137 ? 16.42742  -37.38121 -4.93047  1.000 71.81055  ?  137 PRO A CB  1 
ATOM   1031 C  CG  . PRO A 1 137 ? 16.44015  -38.90016 -5.02804  1.000 75.24017  ?  137 PRO A CG  1 
ATOM   1032 C  CD  . PRO A 1 137 ? 16.88894  -39.22858 -6.40073  1.000 78.92731  ?  137 PRO A CD  1 
ATOM   1033 N  N   . LEU A 1 138 ? 16.95084  -34.56874 -6.41606  1.000 66.77032  ?  138 LEU A N   1 
ATOM   1034 C  CA  . LEU A 1 138 ? 17.87083  -33.49328 -6.77029  1.000 70.09260  ?  138 LEU A CA  1 
ATOM   1035 C  C   . LEU A 1 138 ? 19.24088  -33.68470 -6.12240  1.000 78.71959  ?  138 LEU A C   1 
ATOM   1036 O  O   . LEU A 1 138 ? 20.26191  -33.36522 -6.74051  1.000 84.31200  ?  138 LEU A O   1 
ATOM   1037 C  CB  . LEU A 1 138 ? 17.26344  -32.13322 -6.39969  1.000 68.56238  ?  138 LEU A CB  1 
ATOM   1038 C  CG  . LEU A 1 138 ? 15.99127  -31.79513 -7.18196  1.000 68.98571  ?  138 LEU A CG  1 
ATOM   1039 C  CD1 . LEU A 1 138 ? 15.47439  -30.37578 -6.97292  1.000 65.06536  ?  138 LEU A CD1 1 
ATOM   1040 C  CD2 . LEU A 1 138 ? 16.23738  -32.04791 -8.65581  1.000 68.74148  ?  138 LEU A CD2 1 
ATOM   1041 N  N   . LEU A 1 139 ? 19.29944  -34.22847 -4.89806  1.000 77.36367  ?  139 LEU A N   1 
ATOM   1042 C  CA  . LEU A 1 139 ? 20.58856  -34.38500 -4.22473  1.000 77.52839  ?  139 LEU A CA  1 
ATOM   1043 C  C   . LEU A 1 139 ? 21.59912  -35.16716 -5.05837  1.000 82.55851  ?  139 LEU A C   1 
ATOM   1044 O  O   . LEU A 1 139 ? 22.80022  -35.12859 -4.74355  1.000 82.84582  ?  139 LEU A O   1 
ATOM   1045 C  CB  . LEU A 1 139 ? 20.39878  -35.04820 -2.84787  1.000 78.44948  ?  139 LEU A CB  1 
ATOM   1046 C  CG  . LEU A 1 139 ? 19.74612  -36.43402 -2.79931  1.000 78.04866  ?  139 LEU A CG  1 
ATOM   1047 C  CD1 . LEU A 1 139 ? 20.78165  -37.52601 -2.94356  1.000 75.93195  ?  139 LEU A CD1 1 
ATOM   1048 C  CD2 . LEU A 1 139 ? 18.90449  -36.62519 -1.53712  1.000 71.58368  ?  139 LEU A CD2 1 
ATOM   1049 N  N   . THR A 1 140 ? 21.15978  -35.85179 -6.12097  1.000 75.50378  ?  140 THR A N   1 
ATOM   1050 C  CA  . THR A 1 140 ? 22.10637  -36.59353 -6.94585  1.000 79.98026  ?  140 THR A CA  1 
ATOM   1051 C  C   . THR A 1 140 ? 22.92400  -35.66974 -7.84043  1.000 84.48284  ?  140 THR A C   1 
ATOM   1052 O  O   . THR A 1 140 ? 23.99027  -36.06604 -8.32283  1.000 80.93468  ?  140 THR A O   1 
ATOM   1053 C  CB  . THR A 1 140 ? 21.37311  -37.64621 -7.77620  1.000 78.23699  ?  140 THR A CB  1 
ATOM   1054 O  OG1 . THR A 1 140 ? 20.28580  -37.04239 -8.48845  1.000 81.34105  ?  140 THR A OG1 1 
ATOM   1055 C  CG2 . THR A 1 140 ? 20.81753  -38.72625 -6.88196  1.000 82.25284  ?  140 THR A CG2 1 
ATOM   1056 N  N   . LEU A 1 141 ? 22.44843  -34.44530 -8.06070  1.000 83.53484  ?  141 LEU A N   1 
ATOM   1057 C  CA  . LEU A 1 141 ? 23.23997  -33.44860 -8.76930  1.000 81.18861  ?  141 LEU A CA  1 
ATOM   1058 C  C   . LEU A 1 141 ? 24.30999  -32.86833 -7.87515  1.000 94.99128  ?  141 LEU A C   1 
ATOM   1059 O  O   . LEU A 1 141 ? 25.33069  -32.35967 -8.36349  1.000 96.27253  ?  141 LEU A O   1 
ATOM   1060 C  CB  . LEU A 1 141 ? 22.33262  -32.32330 -9.24803  1.000 80.47210  ?  141 LEU A CB  1 
ATOM   1061 C  CG  . LEU A 1 141 ? 21.31069  -32.77854 -10.26853 1.000 70.05898  ?  141 LEU A CG  1 
ATOM   1062 C  CD1 . LEU A 1 141 ? 20.27774  -31.71557 -10.45390 1.000 74.59335  ?  141 LEU A CD1 1 
ATOM   1063 C  CD2 . LEU A 1 141 ? 22.07479  -33.01396 -11.55188 1.000 78.98533  ?  141 LEU A CD2 1 
ATOM   1064 N  N   . SER A 1 142 ? 24.09005  -32.95974 -6.56452  1.000 97.66219  ?  142 SER A N   1 
ATOM   1065 C  CA  . SER A 1 142 ? 24.74999  -32.14168 -5.56536  1.000 92.99943  ?  142 SER A CA  1 
ATOM   1066 C  C   . SER A 1 142 ? 25.67826  -32.95616 -4.68355  1.000 95.31076  ?  142 SER A C   1 
ATOM   1067 O  O   . SER A 1 142 ? 26.08917  -32.48306 -3.61648  1.000 96.17563  ?  142 SER A O   1 
ATOM   1068 C  CB  . SER A 1 142 ? 23.68147  -31.43685 -4.72303  1.000 90.47063  ?  142 SER A CB  1 
ATOM   1069 O  OG  . SER A 1 142 ? 24.20651  -30.28416 -4.08251  1.000 99.82247  ?  142 SER A OG  1 
ATOM   1070 N  N   . GLY A 1 143 ? 26.00512  -34.17830 -5.09625  1.000 98.69928  ?  143 GLY A N   1 
ATOM   1071 C  CA  . GLY A 1 143 ? 26.81119  -35.03988 -4.24817  1.000 93.38701  ?  143 GLY A CA  1 
ATOM   1072 C  C   . GLY A 1 143 ? 26.21858  -35.26846 -2.87872  1.000 87.66225  ?  143 GLY A C   1 
ATOM   1073 O  O   . GLY A 1 143 ? 26.95548  -35.56711 -1.93452  1.000 95.89782  ?  143 GLY A O   1 
ATOM   1074 N  N   . GLY A 1 144 ? 24.90071  -35.12721 -2.74134  1.000 89.67872  ?  144 GLY A N   1 
ATOM   1075 C  CA  . GLY A 1 144 ? 24.20645  -35.42992 -1.50194  1.000 86.77460  ?  144 GLY A CA  1 
ATOM   1076 C  C   . GLY A 1 144 ? 23.77791  -34.20931 -0.70938  1.000 84.48561  ?  144 GLY A C   1 
ATOM   1077 O  O   . GLY A 1 144 ? 22.67140  -34.17150 -0.16105  1.000 84.88009  ?  144 GLY A O   1 
ATOM   1078 N  N   . VAL A 1 145 ? 24.63583  -33.20480 -0.63077  1.000 84.70663  ?  145 VAL A N   1 
ATOM   1079 C  CA  . VAL A 1 145 ? 24.33134  -32.04947 0.19907   1.000 86.54415  ?  145 VAL A CA  1 
ATOM   1080 C  C   . VAL A 1 145 ? 23.26941  -31.20139 -0.48321  1.000 86.73936  ?  145 VAL A C   1 
ATOM   1081 O  O   . VAL A 1 145 ? 23.30522  -30.98522 -1.69720  1.000 87.84042  ?  145 VAL A O   1 
ATOM   1082 C  CB  . VAL A 1 145 ? 25.60169  -31.23578 0.49473   1.000 91.88591  ?  145 VAL A CB  1 
ATOM   1083 C  CG1 . VAL A 1 145 ? 26.70516  -31.54177 -0.52170  1.000 91.63413  ?  145 VAL A CG1 1 
ATOM   1084 C  CG2 . VAL A 1 145 ? 25.25792  -29.75499 0.51018   1.000 85.86379  ?  145 VAL A CG2 1 
ATOM   1085 N  N   . HIS A 1 146 ? 22.31701  -30.71530 0.29684   1.000 80.29210  ?  146 HIS A N   1 
ATOM   1086 C  CA  . HIS A 1 146 ? 21.23737  -29.91922 -0.25428  1.000 81.45998  ?  146 HIS A CA  1 
ATOM   1087 C  C   . HIS A 1 146 ? 20.54848  -29.20357 0.88673   1.000 76.80856  ?  146 HIS A C   1 
ATOM   1088 O  O   . HIS A 1 146 ? 20.84456  -29.44086 2.05644   1.000 74.03277  ?  146 HIS A O   1 
ATOM   1089 C  CB  . HIS A 1 146 ? 20.23508  -30.78900 -1.00436  1.000 75.62888  ?  146 HIS A CB  1 
ATOM   1090 C  CG  . HIS A 1 146 ? 19.58406  -31.82400 -0.14703  1.000 75.44088  ?  146 HIS A CG  1 
ATOM   1091 N  ND1 . HIS A 1 146 ? 20.24762  -32.94917 0.29719   1.000 76.96453  ?  146 HIS A ND1 1 
ATOM   1092 C  CD2 . HIS A 1 146 ? 18.32160  -31.91567 0.33670   1.000 72.45675  ?  146 HIS A CD2 1 
ATOM   1093 C  CE1 . HIS A 1 146 ? 19.41760  -33.69118 1.00952   1.000 75.19809  ?  146 HIS A CE1 1 
ATOM   1094 N  NE2 . HIS A 1 146 ? 18.24364  -33.08807 1.04215   1.000 69.04735  ?  146 HIS A NE2 1 
ATOM   1095 N  N   . LEU A 1 147 ? 19.56442  -28.38036 0.53292   1.000 76.92270  ?  147 LEU A N   1 
ATOM   1096 C  CA  . LEU A 1 147 ? 18.81783  -27.58894 1.49224   1.000 72.28785  ?  147 LEU A CA  1 
ATOM   1097 C  C   . LEU A 1 147 ? 17.35687  -28.01143 1.47805   1.000 69.27683  ?  147 LEU A C   1 
ATOM   1098 O  O   . LEU A 1 147 ? 16.84311  -28.52417 0.47501   1.000 71.36151  ?  147 LEU A O   1 
ATOM   1099 C  CB  . LEU A 1 147 ? 18.92713  -26.09456 1.18238   1.000 70.67637  ?  147 LEU A CB  1 
ATOM   1100 C  CG  . LEU A 1 147 ? 20.34320  -25.50854 1.10660   1.000 80.74061  ?  147 LEU A CG  1 
ATOM   1101 C  CD1 . LEU A 1 147 ? 20.32134  -24.09754 0.53246   1.000 78.20526  ?  147 LEU A CD1 1 
ATOM   1102 C  CD2 . LEU A 1 147 ? 21.04250  -25.50425 2.46018   1.000 74.36856  ?  147 LEU A CD2 1 
ATOM   1103 N  N   . HIS A 1 148 ? 16.68743  -27.77877 2.59661   1.000 65.14752  ?  148 HIS A N   1 
ATOM   1104 C  CA  . HIS A 1 148 ? 15.24396  -27.88271 2.66230   1.000 68.13140  ?  148 HIS A CA  1 
ATOM   1105 C  C   . HIS A 1 148 ? 14.69313  -26.62418 3.30348   1.000 70.35323  ?  148 HIS A C   1 
ATOM   1106 O  O   . HIS A 1 148 ? 15.31575  -26.05197 4.19729   1.000 71.78665  ?  148 HIS A O   1 
ATOM   1107 C  CB  . HIS A 1 148 ? 14.80504  -29.09581 3.45951   1.000 68.76757  ?  148 HIS A CB  1 
ATOM   1108 C  CG  . HIS A 1 148 ? 14.92175  -30.38033 2.71132   1.000 66.10366  ?  148 HIS A CG  1 
ATOM   1109 N  ND1 . HIS A 1 148 ? 14.23638  -30.61786 1.54272   1.000 64.09848  ?  148 HIS A ND1 1 
ATOM   1110 C  CD2 . HIS A 1 148 ? 15.62072  -31.50578 2.97503   1.000 72.65656  ?  148 HIS A CD2 1 
ATOM   1111 C  CE1 . HIS A 1 148 ? 14.51992  -31.82992 1.10989   1.000 64.45152  ?  148 HIS A CE1 1 
ATOM   1112 N  NE2 . HIS A 1 148 ? 15.33312  -32.39816 1.97643   1.000 68.46288  ?  148 HIS A NE2 1 
ATOM   1113 N  N   . THR A 1 149 ? 13.52687  -26.19472 2.83828   1.000 66.69326  ?  149 THR A N   1 
ATOM   1114 C  CA  . THR A 1 149 ? 12.76455  -25.16706 3.52837   1.000 70.52976  ?  149 THR A CA  1 
ATOM   1115 C  C   . THR A 1 149 ? 11.73257  -25.86941 4.39260   1.000 71.88740  ?  149 THR A C   1 
ATOM   1116 O  O   . THR A 1 149 ? 10.87379  -26.58698 3.87404   1.000 76.51714  ?  149 THR A O   1 
ATOM   1117 C  CB  . THR A 1 149 ? 12.09070  -24.19847 2.55403   1.000 76.74281  ?  149 THR A CB  1 
ATOM   1118 O  OG1 . THR A 1 149 ? 13.08281  -23.60661 1.70758   1.000 73.19885  ?  149 THR A OG1 1 
ATOM   1119 C  CG2 . THR A 1 149 ? 11.40395  -23.07769 3.31173   1.000 73.43107  ?  149 THR A CG2 1 
ATOM   1120 N  N   . ILE A 1 150 ? 11.85040  -25.69409 5.70558   1.000 76.60185  ?  150 ILE A N   1 
ATOM   1121 C  CA  . ILE A 1 150 ? 10.98141  -26.32055 6.69564   1.000 80.15806  ?  150 ILE A CA  1 
ATOM   1122 C  C   . ILE A 1 150 ? 10.07445  -25.25805 7.29354   1.000 84.93361  ?  150 ILE A C   1 
ATOM   1123 O  O   . ILE A 1 150 ? 10.53085  -24.16288 7.64343   1.000 81.95698  ?  150 ILE A O   1 
ATOM   1124 C  CB  . ILE A 1 150 ? 11.78506  -27.00282 7.81890   1.000 80.24073  ?  150 ILE A CB  1 
ATOM   1125 C  CG1 . ILE A 1 150 ? 12.67527  -28.09484 7.25656   1.000 74.25901  ?  150 ILE A CG1 1 
ATOM   1126 C  CG2 . ILE A 1 150 ? 10.84420  -27.56648 8.85525   1.000 78.67673  ?  150 ILE A CG2 1 
ATOM   1127 C  CD1 . ILE A 1 150 ? 11.88406  -29.08495 6.45985   1.000 75.16886  ?  150 ILE A CD1 1 
ATOM   1128 N  N   . GLU A 1 151 ? 8.79798   -25.59015 7.43909   1.000 84.99356  ?  151 GLU A N   1 
ATOM   1129 C  CA  . GLU A 1 151 ? 7.84339   -24.71747 8.10095   1.000 90.40257  ?  151 GLU A CA  1 
ATOM   1130 C  C   . GLU A 1 151 ? 7.30699   -25.39997 9.35081   1.000 91.52724  ?  151 GLU A C   1 
ATOM   1131 O  O   . GLU A 1 151 ? 7.18504   -26.62750 9.40297   1.000 88.79071  ?  151 GLU A O   1 
ATOM   1132 C  CB  . GLU A 1 151 ? 6.68703   -24.35224 7.17044   1.000 89.93669  ?  151 GLU A CB  1 
ATOM   1133 C  CG  . GLU A 1 151 ? 6.98250   -23.20784 6.22093   1.000 89.95941  ?  151 GLU A CG  1 
ATOM   1134 C  CD  . GLU A 1 151 ? 5.81574   -22.92410 5.29756   1.000 92.93599  ?  151 GLU A CD  1 
ATOM   1135 O  OE1 . GLU A 1 151 ? 4.71601   -23.48095 5.54702   1.000 86.08730  ?  151 GLU A OE1 1 
ATOM   1136 O  OE2 . GLU A 1 151 ? 6.00526   -22.14992 4.32849   1.000 94.85314  ?  151 GLU A OE2 1 
ATOM   1137 N  N   . ALA A 1 152 ? 6.97666   -24.59840 10.35729  1.000 102.51003 ?  152 ALA A N   1 
ATOM   1138 C  CA  . ALA A 1 152 ? 6.46323   -25.14791 11.60478  1.000 106.00122 ?  152 ALA A CA  1 
ATOM   1139 C  C   . ALA A 1 152 ? 5.62440   -24.08045 12.29373  1.000 113.37712 ?  152 ALA A C   1 
ATOM   1140 O  O   . ALA A 1 152 ? 5.73015   -22.89371 11.97281  1.000 113.10004 ?  152 ALA A O   1 
ATOM   1141 C  CB  . ALA A 1 152 ? 7.60076   -25.61786 12.51790  1.000 105.53631 ?  152 ALA A CB  1 
ATOM   1142 N  N   . PRO A 1 153 ? 4.77885   -24.48919 13.24383  1.000 115.52841 ?  153 PRO A N   1 
ATOM   1143 C  CA  . PRO A 1 153 ? 3.94316   -23.49485 13.95000  1.000 119.95030 ?  153 PRO A CA  1 
ATOM   1144 C  C   . PRO A 1 153 ? 4.74359   -22.42740 14.67380  1.000 124.77695 ?  153 PRO A C   1 
ATOM   1145 O  O   . PRO A 1 153 ? 4.41572   -21.23857 14.57926  1.000 127.72419 ?  153 PRO A O   1 
ATOM   1146 C  CB  . PRO A 1 153 ? 3.13671   -24.36339 14.92751  1.000 121.77289 ?  153 PRO A CB  1 
ATOM   1147 C  CG  . PRO A 1 153 ? 3.15391   -25.73541 14.33139  1.000 124.73581 ?  153 PRO A CG  1 
ATOM   1148 C  CD  . PRO A 1 153 ? 4.46049   -25.87288 13.61569  1.000 113.84004 ?  153 PRO A CD  1 
ATOM   1149 N  N   . ASP A 1 154 ? 5.78942   -22.81493 15.39687  1.000 129.02918 ?  154 ASP A N   1 
ATOM   1150 C  CA  . ASP A 1 154 ? 6.51245   -21.89703 16.26223  1.000 137.31812 ?  154 ASP A CA  1 
ATOM   1151 C  C   . ASP A 1 154 ? 8.01129   -22.13490 16.13157  1.000 136.17410 ?  154 ASP A C   1 
ATOM   1152 O  O   . ASP A 1 154 ? 8.46123   -23.11563 15.53126  1.000 129.88029 ?  154 ASP A O   1 
ATOM   1153 C  CB  . ASP A 1 154 ? 6.07147   -22.06716 17.71746  1.000 136.09174 ?  154 ASP A CB  1 
ATOM   1154 C  CG  . ASP A 1 154 ? 5.89156   -23.52037 18.08632  1.000 137.18189 ?  154 ASP A CG  1 
ATOM   1155 O  OD1 . ASP A 1 154 ? 6.91467   -24.21270 18.25932  1.000 136.94115 ?  154 ASP A OD1 1 
ATOM   1156 O  OD2 . ASP A 1 154 ? 4.72924   -23.97534 18.17070  1.000 135.51919 ?  154 ASP A OD2 1 
ATOM   1157 N  N   . GLU A 1 155 ? 8.78923   -21.21408 16.70906  1.000 136.70961 ?  155 GLU A N   1 
ATOM   1158 C  CA  . GLU A 1 155 ? 10.23713  -21.38345 16.73771  1.000 136.67562 ?  155 GLU A CA  1 
ATOM   1159 C  C   . GLU A 1 155 ? 10.64103  -22.56439 17.61092  1.000 140.98637 ?  155 GLU A C   1 
ATOM   1160 O  O   . GLU A 1 155 ? 11.65762  -23.21412 17.33919  1.000 136.34320 ?  155 GLU A O   1 
ATOM   1161 C  CB  . GLU A 1 155 ? 10.90972  -20.10321 17.23431  1.000 133.48205 ?  155 GLU A CB  1 
ATOM   1162 C  CG  . GLU A 1 155 ? 12.33296  -20.31097 17.72489  1.000 134.17781 ?  155 GLU A CG  1 
ATOM   1163 C  CD  . GLU A 1 155 ? 13.37770  -20.25282 16.61839  1.000 133.55956 ?  155 GLU A CD  1 
ATOM   1164 O  OE1 . GLU A 1 155 ? 13.03301  -20.52095 15.43306  1.000 122.84331 ?  155 GLU A OE1 1 
ATOM   1165 O  OE2 . GLU A 1 155 ? 14.54725  -19.93268 16.95656  1.000 125.84129 ?  155 GLU A OE2 1 
ATOM   1166 N  N   . GLU A 1 156 ? 9.85823   -22.86319 18.65220  1.000 153.90029 ?  156 GLU A N   1 
ATOM   1167 C  CA  . GLU A 1 156 ? 10.14116  -24.03663 19.47364  1.000 152.54667 ?  156 GLU A CA  1 
ATOM   1168 C  C   . GLU A 1 156 ? 10.05447  -25.32151 18.65764  1.000 150.31595 ?  156 GLU A C   1 
ATOM   1169 O  O   . GLU A 1 156 ? 10.94610  -26.17633 18.73306  1.000 147.42654 ?  156 GLU A O   1 
ATOM   1170 C  CB  . GLU A 1 156 ? 9.17775   -24.09092 20.65582  1.000 158.33222 ?  156 GLU A CB  1 
ATOM   1171 C  CG  . GLU A 1 156 ? 9.84101   -23.84919 22.00558  1.000 179.89877 ?  156 GLU A CG  1 
ATOM   1172 C  CD  . GLU A 1 156 ? 10.73582  -22.61310 22.01708  1.000 186.95274 ?  156 GLU A CD  1 
ATOM   1173 O  OE1 . GLU A 1 156 ? 11.76192  -22.59935 21.29725  1.000 181.77735 ?  156 GLU A OE1 1 
ATOM   1174 O  OE2 . GLU A 1 156 ? 10.40627  -21.64963 22.74454  1.000 196.19325 ?  156 GLU A OE2 1 
ATOM   1175 N  N   . THR A 1 157 ? 8.98570   -25.47526 17.87089  1.000 135.94177 ?  157 THR A N   1 
ATOM   1176 C  CA  . THR A 1 157 ? 8.83121   -26.66876 17.04616  1.000 129.49710 ?  157 THR A CA  1 
ATOM   1177 C  C   . THR A 1 157 ? 9.98142   -26.81554 16.05927  1.000 124.16748 ?  157 THR A C   1 
ATOM   1178 O  O   . THR A 1 157 ? 10.45459  -27.93104 15.81564  1.000 114.72664 ?  157 THR A O   1 
ATOM   1179 C  CB  . THR A 1 157 ? 7.49893   -26.62102 16.30623  1.000 125.26283 ?  157 THR A CB  1 
ATOM   1180 O  OG1 . THR A 1 157 ? 6.43808   -26.49213 17.25751  1.000 129.31630 ?  157 THR A OG1 1 
ATOM   1181 C  CG2 . THR A 1 157 ? 7.29798   -27.88520 15.48841  1.000 108.95569 ?  157 THR A CG2 1 
ATOM   1182 N  N   . MET A 1 158 ? 10.44493  -25.70314 15.48217  1.000 120.10811 ?  158 MET A N   1 
ATOM   1183 C  CA  . MET A 1 158 ? 11.58506  -25.75444 14.56970  1.000 113.54120 ?  158 MET A CA  1 
ATOM   1184 C  C   . MET A 1 158 ? 12.82651  -26.30086 15.26975  1.000 118.20263 ?  158 MET A C   1 
ATOM   1185 O  O   . MET A 1 158 ? 13.46202  -27.24176 14.77992  1.000 110.01360 ?  158 MET A O   1 
ATOM   1186 C  CB  . MET A 1 158 ? 11.85953  -24.36862 13.97620  1.000 111.52387 ?  158 MET A CB  1 
ATOM   1187 C  CG  . MET A 1 158 ? 11.13809  -24.08279 12.65592  1.000 119.09100 ?  158 MET A CG  1 
ATOM   1188 S  SD  . MET A 1 158 ? 11.82700  -24.94686 11.21025  1.000 101.76186 ?  158 MET A SD  1 
ATOM   1189 C  CE  . MET A 1 158 ? 13.57845  -24.82150 11.63108  1.000 105.75921 ?  158 MET A CE  1 
ATOM   1190 N  N   . GLU A 1 159 ? 13.20324  -25.70754 16.41213  1.000 119.38476 ?  159 GLU A N   1 
ATOM   1191 C  CA  . GLU A 1 159 ? 14.31023  -26.25419 17.19384  1.000 118.95984 ?  159 GLU A CA  1 
ATOM   1192 C  C   . GLU A 1 159 ? 14.09868  -27.73976 17.45194  1.000 117.51186 ?  159 GLU A C   1 
ATOM   1193 O  O   . GLU A 1 159 ? 14.96930  -28.56785 17.16086  1.000 116.71569 ?  159 GLU A O   1 
ATOM   1194 C  CB  . GLU A 1 159 ? 14.45578  -25.49953 18.52390  1.000 128.39254 ?  159 GLU A CB  1 
ATOM   1195 C  CG  . GLU A 1 159 ? 14.91161  -24.04771 18.40127  1.000 122.43526 ?  159 GLU A CG  1 
ATOM   1196 C  CD  . GLU A 1 159 ? 16.20484  -23.91143 17.61874  1.000 124.61834 ?  159 GLU A CD  1 
ATOM   1197 O  OE1 . GLU A 1 159 ? 16.94939  -24.91967 17.52686  1.000 116.30786 ?  159 GLU A OE1 1 
ATOM   1198 O  OE2 . GLU A 1 159 ? 16.46265  -22.80024 17.09238  1.000 126.78223 ?  159 GLU A OE2 1 
ATOM   1199 N  N   . ARG A 1 160 ? 12.93757  -28.08155 18.01742  1.000 117.09307 ?  160 ARG A N   1 
ATOM   1200 C  CA  . ARG A 1 160 ? 12.48478  -29.46201 18.14729  1.000 117.29237 ?  160 ARG A CA  1 
ATOM   1201 C  C   . ARG A 1 160 ? 12.81293  -30.28560 16.90158  1.000 113.25351 ?  160 ARG A C   1 
ATOM   1202 O  O   . ARG A 1 160 ? 13.41612  -31.36108 16.98640  1.000 110.61776 ?  160 ARG A O   1 
ATOM   1203 C  CB  . ARG A 1 160 ? 10.97656  -29.43749 18.41061  1.000 123.01742 ?  160 ARG A CB  1 
ATOM   1204 C  CG  . ARG A 1 160 ? 10.36417  -30.66007 19.05803  1.000 127.80460 ?  160 ARG A CG  1 
ATOM   1205 C  CD  . ARG A 1 160 ? 8.90907   -30.34133 19.41140  1.000 136.12263 ?  160 ARG A CD  1 
ATOM   1206 N  NE  . ARG A 1 160 ? 8.79945   -29.01278 20.01159  1.000 135.37473 ?  160 ARG A NE  1 
ATOM   1207 C  CZ  . ARG A 1 160 ? 7.69448   -28.49853 20.54033  1.000 145.52711 ?  160 ARG A CZ  1 
ATOM   1208 N  NH1 . ARG A 1 160 ? 6.55757   -29.17417 20.56349  1.000 152.74050 ?  160 ARG A NH1 1 
ATOM   1209 N  NH2 . ARG A 1 160 ? 7.73419   -27.27635 21.06913  1.000 150.57381 ?  160 ARG A NH2 1 
ATOM   1210 N  N   . ILE A 1 161 ? 12.42325  -29.78393 15.72980  1.000 107.45620 ?  161 ILE A N   1 
ATOM   1211 C  CA  . ILE A 1 161 ? 12.69235  -30.49932 14.48435  1.000 110.64119 ?  161 ILE A CA  1 
ATOM   1212 C  C   . ILE A 1 161 ? 14.18844  -30.55359 14.20021  1.000 106.36767 ?  161 ILE A C   1 
ATOM   1213 O  O   . ILE A 1 161 ? 14.71743  -31.57796 13.74667  1.000 98.06339  ?  161 ILE A O   1 
ATOM   1214 C  CB  . ILE A 1 161 ? 11.92862  -29.83651 13.32291  1.000 105.08238 ?  161 ILE A CB  1 
ATOM   1215 C  CG1 . ILE A 1 161 ? 10.47403  -30.30961 13.27834  1.000 95.05149  ?  161 ILE A CG1 1 
ATOM   1216 C  CG2 . ILE A 1 161 ? 12.64844  -30.07086 12.01027  1.000 98.10703  ?  161 ILE A CG2 1 
ATOM   1217 C  CD1 . ILE A 1 161 ? 9.51131   -29.20767 12.91331  1.000 96.43800  ?  161 ILE A CD1 1 
ATOM   1218 N  N   . MET A 1 162 ? 14.88456  -29.44109 14.42113  1.000 105.56168 ?  162 MET A N   1 
