data_9H1F
# 
_entry.id   9H1F 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9H1F         pdb_00009h1f 10.2210/pdb9h1f/pdb 
WWPDB D_1292142328 ?            ?                   
# 
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 2025-03-19 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.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.journal_volume'          
7 2 'Structure model' '_citation.page_last'               
8 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
9 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H1F 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              s.windhorst@uke.de 
_pdbx_contact_author.name_first         Sabine 
_pdbx_contact_author.name_last          Windhorst 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6712-1259 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Paraschiakos, T.' 1 0000-0003-1736-2561 
'Windhorst, S.'    2 0000-0002-6712-1259 
'Pogenberg, V.'    3 0000-0002-1021-6804 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Biochem Pharmacol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1873-2968 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            236 
_citation.language                  ? 
_citation.page_first                116866 
_citation.page_last                 116866 
_citation.title                     'A high affinity Sybody blocks Cofilin-1 binding to F-actin in vitro and in cancer cells.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bcp.2025.116866 
_citation.pdbx_database_id_PubMed   40064451 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Paraschiakos, T.' 1 ? 
primary 'Li, J.'           2 ? 
primary 'Scholz, J.'       3 ? 
primary 'Han, S.J.'        4 ? 
primary 'Deckers, M.'      5 ? 
primary 'Pogenberg, V.'    6 ? 
primary 'Faix, J.'         7 ? 
primary 'Windhorst, S.'    8 ? 
# 
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 Cofilin-1 19135.133 1   ? ? ? ? 
2 polymer man SybodyB12 12652.074 1   ? ? ? ? 
3 water   nat water     18.015    183 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '18 kDa phosphoprotein,p18,Cofilin,non-muscle isoform' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;SNIGSGSMASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVK
MLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKL
GGSAVISLEGKPL
;
;SNIGSGSMASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVK
MLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKL
GGSAVISLEGKPL
;
A ? 
2 'polypeptide(L)' no no 
;GHQVQLVESGGGLVQAGGSLRLSCAASGFPVNHRTMAWYRQAPGKEREWVAAIESHGQETWYADSVKGRFTISRDNAKNT
VYLQMNSLKPEDTAVYYCVRVGAEYVGQGTQVTVSA
;
;GHQVQLVESGGGLVQAGGSLRLSCAASGFPVNHRTMAWYRQAPGKEREWVAAIESHGQETWYADSVKGRFTISRDNAKNT
VYLQMNSLKPEDTAVYYCVRVGAEYVGQGTQVTVSA
;
B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASN n 
1 3   ILE n 
1 4   GLY n 
1 5   SER n 
1 6   GLY n 
1 7   SER n 
1 8   MET n 
1 9   ALA n 
1 10  SER n 
1 11  GLY n 
1 12  VAL n 
1 13  ALA n 
1 14  VAL n 
1 15  SER n 
1 16  ASP n 
1 17  GLY n 
1 18  VAL n 
1 19  ILE n 
1 20  LYS n 
1 21  VAL n 
1 22  PHE n 
1 23  ASN n 
1 24  ASP n 
1 25  MET n 
1 26  LYS n 
1 27  VAL n 
1 28  ARG n 
1 29  LYS n 
1 30  SER n 
1 31  SER n 
1 32  THR n 
1 33  PRO n 
1 34  GLU n 
1 35  GLU n 
1 36  VAL n 
1 37  LYS n 
1 38  LYS n 
1 39  ARG n 
1 40  LYS n 
1 41  LYS n 
1 42  ALA n 
1 43  VAL n 
1 44  LEU n 
1 45  PHE n 
1 46  CYS n 
1 47  LEU n 
1 48  SER n 
1 49  GLU n 
1 50  ASP n 
1 51  LYS n 
1 52  LYS n 
1 53  ASN n 
1 54  ILE n 
1 55  ILE n 
1 56  LEU n 
1 57  GLU n 
1 58  GLU n 
1 59  GLY n 
1 60  LYS n 
1 61  GLU n 
1 62  ILE n 
1 63  LEU n 
1 64  VAL n 
1 65  GLY n 
1 66  ASP n 
1 67  VAL n 
1 68  GLY n 
1 69  GLN n 
1 70  THR n 
1 71  VAL n 
1 72  ASP n 
1 73  ASP n 
1 74  PRO n 
1 75  TYR n 
1 76  ALA n 
1 77  THR n 
1 78  PHE n 
1 79  VAL n 
1 80  LYS n 
1 81  MET n 
1 82  LEU n 
1 83  PRO n 
1 84  ASP n 
1 85  LYS n 
1 86  ASP n 
1 87  CYS n 
1 88  ARG n 
1 89  TYR n 
1 90  ALA n 
1 91  LEU n 
1 92  TYR n 
1 93  ASP n 
1 94  ALA n 
1 95  THR n 
1 96  TYR n 
1 97  GLU n 
1 98  THR n 
1 99  LYS n 
1 100 GLU n 
1 101 SER n 
1 102 LYS n 
1 103 LYS n 
1 104 GLU n 
1 105 ASP n 
1 106 LEU n 
1 107 VAL n 
1 108 PHE n 
1 109 ILE n 
1 110 PHE n 
1 111 TRP n 
1 112 ALA n 
1 113 PRO n 
1 114 GLU n 
1 115 SER n 
1 116 ALA n 
1 117 PRO n 
1 118 LEU n 
1 119 LYS n 
1 120 SER n 
1 121 LYS n 
1 122 MET n 
1 123 ILE n 
1 124 TYR n 
1 125 ALA n 
1 126 SER n 
1 127 SER n 
1 128 LYS n 
1 129 ASP n 
1 130 ALA n 
1 131 ILE n 
1 132 LYS n 
1 133 LYS n 
1 134 LYS n 
1 135 LEU n 
1 136 THR n 
1 137 GLY n 
1 138 ILE n 
1 139 LYS n 
1 140 HIS n 
1 141 GLU n 
1 142 LEU n 
1 143 GLN n 
1 144 ALA n 
1 145 ASN n 
1 146 CYS n 
1 147 TYR n 
1 148 GLU n 
1 149 GLU n 
1 150 VAL n 
1 151 LYS n 
1 152 ASP n 
1 153 ARG n 
1 154 CYS n 
1 155 THR n 
1 156 LEU n 
1 157 ALA n 
1 158 GLU n 
1 159 LYS n 
1 160 LEU n 
1 161 GLY n 
1 162 GLY n 
1 163 SER n 
1 164 ALA n 
1 165 VAL n 
1 166 ILE n 
1 167 SER n 
1 168 LEU n 
1 169 GLU n 
1 170 GLY n 
1 171 LYS n 
1 172 PRO n 
1 173 LEU n 
2 1   GLY n 
2 2   HIS n 
2 3   GLN n 
2 4   VAL n 
2 5   GLN n 
2 6   LEU n 
2 7   VAL n 
2 8   GLU n 
2 9   SER n 
2 10  GLY n 
2 11  GLY n 
2 12  GLY n 
2 13  LEU n 
2 14  VAL n 
2 15  GLN n 
2 16  ALA n 
2 17  GLY n 
2 18  GLY n 
2 19  SER n 
2 20  LEU n 
2 21  ARG n 
2 22  LEU n 
2 23  SER n 
2 24  CYS n 
2 25  ALA n 
2 26  ALA n 
2 27  SER n 
2 28  GLY n 
2 29  PHE n 
2 30  PRO n 
2 31  VAL n 
2 32  ASN n 
2 33  HIS n 
2 34  ARG n 
2 35  THR n 
2 36  MET n 
2 37  ALA n 
2 38  TRP n 
2 39  TYR n 
2 40  ARG n 
2 41  GLN n 
2 42  ALA n 
2 43  PRO n 
2 44  GLY n 
2 45  LYS n 
2 46  GLU n 
2 47  ARG n 
2 48  GLU n 
2 49  TRP n 
2 50  VAL n 
2 51  ALA n 
2 52  ALA n 
2 53  ILE n 
2 54  GLU n 
2 55  SER n 
2 56  HIS n 
2 57  GLY n 
2 58  GLN n 
2 59  GLU n 
2 60  THR n 
2 61  TRP n 
2 62  TYR n 
2 63  ALA n 
2 64  ASP n 
2 65  SER n 
2 66  VAL n 
2 67  LYS n 
2 68  GLY n 
2 69  ARG n 
2 70  PHE n 
2 71  THR n 
2 72  ILE n 
2 73  SER n 
2 74  ARG n 
2 75  ASP n 
2 76  ASN n 
2 77  ALA n 
2 78  LYS n 
2 79  ASN n 
2 80  THR n 
2 81  VAL n 
2 82  TYR n 
2 83  LEU n 
2 84  GLN n 
2 85  MET n 
2 86  ASN n 
2 87  SER n 
2 88  LEU n 
2 89  LYS n 
2 90  PRO n 
2 91  GLU n 
2 92  ASP n 
2 93  THR n 
2 94  ALA n 
2 95  VAL n 
2 96  TYR n 
2 97  TYR n 
2 98  CYS n 
2 99  VAL n 
2 100 ARG n 
2 101 VAL n 
2 102 GLY n 
2 103 ALA n 
2 104 GLU n 
2 105 TYR n 
2 106 VAL n 
2 107 GLY n 
2 108 GLN n 
2 109 GLY n 
2 110 THR n 
2 111 GLN n 
2 112 VAL n 
2 113 THR n 
2 114 VAL n 
2 115 SER n 
2 116 ALA n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 173 human ? 'CFL1, CFL' ? ? ? ? ? ? 'Homo sapiens'        9606  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 116 ?     ? ?           ? ? ? ? ? ? 'synthetic construct' 32630 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   ASN 2   2   ?   ?   ?   A . n 
A 1 3   ILE 3   3   ?   ?   ?   A . n 
A 1 4   GLY 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   ?   ?   ?   A . n 
A 1 8   MET 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  SER 10  10  ?   ?   ?   A . n 
A 1 11  GLY 11  11  ?   ?   ?   A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  MET 25  25  25  MET MET A . n 
A 1 26  LYS 26  26  26  LYS LYS A . n 
A 1 27  VAL 27  27  ?   ?   ?   A . n 
A 1 28  ARG 28  28  ?   ?   ?   A . n 
A 1 29  LYS 29  29  ?   ?   ?   A . n 
A 1 30  SER 30  30  ?   ?   ?   A . n 
A 1 31  SER 31  31  ?   ?   ?   A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  CYS 46  46  46  CYS CYS A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  ILE 54  54  54  ILE ILE A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  MET 81  81  81  MET MET A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  CYS 87  87  87  CYS CYS A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  TYR 89  89  89  TYR TYR A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  TYR 92  92  92  TYR TYR A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 LYS 103 103 103 LYS LYS A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 TRP 111 111 111 TRP TRP A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 MET 122 122 122 MET MET A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 TYR 124 124 124 TYR TYR A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 HIS 140 140 140 HIS HIS A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 GLN 143 143 143 GLN GLN A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 TYR 147 147 147 TYR TYR A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 ASP 152 152 152 ASP ASP A . n 
A 1 153 ARG 153 153 153 ARG ARG A . n 
A 1 154 CYS 154 154 154 CYS CYS A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
B 2 1   GLY 1   1   ?   ?   ?   B . n 
B 2 2   HIS 2   2   ?   ?   ?   B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   VAL 4   4   4   VAL VAL B . n 
B 2 5   GLN 5   5   5   GLN GLN B . n 
B 2 6   LEU 6   6   6   LEU LEU B . n 
B 2 7   VAL 7   7   7   VAL VAL B . n 
B 2 8   GLU 8   8   8   GLU GLU B . n 
B 2 9   SER 9   9   9   SER SER B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  GLY 11  11  11  GLY GLY B . n 
B 2 12  GLY 12  12  12  GLY GLY B . n 
B 2 13  LEU 13  13  13  LEU LEU B . n 
B 2 14  VAL 14  14  14  VAL VAL B . n 
B 2 15  GLN 15  15  15  GLN GLN B . n 
B 2 16  ALA 16  16  16  ALA ALA B . n 
B 2 17  GLY 17  17  17  GLY GLY B . n 
B 2 18  GLY 18  18  18  GLY GLY B . n 
B 2 19  SER 19  19  19  SER SER B . n 
B 2 20  LEU 20  20  20  LEU LEU B . n 
B 2 21  ARG 21  21  21  ARG ARG B . n 
B 2 22  LEU 22  22  22  LEU LEU B . n 
B 2 23  SER 23  23  23  SER SER B . n 
B 2 24  CYS 24  24  24  CYS CYS B . n 
B 2 25  ALA 25  25  25  ALA ALA B . n 
B 2 26  ALA 26  26  26  ALA ALA B . n 
B 2 27  SER 27  27  27  SER SER B . n 
B 2 28  GLY 28  28  28  GLY GLY B . n 
B 2 29  PHE 29  29  29  PHE PHE B . n 
B 2 30  PRO 30  30  30  PRO PRO B . n 
B 2 31  VAL 31  31  31  VAL VAL B . n 
B 2 32  ASN 32  32  32  ASN ASN B . n 
B 2 33  HIS 33  33  33  HIS HIS B . n 
B 2 34  ARG 34  34  34  ARG ARG B . n 
B 2 35  THR 35  35  35  THR THR B . n 
B 2 36  MET 36  36  36  MET MET B . n 
B 2 37  ALA 37  37  37  ALA ALA B . n 
B 2 38  TRP 38  38  38  TRP TRP B . n 
B 2 39  TYR 39  39  39  TYR TYR B . n 
B 2 40  ARG 40  40  40  ARG ARG B . n 
B 2 41  GLN 41  41  41  GLN GLN B . n 
B 2 42  ALA 42  42  42  ALA ALA B . n 
B 2 43  PRO 43  43  43  PRO PRO B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  LYS 45  45  45  LYS LYS B . n 
B 2 46  GLU 46  46  46  GLU GLU B . n 
B 2 47  ARG 47  47  47  ARG ARG B . n 
B 2 48  GLU 48  48  48  GLU GLU B . n 
B 2 49  TRP 49  49  49  TRP TRP B . n 
B 2 50  VAL 50  50  50  VAL VAL B . n 
B 2 51  ALA 51  51  51  ALA ALA B . n 
B 2 52  ALA 52  52  52  ALA ALA B . n 
B 2 53  ILE 53  53  53  ILE ILE B . n 
B 2 54  GLU 54  54  54  GLU GLU B . n 
B 2 55  SER 55  55  55  SER SER B . n 
B 2 56  HIS 56  56  56  HIS HIS B . n 
B 2 57  GLY 57  57  57  GLY GLY B . n 
B 2 58  GLN 58  58  58  GLN GLN B . n 
B 2 59  GLU 59  59  59  GLU GLU B . n 
B 2 60  THR 60  60  60  THR THR B . n 
B 2 61  TRP 61  61  61  TRP TRP B . n 
B 2 62  TYR 62  62  62  TYR TYR B . n 
B 2 63  ALA 63  63  63  ALA ALA B . n 
B 2 64  ASP 64  64  64  ASP ASP B . n 
B 2 65  SER 65  65  65  SER SER B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  LYS 67  67  67  LYS LYS B . n 
B 2 68  GLY 68  68  68  GLY GLY B . n 
B 2 69  ARG 69  69  69  ARG ARG B . n 
B 2 70  PHE 70  70  70  PHE PHE B . n 
B 2 71  THR 71  71  71  THR THR B . n 
B 2 72  ILE 72  72  72  ILE ILE B . n 
B 2 73  SER 73  73  73  SER SER B . n 
B 2 74  ARG 74  74  74  ARG ARG B . n 
B 2 75  ASP 75  75  75  ASP ASP B . n 
B 2 76  ASN 76  76  76  ASN ASN B . n 
B 2 77  ALA 77  77  77  ALA ALA B . n 
B 2 78  LYS 78  78  78  LYS LYS B . n 
B 2 79  ASN 79  79  79  ASN ASN B . n 
B 2 80  THR 80  80  80  THR THR B . n 
B 2 81  VAL 81  81  81  VAL VAL B . n 
B 2 82  TYR 82  82  82  TYR TYR B . n 
B 2 83  LEU 83  83  83  LEU LEU B . n 
B 2 84  GLN 84  84  84  GLN GLN B . n 
B 2 85  MET 85  85  85  MET MET B . n 
B 2 86  ASN 86  86  86  ASN ASN B . n 
B 2 87  SER 87  87  87  SER SER B . n 
B 2 88  LEU 88  88  88  LEU LEU B . n 
B 2 89  LYS 89  89  89  LYS LYS B . n 
B 2 90  PRO 90  90  90  PRO PRO B . n 
B 2 91  GLU 91  91  91  GLU GLU B . n 
B 2 92  ASP 92  92  92  ASP ASP B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  ALA 94  94  94  ALA ALA B . n 
B 2 95  VAL 95  95  95  VAL VAL B . n 
B 2 96  TYR 96  96  96  TYR TYR B . n 
B 2 97  TYR 97  97  97  TYR TYR B . n 
B 2 98  CYS 98  98  98  CYS CYS B . n 
B 2 99  VAL 99  99  99  VAL VAL B . n 
B 2 100 ARG 100 100 100 ARG ARG B . n 
B 2 101 VAL 101 101 101 VAL VAL B . n 
B 2 102 GLY 102 102 102 GLY GLY B . n 
B 2 103 ALA 103 103 103 ALA ALA B . n 
B 2 104 GLU 104 104 104 GLU GLU B . n 
B 2 105 TYR 105 105 105 TYR TYR B . n 
B 2 106 VAL 106 106 106 VAL VAL B . n 
B 2 107 GLY 107 107 107 GLY GLY B . n 
B 2 108 GLN 108 108 108 GLN GLN B . n 
B 2 109 GLY 109 109 109 GLY GLY B . n 
B 2 110 THR 110 110 110 THR THR B . n 
B 2 111 GLN 111 111 111 GLN GLN B . n 
B 2 112 VAL 112 112 112 VAL VAL B . n 
B 2 113 THR 113 113 113 THR THR B . n 
B 2 114 VAL 114 114 114 VAL VAL B . n 
B 2 115 SER 115 115 115 SER SER B . n 
B 2 116 ALA 116 116 116 ALA ALA B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 HOH 1  201 17  HOH HOH A . 
C 3 HOH 2  202 86  HOH HOH A . 
C 3 HOH 3  203 129 HOH HOH A . 
C 3 HOH 4  204 8   HOH HOH A . 
C 3 HOH 5  205 186 HOH HOH A . 
C 3 HOH 6  206 95  HOH HOH A . 
C 3 HOH 7  207 82  HOH HOH A . 
C 3 HOH 8  208 170 HOH HOH A . 
C 3 HOH 9  209 13  HOH HOH A . 
C 3 HOH 10 210 159 HOH HOH A . 
C 3 HOH 11 211 90  HOH HOH A . 
C 3 HOH 12 212 103 HOH HOH A . 
C 3 HOH 13 213 46  HOH HOH A . 
C 3 HOH 14 214 14  HOH HOH A . 
C 3 HOH 15 215 43  HOH HOH A . 
C 3 HOH 16 216 9   HOH HOH A . 
C 3 HOH 17 217 122 HOH HOH A . 
C 3 HOH 18 218 40  HOH HOH A . 
C 3 HOH 19 219 158 HOH HOH A . 
C 3 HOH 20 220 114 HOH HOH A . 
C 3 HOH 21 221 137 HOH HOH A . 
C 3 HOH 22 222 182 HOH HOH A . 
C 3 HOH 23 223 47  HOH HOH A . 
C 3 HOH 24 224 154 HOH HOH A . 
C 3 HOH 25 225 65  HOH HOH A . 
C 3 HOH 26 226 145 HOH HOH A . 
C 3 HOH 27 227 138 HOH HOH A . 
C 3 HOH 28 228 39  HOH HOH A . 
C 3 HOH 29 229 94  HOH HOH A . 
C 3 HOH 30 230 5   HOH HOH A . 
C 3 HOH 31 231 11  HOH HOH A . 
C 3 HOH 32 232 166 HOH HOH A . 
C 3 HOH 33 233 110 HOH HOH A . 
C 3 HOH 34 234 120 HOH HOH A . 
C 3 HOH 35 235 128 HOH HOH A . 
C 3 HOH 36 236 64  HOH HOH A . 
C 3 HOH 37 237 72  HOH HOH A . 
C 3 HOH 38 238 30  HOH HOH A . 
C 3 HOH 39 239 59  HOH HOH A . 
C 3 HOH 40 240 53  HOH HOH A . 
C 3 HOH 41 241 16  HOH HOH A . 
C 3 HOH 42 242 45  HOH HOH A . 
C 3 HOH 43 243 23  HOH HOH A . 
C 3 HOH 44 244 19  HOH HOH A . 
C 3 HOH 45 245 98  HOH HOH A . 
C 3 HOH 46 246 50  HOH HOH A . 
C 3 HOH 47 247 66  HOH HOH A . 
C 3 HOH 48 248 100 HOH HOH A . 
C 3 HOH 49 249 191 HOH HOH A . 
C 3 HOH 50 250 113 HOH HOH A . 
C 3 HOH 51 251 179 HOH HOH A . 
C 3 HOH 52 252 61  HOH HOH A . 
C 3 HOH 53 253 99  HOH HOH A . 
C 3 HOH 54 254 115 HOH HOH A . 
C 3 HOH 55 255 76  HOH HOH A . 
C 3 HOH 56 256 190 HOH HOH A . 
C 3 HOH 57 257 172 HOH HOH A . 
C 3 HOH 58 258 130 HOH HOH A . 
C 3 HOH 59 259 148 HOH HOH A . 
C 3 HOH 60 260 97  HOH HOH A . 
C 3 HOH 61 261 124 HOH HOH A . 
C 3 HOH 62 262 168 HOH HOH A . 
C 3 HOH 63 263 176 HOH HOH A . 
C 3 HOH 64 264 140 HOH HOH A . 
C 3 HOH 65 265 175 HOH HOH A . 
C 3 HOH 66 266 83  HOH HOH A . 
C 3 HOH 67 267 150 HOH HOH A . 
C 3 HOH 68 268 87  HOH HOH A . 
C 3 HOH 69 269 119 HOH HOH A . 
C 3 HOH 70 270 152 HOH HOH A . 
C 3 HOH 71 271 156 HOH HOH A . 
C 3 HOH 72 272 162 HOH HOH A . 
C 3 HOH 73 273 169 HOH HOH A . 
C 3 HOH 74 274 161 HOH HOH A . 
C 3 HOH 75 275 106 HOH HOH A . 
C 3 HOH 76 276 69  HOH HOH A . 
C 3 HOH 77 277 184 HOH HOH A . 
C 3 HOH 78 278 178 HOH HOH A . 
C 3 HOH 79 279 109 HOH HOH A . 
C 3 HOH 80 280 123 HOH HOH A . 
C 3 HOH 81 281 181 HOH HOH A . 
C 3 HOH 82 282 153 HOH HOH A . 
C 3 HOH 83 283 85  HOH HOH A . 
C 3 HOH 84 284 116 HOH HOH A . 
C 3 HOH 85 285 155 HOH HOH A . 
C 3 HOH 86 286 118 HOH HOH A . 
C 3 HOH 87 287 108 HOH HOH A . 
C 3 HOH 88 288 89  HOH HOH A . 
D 3 HOH 1  201 164 HOH HOH B . 
D 3 HOH 2  202 55  HOH HOH B . 
D 3 HOH 3  203 71  HOH HOH B . 
D 3 HOH 4  204 7   HOH HOH B . 
D 3 HOH 5  205 84  HOH HOH B . 
D 3 HOH 6  206 131 HOH HOH B . 
D 3 HOH 7  207 75  HOH HOH B . 
D 3 HOH 8  208 1   HOH HOH B . 
D 3 HOH 9  209 52  HOH HOH B . 
D 3 HOH 10 210 104 HOH HOH B . 
D 3 HOH 11 211 3   HOH HOH B . 
D 3 HOH 12 212 4   HOH HOH B . 
D 3 HOH 13 213 125 HOH HOH B . 
D 3 HOH 14 214 48  HOH HOH B . 
D 3 HOH 15 215 18  HOH HOH B . 
D 3 HOH 16 216 44  HOH HOH B . 
D 3 HOH 17 217 10  HOH HOH B . 
D 3 HOH 18 218 41  HOH HOH B . 
D 3 HOH 19 219 68  HOH HOH B . 
D 3 HOH 20 220 51  HOH HOH B . 
D 3 HOH 21 221 54  HOH HOH B . 
D 3 HOH 22 222 31  HOH HOH B . 
D 3 HOH 23 223 22  HOH HOH B . 
D 3 HOH 24 224 73  HOH HOH B . 
D 3 HOH 25 225 12  HOH HOH B . 
D 3 HOH 26 226 21  HOH HOH B . 
D 3 HOH 27 227 135 HOH HOH B . 
D 3 HOH 28 228 107 HOH HOH B . 
D 3 HOH 29 229 36  HOH HOH B . 
D 3 HOH 30 230 2   HOH HOH B . 
D 3 HOH 31 231 139 HOH HOH B . 
D 3 HOH 32 232 35  HOH HOH B . 
D 3 HOH 33 233 81  HOH HOH B . 
D 3 HOH 34 234 177 HOH HOH B . 
D 3 HOH 35 235 57  HOH HOH B . 
D 3 HOH 36 236 34  HOH HOH B . 
D 3 HOH 37 237 25  HOH HOH B . 
D 3 HOH 38 238 194 HOH HOH B . 
D 3 HOH 39 239 26  HOH HOH B . 
D 3 HOH 40 240 56  HOH HOH B . 
D 3 HOH 41 241 165 HOH HOH B . 
D 3 HOH 42 242 187 HOH HOH B . 
D 3 HOH 43 243 15  HOH HOH B . 
D 3 HOH 44 244 33  HOH HOH B . 
D 3 HOH 45 245 74  HOH HOH B . 
D 3 HOH 46 246 127 HOH HOH B . 
D 3 HOH 47 247 37  HOH HOH B . 
D 3 HOH 48 248 58  HOH HOH B . 
D 3 HOH 49 249 77  HOH HOH B . 
D 3 HOH 50 250 20  HOH HOH B . 
D 3 HOH 51 251 192 HOH HOH B . 
D 3 HOH 52 252 157 HOH HOH B . 
D 3 HOH 53 253 133 HOH HOH B . 
D 3 HOH 54 254 27  HOH HOH B . 
D 3 HOH 55 255 149 HOH HOH B . 
D 3 HOH 56 256 29  HOH HOH B . 
D 3 HOH 57 257 111 HOH HOH B . 
D 3 HOH 58 258 63  HOH HOH B . 
D 3 HOH 59 259 42  HOH HOH B . 
D 3 HOH 60 260 105 HOH HOH B . 
D 3 HOH 61 261 96  HOH HOH B . 
D 3 HOH 62 262 62  HOH HOH B . 
D 3 HOH 63 263 92  HOH HOH B . 
D 3 HOH 64 264 79  HOH HOH B . 
D 3 HOH 65 265 6   HOH HOH B . 
D 3 HOH 66 266 49  HOH HOH B . 
D 3 HOH 67 267 24  HOH HOH B . 
D 3 HOH 68 268 88  HOH HOH B . 
D 3 HOH 69 269 93  HOH HOH B . 
D 3 HOH 70 270 32  HOH HOH B . 
D 3 HOH 71 271 167 HOH HOH B . 
D 3 HOH 72 272 28  HOH HOH B . 
D 3 HOH 73 273 70  HOH HOH B . 
D 3 HOH 74 274 38  HOH HOH B . 
D 3 HOH 75 275 143 HOH HOH B . 
D 3 HOH 76 276 67  HOH HOH B . 
D 3 HOH 77 277 180 HOH HOH B . 
D 3 HOH 78 278 121 HOH HOH B . 
D 3 HOH 79 279 142 HOH HOH B . 
D 3 HOH 80 280 134 HOH HOH B . 
D 3 HOH 81 281 60  HOH HOH B . 
D 3 HOH 82 282 171 HOH HOH B . 
D 3 HOH 83 283 132 HOH HOH B . 
D 3 HOH 84 284 80  HOH HOH B . 
D 3 HOH 85 285 101 HOH HOH B . 
D 3 HOH 86 286 91  HOH HOH B . 
D 3 HOH 87 287 126 HOH HOH B . 
D 3 HOH 88 288 78  HOH HOH B . 
D 3 HOH 89 289 151 HOH HOH B . 
D 3 HOH 90 290 173 HOH HOH B . 
D 3 HOH 91 291 141 HOH HOH B . 
D 3 HOH 92 292 193 HOH HOH B . 
D 3 HOH 93 293 112 HOH HOH B . 
D 3 HOH 94 294 117 HOH HOH B . 
D 3 HOH 95 295 146 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 26  ? CD  ? A LYS 26  CD  
2  1 Y 1 A LYS 26  ? CE  ? A LYS 26  CE  
3  1 Y 1 A LYS 26  ? NZ  ? A LYS 26  NZ  
4  1 Y 1 A GLU 49  ? CG  ? A GLU 49  CG  
5  1 Y 1 A GLU 49  ? CD  ? A GLU 49  CD  
6  1 Y 1 A GLU 49  ? OE1 ? A GLU 49  OE1 
7  1 Y 1 A GLU 49  ? OE2 ? A GLU 49  OE2 
8  1 Y 1 A LYS 99  ? CG  ? A LYS 99  CG  
9  1 Y 1 A LYS 99  ? CD  ? A LYS 99  CD  
10 1 Y 1 A LYS 99  ? CE  ? A LYS 99  CE  
11 1 Y 1 A LYS 99  ? NZ  ? A LYS 99  NZ  
12 1 Y 1 A GLU 100 ? CG  ? A GLU 100 CG  
13 1 Y 1 A GLU 100 ? CD  ? A GLU 100 CD  
14 1 Y 1 A GLU 100 ? OE1 ? A GLU 100 OE1 
15 1 Y 1 A GLU 100 ? OE2 ? A GLU 100 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487            1 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? MxCuBE   ? ? ? .                      2 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? '1.1.7 (20210504)'     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? 'VERSION Jun 30, 2023' 4 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? 0.7.15                 5 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? 2.8.3                  6 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? 0.9                    7 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H1F 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     121.575 
_cell.length_a_esd                 ? 
_cell.length_b                     121.575 
_cell.length_b_esd                 ? 
_cell.length_c                     52.346 
_cell.length_c_esd                 ? 
_cell.volume                       773699.039 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9H1F 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                90 
_symmetry.space_group_name_Hall            'P 4ab 2ab' 
_symmetry.space_group_name_H-M             'P 4 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H1F 
_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             3.04 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.57 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Citric acid pH 4.0 and 2.4 M Ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97623 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97623 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          38.24 
_reflns.entry_id                                       9H1F 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               29.49 
_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                                     36823 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                26.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.79 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.085 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.8 
_reflns_shell.d_res_low                                     1.864 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.36 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3644 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.69 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.897 
_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                               43.10 
_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                                 9H1F 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             29.49 
_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                     36817 
_refine.ls_number_reflns_R_free                  1789 
_refine.ls_number_reflns_R_work                  35028 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.67 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2037 
_refine.ls_R_factor_R_free                       0.2263 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2026 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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                 23.2035 
_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                            0.2837 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        29.49 
_refine_hist.number_atoms_solvent             183 
_refine_hist.number_atoms_total               2278 
_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        2095 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0103  ? 2138 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0101  ? 2887 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0654  ? 323  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0076  ? 369  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.6488 ? 796  ? 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' 1.80 1.85  . . 111 2679 99.89  . . . . 0.4739 . . . . . . . . . . . 0.6009 
'X-RAY DIFFRACTION' 1.85 1.90  . . 163 2617 100.00 . . . . 0.3362 . . . . . . . . . . . 0.4019 
'X-RAY DIFFRACTION' 1.90 1.96  . . 148 2650 99.96  . . . . 0.2579 . . . . . . . . . . . 0.2756 
'X-RAY DIFFRACTION' 1.96 2.03  . . 134 2672 99.96  . . . . 0.2201 . . . . . . . . . . . 0.2286 
'X-RAY DIFFRACTION' 2.03 2.12  . . 135 2666 100.00 . . . . 0.2233 . . . . . . . . . . . 0.2629 
'X-RAY DIFFRACTION' 2.12 2.21  . . 139 2663 100.00 . . . . 0.2237 . . . . . . . . . . . 0.2720 
'X-RAY DIFFRACTION' 2.21 2.33  . . 123 2697 100.00 . . . . 0.2288 . . . . . . . . . . . 0.2873 
'X-RAY DIFFRACTION' 2.33 2.47  . . 138 2678 100.00 . . . . 0.2140 . . . . . . . . . . . 0.2404 
'X-RAY DIFFRACTION' 2.48 2.67  . . 127 2691 100.00 . . . . 0.2131 . . . . . . . . . . . 0.2013 
'X-RAY DIFFRACTION' 2.67 2.93  . . 143 2718 100.00 . . . . 0.2048 . . . . . . . . . . . 0.2536 
'X-RAY DIFFRACTION' 2.93 3.36  . . 138 2724 100.00 . . . . 0.2021 . . . . . . . . . . . 0.2024 
'X-RAY DIFFRACTION' 3.36 4.23  . . 136 2659 96.05  . . . . 0.1639 . . . . . . . . . . . 0.1959 
'X-RAY DIFFRACTION' 4.23 29.49 . . 154 2914 99.90  . . . . 0.1943 . . . . . . . . . . . 0.2124 
# 
_struct.entry_id                     9H1F 
_struct.title                        'Cofilin-1 in complex with high-affinity Sybody B12' 
_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        9H1F 
_struct_keywords.text            
;Cofilin-1, CFL1, ADF/cofilin, G-Actin, F-Actin, Actin, Sybody, Nanobody, Synthetic Nanobody, Actin binding protein, ABP, PROTEIN BINDING
;
_struct_keywords.pdbx_keywords   'PROTEIN BINDING' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP COF1_HUMAN P23528 ? 1 
;MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVKMLPDKDC
RYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVIS
LEGKPL
;
1 
2 PDB 9H1F       9H1F   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9H1F A 8 ? 173 ? P23528 1 ? 166 ? 8 173 
2 2 9H1F B 1 ? 116 ? 9H1F   1 ? 116 ? 1 116 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9H1F SER A 1 ? UNP P23528 ? ? 'expression tag' 1 1 
1 9H1F ASN A 2 ? UNP P23528 ? ? 'expression tag' 2 2 
1 9H1F ILE A 3 ? UNP P23528 ? ? 'expression tag' 3 3 
1 9H1F GLY A 4 ? UNP P23528 ? ? 'expression tag' 4 4 
1 9H1F SER A 5 ? UNP P23528 ? ? 'expression tag' 5 5 
1 9H1F GLY A 6 ? UNP P23528 ? ? 'expression tag' 6 6 
1 9H1F SER A 7 ? UNP P23528 ? ? 'expression tag' 7 7 
# 
_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)' 1360  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  13200 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'isothermal titration calorimetry' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 15  ? LYS A 26  ? SER A 15  LYS A 26  1 ? 12 
HELX_P HELX_P2  AA2 PRO A 33  ? LYS A 38  ? PRO A 33  LYS A 38  1 ? 6  
HELX_P HELX_P3  AA3 GLY A 65  ? VAL A 67  ? GLY A 65  VAL A 67  5 ? 3  
HELX_P HELX_P4  AA4 ASP A 73  ? LEU A 82  ? ASP A 73  LEU A 82  1 ? 10 
HELX_P HELX_P5  AA5 PRO A 117 ? LEU A 135 ? PRO A 117 LEU A 135 1 ? 19 
HELX_P HELX_P6  AA6 CYS A 146 ? LYS A 151 ? CYS A 146 LYS A 151 1 ? 6  
HELX_P HELX_P7  AA7 ASP A 152 ? GLY A 162 ? ASP A 152 GLY A 162 1 ? 11 
HELX_P HELX_P8  AA8 SER A 163 ? VAL A 165 ? SER A 163 VAL A 165 5 ? 3  
HELX_P HELX_P9  AA9 PRO B 30  ? ARG B 34  ? PRO B 30  ARG B 34  5 ? 5  
HELX_P HELX_P10 AB1 LYS B 89  ? THR B 93  ? LYS B 89  THR B 93  5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 13  ? VAL A 14  ? ALA A 13  VAL A 14  
AA1 2 ASN A 53  ? LEU A 63  ? ASN A 53  LEU A 63  
AA1 3 LYS A 40  ? LEU A 47  ? LYS A 40  LEU A 47  
AA1 4 ARG A 88  ? GLU A 97  ? ARG A 88  GLU A 97  
AA1 5 LYS A 102 ? TRP A 111 ? LYS A 102 TRP A 111 
AA1 6 GLU A 141 ? ALA A 144 ? GLU A 141 ALA A 144 
AA2 1 ALA A 13  ? VAL A 14  ? ALA A 13  VAL A 14  
AA2 2 ASN A 53  ? LEU A 63  ? ASN A 53  LEU A 63  
AA2 3 LYS A 40  ? LEU A 47  ? LYS A 40  LEU A 47  
AA2 4 ARG A 88  ? GLU A 97  ? ARG A 88  GLU A 97  
AA2 5 SER A 167 ? LEU A 168 ? SER A 167 LEU A 168 
AA2 6 LYS A 171 ? PRO A 172 ? LYS A 171 PRO A 172 
AA3 1 GLN B 5   ? SER B 9   ? GLN B 5   SER B 9   
AA3 2 LEU B 20  ? SER B 27  ? LEU B 20  SER B 27  
AA3 3 THR B 80  ? MET B 85  ? THR B 80  MET B 85  
AA3 4 PHE B 70  ? ASP B 75  ? PHE B 70  ASP B 75  
AA4 1 GLY B 12  ? GLN B 15  ? GLY B 12  GLN B 15  
AA4 2 THR B 110 ? SER B 115 ? THR B 110 SER B 115 
AA4 3 ALA B 94  ? ARG B 100 ? ALA B 94  ARG B 100 
AA4 4 MET B 36  ? GLN B 41  ? MET B 36  GLN B 41  
AA4 5 GLU B 48  ? ILE B 53  ? GLU B 48  ILE B 53  
AA4 6 THR B 60  ? TYR B 62  ? THR B 60  TYR B 62  
# 
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 ALA A 13  ? N ALA A 13  O ILE A 54  ? O ILE A 54  
AA1 2 3 O ILE A 62  ? O ILE A 62  N LYS A 41  ? N LYS A 41  
AA1 3 4 N PHE A 45  ? N PHE A 45  O TYR A 89  ? O TYR A 89  
AA1 4 5 N TYR A 96  ? N TYR A 96  O LYS A 103 ? O LYS A 103 
AA1 5 6 N PHE A 108 ? N PHE A 108 O LEU A 142 ? O LEU A 142 
AA2 1 2 N ALA A 13  ? N ALA A 13  O ILE A 54  ? O ILE A 54  
AA2 2 3 O ILE A 62  ? O ILE A 62  N LYS A 41  ? N LYS A 41  
AA2 3 4 N PHE A 45  ? N PHE A 45  O TYR A 89  ? O TYR A 89  
AA2 4 5 N GLU A 97  ? N GLU A 97  O SER A 167 ? O SER A 167 
AA2 5 6 N LEU A 168 ? N LEU A 168 O LYS A 171 ? O LYS A 171 
AA3 1 2 N VAL B 7   ? N VAL B 7   O ALA B 25  ? O ALA B 25  
AA3 2 3 N LEU B 20  ? N LEU B 20  O MET B 85  ? O MET B 85  
AA3 3 4 O GLN B 84  ? O GLN B 84  N THR B 71  ? N THR B 71  
AA4 1 2 N VAL B 14  ? N VAL B 14  O THR B 113 ? O THR B 113 
AA4 2 3 O THR B 110 ? O THR B 110 N TYR B 96  ? N TYR B 96  
AA4 3 4 O TYR B 97  ? O TYR B 97  N TYR B 39  ? N TYR B 39  
AA4 4 5 N TRP B 38  ? N TRP B 38  O ALA B 51  ? O ALA B 51  
AA4 5 6 N ALA B 52  ? N ALA B 52  O TRP B 61  ? O TRP B 61  
# 
_pdbx_entry_details.entry_id                   9H1F 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    HIS 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     56 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             61.04 
_pdbx_validate_torsion.psi             -84.81 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -y+1/2,x+1/2,z  
3 y+1/2,-x+1/2,z  
4 x+1/2,-y+1/2,-z 
5 -x+1/2,y+1/2,-z 
6 -x,-y,z         
7 y,x,-z          
8 -y,-x,-z        
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 20.7861775752 14.8772695946  2.43661747815  0.25371236309  ? -0.00667104012543  ? 0.0110976507622 
? 0.190249961905 ? -0.0155862372165 ? 0.433328028594 ? 6.41241288553  ? -2.43940201379  ? -5.67266644278   ? 1.44949346867 ? 
2.08252506151   ? 7.93468128616 ? -0.113772935229 ? 0.184922376857  ? -0.106116542019  ? 0.00821037541764 ? -0.0392418510933 ? 
-0.0238472618565 ? 0.0802963086402  ? -0.203612254237 ? 0.105834660916   ? 
2  'X-RAY DIFFRACTION' ? refined 20.8675652092 14.2280596355  14.5368857104  0.253851795631 ? -0.0184958950122   ? 
-0.00504469867414 ? 0.222461851746 ? 0.007631423884   ? 0.318629311874 ? 0.378954597694 ? -0.493557695028 ? 0.618857261628   ? 
8.1530646905  ? 1.39225809286   ? 3.9082031861  ? -0.107069200428 ? -0.265431740733 ? -0.0953981202376 ? 0.578173962738   ? 
0.249365036482   ? -0.305083263948  ? 0.191444906696   ? -0.162054499339 ? -0.151821074433  ? 
3  'X-RAY DIFFRACTION' ? refined 32.1962375244 3.272883452    9.55510601823  0.358480532614 ? 0.0378844620955    ? -0.103450782146 
? 0.274126098269 ? -0.0346560697771 ? 0.67860248731  ? 1.61783329887  ? -0.467743780007 ? -0.199570114179  ? 5.22979987355 ? 
1.19032918626   ? 0.33615699895 ? 0.320849957149  ? -0.119560376289 ? -0.148960356588  ? 0.725561181564   ? 0.188598119217   ? 
-1.94864079122   ? 0.167082998332   ? 0.251218963481  ? -0.578665046274  ? 
4  'X-RAY DIFFRACTION' ? refined 22.6424075074 20.8536994933  19.2151299651  0.320248421456 ? -0.0107275356868   ? 
-0.00669151888798 ? 0.270501508063 ? -0.0383642069483 ? 0.401451947557 ? 7.28101411711  ? -2.42712740868  ? -3.96297873184   ? 
9.5202818821  ? 3.31782974357   ? 9.35309119956 ? 0.0711196860563 ? -0.226915618322 ? 0.286428129515   ? 0.742410497255   ? 
0.00503983336637 ? 0.279767772934   ? -0.423423790257  ? -0.249351226507 ? -0.178516334041  ? 
5  'X-RAY DIFFRACTION' ? refined 20.1044519855 -17.4656790261 20.9754590736  0.446841727483 ? 0.0857378060131    ? 0.0799394170008 
? 0.520067944587 ? 0.0444765011477  ? 0.543043158387 ? 4.57146258065  ? -4.42285893779  ? 1.86375027463    ? 4.31520898511 ? 
-1.4660873517   ? 8.94400385532 ? -0.88047096508  ? -1.32900707984  ? -0.188217994855  ? 1.0834075321     ? 0.6709882497     ? 
-0.333421683471  ? 0.610965186221   ? -0.572556774495 ? 0.00933334190211 ? 
6  'X-RAY DIFFRACTION' ? refined 27.6343414393 -33.4595424156 19.1356344452  0.371187437774 ? 0.0475489383237    ? 0.065696828466 
? 0.451852108199 ? 0.0927275497941  ? 0.505072135904 ? 7.17915686109  ? -5.74632782077  ? 0.341282570882   ? 4.67249046187 ? 
-0.749465272919 ? 2.42640960602 ? -0.231690548449 ? -0.284487772259 ? -0.897260583049  ? 0.612535365559   ? 0.636217082188   ? 
1.3065848369     ? 0.997316525253   ? -0.300066459884 ? -0.383983343333  ? 
7  'X-RAY DIFFRACTION' ? refined 16.2343570928 -16.2528558559 11.6732783066  0.283690266553 ? 0.0118463098339    ? 0.044280225943 
? 0.273855097377 ? 0.0454865556407  ? 0.587680371093 ? 2.65665957052  ? -1.85859784662  ? -2.01552283106   ? 5.04035328379 ? 
2.4238716212    ? 8.29267456074 ? 0.0476288733266 ? 0.189536356507  ? -0.492668776779  ? 0.237155869882   ? -0.11630895772   ? 
0.977783006407   ? 0.177657706056   ? -0.903701475884 ? 0.0102009470315  ? 
8  'X-RAY DIFFRACTION' ? refined 26.501498281  -23.0053569772 3.94084722843  0.263705835249 ? -0.0116509094603   ? 
-0.00156118355941 ? 0.209108909839 ? -0.0321562425182 ? 0.428372802053 ? 5.36507584224  ? -1.44627187323  ? 1.44585003638    ? 
3.39587945665 ? -2.04412130581  ? 5.7070807477  ? 0.0537444115218 ? 0.0592245492594 ? -0.470338734193  ? -0.575601430897  ? 
-0.0436898348992 ? -0.0756761369263 ? 0.653902770821   ? 0.283731450099  ? -0.0203791588106 ? 
9  'X-RAY DIFFRACTION' ? refined 31.8177561746 -17.573529546  11.5214004273  0.218625602884 ? 0.00903038619665   ? 0.0167757139649 
? 0.188237544107 ? -0.027941397291  ? 0.338592548847 ? 6.9264616612   ? -4.26722857125  ? 1.43556787192    ? 7.00229879822 ? 
-0.795128995845 ? 4.13924956026 ? -0.181948360404 ? -0.610003803665 ? -0.325910394517  ? 0.203612006065   ? 0.306197304033   ? 
-0.30397427597   ? 0.0866680037122  ? 0.348607270548  ? -0.120304496944  ? 
10 'X-RAY DIFFRACTION' ? refined 32.1815069039 -13.151851692  9.60629187371  0.207895417914 ? -0.0222590322899   ? 
-0.0339223531072  ? 0.17275394855  ? -0.0178257587405 ? 0.442993259496 ? 4.26579045155  ? -2.94240591493  ? 0.53365849344    ? 
4.01234881691 ? -0.29995235915  ? 2.81014865862 ? -0.276693702082 ? -0.250854248358 ? -0.0126275649244 ? 0.256358975497   ? 
0.229002885591   ? -0.269741468229  ? -0.0830159536217 ? 0.292697043458  ? -0.0109995493617 ? 
11 'X-RAY DIFFRACTION' ? refined 19.4296910539 -4.28468780997 12.9356070065  0.411158762677 ? 0.00410430398071   ? 0.105162954622 
? 0.169139478344 ? -0.0329575444488 ? 0.488473866837 ? 3.80692134378  ? -1.16117403517  ? 2.18448095936    ? 8.45690153416 ? 
-6.60590057661  ? 8.77657762719 ? -0.135310672189 ? -0.315488762565 ? 0.206581382495   ? 0.94145103855    ? -0.024820559435  ? 
0.356518463591   ? -0.366061168096  ? -0.199504850758 ? 0.172309373885   ? 
12 'X-RAY DIFFRACTION' ? refined 35.0039869852 -10.8302912792 7.92421362058  0.325889861803 ? -0.00371344896792  ? 0.0451115500426 
? 0.244464359575 ? -0.0383331598688 ? 0.666739292531 ? 8.06338603454  ? -2.55249733446  ? 2.84350435018    ? 4.56084178858 ? 