ATOM   1219 C  CA  . MET A 1 162 ? 16.31563  -29.40700 14.16376  1.000 104.33456 ?  162 MET A CA  1 
ATOM   1220 C  C   . MET A 1 162 ? 17.06032  -30.34449 15.10443  1.000 105.70673 ?  162 MET A C   1 
ATOM   1221 O  O   . MET A 1 162 ? 17.99852  -31.03470 14.68825  1.000 103.24270 ?  162 MET A O   1 
ATOM   1222 C  CB  . MET A 1 162 ? 16.82800  -27.97219 14.29943  1.000 110.69037 ?  162 MET A CB  1 
ATOM   1223 C  CG  . MET A 1 162 ? 16.26867  -26.99514 13.25470  1.000 105.14028 ?  162 MET A CG  1 
ATOM   1224 S  SD  . MET A 1 162 ? 16.95171  -27.23436 11.60306  1.000 95.74116  ?  162 MET A SD  1 
ATOM   1225 C  CE  . MET A 1 162 ? 18.71194  -27.04787 11.91802  1.000 95.27210  ?  162 MET A CE  1 
ATOM   1226 N  N   . ARG A 1 163 ? 16.66347  -30.37871 16.37716  1.000 106.51619 ?  163 ARG A N   1 
ATOM   1227 C  CA  . ARG A 1 163 ? 17.23540  -31.35952 17.29280  1.000 111.35920 ?  163 ARG A CA  1 
ATOM   1228 C  C   . ARG A 1 163 ? 17.15790  -32.75790 16.69146  1.000 107.76529 ?  163 ARG A C   1 
ATOM   1229 O  O   . ARG A 1 163 ? 18.16539  -33.47310 16.61508  1.000 107.57407 ?  163 ARG A O   1 
ATOM   1230 C  CB  . ARG A 1 163 ? 16.51948  -31.31017 18.64597  1.000 115.03207 ?  163 ARG A CB  1 
ATOM   1231 C  CG  . ARG A 1 163 ? 17.26998  -30.52721 19.71938  1.000 127.58278 ?  163 ARG A CG  1 
ATOM   1232 C  CD  . ARG A 1 163 ? 16.53244  -30.52443 21.05927  1.000 129.71842 ?  163 ARG A CD  1 
ATOM   1233 N  NE  . ARG A 1 163 ? 15.18662  -29.96420 20.95997  1.000 129.73477 ?  163 ARG A NE  1 
ATOM   1234 C  CZ  . ARG A 1 163 ? 14.90826  -28.66570 20.93175  1.000 133.51053 ?  163 ARG A CZ  1 
ATOM   1235 N  NH1 . ARG A 1 163 ? 15.86690  -27.75188 20.98397  1.000 132.55596 ?  163 ARG A NH1 1 
ATOM   1236 N  NH2 . ARG A 1 163 ? 13.63637  -28.27409 20.83841  1.000 130.59316 ?  163 ARG A NH2 1 
ATOM   1237 N  N   . GLU A 1 164 ? 15.96850  -33.15661 16.23185  1.000 101.92769 ?  164 GLU A N   1 
ATOM   1238 C  CA  . GLU A 1 164 ? 15.80580  -34.51778 15.73245  1.000 104.07307 ?  164 GLU A CA  1 
ATOM   1239 C  C   . GLU A 1 164 ? 16.65711  -34.74648 14.48860  1.000 101.54483 ?  164 GLU A C   1 
ATOM   1240 O  O   . GLU A 1 164 ? 17.34189  -35.77162 14.37870  1.000 95.02760  ?  164 GLU A O   1 
ATOM   1241 C  CB  . GLU A 1 164 ? 14.32740  -34.81944 15.46464  1.000 103.65443 ?  164 GLU A CB  1 
ATOM   1242 C  CG  . GLU A 1 164 ? 13.56807  -35.24391 16.71209  1.000 112.70123 ?  164 GLU A CG  1 
ATOM   1243 C  CD  . GLU A 1 164 ? 14.17732  -36.47078 17.36601  1.000 114.61675 ?  164 GLU A CD  1 
ATOM   1244 O  OE1 . GLU A 1 164 ? 14.72207  -37.31763 16.62795  1.000 123.40143 ?  164 GLU A OE1 1 
ATOM   1245 O  OE2 . GLU A 1 164 ? 14.12348  -36.58637 18.60394  1.000 117.87998 ?  164 GLU A OE2 1 
ATOM   1246 N  N   . LEU A 1 165 ? 16.64321  -33.78513 13.55020  1.000 97.29918  ?  165 LEU A N   1 
ATOM   1247 C  CA  . LEU A 1 165 ? 17.49336  -33.87477 12.36525  1.000 92.78306  ?  165 LEU A CA  1 
ATOM   1248 C  C   . LEU A 1 165 ? 18.96952  -33.99143 12.73345  1.000 96.40609  ?  165 LEU A C   1 
ATOM   1249 O  O   . LEU A 1 165 ? 19.72430  -34.71821 12.07425  1.000 94.90891  ?  165 LEU A O   1 
ATOM   1250 C  CB  . LEU A 1 165 ? 17.27535  -32.66253 11.46940  1.000 87.89014  ?  165 LEU A CB  1 
ATOM   1251 C  CG  . LEU A 1 165 ? 15.93530  -32.62161 10.73637  1.000 85.80194  ?  165 LEU A CG  1 
ATOM   1252 C  CD1 . LEU A 1 165 ? 15.81940  -31.35242 9.93235   1.000 74.36372  ?  165 LEU A CD1 1 
ATOM   1253 C  CD2 . LEU A 1 165 ? 15.80245  -33.82136 9.84016   1.000 80.14383  ?  165 LEU A CD2 1 
ATOM   1254 N  N   . LYS A 1 166 ? 19.41155  -33.27553 13.77029  1.000 92.48224  ?  166 LYS A N   1 
ATOM   1255 C  CA  . LYS A 1 166 ? 20.82487  -33.34140 14.12073  1.000 95.71178  ?  166 LYS A CA  1 
ATOM   1256 C  C   . LYS A 1 166 ? 21.17677  -34.68447 14.74333  1.000 99.41035  ?  166 LYS A C   1 
ATOM   1257 O  O   . LYS A 1 166 ? 22.16268  -35.31381 14.34633  1.000 99.51709  ?  166 LYS A O   1 
ATOM   1258 C  CB  . LYS A 1 166 ? 21.21186  -32.19984 15.06826  1.000 105.02700 ?  166 LYS A CB  1 
ATOM   1259 C  CG  . LYS A 1 166 ? 22.71424  -32.16326 15.43370  1.000 104.37625 ?  166 LYS A CG  1 
ATOM   1260 C  CD  . LYS A 1 166 ? 23.28574  -30.74537 15.42790  1.000 105.92794 ?  166 LYS A CD  1 
ATOM   1261 C  CE  . LYS A 1 166 ? 24.69177  -30.72374 16.02816  1.000 111.45715 ?  166 LYS A CE  1 
ATOM   1262 N  NZ  . LYS A 1 166 ? 25.12545  -29.35941 16.44923  1.000 115.46842 ?  166 LYS A NZ  1 
ATOM   1263 N  N   . LYS A 1 167 ? 20.38536  -35.15370 15.70909  1.000 103.15827 ?  167 LYS A N   1 
ATOM   1264 C  CA  . LYS A 1 167 ? 20.77791  -36.39031 16.37094  1.000 107.84923 ?  167 LYS A CA  1 
ATOM   1265 C  C   . LYS A 1 167 ? 20.62575  -37.59940 15.45398  1.000 104.79273 ?  167 LYS A C   1 
ATOM   1266 O  O   . LYS A 1 167 ? 21.34321  -38.58759 15.62907  1.000 107.93407 ?  167 LYS A O   1 
ATOM   1267 C  CB  . LYS A 1 167 ? 20.02848  -36.56271 17.69701  1.000 113.98453 ?  167 LYS A CB  1 
ATOM   1268 C  CG  . LYS A 1 167 ? 18.57256  -37.00122 17.71489  1.000 113.58871 ?  167 LYS A CG  1 
ATOM   1269 C  CD  . LYS A 1 167 ? 18.19037  -37.20320 19.21082  1.000 128.47540 ?  167 LYS A CD  1 
ATOM   1270 C  CE  . LYS A 1 167 ? 16.72775  -37.57822 19.46110  1.000 130.28522 ?  167 LYS A CE  1 
ATOM   1271 N  NZ  . LYS A 1 167 ? 16.50145  -39.04380 19.58520  1.000 126.89563 ?  167 LYS A NZ  1 
ATOM   1272 N  N   . LYS A 1 168 ? 19.74953  -37.52863 14.44247  1.000 99.26730  ?  168 LYS A N   1 
ATOM   1273 C  CA  . LYS A 1 168 ? 19.76129  -38.53706 13.38218  1.000 99.66433  ?  168 LYS A CA  1 
ATOM   1274 C  C   . LYS A 1 168 ? 20.96651  -38.40225 12.44704  1.000 94.79177  ?  168 LYS A C   1 
ATOM   1275 O  O   . LYS A 1 168 ? 21.24972  -39.34151 11.69986  1.000 92.74729  ?  168 LYS A O   1 
ATOM   1276 C  CB  . LYS A 1 168 ? 18.45678  -38.48319 12.56356  1.000 98.98053  ?  168 LYS A CB  1 
ATOM   1277 C  CG  . LYS A 1 168 ? 17.21703  -39.09300 13.24406  1.000 104.18902 ?  168 LYS A CG  1 
ATOM   1278 C  CD  . LYS A 1 168 ? 16.01532  -39.19644 12.27540  1.000 103.78809 ?  168 LYS A CD  1 
ATOM   1279 C  CE  . LYS A 1 168 ? 14.98217  -40.25089 12.72161  1.000 108.10333 ?  168 LYS A CE  1 
ATOM   1280 N  NZ  . LYS A 1 168 ? 14.55896  -40.11563 14.15913  1.000 113.61406 ?  168 LYS A NZ  1 
ATOM   1281 N  N   . GLY A 1 169 ? 21.69170  -37.28434 12.47575  1.000 97.50570  ?  169 GLY A N   1 
ATOM   1282 C  CA  . GLY A 1 169 ? 22.88388  -37.14778 11.66013  1.000 95.90243  ?  169 GLY A CA  1 
ATOM   1283 C  C   . GLY A 1 169 ? 22.63622  -36.60380 10.27392  1.000 89.76681  ?  169 GLY A C   1 
ATOM   1284 O  O   . GLY A 1 169 ? 23.35944  -36.95821 9.33574   1.000 90.09263  ?  169 GLY A O   1 
ATOM   1285 N  N   . PHE A 1 170 ? 21.63130  -35.75154 10.10978  1.000 85.10083  ?  170 PHE A N   1 
ATOM   1286 C  CA  . PHE A 1 170 ? 21.31691  -35.17299 8.81230   1.000 90.57683  ?  170 PHE A CA  1 
ATOM   1287 C  C   . PHE A 1 170 ? 21.83312  -33.75182 8.64451   1.000 89.61201  ?  170 PHE A C   1 
ATOM   1288 O  O   . PHE A 1 170 ? 21.93688  -33.27639 7.50727   1.000 90.78143  ?  170 PHE A O   1 
ATOM   1289 C  CB  . PHE A 1 170 ? 19.79969  -35.16778 8.58677   1.000 84.63392  ?  170 PHE A CB  1 
ATOM   1290 C  CG  . PHE A 1 170 ? 19.21350  -36.52185 8.29719   1.000 90.02560  ?  170 PHE A CG  1 
ATOM   1291 C  CD1 . PHE A 1 170 ? 19.74673  -37.33143 7.29953   1.000 90.05703  ?  170 PHE A CD1 1 
ATOM   1292 C  CD2 . PHE A 1 170 ? 18.11269  -36.97936 9.01350   1.000 91.72970  ?  170 PHE A CD2 1 
ATOM   1293 C  CE1 . PHE A 1 170 ? 19.19364  -38.56893 7.01758   1.000 84.07972  ?  170 PHE A CE1 1 
ATOM   1294 C  CE2 . PHE A 1 170 ? 17.54481  -38.22166 8.73786   1.000 91.66183  ?  170 PHE A CE2 1 
ATOM   1295 C  CZ  . PHE A 1 170 ? 18.09231  -39.01836 7.73733   1.000 85.64524  ?  170 PHE A CZ  1 
ATOM   1296 N  N   . LEU A 1 171 ? 22.13914  -33.06076 9.73316   1.000 88.21662  ?  171 LEU A N   1 
ATOM   1297 C  CA  . LEU A 1 171 ? 22.46666  -31.64904 9.65444   1.000 94.83432  ?  171 LEU A CA  1 
ATOM   1298 C  C   . LEU A 1 171 ? 23.88335  -31.43287 9.14524   1.000 101.20725 ?  171 LEU A C   1 
ATOM   1299 O  O   . LEU A 1 171 ? 24.80814  -32.19597 9.45058   1.000 86.63636  ?  171 LEU A O   1 
ATOM   1300 C  CB  . LEU A 1 171 ? 22.30679  -30.98469 11.02325  1.000 100.19340 ?  171 LEU A CB  1 
ATOM   1301 C  CG  . LEU A 1 171 ? 20.84536  -30.67542 11.30746  1.000 95.45337  ?  171 LEU A CG  1 
ATOM   1302 C  CD1 . LEU A 1 171 ? 20.70261  -29.64892 12.41967  1.000 89.74816  ?  171 LEU A CD1 1 
ATOM   1303 C  CD2 . LEU A 1 171 ? 20.21975  -30.20079 10.01258  1.000 79.88917  ?  171 LEU A CD2 1 
ATOM   1304 N  N   . ILE A 1 172 ? 24.03489  -30.38693 8.34503   1.000 98.84960  ?  172 ILE A N   1 
ATOM   1305 C  CA  . ILE A 1 172 ? 25.33593  -29.81855 8.03848   1.000 100.23926 ?  172 ILE A CA  1 
ATOM   1306 C  C   . ILE A 1 172 ? 25.65412  -28.83897 9.15867   1.000 108.35291 ?  172 ILE A C   1 
ATOM   1307 O  O   . ILE A 1 172 ? 24.97053  -27.82517 9.32290   1.000 112.17679 ?  172 ILE A O   1 
ATOM   1308 C  CB  . ILE A 1 172 ? 25.32766  -29.13961 6.66674   1.000 97.76362  ?  172 ILE A CB  1 
ATOM   1309 C  CG1 . ILE A 1 172 ? 25.24976  -30.20710 5.57658   1.000 93.47270  ?  172 ILE A CG1 1 
ATOM   1310 C  CG2 . ILE A 1 172 ? 26.54468  -28.28106 6.48728   1.000 106.21463 ?  172 ILE A CG2 1 
ATOM   1311 C  CD1 . ILE A 1 172 ? 26.25072  -31.32482 5.79259   1.000 105.49755 ?  172 ILE A CD1 1 
ATOM   1312 N  N   . GLU A 1 173 ? 26.66846  -29.15495 9.95335   1.000 117.66440 ?  173 GLU A N   1 
ATOM   1313 C  CA  . GLU A 1 173 ? 27.00096  -28.31513 11.08976  1.000 121.84176 ?  173 GLU A CA  1 
ATOM   1314 C  C   . GLU A 1 173 ? 28.47309  -27.93305 11.07016  1.000 124.16312 ?  173 GLU A C   1 
ATOM   1315 O  O   . GLU A 1 173 ? 28.84275  -26.92391 10.47095  1.000 129.13101 ?  173 GLU A O   1 
ATOM   1316 C  CB  . GLU A 1 173 ? 26.63538  -29.02392 12.39837  1.000 124.24178 ?  173 GLU A CB  1 
ATOM   1317 C  CG  . GLU A 1 173 ? 25.13538  -29.03678 12.71052  1.000 120.54055 ?  173 GLU A CG  1 
ATOM   1318 C  CD  . GLU A 1 173 ? 24.57031  -27.64869 12.99497  1.000 123.16828 ?  173 GLU A CD  1 
ATOM   1319 O  OE1 . GLU A 1 173 ? 25.01070  -27.01946 13.97744  1.000 133.80387 ?  173 GLU A OE1 1 
ATOM   1320 O  OE2 . GLU A 1 173 ? 23.68855  -27.18425 12.23985  1.000 124.15534 ?  173 GLU A OE2 1 
HETATM 1321 FE FE  . FE2 B 2 .   ? 16.62069  -34.24841 2.17660   1.000 61.43463  ?  201 FE2 A FE  1 
HETATM 1322 N  N   . NIO C 3 .   ? 15.25274  -34.75154 0.28125   1.000 61.95148  ?  202 NIO A N   1 
HETATM 1323 C  C1  . NIO C 3 .   ? 15.88603  -34.60256 -0.90345  1.000 66.48039  ?  202 NIO A C1  1 
HETATM 1324 C  C2  . NIO C 3 .   ? 15.17783  -34.74351 -2.08360  1.000 65.64612  ?  202 NIO A C2  1 
HETATM 1325 C  C3  . NIO C 3 .   ? 13.84557  -35.02289 -2.01450  1.000 63.82722  ?  202 NIO A C3  1 
HETATM 1326 C  C4  . NIO C 3 .   ? 13.21916  -35.16206 -0.79979  1.000 69.23117  ?  202 NIO A C4  1 
HETATM 1327 C  C5  . NIO C 3 .   ? 13.94291  -35.01560 0.37881   1.000 61.90183  ?  202 NIO A C5  1 
HETATM 1328 C  C6  . NIO C 3 .   ? 15.84607  -34.56901 -3.45069  1.000 67.62366  ?  202 NIO A C6  1 
HETATM 1329 O  O1  . NIO C 3 .   ? 17.09616  -34.62209 -3.59849  1.000 69.46180  ?  202 NIO A O1  1 
HETATM 1330 O  O2  . NIO C 3 .   ? 15.12616  -34.33993 -4.45666  1.000 73.03916  -1 202 NIO A O2  1 
HETATM 1331 H  H1  . NIO C 3 .   ? 16.79475  -34.40597 -0.92526  1.000 79.90337  ?  202 NIO A H1  1 
HETATM 1332 H  H3  . NIO C 3 .   ? 13.35503  -35.12040 -2.79856  1.000 76.71957  ?  202 NIO A H3  1 
HETATM 1333 H  H4  . NIO C 3 .   ? 12.30993  -35.35446 -0.76545  1.000 83.20431  ?  202 NIO A H4  1 
HETATM 1334 H  H5  . NIO C 3 .   ? 13.53069  -35.09835 1.20834   1.000 74.40910  ?  202 NIO A H5  1 
HETATM 1335 N  N   . PRO D 4 .   ? -14.85024 -18.39836 19.20734  1.000 110.13966 ?  203 PRO A N   1 
HETATM 1336 C  CA  . PRO D 4 .   ? -14.97679 -16.97807 18.83748  1.000 109.80244 ?  203 PRO A CA  1 
HETATM 1337 C  C   . PRO D 4 .   ? -16.13705 -16.24847 19.51873  1.000 108.63462 ?  203 PRO A C   1 
HETATM 1338 O  O   . PRO D 4 .   ? -16.90512 -16.80531 20.30836  1.000 107.46404 ?  203 PRO A O   1 
HETATM 1339 C  CB  . PRO D 4 .   ? -15.20707 -17.03195 17.32888  1.000 100.52589 ?  203 PRO A CB  1 
HETATM 1340 C  CG  . PRO D 4 .   ? -15.85650 -18.36590 17.11308  1.000 99.78911  ?  203 PRO A CG  1 
HETATM 1341 C  CD  . PRO D 4 .   ? -15.18700 -19.29444 18.08770  1.000 98.12185  ?  203 PRO A CD  1 
HETATM 1342 O  OXT . PRO D 4 .   ? -16.33349 -15.05760 19.28051  1.000 110.36803 ?  203 PRO A OXT 1 
HETATM 1343 O  O   . HOH E 5 .   ? -32.34096 -22.00555 5.16547   1.000 63.67234  ?  301 HOH A O   1 
HETATM 1344 O  O   . HOH E 5 .   ? -32.70619 -15.06513 1.34536   1.000 60.51248  ?  302 HOH A O   1 
HETATM 1345 O  O   . HOH E 5 .   ? 14.17580  -43.88523 -8.43580  1.000 88.64293  ?  303 HOH A O   1 
HETATM 1346 O  O   . HOH E 5 .   ? 29.582    -21.958   -9.832    1.000 65.02822  ?  304 HOH A O   1 
HETATM 1347 O  O   . HOH E 5 .   ? -31.53625 -24.14021 16.53184  1.000 79.06800  ?  305 HOH A O   1 
HETATM 1348 O  O   . HOH E 5 .   ? 19.825    -22.151   -13.745   1.000 57.04609  ?  306 HOH A O   1 
HETATM 1349 O  O   . HOH E 5 .   ? -24.33901 -19.34698 0.63242   1.000 75.04340  ?  307 HOH A O   1 
HETATM 1350 O  O   . HOH E 5 .   ? -26.78397 -20.12124 0.79753   1.000 70.80873  ?  308 HOH A O   1 
HETATM 1351 O  O   . HOH E 5 .   ? -32.29184 -18.93753 4.38727   1.000 56.63557  ?  309 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . VAL A 6   ? 1.69756 1.13568 0.54445 0.36334  -0.15784 -0.11308 6   VAL A N   
2    C CA  . VAL A 6   ? 1.72060 1.20497 0.69826 0.36088  -0.09556 -0.07027 6   VAL A CA  
3    C C   . VAL A 6   ? 1.71032 1.20510 0.80444 0.28037  -0.11864 -0.07346 6   VAL A C   
4    O O   . VAL A 6   ? 1.57124 1.14524 0.78830 0.25873  -0.08862 -0.03456 6   VAL A O   
5    C CB  . VAL A 6   ? 1.73521 1.15174 0.66518 0.41362  -0.04857 -0.07287 6   VAL A CB  
6    C CG1 . VAL A 6   ? 1.57835 1.04403 0.65503 0.38594  -0.00647 -0.03289 6   VAL A CG1 
7    C CG2 . VAL A 6   ? 1.63644 1.07259 0.48878 0.50349  -0.00177 -0.04698 6   VAL A CG2 
8    N N   . ARG A 7   ? 1.74741 1.15295 0.79830 0.24004  -0.16817 -0.11882 7   ARG A N   
9    C CA  . ARG A 7   ? 1.68644 1.11109 0.84462 0.16449  -0.19302 -0.11514 7   ARG A CA  
10   C C   . ARG A 7   ? 1.62056 1.14087 0.84954 0.12343  -0.22389 -0.09260 7   ARG A C   
11   O O   . ARG A 7   ? 1.47719 1.06688 0.82347 0.08810  -0.20762 -0.06249 7   ARG A O   
12   C CB  . ARG A 7   ? 1.75305 1.06308 0.85698 0.12768  -0.24381 -0.15984 7   ARG A CB  
13   C CG  . ARG A 7   ? 1.79185 1.13843 1.01350 0.05010  -0.26965 -0.14417 7   ARG A CG  
14   C CD  . ARG A 7   ? 1.83836 1.08166 1.02859 0.00032  -0.33004 -0.17762 7   ARG A CD  
15   N NE  . ARG A 7   ? 1.92311 1.13163 1.16702 -0.01285 -0.30256 -0.16717 7   ARG A NE  
16   C CZ  . ARG A 7   ? 1.82339 1.10994 1.18818 -0.05311 -0.28583 -0.12926 7   ARG A CZ  
17   N NH1 . ARG A 7   ? 1.65551 1.05562 1.10512 -0.08070 -0.28695 -0.09799 7   ARG A NH1 
18   N NH2 . ARG A 7   ? 1.81699 1.06789 1.21310 -0.05954 -0.26401 -0.11967 7   ARG A NH2 
19   N N   . GLN A 8   ? 1.74726 1.27575 0.90133 0.13305  -0.26657 -0.10382 8   GLN A N   
20   C CA  . GLN A 8   ? 1.66651 1.29914 0.89241 0.09942  -0.29659 -0.07214 8   GLN A CA  
21   C C   . GLN A 8   ? 1.51625 1.25339 0.83654 0.13132  -0.23126 -0.01788 8   GLN A C   
22   O O   . GLN A 8   ? 1.40823 1.22846 0.83545 0.10122  -0.22887 0.01708  8   GLN A O   
23   C CB  . GLN A 8   ? 1.78771 1.41023 0.90276 0.10567  -0.36072 -0.09347 8   GLN A CB  
24   C CG  . GLN A 8   ? 1.98424 1.52873 1.05162 0.03971  -0.45143 -0.13702 8   GLN A CG  
25   C CD  . GLN A 8   ? 2.05935 1.46232 1.07497 0.03206  -0.45049 -0.18399 8   GLN A CD  
26   O OE1 . GLN A 8   ? 1.93384 1.33273 1.04675 -0.01758 -0.44971 -0.17312 8   GLN A OE1 
27   N NE2 . GLN A 8   ? 2.16420 1.46117 1.03958 0.08658  -0.44062 -0.22828 8   GLN A NE2 
28   N N   . GLU A 9   ? 1.47375 1.20528 0.76006 0.19409  -0.17552 -0.00594 9   GLU A N   
29   C CA  . GLU A 9   ? 1.37018 1.18422 0.75021 0.21988  -0.11648 0.04626  9   GLU A CA  
30   C C   . GLU A 9   ? 1.28384 1.09814 0.76848 0.18994  -0.07977 0.05523  9   GLU A C   
31   O O   . GLU A 9   ? 1.10311 0.97676 0.68071 0.18237  -0.05264 0.08762  9   GLU A O   
32   C CB  . GLU A 9   ? 1.34116 1.15690 0.66539 0.29186  -0.07103 0.06713  9   GLU A CB  
33   C CG  . GLU A 9   ? 1.45557 1.32473 0.71708 0.32989  -0.08857 0.08717  9   GLU A CG  
34   C CD  . GLU A 9   ? 1.41209 1.38065 0.77707 0.31151  -0.08941 0.13288  9   GLU A CD  
35   O OE1 . GLU A 9   ? 1.42298 1.41432 0.90472 0.29041  -0.05332 0.15559  9   GLU A OE1 
36   O OE2 . GLU A 9   ? 1.50033 1.52211 0.82574 0.32018  -0.12663 0.14638  9   GLU A OE2 
37   N N   . ARG A 10  ? 1.33344 1.07821 0.79813 0.17505  -0.07903 0.02669  10  ARG A N   
38   C CA  . ARG A 10  ? 1.20715 0.95636 0.75837 0.14052  -0.05604 0.03228  10  ARG A CA  
39   C C   . ARG A 10  ? 1.17418 0.95980 0.78413 0.08935  -0.08549 0.03377  10  ARG A C   
40   O O   . ARG A 10  ? 1.04173 0.87039 0.73029 0.07761  -0.05702 0.05441  10  ARG A O   
41   C CB  . ARG A 10  ? 1.14687 0.82536 0.66628 0.13744  -0.05148 0.00992  10  ARG A CB  
42   C CG  . ARG A 10  ? 1.11470 0.80547 0.71338 0.10899  -0.02493 0.02037  10  ARG A CG  
43   C CD  . ARG A 10  ? 1.07516 0.71422 0.65249 0.11340  -0.01537 0.01239  10  ARG A CD  
44   N NE  . ARG A 10  ? 1.10064 0.67770 0.62917 0.09292  -0.05326 -0.01629 10  ARG A NE  
45   C CZ  . ARG A 10  ? 1.26102 0.76873 0.69862 0.12233  -0.06939 -0.03889 10  ARG A CZ  
46   N NH1 . ARG A 10  ? 1.43195 0.93429 0.81101 0.18032  -0.04659 -0.03327 10  ARG A NH1 
47   N NH2 . ARG A 10  ? 1.41280 0.84968 0.81347 0.09535  -0.10828 -0.06652 10  ARG A NH2 
48   N N   . LEU A 11  ? 1.20689 0.97467 0.77924 0.05990  -0.14249 0.01488  11  LEU A N   
49   C CA  . LEU A 11  ? 1.17087 0.99143 0.81376 0.01097  -0.17191 0.03099  11  LEU A CA  
50   C C   . LEU A 11  ? 1.22776 1.14574 0.93803 0.02607  -0.15119 0.07337  11  LEU A C   
51   O O   . LEU A 11  ? 1.16202 1.13088 0.95502 0.01238  -0.12610 0.09894  11  LEU A O   
52   C CB  . LEU A 11  ? 1.21973 1.00699 0.81487 -0.02705 -0.24661 0.00985  11  LEU A CB  
53   C CG  . LEU A 11  ? 1.37831 1.07283 0.94347 -0.06092 -0.27368 -0.02204 11  LEU A CG  
54   C CD1 . LEU A 11  ? 1.48284 1.12455 0.98850 -0.09805 -0.35449 -0.04791 11  LEU A CD1 
55   C CD2 . LEU A 11  ? 1.26375 0.99675 0.92829 -0.09874 -0.25557 0.00359  11  LEU A CD2 
56   N N   . LYS A 12  ? 1.15002 1.09520 0.82127 0.06055  -0.15811 0.08457  12  LYS A N   
57   C CA  . LYS A 12  ? 1.10607 1.14350 0.84502 0.08249  -0.13359 0.13246  12  LYS A CA  
58   C C   . LYS A 12  ? 1.05068 1.08794 0.85014 0.10772  -0.06213 0.14866  12  LYS A C   
59   O O   . LYS A 12  ? 1.08232 1.17228 0.95934 0.10860  -0.03531 0.17945  12  LYS A O   
60   C CB  . LYS A 12  ? 1.19539 1.26134 0.87508 0.12181  -0.14848 0.14605  12  LYS A CB  
61   C CG  . LYS A 12  ? 1.17477 1.29949 0.84138 0.09518  -0.21895 0.15840  12  LYS A CG  
62   C CD  . LYS A 12  ? 1.26851 1.41919 0.85617 0.14037  -0.23257 0.16946  12  LYS A CD  