-1.39939618496  ? 5.11420697878 ? -0.116770193389 ? 0.148086086461  ? 0.547276444888   ? 0.131230101755   ? 0.0940455803529  ? 
-1.03866748712   ? -0.024078515351  ? 0.125908418916  ? 0.0146493369515  ? 
13 'X-RAY DIFFRACTION' ? refined 43.6101591747 -20.3962124687 5.73877143619  0.307762170491 ? 0.0134248778643    ? 0.0713490714693 
? 0.27373935634  ? 0.00990102271891 ? 0.730300899002 ? 6.30293528264  ? 4.21246026553   ? -1.78735146776   ? 8.3624235508  ? 
4.1758348896    ? 8.2831120887  ? 0.119302930848  ? 0.211928680324  ? 1.25109428456    ? -1.00237328078   ? 0.0142143599898  ? 
-0.37379639757   ? -0.61126143245   ? -0.346871584812 ? -0.0782052323934 ? 
14 'X-RAY DIFFRACTION' ? refined 35.0655898466 10.5951181938  5.35056529539  0.316572033338 ? 0.0344167954257    ? 0.0491946089197 
? 0.296408627079 ? -0.0176232910963 ? 0.702813853438 ? 3.10347284015  ? -2.90786288935  ? -0.0239600762434 ? 3.18091997869 ? 
1.34661616246   ? 3.29594444159 ? 0.124289913725  ? 0.0534803958134 ? 0.395482296279   ? 0.106807669469   ? 0.07081746796    ? 
-2.06184968379   ? 0.443654712754   ? 0.794419526078  ? -0.281299388142  ? 
15 'X-RAY DIFFRACTION' ? refined 19.8370939666 25.1753879486  15.8001771271  0.376307692631 ? 0.0172290655732    ? 0.0323273141952 
? 0.237771113928 ? -0.0938659819051 ? 0.449090929563 ? 5.65003308367  ? 2.70885622625   ? 0.89522620333    ? 3.06067761048 ? 
-2.38760554957  ? 4.65113908942 ? 0.0724612781027 ? -0.341286808168 ? 0.0184198434421  ? 0.362630168798   ? -0.161705147792  ? 
0.353284914367   ? -0.770283212056  ? -0.60884592501  ? 0.0466127368952  ? 
16 'X-RAY DIFFRACTION' ? refined 28.1630445066 10.1775911487  0.699995460269 0.282617975531 ? 0.025340106313     ? 
2.47093339213e-05 ? 0.180082238124 ? 0.00338608388749 ? 0.47399890147  ? 6.62395031955  ? -1.57009377599  ? -4.33806606756   ? 
1.10428795249 ? 2.21543309027   ? 7.82261052833 ? 0.0983286832965 ? 0.0590100577613 ? 0.136486656111   ? -0.382207922662  ? 
0.105044403763   ? -0.915194103124  ? 0.16205090793    ? 0.321986752882  ? -0.212547726616  ? 
17 'X-RAY DIFFRACTION' ? refined 23.3843760638 7.52267400594  16.3530544191  0.419671033013 ? -0.000873797504484 ? 
-0.0251037846039  ? 0.293389749867 ? 0.0413565408289  ? 0.43713573125  ? 7.79053380812  ? 0.465327421062  ? 0.534981677486   ? 
8.88175697737 ? 4.83737369421   ? 2.7499036252  ? 0.013453123528  ? -1.18101320322  ? -0.25445225324   ? 1.27013104471    ? 
-0.252376602533  ? -0.135892063184  ? 1.07444383089    ? 0.0602291707398 ? 0.269633423652   ? 
18 'X-RAY DIFFRACTION' ? refined 16.4183051682 6.42479085866  5.00307133542  0.257861073531 ? -0.0153945140425   ? 0.0177509559525 
? 0.179423134937 ? 0.00265150645611 ? 0.462203618161 ? 3.52553053646  ? 0.337425667991  ? 1.46017753187    ? 4.15952429902 ? 
-0.351898355105 ? 9.7923359643  ? 0.117554205309  ? 0.161592516777  ? -0.20347072793   ? -0.126413812741  ? -0.0518117487268 ? 
0.335000352383   ? 0.529244113061   ? -0.224393564402 ? -0.0222323850191 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  B 65  B 67  ? B 83  B 85  ? ? 
;chain 'B' and (resid 67 through 85 )
;
2  'X-RAY DIFFRACTION' 2  B 84  B 86  ? B 98  B 100 ? ? 
;chain 'B' and (resid 86 through 100 )
;
3  'X-RAY DIFFRACTION' 3  B 99  B 101 ? B 107 B 109 ? ? 
;chain 'B' and (resid 101 through 109 )
;
4  'X-RAY DIFFRACTION' 4  B 108 B 110 ? B 114 B 116 ? ? 
;chain 'B' and (resid 110 through 116 )
;
5  'X-RAY DIFFRACTION' 5  A 1   A 12  ? A 14  A 25  ? ? 
;chain 'A' and (resid 12 through 25 )
;
6  'X-RAY DIFFRACTION' 6  A 15  A 26  ? A 23  A 39  ? ? 
;chain 'A' and (resid 26 through 39 )
;
7  'X-RAY DIFFRACTION' 7  A 24  A 40  ? A 44  A 60  ? ? 
;chain 'A' and (resid 40 through 60 )
;
8  'X-RAY DIFFRACTION' 8  A 45  A 61  ? A 71  A 87  ? ? 
;chain 'A' and (resid 61 through 87 )
;
9  'X-RAY DIFFRACTION' 9  A 72  A 88  ? A 81  A 97  ? ? 
;chain 'A' and (resid 88 through 97 )
;
10 'X-RAY DIFFRACTION' 10 A 82  A 98  ? A 101 A 117 ? ? 
;chain 'A' and (resid 98 through 117 )
;
11 'X-RAY DIFFRACTION' 11 A 102 A 118 ? A 118 A 134 ? ? 
;chain 'A' and (resid 118 through 134 )
;
12 'X-RAY DIFFRACTION' 12 A 119 A 135 ? A 148 A 164 ? ? 
;chain 'A' and (resid 135 through 164 )
;
13 'X-RAY DIFFRACTION' 13 A 149 A 165 ? A 157 A 173 ? ? 
;chain 'A' and (resid 165 through 173 )
;
14 'X-RAY DIFFRACTION' 14 B 1   B 3   ? B 7   B 9   ? ? 
;chain 'B' and (resid 3 through 9 )
;
15 'X-RAY DIFFRACTION' 15 B 8   B 10  ? B 17  B 19  ? ? 
;chain 'B' and (resid 10 through 19 )
;
16 'X-RAY DIFFRACTION' 16 B 18  B 20  ? B 33  B 35  ? ? 
;chain 'B' and (resid 20 through 35 )
;
17 'X-RAY DIFFRACTION' 17 B 34  B 36  ? B 45  B 47  ? ? 
;chain 'B' and (resid 36 through 47 )
;
18 'X-RAY DIFFRACTION' 18 B 46  B 48  ? B 64  B 66  ? ? 
;chain 'B' and (resid 48 through 66 )
;
# 
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 SER 1  ? A SER 1  
2  1 Y 1 A ASN 2  ? A ASN 2  
3  1 Y 1 A ILE 3  ? A ILE 3  
4  1 Y 1 A GLY 4  ? A GLY 4  
5  1 Y 1 A SER 5  ? A SER 5  
6  1 Y 1 A GLY 6  ? A GLY 6  
7  1 Y 1 A SER 7  ? A SER 7  
8  1 Y 1 A MET 8  ? A MET 8  
9  1 Y 1 A ALA 9  ? A ALA 9  
10 1 Y 1 A SER 10 ? A SER 10 
11 1 Y 1 A GLY 11 ? A GLY 11 
12 1 Y 1 A VAL 27 ? A VAL 27 
13 1 Y 1 A ARG 28 ? A ARG 28 
14 1 Y 1 A LYS 29 ? A LYS 29 
15 1 Y 1 A SER 30 ? A SER 30 
16 1 Y 1 A SER 31 ? A SER 31 
17 1 Y 1 B GLY 1  ? B GLY 1  
18 1 Y 1 B HIS 2  ? B HIS 2  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other government' Germany 'HAMBURG INNOVATION C4T963'             1 
'Other private'    Germany 'Erich und Gertrud Roggenbuck-Stiftung' 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 4 21 2' 
_space_group.name_Hall        'P 4ab 2ab' 
_space_group.IT_number        90 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9H1F 
_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]   0.008225 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008225 
_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]   0.019104 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . VAL A 1 12  ? 12.69500 -4.34900  17.97700 1.000 64.85751 ? 12  VAL A N   1 
ATOM   2    C CA  . VAL A 1 12  ? 12.79000 -5.72500  17.50600 1.000 54.82523 ? 12  VAL A CA  1 
ATOM   3    C C   . VAL A 1 12  ? 13.34100 -6.59000  18.63300 1.000 58.16832 ? 12  VAL A C   1 
ATOM   4    O O   . VAL A 1 12  ? 14.41200 -6.30300  19.17900 1.000 65.01524 ? 12  VAL A O   1 
ATOM   5    C CB  . VAL A 1 12  ? 13.67100 -5.80400  16.24800 1.000 55.50782 ? 12  VAL A CB  1 
ATOM   6    C CG1 . VAL A 1 12  ? 13.81300 -7.22700  15.78000 1.000 53.33365 ? 12  VAL A CG1 1 
ATOM   7    C CG2 . VAL A 1 12  ? 13.08400 -4.94600  15.13200 1.000 55.86653 ? 12  VAL A CG2 1 
ATOM   8    N N   . ALA A 1 13  ? 12.60600 -7.64000  18.99800 1.000 56.53817 ? 13  ALA A N   1 
ATOM   9    C CA  . ALA A 1 13  ? 13.04400 -8.59000  20.01600 1.000 53.55166 ? 13  ALA A CA  1 
ATOM   10   C C   . ALA A 1 13  ? 13.91600 -9.68400  19.41100 1.000 50.56892 ? 13  ALA A C   1 
ATOM   11   O O   . ALA A 1 13  ? 13.84700 -9.98100  18.21800 1.000 49.85814 ? 13  ALA A O   1 
ATOM   12   C CB  . ALA A 1 13  ? 11.84600 -9.23500  20.71200 1.000 57.35267 ? 13  ALA A CB  1 
ATOM   13   N N   . VAL A 1 14  ? 14.73600 -10.29200 20.26200 1.000 49.61583 ? 14  VAL A N   1 
ATOM   14   C CA  . VAL A 1 14  ? 15.56600 -11.43300 19.89000 1.000 50.81853 ? 14  VAL A CA  1 
ATOM   15   C C   . VAL A 1 14  ? 14.92700 -12.68600 20.46800 1.000 48.58150 ? 14  VAL A C   1 
ATOM   16   O O   . VAL A 1 14  ? 14.66100 -12.75000 21.67000 1.000 52.42827 ? 14  VAL A O   1 
ATOM   17   C CB  . VAL A 1 14  ? 17.00500 -11.26500 20.40300 1.000 54.51466 ? 14  VAL A CB  1 
ATOM   18   C CG1 . VAL A 1 14  ? 17.88500 -12.40400 19.89500 1.000 53.54451 ? 14  VAL A CG1 1 
ATOM   19   C CG2 . VAL A 1 14  ? 17.55700 -9.90600  19.99400 1.000 54.99152 ? 14  VAL A CG2 1 
ATOM   20   N N   . SER A 1 15  ? 14.67400 -13.67900 19.62300 1.000 48.20450 ? 15  SER A N   1 
ATOM   21   C CA  . SER A 1 15  ? 13.94900 -14.85100 20.09100 1.000 48.35349 ? 15  SER A CA  1 
ATOM   22   C C   . SER A 1 15  ? 14.80400 -15.70300 21.03100 1.000 55.55452 ? 15  SER A C   1 
ATOM   23   O O   . SER A 1 15  ? 16.04000 -15.64700 21.02400 1.000 55.53451 ? 15  SER A O   1 
ATOM   24   C CB  . SER A 1 15  ? 13.49800 -15.70700 18.91400 1.000 52.50049 ? 15  SER A CB  1 
ATOM   25   O OG  . SER A 1 15  ? 14.60300 -16.40200 18.36600 1.000 50.54285 ? 15  SER A OG  1 
ATOM   26   N N   . ASP A 1 16  ? 14.11100 -16.51700 21.83800 1.000 56.00088 ? 16  ASP A N   1 
ATOM   27   C CA  . ASP A 1 16  ? 14.77900 -17.49200 22.69500 1.000 57.98468 ? 16  ASP A CA  1 
ATOM   28   C C   . ASP A 1 16  ? 15.71900 -18.37600 21.89000 1.000 57.38479 ? 16  ASP A C   1 
ATOM   29   O O   . ASP A 1 16  ? 16.82800 -18.68600 22.34200 1.000 59.01133 ? 16  ASP A O   1 
ATOM   30   C CB  . ASP A 1 16  ? 13.75300 -18.37100 23.41100 1.000 63.48674 ? 16  ASP A CB  1 
ATOM   31   C CG  . ASP A 1 16  ? 12.96000 -17.62400 24.47600 1.000 67.19304 ? 16  ASP A CG  1 
ATOM   32   O OD1 . ASP A 1 16  ? 13.32700 -16.47800 24.81900 1.000 67.47261 ? 16  ASP A OD1 1 
ATOM   33   O OD2 . ASP A 1 16  ? 11.95900 -18.19000 24.96000 1.000 67.24856 ? 16  ASP A OD2 1 
ATOM   34   N N   . GLY A 1 17  ? 15.27800 -18.80800 20.70200 1.000 57.10543 ? 17  GLY A N   1 
ATOM   35   C CA  . GLY A 1 17  ? 16.08400 -19.71500 19.89800 1.000 54.74501 ? 17  GLY A CA  1 
ATOM   36   C C   . GLY A 1 17  ? 17.44200 -19.14100 19.55600 1.000 51.34990 ? 17  GLY A C   1 
ATOM   37   O O   . GLY A 1 17  ? 18.46400 -19.82800 19.66200 1.000 51.23255 ? 17  GLY A O   1 
ATOM   38   N N   . VAL A 1 18  ? 17.47300 -17.87300 19.14700 1.000 48.68187 ? 18  VAL A N   1 
ATOM   39   C CA  . VAL A 1 18  ? 18.74400 -17.20600 18.87800 1.000 51.30087 ? 18  VAL A CA  1 
ATOM   40   C C   . VAL A 1 18  ? 19.60500 -17.16600 20.13700 1.000 52.25529 ? 18  VAL A C   1 
ATOM   41   O O   . VAL A 1 18  ? 20.82200 -17.37700 20.07700 1.000 52.53332 ? 18  VAL A O   1 
ATOM   42   C CB  . VAL A 1 18  ? 18.48900 -15.79700 18.30400 1.000 50.02773 ? 18  VAL A CB  1 
ATOM   43   C CG1 . VAL A 1 18  ? 19.79200 -15.05400 18.08000 1.000 50.33179 ? 18  VAL A CG1 1 
ATOM   44   C CG2 . VAL A 1 18  ? 17.66700 -15.89900 17.01000 1.000 46.97036 ? 18  VAL A CG2 1 
ATOM   45   N N   . ILE A 1 19  ? 18.98800 -16.91900 21.29700 1.000 52.58829 ? 19  ILE A N   1 
ATOM   46   C CA  . ILE A 1 19  ? 19.74000 -16.89000 22.55400 1.000 52.51679 ? 19  ILE A CA  1 
ATOM   47   C C   . ILE A 1 19  ? 20.34000 -18.26600 22.84800 1.000 49.87538 ? 19  ILE A C   1 
ATOM   48   O O   . ILE A 1 19  ? 21.51100 -18.38600 23.23200 1.000 49.43420 ? 19  ILE A O   1 
ATOM   49   C CB  . ILE A 1 19  ? 18.84200 -16.42500 23.71800 1.000 52.63872 ? 19  ILE A CB  1 
ATOM   50   C CG1 . ILE A 1 19  ? 18.17300 -15.07300 23.41900 1.000 62.67991 ? 19  ILE A CG1 1 
ATOM   51   C CG2 . ILE A 1 19  ? 19.63900 -16.36800 25.01500 1.000 51.26577 ? 19  ILE A CG2 1 
ATOM   52   C CD1 . ILE A 1 19  ? 19.11800 -13.99200 22.96300 1.000 61.74412 ? 19  ILE A CD1 1 
ATOM   53   N N   . LYS A 1 20  ? 19.53500 -19.31900 22.69100 1.000 45.89615 ? 20  LYS A N   1 
ATOM   54   C CA  . LYS A 1 20  ? 20.01200 -20.68100 22.92800 1.000 48.67614 ? 20  LYS A CA  1 
ATOM   55   C C   . LYS A 1 20  ? 21.12700 -21.06900 21.95900 1.000 49.23120 ? 20  LYS A C   1 
ATOM   56   O O   . LYS A 1 20  ? 22.14700 -21.64400 22.36100 1.000 49.90110 ? 20  LYS A O   1 
ATOM   57   C CB  . LYS A 1 20  ? 18.84500 -21.65800 22.80800 1.000 53.90643 ? 20  LYS A CB  1 
ATOM   58   C CG  . LYS A 1 20  ? 19.22600 -23.11900 22.94700 1.000 60.03649 ? 20  LYS A CG  1 
ATOM   59   C CD  . LYS A 1 20  ? 18.00700 -24.03200 22.82900 1.000 62.04958 ? 20  LYS A CD  1 
ATOM   60   C CE  . LYS A 1 20  ? 18.33200 -25.45800 23.27900 1.000 67.15057 ? 20  LYS A CE  1 
ATOM   61   N NZ  . LYS A 1 20  ? 19.60400 -25.96800 22.68600 1.000 69.74159 ? 20  LYS A NZ  1 
ATOM   62   N N   . VAL A 1 21  ? 20.93600 -20.79800 20.66600 1.000 47.40603 ? 21  VAL A N   1 
ATOM   63   C CA  . VAL A 1 21  ? 21.92200 -21.23000 19.68200 1.000 48.77094 ? 21  VAL A CA  1 
ATOM   64   C C   . VAL A 1 21  ? 23.25900 -20.54200 19.92500 1.000 44.98265 ? 21  VAL A C   1 
ATOM   65   O O   . VAL A 1 21  ? 24.32000 -21.17500 19.85900 1.000 47.15055 ? 21  VAL A O   1 
ATOM   66   C CB  . VAL A 1 21  ? 21.39400 -20.99300 18.25400 1.000 46.27212 ? 21  VAL A CB  1 
ATOM   67   C CG1 . VAL A 1 21  ? 22.53400 -20.97900 17.25200 1.000 48.87225 ? 21  VAL A CG1 1 
ATOM   68   C CG2 . VAL A 1 21  ? 20.39900 -22.08600 17.88800 1.000 52.39958 ? 21  VAL A CG2 1 
ATOM   69   N N   . PHE A 1 22  ? 23.23800 -19.24400 20.22700 1.000 46.86451 ? 22  PHE A N   1 
ATOM   70   C CA  . PHE A 1 22  ? 24.49700 -18.56600 20.51000 1.000 50.90613 ? 22  PHE A CA  1 
ATOM   71   C C   . PHE A 1 22  ? 25.20100 -19.20800 21.69300 1.000 50.94005 ? 22  PHE A C   1 
ATOM   72   O O   . PHE A 1 22  ? 26.39700 -19.50900 21.63500 1.000 53.63601 ? 22  PHE A O   1 
ATOM   73   C CB  . PHE A 1 22  ? 24.27700 -17.08200 20.78600 1.000 49.79100 ? 22  PHE A CB  1 
ATOM   74   C CG  . PHE A 1 22  ? 25.49300 -16.40600 21.35700 1.000 54.92799 ? 22  PHE A CG  1 
ATOM   75   C CD1 . PHE A 1 22  ? 26.62500 -16.20900 20.57500 1.000 58.09754 ? 22  PHE A CD1 1 
ATOM   76   C CD2 . PHE A 1 22  ? 25.52100 -15.99200 22.68000 1.000 58.66918 ? 22  PHE A CD2 1 
ATOM   77   C CE1 . PHE A 1 22  ? 27.76500 -15.60100 21.10500 1.000 60.48468 ? 22  PHE A CE1 1 
ATOM   78   C CE2 . PHE A 1 22  ? 26.65000 -15.38800 23.21500 1.000 61.22360 ? 22  PHE A CE2 1 
ATOM   79   C CZ  . PHE A 1 22  ? 27.77100 -15.18600 22.42700 1.000 64.56459 ? 22  PHE A CZ  1 
ATOM   80   N N   . ASN A 1 23  ? 24.47200 -19.41800 22.78400 1.000 48.98524 ? 23  ASN A N   1 
ATOM   81   C CA  . ASN A 1 23  ? 25.09800 -19.98900 23.96300 1.000 51.81129 ? 23  ASN A CA  1 
ATOM   82   C C   . ASN A 1 23  ? 25.61400 -21.39400 23.69900 1.000 50.64300 ? 23  ASN A C   1 
ATOM   83   O O   . ASN A 1 23  ? 26.63500 -21.79400 24.26800 1.000 55.21833 ? 23  ASN A O   1 
ATOM   84   C CB  . ASN A 1 23  ? 24.10800 -19.95400 25.11700 1.000 55.86588 ? 23  ASN A CB  1 
ATOM   85   C CG  . ASN A 1 23  ? 23.93000 -18.55300 25.66500 1.000 62.23397 ? 23  ASN A CG  1 
ATOM   86   O OD1 . ASN A 1 23  ? 24.91100 -17.88500 26.00900 1.000 67.73188 ? 23  ASN A OD1 1 
ATOM   87   N ND2 . ASN A 1 23  ? 22.68300 -18.09300 25.74000 1.000 63.77934 ? 23  ASN A ND2 1 
ATOM   88   N N   . ASP A 1 24  ? 24.95100 -22.14900 22.82100 1.000 49.24056 ? 24  ASP A N   1 
ATOM   89   C CA  . ASP A 1 24  ? 25.48800 -23.45800 22.45800 1.000 53.56883 ? 24  ASP A CA  1 
ATOM   90   C C   . ASP A 1 24  ? 26.77200 -23.33500 21.64900 1.000 50.77711 ? 24  ASP A C   1 
ATOM   91   O O   . ASP A 1 24  ? 27.65400 -24.19300 21.76100 1.000 51.86545 ? 24  ASP A O   1 
ATOM   92   C CB  . ASP A 1 24  ? 24.46400 -24.27200 21.67000 1.000 53.84057 ? 24  ASP A CB  1 
ATOM   93   C CG  . ASP A 1 24  ? 23.30100 -24.73900 22.52500 1.000 59.78069 ? 24  ASP A CG  1 
ATOM   94   O OD1 . ASP A 1 24  ? 23.45500 -24.85500 23.76200 1.000 63.13475 ? 24  ASP A OD1 1 
ATOM   95   O OD2 . ASP A 1 24  ? 22.22200 -24.99500 21.94900 1.000 65.33519 ? 24  ASP A OD2 1 
ATOM   96   N N   . MET A 1 25  ? 26.89200 -22.28900 20.83100 1.000 51.66317 ? 25  MET A N   1 
ATOM   97   C CA  . MET A 1 25  ? 28.07700 -22.12600 19.99600 1.000 52.12498 ? 25  MET A CA  1 
ATOM   98   C C   . MET A 1 25  ? 29.25800 -21.51700 20.75500 1.000 53.52288 ? 25  MET A C   1 
ATOM   99   O O   . MET A 1 25  ? 30.40000 -21.69000 20.32000 1.000 57.00946 ? 25  MET A O   1 
ATOM   100  C CB  . MET A 1 25  ? 27.73900 -21.27600 18.76500 1.000 48.53062 ? 25  MET A CB  1 
ATOM   101  C CG  . MET A 1 25  ? 26.74200 -21.94700 17.79400 1.000 43.47903 ? 25  MET A CG  1 
ATOM   102  S SD  . MET A 1 25  ? 26.33600 -20.96600 16.32200 1.000 39.52395 ? 25  MET A SD  1 
ATOM   103  C CE  . MET A 1 25  ? 27.78600 -21.26100 15.28000 1.000 38.35036 ? 25  MET A CE  1 
ATOM   104  N N   . LYS A 1 26  ? 29.01000 -20.82700 21.87300 1.000 57.84101 ? 26  LYS A N   1 
ATOM   105  C CA  . LYS A 1 26  ? 30.07400 -20.21500 22.67100 1.000 55.47258 ? 26  LYS A CA  1 
ATOM   106  C C   . LYS A 1 26  ? 31.11200 -21.23800 23.12500 1.000 54.75224 ? 26  LYS A C   1 
ATOM   107  O O   . LYS A 1 26  ? 32.18600 -21.33800 22.53200 1.000 62.51358 ? 26  LYS A O   1 
ATOM   108  C CB  . LYS A 1 26  ? 29.49700 -19.51100 23.89900 1.000 56.73274 ? 26  LYS A CB  1 
ATOM   109  C CG  . LYS A 1 26  ? 28.94700 -18.12200 23.64500 1.000 60.94285 ? 26  LYS A CG  1 
ATOM   110  N N   . THR A 1 32  ? 30.08500 -36.28000 23.91000 1.000 57.35351 ? 32  THR A N   1 
ATOM   111  C CA  . THR A 1 32  ? 29.76400 -37.49900 23.17100 1.000 53.42167 ? 32  THR A CA  1 
ATOM   112  C C   . THR A 1 32  ? 29.84000 -37.23000 21.67300 1.000 46.06691 ? 32  THR A C   1 
ATOM   113  O O   . THR A 1 32  ? 29.48800 -36.14100 21.19900 1.000 46.25101 ? 32  THR A O   1 
ATOM   114  C CB  . THR A 1 32  ? 28.36900 -38.06700 23.57000 1.000 55.39982 ? 32  THR A CB  1 
ATOM   115  O OG1 . THR A 1 32  ? 27.39400 -37.83700 22.53800 1.000 56.43808 ? 32  THR A OG1 1 
ATOM   116  C CG2 . THR A 1 32  ? 27.88800 -37.41400 24.86900 1.000 70.17685 ? 32  THR A CG2 1 
ATOM   117  N N   . PRO A 1 33  ? 30.35400 -38.20400 20.91800 1.000 43.95927 ? 33  PRO A N   1 
ATOM   118  C CA  . PRO A 1 33  ? 30.48200 -37.98600 19.46800 1.000 43.54609 ? 33  PRO A CA  1 
ATOM   119  C C   . PRO A 1 33  ? 29.17000 -37.61500 18.79400 1.000 42.43439 ? 33  PRO A C   1 
ATOM   120  O O   . PRO A 1 33  ? 29.16300 -36.74700 17.91600 1.000 42.00218 ? 33  PRO A O   1 
ATOM   121  C CB  . PRO A 1 33  ? 31.02900 -39.33100 18.96300 1.000 44.84144 ? 33  PRO A CB  1 
ATOM   122  C CG  . PRO A 1 33  ? 31.79900 -39.86900 20.13800 1.000 43.85771 ? 33  PRO A CG  1 
ATOM   123  C CD  . PRO A 1 33  ? 30.96100 -39.48000 21.34600 1.000 44.18465 ? 33  PRO A CD  1 
ATOM   124  N N   . GLU A 1 34  ? 28.05900 -38.25300 19.17300 1.000 44.93989 ? 34  GLU A N   1 
ATOM   125  C CA  . GLU A 1 34  ? 26.77900 -37.92200 18.55100 1.000 46.44562 ? 34  GLU A CA  1 
ATOM   126  C C   . GLU A 1 34  ? 26.33700 -36.51200 18.90900 1.000 46.91284 ? 34  GLU A C   1 
ATOM   127  O O   . GLU A 1 34  ? 25.78900 -35.79400 18.06600 1.000 50.17140 ? 34  GLU A O   1 
ATOM   128  C CB  . GLU A 1 34  ? 25.71700 -38.94500 18.96000 1.000 53.07057 ? 34  GLU A CB  1 
ATOM   129  C CG  . GLU A 1 34  ? 25.89800 -40.27900 18.25600 1.000 59.17056 ? 34  GLU A CG  1 
ATOM   130  C CD  . GLU A 1 34  ? 25.96600 -40.11600 16.74500 1.000 64.46266 ? 34  GLU A CD  1 
ATOM   131  O OE1 . GLU A 1 34  ? 25.01700 -39.53300 16.17900 1.000 73.20645 ? 34  GLU A OE1 1 
ATOM   132  O OE2 . GLU A 1 34  ? 26.96800 -40.55300 16.12800 1.000 62.33301 ? 34  GLU A OE2 1 
ATOM   133  N N   . GLU A 1 35  ? 26.56000 -36.09200 20.15100 1.000 47.37517 ? 35  GLU A N   1 
ATOM   134  C CA  . GLU A 1 35  ? 26.17300 -34.73600 20.52100 1.000 49.14194 ? 35  GLU A CA  1 
ATOM   135  C C   . GLU A 1 35  ? 27.03700 -33.69900 19.81800 1.000 49.51834 ? 35  GLU A C   1 
ATOM   136  O O   . GLU A 1 35  ? 26.54300 -32.62600 19.45500 1.000 45.99790 ? 35  GLU A O   1 
ATOM   137  C CB  . GLU A 1 35  ? 26.23700 -34.56200 22.04000 1.000 53.53741 ? 35  GLU A CB  1 
ATOM   138  C CG  . GLU A 1 35  ? 25.09500 -35.26300 22.76600 1.000 63.31778 ? 35  GLU A CG  1 
ATOM   139  C CD  . GLU A 1 35  ? 23.72600 -34.70900 22.37300 1.000 71.51020 ? 35  GLU A CD  1 
ATOM   140  O OE1 . GLU A 1 35  ? 23.53600 -33.47300 22.43900 1.000 75.87589 ? 35  GLU A OE1 1 
ATOM   141  O OE2 . GLU A 1 35  ? 22.84000 -35.51100 21.99400 1.000 81.84874 ? 35  GLU A OE2 1 
ATOM   142  N N   . VAL A 1 36  ? 28.31500 -34.00100 19.59300 1.000 41.17930 ? 36  VAL A N   1 
ATOM   143  C CA  . VAL A 1 36  ? 29.18900 -33.02600 18.95200 1.000 45.67796 ? 36  VAL A CA  1 
ATOM   144  C C   . VAL A 1 36  ? 28.77200 -32.81300 17.50300 1.000 43.45271 ? 36  VAL A C   1 
ATOM   145  O O   . VAL A 1 36  ? 28.83900 -31.69100 16.98600 1.000 42.13866 ? 36  VAL A O   1 
ATOM   146  C CB  . VAL A 1 36  ? 30.66400 -33.46600 19.07600 1.000 46.82825 ? 36  VAL A CB  1 
ATOM   147  C CG1 . VAL A 1 36  ? 31.54500 -32.69500 18.10400 1.000 50.75138 ? 36  VAL A CG1 1 
ATOM   148  C CG2 . VAL A 1 36  ? 31.14100 -33.27400 20.50600 1.000 51.74441 ? 36  VAL A CG2 1 
ATOM   149  N N   . LYS A 1 37  ? 28.30100 -33.87300 16.83400 1.000 39.39938 ? 37  LYS A N   1 
ATOM   150  C CA  . LYS A 1 37  ? 27.84200 -33.75400 15.45300 1.000 37.49303 ? 37  LYS A CA  1 
ATOM   151  C C   . LYS A 1 37  ? 26.64700 -32.81900 15.30500 1.000 43.21241 ? 37  LYS A C   1 
ATOM   152  O O   . LYS A 1 37  ? 26.39800 -32.34100 14.19300 1.000 38.60275 ? 37  LYS A O   1 
ATOM   153  C CB  . LYS A 1 37  ? 27.43500 -35.10900 14.88000 1.000 40.58090 ? 37  LYS A CB  1 
ATOM   154  C CG  . LYS A 1 37  ? 28.55500 -36.10900 14.72200 1.000 42.35320 ? 37  LYS A CG  1 
ATOM   155  C CD  . LYS A 1 37  ? 28.00900 -37.39100 14.09800 1.000 50.56239 ? 37  LYS A CD  1 
ATOM   156  C CE  . LYS A 1 37  ? 29.07600 -38.47800 14.02600 1.000 54.57518 ? 37  LYS A CE  1 
ATOM   157  N NZ  . LYS A 1 37  ? 28.54900 -39.74000 13.41100 1.000 63.27643 ? 37  LYS A NZ  1 
ATOM   158  N N   . LYS A 1 38  ? 25.88000 -32.58700 16.37800 1.000 38.41264 ? 38  LYS A N   1 
ATOM   159  C CA  . LYS A 1 38  ? 24.71500 -31.70600 16.30800 1.000 39.45560 ? 38  LYS A CA  1 
ATOM   160  C C   . LYS A 1 38  ? 25.04500 -30.24000 16.58700 1.000 41.15736 ? 38  LYS A C   1 
ATOM   161  O O   . LYS A 1 38  ? 24.16400 -29.38300 16.42100 1.000 44.08725 ? 38  LYS A O   1 
ATOM   162  C CB  . LYS A 1 38  ? 23.63400 -32.16500 17.29100 1.000 44.08980 ? 38  LYS A CB  1 
ATOM   163  C CG  . LYS A 1 38  ? 23.08200 -33.53000 16.98600 1.000 48.71946 ? 38  LYS A CG  1 
ATOM   164  C CD  . LYS A 1 38  ? 22.02600 -33.92400 18.00700 1.000 56.70203 ? 38  LYS A CD  1 
ATOM   165  C CE  . LYS A 1 38  ? 22.13600 -35.40300 18.33800 1.000 65.42568 ? 38  LYS A CE  1 
ATOM   166  N NZ  . LYS A 1 38  ? 21.39200 -35.74600 19.58300 1.000 75.67715 ? 38  LYS A NZ  1 
ATOM   167  N N   . ARG A 1 39  ? 26.26600 -29.93900 17.02400 1.000 43.48850 ? 39  ARG A N   1 
ATOM   168  C CA  . ARG A 1 39  ? 26.69100 -28.55300 17.20700 1.000 45.44366 ? 39  ARG A CA  1 
ATOM   169  C C   . ARG A 1 39  ? 26.63600 -27.79500 15.88400 1.000 40.57801 ? 39  ARG A C   1 
ATOM   170  O O   . ARG A 1 39  ? 26.88600 -28.35500 14.81500 1.000 38.14668 ? 39  ARG A O   1 
ATOM   171  C CB  . ARG A 1 39  ? 28.11200 -28.50800 17.77700 1.000 41.15146 ? 39  ARG A CB  1 
ATOM   172  C CG  . ARG A 1 39  ? 28.18700 -28.94800 19.25000 1.000 51.16777 ? 39  ARG A CG  1 
ATOM   173  C CD  . ARG A 1 39  ? 29.61200 -29.05500 19.76700 1.000 57.25035 ? 39  ARG A CD  1 
ATOM   174  N NE  . ARG A 1 39  ? 29.62400 -29.59700 21.12400 1.000 63.53963 ? 39  ARG A NE  1 
ATOM   175  C CZ  . ARG A 1 39  ? 30.71500 -29.90200 21.81600 1.000 66.20773 ? 39  ARG A CZ  1 
ATOM   176  N NH1 . ARG A 1 39  ? 31.92800 -29.72500 21.31400 1.000 65.99547 ? 39  ARG A NH1 1 
ATOM   177  N NH2 . ARG A 1 39  ? 30.58500 -30.40300 23.04400 1.000 71.73447 ? 39  ARG A NH2 1 
ATOM   178  N N   . LYS A 1 40  ? 26.33100 -26.50200 15.96300 1.000 43.18310 ? 40  LYS A N   1 
ATOM   179  C CA  . LYS A 1 40  ? 26.28000 -25.68700 14.76400 1.000 40.26272 ? 40  LYS A CA  1 
ATOM   180  C C   . LYS A 1 40  ? 27.68000 -25.28400 14.32400 1.000 41.86939 ? 40  LYS A C   1 
ATOM   181  O O   . LYS A 1 40  ? 28.52700 -24.93200 15.14700 1.000 44.27116 ? 40  LYS A O   1 
ATOM   182  C CB  . LYS A 1 40  ? 25.48500 -24.39700 14.97900 1.000 40.61610 ? 40  LYS A CB  1 
ATOM   183  C CG  . LYS A 1 40  ? 24.21100 -24.50800 15.76900 1.000 48.88727 ? 40  LYS A CG  1 
ATOM   184  C CD  . LYS A 1 40  ? 23.21500 -25.41300 15.10600 1.000 50.91221 ? 40  LYS A CD  1 
ATOM   185  C CE  . LYS A 1 40  ? 21.79900 -25.08100 15.60300 1.000 50.91735 ? 40  LYS A CE  1 
ATOM   186  N NZ  . LYS A 1 40  ? 20.90300 -26.23700 15.35100 1.000 50.39841 ? 40  LYS A NZ  1 
ATOM   187  N N   . LYS A 1 41  ? 27.90300 -25.30700 13.01400 1.000 41.20395 ? 41  LYS A N   1 
ATOM   188  C CA  . LYS A 1 41  ? 29.08300 -24.69000 12.40800 1.000 39.39622 ? 41  LYS A CA  1 
ATOM   189  C C   . LYS A 1 41  ? 28.76700 -23.29700 11.91100 1.000 36.10032 ? 41  LYS A C   1 
ATOM   190  O O   . LYS A 1 41  ? 29.56900 -22.36900 12.08200 1.000 33.29344 ? 41  LYS A O   1 
ATOM   191  C CB  . LYS A 1 41  ? 29.60800 -25.56300 11.25700 1.000 41.51029 ? 41  LYS A CB  1 
ATOM   192  C CG  . LYS A 1 41  ? 30.76500 -24.96600 10.43200 1.000 39.62286 ? 41  LYS A CG  1 
ATOM   193  C CD  . LYS A 1 41  ? 32.05900 -24.82200 11.28400 1.000 41.04139 ? 41  LYS A CD  1 
ATOM   194  C CE  . LYS A 1 41  ? 33.28400 -24.55400 10.37700 1.000 43.07808 ? 41  LYS A CE  1 
ATOM   195  N NZ  . LYS A 1 41  ? 34.53000 -24.40300 11.20700 1.000 41.20914 ? 41  LYS A NZ  1 
ATOM   196  N N   . ALA A 1 42  ? 27.58000 -23.12400 11.33400 1.000 32.32570 ? 42  ALA A N   1 
ATOM   197  C CA  . ALA A 1 42  ? 27.10300 -21.82300 10.89900 1.000 31.45124 ? 42  ALA A CA  1 
ATOM   198  C C   . ALA A 1 42  ? 25.58700 -21.81600 11.05900 1.000 31.96752 ? 42  ALA A C   1 
ATOM   199  O O   . ALA A 1 42  ? 24.95100 -22.85900 10.92200 1.000 30.90399 ? 42  ALA A O   1 
ATOM   200  C CB  . ALA A 1 42  ? 27.44700 -21.54300 9.43000  1.000 31.41830 ? 42  ALA A CB  1 
ATOM   201  N N   . VAL A 1 43  ? 25.02200 -20.63900 11.32400 1.000 33.10285 ? 43  VAL A N   1 
ATOM   202  C CA  . VAL A 1 43  ? 23.56800 -20.47700 11.46400 1.000 33.61592 ? 43  VAL A CA  1 
ATOM   203  C C   . VAL A 1 43  ? 23.17400 -19.09400 10.96200 1.000 31.64633 ? 43  VAL A C   1 
ATOM   204  O O   . VAL A 1 43  ? 23.88700 -18.11100 11.17700 1.000 29.96270 ? 43  VAL A O   1 
ATOM   205  C CB  . VAL A 1 43  ? 23.08800 -20.65500 12.92700 1.000 35.69570 ? 43  VAL A CB  1 
ATOM   206  C CG1 . VAL A 1 43  ? 23.17800 -22.03900 13.37100 1.000 43.81997 ? 43  VAL A CG1 1 
ATOM   207  C CG2 . VAL A 1 43  ? 23.89600 -19.76400 13.84200 1.000 37.67005 ? 43  VAL A CG2 1 
ATOM   208  N N   . LEU A 1 44  ? 22.02400 -19.01700 10.30200 1.000 29.37673 ? 44  LEU A N   1 
ATOM   209  C CA  . LEU A 1 44  ? 21.50000 -17.75600 9.80900  1.000 31.80716 ? 44  LEU A CA  1 
ATOM   210  C C   . LEU A 1 44  ? 20.30800 -17.34300 10.66100 1.000 30.51803 ? 44  LEU A C   1 
ATOM   211  O O   . LEU A 1 44  ? 19.54400 -18.20300 11.11600 1.000 31.17760 ? 44  LEU A O   1 
ATOM   212  C CB  . LEU A 1 44  ? 21.06900 -17.86700 8.33400  1.000 30.15356 ? 44  LEU A CB  1 
ATOM   213  C CG  . LEU A 1 44  ? 22.12600 -17.67200 7.25000  1.000 33.18907 ? 44  LEU A CG  1 
ATOM   214  C CD1 . LEU A 1 44  ? 23.16500 -18.77500 7.27900  1.000 35.27052 ? 44  LEU A CD1 1 
ATOM   215  C CD2 . LEU A 1 44  ? 21.45900 -17.62200 5.86600  1.000 33.03875 ? 44  LEU A CD2 1 
ATOM   216  N N   . PHE A 1 45  ? 20.17300 -16.02300 10.87200 1.000 29.99820 ? 45  PHE A N   1 
ATOM   217  C CA  . PHE A 1 45  ? 19.05000 -15.39200 11.56000 1.000 31.11570 ? 45  PHE A CA  1 
ATOM   218  C C   . PHE A 1 45  ? 18.34800 -14.41500 10.63500 1.000 28.25969 ? 45  PHE A C   1 
ATOM   219  O O   . PHE A 1 45  ? 18.99800 -13.68200 9.87600  1.000 29.81327 ? 45  PHE A O   1 
ATOM   220  C CB  . PHE A 1 45  ? 19.49800 -14.60500 12.80100 1.000 33.00217 ? 45  PHE A CB  1 
ATOM   221  C CG  . PHE A 1 45  ? 20.39400 -15.38700 13.72600 1.000 32.98285 ? 45  PHE A CG  1 
ATOM   222  C CD1 . PHE A 1 45  ? 20.06500 -16.66200 14.11700 1.000 41.57530 ? 45  PHE A CD1 1 
ATOM   223  C CD2 . PHE A 1 45  ? 21.57300 -14.84300 14.18200 1.000 41.74636 ? 45  PHE A CD2 1 
ATOM   224  C CE1 . PHE A 1 45  ? 20.91200 -17.37600 14.97600 1.000 45.44989 ? 45  PHE A CE1 1 
ATOM   225  C CE2 . PHE A 1 45  ? 22.41200 -15.57000 15.03600 1.000 39.81064 ? 45  PHE A CE2 1 
ATOM   226  C CZ  . PHE A 1 45  ? 22.08100 -16.80500 15.42500 1.000 39.85001 ? 45  PHE A CZ  1 
ATOM   227  N N   . CYS A 1 46  ? 17.02500 -14.32800 10.76500 1.000 33.05117 ? 46  CYS A N   1 
ATOM   228  C CA  . CYS A 1 46  ? 16.25300 -13.41600 9.93400  1.000 32.03190 ? 46  CYS A CA  1 
ATOM   229  C C   . CYS A 1 46  ? 15.14600 -12.77600 10.76200 1.000 33.72042 ? 46  CYS A C   1 
ATOM   230  O O   . CYS A 1 46  ? 14.89500 -13.15300 11.90700 1.000 33.97220 ? 46  CYS A O   1 
ATOM   231  C CB  . CYS A 1 46  ? 15.66400 -14.13900 8.70900  1.000 37.15234 ? 46  CYS A CB  1 
ATOM   232  S SG  . CYS A 1 46  ? 14.55500 -15.51500 9.13700  1.000 37.55027 ? 46  CYS A SG  1 
ATOM   233  N N   . LEU A 1 47  ? 14.48500 -11.79200 10.15800 1.000 34.79687 ? 47  LEU A N   1 
ATOM   234  C CA  . LEU A 1 47  ? 13.30000 -11.19700 10.76100 1.000 39.98154 ? 47  LEU A CA  1 
ATOM   235  C C   . LEU A 1 47  ? 12.11500 -12.15400 10.68000 1.000 43.30842 ? 47  LEU A C   1 
ATOM   236  O O   . LEU A 1 47  ? 11.94400 -12.87800 9.69100  1.000 46.74347 ? 47  LEU A O   1 
ATOM   237  C CB  . LEU A 1 47  ? 12.94700 -9.89200  10.05300 1.000 42.08154 ? 47  LEU A CB  1 
ATOM   238  C CG  . LEU A 1 47  ? 13.90100 -8.73300  10.32400 1.000 45.88060 ? 47  LEU A CG  1 
ATOM   239  C CD1 . LEU A 1 47  ? 13.42000 -7.49400  9.59200  1.000 44.22071 ? 47  LEU A CD1 1 
ATOM   240  C CD2 . LEU A 1 47  ? 13.93300 -8.48600  11.83900 1.000 46.80969 ? 47  LEU A CD2 1 
ATOM   241  N N   . SER A 1 48  ? 11.29300 -12.15200 11.72500 1.000 39.62536 ? 48  SER A N   1 
ATOM   242  C CA  . SER A 1 48  ? 10.01400 -12.85500 11.69300 1.000 43.31472 ? 48  SER A CA  1 
ATOM   243  C C   . SER A 1 48  ? 9.07300  -12.19200 10.68700 1.000 50.37896 ? 48  SER A C   1 
ATOM   244  O O   . SER A 1 48  ? 9.35300  -11.11500 10.15500 1.000 50.55508 ? 48  SER A O   1 
ATOM   245  C CB  . SER A 1 48  ? 9.38400  -12.85500 13.08000 1.000 47.21083 ? 48  SER A CB  1 
ATOM   246  O OG  . SER A 1 48  ? 9.11300  -11.51700 13.48700 1.000 50.71665 ? 48  SER A OG  1 
ATOM   247  N N   . GLU A 1 49  ? 7.91900  -12.83500 10.44900 1.000 50.57641 ? 49  GLU A N   1 
ATOM   248  C CA  . GLU A 1 49  ? 6.99400  -12.32800 9.43700  1.000 54.31455 ? 49  GLU A CA  1 
ATOM   249  C C   . GLU A 1 49  ? 6.51700  -10.92300 9.77200  1.000 59.05902 ? 49  GLU A C   1 
ATOM   250  O O   . GLU A 1 49  ? 6.43600  -10.06400 8.88700  1.000 62.70819 ? 49  GLU A O   1 
ATOM   251  C CB  . GLU A 1 49  ? 5.79200  -13.26700 9.27700  1.000 59.19801 ? 49  GLU A CB  1 
ATOM   252  N N   . ASP A 1 50  ? 6.18600  -10.66700 11.04100 1.000 58.18197 ? 50  ASP A N   1 
ATOM   253  C CA  . ASP A 1 50  ? 5.72900  -9.34000  11.42700 1.000 61.77378 ? 50  ASP A CA  1 
ATOM   254  C C   . ASP A 1 50  ? 6.87700  -8.34800  11.60300 1.000 56.09329 ? 50  ASP A C   1 
ATOM   255  O O   . ASP A 1 50  ? 6.62200  -7.18400  11.94000 1.000 61.57028 ? 50  ASP A O   1 
ATOM   256  C CB  . ASP A 1 50  ? 4.85900  -9.41700  12.69900 1.000 61.83658 ? 50  ASP A CB  1 
ATOM   257  C CG  . ASP A 1 50  ? 5.62100  -9.88600  13.94600 1.000 60.64863 ? 50  ASP A CG  1 
ATOM   258  O OD1 . ASP A 1 50  ? 6.84800  -10.10700 13.90500 1.000 59.03053 ? 50  ASP A OD1 1 
ATOM   259  O OD2 . ASP A 1 50  ? 4.96200  -10.01900 15.00300 1.000 67.27437 ? 50  ASP A OD2 1 
ATOM   260  N N   . LYS A 1 51  ? 8.11200  -8.78000  11.35600 1.000 57.38582 ? 51  LYS A N   1 
ATOM   261  C CA  . LYS A 1 51  ? 9.32000  -7.95800  11.43000 1.000 58.43190 ? 51  LYS A CA  1 
ATOM   262  C C   . LYS A 1 51  ? 9.55500  -7.39000  12.83200 1.000 56.22726 ? 51  LYS A C   1 
ATOM   263  O O   . LYS A 1 51  ? 10.23700 -6.37400  12.98200 1.000 51.75111 ? 51  LYS A O   1 
ATOM   264  C CB  . LYS A 1 51  ? 9.28900  -6.82600  10.38900 1.000 59.20835 ? 51  LYS A CB  1 
ATOM   265  C CG  . LYS A 1 51  ? 9.50200  -7.28300  8.94700  1.000 61.60788 ? 51  LYS A CG  1 
ATOM   266  C CD  . LYS A 1 51  ? 9.18100  -6.13700  8.00000  1.000 66.69892 ? 51  LYS A CD  1 
ATOM   267  C CE  . LYS A 1 51  ? 9.48000  -6.46800  6.54700  1.000 69.59335 ? 51  LYS A CE  1 
ATOM   268  N NZ  . LYS A 1 51  ? 9.18800  -5.26300  5.69900  1.000 76.07976 ? 51  LYS A NZ  1 
ATOM   269  N N   . LYS A 1 52  ? 9.02000  -8.03800  13.86700 1.000 54.19404 ? 52  LYS A N   1 
ATOM   270  C CA  . LYS A 1 52  ? 9.18600  -7.58700  15.24000 1.000 52.91162 ? 52  LYS A CA  1 
ATOM   271  C C   . LYS A 1 52  ? 10.12300 -8.46400  16.05400 1.000 50.57035 ? 52  LYS A C   1 
ATOM   272  O O   . LYS A 1 52  ? 10.35200 -8.17000  17.23300 1.000 49.19238 ? 52  LYS A O   1 
ATOM   273  C CB  . LYS A 1 52  ? 7.82200  -7.51700  15.93800 1.000 54.79572 ? 52  LYS A CB  1 
ATOM   274  C CG  . LYS A 1 52  ? 6.83400  -6.62700  15.22900 1.000 60.97876 ? 52  LYS A CG  1 
ATOM   275  C CD  . LYS A 1 52  ? 7.40000  -5.22600  15.07300 1.000 65.39866 ? 52  LYS A CD  1 
ATOM   276  C CE  . LYS A 1 52  ? 6.36600  -4.26300  14.53400 1.000 65.96559 ? 52  LYS A CE  1 
ATOM   277  N NZ  . LYS A 1 52  ? 5.80900  -3.34100  15.57800 1.000 72.89773 ? 52  LYS A NZ  1 
ATOM   278  N N   . ASN A 1 53  ? 10.66200 -9.53000  15.46200 1.000 45.50697 ? 53  ASN A N   1 
ATOM   279  C CA  . ASN A 1 53  ? 11.49400 -10.49900 16.16000 1.000 46.57789 ? 53  ASN A CA  1 
ATOM   280  C C   . ASN A 1 53  ? 12.59200 -10.97100 15.22300 1.000 43.38942 ? 53  ASN A C   1 
ATOM   281  O O   . ASN A 1 53  ? 12.38300 -11.09200 14.01400 1.000 38.91661 ? 53  ASN A O   1 
ATOM   282  C CB  . ASN A 1 53  ? 10.71900 -11.73500 16.62100 1.000 42.36180 ? 53  ASN A CB  1 
ATOM   283  C CG  . ASN A 1 53  ? 9.53200  -11.39100 17.49200 1.000 51.04240 ? 53  ASN A CG  1 
ATOM   284  O OD1 . ASN A 1 53  ? 9.66900  -11.23200 18.70100 1.000 61.10590 ? 53  ASN A OD1 1 
ATOM   285  N ND2 . ASN A 1 53  ? 8.35500  -11.28300 16.88100 1.000 55.88473 ? 53  ASN A ND2 1 
ATOM   286  N N   . ILE A 1 54  ? 13.75500 -11.24200 15.80200 1.000 41.16075 ? 54  ILE A N   1 
ATOM   287  C CA  . ILE A 1 54  ? 14.86800 -11.87000 15.10100 1.000 39.73964 ? 54  ILE A CA  1 
ATOM   288  C C   . ILE A 1 54  ? 14.84800 -13.34200 15.49000 1.000 41.38184 ? 54  ILE A C   1 
ATOM   289  O O   . ILE A 1 54  ? 14.88800 -13.66100 16.68100 1.000 40.49480 ? 54  ILE A O   1 
ATOM   290  C CB  . ILE A 1 54  ? 16.20700 -11.21300 15.46300 1.000 38.78357 ? 54  ILE A CB  1 
ATOM   291  C CG1 . ILE A 1 54  ? 16.25000 -9.77500  14.94200 1.000 46.27003 ? 54  ILE A CG1 1 
ATOM   292  C CG2 . ILE A 1 54  ? 17.37600 -12.06700 14.88400 1.000 37.31365 ? 54  ILE A CG2 1 
ATOM   293  C CD1 . ILE A 1 54  ? 17.23600 -8.84500  15.67600 1.000 47.29064 ? 54  ILE A CD1 1 
ATOM   294  N N   . ILE A 1 55  ? 14.76300 -14.23800 14.49600 1.000 35.51180 ? 55  ILE A N   1 
ATOM   295  C CA  . ILE A 1 55  ? 14.53500 -15.65600 14.71700 1.000 37.89742 ? 55  ILE A CA  1 
ATOM   296  C C   . ILE A 1 55  ? 15.57600 -16.46700 13.94600 1.000 37.49378 ? 55  ILE A C   1 
ATOM   297  O O   . ILE A 1 55  ? 16.26800 -15.96200 13.05800 1.000 35.98076 ? 55  ILE A O   1 
ATOM   298  C CB  . ILE A 1 55  ? 13.10600 -16.09400 14.31300 1.000 42.51749 ? 55  ILE A CB  1 
ATOM   299  C CG1 . ILE A 1 55  ? 12.86400 -15.83100 12.81300 1.000 40.61411 ? 55  ILE A CG1 1 
ATOM   300  C CG2 . ILE A 1 55  ? 12.03600 -15.36300 15.17200 1.000 39.00522 ? 55  ILE A CG2 1 
ATOM   301  C CD1 . ILE A 1 55  ? 11.52600 -16.31600 12.31100 1.000 42.31558 ? 55  ILE A CD1 1 
ATOM   302  N N   . LEU A 1 56  ? 15.68700 -17.74200 14.31600 1.000 40.21042 ? 56  LEU A N   1 
ATOM   303  C CA  . LEU A 1 56  ? 16.46500 -18.68600 13.52000 1.000 38.18902 ? 56  LEU A CA  1 
ATOM   304  C C   . LEU A 1 56  ? 15.78800 -18.87700 12.17200 1.000 41.44479 ? 56  LEU A C   1 
ATOM   305  O O   . LEU A 1 56  ? 14.57100 -19.09000 12.10700 1.000 40.43757 ? 56  LEU A O   1 
ATOM   306  C CB  . LEU A 1 56  ? 16.56200 -20.04300 14.22100 1.000 44.43637 ? 56  LEU A CB  1 
ATOM   307  C CG  . LEU A 1 56  ? 17.27200 -20.12600 15.56700 1.000 50.71139 ? 56  LEU A CG  1 
ATOM   308  C CD1 . LEU A 1 56  ? 17.02600 -21.49200 16.24400 1.000 49.80148 ? 56  LEU A CD1 1 
ATOM   309  C CD2 . LEU A 1 56  ? 18.74100 -19.88500 15.35600 1.000 41.18796 ? 56  LEU A CD2 1 
ATOM   310  N N   . GLU A 1 57  ? 16.57300 -18.83600 11.09900 1.000 37.27519 ? 57  GLU A N   1 
ATOM   311  C CA  . GLU A 1 57  ? 16.02200 -19.12300 9.78000  1.000 38.69450 ? 57  GLU A CA  1 
ATOM   312  C C   . GLU A 1 57  ? 16.01900 -20.62800 9.56900  1.000 39.26987 ? 57  GLU A C   1 
ATOM   313  O O   . GLU A 1 57  ? 17.08000 -21.25900 9.51400  1.000 40.41892 ? 57  GLU A O   1 
ATOM   314  C CB  . GLU A 1 57  ? 16.80700 -18.42700 8.67100  1.000 33.33911 ? 57  GLU A CB  1 
ATOM   315  C CG  . GLU A 1 57  ? 16.07400 -18.56500 7.34100  1.000 38.25509 ? 57  GLU A CG  1 
ATOM   316  C CD  . GLU A 1 57  ? 16.72100 -17.82400 6.19400  1.000 35.50397 ? 57  GLU A CD  1 
ATOM   317  O OE1 . GLU A 1 57  ? 17.93500 -17.52700 6.26200  1.000 35.64471 ? 57  GLU A OE1 1 
ATOM   318  O OE2 . GLU A 1 57  ? 15.99200 -17.54900 5.22300  1.000 37.70675 ? 57  GLU A OE2 1 
ATOM   319  N N   . GLU A 1 58  ? 14.82300 -21.19800 9.43600  1.000 41.26263 ? 58  GLU A N   1 
ATOM   320  C CA  . GLU A 1 58  ? 14.65600 -22.64700 9.42300  1.000 45.53511 ? 58  GLU A CA  1 
ATOM   321  C C   . GLU A 1 58  ? 15.51800 -23.31300 8.35300  1.000 51.37579 ? 58  GLU A C   1 
ATOM   322  O O   . GLU A 1 58  ? 15.50100 -22.92000 7.18500  1.000 43.84175 ? 58  GLU A O   1 
ATOM   323  C CB  . GLU A 1 58  ? 13.19400 -22.99600 9.18800  1.000 53.15386 ? 58  GLU A CB  1 
ATOM   324  C CG  . GLU A 1 58  ? 12.93300 -24.49200 9.19400  1.000 63.67802 ? 58  GLU A CG  1 
ATOM   325  C CD  . GLU A 1 58  ? 13.12500 -25.10800 10.57200 1.000 81.63114 ? 58  GLU A CD  1 
ATOM   326  O OE1 . GLU A 1 58  ? 13.03400 -24.35600 11.57400 1.000 77.31730 ? 58  GLU A OE1 1 
ATOM   327  O OE2 . GLU A 1 58  ? 13.36600 -26.33800 10.65300 1.000 83.18991 ? 58  GLU A OE2 1 
ATOM   328  N N   . GLY A 1 59  ? 16.27900 -24.33000 8.76000  1.000 44.90839 ? 59  GLY A N   1 
ATOM   329  C CA  . GLY A 1 59  ? 17.07000 -25.10100 7.83100  1.000 49.99285 ? 59  GLY A CA  1 
ATOM   330  C C   . GLY A 1 59  ? 18.33000 -24.43800 7.31700  1.000 41.53113 ? 59  GLY A C   1 
ATOM   331  O O   . GLY A 1 59  ? 19.11300 -25.11100 6.62100  1.000 43.57100 ? 59  GLY A O   1 
ATOM   332  N N   . LYS A 1 60  ? 18.56400 -23.15700 7.62400  1.000 35.76314 ? 60  LYS A N   1 
ATOM   333  C CA  . LYS A 1 60  ? 19.69100 -22.41900 7.05900  1.000 35.65874 ? 60  LYS A CA  1 
ATOM   334  C C   . LYS A 1 60  ? 20.83500 -22.42300 8.06100  1.000 34.50402 ? 60  LYS A C   1 
ATOM   335  O O   . LYS A 1 60  ? 21.17400 -21.43400 8.69700  1.000 31.77558 ? 60  LYS A O   1 
ATOM   336  C CB  . LYS A 1 60  ? 19.27700 -21.00700 6.67200  1.000 34.84155 ? 60  LYS A CB  1 
ATOM   337  C CG  . LYS A 1 60  ? 18.14200 -21.00300 5.67400  1.000 35.11057 ? 60  LYS A CG  1 
ATOM   338  C CD  . LYS A 1 60  ? 18.51000 -21.70100 4.39800  1.000 38.05904 ? 60  LYS A CD  1 
ATOM   339  C CE  . LYS A 1 60  ? 17.31700 -21.63200 3.45600  1.000 38.80207 ? 60  LYS A CE  1 
ATOM   340  N NZ  . LYS A 1 60  ? 17.39300 -22.64500 2.41100  1.000 43.74406 ? 60  LYS A NZ  1 
ATOM   341  N N   . GLU A 1 61  ? 21.44100 -23.59900 8.15600  1.000 33.05593 ? 61  GLU A N   1 
ATOM   342  C CA  . GLU A 1 61  ? 22.52000 -23.85000 9.08600  1.000 35.90398 ? 61  GLU A CA  1 
ATOM   343  C C   . GLU A 1 61  ? 23.37300 -24.97000 8.51700  1.000 32.53053 ? 61  GLU A C   1 
ATOM   344  O O   . GLU A 1 61  ? 22.92400 -25.75800 7.68200  1.000 35.96250 ? 61  GLU A O   1 
ATOM   345  C CB  . GLU A 1 61  ? 21.99500 -24.27600 10.45200 1.000 34.90398 ? 61  GLU A CB  1 
ATOM   346  C CG  . GLU A 1 61  ? 21.34200 -25.65800 10.39900 1.000 36.70575 ? 61  GLU A CG  1 
ATOM   347  C CD  . GLU A 1 61  ? 20.73800 -26.10000 11.72000 1.000 48.58264 ? 61  GLU A CD  1 
ATOM   348  O OE1 . GLU A 1 61  ? 20.78800 -25.31400 12.69300 1.000 48.73042 ? 61  GLU A OE1 1 
ATOM   349  O OE2 . GLU A 1 61  ? 20.22400 -27.24700 11.79000 1.000 48.12678 ? 61  GLU A OE2 1 
ATOM   350  N N   . ILE A 1 62  ? 24.58800 -25.04800 9.02200  1.000 32.25110 ? 62  ILE A N   1 
ATOM   351  C CA  . ILE A 1 62  ? 25.48900 -26.17300 8.79600  1.000 33.54797 ? 62  ILE A CA  1 
ATOM   352  C C   . ILE A 1 62  ? 25.82700 -26.76300 10.15300 1.000 32.95825 ? 62  ILE A C   1 
ATOM   353  O O   . ILE A 1 62  ? 26.23100 -26.02600 11.05700 1.000 32.09678 ? 62  ILE A O   1 
ATOM   354  C CB  . ILE A 1 62  ? 26.77800 -25.71800 8.09400  1.000 33.82704 ? 62  ILE A CB  1 
ATOM   355  C CG1 . ILE A 1 62  ? 26.46200 -25.03500 6.76800  1.000 34.43723 ? 62  ILE A CG1 1 
ATOM   356  C CG2 . ILE A 1 62  ? 27.75900 -26.92600 7.91100  1.000 34.72996 ? 62  ILE A CG2 1 
ATOM   357  C CD1 . ILE A 1 62  ? 27.67800 -24.37600 6.15000  1.000 34.65546 ? 62  ILE A CD1 1 
ATOM   358  N N   . LEU A 1 63  ? 25.68800 -28.08300 10.29200 1.000 31.52391 ? 63  LEU A N   1 
ATOM   359  C CA  . LEU A 1 63  ? 26.08800 -28.75300 11.51200 1.000 32.04382 ? 63  LEU A CA  1 
ATOM   360  C C   . LEU A 1 63  ? 27.49700 -29.31800 11.36600 1.000 36.80998 ? 63  LEU A C   1 
ATOM   361  O O   . LEU A 1 63  ? 27.96200 -29.62900 10.26200 1.000 35.01121 ? 63  LEU A O   1 
ATOM   362  C CB  . LEU A 1 63  ? 25.12300 -29.87800 11.87700 1.000 34.87210 ? 63  LEU A CB  1 
ATOM   363  C CG  . LEU A 1 63  ? 23.64300 -29.49100 11.99400 1.000 39.56296 ? 63  LEU A CG  1 
ATOM   364  C CD1 . LEU A 1 63  ? 22.85100 -30.70300 12.53800 1.000 42.31101 ? 63  LEU A CD1 1 
ATOM   365  C CD2 . LEU A 1 63  ? 23.49300 -28.24800 12.88400 1.000 39.38585 ? 63  LEU A CD2 1 
ATOM   366  N N   . VAL A 1 64  ? 28.16700 -29.44700 12.51000 1.000 33.41835 ? 64  VAL A N   1 
ATOM   367  C CA  . VAL A 1 64  ? 29.49200 -30.05300 12.54600 1.000 34.15593 ? 64  VAL A CA  1 
ATOM   368  C C   . VAL A 1 64  ? 29.46200 -31.43400 11.90400 1.000 38.44751 ? 64  VAL A C   1 
ATOM   369  O O   . VAL A 1 64  ? 30.36900 -31.80300 11.14600 1.000 40.89321 ? 64  VAL A O   1 
ATOM   370  C CB  . VAL A 1 64  ? 29.99500 -30.07800 14.00000 1.000 37.70350 ? 64  VAL A CB  1 
ATOM   371  C CG1 . VAL A 1 64  ? 31.22300 -31.00300 14.16800 1.000 40.58860 ? 64  VAL A CG1 1 
ATOM   372  C CG2 . VAL A 1 64  ? 30.30900 -28.62800 14.44100 1.000 40.83968 ? 64  VAL A CG2 1 
ATOM   373  N N   . GLY A 1 65  ? 28.41000 -32.20800 12.17100 1.000 38.77665 ? 65  GLY A N   1 
ATOM   374  C CA  . GLY A 1 65  ? 28.29600 -33.52900 11.57900 1.000 42.21043 ? 65  GLY A CA  1 
ATOM   375  C C   . GLY A 1 65  ? 28.02600 -33.53100 10.08500 1.000 41.45646 ? 65  GLY A C   1 
ATOM   376  O O   . GLY A 1 65  ? 28.17000 -34.58500 9.45300  1.000 48.26979 ? 65  GLY A O   1 
ATOM   377  N N   . ASP A 1 66  ? 27.63000 -32.38500 9.51300  1.000 40.05065 ? 66  ASP A N   1 
ATOM   378  C CA  . ASP A 1 66  ? 27.47000 -32.26300 8.06100  1.000 43.80174 ? 66  ASP A CA  1 
ATOM   379  C C   . ASP A 1 66  ? 28.81700 -32.25500 7.35400  1.000 46.02917 ? 66  ASP A C   1 
ATOM   380  O O   . ASP A 1 66  ? 28.91700 -32.69500 6.20100  1.000 46.53770 ? 66  ASP A O   1 
ATOM   381  C CB  . ASP A 1 66  ? 26.73100 -30.97300 7.68100  1.000 42.87521 ? 66  ASP A CB  1 
ATOM   382  C CG  . ASP A 1 66  ? 25.28700 -30.93400 8.17000  1.000 42.46725 ? 66  ASP A CG  1 
ATOM   383  O OD1 . ASP A 1 66  ? 24.69300 -32.01400 8.35500  1.000 43.36895 ? 66  ASP A OD1 1 
ATOM   384  O OD2 . ASP A 1 66  ? 24.75900 -29.81100 8.36300  1.000 42.18819 ? 66  ASP A OD2 1 
ATOM   385  N N   . VAL A 1 67  ? 29.85000 -31.74700 8.01800  1.000 43.17694 ? 67  VAL A N   1 
ATOM   386  C CA  . VAL A 1 67  ? 31.12500 -31.47900 7.36200  1.000 47.46098 ? 67  VAL A CA  1 
ATOM   387  C C   . VAL A 1 67  ? 31.86100 -32.80100 7.16900  1.000 50.39886 ? 67  VAL A C   1 
ATOM   388  O O   . VAL A 1 67  ? 32.07400 -33.55200 8.12600  1.000 52.39707 ? 67  VAL A O   1 
ATOM   389  C CB  . VAL A 1 67  ? 31.96100 -30.47400 8.17100  1.000 44.34458 ? 67  VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 67  ? 33.26400 -30.16300 7.43900  1.000 50.59393 ? 67  VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 67  ? 31.16400 -29.19500 8.43400  1.000 38.84376 ? 67  VAL A CG2 1 
ATOM   392  N N   . GLY A 1 68  ? 32.22000 -33.10900 5.92000  1.000 49.78986 ? 68  GLY A N   1 
ATOM   393  C CA  . GLY A 1 68  ? 32.72600 -34.41900 5.57100  1.000 49.98043 ? 68  GLY A CA  1 
ATOM   394  C C   . GLY A 1 68  ? 31.66900 -35.42600 5.15300  1.000 58.83862 ? 68  GLY A C   1 
ATOM   395  O O   . GLY A 1 68  ? 32.02600 -36.50400 4.65300  1.000 60.83672 ? 68  GLY A O   1 
ATOM   396  N N   . GLN A 1 69  ? 30.37900 -35.10500 5.31500  1.000 58.78368 ? 69  GLN A N   1 
ATOM   397  C CA  . GLN A 1 69  ? 29.28900 -35.98200 4.89100  1.000 62.64503 ? 69  GLN A CA  1 
ATOM   398  C C   . GLN A 1 69  ? 28.51200 -35.40400 3.71100  1.000 62.51107 ? 69  GLN A C   1 
ATOM   399  O O   . GLN A 1 69  ? 28.47500 -36.01300 2.63700  1.000 68.22024 ? 69  GLN A O   1 
ATOM   400  C CB  . GLN A 1 69  ? 28.33100 -36.27000 6.06200  1.000 59.81762 ? 69  GLN A CB  1 
ATOM   401  C CG  . GLN A 1 69  ? 28.98500 -36.77400 7.36600  1.000 62.38347 ? 69  GLN A CG  1 
ATOM   402  C CD  . GLN A 1 69  ? 29.78400 -38.06400 7.22200  1.000 68.92922 ? 69  GLN A CD  1 
ATOM   403  O OE1 . GLN A 1 69  ? 29.26300 -39.11500 6.81400  1.000 70.15223 ? 69  GLN A OE1 1 
ATOM   404  N NE2 . GLN A 1 69  ? 31.06300 -37.99500 7.58500  1.000 66.64423 ? 69  GLN A NE2 1 
ATOM   405  N N   . THR A 1 70  ? 27.85700 -34.25500 3.88800  1.000 52.30257 ? 70  THR A N   1 
ATOM   406  C CA  . THR A 1 70  ? 27.18000 -33.57300 2.79700  1.000 50.99397 ? 70  THR A CA  1 
ATOM   407  C C   . THR A 1 70  ? 27.77400 -32.21300 2.50800  1.000 51.61927 ? 70  THR A C   1 
ATOM   408  O O   . THR A 1 70  ? 27.33400 -31.55300 1.55700  1.000 52.46614 ? 70  THR A O   1 
ATOM   409  C CB  . THR A 1 70  ? 25.67900 -33.38500 3.09100  1.000 50.25053 ? 70  THR A CB  1 
ATOM   410  O OG1 . THR A 1 70  ? 25.51400 -32.56900 4.26200  1.000 50.56251 ? 70  THR A OG1 1 
ATOM   411  C CG2 . THR A 1 70  ? 24.97800 -34.72500 3.28100  1.000 57.11277 ? 70  THR A CG2 1 
ATOM   412  N N   . VAL A 1 71  ? 28.72200 -31.75300 3.32200  1.000 49.88052 ? 71  VAL A N   1 
ATOM   413  C CA  . VAL A 1 71  ? 29.30400 -30.42400 3.19000  1.000 42.40231 ? 71  VAL A CA  1 
ATOM   414  C C   . VAL A 1 71  ? 30.81400 -30.60000 3.14000  1.000 49.58284 ? 71  VAL A C   1 
ATOM   415  O O   . VAL A 1 71  ? 31.40400 -31.19200 4.05100  1.000 47.37320 ? 71  VAL A O   1 
ATOM   416  C CB  . VAL A 1 71  ? 28.88600 -29.49700 4.34200  1.000 41.99129 ? 71  VAL A CB  1 
ATOM   417  C CG1 . VAL A 1 71  ? 29.63800 -28.15000 4.26200  1.000 40.71338 ? 71  VAL A CG1 1 
ATOM   418  C CG2 . VAL A 1 71  ? 27.34800 -29.24400 4.27900  1.000 38.56235 ? 71  VAL A CG2 1 
ATOM   419  N N   . ASP A 1 72  ? 31.42700 -30.14300 2.05900  1.000 47.13520 ? 72  ASP A N   1 
ATOM   420  C CA  . ASP A 1 72  ? 32.86200 -30.28500 1.86900  1.000 52.25704 ? 72  ASP A CA  1 
ATOM   421  C C   . ASP A 1 72  ? 33.61600 -28.99700 2.22600  1.000 46.56274 ? 72  ASP A C   1 
ATOM   422  O O   . ASP A 1 72  ? 34.73700 -29.05000 2.74200  1.000 57.35866 ? 72  ASP A O   1 
ATOM   423  C CB  . ASP A 1 72  ? 33.10800 -30.71700 0.41400  1.000 53.48495 ? 72  ASP A CB  1 
ATOM   424  C CG  . ASP A 1 72  ? 34.56000 -30.88900 0.07800  1.000 63.05898 ? 72  ASP A CG  1 
ATOM   425  O OD1 . ASP A 1 72  ? 35.30600 -29.89800 0.23100  1.000 68.75189 ? 72  ASP A OD1 1 
ATOM   426  O OD2 . ASP A 1 72  ? 34.96300 -32.00300 -0.36800 1.000 73.11861 ? 72  ASP A OD2 1 
ATOM   427  N N   . ASP A 1 73  ? 33.03200 -27.84800 1.93000  1.000 39.12511 ? 73  ASP A N   1 
ATOM   428  C CA  . ASP A 1 73  ? 33.61500 -26.52700 2.18700  1.000 41.37132 ? 73  ASP A CA  1 
ATOM   429  C C   . ASP A 1 73  ? 32.53500 -25.72700 2.91600  1.000 35.19185 ? 73  ASP A C   1 
ATOM   430  O O   . ASP A 1 73  ? 31.65900 -25.12100 2.27700  1.000 34.14382 ? 73  ASP A O   1 
ATOM   431  C CB  . ASP A 1 73  ? 34.03400 -25.87600 0.86400  1.000 41.66209 ? 73  ASP A CB  1 
ATOM   432  C CG  . ASP A 1 73  ? 34.74700 -24.53700 1.02800  1.000 47.57151 ? 73  ASP A CG  1 
ATOM   433  O OD1 . ASP A 1 73  ? 34.50200 -23.79600 1.98900  1.000 40.54045 ? 73  ASP A OD1 1 
ATOM   434  O OD2 . ASP A 1 73  ? 35.56500 -24.22300 0.14100  1.000 51.04965 ? 73  ASP A OD2 1 
ATOM   435  N N   . PRO A 1 74  ? 32.53700 -25.72400 4.25600  1.000 34.52698 ? 74  PRO A N   1 
ATOM   436  C CA  . PRO A 1 74  ? 31.40600 -25.08500 4.95600  1.000 32.82955 ? 74  PRO A CA  1 
ATOM   437  C C   . PRO A 1 74  ? 31.29600 -23.58900 4.70000  1.000 32.28906 ? 74  PRO A C   1 
ATOM   438  O O   . PRO A 1 74  ? 30.18000 -23.07200 4.64900  1.000 32.50456 ? 74  PRO A O   1 
ATOM   439  C CB  . PRO A 1 74  ? 31.65400 -25.38800 6.44800  1.000 35.89374 ? 74  PRO A CB  1 
ATOM   440  C CG  . PRO A 1 74  ? 33.02800 -25.96800 6.54800  1.000 35.44528 ? 74  PRO A CG  1 
ATOM   441  C CD  . PRO A 1 74  ? 33.42600 -26.47900 5.16800  1.000 38.67573 ? 74  PRO A CD  1 
ATOM   442  N N   . TYR A 1 75  ? 32.40700 -22.87400 4.53600  1.000 34.41509 ? 75  TYR A N   1 
ATOM   443  C CA  . TYR A 1 75  ? 32.26000 -21.44300 4.28400  1.000 35.68033 ? 75  TYR A CA  1 
ATOM   444  C C   . TYR A 1 75  ? 31.62000 -21.18800 2.92400  1.000 31.04754 ? 75  TYR A C   1 
ATOM   445  O O   . TYR A 1 75  ? 30.77200 -20.30800 2.79200  1.000 31.66799 ? 75  TYR A O   1 
ATOM   446  C CB  . TYR A 1 75  ? 33.59600 -20.70900 4.38000  1.000 37.82503 ? 75  TYR A CB  1 
ATOM   447  C CG  . TYR A 1 75  ? 33.33200 -19.20800 4.51100  1.000 39.43528 ? 75  TYR A CG  1 
ATOM   448  C CD1 . TYR A 1 75  ? 32.84100 -18.68500 5.69900  1.000 40.79912 ? 75  TYR A CD1 1 
ATOM   449  C CD2 . TYR A 1 75  ? 33.51300 -18.33200 3.43100  1.000 48.26801 ? 75  TYR A CD2 1 
ATOM   450  C CE1 . TYR A 1 75  ? 32.55700 -17.32500 5.83600  1.000 43.42168 ? 75  TYR A CE1 1 
ATOM   451  C CE2 . TYR A 1 75  ? 33.24700 -16.95000 3.56300  1.000 41.41912 ? 75  TYR A CE2 1 
ATOM   452  C CZ  . TYR A 1 75  ? 32.76900 -16.46500 4.77000  1.000 46.97282 ? 75  TYR A CZ  1 
ATOM   453  O OH  . TYR A 1 75  ? 32.48200 -15.11800 4.93600  1.000 47.68662 ? 75  TYR A OH  1 
ATOM   454  N N   . ALA A 1 76  ? 32.00500 -21.95300 1.90600  1.000 33.18026 ? 76  ALA A N   1 
ATOM   455  C CA  . ALA A 1 76  ? 31.37900 -21.78600 0.59900  1.000 33.53483 ? 76  ALA A CA  1 
ATOM   456  C C   . ALA A 1 76  ? 29.89800 -22.15200 0.66000  1.000 33.45024 ? 76  ALA A C   1 
ATOM   457  O O   . ALA A 1 76  ? 29.05600 -21.50800 0.02100  1.000 31.70436 ? 76  ALA A O   1 
ATOM   458  C CB  . ALA A 1 76  ? 32.11400 -22.64100 -0.43900 1.000 37.60601 ? 76  ALA A CB  1 
ATOM   459  N N   . THR A 1 77  ? 29.55600 -23.18800 1.41800  1.000 31.57690 ? 77  THR A N   1 
ATOM   460  C CA  . THR A 1 77  ? 28.14200 -23.53600 1.53200  1.000 33.86267 ? 77  THR A CA  1 
ATOM   461  C C   . THR A 1 77  ? 27.37700 -22.46600 2.30400  1.000 32.74171 ? 77  THR A C   1 
ATOM   462  O O   . THR A 1 77  ? 26.23200 -22.14100 1.96200  1.000 31.36959 ? 77  THR A O   1 
ATOM   463  C CB  . THR A 1 77  ? 27.99200 -24.90300 2.19600  1.000 33.75424 ? 77  THR A CB  1 
ATOM   464  O OG1 . THR A 1 77  ? 28.72600 -25.87600 1.43300  1.000 34.63991 ? 77  THR A OG1 1 
ATOM   465  C CG2 . THR A 1 77  ? 26.51600 -25.31300 2.26400  1.000 34.67086 ? 77  THR A CG2 1 
ATOM   466  N N   . PHE A 1 78  ? 27.98700 -21.92900 3.36100  1.000 29.75304 ? 78  PHE A N   1 
ATOM   467  C CA  . PHE A 1 78  ? 27.40300 -20.78800 4.06900  1.000 30.06566 ? 78  PHE A CA  1 
ATOM   468  C C   . PHE A 1 78  ? 27.07300 -19.64600 3.10600  1.000 31.84186 ? 78  PHE A C   1 
ATOM   469  O O   . PHE A 1 78  ? 25.94700 -19.13800 3.08500  1.000 31.85510 ? 78  PHE A O   1 
ATOM   470  C CB  . PHE A 1 78  ? 28.36800 -20.31900 5.15800  1.000 31.31615 ? 78  PHE A CB  1 
ATOM   471  C CG  . PHE A 1 78  ? 28.07100 -18.93900 5.68000  1.000 33.73173 ? 78  PHE A CG  1 
ATOM   472  C CD1 . PHE A 1 78  ? 26.94600 -18.71200 6.46100  1.000 33.07585 ? 78  PHE A CD1 1 
ATOM   473  C CD2 . PHE A 1 78  ? 28.91300 -17.88100 5.38500  1.000 32.69409 ? 78  PHE A CD2 1 
ATOM   474  C CE1 . PHE A 1 78  ? 26.65500 -17.42500 6.94700  1.000 35.31928 ? 78  PHE A CE1 1 
ATOM   475  C CE2 . PHE A 1 78  ? 28.63200 -16.58300 5.86200  1.000 36.08864 ? 78  PHE A CE2 1 
ATOM   476  C CZ  . PHE A 1 78  ? 27.50400 -16.36400 6.63900  1.000 33.79356 ? 78  PHE A CZ  1 
ATOM   477  N N   . VAL A 1 79  ? 28.04000 -19.25100 2.28100  1.000 30.24471 ? 79  VAL A N   1 
ATOM   478  C CA  . VAL A 1 79  ? 27.81400 -18.14000 1.34500  1.000 30.91462 ? 79  VAL A CA  1 
ATOM   479  C C   . VAL A 1 79  ? 26.66400 -18.45100 0.38900  1.000 33.16591 ? 79  VAL A C   1 
ATOM   480  O O   . VAL A 1 79  ? 25.86400 -17.56000 0.04100  1.000 29.95379 ? 79  VAL A O   1 
ATOM   481  C CB  . VAL A 1 79  ? 29.11600 -17.81200 0.58800  1.000 32.66000 ? 79  VAL A CB  1 
ATOM   482  C CG1 . VAL A 1 79  ? 28.82700 -16.82400 -0.54200 1.000 35.64642 ? 79  VAL A CG1 1 
ATOM   483  C CG2 . VAL A 1 79  ? 30.17300 -17.23800 1.56800  1.000 35.18288 ? 79  VAL A CG2 1 
ATOM   484  N N   . LYS A 1 80  ? 26.53100 -19.72600 -0.02500 1.000 30.86936 ? 80  LYS A N   1 
ATOM   485  C CA  . LYS A 1 80  ? 25.45100 -20.10000 -0.94100 1.000 31.87007 ? 80  LYS A CA  1 
ATOM   486  C C   . LYS A 1 80  ? 24.08200 -19.95900 -0.28900 1.000 30.53890 ? 80  LYS A C   1 
ATOM   487  O O   . LYS A 1 80  ? 23.08100 -19.85100 -1.00000 1.000 32.52670 ? 80  LYS A O   1 
ATOM   488  C CB  . LYS A 1 80  ? 25.63900 -21.54100 -1.47100 1.000 34.72991 ? 80  LYS A CB  1 
ATOM   489  C CG  . LYS A 1 80  ? 26.55700 -21.60700 -2.70500 1.000 38.86790 ? 80  LYS A CG  1 
ATOM   490  C CD  . LYS A 1 80  ? 26.76100 -23.00400 -3.30800 1.000 49.94201 ? 80  LYS A CD  1 
ATOM   491  C CE  . LYS A 1 80  ? 27.29700 -22.84700 -4.75500 1.000 50.34118 ? 80  LYS A CE  1 
ATOM   492  N NZ  . LYS A 1 80  ? 27.75100 -24.10100 -5.46600 1.000 57.02763 ? 80  LYS A NZ  1 
ATOM   493  N N   . MET A 1 81  ? 24.01700 -19.92400 1.03300  1.000 29.45740 ? 81  MET A N   1 
ATOM   494  C CA  . MET A 1 81  ? 22.73500 -19.77600 1.70900  1.000 30.66660 ? 81  MET A CA  1 
ATOM   495  C C   . MET A 1 81  ? 22.34100 -18.31300 1.91900  1.000 30.10684 ? 81  MET A C   1 
ATOM   496  O O   . MET A 1 81  ? 21.20200 -18.05600 2.32300  1.000 34.18107 ? 81  MET A O   1 
ATOM   497  C CB  . MET A 1 81  ? 22.74900 -20.49200 3.06900  1.000 33.01114 ? 81  MET A CB  1 
ATOM   498  C CG  . MET A 1 81  ? 22.68100 -22.00800 2.97100  1.000 36.59574 ? 81  MET A CG  1 
ATOM   499  S SD  . MET A 1 81  ? 22.44100 -22.77900 4.59700  1.000 39.36112 ? 81  MET A SD  1 
ATOM   500  C CE  . MET A 1 81  ? 23.98800 -22.39500 5.38400  1.000 34.95585 ? 81  MET A CE  1 
ATOM   501  N N   . LEU A 1 82  ? 23.23000 -17.36400 1.63500  1.000 29.21673 ? 82  LEU A N   1 
ATOM   502  C CA  . LEU A 1 82  ? 22.88500 -15.93900 1.79200  1.000 31.06255 ? 82  LEU A CA  1 
ATOM   503  C C   . LEU A 1 82  ? 21.94900 -15.50000 0.66600  1.000 33.23584 ? 82  LEU A C   1 
ATOM   504  O O   . LEU A 1 82  ? 22.18800 -15.83100 -0.50400 1.000 35.54071 ? 82  LEU A O   1 
ATOM   505  C CB  . LEU A 1 82  ? 24.15600 -15.06400 1.81900  1.000 30.06027 ? 82  LEU A CB  1 
ATOM   506  C CG  . LEU A 1 82  ? 25.13500 -15.33100 2.97200  1.000 31.42120 ? 82  LEU A CG  1 
ATOM   507  C CD1 . LEU A 1 82  ? 26.45600 -14.63100 2.80300  1.000 34.36768 ? 82  LEU A CD1 1 
ATOM   508  C CD2 . LEU A 1 82  ? 24.51500 -14.96300 4.29500  1.000 30.22448 ? 82  LEU A CD2 1 
ATOM   509  N N   . PRO A 1 83  ? 20.85300 -14.79400 0.97300  1.000 31.74995 ? 83  PRO A N   1 
ATOM   510  C CA  . PRO A 1 83  ? 19.93600 -14.34400 -0.08700 1.000 31.70051 ? 83  PRO A CA  1 
ATOM   511  C C   . PRO A 1 83  ? 20.50200 -13.18300 -0.89600 1.000 33.69513 ? 83  PRO A C   1 
ATOM   512  O O   . PRO A 1 83  ? 21.12000 -12.26100 -0.34800 1.000 32.39512 ? 83  PRO A O   1 
ATOM   513  C CB  . PRO A 1 83  ? 18.68200 -13.91100 0.68700  1.000 33.32781 ? 83  PRO A CB  1 
ATOM   514  C CG  . PRO A 1 83  ? 19.23400 -13.44600 2.04700  1.000 33.56777 ? 83  PRO A CG  1 
ATOM   515  C CD  . PRO A 1 83  ? 20.40500 -14.41000 2.33100  1.000 31.61591 ? 83  PRO A CD  1 
ATOM   516  N N   . ASP A 1 84  ? 20.28500 -13.24200 -2.22200 1.000 29.63742 ? 84  ASP A N   1 
ATOM   517  C CA  . ASP A 1 84  ? 20.78100 -12.18200 -3.10600 1.000 32.02137 ? 84  ASP A CA  1 
ATOM   518  C C   . ASP A 1 84  ? 20.17300 -10.82600 -2.76900 1.000 33.48792 ? 84  ASP A C   1 
ATOM   519  O O   . ASP A 1 84  ? 20.82400 -9.78600  -2.93700 1.000 32.95016 ? 84  ASP A O   1 
ATOM   520  C CB  . ASP A 1 84  ? 20.45200 -12.50300 -4.56900 1.000 34.89089 ? 84  ASP A CB  1 
ATOM   521  C CG  . ASP A 1 84  ? 21.43000 -13.45400 -5.19400 1.000 40.78981 ? 84  ASP A CG  1 
ATOM   522  O OD1 . ASP A 1 84  ? 22.38600 -13.85500 -4.50800 1.000 40.97697 ? 84  ASP A OD1 1 
ATOM   523  O OD2 . ASP A 1 84  ? 21.23800 -13.78200 -6.38200 1.000 40.09684 ? 84  ASP A OD2 1 
ATOM   524  N N   . LYS A 1 85  ? 18.90500 -10.80900 -2.37100 1.000 33.38803 ? 85  LYS A N   1 
ATOM   525  C CA  . LYS A 1 85  ? 18.17400 -9.55200  -2.25400 1.000 35.90042 ? 85  LYS A CA  1 
ATOM   526  C C   . LYS A 1 85  ? 17.46300 -9.42900  -0.90800 1.000 34.72471 ? 85  LYS A C   1 
ATOM   527  O O   . LYS A 1 85  ? 16.35000 -8.89000  -0.82200 1.000 33.07453 ? 85  LYS A O   1 
ATOM   528  C CB  . LYS A 1 85  ? 17.18300 -9.40100  -3.40400 1.000 37.77248 ? 85  LYS A CB  1 
ATOM   529  C CG  . LYS A 1 85  ? 17.85900 -9.30000  -4.76800 1.000 42.60450 ? 85  LYS A CG  1 
ATOM   530  C CD  . LYS A 1 85  ? 16.86200 -9.07400  -5.88300 1.000 47.20578 ? 85  LYS A CD  1 
ATOM   531  C CE  . LYS A 1 85  ? 17.59200 -8.68800  -7.17600 1.000 53.03908 ? 85  LYS A CE  1 
ATOM   532  N NZ  . LYS A 1 85  ? 16.66300 -8.54000  -8.34300 1.000 62.49020 ? 85  LYS A NZ  1 
ATOM   533  N N   . ASP A 1 86  ? 18.09100 -9.91500  0.16100  1.000 31.91656 ? 86  ASP A N   1 
ATOM   534  C CA  . ASP A 1 86  ? 17.58800 -9.67200  1.50800  1.000 31.81925 ? 86  ASP A CA  1 
ATOM   535  C C   . ASP A 1 86  ? 18.76000 -9.67100  2.46900  1.000 31.95021 ? 86  ASP A C   1 
ATOM   536  O O   . ASP A 1 86  ? 19.83600 -10.19000 2.16600  1.000 32.10862 ? 86  ASP A O   1 
ATOM   537  C CB  . ASP A 1 86  ? 16.55600 -10.72100 1.93500  1.000 33.03660 ? 86  ASP A CB  1 
ATOM   538  C CG  . ASP A 1 86  ? 15.64400 -10.24100 3.06500  1.000 40.53513 ? 86  ASP A CG  1 
ATOM   539  O OD1 . ASP A 1 86  ? 15.69300 -9.03600  3.47100  1.000 42.00660 ? 86  ASP A OD1 1 
ATOM   540  O OD2 . ASP A 1 86  ? 14.84900 -11.08300 3.54100  1.000 43.15658 ? 86  ASP A OD2 1 
ATOM   541  N N   . CYS A 1 87  ? 18.53600 -9.10900  3.65300  1.000 28.01340 ? 87  CYS A N   1 
ATOM   542  C CA  . CYS A 1 87  ? 19.58700 -9.05600  4.65700  1.000 27.62474 ? 87  CYS A CA  1 
ATOM   543  C C   . CYS A 1 87  ? 19.48100 -10.24300 5.60400  1.000 30.71378 ? 87  CYS A C   1 
ATOM   544  O O   . CYS A 1 87  ? 18.41700 -10.83500 5.75300  1.000 29.50643 ? 87  CYS A O   1 
ATOM   545  C CB  . CYS A 1 87  ? 19.50700 -7.76200  5.47600  1.000 28.42848 ? 87  CYS A CB  1 
ATOM   546  S SG  . CYS A 1 87  ? 19.68100 -6.25600  4.49700  1.000 33.58644 ? 87  CYS A SG  1 
ATOM   547  N N   . ARG A 1 88  ? 20.58800 -10.53200 6.30500  1.000 27.96132 ? 88  ARG A N   1 
ATOM   548  C CA  . ARG A 1 88  ? 20.65100 -11.62100 7.28500  1.000 27.01130 ? 88  ARG A CA  1 
ATOM   549  C C   . ARG A 1 88  ? 21.69400 -11.29000 8.34300  1.000 28.13877 ? 88  ARG A C   1 
ATOM   550  O O   . ARG A 1 88  ? 22.62000 -10.50300 8.10600  1.000 28.63680 ? 88  ARG A O   1 
ATOM   551  C CB  . ARG A 1 88  ? 21.01900 -13.01000 6.66800  1.000 29.25739 ? 88  ARG A CB  1 
ATOM   552  C CG  . ARG A 1 88  ? 19.98600 -13.61300 5.74400  1.000 29.13390 ? 88  ARG A CG  1 
ATOM   553  C CD  . ARG A 1 88  ? 18.71200 -14.03600 6.52100  1.000 33.08571 ? 88  ARG A CD  1 
ATOM   554  N NE  . ARG A 1 88  ? 17.74300 -14.71200 5.66100  1.000 32.31197 ? 88  ARG A NE  1 
ATOM   555  C CZ  . ARG A 1 88  ? 16.79800 -14.10300 4.95900  1.000 32.50859 ? 88  ARG A CZ  1 
ATOM   556  N NH1 . ARG A 1 88  ? 16.64500 -12.78700 4.98700  1.000 32.92744 ? 88  ARG A NH1 1 
ATOM   557  N NH2 . ARG A 1 88  ? 15.97700 -14.83400 4.21300  1.000 37.06931 ? 88  ARG A NH2 1 
ATOM   558  N N   . TYR A 1 89  ? 21.51300 -11.85900 9.53200  1.000 27.35472 ? 89  TYR A N   1 
ATOM   559  C CA  . TYR A 1 89  ? 22.62100 -12.01000 10.46000 1.000 26.56014 ? 89  TYR A CA  1 
ATOM   560  C C   . TYR A 1 89  ? 23.05000 -13.46600 10.43300 1.000 30.00185 ? 89  TYR A C   1 