63   C CE  . LYS A 12  ? 1.40258 1.64104 0.99786 0.11451  -0.30159 0.19711  12  LYS A CE  
64   N NZ  . LYS A 12  ? 1.47186 1.76409 1.00355 0.16483  -0.30832 0.22345  12  LYS A NZ  
65   N N   . SER A 13  ? 1.05534 1.03058 0.82052 0.12820  -0.03162 0.12960  13  SER A N   
66   C CA  . SER A 13  ? 1.08876 1.05572 0.90977 0.14403  0.02537  0.14350  13  SER A CA  
67   C C   . SER A 13  ? 1.02705 0.98094 0.89082 0.11041  0.03678  0.13013  13  SER A C   
68   O O   . SER A 13  ? 0.95623 0.91597 0.86913 0.12073  0.07640  0.14347  13  SER A O   
69   C CB  . SER A 13  ? 1.00127 0.91898 0.79006 0.16713  0.04902  0.13665  13  SER A CB  
70   O OG  . SER A 13  ? 1.06808 1.01499 0.83866 0.21142  0.06031  0.16657  13  SER A OG  
71   N N   . ILE A 14  ? 1.03147 0.96290 0.87249 0.07373  0.00452  0.10513  14  ILE A N   
72   C CA  . ILE A 14  ? 0.97758 0.90834 0.85452 0.04689  0.01791  0.09973  14  ILE A CA  
73   C C   . ILE A 14  ? 1.00937 1.01088 0.94698 0.05044  0.03056  0.13272  14  ILE A C   
74   O O   . ILE A 14  ? 0.98393 0.98702 0.95169 0.06449  0.07381  0.13907  14  ILE A O   
75   C CB  . ILE A 14  ? 0.96112 0.86187 0.81125 0.00849  -0.01895 0.07826  14  ILE A CB  
76   C CG1 . ILE A 14  ? 0.92401 0.75823 0.72999 0.01300  -0.01155 0.05338  14  ILE A CG1 
77   C CG2 . ILE A 14  ? 0.89617 0.82698 0.79088 -0.01780 -0.01022 0.08879  14  ILE A CG2 
78   C CD1 . ILE A 14  ? 0.98721 0.77697 0.75139 -0.00899 -0.04923 0.03443  14  ILE A CD1 
79   N N   . VAL A 15  ? 0.96927 1.02950 0.92293 0.04057  -0.00729 0.15612  15  VAL A N   
80   C CA  . VAL A 15  ? 0.98170 1.12988 1.00724 0.04965  0.00611  0.20269  15  VAL A CA  
81   C C   . VAL A 15  ? 0.99019 1.14503 1.04087 0.10076  0.06292  0.22284  15  VAL A C   
82   O O   . VAL A 15  ? 0.93923 1.10357 1.02789 0.12069  0.11044  0.23698  15  VAL A O   
83   C CB  . VAL A 15  ? 1.00254 1.21908 1.04220 0.02880  -0.05387 0.22974  15  VAL A CB  
84   C CG1 . VAL A 15  ? 0.92907 1.25768 1.06024 0.04128  -0.03827 0.29285  15  VAL A CG1 
85   C CG2 . VAL A 15  ? 1.00104 1.18770 1.01629 -0.02700 -0.11345 0.20649  15  VAL A CG2 
86   N N   . ARG A 16  ? 0.92906 1.07315 0.95435 0.12649  0.06091  0.22602  16  ARG A N   
87   C CA  . ARG A 16  ? 0.99015 1.13392 1.04582 0.17399  0.11233  0.25175  16  ARG A CA  
88   C C   . ARG A 16  ? 1.01208 1.08470 1.07568 0.18249  0.16418  0.22954  16  ARG A C   
89   O O   . ARG A 16  ? 1.01971 1.09686 1.12432 0.21547  0.21030  0.25257  16  ARG A O   
90   C CB  . ARG A 16  ? 0.96236 1.08566 0.97740 0.19529  0.10468  0.25218  16  ARG A CB  
91   C CG  . ARG A 16  ? 1.01207 1.17183 1.06635 0.24357  0.13853  0.30068  16  ARG A CG  
92   C CD  . ARG A 16  ? 1.03163 1.21925 1.03586 0.26118  0.10893  0.31417  16  ARG A CD  
93   N NE  . ARG A 16  ? 1.11523 1.24053 1.04302 0.24360  0.08516  0.26927  16  ARG A NE  
94   C CZ  . ARG A 16  ? 1.16542 1.29908 1.01779 0.25406  0.04999  0.26307  16  ARG A CZ  
95   N NH1 . ARG A 16  ? 1.15460 1.35988 0.99083 0.27347  0.02374  0.29456  16  ARG A NH1 
96   N NH2 . ARG A 16  ? 1.07222 1.14106 0.85782 0.24894  0.04144  0.22580  16  ARG A NH2 
97   N N   . ILE A 17  ? 0.99683 0.99976 1.01668 0.15438  0.15571  0.18478  17  ILE A N   
98   C CA  . ILE A 17  ? 1.07184 1.00217 1.08543 0.15529  0.19277  0.15815  17  ILE A CA  
99   C C   . ILE A 17  ? 1.02943 0.97671 1.05603 0.15843  0.21694  0.15889  17  ILE A C   
100  O O   . ILE A 17  ? 0.89179 0.78724 0.91471 0.18104  0.26005  0.14779  17  ILE A O   
101  C CB  . ILE A 17  ? 1.06768 0.94056 1.03633 0.12196  0.17003  0.11968  17  ILE A CB  
102  C CG1 . ILE A 17  ? 1.10291 0.96732 1.06239 0.13256  0.15873  0.12986  17  ILE A CG1 
103  C CG2 . ILE A 17  ? 1.03952 0.84039 0.99401 0.11289  0.19438  0.08956  17  ILE A CG2 
104  C CD1 . ILE A 17  ? 0.96758 0.79081 0.89401 0.10902  0.14101  0.10599  17  ILE A CD1 
105  N N   . LEU A 18  ? 0.99810 1.01478 1.03850 0.13824  0.19062  0.17460  18  LEU A N   
106  C CA  . LEU A 18  ? 0.97866 1.02908 1.03569 0.14234  0.21490  0.18630  18  LEU A CA  
107  C C   . LEU A 18  ? 0.96777 1.08435 1.08328 0.18869  0.25497  0.23743  18  LEU A C   
108  O O   . LEU A 18  ? 0.99520 1.12313 1.11701 0.21385  0.29794  0.24797  18  LEU A O   
109  C CB  . LEU A 18  ? 0.85022 0.95437 0.91624 0.09808  0.16970  0.19503  18  LEU A CB  
110  C CG  . LEU A 18  ? 0.93300 0.97192 0.94426 0.05891  0.13558  0.15072  18  LEU A CG  
111  C CD1 . LEU A 18  ? 0.83628 0.91492 0.86155 0.01615  0.09175  0.16281  18  LEU A CD1 
112  C CD2 . LEU A 18  ? 0.96768 0.93628 0.93322 0.06377  0.16771  0.11406  18  LEU A CD2 
113  N N   . GLU A 19  ? 0.89384 1.05804 1.04907 0.20696  0.24597  0.27377  19  GLU A N   
114  C CA  . GLU A 19  ? 0.90644 1.14297 1.12682 0.25573  0.28647  0.33239  19  GLU A CA  
115  C C   . GLU A 19  ? 1.00511 1.15958 1.21619 0.31046  0.35179  0.32427  19  GLU A C   
116  O O   . GLU A 19  ? 1.01158 1.19503 1.26041 0.36181  0.40553  0.36197  19  GLU A O   
117  C CB  . GLU A 19  ? 0.91593 1.25024 1.18501 0.25285  0.24547  0.38279  19  GLU A CB  
118  C CG  . GLU A 19  ? 0.97583 1.37229 1.24741 0.19372  0.17132  0.38575  19  GLU A CG  
119  C CD  . GLU A 19  ? 1.02054 1.48713 1.30724 0.18552  0.11829  0.41763  19  GLU A CD  
120  O OE1 . GLU A 19  ? 1.01760 1.45475 1.28028 0.21588  0.12968  0.41546  19  GLU A OE1 
121  O OE2 . GLU A 19  ? 1.08841 1.64044 1.41039 0.14697  0.06258  0.44741  19  GLU A OE2 
122  N N   . ARG A 20  ? 1.06746 1.11829 1.23411 0.30223  0.34950  0.28079  20  ARG A N   
123  C CA  . ARG A 20  ? 1.14441 1.10218 1.30819 0.34505  0.40263  0.27350  20  ARG A CA  
124  C C   . ARG A 20  ? 1.19419 1.02586 1.28862 0.33509  0.42273  0.20843  20  ARG A C   
125  O O   . ARG A 20  ? 1.26558 1.00551 1.34767 0.37300  0.47049  0.19648  20  ARG A O   
126  C CB  . ARG A 20  ? 1.07617 1.01082 1.25562 0.34519  0.38852  0.28527  20  ARG A CB  
127  C CG  . ARG A 20  ? 1.09534 0.98917 1.23028 0.29460  0.34205  0.24399  20  ARG A CG  
128  C CD  . ARG A 20  ? 1.14473 1.02282 1.30088 0.30592  0.34072  0.26757  20  ARG A CD  
129  N NE  . ARG A 20  ? 1.11447 0.91182 1.23842 0.27086  0.32456  0.22807  20  ARG A NE  
130  C CZ  . ARG A 20  ? 1.12534 0.94482 1.22065 0.24080  0.28420  0.21624  20  ARG A CZ  
131  N NH1 . ARG A 20  ? 1.14804 1.05014 1.23150 0.24171  0.25286  0.23445  20  ARG A NH1 
132  N NH2 . ARG A 20  ? 1.12594 0.88010 1.20101 0.20939  0.27315  0.18549  20  ARG A NH2 
133  N N   . SER A 21  ? 1.11072 0.93151 1.15617 0.28632  0.38610  0.16697  21  SER A N   
134  C CA  . SER A 21  ? 1.21419 0.92393 1.18672 0.27027  0.39369  0.10563  21  SER A CA  
135  C C   . SER A 21  ? 1.26355 0.96235 1.19962 0.30855  0.44152  0.09818  21  SER A C   
136  O O   . SER A 21  ? 1.15466 0.95454 1.11351 0.31602  0.44594  0.13189  21  SER A O   
137  C CB  . SER A 21  ? 1.19388 0.90920 1.13252 0.20999  0.33940  0.07479  21  SER A CB  
138  O OG  . SER A 21  ? 1.32790 0.93731 1.20535 0.18757  0.33511  0.02107  21  SER A OG  
139  N N   . LYS A 22  ? 1.29782 0.87068 1.17684 0.33506  0.47820  0.05700  22  LYS A N   
140  C CA  . LYS A 22  ? 1.31048 0.84927 1.13763 0.39072  0.53708  0.04721  22  LYS A CA  
141  C C   . LYS A 22  ? 1.38841 0.90372 1.12191 0.36812  0.52630  -0.00053 22  LYS A C   
142  O O   . LYS A 22  ? 1.43679 0.95248 1.12089 0.41803  0.57621  -0.00057 22  LYS A O   
143  C CB  . LYS A 22  ? 1.52311 0.92234 1.31809 0.42626  0.57223  0.02068  22  LYS A CB  
144  C CG  . LYS A 22  ? 1.42922 0.86340 1.31782 0.45175  0.58572  0.08023  22  LYS A CG  
145  C CD  . LYS A 22  ? 1.56357 0.86528 1.42257 0.46501  0.60268  0.05407  22  LYS A CD  
146  C CE  . LYS A 22  ? 1.56524 0.89913 1.51625 0.48251  0.61351  0.11422  22  LYS A CE  
147  N NZ  . LYS A 22  ? 1.52353 0.97096 1.53166 0.53471  0.65154  0.18927  22  LYS A NZ  
148  N N   . GLU A 23  ? 1.38833 0.89050 1.09707 0.30067  0.46664  -0.03409 23  GLU A N   
149  C CA  . GLU A 23  ? 1.40425 0.89951 1.03321 0.27015  0.44512  -0.07154 23  GLU A CA  
150  C C   . GLU A 23  ? 1.27718 0.88661 0.95955 0.21899  0.39500  -0.04007 23  GLU A C   
151  O O   . GLU A 23  ? 1.14124 0.79661 0.89790 0.19691  0.36549  -0.01123 23  GLU A O   
152  C CB  . GLU A 23  ? 1.47829 0.83676 1.02533 0.23274  0.41431  -0.14204 23  GLU A CB  
153  C CG  . GLU A 23  ? 1.77355 0.98300 1.24521 0.27625  0.45586  -0.18841 23  GLU A CG  
154  C CD  . GLU A 23  ? 1.93913 1.01017 1.34531 0.22485  0.41042  -0.25449 23  GLU A CD  
155  O OE1 . GLU A 23  ? 1.85876 0.96550 1.28001 0.15911  0.35049  -0.25872 23  GLU A OE1 
156  O OE2 . GLU A 23  ? 2.01936 0.98866 1.38933 0.24011  0.41615  -0.28633 23  GLU A OE2 
157  N N   . PRO A 24  ? 1.22865 0.87974 0.86885 0.20270  0.38562  -0.04422 24  PRO A N   
158  C CA  . PRO A 24  ? 1.17548 0.90965 0.86119 0.15093  0.33526  -0.01939 24  PRO A CA  
159  C C   . PRO A 24  ? 1.13933 0.82087 0.82659 0.10220  0.28467  -0.04748 24  PRO A C   
160  O O   . PRO A 24  ? 1.21948 0.81092 0.84897 0.08844  0.27546  -0.09301 24  PRO A O   
161  C CB  . PRO A 24  ? 1.16098 0.92206 0.78509 0.14726  0.34111  -0.02457 24  PRO A CB  
162  C CG  . PRO A 24  ? 1.24043 0.95756 0.79231 0.20992  0.40375  -0.04107 24  PRO A CG  
163  C CD  . PRO A 24  ? 1.30385 0.91338 0.84114 0.23165  0.41919  -0.07564 24  PRO A CD  
164  N N   . VAL A 25  ? 1.07654 0.81372 0.82849 0.07658  0.25043  -0.01831 25  VAL A N   
165  C CA  . VAL A 25  ? 1.07757 0.77782 0.83742 0.04257  0.21178  -0.03304 25  VAL A CA  
166  C C   . VAL A 25  ? 1.01623 0.75272 0.77156 0.00401  0.17324  -0.02817 25  VAL A C   
167  O O   . VAL A 25  ? 0.98725 0.78585 0.77761 -0.00268 0.15954  0.00136  25  VAL A O   
168  C CB  . VAL A 25  ? 1.09527 0.81211 0.91501 0.05601  0.20923  -0.00674 25  VAL A CB  
169  C CG1 . VAL A 25  ? 1.10909 0.90818 0.97465 0.07843  0.22049  0.03417  25  VAL A CG1 
170  C CG2 . VAL A 25  ? 0.97716 0.69738 0.81035 0.02666  0.16943  -0.00352 25  VAL A CG2 
171  N N   . SER A 26  ? 1.02701 0.72211 0.74223 -0.02308 0.15291  -0.05438 26  SER A N   
172  C CA  . SER A 26  ? 1.04677 0.77544 0.75281 -0.05270 0.12423  -0.04590 26  SER A CA  
173  C C   . SER A 26  ? 0.99581 0.74280 0.74645 -0.06504 0.09720  -0.02474 26  SER A C   
174  O O   . SER A 26  ? 0.95007 0.67803 0.72621 -0.05538 0.09647  -0.02209 26  SER A O   
175  C CB  . SER A 26  ? 1.15967 0.84964 0.81184 -0.07758 0.10683  -0.07373 26  SER A CB  
176  O OG  . SER A 26  ? 1.15226 0.80366 0.82563 -0.09451 0.08661  -0.08039 26  SER A OG  
177  N N   . GLY A 27  ? 1.01017 0.79030 0.76553 -0.08203 0.07784  -0.00744 27  GLY A N   
178  C CA  . GLY A 27  ? 0.90050 0.67769 0.67735 -0.08921 0.05340  0.00567  27  GLY A CA  
179  C C   . GLY A 27  ? 0.92354 0.67069 0.70084 -0.09057 0.04698  -0.00015 27  GLY A C   
180  O O   . GLY A 27  ? 0.88859 0.62703 0.68399 -0.07536 0.04476  0.00910  27  GLY A O   
181  N N   . ALA A 28  ? 0.92633 0.66180 0.68318 -0.10844 0.04288  -0.01199 28  ALA A N   
182  C CA  . ALA A 28  ? 0.96725 0.68647 0.74101 -0.11880 0.03101  -0.00731 28  ALA A CA  
183  C C   . ALA A 28  ? 1.01988 0.71155 0.82013 -0.10248 0.04623  -0.00940 28  ALA A C   
184  O O   . ALA A 28  ? 0.92009 0.61379 0.75628 -0.09987 0.04215  0.01259  28  ALA A O   
185  C CB  . ALA A 28  ? 0.99976 0.71132 0.74255 -0.14979 0.01367  -0.02231 28  ALA A CB  
186  N N   . GLN A 29  ? 1.01624 0.68689 0.80472 -0.08750 0.06782  -0.02767 29  GLN A N   
187  C CA  . GLN A 29  ? 1.05053 0.69407 0.87002 -0.06886 0.08531  -0.02279 29  GLN A CA  
188  C C   . GLN A 29  ? 0.92630 0.60291 0.77463 -0.04000 0.09217  0.00465  29  GLN A C   
189  O O   . GLN A 29  ? 0.94362 0.61834 0.82473 -0.02694 0.09760  0.02657  29  GLN A O   
190  C CB  . GLN A 29  ? 1.04584 0.65238 0.84292 -0.05332 0.11160  -0.04663 29  GLN A CB  
191  C CG  . GLN A 29  ? 1.19522 0.73769 0.95076 -0.07785 0.10358  -0.08164 29  GLN A CG  
192  C CD  . GLN A 29  ? 1.32468 0.83200 1.02018 -0.05697 0.13107  -0.11370 29  GLN A CD  
193  O OE1 . GLN A 29  ? 1.23946 0.78533 0.94066 -0.02389 0.15936  -0.10008 29  GLN A OE1 
194  N NE2 . GLN A 29  ? 1.44541 0.88026 1.08024 -0.07516 0.12165  -0.15434 29  GLN A NE2 
195  N N   . LEU A 30  ? 0.95298 0.66114 0.78762 -0.03144 0.08905  0.00634  30  LEU A N   
196  C CA  . LEU A 30  ? 0.91941 0.65100 0.76117 -0.01014 0.08294  0.02453  30  LEU A CA  
197  C C   . LEU A 30  ? 0.89482 0.62167 0.73399 -0.00600 0.07187  0.03823  30  LEU A C   
198  O O   . LEU A 30  ? 0.90261 0.63496 0.74616 0.02242  0.07865  0.05603  30  LEU A O   
199  C CB  . LEU A 30  ? 0.89385 0.65188 0.72287 -0.01737 0.06807  0.02270  30  LEU A CB  
200  C CG  . LEU A 30  ? 0.93796 0.72009 0.78143 -0.01191 0.08643  0.02395  30  LEU A CG  
201  C CD1 . LEU A 30  ? 0.97292 0.79449 0.82244 -0.02700 0.06948  0.03450  30  LEU A CD1 
202  C CD2 . LEU A 30  ? 0.89723 0.69228 0.76540 0.01852  0.10313  0.03940  30  LEU A CD2 
203  N N   . ALA A 31  ? 0.93654 0.65940 0.76794 -0.02803 0.05869  0.03629  31  ALA A N   
204  C CA  . ALA A 31  ? 0.89268 0.61763 0.72538 -0.01498 0.05444  0.05761  31  ALA A CA  
205  C C   . ALA A 31  ? 0.91764 0.65043 0.79035 -0.00332 0.06910  0.08429  31  ALA A C   
206  O O   . ALA A 31  ? 0.89237 0.63590 0.76790 0.03109  0.08080  0.11063  31  ALA A O   
207  C CB  . ALA A 31  ? 0.92251 0.65195 0.74988 -0.03884 0.03916  0.06039  31  ALA A CB  
208  N N   . GLU A 32  ? 0.86661 0.59035 0.76800 -0.03050 0.06875  0.07959  32  GLU A N   
209  C CA  . GLU A 32  ? 0.97645 0.70495 0.93189 -0.02912 0.07763  0.11131  32  GLU A CA  
210  C C   . GLU A 32  ? 0.88820 0.61760 0.85696 0.00844  0.10254  0.12668  32  GLU A C   
211  O O   . GLU A 32  ? 0.79158 0.54537 0.79673 0.03296  0.11746  0.16949  32  GLU A O   
212  C CB  . GLU A 32  ? 0.99851 0.69671 0.97354 -0.07412 0.06262  0.09537  32  GLU A CB  
213  C CG  . GLU A 32  ? 1.10870 0.81627 1.15746 -0.08875 0.05914  0.13832  32  GLU A CG  
214  C CD  . GLU A 32  ? 1.31119 0.95914 1.37615 -0.13120 0.04355  0.11579  32  GLU A CD  
215  O OE1 . GLU A 32  ? 1.35168 0.94559 1.38297 -0.12201 0.05822  0.07875  32  GLU A OE1 
216  O OE2 . GLU A 32  ? 1.34999 1.00171 1.46125 -0.17353 0.01518  0.13657  32  GLU A OE2 
217  N N   . GLU A 33  ? 0.85970 0.57513 0.80180 0.01817  0.10927  0.10097  33  GLU A N   
218  C CA  . GLU A 33  ? 0.96834 0.69383 0.92640 0.05405  0.13121  0.12142  33  GLU A CA  
219  C C   . GLU A 33  ? 0.93535 0.69387 0.86260 0.09452  0.13341  0.14090  33  GLU A C   
220  O O   . GLU A 33  ? 0.85730 0.63756 0.80113 0.12992  0.15279  0.17520  33  GLU A O   
221  C CB  . GLU A 33  ? 0.99143 0.70549 0.93614 0.05621  0.13809  0.09721  33  GLU A CB  
222  C CG  . GLU A 33  ? 1.11817 0.84585 1.09136 0.09194  0.16220  0.12543  33  GLU A CG  
223  C CD  . GLU A 33  ? 1.26038 0.96239 1.24488 0.09330  0.18005  0.11089  33  GLU A CD  
224  O OE1 . GLU A 33  ? 1.34853 0.99587 1.33276 0.06815  0.18245  0.08529  33  GLU A OE1 
225  O OE2 . GLU A 33  ? 1.25512 0.99160 1.24371 0.12205  0.19120  0.12577  33  GLU A OE2 
226  N N   . LEU A 34  ? 0.81787 0.57420 0.69348 0.09217  0.11369  0.11902  34  LEU A N   
227  C CA  . LEU A 34  ? 0.96342 0.72731 0.78532 0.13006  0.10965  0.12308  34  LEU A CA  
228  C C   . LEU A 34  ? 0.97614 0.73385 0.77582 0.15036  0.11385  0.13794  34  LEU A C   
229  O O   . LEU A 34  ? 0.98287 0.72471 0.71583 0.18373  0.10896  0.13013  34  LEU A O   
230  C CB  . LEU A 34  ? 0.91078 0.66405 0.68765 0.11550  0.08122  0.08870  34  LEU A CB  
231  C CG  . LEU A 34  ? 0.96546 0.74067 0.77597 0.10425  0.08510  0.08732  34  LEU A CG  
232  C CD1 . LEU A 34  ? 0.84487 0.62627 0.64497 0.07598  0.05995  0.06529  34  LEU A CD1 
233  C CD2 . LEU A 34  ? 0.93567 0.74130 0.74807 0.14312  0.09787  0.11394  34  LEU A CD2 
234  N N   . SER A 35  ? 0.97064 0.73800 0.82149 0.13136  0.12082  0.15926  35  SER A N   
235  C CA  . SER A 35  ? 0.89324 0.67309 0.74552 0.15606  0.13259  0.19109  35  SER A CA  
236  C C   . SER A 35  ? 0.90696 0.64893 0.68824 0.16825  0.11891  0.16408  35  SER A C   
237  O O   . SER A 35  ? 1.07341 0.80837 0.82048 0.21436  0.13572  0.18327  35  SER A O   
238  C CB  . SER A 35  ? 0.97012 0.78309 0.83119 0.21175  0.16571  0.23969  35  SER A CB  
239  O OG  . SER A 35  ? 1.03532 0.86872 0.95115 0.20271  0.17562  0.25837  35  SER A OG  
240  N N   . VAL A 36  ? 0.98418 0.69825 0.74565 0.12917  0.09119  0.12353  36  VAL A N   
241  C CA  . VAL A 36  ? 0.96956 0.64490 0.68884 0.12635  0.07559  0.10590  36  VAL A CA  
242  C C   . VAL A 36  ? 0.93745 0.62842 0.70018 0.07668  0.06179  0.10579  36  VAL A C   
243  O O   . VAL A 36  ? 0.88713 0.60503 0.69183 0.04228  0.05859  0.10435  36  VAL A O   
244  C CB  . VAL A 36  ? 1.00058 0.62732 0.65339 0.12477  0.04955  0.06523  36  VAL A CB  
245  C CG1 . VAL A 36  ? 1.00465 0.61182 0.59134 0.17680  0.05645  0.06113  36  VAL A CG1 
246  C CG2 . VAL A 36  ? 0.92487 0.57254 0.60709 0.07953  0.03074  0.04655  36  VAL A CG2 
247  N N   . SER A 37  ? 1.00819 0.67569 0.75234 0.07708  0.05423  0.10739  37  SER A N   
248  C CA  . SER A 37  ? 0.90632 0.59225 0.67979 0.03369  0.03905  0.10983  37  SER A CA  
249  C C   . SER A 37  ? 0.93567 0.61647 0.70090 -0.00370 0.02061  0.07752  37  SER A C   
250  O O   . SER A 37  ? 0.96530 0.62066 0.70223 0.00202  0.01245  0.05575  37  SER A O   
251  C CB  . SER A 37  ? 0.94851 0.60702 0.70508 0.04878  0.03796  0.12468  37  SER A CB  
252  O OG  . SER A 37  ? 0.93444 0.53310 0.64599 0.04412  0.02057  0.09509  37  SER A OG  
253  N N   . ARG A 38  ? 0.78121 0.49232 0.56966 -0.04059 0.01327  0.07853  38  ARG A N   
254  C CA  . ARG A 38  ? 0.84048 0.55535 0.62115 -0.06670 0.00405  0.05803  38  ARG A CA  
255  C C   . ARG A 38  ? 0.88971 0.57950 0.65614 -0.07266 -0.01128 0.05930  38  ARG A C   
256  O O   . ARG A 38  ? 0.88947 0.58138 0.65689 -0.08722 -0.02056 0.04957  38  ARG A O   
257  C CB  . ARG A 38  ? 0.91561 0.66329 0.70476 -0.09670 0.00292  0.05703  38  ARG A CB  
258  C CG  . ARG A 38  ? 0.88332 0.64500 0.66170 -0.11370 0.00256  0.04602  38  ARG A CG  
259  C CD  . ARG A 38  ? 0.91179 0.69729 0.67333 -0.13343 0.00478  0.03946  38  ARG A CD  
260  N NE  . ARG A 38  ? 0.97475 0.78045 0.73427 -0.14813 -0.00965 0.06058  38  ARG A NE  
261  C CZ  . ARG A 38  ? 0.95751 0.78411 0.71610 -0.15608 -0.01514 0.08281  38  ARG A CZ  
262  N NH1 . ARG A 38  ? 0.89188 0.72157 0.65648 -0.15611 -0.00995 0.08796  38  ARG A NH1 
263  N NH2 . ARG A 38  ? 0.85644 0.70785 0.61805 -0.16545 -0.02737 0.10879  38  ARG A NH2 
264  N N   . GLN A 39  ? 0.90431 0.57042 0.66510 -0.06168 -0.01404 0.07685  39  GLN A N   
265  C CA  . GLN A 39  ? 0.96288 0.58146 0.70960 -0.06613 -0.03030 0.07696  39  GLN A CA  
266  C C   . GLN A 39  ? 0.94719 0.51380 0.66006 -0.05446 -0.04483 0.04984  39  GLN A C   
267  O O   . GLN A 39  ? 0.97984 0.52244 0.69365 -0.07918 -0.06970 0.04318  39  GLN A O   
268  C CB  . GLN A 39  ? 0.96225 0.55074 0.70445 -0.04358 -0.02369 0.10163  39  GLN A CB  
269  C CG  . GLN A 39  ? 0.87802 0.52409 0.65508 -0.06200 -0.02002 0.13585  39  GLN A CG  
270  C CD  . GLN A 39  ? 0.82652 0.53943 0.62325 -0.06975 -0.01252 0.14192  39  GLN A CD  
271  O OE1 . GLN A 39  ? 0.78406 0.49782 0.58157 -0.05021 -0.00209 0.13547  39  GLN A OE1 
272  N NE2 . GLN A 39  ? 0.76100 0.52729 0.57130 -0.09956 -0.02035 0.15639  39  GLN A NE2 