ATOM   561  O O   . TYR A 1 89  ? 22.29000 -14.34300 10.02400 1.000 29.21682 ? 89  TYR A O   1 
ATOM   562  C CB  . TYR A 1 89  ? 22.22800 -11.65400 11.88600 1.000 28.58233 ? 89  TYR A CB  1 
ATOM   563  C CG  . TYR A 1 89  ? 21.50300 -10.34700 12.08000 1.000 31.63641 ? 89  TYR A CG  1 
ATOM   564  C CD1 . TYR A 1 89  ? 22.09400 -9.13500  11.72900 1.000 31.14137 ? 89  TYR A CD1 1 
ATOM   565  C CD2 . TYR A 1 89  ? 20.25900 -10.32600 12.67600 1.000 34.29708 ? 89  TYR A CD2 1 
ATOM   566  C CE1 . TYR A 1 89  ? 21.44100 -7.91700  11.97800 1.000 31.23213 ? 89  TYR A CE1 1 
ATOM   567  C CE2 . TYR A 1 89  ? 19.58100 -9.12400  12.91100 1.000 37.89960 ? 89  TYR A CE2 1 
ATOM   568  C CZ  . TYR A 1 89  ? 20.18100 -7.92400  12.55600 1.000 37.03695 ? 89  TYR A CZ  1 
ATOM   569  O OH  . TYR A 1 89  ? 19.49600 -6.75300  12.82400 1.000 41.16069 ? 89  TYR A OH  1 
ATOM   570  N N   . ALA A 1 90  ? 24.27100 -13.72300 10.89900 1.000 30.43512 ? 90  ALA A N   1 
ATOM   571  C CA  . ALA A 1 90  ? 24.75000 -15.09700 10.96900 1.000 27.58784 ? 90  ALA A CA  1 
ATOM   572  C C   . ALA A 1 90  ? 25.81400 -15.21200 12.04800 1.000 31.81879 ? 90  ALA A C   1 
ATOM   573  O O   . ALA A 1 90  ? 26.44200 -14.22300 12.43800 1.000 30.65809 ? 90  ALA A O   1 
ATOM   574  C CB  . ALA A 1 90  ? 25.32500 -15.57100 9.62000  1.000 30.60977 ? 90  ALA A CB  1 
ATOM   575  N N   . LEU A 1 91  ? 25.96900 -16.42800 12.57500 1.000 26.71906 ? 91  LEU A N   1 
ATOM   576  C CA  . LEU A 1 91  ? 27.14400 -16.79000 13.35500 1.000 33.07436 ? 91  LEU A CA  1 
ATOM   577  C C   . LEU A 1 91  ? 27.89500 -17.84100 12.55900 1.000 31.07619 ? 91  LEU A C   1 
ATOM   578  O O   . LEU A 1 91  ? 27.28300 -18.79400 12.06500 1.000 30.59087 ? 91  LEU A O   1 
ATOM   579  C CB  . LEU A 1 91  ? 26.76800 -17.35400 14.72200 1.000 31.49310 ? 91  LEU A CB  1 
ATOM   580  C CG  . LEU A 1 91  ? 26.13700 -16.35700 15.68100 1.000 36.90673 ? 91  LEU A CG  1 
ATOM   581  C CD1 . LEU A 1 91  ? 25.53900 -17.09000 16.87200 1.000 38.74031 ? 91  LEU A CD1 1 
ATOM   582  C CD2 . LEU A 1 91  ? 27.19000 -15.35500 16.11700 1.000 40.54426 ? 91  LEU A CD2 1 
ATOM   583  N N   . TYR A 1 92  ? 29.20500 -17.67600 12.44000 1.000 28.33894 ? 92  TYR A N   1 
ATOM   584  C CA  . TYR A 1 92  ? 30.05000 -18.66200 11.79300 1.000 29.37500 ? 92  TYR A CA  1 
ATOM   585  C C   . TYR A 1 92  ? 31.19000 -18.99200 12.74300 1.000 31.86595 ? 92  TYR A C   1 
ATOM   586  O O   . TYR A 1 92  ? 31.86700 -18.08200 13.22400 1.000 31.47178 ? 92  TYR A O   1 
ATOM   587  C CB  . TYR A 1 92  ? 30.60200 -18.13300 10.45800 1.000 31.93106 ? 92  TYR A CB  1 
ATOM   588  C CG  . TYR A 1 92  ? 31.24100 -19.21000 9.64800  1.000 33.45779 ? 92  TYR A CG  1 
ATOM   589  C CD1 . TYR A 1 92  ? 32.56500 -19.62100 9.91200  1.000 30.80522 ? 92  TYR A CD1 1 
ATOM   590  C CD2 . TYR A 1 92  ? 30.52800 -19.87700 8.66200  1.000 31.13624 ? 92  TYR A CD2 1 
ATOM   591  C CE1 . TYR A 1 92  ? 33.14500 -20.63900 9.20600  1.000 33.88865 ? 92  TYR A CE1 1 
ATOM   592  C CE2 . TYR A 1 92  ? 31.10800 -20.91500 7.94700  1.000 35.73129 ? 92  TYR A CE2 1 
ATOM   593  C CZ  . TYR A 1 92  ? 32.42100 -21.28700 8.22000  1.000 35.45658 ? 92  TYR A CZ  1 
ATOM   594  O OH  . TYR A 1 92  ? 32.97900 -22.31100 7.49800  1.000 37.09542 ? 92  TYR A OH  1 
ATOM   595  N N   . ASP A 1 93  ? 31.39600 -20.28300 13.00800 1.000 30.39168 ? 93  ASP A N   1 
ATOM   596  C CA  . ASP A 1 93  ? 32.45800 -20.75000 13.90700 1.000 33.86209 ? 93  ASP A CA  1 
ATOM   597  C C   . ASP A 1 93  ? 33.68400 -21.04600 13.03800 1.000 36.49042 ? 93  ASP A C   1 
ATOM   598  O O   . ASP A 1 93  ? 33.72900 -22.06600 12.34000 1.000 34.17265 ? 93  ASP A O   1 
ATOM   599  C CB  . ASP A 1 93  ? 31.98400 -21.97900 14.68100 1.000 36.27276 ? 93  ASP A CB  1 
ATOM   600  C CG  . ASP A 1 93  ? 32.91200 -22.34400 15.83500 1.000 46.55871 ? 93  ASP A CG  1 
ATOM   601  O OD1 . ASP A 1 93  ? 33.94600 -21.68100 16.03100 1.000 49.54849 ? 93  ASP A OD1 1 
ATOM   602  O OD2 . ASP A 1 93  ? 32.60100 -23.28900 16.56800 1.000 52.12568 ? 93  ASP A OD2 1 
ATOM   603  N N   . ALA A 1 94  ? 34.66600 -20.14000 13.04700 1.000 32.16796 ? 94  ALA A N   1 
ATOM   604  C CA  . ALA A 1 94  ? 35.77200 -20.18400 12.09100 1.000 36.13347 ? 94  ALA A CA  1 
ATOM   605  C C   . ALA A 1 94  ? 37.06100 -20.68800 12.74100 1.000 36.06041 ? 94  ALA A C   1 
ATOM   606  O O   . ALA A 1 94  ? 37.43100 -20.24100 13.83200 1.000 37.45907 ? 94  ALA A O   1 
ATOM   607  C CB  . ALA A 1 94  ? 36.00800 -18.79300 11.49100 1.000 34.73604 ? 94  ALA A CB  1 
ATOM   608  N N   . THR A 1 95  ? 37.73800 -21.61200 12.07000 1.000 36.03212 ? 95  THR A N   1 
ATOM   609  C CA  . THR A 1 95  ? 39.07700 -22.04300 12.45300 1.000 36.53676 ? 95  THR A CA  1 
ATOM   610  C C   . THR A 1 95  ? 40.10200 -21.31100 11.59500 1.000 37.69636 ? 95  THR A C   1 
ATOM   611  O O   . THR A 1 95  ? 39.87500 -21.08900 10.39800 1.000 37.77159 ? 95  THR A O   1 
ATOM   612  C CB  . THR A 1 95  ? 39.22000 -23.55900 12.27900 1.000 40.43576 ? 95  THR A CB  1 
ATOM   613  O OG1 . THR A 1 95  ? 38.31500 -24.20900 13.18800 1.000 51.70632 ? 95  THR A OG1 1 
ATOM   614  C CG2 . THR A 1 95  ? 40.63100 -24.00500 12.57700 1.000 45.12283 ? 95  THR A CG2 1 
ATOM   615  N N   . TYR A 1 96  ? 41.21500 -20.91200 12.21300 1.000 39.36075 ? 96  TYR A N   1 
ATOM   616  C CA  . TYR A 1 96  ? 42.23900 -20.17800 11.49000 1.000 40.63986 ? 96  TYR A CA  1 
ATOM   617  C C   . TYR A 1 96  ? 43.57600 -20.32400 12.21400 1.000 43.36154 ? 96  TYR A C   1 
ATOM   618  O O   . TYR A 1 96  ? 43.63900 -20.70800 13.38900 1.000 41.48266 ? 96  TYR A O   1 
ATOM   619  C CB  . TYR A 1 96  ? 41.84300 -18.70500 11.32400 1.000 40.40950 ? 96  TYR A CB  1 
ATOM   620  C CG  . TYR A 1 96  ? 41.68800 -17.96400 12.63300 1.000 42.00026 ? 96  TYR A CG  1 
ATOM   621  C CD1 . TYR A 1 96  ? 40.55400 -18.13600 13.42600 1.000 40.73274 ? 96  TYR A CD1 1 
ATOM   622  C CD2 . TYR A 1 96  ? 42.68200 -17.09600 13.08000 1.000 49.64759 ? 96  TYR A CD2 1 
ATOM   623  C CE1 . TYR A 1 96  ? 40.42400 -17.45700 14.64400 1.000 47.12922 ? 96  TYR A CE1 1 
ATOM   624  C CE2 . TYR A 1 96  ? 42.56600 -16.41900 14.28300 1.000 49.08172 ? 96  TYR A CE2 1 
ATOM   625  C CZ  . TYR A 1 96  ? 41.42700 -16.59100 15.05900 1.000 49.06539 ? 96  TYR A CZ  1 
ATOM   626  O OH  . TYR A 1 96  ? 41.31600 -15.90800 16.27000 1.000 56.90384 ? 96  TYR A OH  1 
ATOM   627  N N   . GLU A 1 97  ? 44.65300 -20.04400 11.48600 1.000 42.36309 ? 97  GLU A N   1 
ATOM   628  C CA  . GLU A 1 97  ? 45.97800 -20.21900 12.06200 1.000 45.32252 ? 97  GLU A CA  1 
ATOM   629  C C   . GLU A 1 97  ? 46.88300 -19.04800 11.73000 1.000 52.06660 ? 97  GLU A C   1 
ATOM   630  O O   . GLU A 1 97  ? 46.84000 -18.50500 10.62100 1.000 47.99571 ? 97  GLU A O   1 
ATOM   631  C CB  . GLU A 1 97  ? 46.65400 -21.52500 11.57700 1.000 47.06778 ? 97  GLU A CB  1 
ATOM   632  C CG  . GLU A 1 97  ? 45.73600 -22.73300 11.77700 1.000 52.21034 ? 97  GLU A CG  1 
ATOM   633  C CD  . GLU A 1 97  ? 46.20300 -23.96500 11.06600 1.000 57.15991 ? 97  GLU A CD  1 
ATOM   634  O OE1 . GLU A 1 97  ? 47.26000 -23.91200 10.40600 1.000 55.04888 ? 97  GLU A OE1 1 
ATOM   635  O OE2 . GLU A 1 97  ? 45.49500 -24.99400 11.16300 1.000 62.12303 ? 97  GLU A OE2 1 
ATOM   636  N N   . THR A 1 98  ? 47.74300 -18.71600 12.69900 1.000 52.96625 ? 98  THR A N   1 
ATOM   637  C CA  . THR A 1 98  ? 48.89700 -17.85600 12.53200 1.000 56.53083 ? 98  THR A CA  1 
ATOM   638  C C   . THR A 1 98  ? 50.11200 -18.75400 12.36400 1.000 57.79557 ? 98  THR A C   1 
ATOM   639  O O   . THR A 1 98  ? 49.98900 -19.97900 12.28800 1.000 57.78323 ? 98  THR A O   1 
ATOM   640  C CB  . THR A 1 98  ? 49.04300 -16.92600 13.73700 1.000 57.34119 ? 98  THR A CB  1 
ATOM   641  O OG1 . THR A 1 98  ? 49.34900 -17.71000 14.90000 1.000 62.95739 ? 98  THR A OG1 1 
ATOM   642  C CG2 . THR A 1 98  ? 47.74900 -16.14500 13.96800 1.000 55.81085 ? 98  THR A CG2 1 
ATOM   643  N N   . LYS A 1 99  ? 51.31100 -18.16300 12.33300 1.000 60.04647 ? 99  LYS A N   1 
ATOM   644  C CA  . LYS A 1 99  ? 52.49100 -19.00700 12.26700 1.000 51.86121 ? 99  LYS A CA  1 
ATOM   645  C C   . LYS A 1 99  ? 52.66300 -19.83200 13.53300 1.000 54.86592 ? 99  LYS A C   1 
ATOM   646  O O   . LYS A 1 99  ? 53.27400 -20.89800 13.48100 1.000 57.00312 ? 99  LYS A O   1 
ATOM   647  C CB  . LYS A 1 99  ? 53.75400 -18.16600 12.01400 1.000 59.22067 ? 99  LYS A CB  1 
ATOM   648  N N   . GLU A 1 100 ? 52.13300 -19.37700 14.66400 1.000 55.50714 ? 100 GLU A N   1 
ATOM   649  C CA  . GLU A 1 100 ? 52.42600 -20.02000 15.93400 1.000 62.82701 ? 100 GLU A CA  1 
ATOM   650  C C   . GLU A 1 100 ? 51.22900 -20.66600 16.61300 1.000 58.23603 ? 100 GLU A C   1 
ATOM   651  O O   . GLU A 1 100 ? 51.42800 -21.39600 17.59500 1.000 61.35898 ? 100 GLU A O   1 
ATOM   652  C CB  . GLU A 1 100 ? 53.05700 -19.01000 16.91200 1.000 70.87148 ? 100 GLU A CB  1 
ATOM   653  N N   . SER A 1 101 ? 50.00700 -20.45200 16.12800 1.000 58.93337 ? 101 SER A N   1 
ATOM   654  C CA  . SER A 1 101 ? 48.86600 -20.96400 16.86500 1.000 58.27220 ? 101 SER A CA  1 
ATOM   655  C C   . SER A 1 101 ? 47.73500 -21.32200 15.91400 1.000 48.70015 ? 101 SER A C   1 
ATOM   656  O O   . SER A 1 101 ? 47.63600 -20.81100 14.79600 1.000 52.17820 ? 101 SER A O   1 
ATOM   657  C CB  . SER A 1 101 ? 48.38500 -19.95000 17.90900 1.000 58.24917 ? 101 SER A CB  1 
ATOM   658  O OG  . SER A 1 101 ? 47.76600 -18.85500 17.26400 1.000 63.92158 ? 101 SER A OG  1 
ATOM   659  N N   . LYS A 1 102 ? 46.88500 -22.21900 16.38300 1.000 49.53985 ? 102 LYS A N   1 
ATOM   660  C CA  . LYS A 1 102 ? 45.63600 -22.55500 15.72200 1.000 44.89769 ? 102 LYS A CA  1 
ATOM   661  C C   . LYS A 1 102 ? 44.51500 -22.09900 16.64000 1.000 46.47379 ? 102 LYS A C   1 
ATOM   662  O O   . LYS A 1 102 ? 44.56000 -22.35900 17.84800 1.000 48.30638 ? 102 LYS A O   1 
ATOM   663  C CB  . LYS A 1 102 ? 45.55000 -24.05800 15.44600 1.000 46.91847 ? 102 LYS A CB  1 
ATOM   664  C CG  . LYS A 1 102 ? 44.23500 -24.51300 14.79000 1.000 49.20588 ? 102 LYS A CG  1 
ATOM   665  C CD  . LYS A 1 102 ? 44.32200 -26.02500 14.43700 1.000 51.18972 ? 102 LYS A CD  1 
ATOM   666  C CE  . LYS A 1 102 ? 43.04400 -26.50200 13.70400 1.000 50.63613 ? 102 LYS A CE  1 
ATOM   667  N NZ  . LYS A 1 102 ? 43.18600 -27.93900 13.27300 1.000 52.44584 ? 102 LYS A NZ  1 
ATOM   668  N N   . LYS A 1 103 ? 43.52700 -21.40900 16.07900 1.000 41.68993 ? 103 LYS A N   1 
ATOM   669  C CA  . LYS A 1 103 ? 42.49700 -20.76700 16.87600 1.000 45.48256 ? 103 LYS A CA  1 
ATOM   670  C C   . LYS A 1 103 ? 41.13200 -21.06200 16.27700 1.000 47.38950 ? 103 LYS A C   1 
ATOM   671  O O   . LYS A 1 103 ? 40.99900 -21.41000 15.09800 1.000 42.30248 ? 103 LYS A O   1 
ATOM   672  C CB  . LYS A 1 103 ? 42.70600 -19.24800 16.95200 1.000 48.08858 ? 103 LYS A CB  1 
ATOM   673  C CG  . LYS A 1 103 ? 44.02400 -18.80400 17.58700 1.000 55.91516 ? 103 LYS A CG  1 
ATOM   674  C CD  . LYS A 1 103 ? 44.11700 -17.27600 17.55900 1.000 56.70696 ? 103 LYS A CD  1 
ATOM   675  C CE  . LYS A 1 103 ? 45.33700 -16.75600 18.30700 1.000 65.91743 ? 103 LYS A CE  1 
ATOM   676  N NZ  . LYS A 1 103 ? 45.23200 -15.27100 18.42400 1.000 75.43871 ? 103 LYS A NZ  1 
ATOM   677  N N   . GLU A 1 104 ? 40.10900 -20.89900 17.10900 1.000 47.09484 ? 104 GLU A N   1 
ATOM   678  C CA  . GLU A 1 104 ? 38.73800 -21.02500 16.65500 1.000 49.38538 ? 104 GLU A CA  1 
ATOM   679  C C   . GLU A 1 104 ? 37.93200 -19.92700 17.32900 1.000 48.64863 ? 104 GLU A C   1 
ATOM   680  O O   . GLU A 1 104 ? 38.05900 -19.71200 18.53900 1.000 49.08279 ? 104 GLU A O   1 
ATOM   681  C CB  . GLU A 1 104 ? 38.15900 -22.41000 16.97100 1.000 51.47284 ? 104 GLU A CB  1 
ATOM   682  C CG  . GLU A 1 104 ? 36.96700 -22.72900 16.10900 1.000 57.99427 ? 104 GLU A CG  1 
ATOM   683  C CD  . GLU A 1 104 ? 36.15700 -23.91100 16.60400 1.000 71.26476 ? 104 GLU A CD  1 
ATOM   684  O OE1 . GLU A 1 104 ? 36.11800 -24.13700 17.83500 1.000 70.31816 ? 104 GLU A OE1 1 
ATOM   685  O OE2 . GLU A 1 104 ? 35.55800 -24.60800 15.74900 1.000 77.32524 ? 104 GLU A OE2 1 
ATOM   686  N N   . ASP A 1 105 ? 37.16600 -19.18600 16.54300 1.000 38.57490 ? 105 ASP A N   1 
ATOM   687  C CA  . ASP A 1 105 ? 36.40200 -18.08500 17.11000 1.000 40.07689 ? 105 ASP A CA  1 
ATOM   688  C C   . ASP A 1 105 ? 35.09400 -17.94300 16.36600 1.000 41.05996 ? 105 ASP A C   1 
ATOM   689  O O   . ASP A 1 105 ? 35.02900 -18.17500 15.16000 1.000 34.45371 ? 105 ASP A O   1 
ATOM   690  C CB  . ASP A 1 105 ? 37.15000 -16.75500 17.02900 1.000 43.68473 ? 105 ASP A CB  1 
ATOM   691  C CG  . ASP A 1 105 ? 38.07200 -16.53100 18.20800 1.000 56.65639 ? 105 ASP A CG  1 
ATOM   692  O OD1 . ASP A 1 105 ? 37.57400 -16.41100 19.35000 1.000 60.97454 ? 105 ASP A OD1 1 
ATOM   693  O OD2 . ASP A 1 105 ? 39.29200 -16.48000 17.99400 1.000 51.94195 ? 105 ASP A OD2 1 
ATOM   694  N N   . LEU A 1 106 ? 34.07000 -17.50700 17.09500 1.000 39.21676 ? 106 LEU A N   1 
ATOM   695  C CA  . LEU A 1 106 ? 32.80500 -17.14500 16.49000 1.000 36.89062 ? 106 LEU A CA  1 
ATOM   696  C C   . LEU A 1 106 ? 32.91500 -15.78800 15.81700 1.000 38.84576 ? 106 LEU A C   1 
ATOM   697  O O   . LEU A 1 106 ? 33.52400 -14.85300 16.35000 1.000 39.34744 ? 106 LEU A O   1 
ATOM   698  C CB  . LEU A 1 106 ? 31.69300 -17.08200 17.53600 1.000 37.65704 ? 106 LEU A CB  1 
ATOM   699  C CG  . LEU A 1 106 ? 31.19000 -18.37200 18.16200 1.000 46.51334 ? 106 LEU A CG  1 
ATOM   700  C CD1 . LEU A 1 106 ? 29.91700 -18.03700 18.95400 1.000 51.50557 ? 106 LEU A CD1 1 
ATOM   701  C CD2 . LEU A 1 106 ? 30.91900 -19.43000 17.09100 1.000 42.21214 ? 106 LEU A CD2 1 
ATOM   702  N N   . VAL A 1 107 ? 32.31000 -15.68200 14.64800 1.000 34.21962 ? 107 VAL A N   1 
ATOM   703  C CA  . VAL A 1 107 ? 32.21800 -14.42300 13.92600 1.000 36.97983 ? 107 VAL A CA  1 
ATOM   704  C C   . VAL A 1 107 ? 30.75100 -14.10400 13.72800 1.000 34.80905 ? 107 VAL A C   1 
ATOM   705  O O   . VAL A 1 107 ? 30.00400 -14.93500 13.20200 1.000 32.21539 ? 107 VAL A O   1 
ATOM   706  C CB  . VAL A 1 107 ? 32.93100 -14.49300 12.56400 1.000 37.29973 ? 107 VAL A CB  1 
ATOM   707  C CG1 . VAL A 1 107 ? 32.96200 -13.10500 11.96000 1.000 34.51631 ? 107 VAL A CG1 1 
ATOM   708  C CG2 . VAL A 1 107 ? 34.31600 -15.02800 12.74900 1.000 44.77985 ? 107 VAL A CG2 1 
ATOM   709  N N   . PHE A 1 108 ? 30.35000 -12.90400 14.13600 1.000 32.21617 ? 108 PHE A N   1 
ATOM   710  C CA  . PHE A 1 108 ? 29.01400 -12.37700 13.86500 1.000 32.90972 ? 108 PHE A CA  1 
ATOM   711  C C   . PHE A 1 108 ? 29.04900 -11.67900 12.51400 1.000 30.78185 ? 108 PHE A C   1 
ATOM   712  O O   . PHE A 1 108 ? 29.89200 -10.81500 12.27800 1.000 33.27407 ? 108 PHE A O   1 
ATOM   713  C CB  . PHE A 1 108 ? 28.58300 -11.39700 14.96200 1.000 34.01318 ? 108 PHE A CB  1 
ATOM   714  C CG  . PHE A 1 108 ? 27.22100 -10.78800 14.74000 1.000 34.88627 ? 108 PHE A CG  1 
ATOM   715  C CD1 . PHE A 1 108 ? 26.08000 -11.51400 14.97100 1.000 33.74729 ? 108 PHE A CD1 1 
ATOM   716  C CD2 . PHE A 1 108 ? 27.09000 -9.47400  14.31800 1.000 40.90196 ? 108 PHE A CD2 1 
ATOM   717  C CE1 . PHE A 1 108 ? 24.80700 -10.94700 14.78200 1.000 38.63840 ? 108 PHE A CE1 1 
ATOM   718  C CE2 . PHE A 1 108 ? 25.80500 -8.90700  14.11200 1.000 44.69144 ? 108 PHE A CE2 1 
ATOM   719  C CZ  . PHE A 1 108 ? 24.68000 -9.65600  14.35200 1.000 39.49024 ? 108 PHE A CZ  1 
ATOM   720  N N   . ILE A 1 109 ? 28.16100 -12.07500 11.61800 1.000 33.41229 ? 109 ILE A N   1 
ATOM   721  C CA  . ILE A 1 109 ? 28.14900 -11.55000 10.26000 1.000 30.76540 ? 109 ILE A CA  1 
ATOM   722  C C   . ILE A 1 109 ? 26.85600 -10.78200 10.03500 1.000 31.27244 ? 109 ILE A C   1 
ATOM   723  O O   . ILE A 1 109 ? 25.77200 -11.26500 10.37900 1.000 31.49585 ? 109 ILE A O   1 
ATOM   724  C CB  . ILE A 1 109 ? 28.31200 -12.68600 9.24700  1.000 32.01006 ? 109 ILE A CB  1 
ATOM   725  C CG1 . ILE A 1 109 ? 29.69600 -13.32300 9.47000  1.000 33.72892 ? 109 ILE A CG1 1 
ATOM   726  C CG2 . ILE A 1 109 ? 28.16000 -12.17400 7.79900  1.000 33.09049 ? 109 ILE A CG2 1 
ATOM   727  C CD1 . ILE A 1 109 ? 29.94100 -14.47800 8.59500  1.000 36.18297 ? 109 ILE A CD1 1 
ATOM   728  N N   . PHE A 1 110 ? 26.97400 -9.58600  9.46800  1.000 29.12784 ? 110 PHE A N   1 
ATOM   729  C CA  . PHE A 1 110 ? 25.81600 -8.83900  8.99400  1.000 31.62253 ? 110 PHE A CA  1 
ATOM   730  C C   . PHE A 1 110 ? 25.91700 -8.77400  7.48000  1.000 29.70846 ? 110 PHE A C   1 
ATOM   731  O O   . PHE A 1 110 ? 26.87500 -8.19900  6.94800  1.000 30.20549 ? 110 PHE A O   1 
ATOM   732  C CB  . PHE A 1 110 ? 25.77600 -7.43400  9.59600  1.000 28.03619 ? 110 PHE A CB  1 
ATOM   733  C CG  . PHE A 1 110 ? 24.62700 -6.56100  9.09400  1.000 29.69625 ? 110 PHE A CG  1 
ATOM   734  C CD1 . PHE A 1 110 ? 23.37800 -7.11500  8.76300  1.000 31.01153 ? 110 PHE A CD1 1 
ATOM   735  C CD2 . PHE A 1 110 ? 24.80500 -5.18700  8.96900  1.000 31.96094 ? 110 PHE A CD2 1 
ATOM   736  C CE1 . PHE A 1 110 ? 22.32700 -6.27400  8.30800  1.000 29.01826 ? 110 PHE A CE1 1 
ATOM   737  C CE2 . PHE A 1 110 ? 23.76400 -4.33200  8.53700  1.000 33.30260 ? 110 PHE A CE2 1 
ATOM   738  C CZ  . PHE A 1 110 ? 22.52400 -4.87400  8.21500  1.000 32.16071 ? 110 PHE A CZ  1 
ATOM   739  N N   . TRP A 1 111 ? 24.93800 -9.37300  6.81000  1.000 27.69124 ? 111 TRP A N   1 
ATOM   740  C CA  . TRP A 1 111 ? 24.85400 -9.45500  5.35500  1.000 28.04759 ? 111 TRP A CA  1 
ATOM   741  C C   . TRP A 1 111 ? 23.79800 -8.45400  4.89500  1.000 29.90669 ? 111 TRP A C   1 
ATOM   742  O O   . TRP A 1 111 ? 22.62500 -8.58600  5.25400  1.000 29.21402 ? 111 TRP A O   1 
ATOM   743  C CB  . TRP A 1 111 ? 24.48600 -10.88900 4.95400  1.000 27.67564 ? 111 TRP A CB  1 
ATOM   744  C CG  . TRP A 1 111 ? 24.05800 -11.09100 3.51800  1.000 26.51048 ? 111 TRP A CG  1 
ATOM   745  C CD1 . TRP A 1 111 ? 22.81100 -11.44400 3.07000  1.000 27.97516 ? 111 TRP A CD1 1 
ATOM   746  C CD2 . TRP A 1 111 ? 24.88100 -10.97400 2.36000  1.000 28.15043 ? 111 TRP A CD2 1 
ATOM   747  N NE1 . TRP A 1 111 ? 22.81200 -11.55200 1.70200  1.000 28.12877 ? 111 TRP A NE1 1 
ATOM   748  C CE2 . TRP A 1 111 ? 24.06700 -11.26200 1.23800  1.000 28.35068 ? 111 TRP A CE2 1 
ATOM   749  C CE3 . TRP A 1 111 ? 26.22900 -10.62600 2.15300  1.000 31.50498 ? 111 TRP A CE3 1 
ATOM   750  C CZ2 . TRP A 1 111 ? 24.55900 -11.23900 -0.07700 1.000 32.63795 ? 111 TRP A CZ2 1 
ATOM   751  C CZ3 . TRP A 1 111 ? 26.71800 -10.61000 0.84400  1.000 35.15019 ? 111 TRP A CZ3 1 
ATOM   752  C CH2 . TRP A 1 111 ? 25.88700 -10.91300 -0.24700 1.000 34.01906 ? 111 TRP A CH2 1 
ATOM   753  N N   . ALA A 1 112 ? 24.21400 -7.43900  4.13400  1.000 29.42260 ? 112 ALA A N   1 
ATOM   754  C CA  . ALA A 1 112 ? 23.32200 -6.35200  3.71000  1.000 29.30561 ? 112 ALA A CA  1 
ATOM   755  C C   . ALA A 1 112 ? 23.57700 -5.99400  2.24700  1.000 28.93971 ? 112 ALA A C   1 
ATOM   756  O O   . ALA A 1 112 ? 24.16900 -4.96000  1.93100  1.000 30.57592 ? 112 ALA A O   1 
ATOM   757  C CB  . ALA A 1 112 ? 23.49800 -5.12400  4.60400  1.000 32.16357 ? 112 ALA A CB  1 
ATOM   758  N N   . PRO A 1 113 ? 23.13300 -6.84600  1.33200  1.000 30.94830 ? 113 PRO A N   1 
ATOM   759  C CA  . PRO A 1 113 ? 23.40400 -6.59500  -0.09400 1.000 33.57686 ? 113 PRO A CA  1 
ATOM   760  C C   . PRO A 1 113 ? 22.65300 -5.36500  -0.60600 1.000 34.62859 ? 113 PRO A C   1 
ATOM   761  O O   . PRO A 1 113 ? 21.58100 -5.00200  -0.11000 1.000 32.99977 ? 113 PRO A O   1 
ATOM   762  C CB  . PRO A 1 113 ? 22.92500 -7.87700  -0.77700 1.000 34.24693 ? 113 PRO A CB  1 
ATOM   763  C CG  . PRO A 1 113 ? 21.88200 -8.47000  0.18600  1.000 34.19151 ? 113 PRO A CG  1 
ATOM   764  C CD  . PRO A 1 113 ? 22.36700 -8.08200  1.57500  1.000 28.25003 ? 113 PRO A CD  1 
ATOM   765  N N   . GLU A 1 114 ? 23.25400 -4.69400  -1.59600 1.000 34.09198 ? 114 GLU A N   1 
ATOM   766  C CA  . GLU A 1 114 ? 22.67600 -3.44200  -2.08100 1.000 35.38056 ? 114 GLU A CA  1 
ATOM   767  C C   . GLU A 1 114 ? 21.25800 -3.61500  -2.62300 1.000 35.93243 ? 114 GLU A C   1 
ATOM   768  O O   . GLU A 1 114 ? 20.43900 -2.69400  -2.51000 1.000 38.97073 ? 114 GLU A O   1 
ATOM   769  C CB  . GLU A 1 114 ? 23.56200 -2.81400  -3.16200 1.000 38.88269 ? 114 GLU A CB  1 
ATOM   770  C CG  . GLU A 1 114 ? 24.90200 -2.30400  -2.65500 1.000 38.94576 ? 114 GLU A CG  1 
ATOM   771  C CD  . GLU A 1 114 ? 24.76100 -1.28800  -1.51500 1.000 39.17977 ? 114 GLU A CD  1 
ATOM   772  O OE1 . GLU A 1 114 ? 23.76100 -0.52500  -1.49800 1.000 35.37809 ? 114 GLU A OE1 1 
ATOM   773  O OE2 . GLU A 1 114 ? 25.66700 -1.26100  -0.65000 1.000 39.94123 ? 114 GLU A OE2 1 
ATOM   774  N N   . SER A 1 115 ? 20.93200 -4.76100  -3.21000 1.000 35.65617 ? 115 SER A N   1 
ATOM   775  C CA  . SER A 1 115 ? 19.61400 -4.87600  -3.82600 1.000 39.44324 ? 115 SER A CA  1 
ATOM   776  C C   . SER A 1 115 ? 18.52500 -5.31300  -2.84700 1.000 41.87676 ? 115 SER A C   1 
ATOM   777  O O   . SER A 1 115 ? 17.36200 -5.42900  -3.25400 1.000 41.99118 ? 115 SER A O   1 
ATOM   778  C CB  . SER A 1 115 ? 19.67100 -5.82600  -5.02700 1.000 43.79046 ? 115 SER A CB  1 
ATOM   779  O OG  . SER A 1 115 ? 20.34800 -7.00500  -4.66900 1.000 49.82874 ? 115 SER A OG  1 
ATOM   780  N N   . ALA A 1 116 ? 18.86100 -5.55000  -1.58100 1.000 35.52126 ? 116 ALA A N   1 
ATOM   781  C CA  . ALA A 1 116 ? 17.84000 -5.81100  -0.57600 1.000 34.30321 ? 116 ALA A CA  1 
ATOM   782  C C   . ALA A 1 116 ? 16.95600 -4.58300  -0.40200 1.000 38.96509 ? 116 ALA A C   1 
ATOM   783  O O   . ALA A 1 116 ? 17.45100 -3.44400  -0.46800 1.000 37.98581 ? 116 ALA A O   1 
ATOM   784  C CB  . ALA A 1 116 ? 18.47800 -6.18700  0.76900  1.000 34.41164 ? 116 ALA A CB  1 
ATOM   785  N N   . PRO A 1 117 ? 15.66500 -4.76400  -0.13000 1.000 36.03057 ? 117 PRO A N   1 
ATOM   786  C CA  . PRO A 1 117 ? 14.76400 -3.60800  0.02200  1.000 40.44390 ? 117 PRO A CA  1 
ATOM   787  C C   . PRO A 1 117 ? 15.15500 -2.73500  1.20700  1.000 36.61249 ? 117 PRO A C   1 
ATOM   788  O O   . PRO A 1 117 ? 15.50000 -3.23000  2.28500  1.000 35.23445 ? 117 PRO A O   1 
ATOM   789  C CB  . PRO A 1 117 ? 13.38600 -4.24900  0.23400  1.000 42.59137 ? 117 PRO A CB  1 
ATOM   790  C CG  . PRO A 1 117 ? 13.53800 -5.70500  -0.21200 1.000 43.66884 ? 117 PRO A CG  1 
ATOM   791  C CD  . PRO A 1 117 ? 14.97100 -6.07200  -0.02400 1.000 37.99528 ? 117 PRO A CD  1 
ATOM   792  N N   . LEU A 1 118 ? 15.08200 -1.42000  0.99300  1.000 38.68392 ? 118 LEU A N   1 
ATOM   793  C CA  . LEU A 1 118 ? 15.58900 -0.46800  1.97800  1.000 38.82613 ? 118 LEU A CA  1 
ATOM   794  C C   . LEU A 1 118 ? 14.85100 -0.57800  3.30500  1.000 38.93182 ? 118 LEU A C   1 
ATOM   795  O O   . LEU A 1 118 ? 15.46100 -0.47500  4.37300  1.000 36.68200 ? 118 LEU A O   1 
ATOM   796  C CB  . LEU A 1 118 ? 15.46700 0.95300   1.43000  1.000 39.32105 ? 118 LEU A CB  1 
ATOM   797  C CG  . LEU A 1 118 ? 16.08300 2.04400   2.31300  1.000 33.76362 ? 118 LEU A CG  1 
ATOM   798  C CD1 . LEU A 1 118 ? 17.57100 1.85400   2.53700  1.000 35.78377 ? 118 LEU A CD1 1 
ATOM   799  C CD2 . LEU A 1 118 ? 15.79600 3.41300   1.69300  1.000 35.90827 ? 118 LEU A CD2 1 
ATOM   800  N N   . LYS A 1 119 ? 13.53900 -0.78800  3.25900  1.000 38.99678 ? 119 LYS A N   1 
ATOM   801  C CA  . LYS A 1 119 ? 12.72800 -0.73700  4.46900  1.000 42.32656 ? 119 LYS A CA  1 
ATOM   802  C C   . LYS A 1 119 ? 13.15800 -1.79900  5.48300  1.000 42.18838 ? 119 LYS A C   1 
ATOM   803  O O   . LYS A 1 119 ? 13.41300 -1.49600  6.65700  1.000 44.22442 ? 119 LYS A O   1 
ATOM   804  C CB  . LYS A 1 119 ? 11.26100 -0.91200  4.09200  1.000 48.27660 ? 119 LYS A CB  1 
ATOM   805  C CG  . LYS A 1 119 ? 10.34000 -0.96200  5.27000  1.000 62.33174 ? 119 LYS A CG  1 
ATOM   806  C CD  . LYS A 1 119 ? 9.97100  0.43400   5.73100  1.000 61.59231 ? 119 LYS A CD  1 
ATOM   807  C CE  . LYS A 1 119 ? 8.76600  0.37100   6.65400  1.000 68.66180 ? 119 LYS A CE  1 
ATOM   808  N NZ  . LYS A 1 119 ? 8.94200  -0.75700  7.62100  1.000 71.63340 ? 119 LYS A NZ  1 
ATOM   809  N N   . SER A 1 120 ? 13.25100 -3.04900  5.05200  1.000 37.50726 ? 120 SER A N   1 
ATOM   810  C CA  . SER A 1 120 ? 13.64300 -4.07700  6.00100  1.000 39.50489 ? 120 SER A CA  1 
ATOM   811  C C   . SER A 1 120 ? 15.15000 -4.04800  6.25000  1.000 37.20777 ? 120 SER A C   1 
ATOM   812  O O   . SER A 1 120 ? 15.59500 -4.36500  7.35700  1.000 36.96864 ? 120 SER A O   1 
ATOM   813  C CB  . SER A 1 120 ? 13.18100 -5.45200  5.51100  1.000 47.58709 ? 120 SER A CB  1 
ATOM   814  O OG  . SER A 1 120 ? 13.71700 -5.71800  4.22200  1.000 53.00076 ? 120 SER A OG  1 
ATOM   815  N N   . LYS A 1 121 ? 15.93400 -3.61800  5.26500  1.000 35.32586 ? 121 LYS A N   1 
ATOM   816  C CA  . LYS A 1 121 ? 17.36500 -3.42700  5.49500  1.000 36.34535 ? 121 LYS A CA  1 
ATOM   817  C C   . LYS A 1 121 ? 17.62100 -2.45500  6.64500  1.000 37.51370 ? 121 LYS A C   1 
ATOM   818  O O   . LYS A 1 121 ? 18.51100 -2.68000  7.47000  1.000 34.86228 ? 121 LYS A O   1 
ATOM   819  C CB  . LYS A 1 121 ? 18.04600 -2.93300  4.22600  1.000 34.05006 ? 121 LYS A CB  1 
ATOM   820  C CG  . LYS A 1 121 ? 19.50800 -2.52200  4.43500  1.000 33.29816 ? 121 LYS A CG  1 
ATOM   821  C CD  . LYS A 1 121 ? 20.04400 -1.85400  3.17200  1.000 40.43319 ? 121 LYS A CD  1 
ATOM   822  C CE  . LYS A 1 121 ? 20.30600 -2.87700  2.08100  1.000 39.32025 ? 121 LYS A CE  1 
ATOM   823  N NZ  . LYS A 1 121 ? 20.89400 -2.20400  0.86300  1.000 38.66038 ? 121 LYS A NZ  1 
ATOM   824  N N   . MET A 1 122 ? 16.84700 -1.37300  6.72500  1.000 31.64937 ? 122 MET A N   1 
ATOM   825  C CA  . MET A 1 122 ? 17.05700 -0.45200  7.83400  1.000 32.19566 ? 122 MET A CA  1 
ATOM   826  C C   . MET A 1 122 ? 16.59500 -1.05500  9.15600  1.000 34.13505 ? 122 MET A C   1 
ATOM   827  O O   . MET A 1 122 ? 17.09300 -0.66900  10.22000 1.000 34.46743 ? 122 MET A O   1 
ATOM   828  C CB  . MET A 1 122 ? 16.37900 0.88600   7.52800  1.000 30.28337 ? 122 MET A CB  1 
ATOM   829  C CG  . MET A 1 122 ? 17.07300 1.63700   6.35500  1.000 34.54903 ? 122 MET A CG  1 
ATOM   830  S SD  . MET A 1 122 ? 18.90200 1.62700   6.41300  1.000 33.53486 ? 122 MET A SD  1 
ATOM   831  C CE  . MET A 1 122 ? 19.15600 2.52700   7.96400  1.000 31.31587 ? 122 MET A CE  1 
ATOM   832  N N   . ILE A 1 123 ? 15.64500 -1.99100  9.13100  1.000 33.65446 ? 123 ILE A N   1 
ATOM   833  C CA  . ILE A 1 123 ? 15.31400 -2.68200  10.37100 1.000 36.73065 ? 123 ILE A CA  1 
ATOM   834  C C   . ILE A 1 123 ? 16.48600 -3.55900  10.79800 1.000 36.03465 ? 123 ILE A C   1 
ATOM   835  O O   . ILE A 1 123 ? 16.88500 -3.56600  11.96900 1.000 36.09887 ? 123 ILE A O   1 
ATOM   836  C CB  . ILE A 1 123 ? 14.02000 -3.50600  10.22100 1.000 41.65410 ? 123 ILE A CB  1 
ATOM   837  C CG1 . ILE A 1 123 ? 12.84900 -2.61500  9.81200  1.000 45.09112 ? 123 ILE A CG1 1 
ATOM   838  C CG2 . ILE A 1 123 ? 13.70100 -4.26000  11.53400 1.000 45.52115 ? 123 ILE A CG2 1 
ATOM   839  C CD1 . ILE A 1 123 ? 11.57200 -3.40600  9.50100  1.000 48.03644 ? 123 ILE A CD1 1 
ATOM   840  N N   . TYR A 1 124 ? 17.08400 -4.27700  9.84500  1.000 32.60598 ? 124 TYR A N   1 
ATOM   841  C CA  . TYR A 1 124 ? 18.25400 -5.08700  10.17300 1.000 33.60488 ? 124 TYR A CA  1 
ATOM   842  C C   . TYR A 1 124 ? 19.39300 -4.20700  10.67000 1.000 35.18779 ? 124 TYR A C   1 
ATOM   843  O O   . TYR A 1 124 ? 20.05600 -4.52900  11.66300 1.000 33.81348 ? 124 TYR A O   1 
ATOM   844  C CB  . TYR A 1 124 ? 18.72200 -5.90200  8.95400  1.000 32.81836 ? 124 TYR A CB  1 
ATOM   845  C CG  . TYR A 1 124 ? 17.98500 -7.19700  8.69100  1.000 34.71471 ? 124 TYR A CG  1 
ATOM   846  C CD1 . TYR A 1 124 ? 18.37900 -8.39300  9.30000  1.000 32.94612 ? 124 TYR A CD1 1 
ATOM   847  C CD2 . TYR A 1 124 ? 16.91600 -7.24000  7.80300  1.000 33.46524 ? 124 TYR A CD2 1 
ATOM   848  C CE1 . TYR A 1 124 ? 17.70200 -9.58800  9.04600  1.000 34.23229 ? 124 TYR A CE1 1 
ATOM   849  C CE2 . TYR A 1 124 ? 16.23900 -8.42300  7.54900  1.000 34.02393 ? 124 TYR A CE2 1 
ATOM   850  C CZ  . TYR A 1 124 ? 16.62500 -9.58900  8.17300  1.000 34.26307 ? 124 TYR A CZ  1 
ATOM   851  O OH  . TYR A 1 124 ? 15.96800 -10.76700 7.89700  1.000 36.26047 ? 124 TYR A OH  1 
ATOM   852  N N   . ALA A 1 125 ? 19.65000 -3.09400  9.97700  1.000 32.92473 ? 125 ALA A N   1 
ATOM   853  C CA  . ALA A 1 125 ? 20.78800 -2.25200  10.33500 1.000 35.11051 ? 125 ALA A CA  1 
ATOM   854  C C   . ALA A 1 125 ? 20.61500 -1.65800  11.72600 1.000 38.12542 ? 125 ALA A C   1 
ATOM   855  O O   . ALA A 1 125 ? 21.57800 -1.58800  12.50600 1.000 37.90735 ? 125 ALA A O   1 
ATOM   856  C CB  . ALA A 1 125 ? 20.96700 -1.12700  9.31200  1.000 35.71505 ? 125 ALA A CB  1 
ATOM   857  N N   . SER A 1 126 ? 19.40100 -1.18000  12.04000 1.000 35.04201 ? 126 SER A N   1 
ATOM   858  C CA  . SER A 1 126 ? 19.16100 -0.50800  13.30400 1.000 35.02006 ? 126 SER A CA  1 
ATOM   859  C C   . SER A 1 126 ? 18.98600 -1.48400  14.45000 1.000 40.57329 ? 126 SER A C   1 
ATOM   860  O O   . SER A 1 126 ? 19.06300 -1.06900  15.61100 1.000 45.18897 ? 126 SER A O   1 
ATOM   861  C CB  . SER A 1 126 ? 17.92900 0.41700   13.21200 1.000 40.81931 ? 126 SER A CB  1 
ATOM   862  O OG  . SER A 1 126 ? 16.75100 -0.32100  12.92600 1.000 42.99150 ? 126 SER A OG  1 
ATOM   863  N N   . SER A 1 127 ? 18.76600 -2.76300  14.15800 1.000 39.01500 ? 127 SER A N   1 
ATOM   864  C CA  . SER A 1 127 ? 18.60400 -3.77900  15.18500 1.000 42.55002 ? 127 SER A CA  1 
ATOM   865  C C   . SER A 1 127 ? 19.88400 -4.54300  15.45700 1.000 44.81074 ? 127 SER A C   1 
ATOM   866  O O   . SER A 1 127 ? 19.90800 -5.38100  16.36400 1.000 45.54618 ? 127 SER A O   1 
ATOM   867  C CB  . SER A 1 127 ? 17.51300 -4.77000  14.78100 1.000 42.15562 ? 127 SER A CB  1 
ATOM   868  O OG  . SER A 1 127 ? 16.27300 -4.11400  14.60800 1.000 43.96159 ? 127 SER A OG  1 
ATOM   869  N N   . LYS A 1 128 ? 20.93400 -4.30600  14.67300 1.000 39.97610 ? 128 LYS A N   1 
ATOM   870  C CA  . LYS A 1 128 ? 22.12700 -5.13400  14.80400 1.000 45.12128 ? 128 LYS A CA  1 
ATOM   871  C C   . LYS A 1 128 ? 22.75200 -4.98300  16.18900 1.000 45.52295 ? 128 LYS A C   1 
ATOM   872  O O   . LYS A 1 128 ? 23.22500 -5.96100  16.77200 1.000 43.40289 ? 128 LYS A O   1 