273  N N   . VAL A 40  ? 0.95720 0.50988 0.64121 -0.01824 -0.03274 0.03917  40  VAL A N   
274  C CA  . VAL A 40  ? 1.00193 0.51778 0.64332 -0.00558 -0.04913 0.01324  40  VAL A CA  
275  C C   . VAL A 40  ? 0.98604 0.55383 0.66014 -0.03646 -0.06088 0.00838  40  VAL A C   
276  O O   . VAL A 40  ? 1.02748 0.57877 0.69266 -0.05573 -0.09194 -0.00285 40  VAL A O   
277  C CB  . VAL A 40  ? 1.01310 0.52086 0.61749 0.04693  -0.02570 0.01315  40  VAL A CB  
278  C CG1 . VAL A 40  ? 0.95721 0.44810 0.51576 0.05906  -0.04324 -0.01038 40  VAL A CG1 
279  C CG2 . VAL A 40  ? 1.06859 0.51725 0.63057 0.08886  -0.01163 0.02033  40  VAL A CG2 
280  N N   . ILE A 41  ? 0.97798 0.60689 0.69170 -0.04152 -0.03756 0.01916  41  ILE A N   
281  C CA  . ILE A 41  ? 0.91911 0.59678 0.66483 -0.06059 -0.03797 0.01983  41  ILE A CA  
282  C C   . ILE A 41  ? 1.00073 0.69107 0.77095 -0.09696 -0.05912 0.02926  41  ILE A C   
283  O O   . ILE A 41  ? 0.95001 0.66012 0.73727 -0.11143 -0.07909 0.03323  41  ILE A O   
284  C CB  . ILE A 41  ? 0.87830 0.59439 0.65007 -0.05925 -0.00805 0.02465  41  ILE A CB  
285  C CG1 . ILE A 41  ? 0.88540 0.59625 0.65326 -0.02871 0.01033  0.02544  41  ILE A CG1 
286  C CG2 . ILE A 41  ? 0.92026 0.67825 0.71846 -0.06919 -0.00001 0.02736  41  ILE A CG2 
287  C CD1 . ILE A 41  ? 0.89872 0.61045 0.65223 -0.00505 0.00553  0.02355  41  ILE A CD1 
288  N N   . VAL A 42  ? 0.91944 0.60739 0.69930 -0.11287 -0.05650 0.04164  42  VAL A N   
289  C CA  . VAL A 42  ? 0.91192 0.62093 0.72522 -0.14622 -0.07137 0.06289  42  VAL A CA  
290  C C   . VAL A 42  ? 0.99826 0.66242 0.81091 -0.16463 -0.11195 0.06030  42  VAL A C   
291  O O   . VAL A 42  ? 1.00843 0.70860 0.86604 -0.19544 -0.13096 0.08153  42  VAL A O   
292  C CB  . VAL A 42  ? 0.99700 0.70587 0.81436 -0.15464 -0.06326 0.08174  42  VAL A CB  
293  C CG1 . VAL A 42  ? 0.86359 0.57538 0.71658 -0.18617 -0.08296 0.11060  42  VAL A CG1 
294  C CG2 . VAL A 42  ? 0.88251 0.64887 0.70124 -0.15217 -0.03511 0.08634  42  VAL A CG2 
295  N N   . GLN A 43  ? 1.07565 0.65895 0.83599 -0.14614 -0.12747 0.03644  43  GLN A N   
296  C CA  . GLN A 43  ? 1.13889 0.66045 0.87874 -0.16541 -0.17420 0.02245  43  GLN A CA  
297  C C   . GLN A 43  ? 1.17080 0.73305 0.91374 -0.16986 -0.19351 0.01513  43  GLN A C   
298  O O   . GLN A 43  ? 1.18584 0.75625 0.95818 -0.20897 -0.23633 0.02474  43  GLN A O   
299  C CB  . GLN A 43  ? 1.27043 0.68331 0.93138 -0.13283 -0.18064 -0.00725 43  GLN A CB  
300  C CG  . GLN A 43  ? 1.24743 0.61893 0.91448 -0.12870 -0.16599 0.00886  43  GLN A CG  
301  C CD  . GLN A 43  ? 1.37934 0.64107 0.96644 -0.08479 -0.16357 -0.01635 43  GLN A CD  
302  O OE1 . GLN A 43  ? 1.45366 0.61430 0.98490 -0.08898 -0.20043 -0.04612 43  GLN A OE1 
303  N NE2 . GLN A 43  ? 1.39134 0.67032 0.96853 -0.04008 -0.12074 -0.00389 43  GLN A NE2 
304  N N   . ASP A 44  ? 1.06708 0.66086 0.78889 -0.13225 -0.16463 0.00554  44  ASP A N   
305  C CA  . ASP A 44  ? 1.15936 0.79710 0.88524 -0.12998 -0.18006 0.00562  44  ASP A CA  
306  C C   . ASP A 44  ? 1.12515 0.85659 0.93580 -0.16062 -0.17957 0.04212  44  ASP A C   
307  O O   . ASP A 44  ? 1.10545 0.87504 0.94118 -0.18055 -0.21395 0.05538  44  ASP A O   
308  C CB  . ASP A 44  ? 1.12306 0.77886 0.82159 -0.08090 -0.14201 -0.00134 44  ASP A CB  
309  C CG  . ASP A 44  ? 1.18507 0.76383 0.80121 -0.04156 -0.13927 -0.02663 44  ASP A CG  
310  O OD1 . ASP A 44  ? 1.33003 0.83065 0.88702 -0.04648 -0.17577 -0.05015 44  ASP A OD1 
311  O OD2 . ASP A 44  ? 1.15578 0.74892 0.76643 -0.00407 -0.09954 -0.02055 44  ASP A OD2 
312  N N   . ILE A 45  ? 1.05106 0.82512 0.90405 -0.16260 -0.14172 0.06242  45  ILE A N   
313  C CA  . ILE A 45  ? 1.02259 0.88743 0.94854 -0.17918 -0.13072 0.10159  45  ILE A CA  
314  C C   . ILE A 45  ? 1.07898 0.95734 1.05556 -0.22894 -0.17610 0.13108  45  ILE A C   
315  O O   . ILE A 45  ? 1.06284 1.01762 1.10348 -0.24809 -0.19185 0.16805  45  ILE A O   
316  C CB  . ILE A 45  ? 1.01373 0.90942 0.94959 -0.16369 -0.07918 0.11048  45  ILE A CB  
317  C CG1 . ILE A 45  ? 0.98807 0.85955 0.88138 -0.12508 -0.04468 0.08187  45  ILE A CG1 
318  C CG2 . ILE A 45  ? 0.95925 0.94763 0.95843 -0.16620 -0.05743 0.15275  45  ILE A CG2 
319  C CD1 . ILE A 45  ? 1.01495 0.92745 0.92663 -0.10027 -0.02652 0.08887  45  ILE A CD1 
320  N N   . ALA A 46  ? 1.09168 0.89914 1.05021 -0.25133 -0.19813 0.12257  46  ALA A N   
321  C CA  . ALA A 46  ? 1.11801 0.92113 1.12988 -0.30507 -0.24736 0.15202  46  ALA A CA  
322  C C   . ALA A 46  ? 1.21123 0.97942 1.20705 -0.33112 -0.31239 0.13506  46  ALA A C   
323  O O   . ALA A 46  ? 1.21718 1.02414 1.28378 -0.38218 -0.35887 0.17193  46  ALA A O   
324  C CB  . ALA A 46  ? 1.14233 0.86093 1.13428 -0.31771 -0.25359 0.14628  46  ALA A CB  
325  N N   . TYR A 47  ? 1.21231 0.91254 1.11587 -0.29770 -0.31890 0.08391  47  TYR A N   
326  C CA  . TYR A 47  ? 1.30639 0.96913 1.16906 -0.31642 -0.38290 0.06087  47  TYR A CA  
327  C C   . TYR A 47  ? 1.25878 1.04644 1.18695 -0.32375 -0.39081 0.09903  47  TYR A C   
328  O O   . TYR A 47  ? 1.28717 1.09648 1.24609 -0.37061 -0.45695 0.11502  47  TYR A O   
329  C CB  . TYR A 47  ? 1.36494 0.93236 1.10250 -0.26497 -0.37549 0.00236  47  TYR A CB  
330  C CG  . TYR A 47  ? 1.49430 0.99559 1.14951 -0.27529 -0.44300 -0.03477 47  TYR A CG  
331  C CD1 . TYR A 47  ? 1.50596 1.09240 1.18207 -0.28573 -0.47387 -0.01761 47  TYR A CD1 
332  C CD2 . TYR A 47  ? 1.65021 1.00059 1.19585 -0.26791 -0.47385 -0.08769 47  TYR A CD2 
333  C CE1 . TYR A 47  ? 1.61640 1.14590 1.20409 -0.29656 -0.54275 -0.05321 47  TYR A CE1 
334  C CE2 . TYR A 47  ? 1.77240 1.04934 1.21809 -0.27340 -0.53786 -0.13037 47  TYR A CE2 
335  C CZ  . TYR A 47  ? 1.69908 1.06909 1.16408 -0.29084 -0.57591 -0.11382 47  TYR A CZ  
336  O OH  . TYR A 47  ? 1.80361 1.12426 1.17771 -0.28848 -0.62674 -0.14976 47  TYR A OH  
337  N N   . LEU A 48  ? 1.20862 1.07706 1.16134 -0.27864 -0.32593 0.11666  48  LEU A N   
338  C CA  . LEU A 48  ? 1.10006 1.08371 1.11176 -0.26996 -0.32056 0.15591  48  LEU A CA  
339  C C   . LEU A 48  ? 1.14080 1.23157 1.27440 -0.31086 -0.32982 0.22423  48  LEU A C   
340  O O   . LEU A 48  ? 1.15664 1.33714 1.35214 -0.32986 -0.36260 0.26584  48  LEU A O   
341  C CB  . LEU A 48  ? 1.02719 1.04283 1.02700 -0.20743 -0.24481 0.15313  48  LEU A CB  
342  C CG  . LEU A 48  ? 1.10726 1.05387 1.01188 -0.16283 -0.23269 0.10696  48  LEU A CG  
343  C CD1 . LEU A 48  ? 0.96580 0.92118 0.86994 -0.11477 -0.15979 0.10465  48  LEU A CD1 
344  C CD2 . LEU A 48  ? 1.18125 1.16233 1.06615 -0.15546 -0.27075 0.11233  48  LEU A CD2 
345  N N   . ARG A 49  ? 1.05190 1.17190 1.21456 -0.16127 -0.02248 -0.10114 49  ARG A N   
346  C CA  . ARG A 49  ? 1.07425 1.16737 1.30385 -0.19253 0.02501  -0.09875 49  ARG A CA  
347  C C   . ARG A 49  ? 1.07718 1.17856 1.39604 -0.24339 0.04229  -0.16162 49  ARG A C   
348  O O   . ARG A 49  ? 1.06468 1.24766 1.49101 -0.27735 0.04748  -0.19455 49  ARG A O   
349  C CB  . ARG A 49  ? 1.11564 1.07274 1.27218 -0.17354 0.07757  -0.05045 49  ARG A CB  
350  C CG  . ARG A 49  ? 1.12850 1.10576 1.25998 -0.14578 0.07982  -0.00266 49  ARG A CG  
351  C CD  . ARG A 49  ? 1.17907 1.02976 1.22505 -0.11997 0.12705  0.03972  49  ARG A CD  
352  N NE  . ARG A 49  ? 1.27688 1.04272 1.22945 -0.08469 0.11612  0.04262  49  ARG A NE  
353  C CZ  . ARG A 49  ? 1.36836 1.05911 1.22007 -0.03386 0.12075  0.07470  49  ARG A CZ  
354  N NH1 . ARG A 49  ? 1.41933 1.10464 1.24257 -0.01478 0.13807  0.10720  49  ARG A NH1 
355  N NH2 . ARG A 49  ? 1.33788 0.96524 1.11757 0.00349  0.10387  0.06759  49  ARG A NH2 
356  N N   . SER A 50  ? 1.14100 1.16509 1.42720 -0.24869 0.05065  -0.18736 50  SER A N   
357  C CA  . SER A 50  ? 1.10656 1.14381 1.48399 -0.29960 0.06352  -0.25999 50  SER A CA  
358  C C   . SER A 50  ? 1.05647 1.26914 1.51787 -0.31374 0.00282  -0.31855 50  SER A C   
359  O O   . SER A 50  ? 1.07931 1.34314 1.65098 -0.36118 0.01002  -0.39077 50  SER A O   
360  C CB  . SER A 50  ? 1.17445 1.11564 1.49341 -0.29065 0.06704  -0.28122 50  SER A CB  
361  O OG  . SER A 50  ? 1.17040 1.17415 1.42125 -0.24900 0.00614  -0.27919 50  SER A OG  
362  N N   . LEU A 51  ? 1.05886 1.36180 1.46769 -0.27114 -0.05514 -0.29171 51  LEU A N   
363  C CA  . LEU A 51  ? 0.96220 1.42336 1.41943 -0.26676 -0.11722 -0.33498 51  LEU A CA  
364  C C   . LEU A 51  ? 0.98822 1.54178 1.53459 -0.27130 -0.12194 -0.33309 51  LEU A C   
365  O O   . LEU A 51  ? 1.09707 1.78491 1.72288 -0.27664 -0.16639 -0.39217 51  LEU A O   
366  C CB  . LEU A 51  ? 0.92366 1.42184 1.27122 -0.21621 -0.16660 -0.30085 51  LEU A CB  
367  C CG  . LEU A 51  ? 1.00737 1.47183 1.29681 -0.21445 -0.17716 -0.33457 51  LEU A CG  
368  C CD1 . LEU A 51  ? 1.00703 1.52262 1.19848 -0.17198 -0.21786 -0.30988 51  LEU A CD1 
369  C CD2 . LEU A 51  ? 0.98452 1.50477 1.36015 -0.25347 -0.19001 -0.42733 51  LEU A CD2 
370  N N   . GLY A 52  ? 1.07288 1.56614 1.60919 -0.26420 -0.08070 -0.27296 52  GLY A N   
371  C CA  . GLY A 52  ? 1.03211 1.61128 1.66150 -0.26759 -0.07922 -0.27500 52  GLY A CA  
372  C C   . GLY A 52  ? 1.04389 1.61980 1.60844 -0.21950 -0.08859 -0.20061 52  GLY A C   
373  O O   . GLY A 52  ? 1.05589 1.71576 1.68809 -0.20771 -0.10022 -0.20002 52  GLY A O   
374  N N   . TYR A 53  ? 0.99506 1.47979 1.43801 -0.19044 -0.08396 -0.14496 53  TYR A N   
375  C CA  . TYR A 53  ? 1.03397 1.49763 1.42121 -0.15237 -0.08111 -0.08084 53  TYR A CA  
376  C C   . TYR A 53  ? 1.03676 1.39321 1.40961 -0.16290 -0.01664 -0.04787 53  TYR A C   
377  O O   . TYR A 53  ? 1.07894 1.33999 1.42624 -0.18348 0.02183  -0.05394 53  TYR A O   
378  C CB  . TYR A 53  ? 0.95686 1.39689 1.23302 -0.11660 -0.11018 -0.04915 53  TYR A CB  
379  C CG  . TYR A 53  ? 0.94623 1.48092 1.20707 -0.09649 -0.16709 -0.06763 53  TYR A CG  
380  C CD1 . TYR A 53  ? 0.97023 1.54450 1.24023 -0.11337 -0.19279 -0.12295 53  TYR A CD1 
381  C CD2 . TYR A 53  ? 0.92659 1.50201 1.15335 -0.05660 -0.19220 -0.02934 53  TYR A CD2 
382  C CE1 . TYR A 53  ? 0.98384 1.64505 1.22032 -0.08772 -0.24582 -0.14002 53  TYR A CE1 
383  C CE2 . TYR A 53  ? 0.93547 1.58273 1.12254 -0.02885 -0.24063 -0.03793 53  TYR A CE2 
384  C CZ  . TYR A 53  ? 0.98191 1.67595 1.16889 -0.04283 -0.26906 -0.09329 53  TYR A CZ  
385  O OH  . TYR A 53  ? 1.09106 1.85654 1.21990 -0.00827 -0.31799 -0.10180 53  TYR A OH  
386  N N   . ASN A 54  ? 0.96440 1.33201 1.34735 -0.14405 -0.00350 -0.01318 54  ASN A N   
387  C CA  . ASN A 54  ? 0.97220 1.25028 1.33562 -0.14850 0.05763  0.01670  54  ASN A CA  
388  C C   . ASN A 54  ? 1.01317 1.23439 1.27155 -0.10620 0.05110  0.06345  54  ASN A C   
389  O O   . ASN A 54  ? 0.97177 1.22291 1.23448 -0.08261 0.04585  0.08707  54  ASN A O   
390  C CB  . ASN A 54  ? 0.96152 1.30104 1.42729 -0.16195 0.08432  0.00825  54  ASN A CB  
391  C CG  . ASN A 54  ? 1.00691 1.24892 1.45137 -0.17471 0.16105  0.03218  54  ASN A CG  
392  O OD1 . ASN A 54  ? 1.01502 1.14004 1.38134 -0.18124 0.19838  0.04654  54  ASN A OD1 
393  N ND2 . ASN A 54  ? 0.98475 1.27135 1.49110 -0.17245 0.18597  0.03698  54  ASN A ND2 
394  N N   . ILE A 55  ? 1.04952 1.19260 1.22226 -0.09560 0.05101  0.06917  55  ILE A N   
395  C CA  . ILE A 55  ? 1.03458 1.12913 1.11930 -0.05782 0.04623  0.09727  55  ILE A CA  
396  C C   . ILE A 55  ? 1.16526 1.15188 1.18837 -0.04785 0.09288  0.11433  55  ILE A C   
397  O O   . ILE A 55  ? 1.21764 1.13120 1.21240 -0.05757 0.11364  0.10615  55  ILE A O   
398  C CB  . ILE A 55  ? 1.00644 1.10585 1.04158 -0.04376 0.00829  0.08419  55  ILE A CB  
399  C CG1 . ILE A 55  ? 0.96909 1.16285 1.04500 -0.05229 -0.03088 0.07025  55  ILE A CG1 
400  C CG2 . ILE A 55  ? 0.97529 1.04752 0.94608 -0.00834 0.00332  0.09930  55  ILE A CG2 
401  C CD1 . ILE A 55  ? 0.91023 1.11480 0.93376 -0.03860 -0.05860 0.06130  55  ILE A CD1 
402  N N   . VAL A 56  ? 1.16514 1.13427 1.15963 -0.02467 0.11149  0.13808  56  VAL A N   
403  C CA  . VAL A 56  ? 1.16920 1.03603 1.07851 -0.00147 0.15246  0.15832  56  VAL A CA  
404  C C   . VAL A 56  ? 1.13319 0.98742 0.96206 0.04751  0.12165  0.16013  56  VAL A C   
405  O O   . VAL A 56  ? 1.05895 0.98246 0.91741 0.05505  0.09218  0.15288  56  VAL A O   
406  C CB  . VAL A 56  ? 1.20530 1.06637 1.14316 -0.01235 0.20382  0.17435  56  VAL A CB  
407  C CG1 . VAL A 56  ? 1.17249 1.07257 1.22013 -0.06531 0.23231  0.15703  56  VAL A CG1 
408  C CG2 . VAL A 56  ? 1.14022 1.07163 1.10486 0.00697  0.18293  0.17764  56  VAL A CG2 
409  N N   . ALA A 57  ? 1.18092 0.94602 0.91092 0.08272  0.12898  0.16569  57  ALA A N   
410  C CA  . ALA A 57  ? 1.18894 0.95396 0.84945 0.13507  0.09653  0.15480  57  ALA A CA  
411  C C   . ALA A 57  ? 1.25295 0.99237 0.86198 0.16387  0.12214  0.16964  57  ALA A C   
412  O O   . ALA A 57  ? 1.40160 1.06801 0.96864 0.16196  0.17329  0.19695  57  ALA A O   
413  C CB  . ALA A 57  ? 1.28792 0.97957 0.86231 0.17469  0.08134  0.14775  57  ALA A CB  
414  N N   . THR A 58  ? 1.22982 1.02887 0.84559 0.18696  0.09263  0.14735  58  THR A N   
415  C CA  . THR A 58  ? 1.25434 1.04162 0.82303 0.21774  0.11020  0.14906  58  THR A CA  
416  C C   . THR A 58  ? 1.27252 1.07192 0.77548 0.27544  0.06701  0.11228  58  THR A C   
417  O O   . THR A 58  ? 1.27776 1.11221 0.80132 0.28094  0.02702  0.08394  58  THR A O   
418  C CB  . THR A 58  ? 1.18494 1.04458 0.85103 0.18575  0.12032  0.14588  58  THR A CB  
419  O OG1 . THR A 58  ? 1.08555 1.01229 0.79264 0.19274  0.08283  0.11025  58  THR A OG1 
420  C CG2 . THR A 58  ? 1.08465 0.97638 0.84702 0.13229  0.13240  0.16304  58  THR A CG2 
421  N N   . PRO A 59  ? 1.28022 1.06189 0.70879 0.32077  0.07227  0.10364  59  PRO A N   
422  C CA  . PRO A 59  ? 1.32735 1.14153 0.70448 0.38084  0.02213  0.05335  59  PRO A CA  
423  C C   . PRO A 59  ? 1.26523 1.18707 0.75707 0.35605  -0.01541 -0.00117 59  PRO A C   
424  O O   . PRO A 59  ? 1.29609 1.25715 0.78044 0.39035  -0.05969 -0.04918 59  PRO A O   
425  C CB  . PRO A 59  ? 1.44699 1.24225 0.74527 0.42212  0.03940  0.04879  59  PRO A CB  
426  C CG  . PRO A 59  ? 1.41719 1.12875 0.67993 0.39629  0.10764  0.11129  59  PRO A CG  
427  C CD  . PRO A 59  ? 1.33237 1.07669 0.72670 0.32071  0.12291  0.12994  59  PRO A CD  
428  N N   . ARG A 60  ? 1.19632 1.16334 0.79399 0.29964  0.00478  0.00411  60  ARG A N   
429  C CA  . ARG A 60  ? 1.10348 1.15001 0.80224 0.27107  -0.01349 -0.03888 60  ARG A CA  
430  C C   . ARG A 60  ? 1.08174 1.14549 0.83816 0.22929  -0.01831 -0.02506 60  ARG A C   
431  O O   . ARG A 60  ? 1.04282 1.16132 0.86808 0.20711  -0.02678 -0.05896 60  ARG A O   
432  C CB  . ARG A 60  ? 1.09012 1.15993 0.85786 0.24234  0.01438  -0.03848 60  ARG A CB  
433  C CG  . ARG A 60  ? 1.14045 1.18694 0.85199 0.27547  0.03060  -0.04222 60  ARG A CG  
434  C CD  . ARG A 60  ? 1.14222 1.23828 0.91874 0.27074  0.03218  -0.09427 60  ARG A CD  
435  N NE  . ARG A 60  ? 1.29036 1.39010 0.98974 0.32543  0.01866  -0.13706 60  ARG A NE  
436  C CZ  . ARG A 60  ? 1.29509 1.35040 0.91699 0.35135  0.04449  -0.11160 60  ARG A CZ  
437  N NH1 . ARG A 60  ? 1.26516 1.27769 0.89812 0.32198  0.08852  -0.05010 60  ARG A NH1 
438  N NH2 . ARG A 60  ? 1.26618 1.32576 0.79692 0.41050  0.02634  -0.15343 60  ARG A NH2 
439  N N   . GLY A 61  ? 1.10907 1.12722 0.84153 0.21498  -0.00755 0.01978  61  GLY A N   
440  C CA  . GLY A 61  ? 0.94999 0.98770 0.72670 0.18004  -0.01538 0.02716  61  GLY A CA  
441  C C   . GLY A 61  ? 0.99965 1.01107 0.79395 0.14667  0.00759  0.07354  61  GLY A C   
442  O O   . GLY A 61  ? 1.10762 1.08165 0.88343 0.14841  0.03481  0.09983  61  GLY A O   
443  N N   . TYR A 62  ? 0.91565 0.95458 0.75000 0.11588  -0.00205 0.07692  62  TYR A N   
444  C CA  . TYR A 62  ? 0.94826 0.98255 0.81223 0.08514  0.01050  0.10512  62  TYR A CA  
445  C C   . TYR A 62  ? 0.93018 1.00665 0.85633 0.06608  0.02068  0.12420  62  TYR A C   
446  O O   . TYR A 62  ? 0.91939 1.02583 0.86814 0.06671  0.01600  0.11943  62  TYR A O   
447  C CB  . TYR A 62  ? 0.92035 0.97393 0.79514 0.06628  -0.00964 0.09336  62  TYR A CB  
448  C CG  . TYR A 62  ? 1.00268 1.01235 0.82379 0.08778  -0.02096 0.07273  62  TYR A CG  
449  C CD1 . TYR A 62  ? 1.05114 0.98678 0.83464 0.09280  -0.00287 0.08513  62  TYR A CD1 
450  C CD2 . TYR A 62  ? 0.94112 0.97922 0.75297 0.10364  -0.04476 0.03894  62  TYR A CD2 
451  C CE1 . TYR A 62  ? 1.04817 0.92776 0.77418 0.12159  -0.01260 0.07000  62  TYR A CE1 
452  C CE2 . TYR A 62  ? 1.00659 1.00876 0.77358 0.13259  -0.05948 0.01635  62  TYR A CE2 
453  C CZ  . TYR A 62  ? 1.04341 0.96119 0.76212 0.14540  -0.04570 0.03473  62  TYR A CZ  
454  O OH  . TYR A 62  ? 1.13215 1.00036 0.79913 0.18265  -0.05995 0.01565  62  TYR A OH  
455  N N   . VAL A 63  ? 0.87745 0.95394 0.83637 0.04974  0.03796  0.14303  63  VAL A N   
456  C CA  . VAL A 63  ? 0.87550 1.00196 0.90094 0.03880  0.03955  0.15788  63  VAL A CA  
457  C C   . VAL A 63  ? 0.94507 1.10608 1.01887 0.01407  0.03290  0.15617  63  VAL A C   
458  O O   . VAL A 63  ? 0.93283 1.06380 1.00501 -0.00185 0.05063  0.14823  63  VAL A O   
459  C CB  . VAL A 63  ? 0.90464 1.02140 0.94802 0.05045  0.06935  0.16825  63  VAL A CB  
460  C CG1 . VAL A 63  ? 0.88463 0.97178 0.88011 0.07546  0.07345  0.15596  63  VAL A CG1 
461  C CG2 . VAL A 63  ? 0.95916 1.04717 1.00521 0.03909  0.10325  0.17241  63  VAL A CG2 
462  N N   . LEU A 64  ? 0.86096 1.08251 0.97544 0.01320  0.00827  0.16063  64  LEU A N   
463  C CA  . LEU A 64  ? 0.87830 1.15864 1.04905 -0.00354 -0.00957 0.14741  64  LEU A CA  
464  C C   . LEU A 64  ? 0.89424 1.21479 1.14391 -0.00361 0.00703  0.14913  64  LEU A C   
465  O O   . LEU A 64  ? 0.89241 1.23021 1.15803 0.02097  0.00511  0.16777  64  LEU A O   
466  C CB  . LEU A 64  ? 0.84681 1.17551 1.00422 0.00836  -0.04960 0.15054  64  LEU A CB  
467  C CG  . LEU A 64  ? 0.85988 1.26611 1.07051 -0.00056 -0.08018 0.12617  64  LEU A CG  
468  C CD1 . LEU A 64  ? 0.89700 1.28632 1.11389 -0.03425 -0.07334 0.09090  64  LEU A CD1 
469  C CD2 . LEU A 64  ? 0.91502 1.36129 1.08449 0.02421  -0.11955 0.13647  64  LEU A CD2 
470  N N   . ALA A 65  ? 0.95666 1.29116 1.26297 -0.03228 0.02783  0.12572  65  ALA A N   
471  C CA  . ALA A 65  ? 0.87367 1.25265 1.27037 -0.03945 0.05435  0.11665  65  ALA A CA  
472  C C   . ALA A 65  ? 0.92614 1.41433 1.42635 -0.05164 0.02360  0.07889  65  ALA A C   
473  O O   . ALA A 65  ? 0.95442 1.47153 1.45206 -0.06354 -0.00980 0.05489  65  ALA A O   
474  C CB  . ALA A 65  ? 0.93008 1.23751 1.31964 -0.06643 0.11883  0.11423  65  ALA A CB  
475  N N   . GLY A 66  ? 0.95759 1.51492 1.55557 -0.04670 0.03456  0.06534  66  GLY A N   
476  C CA  . GLY A 66  ? 0.99910 1.68599 1.70535 -0.04077 -0.00796 0.02389  66  GLY A CA  
477  C C   . GLY A 66  ? 1.06771 1.80838 1.86988 -0.09238 0.00423  -0.03808 66  GLY A C   
478  O O   . GLY A 66  ? 1.10068 1.83807 1.87465 -0.11008 -0.02088 -0.05926 66  GLY A O   
479  N N   . GLY A 67  ? 1.11117 1.90543 2.03680 -0.11932 0.04682  -0.07430 67  GLY A N   
480  C CA  . GLY A 67  ? 1.17011 2.02003 2.21087 -0.17669 0.06854  -0.14379 67  GLY A CA  
481  C C   . GLY A 67  ? 1.18149 2.17249 2.29288 -0.16163 -0.01378 -0.20154 67  GLY A C   
482  O O   . GLY A 67  ? 1.18955 2.25159 2.27690 -0.09924 -0.08488 -0.18707 67  GLY A O   
483  N N   . LYS A 68  ? 1.15890 2.18276 2.35172 -0.21786 -0.00079 -0.26944 68  LYS A N   
484  C CA  . LYS A 68  ? 0.99068 2.16262 2.26698 -0.21131 -0.07621 -0.34564 68  LYS A CA  
485  C C   . LYS A 68  ? 0.85009 2.20008 2.29302 -0.19028 -0.10698 -0.40700 68  LYS A C   
486  O O   . LYS A 68  ? 0.84789 2.32757 2.31299 -0.13775 -0.19639 -0.44127 68  LYS A O   
487  C CB  . LYS A 68  ? 1.04196 2.21042 2.17649 -0.15070 -0.15913 -0.30796 68  LYS A CB  
488  C CG  . LYS A 68  ? 1.05720 2.12574 2.09027 -0.18023 -0.15233 -0.30252 68  LYS A CG  
489  C CD  . LYS A 68  ? 1.09550 2.14393 1.97608 -0.12141 -0.21602 -0.25396 68  LYS A CD  
490  C CE  . LYS A 68  ? 1.03934 2.00473 1.83427 -0.14968 -0.20981 -0.26018 68  LYS A CE  
491  N NZ  . LYS A 68  ? 0.93024 1.85622 1.57093 -0.10102 -0.25074 -0.20816 68  LYS A NZ  
492  N N   . SER A 69  ? 1.92494 1.85809 1.51714 0.12632  0.04494  -0.26680 69  SER A N   
493  C CA  . SER A 69  ? 1.93244 1.81272 1.50470 0.06847  0.01592  -0.24618 69  SER A CA  
494  C C   . SER A 69  ? 1.92981 1.73893 1.41358 0.06243  0.00515  -0.27800 69  SER A C   
495  O O   . SER A 69  ? 1.94811 1.72436 1.37964 0.10487  0.01608  -0.32138 69  SER A O   
496  C CB  . SER A 69  ? 1.89712 1.70915 1.50916 0.05439  -0.01601 -0.22958 69  SER A CB  
497  O OG  . SER A 69  ? 1.73018 1.54454 1.36143 0.00072  -0.03459 -0.19635 69  SER A OG  
498  N N   . GLY A 70  ? 1.87857 1.66470 1.34435 0.01203  -0.01863 -0.25856 70  GLY A N   
499  C CA  . GLY A 70  ? 1.88428 1.60653 1.27077 -0.00150 -0.03873 -0.28464 70  GLY A CA  
500  C C   . GLY A 70  ? 1.84729 1.48693 1.24442 -0.03732 -0.08230 -0.27871 70  GLY A C   
501  O O   . GLY A 70  ? 1.83799 1.41098 1.25776 -0.02691 -0.09639 -0.28941 70  GLY A O   
502  N N   . VAL A 71  ? 1.79984 1.44666 1.18402 -0.07961 -0.10380 -0.25856 71  VAL A N   
503  C CA  . VAL A 71  ? 1.77525 1.35885 1.16961 -0.11396 -0.14513 -0.25608 71  VAL A CA  
504  C C   . VAL A 71  ? 1.69862 1.31488 1.17198 -0.14209 -0.15244 -0.21112 71  VAL A C   
505  O O   . VAL A 71  ? 1.62840 1.31115 1.12936 -0.14693 -0.13528 -0.18084 71  VAL A O   
506  C CB  . VAL A 71  ? 1.90876 1.47647 1.23401 -0.13686 -0.17142 -0.26914 71  VAL A CB  
507  C CG1 . VAL A 71  ? 1.83984 1.48208 1.15682 -0.15404 -0.16238 -0.23316 71  VAL A CG1 
508  C CG2 . VAL A 71  ? 1.89156 1.40325 1.23870 -0.17222 -0.21660 -0.26972 71  VAL A CG2 
509  N N   . SER A 72  ? 1.62373 1.19122 1.13255 -0.16184 -0.17775 -0.20787 72  SER A N   
510  C CA  . SER A 72  ? 1.55323 1.14625 1.13019 -0.18658 -0.18615 -0.17162 72  SER A CA  
511  C C   . SER A 72  ? 1.52825 1.08707 1.11681 -0.21932 -0.22145 -0.17268 72  SER A C   
512  O O   . SER A 72  ? 1.55773 1.05582 1.12236 -0.22415 -0.23827 -0.19937 72  SER A O   
513  C CB  . SER A 72  ? 1.47217 1.06042 1.09938 -0.17150 -0.17036 -0.16013 72  SER A CB  
514  O OG  . SER A 72  ? 1.54422 1.05970 1.16460 -0.16785 -0.18060 -0.17878 72  SER A OG  
515  N N   . ARG A 73  ? 1.45584 1.05380 1.08461 -0.24153 -0.23429 -0.14448 73  ARG A N   
516  C CA  . ARG A 73  ? 1.36222 0.94940 1.02150 -0.27105 -0.26652 -0.14122 73  ARG A CA  
517  C C   . ARG A 73  ? 1.28457 0.90611 1.01987 -0.28003 -0.26226 -0.11101 73  ARG A C   
518  O O   . ARG A 73  ? 1.19515 0.85190 0.94876 -0.26826 -0.24457 -0.09099 73  ARG A O   
519  C CB  . ARG A 73  ? 1.41081 1.01565 1.03632 -0.28542 -0.29583 -0.14187 73  ARG A CB  
520  C CG  . ARG A 73  ? 1.41137 1.02181 1.08392 -0.31458 -0.33212 -0.13666 73  ARG A CG  
521  C CD  . ARG A 73  ? 1.48908 1.12387 1.13197 -0.32188 -0.36304 -0.13300 73  ARG A CD  
522  N NE  . ARG A 73  ? 1.57085 1.17071 1.12182 -0.31682 -0.37118 -0.16401 73  ARG A NE  
523  C CZ  . ARG A 73  ? 1.57019 1.18034 1.08283 -0.32208 -0.40017 -0.16933 73  ARG A CZ  
524  N NH1 . ARG A 73  ? 1.47227 1.12486 1.03380 -0.33231 -0.42689 -0.14512 73  ARG A NH1 
525  N NH2 . ARG A 73  ? 1.66993 1.24777 1.09084 -0.31339 -0.40261 -0.20122 73  ARG A NH2 
526  N N   . LEU A 74  ? 1.27813 0.89054 1.05721 -0.30248 -0.27883 -0.10929 74  LEU A N   
527  C CA  . LEU A 74  ? 1.19462 0.85030 1.04436 -0.31139 -0.27773 -0.08404 74  LEU A CA  
528  C C   . LEU A 74  ? 1.17461 0.87170 1.04248 -0.32029 -0.30570 -0.07546 74  LEU A C   
529  O O   . LEU A 74  ? 1.23302 0.92837 1.09053 -0.33058 -0.32831 -0.08743 74  LEU A O   
530  C CB  . LEU A 74  ? 1.19014 0.83647 1.08671 -0.32500 -0.27037 -0.08070 74  LEU A CB  
531  C CG  . LEU A 74  ? 1.15702 0.85217 1.12178 -0.32943 -0.25954 -0.05676 74  LEU A CG  
532  C CD1 . LEU A 74  ? 1.08811 0.78885 1.04428 -0.30580 -0.23465 -0.04616 74  LEU A CD1 
533  C CD2 . LEU A 74  ? 1.16520 0.85595 1.17072 -0.34866 -0.24944 -0.05011 74  LEU A CD2 
534  N N   . VAL A 75  ? 1.23419 0.96765 1.12801 -0.31044 -0.30328 -0.05463 75  VAL A N   
535  C CA  . VAL A 75  ? 1.09027 0.85680 1.00090 -0.31331 -0.33345 -0.04240 75  VAL A CA  
536  C C   . VAL A 75  ? 0.99659 0.80599 0.98859 -0.30978 -0.33140 -0.02700 75  VAL A C   
537  O O   . VAL A 75  ? 1.03961 0.85373 1.05299 -0.29562 -0.30289 -0.01956 75  VAL A O   
538  C CB  . VAL A 75  ? 1.11740 0.88218 0.97929 -0.29894 -0.33302 -0.02937 75  VAL A CB  
539  C CG1 . VAL A 75  ? 1.16806 0.95598 1.04026 -0.30000 -0.36996 -0.01336 75  VAL A CG1 
540  C CG2 . VAL A 75  ? 1.17397 0.90884 0.95634 -0.29864 -0.32514 -0.04554 75  VAL A CG2 
541  N N   . ALA A 76  ? 0.98156 0.82696 1.01792 -0.32006 -0.36231 -0.02393 76  ALA A N   
542  C CA  . ALA A 76  ? 1.00752 0.90727 1.12733 -0.31190 -0.36188 -0.01131 76  ALA A CA  
543  C C   . ALA A 76  ? 0.97391 0.88934 1.09774 -0.28762 -0.38275 0.00431  76  ALA A C   
544  O O   . ALA A 76  ? 1.05510 0.96569 1.14668 -0.29070 -0.41827 0.00822  76  ALA A O   
545  C CB  . ALA A 76  ? 1.03180 0.97478 1.21257 -0.33555 -0.38085 -0.01591 76  ALA A CB  
546  N N   . VAL A 77  ? 0.97598 0.90337 1.13290 -0.26258 -0.36286 0.01313  77  VAL A N   
547  C CA  . VAL A 77  ? 0.99705 0.92055 1.15395 -0.23675 -0.38166 0.02820  77  VAL A CA  
548  C C   . VAL A 77  ? 0.89980 0.86219 1.13059 -0.20946 -0.36957 0.02905  77  VAL A C   
549  O O   . VAL A 77  ? 0.86180 0.85536 1.13394 -0.21185 -0.34031 0.01997  77  VAL A O   
550  C CB  . VAL A 77  ? 0.97238 0.83914 1.05878 -0.23177 -0.36911 0.03570  77  VAL A CB  
551  C CG1 . VAL A 77  ? 0.95975 0.79871 0.97214 -0.25376 -0.37474 0.03290  77  VAL A CG1 
552  C CG2 . VAL A 77  ? 0.92656 0.78125 1.01846 -0.22415 -0.32867 0.02747  77  VAL A CG2 
553  N N   . LYS A 78  ? 0.90609 0.86346 1.14860 -0.18143 -0.39230 0.04078  78  LYS A N   
554  C CA  . LYS A 78  ? 0.88488 0.86584 1.18550 -0.14511 -0.38162 0.03763  78  LYS A CA  
555  C C   . LYS A 78  ? 0.93136 0.85262 1.19725 -0.12003 -0.40123 0.05046  78  LYS A C   
556  O O   . LYS A 78  ? 0.91000 0.80636 1.14291 -0.12399 -0.43749 0.06910  78  LYS A O   
557  C CB  . LYS A 78  ? 0.88378 0.94832 1.27607 -0.13121 -0.39895 0.03694  78  LYS A CB  
558  C CG  . LYS A 78  ? 0.87065 0.95781 1.31955 -0.08106 -0.39571 0.03348  78  LYS A CG  
559  C CD  . LYS A 78  ? 0.80246 0.98979 1.35437 -0.06304 -0.41197 0.03337  78  LYS A CD  
560  C CE  . LYS A 78  ? 0.83500 1.02753 1.42970 -0.00201 -0.42046 0.03073  78  LYS A CE  
561  N NZ  . LYS A 78  ? 0.85791 1.16385 1.56672 0.02608  -0.42638 0.02705  78  LYS A NZ  
562  N N   . HIS A 79  ? 0.94995 0.84316 1.21756 -0.09629 -0.37892 0.04114  79  HIS A N   
563  C CA  . HIS A 79  ? 0.92912 0.75714 1.17236 -0.07188 -0.39941 0.05148  79  HIS A CA  
564  C C   . HIS A 79  ? 1.03495 0.84377 1.29051 -0.04475 -0.37176 0.02961  79  HIS A C   
565  O O   . HIS A 79  ? 1.02187 0.86301 1.28732 -0.05041 -0.33510 0.01089  79  HIS A O   
566  C CB  . HIS A 79  ? 0.98784 0.75021 1.15134 -0.10222 -0.40881 0.07078  79  HIS A CB  
567  C CG  . HIS A 79  ? 1.03902 0.78906 1.16473 -0.12926 -0.37283 0.05937  79  HIS A CG  
568  N ND1 . HIS A 79  ? 1.08355 0.80783 1.20671 -0.11960 -0.34936 0.04351  79  HIS A ND1 
569  C CD2 . HIS A 79  ? 0.98429 0.74523 1.07372 -0.16173 -0.35858 0.05947  79  HIS A CD2 
570  C CE1 . HIS A 79  ? 1.00175 0.72685 1.09260 -0.14578 -0.32423 0.03781  79  HIS A CE1 
571  N NE2 . HIS A 79  ? 0.99547 0.74165 1.06719 -0.16931 -0.32779 0.04702  79  HIS A NE2 
572  N N   . ALA A 80  ? 1.06845 0.81670 1.31562 -0.01558 -0.39172 0.03235  80  ALA A N   
573  C CA  . ALA A 80  ? 1.19004 0.91221 1.44479 0.01633  -0.37220 0.00593  80  ALA A CA  
574  C C   . ALA A 80  ? 1.18018 0.84157 1.37191 -0.01228 -0.35576 -0.00003 80  ALA A C   
575  O O   . ALA A 80  ? 1.16246 0.80262 1.31047 -0.05298 -0.35966 0.01917  80  ALA A O   
576  C CB  . ALA A 80  ? 1.35544 1.02812 1.62869 0.06358  -0.40487 0.00746  80  ALA A CB  
577  N N   . PRO A 81  ? 1.20377 0.84129 1.38990 0.00969  -0.33754 -0.02842 81  PRO A N   
578  C CA  . PRO A 81  ? 1.28580 0.86999 1.41681 -0.01844 -0.32845 -0.03518 81  PRO A CA  
579  C C   . PRO A 81  ? 1.25727 0.75937 1.34880 -0.04337 -0.36016 -0.01053 81  PRO A C   
580  O O   . PRO A 81  ? 1.26078 0.75059 1.31655 -0.08449 -0.35425 0.00009  81  PRO A O   
581  C CB  . PRO A 81  ? 1.24076 0.80632 1.37165 0.01884  -0.31349 -0.07324 81  PRO A CB  
582  C CG  . PRO A 81  ? 1.21675 0.86023 1.40604 0.05905  -0.29552 -0.08609 81  PRO A CG  
583  C CD  . PRO A 81  ? 1.21476 0.87873 1.44293 0.06186  -0.32417 -0.05776 81  PRO A CD  
584  N N   . GLU A 82  ? 1.29657 0.74460 1.39564 -0.01950 -0.39350 0.00175  82  GLU A N   
585  C CA  . GLU A 82  ? 1.32366 0.68461 1.38168 -0.04650 -0.42366 0.03096  82  GLU A CA  
586  C C   . GLU A 82  ? 1.30600 0.69073 1.34159 -0.08655 -0.43096 0.07164  82  GLU A C   
587  O O   . GLU A 82  ? 1.36604 0.69294 1.36204 -0.11937 -0.44710 0.10112  82  GLU A O   
588  C CB  . GLU A 82  ? 1.38901 0.67189 1.45654 -0.00527 -0.46018 0.03470  82  GLU A CB  
589  C CG  . GLU A 82  ? 1.50504 0.75515 1.58848 0.04305  -0.45468 -0.01070 82  GLU A CG  
590  C CD  . GLU A 82  ? 1.48398 0.82062 1.62692 0.09676  -0.43715 -0.03484 82  GLU A CD  
591  O OE1 . GLU A 82  ? 1.36130 0.79613 1.53287 0.08334  -0.41879 -0.02445 82  GLU A OE1 
592  O OE2 . GLU A 82  ? 1.62489 0.93113 1.78723 0.15202  -0.44184 -0.06490 82  GLU A OE2 
593  N N   . GLU A 83  ? 1.26500 0.73152 1.32123 -0.08712 -0.41930 0.07382  83  GLU A N   
594  C CA  . GLU A 83  ? 1.28586 0.77217 1.31123 -0.12089 -0.42703 0.10587  83  GLU A CA  
595  C C   . GLU A 83  ? 1.24827 0.77235 1.24739 -0.15992 -0.39464 0.10105  83  GLU A C   
596  O O   . GLU A 83  ? 1.10715 0.66194 1.08121 -0.18269 -0.39323 0.11733  83  GLU A O   
597  C CB  . GLU A 83  ? 1.27091 0.81677 1.32963 -0.10091 -0.44172 0.10997  83  GLU A CB  
598  C CG  . GLU A 83  ? 1.27340 0.81759 1.38704 -0.04803 -0.46269 0.09976  83  GLU A CG  
599  C CD  . GLU A 83  ? 1.28407 0.87063 1.42570 -0.03128 -0.49566 0.11796  83  GLU A CD  
600  O OE1 . GLU A 83  ? 1.28570 0.82124 1.39557 -0.03011 -0.53330 0.15110  83  GLU A OE1 
601  O OE2 . GLU A 83  ? 1.25739 0.92897 1.45309 -0.02113 -0.48628 0.10128  83  GLU A OE2 
602  N N   . ILE A 84  ? 1.03876 0.56116 1.04047 -0.16446 -0.37050 0.07712  84  ILE A N   
603  C CA  . ILE A 84  ? 1.11105 0.67415 1.09483 -0.19352 -0.34191 0.07188  84  ILE A CA  
604  C C   . ILE A 84  ? 1.10144 0.64472 1.04379 -0.23186 -0.34521 0.10102  84  ILE A C   
605  O O   . ILE A 84  ? 1.08269 0.66706 1.00454 -0.25113 -0.32985 0.10803  84  ILE A O   
606  C CB  . ILE A 84  ? 1.15497 0.72345 1.14917 -0.18671 -0.32028 0.04170  84  ILE A CB  
607  C CG1 . ILE A 84  ? 1.10757 0.71972 1.13662 -0.15534 -0.30477 0.01723  84  ILE A CG1 
608  C CG2 . ILE A 84  ? 0.96526 0.56349 0.93914 -0.21622 -0.29828 0.04174  84  ILE A CG2 
609  C CD1 . ILE A 84  ? 1.05434 0.66694 1.08421 -0.14210 -0.28592 -0.01114 84  ILE A CD1 
610  N N   . LYS A 85  ? 1.15231 0.63171 1.08101 -0.24372 -0.36425 0.11846  85  LYS A N   
611  C CA  . LYS A 85  ? 1.26768 0.73413 1.16117 -0.28609 -0.36369 0.15128  85  LYS A CA  
612  C C   . LYS A 85  ? 1.23284 0.71577 1.09231 -0.29490 -0.37070 0.18226  85  LYS A C   
613  O O   . LYS A 85  ? 1.16794 0.69217 0.99914 -0.32085 -0.35046 0.19417  85  LYS A O   
614  C CB  . LYS A 85  ? 1.15173 0.53525 1.03843 -0.30152 -0.38747 0.16816  85  LYS A CB  
615  C CG  . LYS A 85  ? 1.17664 0.57028 1.04181 -0.35016 -0.37506 0.19554  85  LYS A CG  
616  C CD  . LYS A 85  ? 1.47991 0.80771 1.33001 -0.36238 -0.39585 0.22290  85  LYS A CD  
617  C CE  . LYS A 85  ? 1.50148 0.79123 1.37479 -0.35093 -0.40215 0.19300  85  LYS A CE  
618  N NZ  . LYS A 85  ? 1.49294 0.71872 1.35147 -0.37140 -0.42091 0.21934  85  LYS A NZ  
619  N N   . GLU A 86  ? 1.22002 0.67448 1.07986 -0.27034 -0.40025 0.19399  86  GLU A N   
620  C CA  . GLU A 86  ? 1.31495 0.78338 1.13450 -0.27760 -0.41344 0.22297  86  GLU A CA  
621  C C   . GLU A 86  ? 1.22804 0.77119 1.03914 -0.28173 -0.38845 0.20279  86  GLU A C   
622  O O   . GLU A 86  ? 1.20517 0.76958 0.96644 -0.30463 -0.37882 0.22006  86  GLU A O   
623  C CB  . GLU A 86  ? 1.34050 0.78189 1.17448 -0.24240 -0.45310 0.23205  86  GLU A CB  
624  C CG  . GLU A 86  ? 1.51967 0.89735 1.39148 -0.21301 -0.47310 0.22398  86  GLU A CG  
625  C CD  . GLU A 86  ? 1.59006 0.93624 1.47490 -0.17475 -0.51628 0.24039  86  GLU A CD  
626  O OE1 . GLU A 86  ? 1.38902 0.78614 1.27343 -0.16510 -0.52985 0.24625  86  GLU A OE1 
627  O OE2 . GLU A 86  ? 1.53074 0.79873 1.42615 -0.15379 -0.53913 0.24583  86  GLU A OE2 
628  N N   . GLU A 87  ? 1.15614 0.73606 1.01233 -0.25934 -0.37674 0.16577  87  GLU A N   
629  C CA  . GLU A 87  ? 1.09294 0.72890 0.94389 -0.26197 -0.35790 0.14503  87  GLU A CA  
630  C C   . GLU A 87  ? 1.12509 0.78378 0.95026 -0.28498 -0.32393 0.14014  87  GLU A C   
631  O O   . GLU A 87  ? 1.20617 0.88962 0.98969 -0.29685 -0.31406 0.14265  87  GLU A O   
632  C CB  . GLU A 87  ? 1.11169 0.77613 1.01888 -0.23790 -0.35157 0.11295  87  GLU A CB  
633  C CG  . GLU A 87  ? 1.00882 0.71700 0.91265 -0.24379 -0.33510 0.09236  87  GLU A CG  
634  C CD  . GLU A 87  ? 1.08374 0.81774 1.03945 -0.22910 -0.31865 0.06585  87  GLU A CD  
635  O OE1 . GLU A 87  ? 0.90232 0.63116 0.86730 -0.22638 -0.29687 0.05570  87  GLU A OE1 
636  O OE2 . GLU A 87  ? 1.08136 0.84395 1.06860 -0.22249 -0.32812 0.05681  87  GLU A OE2 
637  N N   . LEU A 88  ? 1.05797 0.71128 0.90674 -0.28899 -0.30722 0.13120  88  LEU A N   
638  C CA  . LEU A 88  ? 1.17733 0.86404 1.01422 -0.30660 -0.27707 0.12602  88  LEU A CA  
639  C C   . LEU A 88  ? 1.18018 0.87135 0.97212 -0.33498 -0.27200 0.15793  88  LEU A C   
640  O O   . LEU A 88  ? 1.22045 0.95265 0.98302 -0.34099 -0.25018 0.15473  88  LEU A O   
641  C CB  . LEU A 88  ? 1.10102 0.78222 0.97276 -0.30708 -0.26834 0.11248  88  LEU A CB  
642  C CG  . LEU A 88  ? 0.96519 0.65214 0.87142 -0.28010 -0.26382 0.08088  88  LEU A CG  
643  C CD1 . LEU A 88  ? 0.88563 0.56991 0.81080 -0.28219 -0.25657 0.06708  88  LEU A CD1 
644  C CD2 . LEU A 88  ? 0.87263 0.59762 0.77593 -0.26963 -0.24684 0.06381  88  LEU A CD2 
645  N N   . LEU A 89  ? 1.29713 0.94390 1.07995 -0.35199 -0.29090 0.18968  89  LEU A N   
646  C CA  . LEU A 89  ? 1.34484 0.99601 1.08111 -0.38392 -0.28418 0.22783  89  LEU A CA  
647  C C   . LEU A 89  ? 1.37416 1.04464 1.05441 -0.37809 -0.28577 0.23493  89  LEU A C   
648  O O   . LEU A 89  ? 1.39178 1.09756 1.02656 -0.39689 -0.26319 0.25035  89  LEU A O   
649  C CB  . LEU A 89  ? 1.44559 1.02734 1.17659 -0.40273 -0.31151 0.26524  89  LEU A CB  
650  C CG  . LEU A 89  ? 1.45182 1.01137 1.21839 -0.42769 -0.30904 0.26878  89  LEU A CG  
651  C CD1 . LEU A 89  ? 1.48066 0.94892 1.23586 -0.44277 -0.34353 0.30439  89  LEU A CD1 
652  C CD2 . LEU A 89  ? 1.45884 1.08396 1.22172 -0.46379 -0.27425 0.28160  89  LEU A CD2 
653  N N   . CYS A 90  ? 1.31880 0.97165 1.00205 -0.35206 -0.31244 0.22217  90  CYS A N   
654  C CA  . CYS A 90  ? 1.34469 1.01431 0.97600 -0.34613 -0.32176 0.22195  90  CYS A CA  
655  C C   . CYS A 90  ? 1.33377 1.05536 0.94626 -0.34419 -0.28839 0.19069  90  CYS A C   
656  O O   . CYS A 90  ? 1.32807 1.07072 0.87613 -0.35335 -0.27644 0.19802  90  CYS A O   
657  C CB  . CYS A 90  ? 1.34302 0.99622 1.00441 -0.31938 -0.35783 0.20838  90  CYS A CB  
658  S SG  . CYS A 90  ? 1.47136 1.14019 1.07658 -0.31419 -0.38366 0.20646  90  CYS A SG  
659  N N   . VAL A 91  ? 1.29608 1.03513 0.95921 -0.32966 -0.27283 0.15553  91  VAL A N   
660  C CA  . VAL A 91  ? 1.27526 1.04984 0.92312 -0.32113 -0.24655 0.12362  91  VAL A CA  
661  C C   . VAL A 91  ? 1.29337 1.10631 0.91904 -0.33402 -0.21009 0.13194  91  VAL A C   
662  O O   . VAL A 91  ? 1.31196 1.15226 0.88776 -0.33047 -0.19087 0.12092  91  VAL A O   
663  C CB  . VAL A 91  ? 1.12385 0.90044 0.83008 -0.30323 -0.24074 0.09139  91  VAL A CB  
664  C CG1 . VAL A 91  ? 1.17573 0.97975 0.86983 -0.29350 -0.21115 0.06359  91  VAL A CG1 
665  C CG2 . VAL A 91  ? 1.08067 0.83882 0.80773 -0.29203 -0.26987 0.07998  91  VAL A CG2 
666  N N   . VAL A 92  ? 1.22953 1.04904 0.89501 -0.34819 -0.20000 0.14836  92  VAL A N   
667  C CA  . VAL A 92  ? 1.21404 1.08684 0.87944 -0.36139 -0.16449 0.15483  92  VAL A CA  
668  C C   . VAL A 92  ? 1.33566 1.22520 0.93894 -0.38482 -0.15379 0.18937  92  VAL A C   
669  O O   . VAL A 92  ? 1.33665 1.28228 0.91142 -0.38410 -0.11955 0.18447  92  VAL A O   
670  C CB  . VAL A 92  ? 1.23586 1.11142 0.96396 -0.37580 -0.16375 0.16300  92  VAL A CB  
671  C CG1 . VAL A 92  ? 1.30570 1.13295 1.03156 -0.40424 -0.18812 0.20195  92  VAL A CG1 
672  C CG2 . VAL A 92  ? 1.21968 1.16735 0.96909 -0.38431 -0.12865 0.16160  92  VAL A CG2 
673  N N   . ARG A 93  ? 1.35281 1.19395 0.93030 -0.40266 -0.18229 0.22542  93  ARG A N   
674  C CA  . ARG A 93  ? 1.47042 1.31941 0.97831 -0.42754 -0.17483 0.26635  93  ARG A CA  
675  C C   . ARG A 93  ? 1.44640 1.31686 0.87762 -0.40975 -0.16664 0.24819  93  ARG A C   
676  O O   . ARG A 93  ? 1.42490 1.32596 0.79028 -0.42556 -0.14458 0.27249  93  ARG A O   
677  C CB  . ARG A 93  ? 1.39376 1.17161 0.88642 -0.44446 -0.21478 0.30966  93  ARG A CB  
678  C CG  . ARG A 93  ? 1.45910 1.21194 1.00562 -0.47242 -0.21792 0.33520  93  ARG A CG  
679  C CD  . ARG A 93  ? 1.59916 1.26433 1.13842 -0.48097 -0.26167 0.37141  93  ARG A CD  
680  N NE  . ARG A 93  ? 1.57741 1.21537 1.15587 -0.51635 -0.26137 0.39738  93  ARG A NE  
681  C CZ  . ARG A 93  ? 1.57975 1.13005 1.16482 -0.52695 -0.29761 0.42575  93  ARG A CZ  
682  N NH1 . ARG A 93  ? 1.55332 1.03958 1.11584 -0.49920 -0.33747 0.43283  93  ARG A NH1 
683  N NH2 . ARG A 93  ? 1.53165 1.06990 1.15622 -0.55418 -0.29374 0.43567  93  ARG A NH2 
684  N N   . ASN A 94  ? 1.44151 1.29703 0.87696 -0.37932 -0.18291 0.20531  94  ASN A N   
685  C CA  . ASN A 94  ? 1.46704 1.33844 0.83225 -0.36196 -0.17586 0.17695  94  ASN A CA  
686  C C   . ASN A 94  ? 1.45188 1.36446 0.83751 -0.33903 -0.13973 0.13167  94  ASN A C   
687  O O   . ASN A 94  ? 1.46545 1.36978 0.81310 -0.31671 -0.14246 0.09245  94  ASN A O   
688  C CB  . ASN A 94  ? 1.50305 1.32709 0.85312 -0.34859 -0.22344 0.16144  94  ASN A CB  
689  C CG  . ASN A 94  ? 1.61053 1.40180 0.91155 -0.36387 -0.25942 0.20623  94  ASN A CG  
690  O OD1 . ASN A 94  ? 1.50303 1.25703 0.84968 -0.36584 -0.29221 0.22767  94  ASN A OD1 
691  N ND2 . ASN A 94  ? 1.71700 1.52095 0.91993 -0.37132 -0.25333 0.22060  94  ASN A ND2 