ATOM   873  C CB  . LYS A 1 128 ? 23.13700 -4.77700  13.72000 1.000 42.66296 ? 128 LYS A CB  1 
ATOM   874  C CG  . LYS A 1 128 ? 24.37000 -5.65500  13.75700 1.000 44.07819 ? 128 LYS A CG  1 
ATOM   875  C CD  . LYS A 1 128 ? 25.36900 -5.27200  12.69500 1.000 45.47851 ? 128 LYS A CD  1 
ATOM   876  C CE  . LYS A 1 128 ? 26.04100 -3.94300  12.99300 1.000 50.69523 ? 128 LYS A CE  1 
ATOM   877  N NZ  . LYS A 1 128 ? 26.86500 -3.95700  14.23100 1.000 56.12832 ? 128 LYS A NZ  1 
ATOM   878  N N   . ASP A 1 129 ? 22.77700 -3.75800  16.71800 1.000 47.07485 ? 129 ASP A N   1 
ATOM   879  C CA  . ASP A 1 129 ? 23.36100 -3.51700  18.03600 1.000 48.60344 ? 129 ASP A CA  1 
ATOM   880  C C   . ASP A 1 129 ? 22.63800 -4.31000  19.11800 1.000 51.59746 ? 129 ASP A C   1 
ATOM   881  O O   . ASP A 1 129 ? 23.26800 -4.81300  20.05800 1.000 54.36413 ? 129 ASP A O   1 
ATOM   882  C CB  . ASP A 1 129 ? 23.31000 -2.02600  18.37200 1.000 50.18472 ? 129 ASP A CB  1 
ATOM   883  C CG  . ASP A 1 129 ? 24.39100 -1.20900  17.66600 1.000 55.69946 ? 129 ASP A CG  1 
ATOM   884  O OD1 . ASP A 1 129 ? 25.33900 -1.79800  17.09300 1.000 56.56388 ? 129 ASP A OD1 1 
ATOM   885  O OD2 . ASP A 1 129 ? 24.28800 0.04100   17.70300 1.000 59.06686 ? 129 ASP A OD2 1 
ATOM   886  N N   . ALA A 1 130 ? 21.31300 -4.42900  19.00100 1.000 51.87830 ? 130 ALA A N   1 
ATOM   887  C CA  . ALA A 1 130 ? 20.53600 -5.11400  20.03000 1.000 57.16159 ? 130 ALA A CA  1 
ATOM   888  C C   . ALA A 1 130 ? 20.79700 -6.61100  20.01300 1.000 52.21268 ? 130 ALA A C   1 
ATOM   889  O O   . ALA A 1 130 ? 20.90100 -7.23500  21.07600 1.000 51.94704 ? 130 ALA A O   1 
ATOM   890  C CB  . ALA A 1 130 ? 19.04100 -4.83700  19.85400 1.000 56.66872 ? 130 ALA A CB  1 
ATOM   891  N N   . ILE A 1 131 ? 20.90900 -7.21200  18.82400 1.000 48.98242 ? 131 ILE A N   1 
ATOM   892  C CA  . ILE A 1 131 ? 21.17900 -8.64300  18.79800 1.000 51.34518 ? 131 ILE A CA  1 
ATOM   893  C C   . ILE A 1 131 ? 22.61100 -8.91100  19.24500 1.000 53.80433 ? 131 ILE A C   1 
ATOM   894  O O   . ILE A 1 131 ? 22.87400 -9.85500  20.00100 1.000 51.67470 ? 131 ILE A O   1 
ATOM   895  C CB  . ILE A 1 131 ? 20.86900 -9.27400  17.42500 1.000 47.39358 ? 131 ILE A CB  1 
ATOM   896  C CG1 . ILE A 1 131 ? 21.36800 -10.72700 17.42300 1.000 48.32191 ? 131 ILE A CG1 1 
ATOM   897  C CG2 . ILE A 1 131 ? 21.45400 -8.47400  16.26500 1.000 47.29078 ? 131 ILE A CG2 1 
ATOM   898  C CD1 . ILE A 1 131 ? 20.95500 -11.59500 16.20200 1.000 50.79545 ? 131 ILE A CD1 1 
ATOM   899  N N   . LYS A 1 132 ? 23.55000 -8.05800  18.84000 1.000 47.86089 ? 132 LYS A N   1 
ATOM   900  C CA  . LYS A 1 132 ? 24.92900 -8.28000  19.25500 1.000 53.28894 ? 132 LYS A CA  1 
ATOM   901  C C   . LYS A 1 132 ? 25.08400 -8.18900  20.76400 1.000 57.50172 ? 132 LYS A C   1 
ATOM   902  O O   . LYS A 1 132 ? 25.86000 -8.95400  21.34700 1.000 61.41188 ? 132 LYS A O   1 
ATOM   903  C CB  . LYS A 1 132 ? 25.86800 -7.29800  18.56400 1.000 49.76288 ? 132 LYS A CB  1 
ATOM   904  C CG  . LYS A 1 132 ? 26.63300 -7.92600  17.42200 1.000 49.99651 ? 132 LYS A CG  1 
ATOM   905  C CD  . LYS A 1 132 ? 27.67900 -6.96300  16.86000 1.000 54.99605 ? 132 LYS A CD  1 
ATOM   906  C CE  . LYS A 1 132 ? 28.98400 -7.06500  17.63700 1.000 56.40334 ? 132 LYS A CE  1 
ATOM   907  N NZ  . LYS A 1 132 ? 30.01000 -6.12200  17.10900 1.000 59.14784 ? 132 LYS A NZ  1 
ATOM   908  N N   . LYS A 1 133 ? 24.33500 -7.29300  21.42000 1.000 59.69744 ? 133 LYS A N   1 
ATOM   909  C CA  . LYS A 1 133 ? 24.37400 -7.22500  22.88200 1.000 55.66687 ? 133 LYS A CA  1 
ATOM   910  C C   . LYS A 1 133 ? 23.89800 -8.51800  23.53200 1.000 59.17578 ? 133 LYS A C   1 
ATOM   911  O O   . LYS A 1 133 ? 24.30700 -8.83100  24.65800 1.000 59.73920 ? 133 LYS A O   1 
ATOM   912  C CB  . LYS A 1 133 ? 23.53600 -6.05200  23.38200 1.000 59.86519 ? 133 LYS A CB  1 
ATOM   913  C CG  . LYS A 1 133 ? 24.25900 -4.71800  23.32000 1.000 72.43354 ? 133 LYS A CG  1 
ATOM   914  C CD  . LYS A 1 133 ? 23.37700 -3.55800  23.76800 1.000 73.52388 ? 133 LYS A CD  1 
ATOM   915  C CE  . LYS A 1 133 ? 24.00400 -2.21500  23.38100 1.000 77.34591 ? 133 LYS A CE  1 
ATOM   916  N NZ  . LYS A 1 133 ? 25.28300 -1.98100  24.11800 1.000 81.66442 ? 133 LYS A NZ  1 
ATOM   917  N N   . LYS A 1 134 ? 23.02200 -9.27500  22.86400 1.000 59.96063 ? 134 LYS A N   1 
ATOM   918  C CA  . LYS A 1 134 ? 22.64200 -10.57600 23.40900 1.000 62.79719 ? 134 LYS A CA  1 
ATOM   919  C C   . LYS A 1 134 ? 23.77600 -11.57800 23.28000 1.000 63.45231 ? 134 LYS A C   1 
ATOM   920  O O   . LYS A 1 134 ? 23.89900 -12.48500 24.11200 1.000 68.72512 ? 134 LYS A O   1 
ATOM   921  C CB  . LYS A 1 134 ? 21.39000 -11.11800 22.71600 1.000 59.57466 ? 134 LYS A CB  1 
ATOM   922  C CG  . LYS A 1 134 ? 20.13300 -10.29000 22.93300 1.000 58.71774 ? 134 LYS A CG  1 
ATOM   923  C CD  . LYS A 1 134 ? 19.68400 -10.34500 24.37900 1.000 64.09351 ? 134 LYS A CD  1 
ATOM   924  C CE  . LYS A 1 134 ? 18.28900 -9.76500  24.55600 1.000 64.07448 ? 134 LYS A CE  1 
ATOM   925  N NZ  . LYS A 1 134 ? 17.86400 -9.85300  25.97500 1.000 69.67470 ? 134 LYS A NZ  1 
ATOM   926  N N   . LEU A 1 135 ? 24.61000 -11.43200 22.25500 1.000 61.43286 ? 135 LEU A N   1 
ATOM   927  C CA  . LEU A 1 135 ? 25.72100 -12.34600 22.01100 1.000 63.50523 ? 135 LEU A CA  1 
ATOM   928  C C   . LEU A 1 135 ? 26.91600 -11.89200 22.84200 1.000 68.86583 ? 135 LEU A C   1 
ATOM   929  O O   . LEU A 1 135 ? 27.96800 -11.50000 22.33100 1.000 69.42484 ? 135 LEU A O   1 
ATOM   930  C CB  . LEU A 1 135 ? 26.05500 -12.39700 20.52700 1.000 63.91263 ? 135 LEU A CB  1 
ATOM   931  C CG  . LEU A 1 135 ? 24.84100 -12.44300 19.59700 1.000 64.58646 ? 135 LEU A CG  1 
ATOM   932  C CD1 . LEU A 1 135 ? 25.27100 -12.34700 18.14800 1.000 54.85391 ? 135 LEU A CD1 1 
ATOM   933  C CD2 . LEU A 1 135 ? 24.00900 -13.69000 19.83300 1.000 63.62579 ? 135 LEU A CD2 1 
ATOM   934  N N   . THR A 1 136 ? 26.72700 -11.95000 24.15700 1.000 70.45185 ? 136 THR A N   1 
ATOM   935  C CA  . THR A 1 136 ? 27.74600 -11.48700 25.08500 1.000 75.22301 ? 136 THR A CA  1 
ATOM   936  C C   . THR A 1 136 ? 29.02000 -12.30900 24.92100 1.000 76.40040 ? 136 THR A C   1 
ATOM   937  O O   . THR A 1 136 ? 28.98500 -13.54400 24.92200 1.000 78.44409 ? 136 THR A O   1 
ATOM   938  C CB  . THR A 1 136 ? 27.22000 -11.58000 26.51900 1.000 80.47576 ? 136 THR A CB  1 
ATOM   939  O OG1 . THR A 1 136 ? 26.97100 -12.95100 26.84700 1.000 85.72384 ? 136 THR A OG1 1 
ATOM   940  C CG2 . THR A 1 136 ? 25.91400 -10.79500 26.66300 1.000 74.77719 ? 136 THR A CG2 1 
ATOM   941  N N   . GLY A 1 137 ? 30.14800 -11.62000 24.76500 1.000 72.69761 ? 137 GLY A N   1 
ATOM   942  C CA  . GLY A 1 137 ? 31.41500 -12.27800 24.53500 1.000 68.20887 ? 137 GLY A CA  1 
ATOM   943  C C   . GLY A 1 137 ? 31.80500 -12.42000 23.07900 1.000 68.40599 ? 137 GLY A C   1 
ATOM   944  O O   . GLY A 1 137 ? 32.84300 -13.02900 22.79700 1.000 70.62395 ? 137 GLY A O   1 
ATOM   945  N N   . ILE A 1 138 ? 31.01200 -11.87900 22.14800 1.000 64.42613 ? 138 ILE A N   1 
ATOM   946  C CA  . ILE A 1 138 ? 31.33700 -11.96300 20.72500 1.000 62.98639 ? 138 ILE A CA  1 
ATOM   947  C C   . ILE A 1 138 ? 32.51200 -11.03900 20.41900 1.000 58.18506 ? 138 ILE A C   1 
ATOM   948  O O   . ILE A 1 138 ? 32.51400 -9.85700  20.78200 1.000 62.61637 ? 138 ILE A O   1 
ATOM   949  C CB  . ILE A 1 138 ? 30.09800 -11.63100 19.87400 1.000 63.37500 ? 138 ILE A CB  1 
ATOM   950  C CG1 . ILE A 1 138 ? 30.32300 -12.00600 18.41100 1.000 59.79446 ? 138 ILE A CG1 1 
ATOM   951  C CG2 . ILE A 1 138 ? 29.67600 -10.16900 20.02300 1.000 65.00752 ? 138 ILE A CG2 1 
ATOM   952  C CD1 . ILE A 1 138 ? 30.20200 -13.49300 18.17000 1.000 49.62036 ? 138 ILE A CD1 1 
ATOM   953  N N   . LYS A 1 139 ? 33.53700 -11.57800 19.77300 1.000 56.35501 ? 139 LYS A N   1 
ATOM   954  C CA  . LYS A 1 139 ? 34.79200 -10.85400 19.64400 1.000 57.44136 ? 139 LYS A CA  1 
ATOM   955  C C   . LYS A 1 139 ? 35.06600 -10.34600 18.23900 1.000 53.25300 ? 139 LYS A C   1 
ATOM   956  O O   . LYS A 1 139 ? 35.97300 -9.52500  18.06700 1.000 51.90095 ? 139 LYS A O   1 
ATOM   957  C CB  . LYS A 1 139 ? 35.96900 -11.73800 20.09700 1.000 57.42928 ? 139 LYS A CB  1 
ATOM   958  C CG  . LYS A 1 139 ? 35.92100 -12.12100 21.57200 1.000 61.55240 ? 139 LYS A CG  1 
ATOM   959  C CD  . LYS A 1 139 ? 37.26000 -12.66100 22.07900 1.000 68.87148 ? 139 LYS A CD  1 
ATOM   960  C CE  . LYS A 1 139 ? 37.65400 -13.96600 21.39700 1.000 61.87417 ? 139 LYS A CE  1 
ATOM   961  N NZ  . LYS A 1 139 ? 38.85600 -14.57500 22.04200 1.000 65.42071 ? 139 LYS A NZ  1 
ATOM   962  N N   . HIS A 1 140 ? 34.31400 -10.79800 17.23800 1.000 41.03580 ? 140 HIS A N   1 
ATOM   963  C CA  . HIS A 1 140 ? 34.62800 -10.50500 15.84900 1.000 46.98514 ? 140 HIS A CA  1 
ATOM   964  C C   . HIS A 1 140 ? 33.34000 -10.32800 15.06800 1.000 43.95076 ? 140 HIS A C   1 
ATOM   965  O O   . HIS A 1 140 ? 32.36900 -11.05700 15.28600 1.000 38.29402 ? 140 HIS A O   1 
ATOM   966  C CB  . HIS A 1 140 ? 35.45700 -11.62200 15.20100 1.000 47.42709 ? 140 HIS A CB  1 
ATOM   967  C CG  . HIS A 1 140 ? 36.68700 -11.96800 15.98100 1.000 51.90318 ? 140 HIS A CG  1 
ATOM   968  N ND1 . HIS A 1 140 ? 36.82400 -13.15300 16.66600 1.000 56.73007 ? 140 HIS A ND1 1 
ATOM   969  C CD2 . HIS A 1 140 ? 37.81100 -11.25500 16.22800 1.000 50.24122 ? 140 HIS A CD2 1 
ATOM   970  C CE1 . HIS A 1 140 ? 37.99100 -13.16800 17.28600 1.000 55.88851 ? 140 HIS A CE1 1 
ATOM   971  N NE2 . HIS A 1 140 ? 38.60700 -12.02500 17.04000 1.000 56.68168 ? 140 HIS A NE2 1 
ATOM   972  N N   . GLU A 1 141 ? 33.36300 -9.37200  14.14900 1.000 44.88807 ? 141 GLU A N   1 
ATOM   973  C CA  . GLU A 1 141 ? 32.22600 -9.03600  13.30500 1.000 42.22183 ? 141 GLU A CA  1 
ATOM   974  C C   . GLU A 1 141 ? 32.71800 -8.83700  11.88100 1.000 46.68783 ? 141 GLU A C   1 
ATOM   975  O O   . GLU A 1 141 ? 33.76500 -8.22100  11.64800 1.000 47.03803 ? 141 GLU A O   1 
ATOM   976  C CB  . GLU A 1 141 ? 31.51400 -7.77800  13.79400 1.000 45.79742 ? 141 GLU A CB  1 
ATOM   977  C CG  . GLU A 1 141 ? 30.32300 -7.34700  12.92500 1.000 45.84897 ? 141 GLU A CG  1 
ATOM   978  C CD  . GLU A 1 141 ? 29.58200 -6.14500  13.48400 1.000 52.22796 ? 141 GLU A CD  1 
ATOM   979  O OE1 . GLU A 1 141 ? 29.70000 -5.84400  14.68800 1.000 58.33172 ? 141 GLU A OE1 1 
ATOM   980  O OE2 . GLU A 1 141 ? 28.87000 -5.48300  12.71400 1.000 57.32641 ? 141 GLU A OE2 1 
ATOM   981  N N   . LEU A 1 142 ? 31.97600 -9.37500  10.92700 1.000 37.78588 ? 142 LEU A N   1 
ATOM   982  C CA  . LEU A 1 142 ? 32.21300 -9.07000  9.52300  1.000 40.03071 ? 142 LEU A CA  1 
ATOM   983  C C   . LEU A 1 142 ? 30.92200 -8.50400  8.96300  1.000 36.40422 ? 142 LEU A C   1 
ATOM   984  O O   . LEU A 1 142 ? 29.87400 -9.12900  9.10500  1.000 35.52112 ? 142 LEU A O   1 
ATOM   985  C CB  . LEU A 1 142 ? 32.63600 -10.31900 8.75200  1.000 37.40149 ? 142 LEU A CB  1 
ATOM   986  C CG  . LEU A 1 142 ? 32.74700 -10.24700 7.22700  1.000 37.06214 ? 142 LEU A CG  1 
ATOM   987  C CD1 . LEU A 1 142 ? 33.97500 -9.47700  6.84100  1.000 47.98523 ? 142 LEU A CD1 1 
ATOM   988  C CD2 . LEU A 1 142 ? 32.81100 -11.68000 6.64000  1.000 39.95289 ? 142 LEU A CD2 1 
ATOM   989  N N   . GLN A 1 143 ? 30.97900 -7.31800  8.37800  1.000 33.27535 ? 143 GLN A N   1 
ATOM   990  C CA  . GLN A 1 143 ? 29.84600 -6.78400  7.63700  1.000 33.03157 ? 143 GLN A CA  1 
ATOM   991  C C   . GLN A 1 143 ? 30.17400 -6.84900  6.15300  1.000 37.00889 ? 143 GLN A C   1 
ATOM   992  O O   . GLN A 1 143 ? 31.31200 -6.59300  5.74900  1.000 37.22678 ? 143 GLN A O   1 
ATOM   993  C CB  . GLN A 1 143 ? 29.51600 -5.34600  8.04200  1.000 34.70481 ? 143 GLN A CB  1 
ATOM   994  C CG  . GLN A 1 143 ? 29.22000 -5.16700  9.51900  1.000 35.58405 ? 143 GLN A CG  1 
ATOM   995  C CD  . GLN A 1 143 ? 28.59300 -3.83200  9.79800  1.000 37.06769 ? 143 GLN A CD  1 
ATOM   996  O OE1 . GLN A 1 143 ? 27.77300 -3.36800  9.02500  1.000 40.08659 ? 143 GLN A OE1 1 
ATOM   997  N NE2 . GLN A 1 143 ? 28.99300 -3.18500  10.89400 1.000 42.94889 ? 143 GLN A NE2 1 
ATOM   998  N N   . ALA A 1 144 ? 29.17600 -7.16700  5.33800  1.000 31.56214 ? 144 ALA A N   1 
ATOM   999  C CA  . ALA A 1 144 ? 29.38900 -7.22400  3.89900  1.000 32.55827 ? 144 ALA A CA  1 
ATOM   1000 C C   . ALA A 1 144 ? 28.13800 -6.73400  3.18500  1.000 32.93745 ? 144 ALA A C   1 
ATOM   1001 O O   . ALA A 1 144 ? 27.01400 -7.02900  3.61600  1.000 31.24961 ? 144 ALA A O   1 
ATOM   1002 C CB  . ALA A 1 144 ? 29.73400 -8.65900  3.44000  1.000 34.34062 ? 144 ALA A CB  1 
ATOM   1003 N N   . ASN A 1 145 ? 28.33500 -6.02900  2.07100  1.000 36.62270 ? 145 ASN A N   1 
ATOM   1004 C CA  . ASN A 1 145 ? 27.22200 -5.55800  1.25700  1.000 34.90191 ? 145 ASN A CA  1 
ATOM   1005 C C   . ASN A 1 145 ? 27.27600 -6.10500  -0.16800 1.000 39.23959 ? 145 ASN A C   1 
ATOM   1006 O O   . ASN A 1 145 ? 26.57800 -5.58100  -1.04500 1.000 41.47202 ? 145 ASN A O   1 
ATOM   1007 C CB  . ASN A 1 145 ? 27.14900 -4.02000  1.25900  1.000 36.42015 ? 145 ASN A CB  1 
ATOM   1008 C CG  . ASN A 1 145 ? 28.49600 -3.33800  1.03200  1.000 43.63354 ? 145 ASN A CG  1 
ATOM   1009 O OD1 . ASN A 1 145 ? 29.36100 -3.84000  0.29600  1.000 47.68094 ? 145 ASN A OD1 1 
ATOM   1010 N ND2 . ASN A 1 145 ? 28.67200 -2.16200  1.65800  1.000 48.53178 ? 145 ASN A ND2 1 
ATOM   1011 N N   . CYS A 1 146 ? 28.05600 -7.16800  -0.41100 1.000 37.41120 ? 146 CYS A N   1 
ATOM   1012 C CA  . CYS A 1 146 ? 28.16800 -7.81100  -1.72500 1.000 40.18315 ? 146 CYS A CA  1 
ATOM   1013 C C   . CYS A 1 146 ? 28.93300 -9.12700  -1.57800 1.000 42.18833 ? 146 CYS A C   1 
ATOM   1014 O O   . CYS A 1 146 ? 29.63300 -9.33800  -0.58400 1.000 38.37757 ? 146 CYS A O   1 
ATOM   1015 C CB  . CYS A 1 146 ? 28.86000 -6.89700  -2.74200 1.000 42.87172 ? 146 CYS A CB  1 
ATOM   1016 S SG  . CYS A 1 146 ? 30.65000 -6.60400  -2.43300 1.000 45.69916 ? 146 CYS A SG  1 
ATOM   1017 N N   . TYR A 1 147 ? 28.81400 -10.00600 -2.58900 1.000 42.47958 ? 147 TYR A N   1 
ATOM   1018 C CA  . TYR A 1 147 ? 29.44300 -11.33100 -2.49500 1.000 40.86223 ? 147 TYR A CA  1 
ATOM   1019 C C   . TYR A 1 147 ? 30.96300 -11.26700 -2.53600 1.000 40.64282 ? 147 TYR A C   1 
ATOM   1020 O O   . TYR A 1 147 ? 31.63200 -12.08700 -1.88800 1.000 43.48463 ? 147 TYR A O   1 
ATOM   1021 C CB  . TYR A 1 147 ? 28.97000 -12.26100 -3.61300 1.000 45.27643 ? 147 TYR A CB  1 
ATOM   1022 C CG  . TYR A 1 147 ? 27.61200 -12.82400 -3.31500 1.000 42.61484 ? 147 TYR A CG  1 
ATOM   1023 C CD1 . TYR A 1 147 ? 27.42900 -13.71800 -2.26600 1.000 40.58781 ? 147 TYR A CD1 1 
ATOM   1024 C CD2 . TYR A 1 147 ? 26.50900 -12.43500 -4.05600 1.000 46.15270 ? 147 TYR A CD2 1 
ATOM   1025 C CE1 . TYR A 1 147 ? 26.17700 -14.22300 -1.97300 1.000 40.91445 ? 147 TYR A CE1 1 
ATOM   1026 C CE2 . TYR A 1 147 ? 25.25500 -12.93000 -3.76700 1.000 42.06687 ? 147 TYR A CE2 1 
ATOM   1027 C CZ  . TYR A 1 147 ? 25.09400 -13.82500 -2.73300 1.000 43.17042 ? 147 TYR A CZ  1 
ATOM   1028 O OH  . TYR A 1 147 ? 23.83600 -14.30300 -2.45000 1.000 40.60780 ? 147 TYR A OH  1 
ATOM   1029 N N   . GLU A 1 148 ? 31.52300 -10.33400 -3.30400 1.000 41.01723 ? 148 GLU A N   1 
ATOM   1030 C CA  . GLU A 1 148 ? 32.97600 -10.22500 -3.37400 1.000 44.42659 ? 148 GLU A CA  1 
ATOM   1031 C C   . GLU A 1 148 ? 33.56200 -10.01300 -1.98700 1.000 41.77336 ? 148 GLU A C   1 
ATOM   1032 O O   . GLU A 1 148 ? 34.59400 -10.59500 -1.64800 1.000 47.24940 ? 148 GLU A O   1 
ATOM   1033 C CB  . GLU A 1 148 ? 33.37800 -9.09000  -4.32100 1.000 47.16093 ? 148 GLU A CB  1 
ATOM   1034 C CG  . GLU A 1 148 ? 34.88000 -8.96700  -4.52200 1.000 56.99893 ? 148 GLU A CG  1 
ATOM   1035 C CD  . GLU A 1 148 ? 35.26300 -7.87100  -5.51000 1.000 73.09873 ? 148 GLU A CD  1 
ATOM   1036 O OE1 . GLU A 1 148 ? 34.58500 -6.81600  -5.53600 1.000 76.19089 ? 148 GLU A OE1 1 
ATOM   1037 O OE2 . GLU A 1 148 ? 36.24400 -8.06700  -6.26600 1.000 80.54728 ? 148 GLU A OE2 1 
ATOM   1038 N N   . GLU A 1 149 ? 32.88800 -9.22500  -1.15400 1.000 40.41795 ? 149 GLU A N   1 
ATOM   1039 C CA  . GLU A 1 149 ? 33.37800 -8.99600  0.19800  1.000 45.22229 ? 149 GLU A CA  1 
ATOM   1040 C C   . GLU A 1 149 ? 33.19300 -10.23100 1.06400  1.000 46.92999 ? 149 GLU A C   1 
ATOM   1041 O O   . GLU A 1 149 ? 34.10800 -10.63500 1.78900  1.000 47.55154 ? 149 GLU A O   1 
ATOM   1042 C CB  . GLU A 1 149 ? 32.66600 -7.80600  0.83100  1.000 42.94522 ? 149 GLU A CB  1 
ATOM   1043 C CG  . GLU A 1 149 ? 33.03200 -6.47100  0.19800  1.000 47.60307 ? 149 GLU A CG  1 
ATOM   1044 C CD  . GLU A 1 149 ? 32.35000 -5.30300  0.88500  1.000 49.98774 ? 149 GLU A CD  1 
ATOM   1045 O OE1 . GLU A 1 149 ? 31.49300 -5.55700  1.76700  1.000 46.74753 ? 149 GLU A OE1 1 
ATOM   1046 O OE2 . GLU A 1 149 ? 32.67600 -4.14000  0.54300  1.000 56.54066 ? 149 GLU A OE2 1 
ATOM   1047 N N   . VAL A 1 150 ? 32.00900 -10.83800 1.01700  1.000 39.26703 ? 150 VAL A N   1 
ATOM   1048 C CA  . VAL A 1 150 ? 31.74400 -11.91700 1.96700  1.000 42.53145 ? 150 VAL A CA  1 
ATOM   1049 C C   . VAL A 1 150 ? 32.58000 -13.15400 1.63600  1.000 42.93710 ? 150 VAL A C   1 
ATOM   1050 O O   . VAL A 1 150 ? 32.89300 -13.94800 2.53300  1.000 48.75999 ? 150 VAL A O   1 
ATOM   1051 C CB  . VAL A 1 150 ? 30.23100 -12.22600 2.02400  1.000 40.11126 ? 150 VAL A CB  1 
ATOM   1052 C CG1 . VAL A 1 150 ? 29.81500 -13.19200 0.91000  1.000 37.71375 ? 150 VAL A CG1 1 
ATOM   1053 C CG2 . VAL A 1 150 ? 29.82700 -12.75000 3.42200  1.000 38.13272 ? 150 VAL A CG2 1 
ATOM   1054 N N   . LYS A 1 151 ? 32.97000 -13.32800 0.37800  1.000 43.55792 ? 151 LYS A N   1 
ATOM   1055 C CA  . LYS A 1 151 ? 33.84600 -14.40800 -0.05400 1.000 47.11443 ? 151 LYS A CA  1 
ATOM   1056 C C   . LYS A 1 151 ? 35.33500 -14.09700 0.11000  1.000 50.16579 ? 151 LYS A C   1 
ATOM   1057 O O   . LYS A 1 151 ? 36.16400 -14.94500 -0.22800 1.000 53.31032 ? 151 LYS A O   1 
ATOM   1058 C CB  . LYS A 1 151 ? 33.58900 -14.73700 -1.52700 1.000 43.98854 ? 151 LYS A CB  1 
ATOM   1059 C CG  . LYS A 1 151 ? 32.20200 -15.26800 -1.82700 1.000 46.41539 ? 151 LYS A CG  1 
ATOM   1060 C CD  . LYS A 1 151 ? 32.06500 -15.59900 -3.31400 1.000 56.33688 ? 151 LYS A CD  1 
ATOM   1061 C CE  . LYS A 1 151 ? 30.60600 -15.93400 -3.69000 1.000 62.52912 ? 151 LYS A CE  1 
ATOM   1062 N NZ  . LYS A 1 151 ? 30.42700 -16.36000 -5.12200 1.000 64.47416 ? 151 LYS A NZ  1 
ATOM   1063 N N   . ASP A 1 152 ? 35.69900 -12.90600 0.57900  1.000 49.32229 ? 152 ASP A N   1 
ATOM   1064 C CA  . ASP A 1 152 ? 37.10800 -12.52200 0.66900  1.000 51.38841 ? 152 ASP A CA  1 
ATOM   1065 C C   . ASP A 1 152 ? 37.70300 -13.20800 1.88900  1.000 53.01720 ? 152 ASP A C   1 
ATOM   1066 O O   . ASP A 1 152 ? 37.56100 -12.72900 3.01800  1.000 44.94627 ? 152 ASP A O   1 
ATOM   1067 C CB  . ASP A 1 152 ? 37.25900 -11.00500 0.75700  1.000 52.55907 ? 152 ASP A CB  1 
ATOM   1068 C CG  . ASP A 1 152 ? 38.70900 -10.54400 0.54800  1.000 60.09194 ? 152 ASP A CG  1 
ATOM   1069 O OD1 . ASP A 1 152 ? 39.60800 -11.40400 0.44200  1.000 57.43297 ? 152 ASP A OD1 1 
ATOM   1070 O OD2 . ASP A 1 152 ? 38.94700 -9.31600  0.46800  1.000 63.94112 ? 152 ASP A OD2 1 
ATOM   1071 N N   . ARG A 1 153 ? 38.38500 -14.33900 1.67000  1.000 51.06960 ? 153 ARG A N   1 
ATOM   1072 C CA  . ARG A 1 153 ? 38.93000 -15.06500 2.80800  1.000 50.13606 ? 153 ARG A CA  1 
ATOM   1073 C C   . ARG A 1 153 ? 39.98500 -14.23800 3.52200  1.000 53.34008 ? 153 ARG A C   1 
ATOM   1074 O O   . ARG A 1 153 ? 40.11900 -14.32000 4.74700  1.000 55.90457 ? 153 ARG A O   1 
ATOM   1075 C CB  . ARG A 1 153 ? 39.50200 -16.41100 2.34600  1.000 55.27017 ? 153 ARG A CB  1 
ATOM   1076 C CG  . ARG A 1 153 ? 38.46100 -17.29400 1.67500  1.000 61.46071 ? 153 ARG A CG  1 
ATOM   1077 C CD  . ARG A 1 153 ? 38.24300 -18.59700 2.42400  1.000 67.99327 ? 153 ARG A CD  1 
ATOM   1078 N NE  . ARG A 1 153 ? 37.15600 -19.38400 1.85000  1.000 71.30917 ? 153 ARG A NE  1 
ATOM   1079 C CZ  . ARG A 1 153 ? 36.97400 -20.68200 2.06000  1.000 66.90816 ? 153 ARG A CZ  1 
ATOM   1080 N NH1 . ARG A 1 153 ? 37.79500 -21.38100 2.83000  1.000 59.00175 ? 153 ARG A NH1 1 
ATOM   1081 N NH2 . ARG A 1 153 ? 35.94900 -21.29700 1.47200  1.000 61.62822 ? 153 ARG A NH2 1 
ATOM   1082 N N   . CYS A 1 154 ? 40.72400 -13.41700 2.77700  1.000 51.55552 ? 154 CYS A N   1 
ATOM   1083 C CA  . CYS A 1 154 ? 41.68700 -12.51600 3.39600  1.000 56.14093 ? 154 CYS A CA  1 
ATOM   1084 C C   . CYS A 1 154 ? 40.99900 -11.52700 4.32800  1.000 55.89305 ? 154 CYS A C   1 
ATOM   1085 O O   . CYS A 1 154 ? 41.55200 -11.15300 5.36900  1.000 58.91505 ? 154 CYS A O   1 
ATOM   1086 C CB  . CYS A 1 154 ? 42.46900 -11.78200 2.31500  1.000 54.49519 ? 154 CYS A CB  1 
ATOM   1087 S SG  . CYS A 1 154 ? 43.56900 -12.87700 1.39300  1.000 70.52092 ? 154 CYS A SG  1 
ATOM   1088 N N   . THR A 1 155 ? 39.79300 -11.09600 3.97700  1.000 54.51472 ? 155 THR A N   1 
ATOM   1089 C CA  . THR A 1 155 ? 39.10000 -10.12700 4.81800  1.000 60.65184 ? 155 THR A CA  1 
ATOM   1090 C C   . THR A 1 155 ? 38.55400 -10.78800 6.07400  1.000 52.38027 ? 155 THR A C   1 
ATOM   1091 O O   . THR A 1 155 ? 38.73300 -10.26900 7.18000  1.000 52.34650 ? 155 THR A O   1 
ATOM   1092 C CB  . THR A 1 155 ? 37.98300 -9.44200  4.03300  1.000 58.09325 ? 155 THR A CB  1 
ATOM   1093 O OG1 . THR A 1 155 ? 38.56700 -8.63600  3.00500  1.000 60.58602 ? 155 THR A OG1 1 
ATOM   1094 C CG2 . THR A 1 155 ? 37.15000 -8.55100  4.95500  1.000 59.76503 ? 155 THR A CG2 1 
ATOM   1095 N N   . LEU A 1 156 ? 37.90400 -11.94600 5.92800  1.000 53.37137 ? 156 LEU A N   1 
ATOM   1096 C CA  . LEU A 1 156 ? 37.51200 -12.70700 7.11000  1.000 50.66086 ? 156 LEU A CA  1 
ATOM   1097 C C   . LEU A 1 156 ? 38.72700 -13.00700 7.97700  1.000 49.06353 ? 156 LEU A C   1 
ATOM   1098 O O   . LEU A 1 156 ? 38.70100 -12.79400 9.19400  1.000 43.68511 ? 156 LEU A O   1 
ATOM   1099 C CB  . LEU A 1 156 ? 36.78900 -13.99200 6.71100  1.000 48.01243 ? 156 LEU A CB  1 
ATOM   1100 C CG  . LEU A 1 156 ? 36.38300 -14.90300 7.87400  1.000 46.03360 ? 156 LEU A CG  1 
ATOM   1101 C CD1 . LEU A 1 156 ? 35.60000 -14.13400 8.92200  1.000 44.50689 ? 156 LEU A CD1 1 
ATOM   1102 C CD2 . LEU A 1 156 ? 35.59100 -16.09400 7.38500  1.000 46.71697 ? 156 LEU A CD2 1 
ATOM   1103 N N   . ALA A 1 157 ? 39.82700 -13.45900 7.35400  1.000 48.76211 ? 157 ALA A N   1 
ATOM   1104 C CA  . ALA A 1 157 ? 41.03100 -13.76300 8.11900  1.000 46.80230 ? 157 ALA A CA  1 
ATOM   1105 C C   . ALA A 1 157 ? 41.52200 -12.53700 8.88600  1.000 51.06833 ? 157 ALA A C   1 
ATOM   1106 O O   . ALA A 1 157 ? 41.94800 -12.64700 10.04000 1.000 51.25091 ? 157 ALA A O   1 
ATOM   1107 C CB  . ALA A 1 157 ? 42.12500 -14.30200 7.19100  1.000 48.57860 ? 157 ALA A CB  1 
ATOM   1108 N N   . GLU A 1 158 ? 41.46600 -11.36300 8.26500  1.000 52.58822 ? 158 GLU A N   1 
ATOM   1109 C CA  . GLU A 1 158 ? 41.88600 -10.14800 8.95900  1.000 58.31986 ? 158 GLU A CA  1 
ATOM   1110 C C   . GLU A 1 158 ? 40.89400 -9.74800  10.04800 1.000 55.61099 ? 158 GLU A C   1 
ATOM   1111 O O   . GLU A 1 158 ? 41.30200 -9.26600  11.10900 1.000 56.58650 ? 158 GLU A O   1 
ATOM   1112 C CB  . GLU A 1 158 ? 42.08500 -9.01800  7.95500  1.000 61.03767 ? 158 GLU A CB  1 
ATOM   1113 C CG  . GLU A 1 158 ? 43.34300 -9.22100  7.12500  1.000 69.55284 ? 158 GLU A CG  1 
ATOM   1114 C CD  . GLU A 1 158 ? 43.55000 -8.15500  6.07300  1.000 81.03943 ? 158 GLU A CD  1 
ATOM   1115 O OE1 . GLU A 1 158 ? 42.56300 -7.48300  5.69500  1.000 80.09898 ? 158 GLU A OE1 1 
ATOM   1116 O OE2 . GLU A 1 158 ? 44.70900 -7.99600  5.62800  1.000 80.41406 ? 158 GLU A OE2 1 
ATOM   1117 N N   . LYS A 1 159 ? 39.60100 -9.97500  9.83600  1.000 52.17933 ? 159 LYS A N   1 
ATOM   1118 C CA  . LYS A 1 159 ? 38.65800 -9.67100  10.94100 1.000 55.66954 ? 159 LYS A CA  1 
ATOM   1119 C C   . LYS A 1 159 ? 38.94000 -10.61100 12.11800 1.000 56.48840 ? 159 LYS A C   1 
ATOM   1120 O O   . LYS A 1 159 ? 38.63800 -10.21600 13.25100 1.000 57.62171 ? 159 LYS A O   1 
ATOM   1121 C CB  . LYS A 1 159 ? 37.18600 -9.77000  10.52200 1.000 51.22408 ? 159 LYS A CB  1 
ATOM   1122 C CG  . LYS A 1 159 ? 36.74600 -8.75600  9.48500  1.000 53.70681 ? 159 LYS A CG  1 
ATOM   1123 C CD  . LYS A 1 159 ? 36.88500 -7.32500  9.98600  1.000 56.11525 ? 159 LYS A CD  1 
ATOM   1124 C CE  . LYS A 1 159 ? 36.35700 -6.32700  9.00900  1.000 58.31677 ? 159 LYS A CE  1 
ATOM   1125 N NZ  . LYS A 1 159 ? 36.42400 -4.96900  9.55400  1.000 60.21382 ? 159 LYS A NZ  1 
ATOM   1126 N N   . LEU A 1 160 ? 39.49500 -11.79700 11.86200 1.000 49.44307 ? 160 LEU A N   1 
ATOM   1127 C CA  . LEU A 1 160 ? 39.70300 -12.79700 12.90600 1.000 46.43468 ? 160 LEU A CA  1 
ATOM   1128 C C   . LEU A 1 160 ? 40.97800 -12.55100 13.69800 1.000 56.03809 ? 160 LEU A C   1 
ATOM   1129 O O   . LEU A 1 160 ? 40.99200 -12.74000 14.91800 1.000 59.69018 ? 160 LEU A O   1 
ATOM   1130 C CB  . LEU A 1 160 ? 39.75000 -14.20200 12.29300 1.000 46.49598 ? 160 LEU A CB  1 
ATOM   1131 C CG  . LEU A 1 160 ? 38.40300 -14.81900 11.94900 1.000 44.33869 ? 160 LEU A CG  1 
ATOM   1132 C CD1 . LEU A 1 160 ? 38.56000 -15.97400 10.96400 1.000 44.30785 ? 160 LEU A CD1 1 
ATOM   1133 C CD2 . LEU A 1 160 ? 37.76500 -15.31300 13.22400 1.000 48.39496 ? 160 LEU A CD2 1 
ATOM   1134 N N   . GLY A 1 161 ? 42.05700 -12.15700 13.03200 1.000 52.77742 ? 161 GLY A N   1 
ATOM   1135 C CA  . GLY A 1 161 ? 43.34000 -12.04900 13.70200 1.000 56.97095 ? 161 GLY A CA  1 
ATOM   1136 C C   . GLY A 1 161 ? 44.32200 -11.17000 12.95900 1.000 59.27320 ? 161 GLY A C   1 
ATOM   1137 O O   . GLY A 1 161 ? 45.53000 -11.20800 13.22200 1.000 63.49313 ? 161 GLY A O   1 
ATOM   1138 N N   . GLY A 1 162 ? 43.81200 -10.38100 12.01400 1.000 60.21325 ? 162 GLY A N   1 
ATOM   1139 C CA  . GLY A 1 162 ? 44.66400 -9.42100  11.34100 1.000 64.17183 ? 162 GLY A CA  1 
ATOM   1140 C C   . GLY A 1 162 ? 45.61500 -10.07400 10.35500 1.000 64.50451 ? 162 GLY A C   1 
ATOM   1141 O O   . GLY A 1 162 ? 45.37900 -11.17300 9.84500  1.000 62.63226 ? 162 GLY A O   1 
ATOM   1142 N N   . SER A 1 163 ? 46.72500 -9.37800  10.09700 1.000 69.25684 ? 163 SER A N   1 
ATOM   1143 C CA  . SER A 1 163 ? 47.68200 -9.78100  9.07400  1.000 66.00943 ? 163 SER A CA  1 
ATOM   1144 C C   . SER A 1 163 ? 48.50600 -11.00300 9.46400  1.000 65.70171 ? 163 SER A C   1 
ATOM   1145 O O   . SER A 1 163 ? 49.20100 -11.56600 8.60600  1.000 66.74353 ? 163 SER A O   1 
ATOM   1146 C CB  . SER A 1 163 ? 48.62300 -8.62000  8.77900  1.000 69.80280 ? 163 SER A CB  1 
ATOM   1147 O OG  . SER A 1 163 ? 49.45700 -8.38800  9.90200  1.000 75.47880 ? 163 SER A OG  1 
ATOM   1148 N N   . ALA A 1 164 ? 48.48300 -11.40600 10.73100 1.000 64.50481 ? 164 ALA A N   1 
ATOM   1149 C CA  . ALA A 1 164 ? 49.22700 -12.58800 11.12700 1.000 64.42926 ? 164 ALA A CA  1 
ATOM   1150 C C   . ALA A 1 164 ? 48.54200 -13.88600 10.70000 1.000 61.88511 ? 164 ALA A C   1 
ATOM   1151 O O   . ALA A 1 164 ? 49.19000 -14.93700 10.70900 1.000 59.27221 ? 164 ALA A O   1 
ATOM   1152 C CB  . ALA A 1 164 ? 49.44300 -12.59400 12.64100 1.000 67.51957 ? 164 ALA A CB  1 
ATOM   1153 N N   . VAL A 1 165 ? 47.26200 -13.84300 10.33100 1.000 59.11667 ? 165 VAL A N   1 
ATOM   1154 C CA  . VAL A 1 165 ? 46.56000 -15.07100 9.95200  1.000 55.34618 ? 165 VAL A CA  1 
ATOM   1155 C C   . VAL A 1 165 ? 47.02400 -15.51000 8.56800  1.000 56.21303 ? 165 VAL A C   1 
ATOM   1156 O O   . VAL A 1 165 ? 46.99800 -14.72100 7.61100  1.000 54.26651 ? 165 VAL A O   1 
ATOM   1157 C CB  . VAL A 1 165 ? 45.03800 -14.86800 9.98200  1.000 55.16129 ? 165 VAL A CB  1 
ATOM   1158 C CG1 . VAL A 1 165 ? 44.33800 -16.14100 9.50100  1.000 49.65195 ? 165 VAL A CG1 1 
ATOM   1159 C CG2 . VAL A 1 165 ? 44.56600 -14.47800 11.38400 1.000 49.70644 ? 165 VAL A CG2 1 
ATOM   1160 N N   . ILE A 1 166 ? 47.44200 -16.77200 8.45700  1.000 50.35493 ? 166 ILE A N   1 
ATOM   1161 C CA  . ILE A 1 166 ? 47.97500 -17.30500 7.20500  1.000 52.17819 ? 166 ILE A CA  1 
ATOM   1162 C C   . ILE A 1 166 ? 47.15700 -18.45900 6.65300  1.000 50.49425 ? 166 ILE A C   1 
ATOM   1163 O O   . ILE A 1 166 ? 47.37200 -18.84700 5.49600  1.000 51.01100 ? 166 ILE A O   1 
ATOM   1164 C CB  . ILE A 1 166 ? 49.45700 -17.73000 7.34600  1.000 52.82743 ? 166 ILE A CB  1 
ATOM   1165 C CG1 . ILE A 1 166 ? 49.64300 -18.72900 8.49200  1.000 53.69319 ? 166 ILE A CG1 1 
ATOM   1166 C CG2 . ILE A 1 166 ? 50.33300 -16.50500 7.56100  1.000 54.77976 ? 166 ILE A CG2 1 
ATOM   1167 C CD1 . ILE A 1 166 ? 51.03100 -19.35500 8.54300  1.000 55.62011 ? 166 ILE A CD1 1 
ATOM   1168 N N   . SER A 1 167 ? 46.23500 -19.02500 7.42400  1.000 45.59017 ? 167 SER A N   1 
ATOM   1169 C CA  . SER A 1 167 ? 45.32700 -20.01400 6.87600  1.000 44.13889 ? 167 SER A CA  1 
ATOM   1170 C C   . SER A 1 167 ? 43.99500 -19.87700 7.58800  1.000 45.30814 ? 167 SER A C   1 
ATOM   1171 O O   . SER A 1 167 ? 43.90400 -19.31100 8.68300  1.000 42.97888 ? 167 SER A O   1 
ATOM   1172 C CB  . SER A 1 167 ? 45.88400 -21.43800 7.00700  1.000 44.22985 ? 167 SER A CB  1 
ATOM   1173 O OG  . SER A 1 167 ? 45.52600 -21.99400 8.24400  1.000 53.20904 ? 167 SER A OG  1 
ATOM   1174 N N   . LEU A 1 168 ? 42.95600 -20.40900 6.95200  1.000 40.92031 ? 168 LEU A N   1 
ATOM   1175 C CA  . LEU A 1 168 ? 41.58800 -20.16700 7.37700  1.000 41.20468 ? 168 LEU A CA  1 
ATOM   1176 C C   . LEU A 1 168 ? 40.75400 -21.35700 6.94000  1.000 39.37464 ? 168 LEU A C   1 
ATOM   1177 O O   . LEU A 1 168 ? 40.82200 -21.74900 5.77400  1.000 38.12586 ? 168 LEU A O   1 
ATOM   1178 C CB  . LEU A 1 168 ? 41.04600 -18.88400 6.74900  1.000 43.63926 ? 168 LEU A CB  1 
ATOM   1179 C CG  . LEU A 1 168 ? 39.56400 -18.55700 6.89700  1.000 47.03451 ? 168 LEU A CG  1 
ATOM   1180 C CD1 . LEU A 1 168 ? 39.21000 -18.34300 8.34800  1.000 43.70773 ? 168 LEU A CD1 1 
ATOM   1181 C CD2 . LEU A 1 168 ? 39.25900 -17.31000 6.08400  1.000 53.89239 ? 168 LEU A CD2 1 
ATOM   1182 N N   . GLU A 1 169 ? 39.99900 -21.94000 7.86600  1.000 32.83852 ? 169 GLU A N   1 
ATOM   1183 C CA  . GLU A 1 169 ? 39.06600 -23.00900 7.51300  1.000 35.39128 ? 169 GLU A CA  1 