692  N N   . GLY A 95  ? 1.36719 1.32040 0.81209 -0.34377 -0.10977 0.13625  95  GLY A N   
693  C CA  . GLY A 95  ? 1.31487 1.31494 0.77929 -0.31859 -0.07445 0.09968  95  GLY A CA  
694  C C   . GLY A 95  ? 1.35304 1.31798 0.85138 -0.28934 -0.08960 0.05621  95  GLY A C   
695  O O   . GLY A 95  ? 1.37716 1.35190 0.85411 -0.26110 -0.07208 0.01872  95  GLY A O   
696  N N   . GLY A 96  ? 1.29375 1.21495 0.84146 -0.29464 -0.12109 0.06078  96  GLY A N   
697  C CA  . GLY A 96  ? 1.28938 1.18447 0.87976 -0.27353 -0.13036 0.02901  96  GLY A CA  
698  C C   . GLY A 96  ? 1.19239 1.10463 0.85556 -0.27444 -0.12230 0.03615  96  GLY A C   
699  O O   . GLY A 96  ? 1.18627 1.12485 0.87124 -0.29464 -0.11526 0.06377  96  GLY A O   
700  N N   . ARG A 97  ? 1.14295 1.03674 0.83945 -0.25443 -0.12533 0.01126  97  ARG A N   
701  C CA  . ARG A 97  ? 1.09220 0.99434 0.84899 -0.25172 -0.12387 0.01400  97  ARG A CA  
702  C C   . ARG A 97  ? 1.08252 0.93777 0.86129 -0.24737 -0.14659 0.00570  97  ARG A C   
703  O O   . ARG A 97  ? 1.13200 0.95960 0.89341 -0.23688 -0.15278 -0.01362 97  ARG A O   
704  C CB  . ARG A 97  ? 1.12146 1.05920 0.89500 -0.22692 -0.09959 -0.00476 97  ARG A CB  
705  C CG  . ARG A 97  ? 1.08019 1.01169 0.90261 -0.21544 -0.10523 -0.00991 97  ARG A CG  
706  C CD  . ARG A 97  ? 1.04842 1.03142 0.89562 -0.19290 -0.08512 -0.01868 97  ARG A CD  
707  N NE  . ARG A 97  ? 1.18956 1.17487 1.00526 -0.16304 -0.06798 -0.04213 97  ARG A NE  
708  C CZ  . ARG A 97  ? 1.35581 1.39846 1.16051 -0.15301 -0.04258 -0.04594 97  ARG A CZ  
709  N NH1 . ARG A 97  ? 1.35825 1.47015 1.18998 -0.17458 -0.02961 -0.02335 97  ARG A NH1 
710  N NH2 . ARG A 97  ? 1.30913 1.33916 1.07435 -0.12140 -0.02901 -0.07376 97  ARG A NH2 
711  N N   . ILE A 98  ? 0.98367 0.82970 0.79903 -0.25687 -0.15904 0.01945  98  ILE A N   
712  C CA  . ILE A 98  ? 1.04067 0.85554 0.88079 -0.25016 -0.17401 0.01180  98  ILE A CA  
713  C C   . ILE A 98  ? 0.99114 0.81140 0.85416 -0.23398 -0.16154 -0.00127 98  ILE A C   
714  O O   . ILE A 98  ? 0.94148 0.77587 0.82738 -0.23467 -0.15948 0.00389  98  ILE A O   
715  C CB  . ILE A 98  ? 0.97637 0.77453 0.83903 -0.25987 -0.19276 0.02759  98  ILE A CB  
716  C CG1 . ILE A 98  ? 0.97275 0.76188 0.80870 -0.27476 -0.20794 0.04772  98  ILE A CG1 
717  C CG2 . ILE A 98  ? 0.81549 0.59593 0.70541 -0.24865 -0.20219 0.01713  98  ILE A CG2 
718  C CD1 . ILE A 98  ? 1.06244 0.86962 0.88225 -0.29333 -0.19803 0.06844  98  ILE A CD1 
719  N N   . VAL A 99  ? 0.93430 0.87441 0.84615 -0.22084 -0.20753 0.21723  99  VAL A N   
720  C CA  . VAL A 99  ? 0.91307 0.87582 0.84679 -0.18688 -0.16525 0.26192  99  VAL A CA  
721  C C   . VAL A 99  ? 0.88234 0.89232 0.82974 -0.18880 -0.19072 0.25851  99  VAL A C   
722  O O   . VAL A 99  ? 0.87646 0.96160 0.83861 -0.17408 -0.19334 0.30110  99  VAL A O   
723  C CB  . VAL A 99  ? 0.95914 0.84264 0.89162 -0.17699 -0.08897 0.26153  99  VAL A CB  
724  C CG1 . VAL A 99  ? 0.89942 0.80979 0.86753 -0.13415 -0.03798 0.32125  99  VAL A CG1 
725  C CG2 . VAL A 99  ? 1.03578 0.86727 0.94981 -0.18252 -0.05392 0.25991  99  VAL A CG2 
726  N N   . ASP A 100 ? 0.86981 0.84629 0.81300 -0.21044 -0.20618 0.21189  100 ASP A N   
727  C CA  . ASP A 100 ? 0.86718 0.87856 0.82378 -0.21230 -0.21978 0.20629  100 ASP A CA  
728  C C   . ASP A 100 ? 0.85242 0.83212 0.80981 -0.23747 -0.24557 0.15575  100 ASP A C   
729  O O   . ASP A 100 ? 0.83229 0.78037 0.78169 -0.25512 -0.25773 0.13234  100 ASP A O   
730  C CB  . ASP A 100 ? 0.87141 0.88302 0.84278 -0.18735 -0.16943 0.23768  100 ASP A CB  
731  C CG  . ASP A 100 ? 0.92076 0.84658 0.88515 -0.19009 -0.12397 0.21202  100 ASP A CG  
732  O OD1 . ASP A 100 ? 0.92006 0.80470 0.86678 -0.22013 -0.14162 0.16501  100 ASP A OD1 
733  O OD2 . ASP A 100 ? 0.97867 0.88444 0.95634 -0.16517 -0.06582 0.24311  100 ASP A OD2 
734  N N   . VAL A 101 ? 0.76726 0.76762 0.73748 -0.24093 -0.25302 0.14474  101 VAL A N   
735  C CA  . VAL A 101 ? 0.83485 0.81260 0.81747 -0.25775 -0.26806 0.10708  101 VAL A CA  
736  C C   . VAL A 101 ? 0.88889 0.85859 0.87756 -0.25099 -0.23949 0.10435  101 VAL A C   
737  O O   . VAL A 101 ? 0.84055 0.84622 0.83119 -0.23872 -0.22561 0.12876  101 VAL A O   
738  C CB  . VAL A 101 ? 0.81442 0.81169 0.80916 -0.25436 -0.28209 0.08968  101 VAL A CB  
739  C CG1 . VAL A 101 ? 0.70103 0.74268 0.69030 -0.26078 -0.28114 0.09990  101 VAL A CG1 
740  C CG2 . VAL A 101 ? 0.87059 0.85028 0.88864 -0.25152 -0.27576 0.06282  101 VAL A CG2 
741  N N   . ILE A 102 ? 0.90483 0.83919 0.89635 -0.26325 -0.23173 0.07818  102 ILE A N   
742  C CA  . ILE A 102 ? 0.90295 0.82152 0.89811 -0.26028 -0.20265 0.07083  102 ILE A CA  
743  C C   . ILE A 102 ? 0.94972 0.87208 0.96480 -0.27836 -0.22550 0.04015  102 ILE A C   
744  O O   . ILE A 102 ? 0.91270 0.83176 0.92977 -0.29298 -0.23654 0.02605  102 ILE A O   
745  C CB  . ILE A 102 ? 0.99423 0.85886 0.96837 -0.26210 -0.15292 0.07058  102 ILE A CB  
746  C CG1 . ILE A 102 ? 0.92325 0.78349 0.89432 -0.23228 -0.11330 0.11392  102 ILE A CG1 
747  C CG2 . ILE A 102 ? 0.94342 0.78540 0.92009 -0.26871 -0.12653 0.05242  102 ILE A CG2 
748  C CD1 . ILE A 102 ? 0.94219 0.73014 0.89510 -0.23447 -0.04767 0.11161  102 ILE A CD1 
749  N N   . VAL A 103 ? 0.88043 0.82089 0.91207 -0.27376 -0.22617 0.03460  103 VAL A N   
750  C CA  . VAL A 103 ? 0.91123 0.85424 0.96872 -0.28230 -0.23458 0.01063  103 VAL A CA  
751  C C   . VAL A 103 ? 0.89420 0.81883 0.94638 -0.28657 -0.20767 0.00140  103 VAL A C   
752  O O   . VAL A 103 ? 0.93923 0.86185 0.97899 -0.27278 -0.18127 0.01607  103 VAL A O   
753  C CB  . VAL A 103 ? 0.91996 0.88654 0.99806 -0.27268 -0.24001 0.00347  103 VAL A CB  
754  C CG1 . VAL A 103 ? 0.98064 0.94698 1.08868 -0.27369 -0.23165 -0.01644 103 VAL A CG1 
755  C CG2 . VAL A 103 ? 0.96114 0.93384 1.04774 -0.26252 -0.25046 0.00734  103 VAL A CG2 
756  N N   . GLU A 104 ? 0.88433 0.80622 0.94775 -0.30118 -0.20846 -0.01704 104 GLU A N   
757  C CA  A GLU A 104 ? 0.92798 0.83125 0.98482 -0.31146 -0.18267 -0.03085 104 GLU A CA  
758  C CA  B GLU A 104 ? 0.92910 0.83251 0.98603 -0.31172 -0.18293 -0.03097 104 GLU A CA  
759  C C   . GLU A 104 ? 0.84514 0.77211 0.93691 -0.30535 -0.19312 -0.04060 104 GLU A C   
760  O O   . GLU A 104 ? 0.85728 0.81054 0.98033 -0.30109 -0.20094 -0.04820 104 GLU A O   
761  C CB  A GLU A 104 ? 0.94134 0.83990 0.98291 -0.33694 -0.17075 -0.04697 104 GLU A CB  
762  C CB  B GLU A 104 ? 0.93791 0.83850 0.98047 -0.33645 -0.17196 -0.04676 104 GLU A CB  
763  C CG  A GLU A 104 ? 0.98058 0.82467 0.97291 -0.35945 -0.13244 -0.05071 104 GLU A CG  
764  C CG  B GLU A 104 ? 0.96534 0.83484 0.96721 -0.35464 -0.15478 -0.04510 104 GLU A CG  
765  C CD  A GLU A 104 ? 1.03856 0.83368 1.01479 -0.34795 -0.07735 -0.05212 104 GLU A CD  
766  C CD  B GLU A 104 ? 1.01899 0.88866 0.99433 -0.38529 -0.12997 -0.06687 104 GLU A CD  
767  O OE1 A GLU A 104 ? 0.98244 0.79226 0.98151 -0.31985 -0.07879 -0.03928 104 GLU A OE1 
768  O OE1 B GLU A 104 ? 1.04079 0.96422 1.03876 -0.38970 -0.14729 -0.07126 104 GLU A OE1 
769  O OE2 A GLU A 104 ? 1.10208 0.84302 1.04190 -0.37104 -0.02663 -0.06604 104 GLU A OE2 
770  O OE2 B GLU A 104 ? 1.04387 0.85936 0.97433 -0.40813 -0.08758 -0.07733 104 GLU A OE2 
771  N N   . HIS A 105 ? 0.86729 0.79657 0.95477 -0.29266 -0.17949 -0.03598 105 HIS A N   
772  C CA  . HIS A 105 ? 0.87296 0.82047 0.98735 -0.29405 -0.18392 -0.05038 105 HIS A CA  
773  C C   . HIS A 105 ? 0.80688 0.74552 0.92749 -0.29999 -0.16623 -0.06539 105 HIS A C   
774  O O   . HIS A 105 ? 0.82145 0.74330 0.91757 -0.29661 -0.13964 -0.05939 105 HIS A O   
775  C CB  . HIS A 105 ? 0.80541 0.77722 0.90519 -0.29106 -0.17792 -0.04071 105 HIS A CB  
776  C CG  . HIS A 105 ? 0.86134 0.84690 0.97906 -0.30435 -0.17525 -0.06350 105 HIS A CG  
777  N ND1 . HIS A 105 ? 0.93528 0.92028 1.06212 -0.30880 -0.15923 -0.07867 105 HIS A ND1 
778  C CD2 . HIS A 105 ? 0.81617 0.80878 0.94147 -0.31864 -0.17807 -0.07753 105 HIS A CD2 
779  C CE1 . HIS A 105 ? 0.88160 0.87342 1.02111 -0.32526 -0.15196 -0.10137 105 HIS A CE1 
780  N NE2 . HIS A 105 ? 0.84024 0.83236 0.97853 -0.33224 -0.15902 -0.10285 105 HIS A NE2 
781  N N   . PRO A 106 ? 0.79401 0.74406 0.95161 -0.30680 -0.17495 -0.08006 106 PRO A N   
782  C CA  . PRO A 106 ? 0.76427 0.71205 0.92691 -0.31599 -0.16001 -0.09375 106 PRO A CA  
783  C C   . PRO A 106 ? 0.84117 0.78004 0.98568 -0.31063 -0.13536 -0.09863 106 PRO A C   
784  O O   . PRO A 106 ? 0.75477 0.67651 0.88222 -0.31570 -0.11324 -0.10299 106 PRO A O   
785  C CB  . PRO A 106 ? 0.72933 0.70468 0.94779 -0.31382 -0.16993 -0.09808 106 PRO A CB  
786  C CG  . PRO A 106 ? 0.81137 0.79798 1.05164 -0.30423 -0.18703 -0.08232 106 PRO A CG  
787  C CD  . PRO A 106 ? 0.83853 0.80570 1.03903 -0.29848 -0.18572 -0.08073 106 PRO A CD  
788  N N   . VAL A 107 ? 0.84714 0.80224 0.99272 -0.30660 -0.13535 -0.09759 107 VAL A N   
789  C CA  . VAL A 107 ? 0.77151 0.74075 0.89920 -0.30720 -0.11494 -0.09349 107 VAL A CA  
790  C C   . VAL A 107 ? 0.72042 0.69707 0.81871 -0.29399 -0.10179 -0.05736 107 VAL A C   
791  O O   . VAL A 107 ? 0.72697 0.69138 0.81556 -0.28475 -0.07406 -0.04184 107 VAL A O   
792  C CB  . VAL A 107 ? 0.85643 0.85394 0.98996 -0.32289 -0.11562 -0.10854 107 VAL A CB  
793  C CG1 . VAL A 107 ? 0.82939 0.87065 0.93517 -0.33072 -0.10096 -0.09013 107 VAL A CG1 
794  C CG2 . VAL A 107 ? 0.82677 0.80961 0.99648 -0.33055 -0.10903 -0.13962 107 VAL A CG2 
795  N N   . TYR A 108 ? 0.74548 0.74224 0.83431 -0.29111 -0.11573 -0.03906 108 TYR A N   
796  C CA  . TYR A 108 ? 0.78159 0.80567 0.85300 -0.27585 -0.10170 0.00695  108 TYR A CA  
797  C C   . TYR A 108 ? 0.81410 0.78999 0.87815 -0.25711 -0.08273 0.02462  108 TYR A C   
798  O O   . TYR A 108 ? 0.72607 0.71377 0.78604 -0.23636 -0.05641 0.07009  108 TYR A O   
799  C CB  . TYR A 108 ? 0.76396 0.84100 0.82584 -0.28751 -0.12349 0.01919  108 TYR A CB  
800  C CG  . TYR A 108 ? 0.80815 0.93469 0.86454 -0.31835 -0.12781 0.00096  108 TYR A CG  
801  C CD1 . TYR A 108 ? 0.73262 0.89913 0.78617 -0.32496 -0.11012 0.01323  108 TYR A CD1 
802  C CD2 . TYR A 108 ? 0.78249 0.91313 0.83443 -0.34577 -0.14229 -0.02995 108 TYR A CD2 
803  C CE1 . TYR A 108 ? 0.72909 0.94539 0.76942 -0.36456 -0.11038 -0.00832 108 TYR A CE1 
804  C CE2 . TYR A 108 ? 0.68094 0.84791 0.71943 -0.38550 -0.13390 -0.05518 108 TYR A CE2 
805  C CZ  . TYR A 108 ? 0.68515 0.89674 0.71536 -0.39737 -0.11963 -0.04633 108 TYR A CZ  
806  O OH  . TYR A 108 ? 0.80086 1.04971 0.81075 -0.44692 -0.10788 -0.07711 108 TYR A OH  
807  N N   . GLY A 109 ? 0.80178 0.73048 0.86573 -0.26705 -0.09017 -0.00603 109 GLY A N   
808  C CA  . GLY A 109 ? 0.83702 0.72033 0.88371 -0.26303 -0.06823 0.00248  109 GLY A CA  
809  C C   . GLY A 109 ? 0.90246 0.80077 0.94424 -0.25661 -0.08913 0.02023  109 GLY A C   
810  O O   . GLY A 109 ? 0.92299 0.84763 0.97445 -0.26579 -0.12870 0.00744  109 GLY A O   
811  N N   . GLU A 110 ? 0.86691 0.74524 0.89730 -0.23923 -0.05649 0.05229  110 GLU A N   
812  C CA  . GLU A 110 ? 0.88287 0.75952 0.90417 -0.23742 -0.07063 0.06242  110 GLU A CA  
813  C C   . GLU A 110 ? 0.94677 0.89047 0.97680 -0.22014 -0.08777 0.10338  110 GLU A C   
814  O O   . GLU A 110 ? 0.95429 0.92955 0.99349 -0.19729 -0.05786 0.15143  110 GLU A O   
815  C CB  . GLU A 110 ? 0.97817 0.78749 0.98045 -0.23505 -0.01750 0.06824  110 GLU A CB  
816  C CG  . GLU A 110 ? 1.07570 0.88628 1.07921 -0.20915 0.00616  0.11290  110 GLU A CG  
817  C CD  . GLU A 110 ? 1.09651 0.82914 1.07330 -0.22469 0.04899  0.09495  110 GLU A CD  
818  O OE1 . GLU A 110 ? 1.15299 0.83954 1.10572 -0.26174 0.06144  0.04817  110 GLU A OE1 
819  O OE2 . GLU A 110 ? 1.22069 0.94406 1.19790 -0.20614 0.07136  0.12638  110 GLU A OE2 
820  N N   . ILE A 111 ? 0.93278 0.90655 0.96237 -0.23454 -0.13328 0.08786  111 ILE A N   
821  C CA  . ILE A 111 ? 0.81036 0.85431 0.83861 -0.23599 -0.15422 0.11328  111 ILE A CA  
822  C C   . ILE A 111 ? 0.89141 0.93237 0.91056 -0.23284 -0.16954 0.12462  111 ILE A C   
823  O O   . ILE A 111 ? 0.89980 0.90387 0.91754 -0.24443 -0.19104 0.09353  111 ILE A O   
824  C CB  . ILE A 111 ? 0.81474 0.88418 0.84605 -0.26352 -0.18240 0.07741  111 ILE A CB  
825  C CG1 . ILE A 111 ? 0.84704 0.93675 0.88384 -0.26928 -0.16618 0.07274  111 ILE A CG1 
826  C CG2 . ILE A 111 ? 0.79026 0.91755 0.80747 -0.28151 -0.20344 0.08808  111 ILE A CG2 
827  C CD1 . ILE A 111 ? 0.84779 0.97445 0.88030 -0.30224 -0.17995 0.04473  111 ILE A CD1 
828  N N   . ARG A 112 ? 0.79555 0.88645 0.81287 -0.21737 -0.15890 0.17537  112 ARG A N   
829  C CA  . ARG A 112 ? 0.84585 0.93018 0.85626 -0.20795 -0.16252 0.19460  112 ARG A CA  
830  C C   . ARG A 112 ? 0.80228 0.96850 0.80387 -0.22311 -0.19390 0.21368  112 ARG A C   
831  O O   . ARG A 112 ? 0.74587 0.99579 0.74767 -0.23188 -0.19374 0.24321  112 ARG A O   
832  C CB  . ARG A 112 ? 0.72657 0.79321 0.74802 -0.17306 -0.10923 0.24584  112 ARG A CB  
833  C CG  . ARG A 112 ? 0.86214 0.91165 0.87695 -0.16337 -0.10537 0.26277  112 ARG A CG  
834  C CD  . ARG A 112 ? 0.87368 0.88769 0.90537 -0.12746 -0.03614 0.31134  112 ARG A CD  
835  N NE  . ARG A 112 ? 0.87444 0.88409 0.90396 -0.11586 -0.02795 0.33599  112 ARG A NE  
836  C CZ  . ARG A 112 ? 0.81749 0.88877 0.87495 -0.08232 -0.00143 0.41186  112 ARG A CZ  
837  N NH1 . ARG A 112 ? 0.92079 1.07553 1.01241 -0.05803 0.01777  0.47761  112 ARG A NH1 
838  N NH2 . ARG A 112 ? 0.91406 0.97193 0.96899 -0.07307 0.00791  0.42844  112 ARG A NH2 
839  N N   . GLY A 113 ? 0.81727 0.84025 0.77385 -0.12378 -0.14787 0.03404  113 GLY A N   
840  C CA  . GLY A 113 ? 0.83303 0.84806 0.77621 -0.12149 -0.14984 0.01620  113 GLY A CA  
841  C C   . GLY A 113 ? 0.77117 0.79108 0.68433 -0.14585 -0.16054 0.01475  113 GLY A C   
842  O O   . GLY A 113 ? 0.86354 0.88033 0.77276 -0.16630 -0.17395 0.03329  113 GLY A O   
843  N N   . ILE A 114 ? 0.78341 0.81264 0.67394 -0.14171 -0.15431 -0.00601 114 ILE A N   
844  C CA  . ILE A 114 ? 0.85045 0.89543 0.71880 -0.16002 -0.15721 -0.00601 114 ILE A CA  
845  C C   . ILE A 114 ? 0.83985 0.87820 0.73082 -0.18252 -0.16997 0.00608  114 ILE A C   
846  O O   . ILE A 114 ? 0.74511 0.76938 0.65969 -0.17949 -0.17576 -0.00067 114 ILE A O   
847  C CB  . ILE A 114 ? 0.94647 1.01478 0.79709 -0.14603 -0.14735 -0.02980 114 ILE A CB  
848  C CG1 . ILE A 114 ? 0.93633 1.00114 0.75636 -0.12080 -0.13428 -0.04085 114 ILE A CG1 
849  C CG2 . ILE A 114 ? 0.74565 0.84275 0.58495 -0.16214 -0.14549 -0.02579 114 ILE A CG2 
850  C CD1 . ILE A 114 ? 0.93165 0.98780 0.71763 -0.12693 -0.13189 -0.02861 114 ILE A CD1 
851  N N   . ILE A 115 ? 0.83802 0.87769 0.71307 -0.20374 -0.17430 0.02421  115 ILE A N   
852  C CA  . ILE A 115 ? 0.79684 0.82573 0.68509 -0.22770 -0.18419 0.04084  115 ILE A CA  
853  C C   . ILE A 115 ? 0.83985 0.89712 0.71008 -0.24333 -0.17314 0.04417  115 ILE A C   
854  O O   . ILE A 115 ? 0.76458 0.83582 0.65925 -0.25790 -0.17312 0.04237  115 ILE A O   
855  C CB  . ILE A 115 ? 0.85349 0.85344 0.73904 -0.23681 -0.19960 0.06611  115 ILE A CB  
856  C CG1 . ILE A 115 ? 0.83057 0.81643 0.75040 -0.21871 -0.20717 0.06597  115 ILE A CG1 
857  C CG2 . ILE A 115 ? 0.85898 0.84009 0.74666 -0.26018 -0.20871 0.08594  115 ILE A CG2 
858  C CD1 . ILE A 115 ? 0.69464 0.65981 0.62696 -0.22545 -0.22765 0.09297  115 ILE A CD1 
859  N N   . ASP A 116 ? 0.75733 0.82299 0.58483 -0.23968 -0.16316 0.04954  116 ASP A N   
860  C CA  . ASP A 116 ? 0.86494 0.96246 0.67160 -0.24670 -0.14534 0.05550  116 ASP A CA  
861  C C   . ASP A 116 ? 0.87165 0.97317 0.70260 -0.27600 -0.14591 0.07587  116 ASP A C   
862  O O   . ASP A 116 ? 0.78706 0.92855 0.64962 -0.28718 -0.13651 0.07429  116 ASP A O   
863  C CB  . ASP A 116 ? 0.84654 0.99103 0.66352 -0.22853 -0.13076 0.03298  116 ASP A CB  
864  C CG  . ASP A 116 ? 0.89327 1.08431 0.70126 -0.23185 -0.10876 0.04252  116 ASP A CG  
865  O OD1 . ASP A 116 ? 0.91077 1.08729 0.66936 -0.23176 -0.09737 0.05948  116 ASP A OD1 
866  O OD2 . ASP A 116 ? 0.83808 1.08037 0.68784 -0.23381 -0.10330 0.03457  116 ASP A OD2 
867  N N   . VAL A 117 ? 0.91878 0.97791 0.73566 -0.28999 -0.15891 0.09748  117 VAL A N   
868  C CA  . VAL A 117 ? 0.99189 1.03995 0.82261 -0.31824 -0.16045 0.12074  117 VAL A CA  
869  C C   . VAL A 117 ? 1.03253 1.07138 0.80662 -0.32476 -0.14731 0.14577  117 VAL A C   
870  O O   . VAL A 117 ? 1.06199 1.05967 0.79058 -0.31812 -0.16065 0.15480  117 VAL A O   
871  C CB  . VAL A 117 ? 0.94718 0.94543 0.79918 -0.32487 -0.18588 0.12804  117 VAL A CB  
872  C CG1 . VAL A 117 ? 0.93339 0.89945 0.76860 -0.34976 -0.18942 0.15982  117 VAL A CG1 
873  C CG2 . VAL A 117 ? 0.84322 0.84445 0.74428 -0.32415 -0.19346 0.10764  117 VAL A CG2 
874  N N   . SER A 118 ? 1.05725 1.13406 0.83349 -0.33768 -0.12185 0.15875  118 SER A N   
875  C CA  . SER A 118 ? 1.07526 1.14725 0.78798 -0.33631 -0.10000 0.18167  118 SER A CA  
876  C C   . SER A 118 ? 1.08362 1.15016 0.80003 -0.36653 -0.08772 0.21594  118 SER A C   
877  O O   . SER A 118 ? 1.13124 1.18646 0.78646 -0.36408 -0.06687 0.23873  118 SER A O   
878  C CB  . SER A 118 ? 1.14528 1.27416 0.84349 -0.31386 -0.06838 0.17074  118 SER A CB  
879  O OG  . SER A 118 ? 1.17161 1.36858 0.93374 -0.32983 -0.04796 0.17696  118 SER A OG  
880  N N   . SER A 119 ? 1.07900 1.14530 0.85715 -0.39412 -0.09957 0.22096  119 SER A N   
881  C CA  . SER A 119 ? 1.12183 1.18407 0.91175 -0.42841 -0.08680 0.25489  119 SER A CA  
882  C C   . SER A 119 ? 1.10277 1.10858 0.92346 -0.44991 -0.11917 0.25801  119 SER A C   
883  O O   . SER A 119 ? 1.07294 1.05681 0.91453 -0.43575 -0.14621 0.23232  119 SER A O   
884  C CB  . SER A 119 ? 1.02507 1.16993 0.87400 -0.44570 -0.05806 0.25990  119 SER A CB  
885  O OG  . SER A 119 ? 1.01566 1.19530 0.92870 -0.44342 -0.07547 0.22753  119 SER A OG  
886  N N   . GLU A 120 ? 1.02965 1.00750 0.84836 -0.48192 -0.11388 0.29154  120 GLU A N   
887  C CA  . GLU A 120 ? 1.15839 1.07005 0.99592 -0.50028 -0.14437 0.29666  120 GLU A CA  
888  C C   . GLU A 120 ? 1.08798 1.01891 0.99631 -0.51337 -0.15936 0.27080  120 GLU A C   
889  O O   . GLU A 120 ? 1.15856 1.04567 1.07767 -0.49991 -0.18836 0.24902  120 GLU A O   
890  C CB  . GLU A 120 ? 1.25255 1.12481 1.06786 -0.53430 -0.13365 0.34063  120 GLU A CB  
891  C CG  . GLU A 120 ? 1.30306 1.14944 1.03541 -0.52090 -0.11837 0.36801  120 GLU A CG  
892  C CD  . GLU A 120 ? 1.46121 1.23057 1.15586 -0.54345 -0.12565 0.40690  120 GLU A CD  
893  O OE1 . GLU A 120 ? 1.52723 1.28742 1.26638 -0.57234 -0.12416 0.41650  120 GLU A OE1 
894  O OE2 . GLU A 120 ? 1.55770 1.27496 1.17822 -0.52470 -0.13562 0.42171  120 GLU A OE2 
895  N N   . GLU A 121 ? 1.07033 1.06673 1.02648 -0.53839 -0.14041 0.27405  121 GLU A N   
896  C CA  . GLU A 121 ? 1.09726 1.11083 1.11665 -0.55374 -0.16035 0.24893  121 GLU A CA  
897  C C   . GLU A 121 ? 1.03076 1.04112 1.04753 -0.51277 -0.17938 0.20583  121 GLU A C   
898  O O   . GLU A 121 ? 1.07916 1.04173 1.10915 -0.51062 -0.20806 0.18459  121 GLU A O   
899  C CB  . GLU A 121 ? 1.12420 1.23290 1.20045 -0.57875 -0.13660 0.25752  121 GLU A CB  
900  C CG  . GLU A 121 ? 1.16325 1.29735 1.30445 -0.59151 -0.16058 0.22978  121 GLU A CG  
901  C CD  . GLU A 121 ? 1.28569 1.33559 1.43200 -0.60605 -0.18890 0.22565  121 GLU A CD  