ATOM   1184 C C   . GLU A 1 169 ? 39.77700 -24.12800 6.74200  1.000 34.87764 ? 169 GLU A C   1 
ATOM   1185 O O   . GLU A 1 169 ? 39.26900 -24.65800 5.75200  1.000 34.97344 ? 169 GLU A O   1 
ATOM   1186 C CB  . GLU A 1 169 ? 37.88300 -22.44300 6.72200  1.000 37.15848 ? 169 GLU A CB  1 
ATOM   1187 C CG  . GLU A 1 169 ? 36.90800 -21.64700 7.59300  1.000 36.20504 ? 169 GLU A CG  1 
ATOM   1188 C CD  . GLU A 1 169 ? 36.12200 -22.55600 8.51500  1.000 37.81236 ? 169 GLU A CD  1 
ATOM   1189 O OE1 . GLU A 1 169 ? 35.20200 -23.22200 8.01600  1.000 40.17871 ? 169 GLU A OE1 1 
ATOM   1190 O OE2 . GLU A 1 169 ? 36.44400 -22.63700 9.71600  1.000 39.68651 ? 169 GLU A OE2 1 
ATOM   1191 N N   . GLY A 1 170 ? 40.98000 -24.47200 7.18800  1.000 32.69772 ? 170 GLY A N   1 
ATOM   1192 C CA  . GLY A 1 170 ? 41.68600 -25.61700 6.64100  1.000 34.46490 ? 170 GLY A CA  1 
ATOM   1193 C C   . GLY A 1 170 ? 42.40200 -25.41100 5.32500  1.000 36.18328 ? 170 GLY A C   1 
ATOM   1194 O O   . GLY A 1 170 ? 42.91900 -26.38300 4.75800  1.000 36.24196 ? 170 GLY A O   1 
ATOM   1195 N N   . LYS A 1 171 ? 42.49100 -24.18500 4.82800  1.000 35.73372 ? 171 LYS A N   1 
ATOM   1196 C CA  . LYS A 1 171 ? 43.18000 -23.94000 3.57700  1.000 38.12591 ? 171 LYS A CA  1 
ATOM   1197 C C   . LYS A 1 171 ? 44.16700 -22.79600 3.74800  1.000 38.94727 ? 171 LYS A C   1 
ATOM   1198 O O   . LYS A 1 171 ? 43.88300 -21.82300 4.46700  1.000 41.04038 ? 171 LYS A O   1 
ATOM   1199 C CB  . LYS A 1 171 ? 42.16600 -23.61000 2.46400  1.000 43.79219 ? 171 LYS A CB  1 
ATOM   1200 C CG  . LYS A 1 171 ? 41.27700 -24.78400 2.06000  1.000 46.14144 ? 171 LYS A CG  1 
ATOM   1201 C CD  . LYS A 1 171 ? 40.05500 -24.34200 1.25700  1.000 60.20340 ? 171 LYS A CD  1 
ATOM   1202 C CE  . LYS A 1 171 ? 39.22900 -25.55400 0.80400  1.000 66.16892 ? 171 LYS A CE  1 
ATOM   1203 N NZ  . LYS A 1 171 ? 38.15600 -25.23200 -0.19900 1.000 69.27440 ? 171 LYS A NZ  1 
ATOM   1204 N N   . PRO A 1 172 ? 45.33500 -22.87000 3.11700  1.000 37.98079 ? 172 PRO A N   1 
ATOM   1205 C CA  . PRO A 1 172 ? 46.24900 -21.72500 3.13700  1.000 39.83741 ? 172 PRO A CA  1 
ATOM   1206 C C   . PRO A 1 172 ? 45.58000 -20.51900 2.50400  1.000 47.78093 ? 172 PRO A C   1 
ATOM   1207 O O   . PRO A 1 172 ? 44.74000 -20.65000 1.61200  1.000 42.13177 ? 172 PRO A O   1 
ATOM   1208 C CB  . PRO A 1 172 ? 47.44300 -22.19100 2.29200  1.000 43.31274 ? 172 PRO A CB  1 
ATOM   1209 C CG  . PRO A 1 172 ? 47.32600 -23.68300 2.25900  1.000 41.76176 ? 172 PRO A CG  1 
ATOM   1210 C CD  . PRO A 1 172 ? 45.87500 -24.01500 2.35700  1.000 38.12373 ? 172 PRO A CD  1 
ATOM   1211 N N   . LEU A 1 173 ? 45.99100 -19.33300 2.94900  1.000 48.47963 ? 173 LEU A N   1 
ATOM   1212 C CA  . LEU A 1 173 ? 45.54200 -18.10700 2.31200  1.000 52.81300 ? 173 LEU A CA  1 
ATOM   1213 C C   . LEU A 1 173 ? 46.43100 -17.78600 1.11000  1.000 64.32486 ? 173 LEU A C   1 
ATOM   1214 O O   . LEU A 1 173 ? 47.61100 -18.16600 1.07200  1.000 61.93099 ? 173 LEU A O   1 
ATOM   1215 C CB  . LEU A 1 173 ? 45.56300 -16.93100 3.29500  1.000 58.21216 ? 173 LEU A CB  1 
ATOM   1216 C CG  . LEU A 1 173 ? 44.62900 -16.90800 4.50100  1.000 55.12993 ? 173 LEU A CG  1 
ATOM   1217 C CD1 . LEU A 1 173 ? 44.80500 -15.56400 5.19600  1.000 58.13653 ? 173 LEU A CD1 1 
ATOM   1218 C CD2 . LEU A 1 173 ? 43.18900 -17.10700 4.06200  1.000 51.70642 ? 173 LEU A CD2 1 
ATOM   1219 O OXT . LEU A 1 173 ? 45.99500 -17.11500 0.16600  1.000 71.55668 ? 173 LEU A OXT 1 
ATOM   1220 N N   . GLN B 2 3   ? 41.82000 4.31100   2.82500  1.000 82.12301 ? 3   GLN B N   1 
ATOM   1221 C CA  . GLN B 2 3   ? 41.32100 5.05600   1.67100  1.000 74.10865 ? 3   GLN B CA  1 
ATOM   1222 C C   . GLN B 2 3   ? 39.92700 5.63100   1.91100  1.000 58.87378 ? 3   GLN B C   1 
ATOM   1223 O O   . GLN B 2 3   ? 39.64500 6.78300   1.51900  1.000 59.90866 ? 3   GLN B O   1 
ATOM   1224 C CB  . GLN B 2 3   ? 41.29500 4.16800   0.42100  1.000 80.95090 ? 3   GLN B CB  1 
ATOM   1225 C CG  . GLN B 2 3   ? 40.75900 4.88300   -0.82400 1.000 71.73586 ? 3   GLN B CG  1 
ATOM   1226 C CD  . GLN B 2 3   ? 41.77200 5.84300   -1.42400 1.000 79.67267 ? 3   GLN B CD  1 
ATOM   1227 O OE1 . GLN B 2 3   ? 42.98300 5.70100   -1.22000 1.000 87.82343 ? 3   GLN B OE1 1 
ATOM   1228 N NE2 . GLN B 2 3   ? 41.28600 6.82100   -2.17400 1.000 81.36341 ? 3   GLN B NE2 1 
ATOM   1229 N N   . VAL B 2 4   ? 39.05200 4.87100   2.56700  1.000 49.87984 ? 4   VAL B N   1 
ATOM   1230 C CA  . VAL B 2 4   ? 37.67100 5.32800   2.74800  1.000 42.75143 ? 4   VAL B CA  1 
ATOM   1231 C C   . VAL B 2 4   ? 37.60900 6.41300   3.81500  1.000 43.65986 ? 4   VAL B C   1 
ATOM   1232 O O   . VAL B 2 4   ? 38.13800 6.25600   4.92200  1.000 44.20080 ? 4   VAL B O   1 
ATOM   1233 C CB  . VAL B 2 4   ? 36.74100 4.15400   3.10100  1.000 50.64298 ? 4   VAL B CB  1 
ATOM   1234 C CG1 . VAL B 2 4   ? 35.44000 4.66600   3.64400  1.000 45.82796 ? 4   VAL B CG1 1 
ATOM   1235 C CG2 . VAL B 2 4   ? 36.48100 3.29100   1.85900  1.000 47.28448 ? 4   VAL B CG2 1 
ATOM   1236 N N   . GLN B 2 5   ? 36.93200 7.51600   3.49700  1.000 40.02134 ? 5   GLN B N   1 
ATOM   1237 C CA  . GLN B 2 5   ? 36.70500 8.57100   4.47000  1.000 39.17383 ? 5   GLN B CA  1 
ATOM   1238 C C   . GLN B 2 5   ? 35.25500 9.00100   4.42600  1.000 37.81979 ? 5   GLN B C   1 
ATOM   1239 O O   . GLN B 2 5   ? 34.64300 9.04300   3.35800  1.000 36.77353 ? 5   GLN B O   1 
ATOM   1240 C CB  . GLN B 2 5   ? 37.59300 9.78900   4.22400  1.000 41.55626 ? 5   GLN B CB  1 
ATOM   1241 C CG  . GLN B 2 5   ? 39.01700 9.56200   4.61300  1.000 45.69377 ? 5   GLN B CG  1 
ATOM   1242 C CD  . GLN B 2 5   ? 39.77800 10.86600  4.73500  1.000 53.15171 ? 5   GLN B CD  1 
ATOM   1243 O OE1 . GLN B 2 5   ? 40.70800 11.12000  3.97100  1.000 55.23353 ? 5   GLN B OE1 1 
ATOM   1244 N NE2 . GLN B 2 5   ? 39.38800 11.69800  5.69800  1.000 50.55291 ? 5   GLN B NE2 1 
ATOM   1245 N N   . LEU B 2 6   ? 34.72400 9.32700   5.59800  1.000 34.20601 ? 6   LEU B N   1 
ATOM   1246 C CA  . LEU B 2 6   ? 33.36500 9.83800   5.76800  1.000 30.79060 ? 6   LEU B CA  1 
ATOM   1247 C C   . LEU B 2 6   ? 33.49600 11.05300  6.67500  1.000 36.29835 ? 6   LEU B C   1 
ATOM   1248 O O   . LEU B 2 6   ? 33.70600 10.88900  7.87900  1.000 39.89561 ? 6   LEU B O   1 
ATOM   1249 C CB  . LEU B 2 6   ? 32.45600 8.78700   6.39800  1.000 29.57070 ? 6   LEU B CB  1 
ATOM   1250 C CG  . LEU B 2 6   ? 32.30500 7.53900   5.55000  1.000 33.67658 ? 6   LEU B CG  1 
ATOM   1251 C CD1 . LEU B 2 6   ? 31.67800 6.44300   6.38300  1.000 37.71937 ? 6   LEU B CD1 1 
ATOM   1252 C CD2 . LEU B 2 6   ? 31.46200 7.84900   4.34400  1.000 37.67580 ? 6   LEU B CD2 1 
ATOM   1253 N N   . VAL B 2 7   ? 33.40700 12.26000  6.12100  1.000 30.40889 ? 7   VAL B N   1 
ATOM   1254 C CA  . VAL B 2 7   ? 33.73400 13.46200  6.89100  1.000 33.10692 ? 7   VAL B CA  1 
ATOM   1255 C C   . VAL B 2 7   ? 32.45700 14.28700  7.05200  1.000 33.85209 ? 7   VAL B C   1 
ATOM   1256 O O   . VAL B 2 7   ? 32.04600 15.02300  6.14200  1.000 32.36889 ? 7   VAL B O   1 
ATOM   1257 C CB  . VAL B 2 7   ? 34.85900 14.27400  6.24500  1.000 34.59965 ? 7   VAL B CB  1 
ATOM   1258 C CG1 . VAL B 2 7   ? 35.23000 15.46200  7.15800  1.000 36.16372 ? 7   VAL B CG1 1 
ATOM   1259 C CG2 . VAL B 2 7   ? 36.10600 13.36400  5.98800  1.000 37.83569 ? 7   VAL B CG2 1 
ATOM   1260 N N   . GLU B 2 8   ? 31.85400 14.20800  8.23400  1.000 29.91416 ? 8   GLU B N   1 
ATOM   1261 C CA  . GLU B 2 8   ? 30.65700 14.99900  8.52900  1.000 34.38324 ? 8   GLU B CA  1 
ATOM   1262 C C   . GLU B 2 8   ? 31.00800 16.42500  8.95500  1.000 33.82213 ? 8   GLU B C   1 
ATOM   1263 O O   . GLU B 2 8   ? 32.04600 16.69600  9.58300  1.000 33.83265 ? 8   GLU B O   1 
ATOM   1264 C CB  . GLU B 2 8   ? 29.81000 14.33700  9.63500  1.000 33.10203 ? 8   GLU B CB  1 
ATOM   1265 C CG  . GLU B 2 8   ? 29.37900 12.88700  9.38800  1.000 31.97818 ? 8   GLU B CG  1 
ATOM   1266 C CD  . GLU B 2 8   ? 30.38100 11.83600  9.92000  1.000 35.10551 ? 8   GLU B CD  1 
ATOM   1267 O OE1 . GLU B 2 8   ? 31.52500 12.16600  10.28900 1.000 36.55369 ? 8   GLU B OE1 1 
ATOM   1268 O OE2 . GLU B 2 8   ? 30.01300 10.66000  9.97300  1.000 34.47099 ? 8   GLU B OE2 1 
ATOM   1269 N N   . SER B 2 9   ? 30.11300 17.35300  8.61100  1.000 29.24823 ? 9   SER B N   1 
ATOM   1270 C CA  . SER B 2 9   ? 30.26400 18.75200  8.99100  1.000 33.78726 ? 9   SER B CA  1 
ATOM   1271 C C   . SER B 2 9   ? 28.87700 19.38400  8.98300  1.000 31.84886 ? 9   SER B C   1 
ATOM   1272 O O   . SER B 2 9   ? 27.88800 18.77400  8.55900  1.000 30.42383 ? 9   SER B O   1 
ATOM   1273 C CB  . SER B 2 9   ? 31.21100 19.51300  8.05400  1.000 34.43381 ? 9   SER B CB  1 
ATOM   1274 O OG  . SER B 2 9   ? 30.68000 19.55100  6.73400  1.000 37.16704 ? 9   SER B OG  1 
ATOM   1275 N N   . GLY B 2 10  ? 28.82000 20.62200  9.45000  1.000 32.59776 ? 10  GLY B N   1 
ATOM   1276 C CA  . GLY B 2 10  ? 27.59400 21.37700  9.40600  1.000 32.29909 ? 10  GLY B CA  1 
ATOM   1277 C C   . GLY B 2 10  ? 26.86900 21.45000  10.72100 1.000 39.31384 ? 10  GLY B C   1 
ATOM   1278 O O   . GLY B 2 10  ? 25.85100 22.13900  10.80400 1.000 36.21963 ? 10  GLY B O   1 
ATOM   1279 N N   . GLY B 2 11  ? 27.34000 20.74700  11.74200 1.000 35.57878 ? 11  GLY B N   1 
ATOM   1280 C CA  . GLY B 2 11  ? 26.67400 20.78300  13.02700 1.000 32.87012 ? 11  GLY B CA  1 
ATOM   1281 C C   . GLY B 2 11  ? 26.91700 22.11000  13.71800 1.000 36.54513 ? 11  GLY B C   1 
ATOM   1282 O O   . GLY B 2 11  ? 27.68200 22.95500  13.27300 1.000 36.17792 ? 11  GLY B O   1 
ATOM   1283 N N   . GLY B 2 12  ? 26.25200 22.29500  14.84800 1.000 36.83084 ? 12  GLY B N   1 
ATOM   1284 C CA  . GLY B 2 12  ? 26.36400 23.55500  15.54400 1.000 37.26545 ? 12  GLY B CA  1 
ATOM   1285 C C   . GLY B 2 12  ? 25.28800 23.66200  16.60300 1.000 33.42708 ? 12  GLY B C   1 
ATOM   1286 O O   . GLY B 2 12  ? 24.55500 22.70900  16.86300 1.000 34.89089 ? 12  GLY B O   1 
ATOM   1287 N N   . LEU B 2 13  ? 25.21900 24.85900  17.20500 1.000 37.87563 ? 13  LEU B N   1 
ATOM   1288 C CA  . LEU B 2 13  ? 24.21300 25.16400  18.24900 1.000 37.08381 ? 13  LEU B CA  1 
ATOM   1289 C C   . LEU B 2 13  ? 23.06000 25.90300  17.57300 1.000 37.65406 ? 13  LEU B C   1 
ATOM   1290 O O   . LEU B 2 13  ? 23.31400 26.90500  16.90300 1.000 37.74584 ? 13  LEU B O   1 
ATOM   1291 C CB  . LEU B 2 13  ? 24.84200 25.99600  19.35900 1.000 38.86831 ? 13  LEU B CB  1 
ATOM   1292 C CG  . LEU B 2 13  ? 23.89400 26.52500  20.43900 1.000 41.24843 ? 13  LEU B CG  1 
ATOM   1293 C CD1 . LEU B 2 13  ? 23.22700 25.40200  21.20700 1.000 41.73719 ? 13  LEU B CD1 1 
ATOM   1294 C CD2 . LEU B 2 13  ? 24.66300 27.42500  21.38500 1.000 45.01277 ? 13  LEU B CD2 1 
ATOM   1295 N N   . VAL B 2 14  ? 21.84700 25.40600  17.75100 1.000 32.87006 ? 14  VAL B N   1 
ATOM   1296 C CA  . VAL B 2 14  ? 20.67900 25.97500  17.03400 1.000 33.78832 ? 14  VAL B CA  1 
ATOM   1297 C C   . VAL B 2 14  ? 19.53200 26.18100  18.02500 1.000 37.19321 ? 14  VAL B C   1 
ATOM   1298 O O   . VAL B 2 14  ? 19.40800 25.39100  18.96200 1.000 36.72991 ? 14  VAL B O   1 
ATOM   1299 C CB  . VAL B 2 14  ? 20.22400 25.06600  15.87600 1.000 39.44814 ? 14  VAL B CB  1 
ATOM   1300 C CG1 . VAL B 2 14  ? 19.11900 25.70300  15.04700 1.000 42.20735 ? 14  VAL B CG1 1 
ATOM   1301 C CG2 . VAL B 2 14  ? 21.38600 24.66800  14.98000 1.000 45.44640 ? 14  VAL B CG2 1 
ATOM   1302 N N   . GLN B 2 15  ? 18.74400 27.22500  17.79700 1.000 37.84339 ? 15  GLN B N   1 
ATOM   1303 C CA  . GLN B 2 15  ? 17.55700 27.47200  18.63900 1.000 37.35155 ? 15  GLN B CA  1 
ATOM   1304 C C   . GLN B 2 15  ? 16.47600 26.45900  18.27400 1.000 38.93249 ? 15  GLN B C   1 
ATOM   1305 O O   . GLN B 2 15  ? 16.27900 26.18600  17.08800 1.000 36.81315 ? 15  GLN B O   1 
ATOM   1306 C CB  . GLN B 2 15  ? 16.98100 28.86700  18.40800 1.000 39.04914 ? 15  GLN B CB  1 
ATOM   1307 C CG  . GLN B 2 15  ? 15.86000 29.26100  19.36400 1.000 47.06783 ? 15  GLN B CG  1 
ATOM   1308 C CD  . GLN B 2 15  ? 16.24600 29.17200  20.82500 1.000 57.55015 ? 15  GLN B CD  1 
ATOM   1309 O OE1 . GLN B 2 15  ? 17.28200 29.68800  21.25200 1.000 56.27715 ? 15  GLN B OE1 1 
ATOM   1310 N NE2 . GLN B 2 15  ? 15.42000 28.49700  21.60800 1.000 53.94193 ? 15  GLN B NE2 1 
ATOM   1311 N N   . ALA B 2 16  ? 15.80100 25.94400  19.28500 1.000 37.34102 ? 16  ALA B N   1 
ATOM   1312 C CA  . ALA B 2 16  ? 14.68300 25.05500  18.99800 1.000 37.79249 ? 16  ALA B CA  1 
ATOM   1313 C C   . ALA B 2 16  ? 13.74700 25.72000  17.99800 1.000 38.32680 ? 16  ALA B C   1 
ATOM   1314 O O   . ALA B 2 16  ? 13.45700 26.92100  18.10100 1.000 40.36009 ? 16  ALA B O   1 
ATOM   1315 C CB  . ALA B 2 16  ? 13.92900 24.70300  20.29200 1.000 39.53043 ? 16  ALA B CB  1 
ATOM   1316 N N   . GLY B 2 17  ? 13.26600 24.92300  17.03200 1.000 37.21674 ? 17  GLY B N   1 
ATOM   1317 C CA  . GLY B 2 17  ? 12.45500 25.40600  15.93300 1.000 38.22382 ? 17  GLY B CA  1 
ATOM   1318 C C   . GLY B 2 17  ? 13.25700 25.77600  14.70000 1.000 36.35528 ? 17  GLY B C   1 
ATOM   1319 O O   . GLY B 2 17  ? 12.66600 25.97600  13.62800 1.000 37.01668 ? 17  GLY B O   1 
ATOM   1320 N N   . GLY B 2 18  ? 14.58100 25.87800  14.83100 1.000 34.38551 ? 18  GLY B N   1 
ATOM   1321 C CA  . GLY B 2 18  ? 15.45700 26.22800  13.72900 1.000 34.99721 ? 18  GLY B CA  1 
ATOM   1322 C C   . GLY B 2 18  ? 15.76400 25.07300  12.77700 1.000 34.58358 ? 18  GLY B C   1 
ATOM   1323 O O   . GLY B 2 18  ? 15.27300 23.94900  12.90400 1.000 32.14756 ? 18  GLY B O   1 
ATOM   1324 N N   . SER B 2 19  ? 16.61300 25.38700  11.79000 1.000 31.89149 ? 19  SER B N   1 
ATOM   1325 C CA  . SER B 2 19  ? 16.96500 24.49000  10.70000 1.000 31.96488 ? 19  SER B CA  1 
ATOM   1326 C C   . SER B 2 19  ? 18.47800 24.37200  10.63600 1.000 30.93470 ? 19  SER B C   1 
ATOM   1327 O O   . SER B 2 19  ? 19.20300 25.30600  11.00700 1.000 33.20335 ? 19  SER B O   1 
ATOM   1328 C CB  . SER B 2 19  ? 16.45000 25.01600  9.32600  1.000 31.66401 ? 19  SER B CB  1 
ATOM   1329 O OG  . SER B 2 19  ? 15.03900 25.18000  9.32300  1.000 32.38803 ? 19  SER B OG  1 
ATOM   1330 N N   . LEU B 2 20  ? 18.94500 23.23200  10.14900 1.000 33.03378 ? 20  LEU B N   1 
ATOM   1331 C CA  . LEU B 2 20  ? 20.37000 23.00400  9.95600  1.000 34.57988 ? 20  LEU B CA  1 
ATOM   1332 C C   . LEU B 2 20  ? 20.53200 22.00100  8.82200  1.000 33.44723 ? 20  LEU B C   1 
ATOM   1333 O O   . LEU B 2 20  ? 19.68700 21.12700  8.65600  1.000 31.12203 ? 20  LEU B O   1 
ATOM   1334 C CB  . LEU B 2 20  ? 20.97400 22.48100  11.25600 1.000 40.54449 ? 20  LEU B CB  1 
ATOM   1335 C CG  . LEU B 2 20  ? 22.43400 22.61200  11.65100 1.000 47.13870 ? 20  LEU B CG  1 
ATOM   1336 C CD1 . LEU B 2 20  ? 22.87800 24.05800  11.76900 1.000 42.60367 ? 20  LEU B CD1 1 
ATOM   1337 C CD2 . LEU B 2 20  ? 22.60300 21.87400  12.97800 1.000 44.87669 ? 20  LEU B CD2 1 
ATOM   1338 N N   . ARG B 2 21  ? 21.60200 22.12100  8.03400  1.000 29.84146 ? 21  ARG B N   1 
ATOM   1339 C CA  . ARG B 2 21  ? 21.89900 21.10200  7.02800  1.000 30.49111 ? 21  ARG B CA  1 
ATOM   1340 C C   . ARG B 2 21  ? 23.25600 20.49100  7.34600  1.000 27.99414 ? 21  ARG B C   1 
ATOM   1341 O O   . ARG B 2 21  ? 24.25100 21.22200  7.45800  1.000 34.15090 ? 21  ARG B O   1 
ATOM   1342 C CB  . ARG B 2 21  ? 21.88700 21.69900  5.61600  1.000 32.33824 ? 21  ARG B CB  1 
ATOM   1343 C CG  . ARG B 2 21  ? 22.06900 20.65300  4.51200  1.000 33.72322 ? 21  ARG B CG  1 
ATOM   1344 C CD  . ARG B 2 21  ? 22.45000 21.32100  3.18900  1.000 43.43997 ? 21  ARG B CD  1 
ATOM   1345 N NE  . ARG B 2 21  ? 23.82400 21.80600  3.26300  1.000 54.01522 ? 21  ARG B NE  1 
ATOM   1346 C CZ  . ARG B 2 21  ? 24.65500 21.91400  2.23300  1.000 55.39566 ? 21  ARG B CZ  1 
ATOM   1347 N NH1 . ARG B 2 21  ? 24.30900 21.51800  1.01800  1.000 57.44833 ? 21  ARG B NH1 1 
ATOM   1348 N NH2 . ARG B 2 21  ? 25.86100 22.44600  2.42600  1.000 64.62840 ? 21  ARG B NH2 1 
ATOM   1349 N N   . LEU B 2 22  ? 23.28900 19.16800  7.52800  1.000 29.53106 ? 22  LEU B N   1 
ATOM   1350 C CA  . LEU B 2 22  ? 24.54400 18.44600  7.70700  1.000 29.51066 ? 22  LEU B CA  1 
ATOM   1351 C C   . LEU B 2 22  ? 25.01900 17.93900  6.35900  1.000 30.05476 ? 22  LEU B C   1 
ATOM   1352 O O   . LEU B 2 22  ? 24.20700 17.63600  5.48100  1.000 28.60764 ? 22  LEU B O   1 
ATOM   1353 C CB  . LEU B 2 22  ? 24.35000 17.24200  8.65000  1.000 29.66194 ? 22  LEU B CB  1 
ATOM   1354 C CG  . LEU B 2 22  ? 23.67300 17.59100  9.99000  1.000 32.92927 ? 22  LEU B CG  1 
ATOM   1355 C CD1 . LEU B 2 22  ? 23.59900 16.32200  10.86500 1.000 33.35581 ? 22  LEU B CD1 1 
ATOM   1356 C CD2 . LEU B 2 22  ? 24.41900 18.72800  10.71600 1.000 30.41195 ? 22  LEU B CD2 1 
ATOM   1357 N N   . SER B 2 23  ? 26.33900 17.79000  6.22800  1.000 31.38465 ? 23  SER B N   1 
ATOM   1358 C CA  . SER B 2 23  ? 26.97300 17.23400  5.04200  1.000 30.07457 ? 23  SER B CA  1 
ATOM   1359 C C   . SER B 2 23  ? 27.93900 16.14500  5.45000  1.000 30.57007 ? 23  SER B C   1 
ATOM   1360 O O   . SER B 2 23  ? 28.59900 16.24500  6.48000  1.000 35.08935 ? 23  SER B O   1 
ATOM   1361 C CB  . SER B 2 23  ? 27.79800 18.29000  4.27200  1.000 33.22017 ? 23  SER B CB  1 
ATOM   1362 O OG  . SER B 2 23  ? 26.98600 19.37600  3.94400  1.000 37.91364 ? 23  SER B OG  1 
ATOM   1363 N N   . CYS B 2 24  ? 28.07100 15.13500  4.59500  1.000 26.58126 ? 24  CYS B N   1 
ATOM   1364 C CA  . CYS B 2 24  ? 29.11200 14.13000  4.73500  1.000 28.17940 ? 24  CYS B CA  1 
ATOM   1365 C C   . CYS B 2 24  ? 29.86100 14.08700  3.41200  1.000 32.35042 ? 24  CYS B C   1 
ATOM   1366 O O   . CYS B 2 24  ? 29.30200 13.66800  2.39400  1.000 32.14771 ? 24  CYS B O   1 
ATOM   1367 C CB  . CYS B 2 24  ? 28.53100 12.75900  5.05800  1.000 29.13646 ? 24  CYS B CB  1 
ATOM   1368 S SG  . CYS B 2 24  ? 29.83700 11.52000  5.20700  1.000 35.54363 ? 24  CYS B SG  1 
ATOM   1369 N N   . ALA B 2 25  ? 31.12100 14.48300  3.43200  1.000 31.53887 ? 25  ALA B N   1 
ATOM   1370 C CA  . ALA B 2 25  ? 31.96600 14.42300  2.24700  1.000 32.10191 ? 25  ALA B CA  1 
ATOM   1371 C C   . ALA B 2 25  ? 32.70300 13.09400  2.28200  1.000 36.59304 ? 25  ALA B C   1 
ATOM   1372 O O   . ALA B 2 25  ? 33.47700 12.85400  3.21000  1.000 36.36903 ? 25  ALA B O   1 
ATOM   1373 C CB  . ALA B 2 25  ? 32.94500 15.59400  2.23900  1.000 35.38625 ? 25  ALA B CB  1 
ATOM   1374 N N   . ALA B 2 26  ? 32.46100 12.23800  1.29000  1.000 31.44199 ? 26  ALA B N   1 
ATOM   1375 C CA  . ALA B 2 26  ? 33.00700 10.89300  1.24700  1.000 33.36117 ? 26  ALA B CA  1 
ATOM   1376 C C   . ALA B 2 26  ? 34.11900 10.80600  0.21700  1.000 36.70192 ? 26  ALA B C   1 
ATOM   1377 O O   . ALA B 2 26  ? 34.10200 11.51400  -0.79100 1.000 35.67202 ? 26  ALA B O   1 
ATOM   1378 C CB  . ALA B 2 26  ? 31.92800 9.86300   0.89000  1.000 34.41826 ? 26  ALA B CB  1 
ATOM   1379 N N   . SER B 2 27  ? 35.07400 9.91200   0.47000  1.000 35.87822 ? 27  SER B N   1 
ATOM   1380 C CA  . SER B 2 27  ? 36.09700 9.60700   -0.50700 1.000 38.00195 ? 27  SER B CA  1 
ATOM   1381 C C   . SER B 2 27  ? 36.41600 8.12300   -0.42200 1.000 39.88926 ? 27  SER B C   1 
ATOM   1382 O O   . SER B 2 27  ? 36.18200 7.47200   0.60400  1.000 40.62157 ? 27  SER B O   1 
ATOM   1383 C CB  . SER B 2 27  ? 37.36500 10.44600  -0.28900 1.000 48.03443 ? 27  SER B CB  1 
ATOM   1384 O OG  . SER B 2 27  ? 37.98400 10.08700  0.92900  1.000 51.42892 ? 27  SER B OG  1 
ATOM   1385 N N   . GLY B 2 28  ? 36.95000 7.59500   -1.52300 1.000 40.07263 ? 28  GLY B N   1 
ATOM   1386 C CA  . GLY B 2 28  ? 37.33400 6.20100   -1.60400 1.000 41.65297 ? 28  GLY B CA  1 
ATOM   1387 C C   . GLY B 2 28  ? 36.26900 5.27800   -2.15700 1.000 40.02009 ? 28  GLY B C   1 
ATOM   1388 O O   . GLY B 2 28  ? 36.56000 4.09800   -2.38200 1.000 42.91131 ? 28  GLY B O   1 
ATOM   1389 N N   . PHE B 2 29  ? 35.05800 5.77400   -2.38800 1.000 38.25830 ? 29  PHE B N   1 
ATOM   1390 C CA  . PHE B 2 29  ? 33.93500 4.97900   -2.88500 1.000 40.75914 ? 29  PHE B CA  1 
ATOM   1391 C C   . PHE B 2 29  ? 32.86800 5.95200   -3.39400 1.000 35.31912 ? 29  PHE B C   1 
ATOM   1392 O O   . PHE B 2 29  ? 32.82400 7.11000   -2.95800 1.000 36.44816 ? 29  PHE B O   1 
ATOM   1393 C CB  . PHE B 2 29  ? 33.34800 4.08400   -1.77900 1.000 38.89042 ? 29  PHE B CB  1 
ATOM   1394 C CG  . PHE B 2 29  ? 32.55900 4.85700   -0.74800 1.000 37.01080 ? 29  PHE B CG  1 
ATOM   1395 C CD1 . PHE B 2 29  ? 33.21000 5.52700   0.28500  1.000 37.04197 ? 29  PHE B CD1 1 
ATOM   1396 C CD2 . PHE B 2 29  ? 31.17600 4.97600   -0.85200 1.000 34.73398 ? 29  PHE B CD2 1 
ATOM   1397 C CE1 . PHE B 2 29  ? 32.48700 6.28500   1.21400  1.000 32.58491 ? 29  PHE B CE1 1 
ATOM   1398 C CE2 . PHE B 2 29  ? 30.45200 5.69900   0.06600  1.000 35.85295 ? 29  PHE B CE2 1 
ATOM   1399 C CZ  . PHE B 2 29  ? 31.10300 6.36800   1.09500  1.000 35.86606 ? 29  PHE B CZ  1 
ATOM   1400 N N   . PRO B 2 30  ? 31.96700 5.50000   -4.29500 1.000 38.96496 ? 30  PRO B N   1 
ATOM   1401 C CA  . PRO B 2 30  ? 30.91300 6.40300   -4.77000 1.000 35.22763 ? 30  PRO B CA  1 
ATOM   1402 C C   . PRO B 2 30  ? 29.66200 6.32200   -3.91300 1.000 33.02773 ? 30  PRO B C   1 
ATOM   1403 O O   . PRO B 2 30  ? 29.11300 5.23300   -3.70400 1.000 34.32863 ? 30  PRO B O   1 
ATOM   1404 C CB  . PRO B 2 30  ? 30.64000 5.91700   -6.20300 1.000 38.53243 ? 30  PRO B CB  1 
ATOM   1405 C CG  . PRO B 2 30  ? 31.56000 4.71300   -6.42200 1.000 40.70226 ? 30  PRO B CG  1 
ATOM   1406 C CD  . PRO B 2 30  ? 31.95800 4.23900   -5.05900 1.000 43.54689 ? 30  PRO B CD  1 
ATOM   1407 N N   . VAL B 2 31  ? 29.20200 7.46900   -3.40800 1.000 32.25483 ? 31  VAL B N   1 
ATOM   1408 C CA  . VAL B 2 31  ? 28.04300 7.43900   -2.51000 1.000 32.20149 ? 31  VAL B CA  1 
ATOM   1409 C C   . VAL B 2 31  ? 26.81200 6.89300   -3.22400 1.000 30.38318 ? 31  VAL B C   1 
ATOM   1410 O O   . VAL B 2 31  ? 25.90800 6.36000   -2.57600 1.000 32.30108 ? 31  VAL B O   1 
ATOM   1411 C CB  . VAL B 2 31  ? 27.75200 8.82200   -1.88300 1.000 34.05593 ? 31  VAL B CB  1 
ATOM   1412 C CG1 . VAL B 2 31  ? 28.91600 9.28000   -0.96700 1.000 34.45838 ? 31  VAL B CG1 1 
ATOM   1413 C CG2 . VAL B 2 31  ? 27.44500 9.87700   -2.93100 1.000 30.80155 ? 31  VAL B CG2 1 
ATOM   1414 N N   . ASN B 2 32  ? 26.74700 7.00300   -4.56000 1.000 33.30317 ? 32  ASN B N   1 
ATOM   1415 C CA  . ASN B 2 32  ? 25.54600 6.51000   -5.22800 1.000 32.81746 ? 32  ASN B CA  1 
ATOM   1416 C C   . ASN B 2 32  ? 25.58200 4.99900   -5.43800 1.000 37.80826 ? 32  ASN B C   1 
ATOM   1417 O O   . ASN B 2 32  ? 24.61300 4.43600   -5.97000 1.000 39.58532 ? 32  ASN B O   1 
ATOM   1418 C CB  . ASN B 2 32  ? 25.32300 7.21400   -6.57400 1.000 36.04637 ? 32  ASN B CB  1 
ATOM   1419 C CG  . ASN B 2 32  ? 26.52000 7.13100   -7.48700 1.000 41.76590 ? 32  ASN B CG  1 
ATOM   1420 O OD1 . ASN B 2 32  ? 27.63200 7.44600   -7.08200 1.000 46.60985 ? 32  ASN B OD1 1 
ATOM   1421 N ND2 . ASN B 2 32  ? 26.29800 6.75300   -8.73800 1.000 43.53445 ? 32  ASN B ND2 1 
ATOM   1422 N N   . HIS B 2 33  ? 26.66100 4.33100   -5.03100 1.000 33.35683 ? 33  HIS B N   1 
ATOM   1423 C CA  . HIS B 2 33  ? 26.74600 2.87000   -5.11300 1.000 37.64666 ? 33  HIS B CA  1 
ATOM   1424 C C   . HIS B 2 33  ? 26.61200 2.18300   -3.76000 1.000 34.66992 ? 33  HIS B C   1 
ATOM   1425 O O   . HIS B 2 33  ? 26.69900 0.94300   -3.68600 1.000 36.94581 ? 33  HIS B O   1 
ATOM   1426 C CB  . HIS B 2 33  ? 28.06500 2.45400   -5.77200 1.000 40.89534 ? 33  HIS B CB  1 
ATOM   1427 C CG  . HIS B 2 33  ? 28.11400 2.75400   -7.23500 1.000 45.55104 ? 33  HIS B CG  1 
ATOM   1428 N ND1 . HIS B 2 33  ? 29.12700 2.31200   -8.05400 1.000 49.32064 ? 33  HIS B ND1 1 
ATOM   1429 C CD2 . HIS B 2 33  ? 27.26000 3.44500   -8.03000 1.000 45.20682 ? 33  HIS B CD2 1 
ATOM   1430 C CE1 . HIS B 2 33  ? 28.90200 2.72200   -9.29100 1.000 53.83948 ? 33  HIS B CE1 1 
ATOM   1431 N NE2 . HIS B 2 33  ? 27.77400 3.40900   -9.30400 1.000 52.22416 ? 33  HIS B NE2 1 
ATOM   1432 N N   . ARG B 2 34  ? 26.39200 2.95200   -2.69600 1.000 35.80037 ? 34  ARG B N   1 
ATOM   1433 C CA  . ARG B 2 34  ? 26.18400 2.42400   -1.36100 1.000 33.79057 ? 34  ARG B CA  1 
ATOM   1434 C C   . ARG B 2 34  ? 24.86400 2.93900   -0.80900 1.000 31.60831 ? 34  ARG B C   1 
ATOM   1435 O O   . ARG B 2 34  ? 24.33900 3.96300   -1.24800 1.000 32.68320 ? 34  ARG B O   1 
ATOM   1436 C CB  . ARG B 2 34  ? 27.33400 2.82400   -0.41100 1.000 33.11326 ? 34  ARG B CB  1 
ATOM   1437 C CG  . ARG B 2 34  ? 28.72300 2.39000   -0.92600 1.000 36.21006 ? 34  ARG B CG  1 
ATOM   1438 C CD  . ARG B 2 34  ? 28.93000 0.84900   -0.97600 1.000 42.61231 ? 34  ARG B CD  1 
ATOM   1439 N NE  . ARG B 2 34  ? 30.31000 0.57300   -1.39200 1.000 50.47877 ? 34  ARG B NE  1 
ATOM   1440 C CZ  . ARG B 2 34  ? 30.73100 0.52700   -2.65200 1.000 50.80359 ? 34  ARG B CZ  1 
ATOM   1441 N NH1 . ARG B 2 34  ? 29.88900 0.65200   -3.67000 1.000 49.59199 ? 34  ARG B NH1 1 
ATOM   1442 N NH2 . ARG B 2 34  ? 32.02600 0.33400   -2.89900 1.000 57.12711 ? 34  ARG B NH2 1 
ATOM   1443 N N   . THR B 2 35  ? 24.34500 2.22600   0.18000  1.000 33.10873 ? 35  THR B N   1 
ATOM   1444 C CA  . THR B 2 35  ? 23.18300 2.68100   0.93800  1.000 32.71192 ? 35  THR B CA  1 
ATOM   1445 C C   . THR B 2 35  ? 23.68600 3.54900   2.08100  1.000 32.03811 ? 35  THR B C   1 
ATOM   1446 O O   . THR B 2 35  ? 24.31200 3.03600   3.01200  1.000 34.24656 ? 35  THR B O   1 
ATOM   1447 C CB  . THR B 2 35  ? 22.41000 1.48300   1.46500  1.000 34.01934 ? 35  THR B CB  1 
ATOM   1448 O OG1 . THR B 2 35  ? 22.04800 0.64700   0.36200  1.000 37.22215 ? 35  THR B OG1 1 
ATOM   1449 C CG2 . THR B 2 35  ? 21.16300 1.94700   2.26400  1.000 35.54606 ? 35  THR B CG2 1 
ATOM   1450 N N   . MET B 2 36  ? 23.43800 4.85300   2.00500  1.000 30.15097 ? 36  MET B N   1 
ATOM   1451 C CA  . MET B 2 36  ? 23.99800 5.78800   2.96400  1.000 32.42733 ? 36  MET B CA  1 
ATOM   1452 C C   . MET B 2 36  ? 22.94100 6.09000   4.01500  1.000 32.59412 ? 36  MET B C   1 
ATOM   1453 O O   . MET B 2 36  ? 21.76700 6.29400   3.68800  1.000 30.32337 ? 36  MET B O   1 
ATOM   1454 C CB  . MET B 2 36  ? 24.46400 7.07800   2.27600  1.000 29.06898 ? 36  MET B CB  1 
ATOM   1455 C CG  . MET B 2 36  ? 25.52300 6.82000   1.17900  1.000 29.60948 ? 36  MET B CG  1 
ATOM   1456 S SD  . MET B 2 36  ? 27.03700 5.99700   1.78400  1.000 32.28294 ? 36  MET B SD  1 
ATOM   1457 C CE  . MET B 2 36  ? 27.62600 7.10700   3.07000  1.000 30.65244 ? 36  MET B CE  1 
ATOM   1458 N N   . ALA B 2 37  ? 23.35300 6.11300   5.28100  1.000 29.24072 ? 37  ALA B N   1 
ATOM   1459 C CA  . ALA B 2 37  ? 22.39400 6.33000   6.35500  1.000 27.64896 ? 37  ALA B CA  1 
ATOM   1460 C C   . ALA B 2 37  ? 22.98300 7.28900   7.37600  1.000 31.15746 ? 37  ALA B C   1 
ATOM   1461 O O   . ALA B 2 37  ? 24.19600 7.30500   7.59700  1.000 31.04894 ? 37  ALA B O   1 
ATOM   1462 C CB  . ALA B 2 37  ? 22.01200 5.01700   7.05700  1.000 29.89903 ? 37  ALA B CB  1 
ATOM   1463 N N   . TRP B 2 38  ? 22.11100 8.09200   7.98100  1.000 28.58891 ? 38  TRP B N   1 
ATOM   1464 C CA  . TRP B 2 38  ? 22.48400 8.94400   9.10300  1.000 30.52620 ? 38  TRP B CA  1 
ATOM   1465 C C   . TRP B 2 38  ? 21.96300 8.29300   10.37400 1.000 29.60289 ? 38  TRP B C   1 
ATOM   1466 O O   . TRP B 2 38  ? 20.80900 7.85900   10.42000 1.000 28.98158 ? 38  TRP B O   1 
ATOM   1467 C CB  . TRP B 2 38  ? 21.91100 10.35700  8.97500  1.000 28.30314 ? 38  TRP B CB  1 
ATOM   1468 C CG  . TRP B 2 38  ? 22.57400 11.22200  7.92300  1.000 30.14051 ? 38  TRP B CG  1 
ATOM   1469 C CD1 . TRP B 2 38  ? 22.17200 11.37400  6.61100  1.000 31.02900 ? 38  TRP B CD1 1 
ATOM   1470 C CD2 . TRP B 2 38  ? 23.68900 12.09600  8.10000  1.000 29.87698 ? 38  TRP B CD2 1 
ATOM   1471 N NE1 . TRP B 2 38  ? 22.99200 12.27700  5.97100  1.000 28.31286 ? 38  TRP B NE1 1 
ATOM   1472 C CE2 . TRP B 2 38  ? 23.93500 12.72800  6.85300  1.000 28.89558 ? 38  TRP B CE2 1 
ATOM   1473 C CE3 . TRP B 2 38  ? 24.51500 12.41100  9.18600  1.000 28.68814 ? 38  TRP B CE3 1 
ATOM   1474 C CZ2 . TRP B 2 38  ? 24.96500 13.64300  6.67300  1.000 30.53873 ? 38  TRP B CZ2 1 
ATOM   1475 C CZ3 . TRP B 2 38  ? 25.52500 13.31200  9.00500  1.000 29.23871 ? 38  TRP B CZ3 1 
ATOM   1476 C CH2 . TRP B 2 38  ? 25.75700 13.91600  7.75900  1.000 31.64428 ? 38  TRP B CH2 1 
ATOM   1477 N N   . TYR B 2 39  ? 22.81900 8.20500   11.38600 1.000 29.57743 ? 39  TYR B N   1 
ATOM   1478 C CA  . TYR B 2 39  ? 22.36200 7.86600   12.72100 1.000 27.51807 ? 39  TYR B CA  1 
ATOM   1479 C C   . TYR B 2 39  ? 22.96000 8.87500   13.68700 1.000 29.88632 ? 39  TYR B C   1 
ATOM   1480 O O   . TYR B 2 39  ? 23.88200 9.61900   13.35300 1.000 28.71124 ? 39  TYR B O   1 
ATOM   1481 C CB  . TYR B 2 39  ? 22.68600 6.42700   13.14300 1.000 31.74164 ? 39  TYR B CB  1 
ATOM   1482 C CG  . TYR B 2 39  ? 24.14300 6.02400   13.30400 1.000 33.61374 ? 39  TYR B CG  1 
ATOM   1483 C CD1 . TYR B 2 39  ? 24.91300 6.46200   14.39900 1.000 33.89047 ? 39  TYR B CD1 1 
ATOM   1484 C CD2 . TYR B 2 39  ? 24.71300 5.11100   12.42500 1.000 35.50250 ? 39  TYR B CD2 1 
ATOM   1485 C CE1 . TYR B 2 39  ? 26.23900 6.03200   14.56800 1.000 34.70879 ? 39  TYR B CE1 1 
ATOM   1486 C CE2 . TYR B 2 39  ? 26.03400 4.65800   12.59400 1.000 40.65023 ? 39  TYR B CE2 1 
ATOM   1487 C CZ  . TYR B 2 39  ? 26.78900 5.14100   13.65500 1.000 39.03972 ? 39  TYR B CZ  1 
ATOM   1488 O OH  . TYR B 2 39  ? 28.08500 4.69000   13.79700 1.000 42.01982 ? 39  TYR B OH  1 
ATOM   1489 N N   . ARG B 2 40  ? 22.40100 8.91400   14.88300 1.000 29.81622 ? 40  ARG B N   1 
ATOM   1490 C CA  . ARG B 2 40  ? 22.85100 9.87400   15.87000 1.000 30.83630 ? 40  ARG B CA  1 
ATOM   1491 C C   . ARG B 2 40  ? 23.03700 9.16100   17.19400 1.000 33.44848 ? 40  ARG B C   1 
ATOM   1492 O O   . ARG B 2 40  ? 22.39800 8.13500   17.47500 1.000 33.49243 ? 40  ARG B O   1 
ATOM   1493 C CB  . ARG B 2 40  ? 21.84600 11.03900  16.00700 1.000 27.89885 ? 40  ARG B CB  1 
ATOM   1494 C CG  . ARG B 2 40  ? 20.48400 10.59100  16.49000 1.000 30.89346 ? 40  ARG B CG  1 