902  O OE1 . GLU A 121 ? 1.35527 1.37659 1.49868 -0.63216 -0.17925 0.25742  121 GLU A OE1 
903  O OE2 . GLU A 121 ? 1.31373 1.32290 1.46121 -0.58973 -0.21930 0.19073  121 GLU A OE2 
904  N N   . GLU A 122 ? 1.04366 1.09488 1.03456 -0.47791 -0.16258 0.19409  122 GLU A N   
905  C CA  . GLU A 122 ? 0.99253 1.04214 0.97925 -0.44015 -0.17598 0.15751  122 GLU A CA  
906  C C   . GLU A 122 ? 0.99282 0.96744 0.95350 -0.42183 -0.19840 0.15422  122 GLU A C   
907  O O   . GLU A 122 ? 0.95720 0.91505 0.92840 -0.39914 -0.21355 0.12705  122 GLU A O   
908  C CB  . GLU A 122 ? 0.95726 1.05815 0.91634 -0.41031 -0.15308 0.14952  122 GLU A CB  
909  C CG  . GLU A 122 ? 0.79356 0.97772 0.78485 -0.41547 -0.13092 0.14717  122 GLU A CG  
910  C CD  . GLU A 122 ? 0.94484 1.16602 0.89824 -0.37882 -0.10935 0.13659  122 GLU A CD  
911  O OE1 . GLU A 122 ? 0.98512 1.16386 0.88136 -0.35802 -0.11036 0.13728  122 GLU A OE1 
912  O OE2 . GLU A 122 ? 0.94274 1.23321 0.92339 -0.37042 -0.09436 0.12744  122 GLU A OE2 
913  N N   . VAL A 123 ? 1.02990 0.96086 0.95609 -0.42810 -0.20005 0.18291  123 VAL A N   
914  C CA  . VAL A 123 ? 1.09798 0.96407 1.01029 -0.41039 -0.22382 0.18397  123 VAL A CA  
915  C C   . VAL A 123 ? 1.05866 0.87433 0.99743 -0.42003 -0.24410 0.17574  123 VAL A C   
916  O O   . VAL A 123 ? 1.05701 0.83956 1.00095 -0.39245 -0.25959 0.15822  123 VAL A O   
917  C CB  . VAL A 123 ? 1.11374 0.94083 0.98138 -0.41594 -0.22664 0.21848  123 VAL A CB  
918  C CG1 . VAL A 123 ? 1.03543 0.79655 0.90201 -0.40121 -0.25451 0.22424  123 VAL A CG1 
919  C CG2 . VAL A 123 ? 1.01546 0.87128 0.84228 -0.39793 -0.21593 0.22050  123 VAL A CG2 
920  N N   . LEU A 124 ? 1.05411 0.86055 1.00803 -0.45877 -0.24352 0.18921  124 LEU A N   
921  C CA  . LEU A 124 ? 1.10044 0.84123 1.06770 -0.47266 -0.26718 0.18282  124 LEU A CA  
922  C C   . LEU A 124 ? 1.11339 0.87030 1.10755 -0.46236 -0.27759 0.14356  124 LEU A C   
923  O O   . LEU A 124 ? 1.10629 0.80070 1.09269 -0.44419 -0.29821 0.12448  124 LEU A O   
924  C CB  . LEU A 124 ? 1.15929 0.88173 1.13341 -0.52149 -0.26440 0.21266  124 LEU A CB  
925  C CG  . LEU A 124 ? 1.34595 1.01788 1.28167 -0.53184 -0.26046 0.25282  124 LEU A CG  
926  C CD1 . LEU A 124 ? 1.42990 1.00501 1.33912 -0.51083 -0.28803 0.25396  124 LEU A CD1 
927  C CD2 . LEU A 124 ? 1.15916 0.87103 1.06253 -0.52116 -0.23969 0.27264  124 LEU A CD2 
928  N N   . LYS A 125 ? 1.06316 0.89933 1.08347 -0.47008 -0.26396 0.13137  125 LYS A N   
929  C CA  . LYS A 125 ? 1.05333 0.90540 1.08974 -0.45297 -0.27568 0.09303  125 LYS A CA  
930  C C   . LYS A 125 ? 0.97925 0.80235 0.98935 -0.40159 -0.27794 0.07118  125 LYS A C   
931  O O   . LYS A 125 ? 0.95397 0.72761 0.95554 -0.38305 -0.29541 0.04649  125 LYS A O   
932  C CB  . LYS A 125 ? 0.90627 0.85611 0.97044 -0.45733 -0.25791 0.08588  125 LYS A CB  
933  C CG  . LYS A 125 ? 1.06718 1.03668 1.16127 -0.46471 -0.27727 0.05724  125 LYS A CG  
934  C CD  . LYS A 125 ? 1.08468 1.01520 1.19986 -0.49603 -0.29211 0.06479  125 LYS A CD  
935  C CE  . LYS A 125 ? 1.09127 0.98143 1.20269 -0.48322 -0.32153 0.02751  125 LYS A CE  
936  N NZ  . LYS A 125 ? 1.15099 0.99720 1.21779 -0.44003 -0.32890 0.00219  125 LYS A NZ  
937  N N   . PHE A 126 ? 0.95835 0.80515 0.95260 -0.37917 -0.26098 0.08305  126 PHE A N   
938  C CA  . PHE A 126 ? 0.90804 0.74648 0.88961 -0.33425 -0.25885 0.06765  126 PHE A CA  
939  C C   . PHE A 126 ? 0.95374 0.71737 0.92638 -0.31625 -0.27413 0.07255  126 PHE A C   
940  O O   . PHE A 126 ? 0.91732 0.65791 0.88678 -0.28123 -0.27642 0.05181  126 PHE A O   
941  C CB  . PHE A 126 ? 0.84509 0.72663 0.81401 -0.32385 -0.24212 0.08202  126 PHE A CB  
942  C CG  . PHE A 126 ? 0.85178 0.73438 0.81709 -0.28505 -0.23943 0.07156  126 PHE A CG  
943  C CD1 . PHE A 126 ? 0.77951 0.62487 0.74688 -0.26897 -0.24939 0.08644  126 PHE A CD1 
944  C CD2 . PHE A 126 ? 0.82492 0.74807 0.78840 -0.26471 -0.22664 0.04972  126 PHE A CD2 
945  C CE1 . PHE A 126 ? 0.82552 0.68230 0.80250 -0.23651 -0.24512 0.08115  126 PHE A CE1 
946  C CE2 . PHE A 126 ? 0.82730 0.75194 0.79123 -0.23318 -0.22165 0.04437  126 PHE A CE2 
947  C CZ  . PHE A 126 ? 0.81341 0.70932 0.78868 -0.22090 -0.23012 0.06103  126 PHE A CZ  
948  N N   . VAL A 127 ? 1.03807 0.76164 1.00282 -0.33542 -0.28247 0.10165  127 VAL A N   
949  C CA  . VAL A 127 ? 1.06490 0.71786 1.02047 -0.31254 -0.29701 0.10889  127 VAL A CA  
950  C C   . VAL A 127 ? 1.13668 0.72553 1.08435 -0.30956 -0.31210 0.08617  127 VAL A C   
951  O O   . VAL A 127 ? 1.20352 0.74968 1.14170 -0.26928 -0.31596 0.07223  127 VAL A O   
952  C CB  . VAL A 127 ? 1.12385 0.74322 1.06520 -0.33238 -0.30484 0.14668  127 VAL A CB  
953  C CG1 . VAL A 127 ? 1.09099 0.62836 1.02164 -0.30901 -0.32285 0.15486  127 VAL A CG1 
954  C CG2 . VAL A 127 ? 1.05369 0.72282 0.99127 -0.32428 -0.29620 0.16449  127 VAL A CG2 
955  N N   . ASN A 128 ? 1.16644 0.75033 1.11762 -0.35081 -0.32053 0.08123  128 ASN A N   
956  C CA  . ASN A 128 ? 1.17851 0.69692 1.11646 -0.35397 -0.34191 0.05591  128 ASN A CA  
957  C C   . ASN A 128 ? 1.20542 0.73044 1.13277 -0.30974 -0.33867 0.01895  128 ASN A C   
958  O O   . ASN A 128 ? 1.24174 0.69122 1.13871 -0.27712 -0.34913 0.00177  128 ASN A O   
959  C CB  . ASN A 128 ? 1.29290 0.83084 1.25121 -0.41041 -0.35252 0.05723  128 ASN A CB  
960  C CG  . ASN A 128 ? 1.41134 0.91499 1.37025 -0.45141 -0.35619 0.09273  128 ASN A CG  
961  O OD1 . ASN A 128 ? 1.52796 0.96473 1.46164 -0.44107 -0.36198 0.11253  128 ASN A OD1 
962  N ND2 . ASN A 128 ? 1.44925 1.00659 1.43770 -0.48813 -0.34662 0.10248  128 ASN A ND2 
963  N N   . LEU A 129 ? 1.09460 0.70306 1.03946 -0.30582 -0.32314 0.00651  129 LEU A N   
964  C CA  . LEU A 129 ? 1.14931 0.76368 1.07817 -0.26301 -0.31718 -0.02583 129 LEU A CA  
965  C C   . LEU A 129 ? 1.21072 0.79346 1.12540 -0.21131 -0.30409 -0.02307 129 LEU A C   
966  O O   . LEU A 129 ? 1.28488 0.80906 1.16879 -0.17476 -0.30749 -0.04457 129 LEU A O   
967  C CB  . LEU A 129 ? 0.93065 0.63922 0.87792 -0.26256 -0.29873 -0.03225 129 LEU A CB  
968  C CG  . LEU A 129 ? 1.11160 0.82512 1.03951 -0.23606 -0.30106 -0.06812 129 LEU A CG  
969  C CD1 . LEU A 129 ? 1.03894 0.68510 0.94542 -0.24987 -0.33384 -0.09152 129 LEU A CD1 
970  C CD2 . LEU A 129 ? 0.96905 0.77178 0.91698 -0.24677 -0.28921 -0.07109 129 LEU A CD2 
971  N N   . MET A 130 ? 1.16758 0.78807 1.10400 -0.20713 -0.28987 0.00496  130 MET A N   
972  C CA  . MET A 130 ? 1.17166 0.78551 1.11310 -0.16084 -0.27682 0.01328  130 MET A CA  
973  C C   . MET A 130 ? 1.23341 0.75884 1.15582 -0.13835 -0.28931 0.01725  130 MET A C   
974  O O   . MET A 130 ? 1.22822 0.73013 1.14366 -0.08829 -0.27778 0.01022  130 MET A O   
975  C CB  . MET A 130 ? 1.13173 0.80278 1.10172 -0.17050 -0.26896 0.04397  130 MET A CB  
976  C CG  . MET A 130 ? 0.99908 0.69564 0.99238 -0.12930 -0.25480 0.05414  130 MET A CG  
977  S SD  . MET A 130 ? 0.99224 0.74043 0.98724 -0.10139 -0.22877 0.02991  130 MET A SD  
978  C CE  . MET A 130 ? 0.80706 0.63046 0.81504 -0.13360 -0.22448 0.04347  130 MET A CE  
979  N N   . GLU A 131 ? 1.22494 0.69828 1.13625 -0.17183 -0.31021 0.02988  131 GLU A N   
980  C CA  . GLU A 131 ? 1.35539 0.73415 1.24042 -0.14484 -0.32237 0.03311  131 GLU A CA  
981  C C   . GLU A 131 ? 1.46381 0.76726 1.30390 -0.12277 -0.33096 -0.00140 131 GLU A C   
982  O O   . GLU A 131 ? 1.45295 0.66257 1.26061 -0.10334 -0.34386 0.00082  131 GLU A O   
983  C CB  . GLU A 131 ? 1.42011 0.74793 1.29713 -0.18591 -0.34345 0.05903  131 GLU A CB  
984  C CG  . GLU A 131 ? 1.42863 0.78473 1.32901 -0.18150 -0.34017 0.09695  131 GLU A CG  
985  C CD  . GLU A 131 ? 1.56039 0.88676 1.45000 -0.23185 -0.35539 0.12470  131 GLU A CD  
986  O OE1 . GLU A 131 ? 1.46737 0.76606 1.34344 -0.27434 -0.36490 0.11568  131 GLU A OE1 
987  O OE2 . GLU A 131 ? 1.73849 1.07006 1.63364 -0.22971 -0.35859 0.15693  131 GLU A OE2 
988  N N   . MET A 132 ? 1.55102 0.87919 1.37945 -0.12187 -0.32738 -0.03205 132 MET A N   
989  C CA  . MET A 132 ? 1.64275 0.88400 1.41392 -0.10156 -0.34254 -0.06750 132 MET A CA  
990  C C   . MET A 132 ? 1.72352 0.92799 1.46592 -0.02650 -0.31975 -0.07637 132 MET A C   
991  O O   . MET A 132 ? 1.66723 0.90761 1.44286 0.00523  -0.29704 -0.05115 132 MET A O   
992  C CB  . MET A 132 ? 1.59517 0.87582 1.36025 -0.12187 -0.34948 -0.09658 132 MET A CB  
993  C CG  . MET A 132 ? 1.56453 0.90305 1.36797 -0.19004 -0.36564 -0.08801 132 MET A CG  
994  S SD  . MET A 132 ? 1.74022 0.99158 1.53170 -0.24919 -0.40713 -0.08214 132 MET A SD  
995  C CE  . MET A 132 ? 1.60093 0.92921 1.42825 -0.30555 -0.42510 -0.09564 132 MET A CE  
996  N N   . ALA A 133 ? 1.77310 0.90763 1.45288 0.00318  -0.32605 -0.11196 133 ALA A N   
997  C CA  . ALA A 133 ? 1.74265 0.83973 1.38297 0.07884  -0.29906 -0.12425 133 ALA A CA  
998  C C   . ALA A 133 ? 1.72252 0.91073 1.38249 0.10249  -0.26577 -0.13034 133 ALA A C   
999  O O   . ALA A 133 ? 1.63967 0.88129 1.30907 0.06800  -0.27340 -0.14301 133 ALA A O   
1000 C CB  . ALA A 133 ? 1.88343 0.84546 1.42834 0.10212  -0.32299 -0.16123 133 ALA A CB  
1001 N N   . LYS A 134 ? 1.19411 1.55507 1.44486 0.21144  -0.27046 -0.26376 134 LYS A N   
1002 C CA  . LYS A 134 ? 1.14567 1.65011 1.40932 0.22450  -0.22189 -0.23383 134 LYS A CA  
1003 C C   . LYS A 134 ? 1.09260 1.59418 1.36507 0.15699  -0.18876 -0.17211 134 LYS A C   
1004 O O   . LYS A 134 ? 1.04025 1.62729 1.31768 0.15082  -0.15523 -0.14856 134 LYS A O   
1005 C CB  . LYS A 134 ? 1.13122 1.72323 1.37709 0.26694  -0.21493 -0.27455 134 LYS A CB  
1006 C CG  . LYS A 134 ? 1.14769 1.77059 1.38193 0.34872  -0.24348 -0.34223 134 LYS A CG  
1007 C CD  . LYS A 134 ? 1.17812 1.86327 1.43908 0.39032  -0.23459 -0.32874 134 LYS A CD  
1008 C CE  . LYS A 134 ? 1.26720 1.88097 1.52534 0.44767  -0.28684 -0.39243 134 LYS A CE  
1009 N NZ  . LYS A 134 ? 1.26721 1.93553 1.56029 0.48650  -0.28348 -0.37906 134 LYS A NZ  
1010 N N   . THR A 135 ? 1.00153 1.40256 1.27227 0.10918  -0.20066 -0.14649 135 THR A N   
1011 C CA  . THR A 135 ? 0.92198 1.31935 1.19916 0.05458  -0.17322 -0.09407 135 THR A CA  
1012 C C   . THR A 135 ? 0.87734 1.23457 1.16201 0.04529  -0.18503 -0.06685 135 THR A C   
1013 O O   . THR A 135 ? 0.89128 1.15297 1.15856 0.04095  -0.21843 -0.07762 135 THR A O   
1014 C CB  . THR A 135 ? 0.98199 1.30664 1.24104 0.00070  -0.17303 -0.09239 135 THR A CB  
1015 O OG1 . THR A 135 ? 1.05658 1.27397 1.29826 -0.03469 -0.19417 -0.07965 135 THR A OG1 
1016 C CG2 . THR A 135 ? 0.96798 1.28757 1.21918 0.01543  -0.18993 -0.13970 135 THR A CG2 
1017 N N   . GLU A 136 ? 0.77047 1.19951 1.08297 0.04218  -0.16221 -0.03014 136 GLU A N   
1018 C CA  . GLU A 136 ? 0.74158 1.15828 1.07140 0.03794  -0.17483 -0.00519 136 GLU A CA  
1019 C C   . GLU A 136 ? 0.69469 1.10883 1.03186 -0.01114 -0.15666 0.03726  136 GLU A C   
1020 O O   . GLU A 136 ? 0.65568 1.12946 1.00902 -0.02230 -0.12827 0.05473  136 GLU A O   
1021 C CB  . GLU A 136 ? 0.70647 1.23345 1.07967 0.08980  -0.17107 -0.00733 136 GLU A CB  
1022 C CG  . GLU A 136 ? 0.81839 1.36427 1.18259 0.14911  -0.18637 -0.05834 136 GLU A CG  
1023 C CD  . GLU A 136 ? 0.90478 1.33480 1.24750 0.16182  -0.23344 -0.08637 136 GLU A CD  
1024 O OE1 . GLU A 136 ? 0.68815 1.07484 1.03833 0.14556  -0.25126 -0.06151 136 GLU A OE1 
1025 O OE2 . GLU A 136 ? 0.99007 1.36777 1.30818 0.18661  -0.25666 -0.13181 136 GLU A OE2 
1026 N N   . PRO A 137 ? 0.72591 1.07071 1.04951 -0.03756 -0.17616 0.05331  137 PRO A N   
1027 C CA  . PRO A 137 ? 0.66138 0.99619 0.98620 -0.08009 -0.16475 0.08377  137 PRO A CA  
1028 C C   . PRO A 137 ? 0.62659 1.05251 1.01046 -0.07405 -0.15561 0.11096  137 PRO A C   
1029 O O   . PRO A 137 ? 0.55256 1.04758 0.97601 -0.04028 -0.16137 0.11151  137 PRO A O   
1030 C CB  . PRO A 137 ? 0.73409 0.97460 1.01978 -0.10099 -0.19429 0.08843  137 PRO A CB  
1031 C CG  . PRO A 137 ? 0.80375 0.98964 1.06539 -0.07603 -0.21998 0.06491  137 PRO A CG  
1032 C CD  . PRO A 137 ? 0.81042 1.07698 1.11148 -0.02685 -0.21420 0.04261  137 PRO A CD  
1033 N N   . LEU A 138 ? 0.57177 0.99920 0.96599 -0.10777 -0.14272 0.13406  138 LEU A N   
1034 C CA  . LEU A 138 ? 0.56639 1.07270 1.02411 -0.11203 -0.13703 0.16687  138 LEU A CA  
1035 C C   . LEU A 138 ? 0.65974 1.17984 1.15141 -0.10775 -0.16565 0.17610  138 LEU A C   
1036 O O   . LEU A 138 ? 0.67640 1.29385 1.23322 -0.09486 -0.16111 0.19760  138 LEU A O   
1037 C CB  . LEU A 138 ? 0.55482 1.03389 1.01635 -0.14954 -0.12946 0.18582  138 LEU A CB  
1038 C CG  . LEU A 138 ? 0.56409 1.04992 1.00713 -0.14843 -0.10222 0.18095  138 LEU A CG  
1039 C CD1 . LEU A 138 ? 0.52416 0.97830 0.96973 -0.17131 -0.09569 0.19571  138 LEU A CD1 
1040 C CD2 . LEU A 138 ? 0.51975 1.10347 0.98864 -0.11546 -0.08193 0.18877  138 LEU A CD2 
1041 N N   . LEU A 139 ? 0.68540 1.11861 1.13545 -0.11754 -0.19548 0.16273  139 LEU A N   
1042 C CA  . LEU A 139 ? 0.67283 1.11820 1.15470 -0.11201 -0.22915 0.17074  139 LEU A CA  
1043 C C   . LEU A 139 ? 0.69072 1.22451 1.22162 -0.06474 -0.23149 0.16551  139 LEU A C   
1044 O O   . LEU A 139 ? 0.66132 1.24238 1.24406 -0.05647 -0.25501 0.17630  139 LEU A O   
1045 C CB  . LEU A 139 ? 0.74428 1.07921 1.15723 -0.12274 -0.26219 0.15741  139 LEU A CB  
1046 C CG  . LEU A 139 ? 0.78318 1.04845 1.13386 -0.10396 -0.26707 0.13520  139 LEU A CG  
1047 C CD1 . LEU A 139 ? 0.74396 1.02470 1.11641 -0.06003 -0.29685 0.12538  139 LEU A CD1 
1048 C CD2 . LEU A 139 ? 0.76488 0.92165 1.03332 -0.13659 -0.27805 0.13471  139 LEU A CD2 
1049 N N   . THR A 140 ? 0.59489 1.15994 1.11397 -0.03055 -0.20966 0.14558  140 THR A N   
1050 C CA  . THR A 140 ? 0.60671 1.26376 1.16842 0.02369  -0.21105 0.13205  140 THR A CA  
1051 C C   . THR A 140 ? 0.59133 1.38993 1.22870 0.02673  -0.18184 0.16199  140 THR A C   
1052 O O   . THR A 140 ? 0.50991 1.38269 1.18255 0.06566  -0.17893 0.15128  140 THR A O   
1053 C CB  . THR A 140 ? 0.60559 1.24354 1.12352 0.06274  -0.20276 0.09267  140 THR A CB  
1054 O OG1 . THR A 140 ? 0.64799 1.29740 1.14519 0.04359  -0.16853 0.09749  140 THR A OG1 
1055 C CG2 . THR A 140 ? 0.72478 1.22231 1.17814 0.06004  -0.23713 0.06759  140 THR A CG2 
1056 N N   . LEU A 141 ? 0.58583 1.37314 1.21498 -0.01387 -0.15276 0.18711  141 LEU A N   
1057 C CA  . LEU A 141 ? 0.52334 1.37627 1.18519 -0.02291 -0.12285 0.21438  141 LEU A CA  
1058 C C   . LEU A 141 ? 0.68706 1.53221 1.38997 -0.04904 -0.14521 0.23184  141 LEU A C   
1059 O O   . LEU A 141 ? 0.66441 1.58162 1.41189 -0.04995 -0.13087 0.25227  141 LEU A O   
1060 C CB  . LEU A 141 ? 0.53178 1.35817 1.16762 -0.05437 -0.09601 0.23927  141 LEU A CB  
1061 C CG  . LEU A 141 ? 0.40622 1.25268 1.00303 -0.02848 -0.07271 0.22317  141 LEU A CG  
1062 C CD1 . LEU A 141 ? 0.48804 1.28833 1.05783 -0.05945 -0.05818 0.24415  141 LEU A CD1 
1063 C CD2 . LEU A 141 ? 0.48035 1.43180 1.08893 0.00923  -0.04620 0.22608  141 LEU A CD2 
1064 N N   . SER A 142 ? 0.75483 1.51498 1.44090 -0.07115 -0.18248 0.22452  142 SER A N   
1065 C CA  . SER A 142 ? 0.70084 1.42479 1.40793 -0.10629 -0.20728 0.23930  142 SER A CA  
1066 C C   . SER A 142 ? 0.72401 1.44851 1.44885 -0.08815 -0.24892 0.22321  142 SER A C   
1067 O O   . SER A 142 ? 0.75005 1.42694 1.47724 -0.11469 -0.28029 0.22719  142 SER A O   
1068 C CB  . SER A 142 ? 0.72024 1.33761 1.37963 -0.14534 -0.21851 0.24058  142 SER A CB  
1069 O OG  . SER A 142 ? 0.84154 1.42926 1.52199 -0.17860 -0.23442 0.25593  142 SER A OG  
1070 N N   . GLY A 143 ? 0.74806 1.52040 1.48166 -0.03855 -0.25446 0.20209  143 GLY A N   
1071 C CA  . GLY A 143 ? 0.68184 1.44197 1.42447 -0.01341 -0.30052 0.18613  143 GLY A CA  
1072 C C   . GLY A 143 ? 0.67178 1.30626 1.35273 -0.03754 -0.34420 0.18359  143 GLY A C   
1073 O O   . GLY A 143 ? 0.78584 1.39256 1.46528 -0.03226 -0.38515 0.17908  143 GLY A O   
1074 N N   . GLY A 144 ? 0.74100 1.30028 1.36610 -0.06378 -0.33646 0.18541  144 GLY A N   
1075 C CA  . GLY A 144 ? 0.77394 1.20662 1.31648 -0.08515 -0.36833 0.17783  144 GLY A CA  
1076 C C   . GLY A 144 ? 0.76696 1.15333 1.28978 -0.13626 -0.37238 0.18823  144 GLY A C   
1077 O O   . GLY A 144 ? 0.82905 1.12586 1.27014 -0.15617 -0.36353 0.17839  144 GLY A O   
1078 N N   . VAL A 145 ? 0.74015 1.16623 1.31208 -0.15038 -0.36942 0.19754  145 VAL A N   
1079 C CA  . VAL A 145 ? 0.79218 1.15756 1.33855 -0.18924 -0.37839 0.19764  145 VAL A CA  
1080 C C   . VAL A 145 ? 0.79934 1.15742 1.33895 -0.20786 -0.33767 0.20298  145 VAL A C   
1081 O O   . VAL A 145 ? 0.77670 1.20177 1.35906 -0.19801 -0.30043 0.21710  145 VAL A O   
1082 C CB  . VAL A 145 ? 0.82842 1.22949 1.43334 -0.19899 -0.39546 0.20507  145 VAL A CB  
1083 C CG1 . VAL A 145 ? 0.76047 1.27510 1.44612 -0.17368 -0.37723 0.21753  145 VAL A CG1 
1084 C CG2 . VAL A 145 ? 0.75876 1.13150 1.37218 -0.23233 -0.38373 0.21165  145 VAL A CG2 
1085 N N   . HIS A 146 ? 0.76414 1.04267 1.24393 -0.23096 -0.34479 0.18990  146 HIS A N   
1086 C CA  . HIS A 146 ? 0.78677 1.05184 1.25650 -0.24295 -0.31006 0.19012  146 HIS A CA  
1087 C C   . HIS A 146 ? 0.77433 0.95716 1.18689 -0.26432 -0.32879 0.16843  146 HIS A C   
1088 O O   . HIS A 146 ? 0.76815 0.90651 1.13826 -0.26991 -0.36606 0.15394  146 HIS A O   
1089 C CB  . HIS A 146 ? 0.71589 0.99530 1.16236 -0.23138 -0.28104 0.18741  146 HIS A CB  
1090 C CG  . HIS A 146 ? 0.76646 0.97433 1.12562 -0.22775 -0.29039 0.16685  146 HIS A CG  
1091 N ND1 . HIS A 146 ? 0.79787 0.99073 1.13570 -0.20905 -0.31626 0.16481  146 HIS A ND1 
1092 C CD2 . HIS A 146 ? 0.77490 0.92039 1.05774 -0.23763 -0.27265 0.14994  146 HIS A CD2 
1093 C CE1 . HIS A 146 ? 0.83025 0.94723 1.07970 -0.21203 -0.31487 0.15303  146 HIS A CE1 
1094 N NE2 . HIS A 146 ? 0.77063 0.86533 0.98752 -0.23067 -0.28584 0.14413  146 HIS A NE2 
1095 N N   . LEU A 147 ? 0.78424 0.94923 1.18925 -0.27165 -0.30372 0.16341  147 LEU A N   
1096 C CA  . LEU A 147 ? 0.76414 0.86105 1.12143 -0.28617 -0.31858 0.13639  147 LEU A CA  
1097 C C   . LEU A 147 ? 0.75155 0.82819 1.05247 -0.28923 -0.29245 0.12079  147 LEU A C   
1098 O O   . LEU A 147 ? 0.76135 0.87570 1.07436 -0.27801 -0.25614 0.13263  147 LEU A O   
1099 C CB  . LEU A 147 ? 0.73057 0.81882 1.13599 -0.29184 -0.32051 0.14049  147 LEU A CB  
1100 C CG  . LEU A 147 ? 0.82900 0.94015 1.29862 -0.29677 -0.34357 0.16095  147 LEU A CG  
1101 C CD1 . LEU A 147 ? 0.78324 0.88520 1.30300 -0.30576 -0.34217 0.17627  147 LEU A CD1 
1102 C CD2 . LEU A 147 ? 0.76999 0.84123 1.21445 -0.30368 -0.39108 0.13797  147 LEU A CD2 
1103 N N   . HIS A 148 ? 0.74393 0.76244 0.96893 -0.29163 -0.29988 0.08915  148 HIS A N   
1104 C CA  . HIS A 148 ? 0.80587 0.80968 0.97313 -0.28488 -0.26191 0.06921  148 HIS A CA  
1105 C C   . HIS A 148 ? 0.85250 0.81811 1.00250 -0.28479 -0.27355 0.03606  148 HIS A C   
1106 O O   . HIS A 148 ? 0.88706 0.81620 1.02430 -0.28983 -0.31498 0.01811  148 HIS A O   
1107 C CB  . HIS A 148 ? 0.85092 0.83328 0.92865 -0.28363 -0.25077 0.06315  148 HIS A CB  
1108 C CG  . HIS A 148 ? 0.80499 0.81234 0.89430 -0.27864 -0.23409 0.08733  148 HIS A CG  
1109 N ND1 . HIS A 148 ? 0.75558 0.80025 0.87962 -0.27225 -0.19923 0.09385  148 HIS A ND1 
1110 C CD2 . HIS A 148 ? 0.89896 0.89417 0.96749 -0.27514 -0.25247 0.10215  148 HIS A CD2 
1111 C CE1 . HIS A 148 ? 0.75716 0.81017 0.88153 -0.26496 -0.19753 0.10744  148 HIS A CE1 