ATOM   1495 C CD  . ARG B 2 40  ? 19.48500 11.77600  16.48000 1.000 33.16689 ? 40  ARG B CD  1 
ATOM   1496 N NE  . ARG B 2 40  ? 18.12100 11.38700  16.83700 1.000 35.96739 ? 40  ARG B NE  1 
ATOM   1497 C CZ  . ARG B 2 40  ? 17.08000 12.20600  16.75600 1.000 39.32712 ? 40  ARG B CZ  1 
ATOM   1498 N NH1 . ARG B 2 40  ? 17.19500 13.41000  16.22500 1.000 34.87876 ? 40  ARG B NH1 1 
ATOM   1499 N NH2 . ARG B 2 40  ? 15.89900 11.81700  17.24400 1.000 39.64623 ? 40  ARG B NH2 1 
ATOM   1500 N N   . GLN B 2 41  ? 23.95600 9.68500   17.99300 1.000 33.64568 ? 41  GLN B N   1 
ATOM   1501 C CA  . GLN B 2 41  ? 24.24400 9.06300   19.27300 1.000 36.15053 ? 41  GLN B CA  1 
ATOM   1502 C C   . GLN B 2 41  ? 24.40200 10.14200  20.32600 1.000 38.50653 ? 41  GLN B C   1 
ATOM   1503 O O   . GLN B 2 41  ? 25.23800 11.03800  20.18000 1.000 38.67742 ? 41  GLN B O   1 
ATOM   1504 C CB  . GLN B 2 41  ? 25.50000 8.19500   19.21200 1.000 39.14951 ? 41  GLN B CB  1 
ATOM   1505 C CG  . GLN B 2 41  ? 25.65700 7.29500   20.46100 1.000 46.99231 ? 41  GLN B CG  1 
ATOM   1506 C CD  . GLN B 2 41  ? 26.50400 6.08900   20.17500 1.000 45.76827 ? 41  GLN B CD  1 
ATOM   1507 O OE1 . GLN B 2 41  ? 27.28800 6.08000   19.22500 1.000 63.29909 ? 41  GLN B OE1 1 
ATOM   1508 N NE2 . GLN B 2 41  ? 26.34000 5.05500   20.96700 1.000 59.51781 ? 41  GLN B NE2 1 
ATOM   1509 N N   . ALA B 2 42  ? 23.61700 10.04600  21.35300 1.000 41.38429 ? 42  ALA B N   1 
ATOM   1510 C CA  . ALA B 2 42  ? 23.70200 10.82400  22.56600 1.000 44.76389 ? 42  ALA B CA  1 
ATOM   1511 C C   . ALA B 2 42  ? 24.56200 10.07300  23.57500 1.000 52.57209 ? 42  ALA B C   1 
ATOM   1512 O O   . ALA B 2 42  ? 24.56300 8.83800   23.59200 1.000 52.80786 ? 42  ALA B O   1 
ATOM   1513 C CB  . ALA B 2 42  ? 22.30500 11.06200  23.14400 1.000 46.60745 ? 42  ALA B CB  1 
ATOM   1514 N N   . PRO B 2 43  ? 25.32500 10.78400  24.40200 1.000 52.45758 ? 43  PRO B N   1 
ATOM   1515 C CA  . PRO B 2 43  ? 26.18700 10.10000  25.37300 1.000 58.03708 ? 43  PRO B CA  1 
ATOM   1516 C C   . PRO B 2 43  ? 25.37800 9.21000   26.30500 1.000 63.33364 ? 43  PRO B C   1 
ATOM   1517 O O   . PRO B 2 43  ? 24.30300 9.58700   26.78100 1.000 64.60756 ? 43  PRO B O   1 
ATOM   1518 C CB  . PRO B 2 43  ? 26.86100 11.25600  26.11900 1.000 60.16933 ? 43  PRO B CB  1 
ATOM   1519 C CG  . PRO B 2 43  ? 26.89900 12.34300  25.09200 1.000 54.36547 ? 43  PRO B CG  1 
ATOM   1520 C CD  . PRO B 2 43  ? 25.59100 12.22800  24.35700 1.000 50.68686 ? 43  PRO B CD  1 
ATOM   1521 N N   . GLY B 2 44  ? 25.89100 8.00000   26.52400 1.000 68.12464 ? 44  GLY B N   1 
ATOM   1522 C CA  . GLY B 2 44  ? 25.23200 7.02300   27.36400 1.000 74.06612 ? 44  GLY B CA  1 
ATOM   1523 C C   . GLY B 2 44  ? 23.99600 6.38400   26.77800 1.000 73.01843 ? 44  GLY B C   1 
ATOM   1524 O O   . GLY B 2 44  ? 23.31400 5.64200   27.48900 1.000 84.71333 ? 44  GLY B O   1 
ATOM   1525 N N   . LYS B 2 45  ? 23.67500 6.64200   25.51500 1.000 67.60180 ? 45  LYS B N   1 
ATOM   1526 C CA  . LYS B 2 45  ? 22.46800 6.10900   24.90400 1.000 66.67207 ? 45  LYS B CA  1 
ATOM   1527 C C   . LYS B 2 45  ? 22.81500 5.26800   23.68300 1.000 58.59189 ? 45  LYS B C   1 
ATOM   1528 O O   . LYS B 2 45  ? 23.92000 5.33600   23.13800 1.000 57.21661 ? 45  LYS B O   1 
ATOM   1529 C CB  . LYS B 2 45  ? 21.49300 7.22800   24.50300 1.000 62.67448 ? 45  LYS B CB  1 
ATOM   1530 C CG  . LYS B 2 45  ? 20.95200 7.99900   25.69600 1.000 65.08657 ? 45  LYS B CG  1 
ATOM   1531 C CD  . LYS B 2 45  ? 19.73500 8.83000   25.31900 1.000 73.09354 ? 45  LYS B CD  1 
ATOM   1532 C CE  . LYS B 2 45  ? 19.02700 9.35500   26.56900 1.000 77.21112 ? 45  LYS B CE  1 
ATOM   1533 N NZ  . LYS B 2 45  ? 17.71200 9.97400   26.24000 1.000 81.28814 ? 45  LYS B NZ  1 
ATOM   1534 N N   . GLU B 2 46  ? 21.85100 4.45300   23.27600 1.000 60.71357 ? 46  GLU B N   1 
ATOM   1535 C CA  . GLU B 2 46  ? 22.00000 3.64600   22.07700 1.000 58.67452 ? 46  GLU B CA  1 
ATOM   1536 C C   . GLU B 2 46  ? 21.89400 4.52100   20.83100 1.000 53.33733 ? 46  GLU B C   1 
ATOM   1537 O O   . GLU B 2 46  ? 21.23700 5.56800   20.84000 1.000 51.19930 ? 46  GLU B O   1 
ATOM   1538 C CB  . GLU B 2 46  ? 20.93500 2.55800   22.06500 1.000 57.98670 ? 46  GLU B CB  1 
ATOM   1539 C CG  . GLU B 2 46  ? 20.89700 1.76800   23.35800 1.000 75.07076 ? 46  GLU B CG  1 
ATOM   1540 C CD  . GLU B 2 46  ? 19.72500 0.82000   23.42600 1.000 83.95102 ? 46  GLU B CD  1 
ATOM   1541 O OE1 . GLU B 2 46  ? 19.07600 0.61100   22.37800 1.000 85.43810 ? 46  GLU B OE1 1 
ATOM   1542 O OE2 . GLU B 2 46  ? 19.45300 0.28300   24.52400 1.000 94.67764 ? 46  GLU B OE2 1 
ATOM   1543 N N   . ARG B 2 47  ? 22.56100 4.08800   19.75200 1.000 47.13058 ? 47  ARG B N   1 
ATOM   1544 C CA  . ARG B 2 47  ? 22.45400 4.78900   18.47800 1.000 44.71860 ? 47  ARG B CA  1 
ATOM   1545 C C   . ARG B 2 47  ? 21.00500 4.81700   18.02500 1.000 42.20677 ? 47  ARG B C   1 
ATOM   1546 O O   . ARG B 2 47  ? 20.26700 3.84200   18.19400 1.000 42.68267 ? 47  ARG B O   1 
ATOM   1547 C CB  . ARG B 2 47  ? 23.28000 4.10000   17.38100 1.000 48.54879 ? 47  ARG B CB  1 
ATOM   1548 C CG  . ARG B 2 47  ? 24.75000 3.98800   17.62100 1.000 53.34066 ? 47  ARG B CG  1 
ATOM   1549 C CD  . ARG B 2 47  ? 25.40700 3.23900   16.46500 1.000 50.04083 ? 47  ARG B CD  1 
ATOM   1550 N NE  . ARG B 2 47  ? 26.84600 3.17300   16.66900 1.000 52.84658 ? 47  ARG B NE  1 
ATOM   1551 C CZ  . ARG B 2 47  ? 27.46200 2.27000   17.41600 1.000 55.46819 ? 47  ARG B CZ  1 
ATOM   1552 N NH1 . ARG B 2 47  ? 26.80200 1.26700   17.98100 1.000 63.45532 ? 47  ARG B NH1 1 
ATOM   1553 N NH2 . ARG B 2 47  ? 28.77300 2.37800   17.61200 1.000 67.36173 ? 47  ARG B NH2 1 
ATOM   1554 N N   . GLU B 2 48  ? 20.60300 5.91900   17.40900 1.000 36.32834 ? 48  GLU B N   1 
ATOM   1555 C CA  . GLU B 2 48  ? 19.28400 6.00900   16.79500 1.000 36.90422 ? 48  GLU B CA  1 
ATOM   1556 C C   . GLU B 2 48  ? 19.47700 6.27800   15.31200 1.000 30.99276 ? 48  GLU B C   1 
ATOM   1557 O O   . GLU B 2 48  ? 19.99600 7.33200   14.93600 1.000 30.79018 ? 48  GLU B O   1 
ATOM   1558 C CB  . GLU B 2 48  ? 18.43600 7.10100   17.43000 1.000 37.24914 ? 48  GLU B CB  1 
ATOM   1559 C CG  . GLU B 2 48  ? 17.04100 7.13500   16.86100 1.000 37.16155 ? 48  GLU B CG  1 
ATOM   1560 C CD  . GLU B 2 48  ? 16.20500 8.27400   17.42300 1.000 39.37042 ? 48  GLU B CD  1 
ATOM   1561 O OE1 . GLU B 2 48  ? 16.77300 9.17800   18.07800 1.000 40.31644 ? 48  GLU B OE1 1 
ATOM   1562 O OE2 . GLU B 2 48  ? 14.97500 8.25400   17.21000 1.000 40.63475 ? 48  GLU B OE2 1 
ATOM   1563 N N   . TRP B 2 49  ? 19.06900 5.32400   14.47200 1.000 33.27832 ? 49  TRP B N   1 
ATOM   1564 C CA  . TRP B 2 49  ? 19.14900 5.51700   13.02600 1.000 29.76458 ? 49  TRP B CA  1 
ATOM   1565 C C   . TRP B 2 49  ? 17.98400 6.39100   12.57800 1.000 30.45283 ? 49  TRP B C   1 
ATOM   1566 O O   . TRP B 2 49  ? 16.83000 6.12600   12.95500 1.000 32.70139 ? 49  TRP B O   1 
ATOM   1567 C CB  . TRP B 2 49  ? 19.10100 4.15200   12.33500 1.000 30.18436 ? 49  TRP B CB  1 
ATOM   1568 C CG  . TRP B 2 49  ? 20.26700 3.31200   12.68400 1.000 31.75711 ? 49  TRP B CG  1 
ATOM   1569 C CD1 . TRP B 2 49  ? 20.52200 2.70700   13.89200 1.000 34.62587 ? 49  TRP B CD1 1 
ATOM   1570 C CD2 . TRP B 2 49  ? 21.36700 2.97700   11.82500 1.000 33.77434 ? 49  TRP B CD2 1 
ATOM   1571 N NE1 . TRP B 2 49  ? 21.71200 2.01200   13.82700 1.000 36.48621 ? 49  TRP B NE1 1 
ATOM   1572 C CE2 . TRP B 2 49  ? 22.24500 2.15600   12.57000 1.000 30.93660 ? 49  TRP B CE2 1 
ATOM   1573 C CE3 . TRP B 2 49  ? 21.69200 3.28800   10.49400 1.000 33.95692 ? 49  TRP B CE3 1 
ATOM   1574 C CZ2 . TRP B 2 49  ? 23.43000 1.64300   12.03300 1.000 35.39771 ? 49  TRP B CZ2 1 
ATOM   1575 C CZ3 . TRP B 2 49  ? 22.87600 2.76600   9.95900  1.000 35.64027 ? 49  TRP B CZ3 1 
ATOM   1576 C CH2 . TRP B 2 49  ? 23.72500 1.95500   10.72900 1.000 36.02815 ? 49  TRP B CH2 1 
ATOM   1577 N N   . VAL B 2 50  ? 18.26400 7.42300   11.78200 1.000 29.60297 ? 50  VAL B N   1 
ATOM   1578 C CA  . VAL B 2 50  ? 17.20400 8.39000   11.50300 1.000 31.83156 ? 50  VAL B CA  1 
ATOM   1579 C C   . VAL B 2 50  ? 16.84500 8.52000   10.02600 1.000 30.62725 ? 50  VAL B C   1 
ATOM   1580 O O   . VAL B 2 50  ? 15.70900 8.88800   9.71000  1.000 30.18601 ? 50  VAL B O   1 
ATOM   1581 C CB  . VAL B 2 50  ? 17.53600 9.78100   12.08300 1.000 31.93030 ? 50  VAL B CB  1 
ATOM   1582 C CG1 . VAL B 2 50  ? 17.60400 9.70500   13.61300 1.000 34.09553 ? 50  VAL B CG1 1 
ATOM   1583 C CG2 . VAL B 2 50  ? 18.82800 10.35200  11.53900 1.000 30.56141 ? 50  VAL B CG2 1 
ATOM   1584 N N   . ALA B 2 51  ? 17.78800 8.26000   9.11600  1.000 30.31193 ? 51  ALA B N   1 
ATOM   1585 C CA  . ALA B 2 51  ? 17.46200 8.47200   7.70200  1.000 29.35217 ? 51  ALA B CA  1 
ATOM   1586 C C   . ALA B 2 51  ? 18.40200 7.64800   6.84000  1.000 29.48506 ? 51  ALA B C   1 
ATOM   1587 O O   . ALA B 2 51  ? 19.56100 7.43300   7.20400  1.000 27.88445 ? 51  ALA B O   1 
ATOM   1588 C CB  . ALA B 2 51  ? 17.54600 9.96900   7.31600  1.000 29.40884 ? 51  ALA B CB  1 
ATOM   1589 N N   . ALA B 2 52  ? 17.89900 7.18000   5.69300  1.000 28.85734 ? 52  ALA B N   1 
ATOM   1590 C CA  . ALA B 2 52  ? 18.77300 6.45300   4.77500  1.000 26.56967 ? 52  ALA B CA  1 
ATOM   1591 C C   . ALA B 2 52  ? 18.31500 6.64300   3.33700  1.000 28.37580 ? 52  ALA B C   1 
ATOM   1592 O O   . ALA B 2 52  ? 17.13100 6.87500   3.07500  1.000 27.45000 ? 52  ALA B O   1 
ATOM   1593 C CB  . ALA B 2 52  ? 18.81800 4.95400   5.08500  1.000 27.75006 ? 52  ALA B CB  1 
ATOM   1594 N N   . ILE B 2 53  ? 19.26200 6.48000   2.40800  1.000 28.83143 ? 53  ILE B N   1 
ATOM   1595 C CA  . ILE B 2 53  ? 18.98000 6.60400   0.98100  1.000 27.45927 ? 53  ILE B CA  1 
ATOM   1596 C C   . ILE B 2 53  ? 19.63700 5.42400   0.25500  1.000 32.69279 ? 53  ILE B C   1 
ATOM   1597 O O   . ILE B 2 53  ? 20.82500 5.12800   0.45600  1.000 30.52055 ? 53  ILE B O   1 
ATOM   1598 C CB  . ILE B 2 53  ? 19.43300 7.97600   0.43300  1.000 27.75796 ? 53  ILE B CB  1 
ATOM   1599 C CG1 . ILE B 2 53  ? 19.02900 8.14500   -1.03800 1.000 29.75145 ? 53  ILE B CG1 1 
ATOM   1600 C CG2 . ILE B 2 53  ? 20.96900 8.18300   0.61300  1.000 29.83179 ? 53  ILE B CG2 1 
ATOM   1601 C CD1 . ILE B 2 53  ? 19.18500 9.58300   -1.54100 1.000 33.21194 ? 53  ILE B CD1 1 
ATOM   1602 N N   . GLU B 2 54  ? 18.85400 4.72100   -0.56800 1.000 29.68170 ? 54  GLU B N   1 
ATOM   1603 C CA  . GLU B 2 54  ? 19.37900 3.50000   -1.16300 1.000 31.24846 ? 54  GLU B CA  1 
ATOM   1604 C C   . GLU B 2 54  ? 20.44300 3.83300   -2.21400 1.000 33.42000 ? 54  GLU B C   1 
ATOM   1605 O O   . GLU B 2 54  ? 20.52600 4.95200   -2.72200 1.000 33.94611 ? 54  GLU B O   1 
ATOM   1606 C CB  . GLU B 2 54  ? 18.25900 2.68500   -1.82100 1.000 37.69712 ? 54  GLU B CB  1 
ATOM   1607 C CG  . GLU B 2 54  ? 17.76800 3.38100   -3.08000 1.000 43.94583 ? 54  GLU B CG  1 
ATOM   1608 C CD  . GLU B 2 54  ? 16.80100 2.58100   -3.95300 1.000 45.26613 ? 54  GLU B CD  1 
ATOM   1609 O OE1 . GLU B 2 54  ? 16.81100 1.31900   -3.93300 1.000 50.10570 ? 54  GLU B OE1 1 
ATOM   1610 O OE2 . GLU B 2 54  ? 16.04000 3.25400   -4.69300 1.000 49.69099 ? 54  GLU B OE2 1 
ATOM   1611 N N   . SER B 2 55  ? 21.23200 2.82600   -2.56400 1.000 34.22742 ? 55  SER B N   1 
ATOM   1612 C CA  . SER B 2 55  ? 22.16700 2.94500   -3.66800 1.000 36.42350 ? 55  SER B CA  1 
ATOM   1613 C C   . SER B 2 55  ? 21.43300 2.90400   -5.01300 1.000 42.95158 ? 55  SER B C   1 
ATOM   1614 O O   . SER B 2 55  ? 20.32600 2.36200   -5.13200 1.000 39.47659 ? 55  SER B O   1 
ATOM   1615 C CB  . SER B 2 55  ? 23.19700 1.82400   -3.60000 1.000 39.28077 ? 55  SER B CB  1 
ATOM   1616 O OG  . SER B 2 55  ? 22.57800 0.55000   -3.76300 1.000 43.08810 ? 55  SER B OG  1 
ATOM   1617 N N   . HIS B 2 56  ? 22.09900 3.45200   -6.04000 1.000 40.81189 ? 56  HIS B N   1 
ATOM   1618 C CA  . HIS B 2 56  ? 21.61400 3.55200   -7.41700 1.000 43.13416 ? 56  HIS B CA  1 
ATOM   1619 C C   . HIS B 2 56  ? 20.33100 4.38800   -7.48100 1.000 49.35328 ? 56  HIS B C   1 
ATOM   1620 O O   . HIS B 2 56  ? 20.40700 5.60300   -7.71500 1.000 51.24553 ? 56  HIS B O   1 
ATOM   1621 C CB  . HIS B 2 56  ? 21.46900 2.15500   -8.02000 1.000 45.11692 ? 56  HIS B CB  1 
ATOM   1622 C CG  . HIS B 2 56  ? 22.76900 1.40500   -8.04300 1.000 47.41090 ? 56  HIS B CG  1 
ATOM   1623 N ND1 . HIS B 2 56  ? 23.08700 0.43900   -7.11500 1.000 49.54108 ? 56  HIS B ND1 1 
ATOM   1624 C CD2 . HIS B 2 56  ? 23.87400 1.56700   -8.80600 1.000 50.23712 ? 56  HIS B CD2 1 
ATOM   1625 C CE1 . HIS B 2 56  ? 24.31200 -0.00300  -7.33600 1.000 50.97300 ? 56  HIS B CE1 1 
ATOM   1626 N NE2 . HIS B 2 56  ? 24.80800 0.65700   -8.36700 1.000 59.84076 ? 56  HIS B NE2 1 
ATOM   1627 N N   . GLY B 2 57  ? 19.16300 3.78700   -7.24900 1.000 49.82406 ? 57  GLY B N   1 
ATOM   1628 C CA  . GLY B 2 57  ? 17.94200 4.56300   -7.02700 1.000 38.64468 ? 57  GLY B CA  1 
ATOM   1629 C C   . GLY B 2 57  ? 18.03100 5.59000   -5.91600 1.000 46.35403 ? 57  GLY B C   1 
ATOM   1630 O O   . GLY B 2 57  ? 19.08500 5.75600   -5.28200 1.000 47.91970 ? 57  GLY B O   1 
ATOM   1631 N N   . GLN B 2 58  ? 16.94600 6.29600   -5.63500 1.000 38.11431 ? 58  GLN B N   1 
ATOM   1632 C CA  . GLN B 2 58  ? 16.99400 7.19900   -4.49400 1.000 35.73973 ? 58  GLN B CA  1 
ATOM   1633 C C   . GLN B 2 58  ? 15.83600 6.97700   -3.52700 1.000 41.07637 ? 58  GLN B C   1 
ATOM   1634 O O   . GLN B 2 58  ? 15.31800 7.93500   -2.93500 1.000 40.61116 ? 58  GLN B O   1 
ATOM   1635 C CB  . GLN B 2 58  ? 17.02800 8.65000   -4.96600 1.000 35.13542 ? 58  GLN B CB  1 
ATOM   1636 C CG  . GLN B 2 58  ? 18.37000 9.04800   -5.52300 1.000 36.77932 ? 58  GLN B CG  1 
ATOM   1637 C CD  . GLN B 2 58  ? 18.41800 10.51800  -5.84400 1.000 40.28634 ? 58  GLN B CD  1 
ATOM   1638 O OE1 . GLN B 2 58  ? 17.40200 11.24800  -5.74900 1.000 41.56587 ? 58  GLN B OE1 1 
ATOM   1639 N NE2 . GLN B 2 58  ? 19.56900 10.96200  -6.28800 1.000 38.33351 ? 58  GLN B NE2 1 
ATOM   1640 N N   . GLU B 2 59  ? 15.40500 5.73800   -3.36100 1.000 38.67929 ? 59  GLU B N   1 
ATOM   1641 C CA  . GLU B 2 59  ? 14.39800 5.45400   -2.35500 1.000 36.33761 ? 59  GLU B CA  1 
ATOM   1642 C C   . GLU B 2 59  ? 14.94600 5.85600   -0.99000 1.000 35.75599 ? 59  GLU B C   1 
ATOM   1643 O O   . GLU B 2 59  ? 16.12900 5.66700   -0.70600 1.000 32.79808 ? 59  GLU B O   1 
ATOM   1644 C CB  . GLU B 2 59  ? 14.01600 3.96200   -2.37700 1.000 39.26348 ? 59  GLU B CB  1 
ATOM   1645 C CG  . GLU B 2 59  ? 12.95100 3.60000   -1.35200 1.000 43.54779 ? 59  GLU B CG  1 
ATOM   1646 C CD  . GLU B 2 59  ? 12.61000 2.11100   -1.32400 1.000 55.07666 ? 59  GLU B CD  1 
ATOM   1647 O OE1 . GLU B 2 59  ? 13.02400 1.38000   -2.25300 1.000 56.93124 ? 59  GLU B OE1 1 
ATOM   1648 O OE2 . GLU B 2 59  ? 11.91800 1.67400   -0.36800 1.000 61.99364 ? 59  GLU B OE2 1 
ATOM   1649 N N   . THR B 2 60  ? 14.09100 6.44900   -0.15700 1.000 29.62531 ? 60  THR B N   1 
ATOM   1650 C CA  . THR B 2 60  ? 14.50200 6.90700   1.16300  1.000 27.48017 ? 60  THR B CA  1 
ATOM   1651 C C   . THR B 2 60  ? 13.73000 6.19900   2.26800  1.000 30.73825 ? 60  THR B C   1 
ATOM   1652 O O   . THR B 2 60  ? 12.65600 5.61700   2.05100  1.000 31.90074 ? 60  THR B O   1 
ATOM   1653 C CB  . THR B 2 60  ? 14.32200 8.42100   1.33200  1.000 28.78666 ? 60  THR B CB  1 
ATOM   1654 O OG1 . THR B 2 60  ? 12.96800 8.79500   1.00100  1.000 30.41240 ? 60  THR B OG1 1 
ATOM   1655 C CG2 . THR B 2 60  ? 15.33300 9.19100   0.46200  1.000 32.25952 ? 60  THR B CG2 1 
ATOM   1656 N N   . TRP B 2 61  ? 14.31700 6.26700   3.46600  1.000 29.86054 ? 61  TRP B N   1 
ATOM   1657 C CA  . TRP B 2 61  ? 13.74700 5.72600   4.69400  1.000 32.70243 ? 61  TRP B CA  1 
ATOM   1658 C C   . TRP B 2 61  ? 13.96800 6.74000   5.80400  1.000 30.19787 ? 61  TRP B C   1 
ATOM   1659 O O   . TRP B 2 61  ? 15.03500 7.33900   5.88500  1.000 27.79013 ? 61  TRP B O   1 
ATOM   1660 C CB  . TRP B 2 61  ? 14.39800 4.38300   5.06600  1.000 30.87359 ? 61  TRP B CB  1 
ATOM   1661 C CG  . TRP B 2 61  ? 14.02400 3.83500   6.45000  1.000 31.60185 ? 61  TRP B CG  1 
ATOM   1662 C CD1 . TRP B 2 61  ? 13.00700 2.96200   6.75300  1.000 35.71469 ? 61  TRP B CD1 1 
ATOM   1663 C CD2 . TRP B 2 61  ? 14.69200 4.11700   7.68500  1.000 30.03959 ? 61  TRP B CD2 1 
ATOM   1664 N NE1 . TRP B 2 61  ? 12.99900 2.68700   8.11200  1.000 34.59415 ? 61  TRP B NE1 1 
ATOM   1665 C CE2 . TRP B 2 61  ? 14.01700 3.40000   8.70300  1.000 31.88482 ? 61  TRP B CE2 1 
ATOM   1666 C CE3 . TRP B 2 61  ? 15.78300 4.93400   8.03300  1.000 32.36690 ? 61  TRP B CE3 1 
ATOM   1667 C CZ2 . TRP B 2 61  ? 14.41400 3.45200   10.04300 1.000 34.95345 ? 61  TRP B CZ2 1 
ATOM   1668 C CZ3 . TRP B 2 61  ? 16.17600 4.98700   9.37200  1.000 34.12546 ? 61  TRP B CZ3 1 
ATOM   1669 C CH2 . TRP B 2 61  ? 15.48400 4.25500   10.35700 1.000 33.40213 ? 61  TRP B CH2 1 
ATOM   1670 N N   . TYR B 2 62  ? 12.96400 6.92400   6.66300  1.000 31.09671 ? 62  TYR B N   1 
ATOM   1671 C CA  . TYR B 2 62  ? 13.09400 7.83600   7.79200  1.000 31.76938 ? 62  TYR B CA  1 
ATOM   1672 C C   . TYR B 2 62  ? 12.52200 7.18100   9.03900  1.000 30.91931 ? 62  TYR B C   1 
ATOM   1673 O O   . TYR B 2 62  ? 11.47400 6.52500   8.98500  1.000 31.98641 ? 62  TYR B O   1 
ATOM   1674 C CB  . TYR B 2 62  ? 12.35500 9.16000   7.55400  1.000 31.72838 ? 62  TYR B CB  1 
ATOM   1675 C CG  . TYR B 2 62  ? 12.90000 9.94600   6.40300  1.000 31.99202 ? 62  TYR B CG  1 
ATOM   1676 C CD1 . TYR B 2 62  ? 14.04100 10.72700  6.54400  1.000 29.68812 ? 62  TYR B CD1 1 
ATOM   1677 C CD2 . TYR B 2 62  ? 12.25600 9.91800   5.16400  1.000 31.31669 ? 62  TYR B CD2 1 
ATOM   1678 C CE1 . TYR B 2 62  ? 14.53000 11.48000  5.47200  1.000 28.81374 ? 62  TYR B CE1 1 
ATOM   1679 C CE2 . TYR B 2 62  ? 12.75300 10.64200  4.08700  1.000 31.11297 ? 62  TYR B CE2 1 
ATOM   1680 C CZ  . TYR B 2 62  ? 13.88100 11.40800  4.24900  1.000 30.54327 ? 62  TYR B CZ  1 
ATOM   1681 O OH  . TYR B 2 62  ? 14.32500 12.12400  3.17200  1.000 27.26445 ? 62  TYR B OH  1 
ATOM   1682 N N   . ALA B 2 63  ? 13.21300 7.37500   10.15900 1.000 31.62561 ? 63  ALA B N   1 
ATOM   1683 C CA  . ALA B 2 63  ? 12.66200 6.97700   11.45000 1.000 35.73313 ? 63  ALA B CA  1 
ATOM   1684 C C   . ALA B 2 63  ? 11.40100 7.79000   11.75800 1.000 35.40785 ? 63  ALA B C   1 
ATOM   1685 O O   . ALA B 2 63  ? 11.26600 8.94400   11.34800 1.000 34.16602 ? 63  ALA B O   1 
ATOM   1686 C CB  . ALA B 2 63  ? 13.70600 7.17800   12.55400 1.000 32.26721 ? 63  ALA B CB  1 
ATOM   1687 N N   . ASP B 2 64  ? 10.48000 7.17800   12.49900 1.000 35.28362 ? 64  ASP B N   1 
ATOM   1688 C CA  . ASP B 2 64  ? 9.27300  7.88900   12.91900 1.000 41.11061 ? 64  ASP B CA  1 
ATOM   1689 C C   . ASP B 2 64  ? 9.60000  9.16400   13.70100 1.000 38.27099 ? 64  ASP B C   1 
ATOM   1690 O O   . ASP B 2 64  ? 8.85600  10.15500  13.62400 1.000 41.09852 ? 64  ASP B O   1 
ATOM   1691 C CB  . ASP B 2 64  ? 8.40000  6.96400   13.76100 1.000 41.76795 ? 64  ASP B CB  1 
ATOM   1692 C CG  . ASP B 2 64  ? 7.59700  5.98100   12.92100 1.000 51.35018 ? 64  ASP B CG  1 
ATOM   1693 O OD1 . ASP B 2 64  ? 7.55400  6.12100   11.67500 1.000 52.33443 ? 64  ASP B OD1 1 
ATOM   1694 O OD2 . ASP B 2 64  ? 6.99700  5.06800   13.50500 1.000 55.94885 ? 64  ASP B OD2 1 
ATOM   1695 N N   . SER B 2 65  ? 10.71000 9.16800   14.44200 1.000 39.19117 ? 65  SER B N   1 
ATOM   1696 C CA  . SER B 2 65  ? 11.06500 10.31500  15.28200 1.000 40.91128 ? 65  SER B CA  1 
ATOM   1697 C C   . SER B 2 65  ? 11.44100 11.56400  14.48000 1.000 39.33993 ? 65  SER B C   1 
ATOM   1698 O O   . SER B 2 65  ? 11.45500 12.66400  15.04500 1.000 39.28410 ? 65  SER B O   1 
ATOM   1699 C CB  . SER B 2 65  ? 12.23400 9.94800   16.19900 1.000 39.24702 ? 65  SER B CB  1 
ATOM   1700 O OG  . SER B 2 65  ? 13.34000 9.48500   15.44100 1.000 42.17360 ? 65  SER B OG  1 
ATOM   1701 N N   . VAL B 2 66  ? 11.77600 11.42600  13.19800 1.000 35.68814 ? 66  VAL B N   1 
ATOM   1702 C CA  . VAL B 2 66  ? 12.17300 12.56400  12.37800 1.000 35.93965 ? 66  VAL B CA  1 
ATOM   1703 C C   . VAL B 2 66  ? 11.31600 12.71800  11.12900 1.000 40.04896 ? 66  VAL B C   1 
ATOM   1704 O O   . VAL B 2 66  ? 11.58700 13.60700  10.31300 1.000 35.28531 ? 66  VAL B O   1 
ATOM   1705 C CB  . VAL B 2 66  ? 13.66200 12.48700  11.98900 1.000 34.86760 ? 66  VAL B CB  1 
ATOM   1706 C CG1 . VAL B 2 66  ? 14.56100 12.32800  13.22700 1.000 32.25408 ? 66  VAL B CG1 1 
ATOM   1707 C CG2 . VAL B 2 66  ? 13.91000 11.35500  10.98900 1.000 33.91856 ? 66  VAL B CG2 1 
ATOM   1708 N N   . LYS B 2 67  ? 10.30200 11.87300  10.95000 1.000 39.25594 ? 67  LYS B N   1 
ATOM   1709 C CA  . LYS B 2 67  ? 9.40500  11.98100  9.81100  1.000 40.05274 ? 67  LYS B CA  1 
ATOM   1710 C C   . LYS B 2 67  ? 8.74000  13.34500  9.78500  1.000 38.73064 ? 67  LYS B C   1 
ATOM   1711 O O   . LYS B 2 67  ? 8.28600  13.86100  10.81500 1.000 38.65142 ? 67  LYS B O   1 
ATOM   1712 C CB  . LYS B 2 67  ? 8.32900  10.88200  9.85900  1.000 41.12469 ? 67  LYS B CB  1 
ATOM   1713 C CG  . LYS B 2 67  ? 8.83200  9.62700   9.24600  1.000 48.49185 ? 67  LYS B CG  1 
ATOM   1714 C CD  . LYS B 2 67  ? 7.77000  8.54800   9.17600  1.000 47.80317 ? 67  LYS B CD  1 
ATOM   1715 C CE  . LYS B 2 67  ? 8.44800  7.21700   8.94300  1.000 48.02095 ? 67  LYS B CE  1 
ATOM   1716 N NZ  . LYS B 2 67  ? 7.43600  6.10500   8.96300  1.000 58.49880 ? 67  LYS B NZ  1 
ATOM   1717 N N   . GLY B 2 68  ? 8.66900  13.91500  8.59200  1.000 37.92893 ? 68  GLY B N   1 
ATOM   1718 C CA  . GLY B 2 68  ? 8.11500  15.23500  8.42600  1.000 35.50538 ? 68  GLY B CA  1 
ATOM   1719 C C   . GLY B 2 68  ? 9.04100  16.38100  8.79000  1.000 37.08317 ? 68  GLY B C   1 
ATOM   1720 O O   . GLY B 2 68  ? 8.62700  17.53500  8.66100  1.000 36.12944 ? 68  GLY B O   1 
ATOM   1721 N N   . ARG B 2 69  ? 10.26700 16.10800  9.25900  1.000 30.78527 ? 69  ARG B N   1 
ATOM   1722 C CA  . ARG B 2 69  ? 11.17800 17.18600  9.64300  1.000 32.44578 ? 69  ARG B CA  1 
ATOM   1723 C C   . ARG B 2 69  ? 12.53100 17.09700  8.95800  1.000 31.31039 ? 69  ARG B C   1 
ATOM   1724 O O   . ARG B 2 69  ? 13.18600 18.12700  8.77100  1.000 31.01423 ? 69  ARG B O   1 
ATOM   1725 C CB  . ARG B 2 69  ? 11.41400 17.21200  11.16600 1.000 32.39066 ? 69  ARG B CB  1 
ATOM   1726 C CG  . ARG B 2 69  ? 10.13600 17.44000  11.99000 1.000 34.65520 ? 69  ARG B CG  1 
ATOM   1727 C CD  . ARG B 2 69  ? 10.43300 17.60200  13.49700 1.000 33.70710 ? 69  ARG B CD  1 
ATOM   1728 N NE  . ARG B 2 69  ? 11.09900 16.44300  14.08900 1.000 31.61373 ? 69  ARG B NE  1 
ATOM   1729 C CZ  . ARG B 2 69  ? 12.28000 16.46400  14.68800 1.000 32.14997 ? 69  ARG B CZ  1 
ATOM   1730 N NH1 . ARG B 2 69  ? 12.98200 17.58500  14.80400 1.000 32.86437 ? 69  ARG B NH1 1 
ATOM   1731 N NH2 . ARG B 2 69  ? 12.76600 15.33600  15.19500 1.000 30.42024 ? 69  ARG B NH2 1 
ATOM   1732 N N   . PHE B 2 70  ? 12.99600 15.88700  8.63700  1.000 31.25569 ? 70  PHE B N   1 
ATOM   1733 C CA  . PHE B 2 70  ? 14.32000 15.70100  8.04100  1.000 32.30523 ? 70  PHE B CA  1 
ATOM   1734 C C   . PHE B 2 70  ? 14.20000 15.19800  6.60300  1.000 29.85218 ? 70  PHE B C   1 
ATOM   1735 O O   . PHE B 2 70  ? 13.27600 14.45900  6.26400  1.000 29.74874 ? 70  PHE B O   1 
ATOM   1736 C CB  . PHE B 2 70  ? 15.19000 14.68200  8.80700  1.000 32.55729 ? 70  PHE B CB  1 
ATOM   1737 C CG  . PHE B 2 70  ? 15.62300 15.09800  10.21900 1.000 32.13139 ? 70  PHE B CG  1 
ATOM   1738 C CD1 . PHE B 2 70  ? 15.11900 16.23100  10.84700 1.000 33.39827 ? 70  PHE B CD1 1 
ATOM   1739 C CD2 . PHE B 2 70  ? 16.53000 14.26700  10.91600 1.000 35.31988 ? 70  PHE B CD2 1 
ATOM   1740 C CE1 . PHE B 2 70  ? 15.52300 16.57500  12.14800 1.000 33.93550 ? 70  PHE B CE1 1 
ATOM   1741 C CE2 . PHE B 2 70  ? 16.95500 14.59500  12.21900 1.000 33.35178 ? 70  PHE B CE2 1 
ATOM   1742 C CZ  . PHE B 2 70  ? 16.43700 15.74300  12.83400 1.000 30.57902 ? 70  PHE B CZ  1 
ATOM   1743 N N   . THR B 2 71  ? 15.16500 15.58100  5.76000  1.000 30.72125 ? 71  THR B N   1 
ATOM   1744 C CA  . THR B 2 71  ? 15.27200 15.07300  4.38600  1.000 27.86291 ? 71  THR B CA  1 
ATOM   1745 C C   . THR B 2 71  ? 16.70800 14.65100  4.14600  1.000 27.90809 ? 71  THR B C   1 
ATOM   1746 O O   . THR B 2 71  ? 17.62700 15.43400  4.39600  1.000 27.57595 ? 71  THR B O   1 
ATOM   1747 C CB  . THR B 2 71  ? 14.93700 16.14600  3.32000  1.000 28.09791 ? 71  THR B CB  1 
ATOM   1748 O OG1 . THR B 2 71  ? 13.60700 16.63500  3.50100  1.000 31.77883 ? 71  THR B OG1 1 
ATOM   1749 C CG2 . THR B 2 71  ? 15.08700 15.55200  1.89300  1.000 31.86032 ? 71  THR B CG2 1 
ATOM   1750 N N   . ILE B 2 72  ? 16.89400 13.46500  3.59700  1.000 26.25041 ? 72  ILE B N   1 
ATOM   1751 C CA  . ILE B 2 72  ? 18.21200 12.99600  3.19800  1.000 26.82919 ? 72  ILE B CA  1 
ATOM   1752 C C   . ILE B 2 72  ? 18.32000 13.11300  1.68300  1.000 28.22288 ? 72  ILE B C   1 
ATOM   1753 O O   . ILE B 2 72  ? 17.33600 12.90700  0.95900  1.000 30.91208 ? 72  ILE B O   1 
ATOM   1754 C CB  . ILE B 2 72  ? 18.46700 11.55000  3.68900  1.000 29.24589 ? 72  ILE B CB  1 
ATOM   1755 C CG1 . ILE B 2 72  ? 19.92400 11.15200  3.44400  1.000 25.99651 ? 72  ILE B CG1 1 
ATOM   1756 C CG2 . ILE B 2 72  ? 17.49400 10.50100  3.06200  1.000 28.26633 ? 72  ILE B CG2 1 
ATOM   1757 C CD1 . ILE B 2 72  ? 20.28400 9.70100   3.99000  1.000 28.66896 ? 72  ILE B CD1 1 
ATOM   1758 N N   . SER B 2 73  ? 19.51000 13.45600  1.20900  1.000 28.41367 ? 73  SER B N   1 
ATOM   1759 C CA  . SER B 2 73  ? 19.75900 13.58400  -0.22300 1.000 28.25693 ? 73  SER B CA  1 
ATOM   1760 C C   . SER B 2 73  ? 21.23700 13.34300  -0.47000 1.000 28.68114 ? 73  SER B C   1 
ATOM   1761 O O   . SER B 2 73  ? 22.03500 13.24600  0.46100  1.000 27.93933 ? 73  SER B O   1 
ATOM   1762 C CB  . SER B 2 73  ? 19.36200 14.96300  -0.75800 1.000 29.30541 ? 73  SER B CB  1 
ATOM   1763 O OG  . SER B 2 73  ? 20.11600 15.99000  -0.13400 1.000 28.93255 ? 73  SER B OG  1 
ATOM   1764 N N   . ARG B 2 74  ? 21.61300 13.27600  -1.74800 1.000 27.70739 ? 74  ARG B N   1 
ATOM   1765 C CA  . ARG B 2 74  ? 23.02600 13.17800  -2.06400 1.000 28.08794 ? 74  ARG B CA  1 
ATOM   1766 C C   . ARG B 2 74  ? 23.28600 13.95100  -3.35100 1.000 30.86992 ? 74  ARG B C   1 
ATOM   1767 O O   . ARG B 2 74  ? 22.37500 14.17800  -4.16000 1.000 29.13818 ? 74  ARG B O   1 
ATOM   1768 C CB  . ARG B 2 74  ? 23.45900 11.69000  -2.17800 1.000 28.81425 ? 74  ARG B CB  1 
ATOM   1769 C CG  . ARG B 2 74  ? 22.80300 10.93300  -3.32100 1.000 34.21990 ? 74  ARG B CG  1 
ATOM   1770 C CD  . ARG B 2 74  ? 23.25400 9.41900   -3.39800 1.000 33.20841 ? 74  ARG B CD  1 
ATOM   1771 N NE  . ARG B 2 74  ? 22.86500 8.84500   -4.68800 1.000 35.40506 ? 74  ARG B NE  1 
ATOM   1772 C CZ  . ARG B 2 74  ? 22.07400 7.79200   -4.83300 1.000 35.92175 ? 74  ARG B CZ  1 
ATOM   1773 N NH1 . ARG B 2 74  ? 21.64100 7.10500   -3.78900 1.000 37.33908 ? 74  ARG B NH1 1 
ATOM   1774 N NH2 . ARG B 2 74  ? 21.70800 7.42000   -6.05500 1.000 39.61891 ? 74  ARG B NH2 1 
ATOM   1775 N N   . ASP B 2 75  ? 24.54100 14.37200  -3.51900 1.000 30.40093 ? 75  ASP B N   1 
ATOM   1776 C CA  . ASP B 2 75  ? 25.02700 14.95800  -4.76400 1.000 30.06542 ? 75  ASP B CA  1 
ATOM   1777 C C   . ASP B 2 75  ? 26.10900 13.99900  -5.25900 1.000 28.84033 ? 75  ASP B C   1 
ATOM   1778 O O   . ASP B 2 75  ? 27.19400 13.93300  -4.66700 1.000 28.71104 ? 75  ASP B O   1 
ATOM   1779 C CB  . ASP B 2 75  ? 25.56500 16.38800  -4.53700 1.000 27.75106 ? 75  ASP B CB  1 
ATOM   1780 C CG  . ASP B 2 75  ? 25.98800 17.07400  -5.82500 1.000 36.59812 ? 75  ASP B CG  1 
ATOM   1781 O OD1 . ASP B 2 75  ? 26.76900 16.49000  -6.60100 1.000 34.07745 ? 75  ASP B OD1 1 
ATOM   1782 O OD2 . ASP B 2 75  ? 25.50100 18.20300  -6.08300 1.000 42.23301 ? 75  ASP B OD2 1 
ATOM   1783 N N   . ASN B 2 76  ? 25.80200 13.26500  -6.33700 1.000 29.82901 ? 76  ASN B N   1 
ATOM   1784 C CA  . ASN B 2 76  ? 26.71100 12.23700  -6.83100 1.000 30.46094 ? 76  ASN B CA  1 
ATOM   1785 C C   . ASN B 2 76  ? 28.02400 12.85800  -7.26900 1.000 33.05251 ? 76  ASN B C   1 
ATOM   1786 O O   . ASN B 2 76  ? 29.09100 12.28100  -7.05800 1.000 33.58255 ? 76  ASN B O   1 
ATOM   1787 C CB  . ASN B 2 76  ? 26.09400 11.47600  -8.01300 1.000 31.59832 ? 76  ASN B CB  1 
ATOM   1788 C CG  . ASN B 2 76  ? 24.86200 10.67800  -7.62800 1.000 32.89166 ? 76  ASN B CG  1 
ATOM   1789 O OD1 . ASN B 2 76  ? 24.48600 10.62800  -6.45700 1.000 32.18966 ? 76  ASN B OD1 1 
ATOM   1790 N ND2 . ASN B 2 76  ? 24.21000 10.07600  -8.62100 1.000 31.84557 ? 76  ASN B ND2 1 
ATOM   1791 N N   . ALA B 2 77  ? 27.95700 14.03700  -7.88400 1.000 30.63758 ? 77  ALA B N   1 
ATOM   1792 C CA  . ALA B 2 77  ? 29.15000 14.62700  -8.49000 1.000 34.53893 ? 77  ALA B CA  1 
ATOM   1793 C C   . ALA B 2 77  ? 30.10900 15.11600  -7.41400 1.000 37.46445 ? 77  ALA B C   1 
ATOM   1794 O O   . ALA B 2 77  ? 31.33300 15.04100  -7.57700 1.000 39.01329 ? 77  ALA B O   1 
ATOM   1795 C CB  . ALA B 2 77  ? 28.74500 15.78100  -9.42200 1.000 34.66718 ? 77  ALA B CB  1 
ATOM   1796 N N   . LYS B 2 78  ? 29.56200 15.63800  -6.31700 1.000 32.78079 ? 78  LYS B N   1 
ATOM   1797 C CA  . LYS B 2 78  ? 30.35000 16.06300  -5.17300 1.000 31.92660 ? 78  LYS B CA  1 
ATOM   1798 C C   . LYS B 2 78  ? 30.67400 14.91100  -4.23500 1.000 34.55465 ? 78  LYS B C   1 
ATOM   1799 O O   . LYS B 2 78  ? 31.44700 15.10900  -3.29100 1.000 33.83503 ? 78  LYS B O   1 
ATOM   1800 C CB  . LYS B 2 78  ? 29.60800 17.14800  -4.39500 1.000 32.75889 ? 78  LYS B CB  1 
ATOM   1801 C CG  . LYS B 2 78  ? 29.49800 18.48300  -5.15100 1.000 34.57745 ? 78  LYS B CG  1 
ATOM   1802 C CD  . LYS B 2 78  ? 28.71300 19.48900  -4.32200 1.000 41.06401 ? 78  LYS B CD  1 
ATOM   1803 C CE  . LYS B 2 78  ? 28.65500 20.85700  -5.01400 1.000 48.60848 ? 78  LYS B CE  1 
ATOM   1804 N NZ  . LYS B 2 78  ? 28.03300 21.86100  -4.10200 1.000 50.56540 ? 78  LYS B NZ  1 
ATOM   1805 N N   . ASN B 2 79  ? 30.11200 13.72800  -4.48200 1.000 30.57824 ? 79  ASN B N   1 