1112 N NE2 . HIS A 148 ? 0.83008 0.84992 0.92128 -0.26595 -0.22920 0.11323  148 HIS A NE2 
1113 N N   . THR A 149 ? 0.80275 0.77710 0.95420 -0.27536 -0.24123 0.02375  149 THR A N   
1114 C CA  . THR A 149 ? 0.87323 0.81236 0.99422 -0.26473 -0.24723 -0.01777 149 THR A CA  
1115 C C   . THR A 149 ? 0.92030 0.86409 0.94700 -0.25716 -0.21638 -0.04293 149 THR A C   
1116 O O   . THR A 149 ? 0.96851 0.94991 0.98888 -0.25657 -0.17474 -0.03208 149 THR A O   
1117 C CB  . THR A 149 ? 0.92823 0.87671 1.11094 -0.25413 -0.23442 -0.01697 149 THR A CB  
1118 O OG1 . THR A 149 ? 0.85298 0.80464 1.12360 -0.26756 -0.25975 0.01930  149 THR A OG1 
1119 C CG2 . THR A 149 ? 0.90965 0.81417 1.06622 -0.23555 -0.24967 -0.06688 149 THR A CG2 
1120 N N   . ILE A 150 ? 1.01519 0.92605 0.96928 -0.25352 -0.23831 -0.07411 150 ILE A N   
1121 C CA  . ILE A 150 ? 1.08936 1.01210 0.94419 -0.24913 -0.20994 -0.09281 150 ILE A CA  
1122 C C   . ILE A 150 ? 1.16118 1.08091 0.98501 -0.22362 -0.20451 -0.14716 150 ILE A C   
1123 O O   . ILE A 150 ? 1.13359 1.00998 0.97042 -0.21068 -0.24697 -0.18043 150 ILE A O   
1124 C CB  . ILE A 150 ? 1.12490 1.02144 0.90244 -0.25872 -0.23803 -0.08642 150 ILE A CB  
1125 C CG1 . ILE A 150 ? 1.03772 0.93628 0.84750 -0.27604 -0.24677 -0.03734 150 ILE A CG1 
1126 C CG2 . ILE A 150 ? 1.13472 1.04994 0.80470 -0.25661 -0.20563 -0.09864 150 ILE A CG2 
1127 C CD1 . ILE A 150 ? 1.03368 0.96644 0.85596 -0.28404 -0.19989 -0.00979 150 ILE A CD1 
1128 N N   . GLU A 151 ? 1.15866 1.12612 0.94458 -0.21550 -0.15518 -0.15872 151 GLU A N   
1129 C CA  . GLU A 151 ? 1.23472 1.21703 0.98313 -0.18400 -0.14340 -0.21514 151 GLU A CA  
1130 C C   . GLU A 151 ? 1.27438 1.29303 0.91021 -0.18467 -0.11515 -0.22619 151 GLU A C   
1131 O O   . GLU A 151 ? 1.24107 1.28682 0.84575 -0.21305 -0.08711 -0.18219 151 GLU A O   
1132 C CB  . GLU A 151 ? 1.19246 1.22091 1.00381 -0.16799 -0.10686 -0.22271 151 GLU A CB  
1133 C CG  . GLU A 151 ? 1.17538 1.16377 1.07889 -0.15312 -0.13927 -0.22850 151 GLU A CG  
1134 C CD  . GLU A 151 ? 1.17826 1.21486 1.13803 -0.13444 -0.10582 -0.23221 151 GLU A CD  
1135 O OE1 . GLU A 151 ? 1.07893 1.18489 1.00711 -0.12954 -0.05880 -0.24265 151 GLU A OE1 
1136 O OE2 . GLU A 151 ? 1.18587 1.19502 1.22310 -0.12647 -0.12788 -0.22105 151 GLU A OE2 
1137 N N   . ALA A 152 ? 1.43430 1.45319 1.00743 -0.15242 -0.12396 -0.28462 152 ALA A N   
1138 C CA  . ALA A 152 ? 1.50193 1.56770 0.95793 -0.14951 -0.09472 -0.29549 152 ALA A CA  
1139 C C   . ALA A 152 ? 1.59790 1.69509 1.01483 -0.09963 -0.08638 -0.37197 152 ALA A C   
1140 O O   . ALA A 152 ? 1.59103 1.64369 1.06257 -0.06808 -0.12194 -0.41890 152 ALA A O   
1141 C CB  . ALA A 152 ? 1.53865 1.55642 0.91484 -0.16470 -0.13604 -0.27964 152 ALA A CB  
1142 N N   . PRO A 153 ? 1.63009 1.80604 0.95342 -0.09076 -0.04006 -0.38445 153 PRO A N   
1143 C CA  . PRO A 153 ? 1.68510 1.90689 0.96557 -0.03405 -0.02834 -0.46522 153 PRO A CA  
1144 C C   . PRO A 153 ? 1.78726 1.92948 1.02422 0.00415  -0.09687 -0.53306 153 PRO A C   
1145 O O   . PRO A 153 ? 1.81987 1.94060 1.09247 0.05244  -0.11952 -0.60209 153 PRO A O   
1146 C CB  . PRO A 153 ? 1.70782 2.03654 0.88246 -0.04301 0.03432  -0.44864 153 PRO A CB  
1147 C CG  . PRO A 153 ? 1.73006 2.07383 0.93550 -0.10647 0.06527  -0.35685 153 PRO A CG  
1148 C CD  . PRO A 153 ? 1.60967 1.84313 0.87261 -0.13191 0.00683  -0.32257 153 PRO A CD  
1149 N N   . ASP A 154 ? 1.88192 1.97533 1.04527 -0.01494 -0.13640 -0.51714 154 ASP A N   
1150 C CA  . ASP A 154 ? 2.02795 2.05528 1.13423 0.01989  -0.20391 -0.58602 154 ASP A CA  
1151 C C   . ASP A 154 ? 2.03561 1.97227 1.16611 -0.01723 -0.26985 -0.54774 154 ASP A C   
1152 O O   . ASP A 154 ? 1.94338 1.87809 1.11339 -0.06434 -0.25744 -0.46959 154 ASP A O   
1153 C CB  . ASP A 154 ? 2.04216 2.13666 0.99205 0.05031  -0.18185 -0.62595 154 ASP A CB  
1154 C CG  . ASP A 154 ? 2.05789 2.22123 0.93317 0.00596  -0.12780 -0.54514 154 ASP A CG  
1155 O OD1 . ASP A 154 ? 2.08157 2.19229 0.92928 -0.03016 -0.16259 -0.49414 154 ASP A OD1 
1156 O OD2 . ASP A 154 ? 2.00895 2.27849 0.86168 0.00571  -0.05295 -0.52976 154 ASP A OD2 
1157 N N   . GLU A 155 ? 2.07346 1.93695 1.18393 0.00693  -0.34405 -0.60820 155 GLU A N   
1158 C CA  . GLU A 155 ? 2.09027 1.88066 1.22212 -0.02568 -0.41169 -0.57910 155 GLU A CA  
1159 C C   . GLU A 155 ? 2.17290 1.99442 1.18952 -0.04631 -0.40338 -0.53543 155 GLU A C   
1160 O O   . GLU A 155 ? 2.11357 1.90291 1.16394 -0.08370 -0.43275 -0.47828 155 GLU A O   
1161 C CB  . GLU A 155 ? 2.07001 1.78265 1.21905 0.00010  -0.48862 -0.64864 155 GLU A CB  
1162 C CG  . GLU A 155 ? 2.09183 1.76321 1.24311 -0.02860 -0.54557 -0.62085 155 GLU A CG  
1163 C CD  . GLU A 155 ? 2.05197 1.67499 1.34770 -0.07118 -0.58297 -0.56855 155 GLU A CD  
1164 O OE1 . GLU A 155 ? 1.88985 1.51834 1.25929 -0.09053 -0.55819 -0.53241 155 GLU A OE1 
1165 O OE2 . GLU A 155 ? 1.95211 1.54073 1.28856 -0.08435 -0.63464 -0.56270 155 GLU A OE2 
1166 N N   . GLU A 156 ? 2.35929 2.24782 1.24041 -0.02096 -0.36346 -0.55850 156 GLU A N   
1167 C CA  . GLU A 156 ? 2.37068 2.29005 1.13535 -0.04292 -0.35123 -0.50514 156 GLU A CA  
1168 C C   . GLU A 156 ? 2.31722 2.25839 1.13571 -0.09451 -0.30356 -0.40523 156 GLU A C   
1169 O O   . GLU A 156 ? 2.29596 2.20431 1.10127 -0.12496 -0.33132 -0.34775 156 GLU A O   
1170 C CB  . GLU A 156 ? 2.46502 2.46566 1.08522 -0.01039 -0.30318 -0.53660 156 GLU A CB  
1171 C CG  . GLU A 156 ? 2.77992 2.75185 1.30356 0.00285  -0.34498 -0.55959 156 GLU A CG  
1172 C CD  . GLU A 156 ? 2.86870 2.76131 1.47334 0.02069  -0.42197 -0.62273 156 GLU A CD  
1173 O OE1 . GLU A 156 ? 2.79008 2.62177 1.49486 -0.00612 -0.47487 -0.59995 156 GLU A OE1 
1174 O OE2 . GLU A 156 ? 2.99576 2.88804 1.57065 0.06204  -0.42837 -0.69145 156 GLU A OE2 
1175 N N   . THR A 157 ? 2.09616 2.09126 0.97775 -0.10179 -0.23647 -0.38728 157 THR A N   
1176 C CA  . THR A 157 ? 1.99042 2.00227 0.92761 -0.14888 -0.19522 -0.30109 157 THR A CA  
1177 C C   . THR A 157 ? 1.90996 1.84856 0.95927 -0.17403 -0.24312 -0.26582 157 THR A C   
1178 O O   . THR A 157 ? 1.79322 1.71782 0.84806 -0.20741 -0.24285 -0.19866 157 THR A O   
1179 C CB  . THR A 157 ? 1.89238 1.97467 0.89236 -0.14829 -0.12523 -0.30100 157 THR A CB  
1180 O OG1 . THR A 157 ? 1.94806 2.11734 0.84803 -0.12309 -0.07696 -0.33389 157 THR A OG1 
1181 C CG2 . THR A 157 ? 1.66325 1.76011 0.71646 -0.19721 -0.08774 -0.21793 157 THR A CG2 
1182 N N   . MET A 158 ? 1.84296 1.73638 0.98422 -0.15770 -0.28526 -0.30902 158 MET A N   
1183 C CA  . MET A 158 ? 1.74110 1.58131 0.99164 -0.18129 -0.32905 -0.27519 158 MET A CA  
1184 C C   . MET A 158 ? 1.82956 1.63238 1.02922 -0.19336 -0.38458 -0.25269 158 MET A C   
1185 O O   . MET A 158 ? 1.71591 1.51021 0.95390 -0.21945 -0.38923 -0.19299 158 MET A O   
1186 C CB  . MET A 158 ? 1.69605 1.49520 1.04615 -0.16507 -0.36799 -0.32251 158 MET A CB  
1187 C CG  . MET A 158 ? 1.74860 1.56882 1.20749 -0.16778 -0.32722 -0.30871 158 MET A CG  
1188 S SD  . MET A 158 ? 1.48981 1.31322 1.06346 -0.20741 -0.31854 -0.22762 158 MET A SD  
1189 C CE  . MET A 158 ? 1.55300 1.32203 1.14333 -0.22107 -0.39977 -0.22108 158 MET A CE  
1190 N N   . GLU A 159 ? 1.88045 1.66094 0.99469 -0.17005 -0.43205 -0.30452 159 GLU A N   
1191 C CA  . GLU A 159 ? 1.90518 1.65734 0.95742 -0.17761 -0.48731 -0.28494 159 GLU A CA  
1192 C C   . GLU A 159 ? 1.90315 1.68126 0.88050 -0.19824 -0.44919 -0.21335 159 GLU A C   
1193 O O   . GLU A 159 ? 1.88955 1.64434 0.90077 -0.21847 -0.47477 -0.16044 159 GLU A O   
1194 C CB  . GLU A 159 ? 2.06715 1.80476 1.00642 -0.14439 -0.53439 -0.35585 159 GLU A CB  
1195 C CG  . GLU A 159 ? 1.97078 1.67409 1.00711 -0.12614 -0.58086 -0.42131 159 GLU A CG  
1196 C CD  . GLU A 159 ? 1.96048 1.63048 1.14397 -0.15308 -0.62617 -0.38777 159 GLU A CD  
1197 O OE1 . GLU A 159 ? 1.85100 1.52732 1.04085 -0.17377 -0.63603 -0.32933 159 GLU A OE1 
1198 O OE2 . GLU A 159 ? 1.96056 1.60179 1.25480 -0.15209 -0.64825 -0.41603 159 GLU A OE2 
1199 N N   . ARG A 160 ? 1.91436 1.74263 0.79201 -0.19269 -0.38946 -0.21077 160 ARG A N   
1200 C CA  . ARG A 160 ? 1.92779 1.78179 0.74699 -0.22011 -0.34332 -0.13636 160 ARG A CA  
1201 C C   . ARG A 160 ? 1.84493 1.67634 0.78185 -0.25083 -0.33508 -0.07619 160 ARG A C   
1202 O O   . ARG A 160 ? 1.82796 1.62989 0.74512 -0.26907 -0.35441 -0.01855 160 ARG A O   
1203 C CB  . ARG A 160 ? 1.99387 1.92365 0.75657 -0.21594 -0.26567 -0.14612 160 ARG A CB  
1204 C CG  . ARG A 160 ? 2.07647 2.04561 0.73391 -0.24237 -0.21962 -0.07921 160 ARG A CG  
1205 C CD  . ARG A 160 ? 2.16598 2.23107 0.77499 -0.23180 -0.14573 -0.10481 160 ARG A CD  
1206 N NE  . ARG A 160 ? 2.16373 2.24902 0.73088 -0.18023 -0.16343 -0.19854 160 ARG A NE  
1207 C CZ  . ARG A 160 ? 2.28264 2.45543 0.79130 -0.15227 -0.11218 -0.24376 160 ARG A CZ  
1208 N NH1 . ARG A 160 ? 2.34903 2.60449 0.84993 -0.17163 -0.03464 -0.19800 160 ARG A NH1 
1209 N NH2 . ARG A 160 ? 2.35784 2.52814 0.83514 -0.09738 -0.14149 -0.33582 160 ARG A NH2 
1210 N N   . ILE A 161 ? 1.72711 1.57126 0.78448 -0.25232 -0.30951 -0.09126 161 ILE A N   
1211 C CA  . ILE A 161 ? 1.73537 1.56703 0.90146 -0.27512 -0.30037 -0.04296 161 ILE A CA  
1212 C C   . ILE A 161 ? 1.67608 1.46218 0.90323 -0.27454 -0.36613 -0.03154 161 ILE A C   
1213 O O   . ILE A 161 ? 1.56625 1.33489 0.82481 -0.28820 -0.37473 0.01794  161 ILE A O   
1214 C CB  . ILE A 161 ? 1.61942 1.48181 0.89143 -0.27220 -0.26114 -0.06497 161 ILE A CB  
1215 C CG1 . ILE A 161 ? 1.48392 1.40214 0.72546 -0.28336 -0.19014 -0.05130 161 ILE A CG1 
1216 C CG2 . ILE A 161 ? 1.49556 1.34024 0.89182 -0.28276 -0.27643 -0.03720 161 ILE A CG2 
1217 C CD1 . ILE A 161 ? 1.47297 1.43399 0.75724 -0.26154 -0.15841 -0.10345 161 ILE A CD1 
1218 N N   . MET A 162 ? 1.66250 1.43155 0.91681 -0.25799 -0.41518 -0.07918 162 MET A N   
1219 C CA  . MET A 162 ? 1.63218 1.37405 0.95801 -0.26028 -0.47801 -0.06926 162 MET A CA  
1220 C C   . MET A 162 ? 1.68655 1.40525 0.92457 -0.25994 -0.51820 -0.03886 162 MET A C   
1221 O O   . MET A 162 ? 1.64020 1.34823 0.93432 -0.26490 -0.54755 -0.00216 162 MET A O   
1222 C CB  . MET A 162 ? 1.70212 1.42823 1.07539 -0.24888 -0.52606 -0.12688 162 MET A CB  
1223 C CG  . MET A 162 ? 1.59372 1.33086 1.07027 -0.24911 -0.49818 -0.14910 162 MET A CG  
1224 S SD  . MET A 162 ? 1.41388 1.17152 1.05234 -0.26913 -0.49158 -0.09948 162 MET A SD  
1225 C CE  . MET A 162 ? 1.39480 1.13723 1.08787 -0.27658 -0.57566 -0.09571 162 MET A CE  
1226 N N   . ARG A 163 ? 1.74467 1.45982 0.84264 -0.25020 -0.52122 -0.05374 163 ARG A N   
1227 C CA  . ARG A 163 ? 1.84680 1.53886 0.84548 -0.25007 -0.55559 -0.01488 163 ARG A CA  
1228 C C   . ARG A 163 ? 1.79753 1.47826 0.81880 -0.26877 -0.52902 0.05659  163 ARG A C   
1229 O O   . ARG A 163 ? 1.79585 1.44865 0.84282 -0.26659 -0.57453 0.08991  163 ARG A O   
1230 C CB  . ARG A 163 ? 1.94086 1.64894 0.78089 -0.23735 -0.53813 -0.03047 163 ARG A CB  
1231 C CG  . ARG A 163 ? 2.10962 1.82025 0.91769 -0.20444 -0.58944 -0.08259 163 ARG A CG  
1232 C CD  . ARG A 163 ? 2.17652 1.92249 0.82969 -0.18437 -0.56501 -0.09832 163 ARG A CD  
1233 N NE  . ARG A 163 ? 2.17864 1.96178 0.78891 -0.18260 -0.50666 -0.13268 163 ARG A NE  
1234 C CZ  . ARG A 163 ? 2.21518 2.00781 0.84980 -0.16009 -0.51392 -0.21218 163 ARG A CZ  
1235 N NH1 . ARG A 163 ? 2.18670 1.95308 0.89674 -0.14458 -0.57511 -0.26195 163 ARG A NH1 
1236 N NH2 . ARG A 163 ? 2.17907 2.01043 0.77244 -0.15422 -0.45651 -0.24102 163 ARG A NH2 
1237 N N   . GLU A 164 ? 1.71700 1.41922 0.73657 -0.28538 -0.45929 0.07733  164 GLU A N   
1238 C CA  . GLU A 164 ? 1.74654 1.42771 0.78005 -0.30510 -0.43884 0.14169  164 GLU A CA  
1239 C C   . GLU A 164 ? 1.67192 1.34153 0.84479 -0.30044 -0.46122 0.14948  164 GLU A C   
1240 O O   . GLU A 164 ? 1.59844 1.23199 0.78019 -0.29862 -0.49208 0.19003  164 GLU A O   
1241 C CB  . GLU A 164 ? 1.73614 1.44995 0.75230 -0.32779 -0.36269 0.15754  164 GLU A CB  
1242 C CG  . GLU A 164 ? 1.89582 1.62255 0.76376 -0.34062 -0.33753 0.18426  164 GLU A CG  
1243 C CD  . GLU A 164 ? 1.96508 1.63463 0.75521 -0.35108 -0.37586 0.24990  164 GLU A CD  
1244 O OE1 . GLU A 164 ? 2.06816 1.69037 0.93016 -0.35676 -0.39870 0.28455  164 GLU A OE1 
1245 O OE2 . GLU A 164 ? 2.03891 1.71748 0.72251 -0.34243 -0.37753 0.26029  164 GLU A OE2 
1246 N N   . LEU A 165 ? 1.57111 1.27360 0.85222 -0.29529 -0.44764 0.11122  165 LEU A N   
1247 C CA  . LEU A 165 ? 1.46768 1.17794 0.87971 -0.28883 -0.46556 0.11737  165 LEU A CA  
1248 C C   . LEU A 165 ? 1.51212 1.20724 0.94363 -0.27355 -0.53652 0.12180  165 LEU A C   
1249 O O   . LEU A 165 ? 1.47028 1.16506 0.97077 -0.26450 -0.55553 0.14650  165 LEU A O   
1250 C CB  . LEU A 165 ? 1.35982 1.10928 0.87032 -0.28773 -0.44436 0.07999  165 LEU A CB  
1251 C CG  . LEU A 165 ? 1.31916 1.09380 0.84712 -0.29779 -0.37752 0.07805  165 LEU A CG  
1252 C CD1 . LEU A 165 ? 1.13375 0.93882 0.75291 -0.29289 -0.36716 0.04428  165 LEU A CD1 
1253 C CD2 . LEU A 165 ? 1.23508 1.00742 0.80260 -0.30405 -0.35632 0.11658  165 LEU A CD2 
1254 N N   . LYS A 166 ? 1.48360 1.17141 0.85890 -0.26693 -0.57933 0.09352  166 LYS A N   
1255 C CA  . LYS A 166 ? 1.51473 1.19847 0.92341 -0.25136 -0.64616 0.09469  166 LYS A CA  
1256 C C   . LYS A 166 ? 1.59691 1.24403 0.93620 -0.24001 -0.66425 0.13895  166 LYS A C   
1257 O O   . LYS A 166 ? 1.57286 1.22258 0.98575 -0.22361 -0.69092 0.15790  166 LYS A O   
1258 C CB  . LYS A 166 ? 1.63792 1.32732 1.02531 -0.24074 -0.67524 0.04632  166 LYS A CB  
1259 C CG  . LYS A 166 ? 1.60527 1.30622 1.05434 -0.22212 -0.72845 0.04279  166 LYS A CG  
1260 C CD  . LYS A 166 ? 1.58910 1.31430 1.12138 -0.22269 -0.75065 -0.00434 166 LYS A CD  
1261 C CE  . LYS A 166 ? 1.64183 1.38076 1.21228 -0.20804 -0.80432 -0.00899 166 LYS A CE  
1262 N NZ  . LYS A 166 ? 1.67676 1.42356 1.28696 -0.21071 -0.83290 -0.05763 166 LYS A NZ  
1263 N N   . LYS A 167 ? 1.70026 1.31695 0.90234 -0.24680 -0.64717 0.15725  167 LYS A N   
1264 C CA  . LYS A 167 ? 1.79311 1.36952 0.93515 -0.23625 -0.66707 0.20289  167 LYS A CA  
1265 C C   . LYS A 167 ? 1.75019 1.29592 0.93554 -0.24269 -0.65344 0.24858  167 LYS A C   
1266 O O   . LYS A 167 ? 1.79908 1.31068 0.99124 -0.22496 -0.68391 0.27780  167 LYS A O   
1267 C CB  . LYS A 167 ? 1.92621 1.48886 0.91582 -0.24189 -0.64933 0.21596  167 LYS A CB  
1268 C CG  . LYS A 167 ? 1.94893 1.50724 0.85968 -0.27149 -0.58679 0.24658  167 LYS A CG  
1269 C CD  . LYS A 167 ? 2.18344 1.74545 0.95259 -0.26734 -0.57782 0.26216  167 LYS A CD  
1270 C CE  . LYS A 167 ? 2.22691 1.80721 0.91613 -0.29676 -0.50834 0.29370  167 LYS A CE  
1271 N NZ  . LYS A 167 ? 2.20618 1.74176 0.87352 -0.31599 -0.49679 0.36781  167 LYS A NZ  
1272 N N   . LYS A 168 ? 1.66436 1.22166 0.88568 -0.26406 -0.61245 0.25059  168 LYS A N   
1273 C CA  . LYS A 168 ? 1.65085 1.18858 0.94736 -0.26110 -0.60078 0.27759  168 LYS A CA  
1274 C C   . LYS A 168 ? 1.53316 1.10531 0.96319 -0.23216 -0.63454 0.25809  168 LYS A C   
1275 O O   . LYS A 168 ? 1.49500 1.04941 0.97956 -0.21663 -0.64096 0.27609  168 LYS A O   
1276 C CB  . LYS A 168 ? 1.62615 1.18387 0.95078 -0.28532 -0.52796 0.27339  168 LYS A CB  
1277 C CG  . LYS A 168 ? 1.73892 1.26607 0.95372 -0.31755 -0.48929 0.30966  168 LYS A CG  
1278 C CD  . LYS A 168 ? 1.70818 1.25974 0.97556 -0.34041 -0.42492 0.30655  168 LYS A CD  
1279 C CE  . LYS A 168 ? 1.80186 1.31408 0.99150 -0.37686 -0.39738 0.35899  168 LYS A CE  
1280 N NZ  . LYS A 168 ? 1.91592 1.43129 0.96960 -0.39430 -0.38966 0.38208  168 LYS A NZ  
1281 N N   . GLY A 169 ? 1.53169 1.15507 1.01801 -0.22418 -0.65759 0.22178  169 GLY A N   
1282 C CA  . GLY A 169 ? 1.44943 1.12365 1.07078 -0.19923 -0.67950 0.20781  169 GLY A CA  
1283 C C   . GLY A 169 ? 1.31529 1.04853 1.04690 -0.20520 -0.64104 0.19222  169 GLY A C   
1284 O O   . GLY A 169 ? 1.27234 1.04688 1.10389 -0.18335 -0.64793 0.19509  169 GLY A O   
1285 N N   . PHE A 170 ? 1.25651 1.00144 0.97549 -0.22885 -0.59305 0.17347  170 PHE A N   
1286 C CA  . PHE A 170 ? 1.27427 1.07385 1.09339 -0.23327 -0.54871 0.16035  170 PHE A CA  
1287 C C   . PHE A 170 ? 1.21999 1.06921 1.11565 -0.24181 -0.56142 0.13503  170 PHE A C   
1288 O O   . PHE A 170 ? 1.18293 1.08722 1.17913 -0.24285 -0.53683 0.13355  170 PHE A O   
1289 C CB  . PHE A 170 ? 1.22120 1.00359 0.99091 -0.25221 -0.48768 0.15821  170 PHE A CB  
1290 C CG  . PHE A 170 ? 1.31355 1.05819 1.04882 -0.25100 -0.46746 0.18479  170 PHE A CG  
1291 C CD1 . PHE A 170 ? 1.28555 1.04285 1.09336 -0.22857 -0.47388 0.19390  170 PHE A CD1 
1292 C CD2 . PHE A 170 ? 1.38414 1.08381 1.01736 -0.27266 -0.44275 0.19960  170 PHE A CD2 
1293 C CE1 . PHE A 170 ? 1.23491 0.94498 1.01476 -0.22749 -0.46304 0.21286  170 PHE A CE1 
1294 C CE2 . PHE A 170 ? 1.40465 1.06300 1.01509 -0.27946 -0.42840 0.22763  170 PHE A CE2 
1295 C CZ  . PHE A 170 ? 1.30480 0.96025 0.98908 -0.25661 -0.44239 0.23207  170 PHE A CZ  
1296 N N   . LEU A 171 ? 1.22458 1.05360 1.07365 -0.24889 -0.60120 0.11617  171 LEU A N   
1297 C CA  . LEU A 171 ? 1.27639 1.13360 1.19329 -0.25794 -0.60584 0.08837  171 LEU A CA  
1298 C C   . LEU A 171 ? 1.29777 1.21151 1.33613 -0.24602 -0.62313 0.09603  171 LEU A C   
1299 O O   . LEU A 171 ? 1.10848 1.03029 1.15301 -0.22692 -0.65270 0.10832  171 LEU A O   
1300 C CB  . LEU A 171 ? 1.38943 1.20351 1.21396 -0.26000 -0.63244 0.05654  171 LEU A CB  
1301 C CG  . LEU A 171 ? 1.37112 1.15417 1.10151 -0.27358 -0.60215 0.03744  171 LEU A CG  
1302 C CD1 . LEU A 171 ? 1.32869 1.08593 0.99540 -0.26931 -0.62416 -0.00851 171 LEU A CD1 
1303 C CD2 . LEU A 171 ? 1.13375 0.94898 0.95269 -0.28153 -0.54979 0.03904  171 LEU A CD2 
1304 N N   . ILE A 172 ? 1.22238 1.17736 1.35609 -0.25731 -0.60230 0.09118  172 ILE A N   
1305 C CA  . ILE A 172 ? 1.18663 1.19550 1.42650 -0.25606 -0.61784 0.09607  172 ILE A CA  
1306 C C   . ILE A 172 ? 1.31072 1.28234 1.52386 -0.26519 -0.65695 0.06608  172 ILE A C   
1307 O O   . ILE A 172 ? 1.37620 1.31441 1.57160 -0.27852 -0.65022 0.04335  172 ILE A O   
1308 C CB  . ILE A 172 ? 1.10230 1.16800 1.44427 -0.26630 -0.57598 0.11266  172 ILE A CB  
1309 C CG1 . ILE A 172 ? 1.02077 1.13730 1.39347 -0.24944 -0.54364 0.13749  172 ILE A CG1 
1310 C CG2 . ILE A 172 ? 1.16163 1.27406 1.59998 -0.27547 -0.59183 0.11857  172 ILE A CG2 
1311 C CD1 . ILE A 172 ? 1.16006 1.30446 1.54390 -0.22333 -0.57158 0.14560  172 ILE A CD1 
1312 N N   . GLU A 173 ? 1.42894 1.40495 1.63682 -0.25433 -0.70064 0.06217  173 GLU A N   
1313 C CA  . GLU A 173 ? 1.50407 1.44574 1.67962 -0.25978 -0.74335 0.02964  173 GLU A CA  
1314 C C   . GLU A 173 ? 1.48257 1.47580 1.75927 -0.26344 -0.77574 0.03412  173 GLU A C   
1315 O O   . GLU A 173 ? 1.50540 1.52613 1.87486 -0.28344 -0.76880 0.03726  173 GLU A O   
1316 C CB  . GLU A 173 ? 1.59871 1.48618 1.63573 -0.24360 -0.77090 0.01457  173 GLU A CB  
1317 C CG  . GLU A 173 ? 1.60717 1.44241 1.53041 -0.24666 -0.74387 0.00002  173 GLU A CG  
1318 C CD  . GLU A 173 ? 1.65173 1.46099 1.56711 -0.25746 -0.74382 -0.04212 173 GLU A CD  
1319 O OE1 . GLU A 173 ? 1.80216 1.59223 1.68955 -0.25283 -0.78430 -0.07529 173 GLU A OE1 
1320 O OE2 . GLU A 173 ? 1.65750 1.46436 1.59547 -0.26787 -0.70586 -0.04437 173 GLU A OE2 
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