ATOM   1806 C CA  . ASN B 2 79  ? 30.26600 12.57300  -3.61000 1.000 31.23129 ? 79  ASN B CA  1 
ATOM   1807 C C   . ASN B 2 79  ? 29.96400 12.93300  -2.15700 1.000 32.24181 ? 79  ASN B C   1 
ATOM   1808 O O   . ASN B 2 79  ? 30.73200 12.61800  -1.23800 1.000 30.89545 ? 79  ASN B O   1 
ATOM   1809 C CB  . ASN B 2 79  ? 31.66600 11.97300  -3.73300 1.000 30.33623 ? 79  ASN B CB  1 
ATOM   1810 C CG  . ASN B 2 79  ? 31.64800 10.47100  -3.57900 1.000 35.67685 ? 79  ASN B CG  1 
ATOM   1811 O OD1 . ASN B 2 79  ? 30.74000 9.81300   -4.07500 1.000 34.05942 ? 79  ASN B OD1 1 
ATOM   1812 N ND2 . ASN B 2 79  ? 32.63500 9.91900   -2.87700 1.000 33.63851 ? 79  ASN B ND2 1 
ATOM   1813 N N   . THR B 2 80  ? 28.83200 13.60500  -1.95800 1.000 28.24662 ? 80  THR B N   1 
ATOM   1814 C CA  . THR B 2 80  ? 28.43900 14.11800  -0.64900 1.000 29.29420 ? 80  THR B CA  1 
ATOM   1815 C C   . THR B 2 80  ? 27.00900 13.69000  -0.33400 1.000 32.14660 ? 80  THR B C   1 
ATOM   1816 O O   . THR B 2 80  ? 26.15200 13.63000  -1.22100 1.000 29.80486 ? 80  THR B O   1 
ATOM   1817 C CB  . THR B 2 80  ? 28.57100 15.66100  -0.62800 1.000 32.39398 ? 80  THR B CB  1 
ATOM   1818 O OG1 . THR B 2 80  ? 29.95200 15.98600  -0.76800 1.000 33.64847 ? 80  THR B OG1 1 
ATOM   1819 C CG2 . THR B 2 80  ? 28.08700 16.26400  0.70500  1.000 33.15835 ? 80  THR B CG2 1 
ATOM   1820 N N   . VAL B 2 81  ? 26.74800 13.39800  0.93700  1.000 25.93363 ? 81  VAL B N   1 
ATOM   1821 C CA  . VAL B 2 81  ? 25.40100 13.09000  1.41600  1.000 28.63838 ? 81  VAL B CA  1 
ATOM   1822 C C   . VAL B 2 81  ? 24.97000 14.19700  2.36700  1.000 27.38453 ? 81  VAL B C   1 
ATOM   1823 O O   . VAL B 2 81  ? 25.79900 14.72000  3.12500  1.000 27.34778 ? 81  VAL B O   1 
ATOM   1824 C CB  . VAL B 2 81  ? 25.38300 11.73100  2.13400  1.000 27.61501 ? 81  VAL B CB  1 
ATOM   1825 C CG1 . VAL B 2 81  ? 23.94800 11.35400  2.55400  1.000 28.14278 ? 81  VAL B CG1 1 
ATOM   1826 C CG2 . VAL B 2 81  ? 26.03000 10.62500  1.25300  1.000 25.98145 ? 81  VAL B CG2 1 
ATOM   1827 N N   . TYR B 2 82  ? 23.67800 14.56400  2.33100  1.000 27.39915 ? 82  TYR B N   1 
ATOM   1828 C CA  . TYR B 2 82  ? 23.17100 15.65900  3.15800  1.000 28.02524 ? 82  TYR B CA  1 
ATOM   1829 C C   . TYR B 2 82  ? 22.03500 15.22200  4.07400  1.000 27.86742 ? 82  TYR B C   1 
ATOM   1830 O O   . TYR B 2 82  ? 21.29700 14.27300  3.78600  1.000 27.18447 ? 82  TYR B O   1 
ATOM   1831 C CB  . TYR B 2 82  ? 22.63600 16.81000  2.30400  1.000 26.99279 ? 82  TYR B CB  1 
ATOM   1832 C CG  . TYR B 2 82  ? 23.62700 17.28800  1.30300  1.000 27.77035 ? 82  TYR B CG  1 
ATOM   1833 C CD1 . TYR B 2 82  ? 24.62700 18.17500  1.67600  1.000 29.76216 ? 82  TYR B CD1 1 
ATOM   1834 C CD2 . TYR B 2 82  ? 23.59000 16.82300  -0.00700 1.000 31.01666 ? 82  TYR B CD2 1 
ATOM   1835 C CE1 . TYR B 2 82  ? 25.55500 18.63600  0.75900  1.000 34.62440 ? 82  TYR B CE1 1 
ATOM   1836 C CE2 . TYR B 2 82  ? 24.53100 17.26600  -0.94100 1.000 33.25222 ? 82  TYR B CE2 1 
ATOM   1837 C CZ  . TYR B 2 82  ? 25.50000 18.17200  -0.54500 1.000 34.21550 ? 82  TYR B CZ  1 
ATOM   1838 O OH  . TYR B 2 82  ? 26.43700 18.61900  -1.44700 1.000 36.97354 ? 82  TYR B OH  1 
ATOM   1839 N N   . LEU B 2 83  ? 21.88200 15.93600  5.18300  1.000 26.71483 ? 83  LEU B N   1 
ATOM   1840 C CA  . LEU B 2 83  ? 20.70400 15.76000  6.03800  1.000 28.09627 ? 83  LEU B CA  1 
ATOM   1841 C C   . LEU B 2 83  ? 20.13800 17.14400  6.31000  1.000 29.01179 ? 83  LEU B C   1 
ATOM   1842 O O   . LEU B 2 83  ? 20.72200 17.91300  7.07200  1.000 29.50314 ? 83  LEU B O   1 
ATOM   1843 C CB  . LEU B 2 83  ? 21.04500 15.03100  7.35300  1.000 26.66818 ? 83  LEU B CB  1 
ATOM   1844 C CG  . LEU B 2 83  ? 19.77500 14.67300  8.15400  1.000 29.51701 ? 83  LEU B CG  1 
ATOM   1845 C CD1 . LEU B 2 83  ? 18.88900 13.64200  7.42100  1.000 29.31589 ? 83  LEU B CD1 1 
ATOM   1846 C CD2 . LEU B 2 83  ? 20.20100 14.09600  9.52600  1.000 29.95315 ? 83  LEU B CD2 1 
ATOM   1847 N N   . GLN B 2 84  ? 19.02600 17.48400  5.66500  1.000 27.26522 ? 84  GLN B N   1 
ATOM   1848 C CA  . GLN B 2 84  ? 18.34300 18.75000  5.94000  1.000 25.94155 ? 84  GLN B CA  1 
ATOM   1849 C C   . GLN B 2 84  ? 17.43400 18.56200  7.15300  1.000 27.87475 ? 84  GLN B C   1 
ATOM   1850 O O   . GLN B 2 84  ? 16.58300 17.67100  7.14700  1.000 29.72596 ? 84  GLN B O   1 
ATOM   1851 C CB  . GLN B 2 84  ? 17.51400 19.17900  4.72900  1.000 28.96675 ? 84  GLN B CB  1 
ATOM   1852 C CG  . GLN B 2 84  ? 16.65400 20.48200  4.96300  1.000 29.55547 ? 84  GLN B CG  1 
ATOM   1853 C CD  . GLN B 2 84  ? 17.50900 21.72900  5.10200  1.000 31.91466 ? 84  GLN B CD  1 
ATOM   1854 O OE1 . GLN B 2 84  ? 18.19800 22.11800  4.16600  1.000 33.57188 ? 84  GLN B OE1 1 
ATOM   1855 N NE2 . GLN B 2 84  ? 17.44800 22.38100  6.26800  1.000 32.76215 ? 84  GLN B NE2 1 
ATOM   1856 N N   . MET B 2 85  ? 17.60700 19.38800  8.18200  1.000 28.12764 ? 85  MET B N   1 
ATOM   1857 C CA  . MET B 2 85  ? 16.80800 19.29100  9.40400  1.000 29.29768 ? 85  MET B CA  1 
ATOM   1858 C C   . MET B 2 85  ? 15.99600 20.56500  9.58900  1.000 29.17643 ? 85  MET B C   1 
ATOM   1859 O O   . MET B 2 85  ? 16.53200 21.67000  9.47500  1.000 31.92065 ? 85  MET B O   1 
ATOM   1860 C CB  . MET B 2 85  ? 17.71300 19.03200  10.61800 1.000 30.33283 ? 85  MET B CB  1 
ATOM   1861 C CG  . MET B 2 85  ? 18.52100 17.72700  10.42800 1.000 32.01589 ? 85  MET B CG  1 
ATOM   1862 S SD  . MET B 2 85  ? 19.57000 17.32500  11.86300 1.000 43.56353 ? 85  MET B SD  1 
ATOM   1863 C CE  . MET B 2 85  ? 20.54800 18.71600  11.82700 1.000 27.14320 ? 85  MET B CE  1 
ATOM   1864 N N   . ASN B 2 86  ? 14.70000 20.41100  9.83800  1.000 28.13597 ? 86  ASN B N   1 
ATOM   1865 C CA  . ASN B 2 86  ? 13.81500 21.52700  10.13600 1.000 28.67515 ? 86  ASN B CA  1 
ATOM   1866 C C   . ASN B 2 86  ? 13.13300 21.26400  11.47200 1.000 31.24830 ? 86  ASN B C   1 
ATOM   1867 O O   . ASN B 2 86  ? 13.08000 20.12800  11.94100 1.000 30.51540 ? 86  ASN B O   1 
ATOM   1868 C CB  . ASN B 2 86  ? 12.75400 21.71200  9.05900  1.000 29.34354 ? 86  ASN B CB  1 
ATOM   1869 C CG  . ASN B 2 86  ? 13.33700 22.21600  7.74600  1.000 31.81531 ? 86  ASN B CG  1 
ATOM   1870 O OD1 . ASN B 2 86  ? 13.91800 23.30400  7.69900  1.000 29.22072 ? 86  ASN B OD1 1 
ATOM   1871 N ND2 . ASN B 2 86  ? 13.13700 21.45300  6.66400  1.000 30.18252 ? 86  ASN B ND2 1 
ATOM   1872 N N   . SER B 2 87  ? 12.61500 22.32900  12.07500 1.000 29.52670 ? 87  SER B N   1 
ATOM   1873 C CA  . SER B 2 87  ? 11.83100 22.22000  13.31000 1.000 33.24611 ? 87  SER B CA  1 
ATOM   1874 C C   . SER B 2 87  ? 12.58000 21.42000  14.37000 1.000 32.56799 ? 87  SER B C   1 
ATOM   1875 O O   . SER B 2 87  ? 12.02800 20.52400  15.02000 1.000 32.42577 ? 87  SER B O   1 
ATOM   1876 C CB  . SER B 2 87  ? 10.46700 21.59000  13.03800 1.000 34.35468 ? 87  SER B CB  1 
ATOM   1877 O OG  . SER B 2 87  ? 9.72100  22.40300  12.16600 1.000 40.17045 ? 87  SER B OG  1 
ATOM   1878 N N   . LEU B 2 88  ? 13.83900 21.78400  14.57500 1.000 31.39877 ? 88  LEU B N   1 
ATOM   1879 C CA  . LEU B 2 88  ? 14.68400 21.05300  15.51400 1.000 30.40334 ? 88  LEU B CA  1 
ATOM   1880 C C   . LEU B 2 88  ? 14.18500 21.21700  16.94400 1.000 33.89433 ? 88  LEU B C   1 
ATOM   1881 O O   . LEU B 2 88  ? 13.59700 22.24200  17.31300 1.000 34.45974 ? 88  LEU B O   1 
ATOM   1882 C CB  . LEU B 2 88  ? 16.13500 21.52500  15.41000 1.000 34.75128 ? 88  LEU B CB  1 
ATOM   1883 C CG  . LEU B 2 88  ? 16.86600 21.02200  14.15300 1.000 32.78930 ? 88  LEU B CG  1 
ATOM   1884 C CD1 . LEU B 2 88  ? 18.03900 21.90400  13.85100 1.000 33.70827 ? 88  LEU B CD1 1 
ATOM   1885 C CD2 . LEU B 2 88  ? 17.34400 19.56000  14.37000 1.000 32.11514 ? 88  LEU B CD2 1 
ATOM   1886 N N   . LYS B 2 89  ? 14.41800 20.18400  17.74000 1.000 30.34744 ? 89  LYS B N   1 
ATOM   1887 C CA  . LYS B 2 89  ? 13.97400 20.06900  19.12500 1.000 35.57509 ? 89  LYS B CA  1 
ATOM   1888 C C   . LYS B 2 89  ? 15.16600 19.71100  19.99000 1.000 37.64898 ? 89  LYS B C   1 
ATOM   1889 O O   . LYS B 2 89  ? 16.14700 19.13800  19.49600 1.000 32.24608 ? 89  LYS B O   1 
ATOM   1890 C CB  . LYS B 2 89  ? 12.90100 18.97600  19.27500 1.000 40.99461 ? 89  LYS B CB  1 
ATOM   1891 C CG  . LYS B 2 89  ? 11.77700 19.10500  18.29000 1.000 48.10457 ? 89  LYS B CG  1 
ATOM   1892 C CD  . LYS B 2 89  ? 10.76900 17.95700  18.40600 1.000 50.74514 ? 89  LYS B CD  1 
ATOM   1893 C CE  . LYS B 2 89  ? 9.69700  18.14600  17.31300 1.000 54.72069 ? 89  LYS B CE  1 
ATOM   1894 N NZ  . LYS B 2 89  ? 8.64300  17.08600  17.26500 1.000 53.75783 ? 89  LYS B NZ  1 
ATOM   1895 N N   . PRO B 2 90  ? 15.11100 20.02200  21.30000 1.000 34.98522 ? 90  PRO B N   1 
ATOM   1896 C CA  . PRO B 2 90  ? 16.18100 19.58000  22.21400 1.000 38.81731 ? 90  PRO B CA  1 
ATOM   1897 C C   . PRO B 2 90  ? 16.47000 18.08800  22.13100 1.000 40.73426 ? 90  PRO B C   1 
ATOM   1898 O O   . PRO B 2 90  ? 17.63500 17.67600  22.26500 1.000 39.49927 ? 90  PRO B O   1 
ATOM   1899 C CB  . PRO B 2 90  ? 15.63600 19.96500  23.60300 1.000 41.93912 ? 90  PRO B CB  1 
ATOM   1900 C CG  . PRO B 2 90  ? 14.72000 21.09600  23.34800 1.000 43.46652 ? 90  PRO B CG  1 
ATOM   1901 C CD  . PRO B 2 90  ? 14.12500 20.88600  21.96900 1.000 37.34882 ? 90  PRO B CD  1 
ATOM   1902 N N   . GLU B 2 91  ? 15.44200 17.26600  21.89800 1.000 38.35754 ? 91  GLU B N   1 
ATOM   1903 C CA  . GLU B 2 91  ? 15.62800 15.82000  21.78400 1.000 40.88715 ? 91  GLU B CA  1 
ATOM   1904 C C   . GLU B 2 91  ? 16.48000 15.41200  20.57600 1.000 37.92145 ? 91  GLU B C   1 
ATOM   1905 O O   . GLU B 2 91  ? 16.86500 14.23600  20.48100 1.000 37.93599 ? 91  GLU B O   1 
ATOM   1906 C CB  . GLU B 2 91  ? 14.25600 15.12800  21.72000 1.000 41.45049 ? 91  GLU B CB  1 
ATOM   1907 C CG  . GLU B 2 91  ? 13.43200 15.19600  23.00800 1.000 51.01379 ? 91  GLU B CG  1 
ATOM   1908 C CD  . GLU B 2 91  ? 12.73700 16.55400  23.27300 1.000 56.36906 ? 91  GLU B CD  1 
ATOM   1909 O OE1 . GLU B 2 91  ? 12.68900 17.44000  22.37100 1.000 47.74667 ? 91  GLU B OE1 1 
ATOM   1910 O OE2 . GLU B 2 91  ? 12.23400 16.72300  24.41300 1.000 60.31387 ? 91  GLU B OE2 1 
ATOM   1911 N N   . ASP B 2 92  ? 16.76500 16.32400  19.64300 1.000 36.72292 ? 92  ASP B N   1 
ATOM   1912 C CA  . ASP B 2 92  ? 17.63300 16.04900  18.50200 1.000 32.54796 ? 92  ASP B CA  1 
ATOM   1913 C C   . ASP B 2 92  ? 19.11500 16.25900  18.80500 1.000 34.08935 ? 92  ASP B C   1 
ATOM   1914 O O   . ASP B 2 92  ? 19.95300 15.99900  17.93000 1.000 33.26768 ? 92  ASP B O   1 
ATOM   1915 C CB  . ASP B 2 92  ? 17.25300 16.93200  17.29700 1.000 30.43546 ? 92  ASP B CB  1 
ATOM   1916 C CG  . ASP B 2 92  ? 15.83000 16.70000  16.80700 1.000 35.13574 ? 92  ASP B CG  1 
ATOM   1917 O OD1 . ASP B 2 92  ? 15.36500 15.52300  16.72000 1.000 34.00458 ? 92  ASP B OD1 1 
ATOM   1918 O OD2 . ASP B 2 92  ? 15.15700 17.71400  16.50900 1.000 35.20322 ? 92  ASP B OD2 1 
ATOM   1919 N N   . THR B 2 93  ? 19.45500 16.77300  19.98500 1.000 32.88418 ? 93  THR B N   1 
ATOM   1920 C CA  . THR B 2 93  ? 20.85100 16.98300  20.35700 1.000 33.28121 ? 93  THR B CA  1 
ATOM   1921 C C   . THR B 2 93  ? 21.59900 15.65300  20.39500 1.000 36.71848 ? 93  THR B C   1 
ATOM   1922 O O   . THR B 2 93  ? 21.20900 14.73900  21.12900 1.000 33.66243 ? 93  THR B O   1 
ATOM   1923 C CB  . THR B 2 93  ? 20.91900 17.68000  21.71400 1.000 33.14210 ? 93  THR B CB  1 
ATOM   1924 O OG1 . THR B 2 93  ? 20.34700 18.97500  21.57800 1.000 32.55945 ? 93  THR B OG1 1 
ATOM   1925 C CG2 . THR B 2 93  ? 22.37200 17.83000  22.23700 1.000 32.73824 ? 93  THR B CG2 1 
ATOM   1926 N N   . ALA B 2 94  ? 22.67300 15.55400  19.61000 1.000 31.93893 ? 94  ALA B N   1 
ATOM   1927 C CA  . ALA B 2 94  ? 23.43300 14.30900  19.48800 1.000 31.69409 ? 94  ALA B CA  1 
ATOM   1928 C C   . ALA B 2 94  ? 24.60800 14.56000  18.54000 1.000 31.70324 ? 94  ALA B C   1 
ATOM   1929 O O   . ALA B 2 94  ? 24.67100 15.59300  17.86800 1.000 31.78608 ? 94  ALA B O   1 
ATOM   1930 C CB  . ALA B 2 94  ? 22.55400 13.16300  18.96000 1.000 32.00975 ? 94  ALA B CB  1 
ATOM   1931 N N   . VAL B 2 95  ? 25.53900 13.59900  18.50000 1.000 34.85969 ? 95  VAL B N   1 
ATOM   1932 C CA  . VAL B 2 95  ? 26.52600 13.51000  17.42800 1.000 33.34097 ? 95  VAL B CA  1 
ATOM   1933 C C   . VAL B 2 95  ? 25.90500 12.73400  16.27400 1.000 32.35497 ? 95  VAL B C   1 
ATOM   1934 O O   . VAL B 2 95  ? 25.36000 11.63500  16.47600 1.000 30.42283 ? 95  VAL B O   1 
ATOM   1935 C CB  . VAL B 2 95  ? 27.82200 12.83900  17.91500 1.000 35.64846 ? 95  VAL B CB  1 
ATOM   1936 C CG1 . VAL B 2 95  ? 28.85900 12.79600  16.78300 1.000 34.04958 ? 95  VAL B CG1 1 
ATOM   1937 C CG2 . VAL B 2 95  ? 28.40200 13.61100  19.11100 1.000 37.63655 ? 95  VAL B CG2 1 
ATOM   1938 N N   . TYR B 2 96  ? 26.00400 13.28300  15.06300 1.000 29.55583 ? 96  TYR B N   1 
ATOM   1939 C CA  . TYR B 2 96  ? 25.39700 12.67700  13.87700 1.000 28.29943 ? 96  TYR B CA  1 
ATOM   1940 C C   . TYR B 2 96  ? 26.47900 12.08900  12.98300 1.000 30.14373 ? 96  TYR B C   1 
ATOM   1941 O O   . TYR B 2 96  ? 27.50100 12.73700  12.72900 1.000 30.58191 ? 96  TYR B O   1 
ATOM   1942 C CB  . TYR B 2 96  ? 24.57300 13.69100  13.06800 1.000 30.15177 ? 96  TYR B CB  1 
ATOM   1943 C CG  . TYR B 2 96  ? 23.23900 14.02300  13.69900 1.000 26.69682 ? 96  TYR B CG  1 
ATOM   1944 C CD1 . TYR B 2 96  ? 23.18000 14.68400  14.93600 1.000 30.21967 ? 96  TYR B CD1 1 
ATOM   1945 C CD2 . TYR B 2 96  ? 22.04000 13.66400  13.08300 1.000 29.18075 ? 96  TYR B CD2 1 
ATOM   1946 C CE1 . TYR B 2 96  ? 21.95500 14.99900  15.53500 1.000 28.23441 ? 96  TYR B CE1 1 
ATOM   1947 C CE2 . TYR B 2 96  ? 20.79000 13.97600  13.67600 1.000 28.84600 ? 96  TYR B CE2 1 
ATOM   1948 C CZ  . TYR B 2 96  ? 20.77100 14.64200  14.90000 1.000 29.54649 ? 96  TYR B CZ  1 
ATOM   1949 O OH  . TYR B 2 96  ? 19.57300 14.94600  15.49300 1.000 30.40310 ? 96  TYR B OH  1 
ATOM   1950 N N   . TYR B 2 97  ? 26.24400 10.86300  12.50800 1.000 28.67672 ? 97  TYR B N   1 
ATOM   1951 C CA  . TYR B 2 97  ? 27.19800 10.10400  11.70900 1.000 29.36667 ? 97  TYR B CA  1 
ATOM   1952 C C   . TYR B 2 97  ? 26.53100 9.71200   10.41000 1.000 26.61027 ? 97  TYR B C   1 
ATOM   1953 O O   . TYR B 2 97  ? 25.36800 9.33400   10.41200 1.000 28.91348 ? 97  TYR B O   1 
ATOM   1954 C CB  . TYR B 2 97  ? 27.62000 8.80100   12.39800 1.000 28.63423 ? 97  TYR B CB  1 
ATOM   1955 C CG  . TYR B 2 97  ? 28.31900 9.03400   13.71300 1.000 31.97611 ? 97  TYR B CG  1 
ATOM   1956 C CD1 . TYR B 2 97  ? 27.58700 9.26800   14.87200 1.000 31.32736 ? 97  TYR B CD1 1 
ATOM   1957 C CD2 . TYR B 2 97  ? 29.70500 9.02700   13.78500 1.000 33.47552 ? 97  TYR B CD2 1 
ATOM   1958 C CE1 . TYR B 2 97  ? 28.23800 9.48000   16.09400 1.000 32.55709 ? 97  TYR B CE1 1 
ATOM   1959 C CE2 . TYR B 2 97  ? 30.37400 9.22100   15.01100 1.000 39.19042 ? 97  TYR B CE2 1 
ATOM   1960 C CZ  . TYR B 2 97  ? 29.62700 9.45700   16.14700 1.000 35.47371 ? 97  TYR B CZ  1 
ATOM   1961 O OH  . TYR B 2 97  ? 30.26200 9.64300   17.34800 1.000 40.69969 ? 97  TYR B OH  1 
ATOM   1962 N N   . CYS B 2 98  ? 27.30000 9.71100   9.32700  1.000 29.72256 ? 98  CYS B N   1 
ATOM   1963 C CA  . CYS B 2 98  ? 26.81600 9.24300   8.03300  1.000 30.90708 ? 98  CYS B CA  1 
ATOM   1964 C C   . CYS B 2 98  ? 27.63500 8.02800   7.62800  1.000 30.22118 ? 98  CYS B C   1 
ATOM   1965 O O   . CYS B 2 98  ? 28.86200 8.12300   7.52400  1.000 29.44417 ? 98  CYS B O   1 
ATOM   1966 C CB  . CYS B 2 98  ? 26.93700 10.37000  7.00200  1.000 30.12652 ? 98  CYS B CB  1 
ATOM   1967 S SG  . CYS B 2 98  ? 26.20900 9.88800   5.39800  1.000 34.96677 ? 98  CYS B SG  1 
ATOM   1968 N N   . VAL B 2 99  ? 26.97600 6.87200   7.44900  1.000 28.59736 ? 99  VAL B N   1 
ATOM   1969 C CA  . VAL B 2 99  ? 27.69300 5.61300   7.25300  1.000 32.34809 ? 99  VAL B CA  1 
ATOM   1970 C C   . VAL B 2 99  ? 27.19300 4.89400   6.00900  1.000 34.67724 ? 99  VAL B C   1 
ATOM   1971 O O   . VAL B 2 99  ? 26.10700 5.16800   5.49900  1.000 30.86951 ? 99  VAL B O   1 
ATOM   1972 C CB  . VAL B 2 99  ? 27.56400 4.66500   8.46800  1.000 35.20941 ? 99  VAL B CB  1 
ATOM   1973 C CG1 . VAL B 2 99  ? 28.18600 5.32000   9.73400  1.000 37.11233 ? 99  VAL B CG1 1 
ATOM   1974 C CG2 . VAL B 2 99  ? 26.08700 4.29600   8.69500  1.000 32.50843 ? 99  VAL B CG2 1 
ATOM   1975 N N   . ARG B 2 100 ? 28.01300 3.94400   5.53300  1.000 29.70035 ? 100 ARG B N   1 
ATOM   1976 C CA  . ARG B 2 100 ? 27.57500 2.94700   4.55700  1.000 33.12015 ? 100 ARG B CA  1 
ATOM   1977 C C   . ARG B 2 100 ? 26.94900 1.76900   5.29600  1.000 34.81963 ? 100 ARG B C   1 
ATOM   1978 O O   . ARG B 2 100 ? 27.59400 1.15900   6.15200  1.000 33.63805 ? 100 ARG B O   1 
ATOM   1979 C CB  . ARG B 2 100 ? 28.74500 2.45100   3.69900  1.000 33.61057 ? 100 ARG B CB  1 
ATOM   1980 C CG  . ARG B 2 100 ? 29.52300 3.56900   2.98300  1.000 35.76293 ? 100 ARG B CG  1 
ATOM   1981 C CD  . ARG B 2 100 ? 30.88700 3.05100   2.61500  1.000 48.30188 ? 100 ARG B CD  1 
ATOM   1982 N NE  . ARG B 2 100 ? 31.62800 2.79800   3.84000  1.000 47.87411 ? 100 ARG B NE  1 
ATOM   1983 C CZ  . ARG B 2 100 ? 32.72900 2.07900   3.93200  1.000 42.85568 ? 100 ARG B CZ  1 
ATOM   1984 N NH1 . ARG B 2 100 ? 33.24900 1.46000   2.87900  1.000 46.57080 ? 100 ARG B NH1 1 
ATOM   1985 N NH2 . ARG B 2 100 ? 33.31100 1.95700   5.12000  1.000 56.00384 ? 100 ARG B NH2 1 
ATOM   1986 N N   . VAL B 2 101 ? 25.70100 1.43800   4.96300  1.000 32.34222 ? 101 VAL B N   1 
ATOM   1987 C CA  . VAL B 2 101 ? 25.07500 0.26300   5.56000  1.000 31.34501 ? 101 VAL B CA  1 
ATOM   1988 C C   . VAL B 2 101 ? 25.81300 -0.98800  5.09400  1.000 30.02506 ? 101 VAL B C   1 
ATOM   1989 O O   . VAL B 2 101 ? 26.09200 -1.16100  3.89800  1.000 34.76507 ? 101 VAL B O   1 
ATOM   1990 C CB  . VAL B 2 101 ? 23.57900 0.21500   5.20100  1.000 30.72129 ? 101 VAL B CB  1 
ATOM   1991 C CG1 . VAL B 2 101 ? 22.94600 -1.08600  5.69400  1.000 31.77394 ? 101 VAL B CG1 1 
ATOM   1992 C CG2 . VAL B 2 101 ? 22.86000 1.38800   5.86400  1.000 31.83812 ? 101 VAL B CG2 1 
ATOM   1993 N N   . GLY B 2 102 ? 26.15900 -1.85700  6.03200  1.000 32.01126 ? 102 GLY B N   1 
ATOM   1994 C CA  . GLY B 2 102 ? 26.90700 -3.05500  5.66900  1.000 31.77298 ? 102 GLY B CA  1 
ATOM   1995 C C   . GLY B 2 102 ? 28.40600 -2.86200  5.59100  1.000 34.31407 ? 102 GLY B C   1 
ATOM   1996 O O   . GLY B 2 102 ? 29.10300 -3.74400  5.07300  1.000 34.14692 ? 102 GLY B O   1 
ATOM   1997 N N   . ALA B 2 103 ? 28.91891 -1.72640  6.06665  1.000 32.58355 ? 103 ALA B N   1 
ATOM   1998 C CA  . ALA B 2 103 ? 30.34523 -1.54772  6.22038  1.000 35.16767 ? 103 ALA B CA  1 
ATOM   1999 C C   . ALA B 2 103 ? 30.60319 -1.02286  7.62296  1.000 39.45511 ? 103 ALA B C   1 
ATOM   2000 O O   . ALA B 2 103 ? 29.88180 -0.13905  8.11212  1.000 38.59433 ? 103 ALA B O   1 
ATOM   2001 C CB  . ALA B 2 103 ? 30.90505 -0.59566  5.15508  1.000 43.51927 ? 103 ALA B CB  1 
ATOM   2002 N N   . GLU B 2 104 ? 31.70977 -1.48814  8.16902  1.000 41.71752 ? 104 GLU B N   1 
ATOM   2003 C CA  A GLU B 2 104 ? 32.15612 -1.27611  9.54654  0.500 43.84590 ? 104 GLU B CA  1 
ATOM   2004 C CA  B GLU B 2 104 ? 31.99685 -1.23034  9.57217  0.500 43.87600 ? 104 GLU B CA  1 
ATOM   2005 C C   . GLU B 2 104 ? 32.58755 0.15914   9.81907  1.000 45.58351 ? 104 GLU B C   1 
ATOM   2006 O O   . GLU B 2 104 ? 32.37140 0.69413   10.90521 1.000 47.76215 ? 104 GLU B O   1 
ATOM   2007 C CB  A GLU B 2 104 ? 33.33907 -2.20518  9.81189  0.500 44.54059 ? 104 GLU B CB  1 
ATOM   2008 C CB  B GLU B 2 104 ? 32.89538 -2.34398  10.10898 0.500 44.12236 ? 104 GLU B CB  1 
ATOM   2009 C CG  A GLU B 2 104 ? 34.49915 -2.19987  8.71814  0.500 48.64250 ? 104 GLU B CG  1 
ATOM   2010 C CG  B GLU B 2 104 ? 32.32854 -3.74031  9.69110  0.500 45.99375 ? 104 GLU B CG  1 
ATOM   2011 C CD  A GLU B 2 104 ? 34.11368 -2.64015  7.25081  0.500 48.41172 ? 104 GLU B CD  1 
ATOM   2012 C CD  B GLU B 2 104 ? 33.29341 -4.93187  9.84980  0.500 47.49154 ? 104 GLU B CD  1 
ATOM   2013 O OE1 A GLU B 2 104 ? 33.11825 -3.39867  7.00944  0.500 42.31764 ? 104 GLU B OE1 1 
ATOM   2014 O OE1 B GLU B 2 104 ? 34.00283 -4.97765  10.88869 0.500 50.59636 ? 104 GLU B OE1 1 
ATOM   2015 O OE2 A GLU B 2 104 ? 34.81362 -2.17457  6.32186  0.500 48.48814 ? 104 GLU B OE2 1 
ATOM   2016 O OE2 B GLU B 2 104 ? 33.35800 -5.81400  8.93452  0.500 40.19999 ? 104 GLU B OE2 1 
ATOM   2017 N N   . TYR B 2 105 ? 33.25065 0.78163   8.86143  1.000 41.48264 ? 105 TYR B N   1 
ATOM   2018 C CA  . TYR B 2 105 ? 33.97148 2.01201   9.15857  1.000 47.78977 ? 105 TYR B CA  1 
ATOM   2019 C C   . TYR B 2 105 ? 33.02337 3.18021   9.41477  1.000 44.03047 ? 105 TYR B C   1 
ATOM   2020 O O   . TYR B 2 105 ? 31.96609 3.29412   8.78945  1.000 44.86535 ? 105 TYR B O   1 
ATOM   2021 C CB  . TYR B 2 105 ? 34.91945 2.34477   8.00927  1.000 53.41027 ? 105 TYR B CB  1 
ATOM   2022 C CG  . TYR B 2 105 ? 35.62165 3.69923   8.14855  1.000 51.88356 ? 105 TYR B CG  1 
ATOM   2023 C CD1 . TYR B 2 105 ? 36.74861 3.83221   8.93988  1.000 55.07765 ? 105 TYR B CD1 1 
ATOM   2024 C CD2 . TYR B 2 105 ? 35.13581 4.83426   7.49206  1.000 53.69706 ? 105 TYR B CD2 1 
ATOM   2025 C CE1 . TYR B 2 105 ? 37.41035 5.06680   9.05653  1.000 57.53163 ? 105 TYR B CE1 1 
ATOM   2026 C CE2 . TYR B 2 105 ? 35.77022 6.08855   7.62445  1.000 48.33741 ? 105 TYR B CE2 1 
ATOM   2027 C CZ  . TYR B 2 105 ? 36.90710 6.17578   8.39442  1.000 54.55322 ? 105 TYR B CZ  1 
ATOM   2028 O OH  . TYR B 2 105 ? 37.56273 7.38269   8.52293  1.000 57.32388 ? 105 TYR B OH  1 
ATOM   2029 N N   . VAL B 2 106 ? 33.36800 4.03400   10.38800 1.000 42.32901 ? 106 VAL B N   1 
ATOM   2030 C CA  . VAL B 2 106 ? 32.56800 5.20700   10.73800 1.000 41.03070 ? 106 VAL B CA  1 
ATOM   2031 C C   . VAL B 2 106 ? 33.51000 6.38800   10.90600 1.000 43.34454 ? 106 VAL B C   1 
ATOM   2032 O O   . VAL B 2 106 ? 34.63000 6.22900   11.40400 1.000 44.03630 ? 106 VAL B O   1 
ATOM   2033 C CB  . VAL B 2 106 ? 31.74700 4.97300   12.03000 1.000 45.61854 ? 106 VAL B CB  1 
ATOM   2034 C CG1 . VAL B 2 106 ? 32.64100 4.51400   13.14100 1.000 54.55482 ? 106 VAL B CG1 1 
ATOM   2035 C CG2 . VAL B 2 106 ? 31.01700 6.22500   12.47100 1.000 45.94252 ? 106 VAL B CG2 1 
ATOM   2036 N N   . GLY B 2 107 ? 33.05600 7.57000   10.49700 1.000 37.59914 ? 107 GLY B N   1 
ATOM   2037 C CA  . GLY B 2 107 ? 33.79400 8.79800   10.72400 1.000 38.76483 ? 107 GLY B CA  1 
ATOM   2038 C C   . GLY B 2 107 ? 33.66100 9.30700   12.15000 1.000 40.11564 ? 107 GLY B C   1 
ATOM   2039 O O   . GLY B 2 107 ? 33.24200 8.59000   13.06200 1.000 41.81126 ? 107 GLY B O   1 
ATOM   2040 N N   . GLN B 2 108 ? 34.02900 10.57400  12.34100 1.000 39.39643 ? 108 GLN B N   1 
ATOM   2041 C CA  . GLN B 2 108 ? 34.03200 11.16800  13.67100 1.000 40.69268 ? 108 GLN B CA  1 
ATOM   2042 C C   . GLN B 2 108 ? 32.72300 11.86600  14.01800 1.000 38.11648 ? 108 GLN B C   1 
ATOM   2043 O O   . GLN B 2 108 ? 32.51700 12.22100  15.18900 1.000 39.00071 ? 108 GLN B O   1 
ATOM   2044 C CB  . GLN B 2 108 ? 35.19000 12.16300  13.79300 1.000 43.41446 ? 108 GLN B CB  1 
ATOM   2045 C CG  . GLN B 2 108 ? 36.52300 11.48400  13.63000 1.000 47.16097 ? 108 GLN B CG  1 
ATOM   2046 C CD  . GLN B 2 108 ? 36.75600 10.42700  14.69300 1.000 50.25165 ? 108 GLN B CD  1 
ATOM   2047 O OE1 . GLN B 2 108 ? 36.58100 10.68300  15.88000 1.000 55.25532 ? 108 GLN B OE1 1 
ATOM   2048 N NE2 . GLN B 2 108 ? 37.15800 9.24300   14.27400 1.000 55.55092 ? 108 GLN B NE2 1 
ATOM   2049 N N   . GLY B 2 109 ? 31.86400 12.10500  13.03900 1.000 36.21397 ? 109 GLY B N   1 
ATOM   2050 C CA  . GLY B 2 109 ? 30.56400 12.68900  13.29600 1.000 33.84507 ? 109 GLY B CA  1 
ATOM   2051 C C   . GLY B 2 109 ? 30.61300 14.20300  13.43100 1.000 32.99582 ? 109 GLY B C   1 
ATOM   2052 O O   . GLY B 2 109 ? 31.67300 14.83900  13.40300 1.000 35.10105 ? 109 GLY B O   1 
ATOM   2053 N N   . THR B 2 110 ? 29.42500 14.78700  13.58600 1.000 32.30116 ? 110 THR B N   1 
ATOM   2054 C CA  . THR B 2 110 ? 29.29400 16.22700  13.79700 1.000 34.80170 ? 110 THR B CA  1 
ATOM   2055 C C   . THR B 2 110 ? 28.26700 16.47300  14.89700 1.000 33.06175 ? 110 THR B C   1 
ATOM   2056 O O   . THR B 2 110 ? 27.17400 15.88900  14.88600 1.000 30.15029 ? 110 THR B O   1 
ATOM   2057 C CB  . THR B 2 110 ? 28.90700 16.97700  12.49400 1.000 32.46176 ? 110 THR B CB  1 
ATOM   2058 O OG1 . THR B 2 110 ? 28.90900 18.40400  12.73700 1.000 36.97831 ? 110 THR B OG1 1 
ATOM   2059 C CG2 . THR B 2 110 ? 27.53200 16.55000  11.91900 1.000 33.08863 ? 110 THR B CG2 1 
ATOM   2060 N N   . GLN B 2 111 ? 28.62700 17.34200  15.84400 1.000 33.76151 ? 111 GLN B N   1 
ATOM   2061 C CA  . GLN B 2 111 ? 27.77100 17.61100  16.99400 1.000 33.19092 ? 111 GLN B CA  1 
ATOM   2062 C C   . GLN B 2 111 ? 26.66700 18.59600  16.63300 1.000 34.84257 ? 111 GLN B C   1 
ATOM   2063 O O   . GLN B 2 111 ? 26.93000 19.67400  16.07000 1.000 32.57621 ? 111 GLN B O   1 
ATOM   2064 C CB  . GLN B 2 111 ? 28.58700 18.17300  18.15400 1.000 34.22405 ? 111 GLN B CB  1 
ATOM   2065 C CG  . GLN B 2 111 ? 27.73100 18.59600  19.37000 1.000 35.91560 ? 111 GLN B CG  1 
ATOM   2066 C CD  . GLN B 2 111 ? 27.24400 17.40700  20.19300 1.000 39.95880 ? 111 GLN B CD  1 
ATOM   2067 O OE1 . GLN B 2 111 ? 28.04000 16.53500  20.55800 1.000 40.04016 ? 111 GLN B OE1 1 
ATOM   2068 N NE2 . GLN B 2 111 ? 25.93900 17.36900  20.49500 1.000 36.74767 ? 111 GLN B NE2 1 
ATOM   2069 N N   . VAL B 2 112 ? 25.43300 18.23100  16.98400 1.000 30.62535 ? 112 VAL B N   1 
ATOM   2070 C CA  . VAL B 2 112 ? 24.26300 19.09100  16.86800 1.000 30.45985 ? 112 VAL B CA  1 
ATOM   2071 C C   . VAL B 2 112 ? 23.71500 19.32400  18.26800 1.000 30.19889 ? 112 VAL B C   1 
ATOM   2072 O O   . VAL B 2 112 ? 23.43000 18.36700  18.99200 1.000 31.52575 ? 112 VAL B O   1 
ATOM   2073 C CB  . VAL B 2 112 ? 23.19000 18.45200  15.97000 1.000 33.40223 ? 112 VAL B CB  1 
ATOM   2074 C CG1 . VAL B 2 112 ? 21.89100 19.25400  16.01500 1.000 33.15823 ? 112 VAL B CG1 1 
ATOM   2075 C CG2 . VAL B 2 112 ? 23.74500 18.29400  14.53100 1.000 30.59222 ? 112 VAL B CG2 1 
ATOM   2076 N N   . THR B 2 113 ? 23.56800 20.59200  18.65100 1.000 31.83869 ? 113 THR B N   1 
ATOM   2077 C CA  . THR B 2 113 ? 23.03100 20.94100  19.96200 1.000 30.73544 ? 113 THR B CA  1 
ATOM   2078 C C   . THR B 2 113 ? 21.87900 21.90700  19.75300 1.000 31.98518 ? 113 THR B C   1 
ATOM   2079 O O   . THR B 2 113 ? 22.04800 22.93500  19.09500 1.000 36.93691 ? 113 THR B O   1 
ATOM   2080 C CB  . THR B 2 113 ? 24.10700 21.57600  20.84200 1.000 34.59344 ? 113 THR B CB  1 
ATOM   2081 O OG1 . THR B 2 113 ? 25.23800 20.69900  20.87700 1.000 38.18987 ? 113 THR B OG1 1 
ATOM   2082 C CG2 . THR B 2 113 ? 23.58200 21.77600  22.26300 1.000 34.25815 ? 113 THR B CG2 1 
ATOM   2083 N N   . VAL B 2 114 ? 20.70900 21.57000  20.28900 1.000 31.54669 ? 114 VAL B N   1 
ATOM   2084 C CA  . VAL B 2 114 ? 19.50000 22.36100  20.10900 1.000 31.89044 ? 114 VAL B CA  1 
ATOM   2085 C C   . VAL B 2 114 ? 19.12200 22.92000  21.46500 1.000 34.79997 ? 114 VAL B C   1 
ATOM   2086 O O   . VAL B 2 114 ? 18.83800 22.15700  22.39600 1.000 37.96529 ? 114 VAL B O   1 
ATOM   2087 C CB  . VAL B 2 114 ? 18.34600 21.52400  19.53200 1.000 33.02496 ? 114 VAL B CB  1 
ATOM   2088 C CG1 . VAL B 2 114 ? 17.10800 22.42600  19.29600 1.000 34.49280 ? 114 VAL B CG1 1 
ATOM   2089 C CG2 . VAL B 2 114 ? 18.79900 20.81600  18.24600 1.000 32.57934 ? 114 VAL B CG2 1 
ATOM   2090 N N   . SER B 2 115 ? 19.12500 24.23800  21.59000 1.000 34.88307 ? 115 SER B N   1 
ATOM   2091 C CA  . SER B 2 115 ? 18.81800 24.84300  22.87400 1.000 37.71203 ? 115 SER B CA  1 
ATOM   2092 C C   . SER B 2 115 ? 17.33100 25.16900  22.92700 1.000 44.11455 ? 115 SER B C   1 
ATOM   2093 O O   . SER B 2 115 ? 16.76400 25.68700  21.95900 1.000 43.28716 ? 115 SER B O   1 
ATOM   2094 C CB  . SER B 2 115 ? 19.65800 26.09500  23.09800 1.000 39.79902 ? 115 SER B CB  1 
ATOM   2095 O OG  . SER B 2 115 ? 19.28900 27.08600  22.17400 1.000 53.26863 ? 115 SER B OG  1 
ATOM   2096 N N   . ALA B 2 116 ? 16.70800 24.86500  24.06700 1.000 42.78926 ? 116 ALA B N   1 
ATOM   2097 C CA  . ALA B 2 116 ? 15.25300 24.96000  24.20700 1.000 46.08111 ? 116 ALA B CA  1 
ATOM   2098 C C   . ALA B 2 116 ? 14.73700 26.37300  24.05000 1.000 54.05269 ? 116 ALA B C   1 
ATOM   2099 O O   . ALA B 2 116 ? 15.40700 27.35400  24.40000 1.000 55.93339 ? 116 ALA B O   1 
ATOM   2100 C CB  . ALA B 2 116 ? 14.81700 24.41000  25.54900 1.000 49.64574 ? 116 ALA B CB  1 
ATOM   2101 O OXT . ALA B 2 116 ? 13.59700 26.54800  23.60400 1.000 60.36047 ? 116 ALA B OXT 1 
HETATM 2102 O O   . HOH C 3 .   ? 46.08500 -27.29200 11.06100 1.000 40.42427 ? 201 HOH A O   1 
HETATM 2103 O O   . HOH C 3 .   ? 45.74700 -12.12800 7.68700  1.000 55.73361 ? 202 HOH A O   1 
HETATM 2104 O O   . HOH C 3 .   ? 24.001   -30.706   4.196    1.000 57.35998 ? 203 HOH A O   1 
HETATM 2105 O O   . HOH C 3 .   ? 15.33900 -18.89500 3.33100  1.000 40.73433 ? 204 HOH A O   1 
HETATM 2106 O O   . HOH C 3 .   ? 40.93100 -13.30100 -0.35600 1.000 61.58159 ? 205 HOH A O   1 
HETATM 2107 O O   . HOH C 3 .   ? 49.18100 -23.09000 9.13300  1.000 52.61037 ? 206 HOH A O   1 
HETATM 2108 O O   . HOH C 3 .   ? 31.16500 -3.75500  3.42600  1.000 48.92630 ? 207 HOH A O   1 
HETATM 2109 O O   . HOH C 3 .   ? 21.75700 -23.61800 25.07900 1.000 59.69607 ? 208 HOH A O   1 
HETATM 2110 O O   . HOH C 3 .   ? 25.75000 0.06900   1.44800  1.000 36.83366 ? 209 HOH A O   1 
HETATM 2111 O O   . HOH C 3 .   ? 35.59700 -14.03800 3.82000  1.000 50.65933 ? 210 HOH A O   1 
HETATM 2112 O O   . HOH C 3 .   ? 21.81400 -28.59600 16.15200 1.000 48.80133 ? 211 HOH A O   1 
HETATM 2113 O O   . HOH C 3 .   ? 28.86200 -41.84400 17.13700 1.000 53.73857 ? 212 HOH A O   1 
HETATM 2114 O O   . HOH C 3 .   ? 25.50000 -5.75400  -3.29900 1.000 40.08958 ? 213 HOH A O   1 
HETATM 2115 O O   . HOH C 3 .   ? 48.52400 -26.06900 10.02900 1.000 41.70315 ? 214 HOH A O   1 
HETATM 2116 O O   . HOH C 3 .   ? 22.15000 0.65200   16.49000 1.000 47.23405 ? 215 HOH A O   1 
HETATM 2117 O O   . HOH C 3 .   ? 14.15500 -10.63400 6.11300  1.000 38.87616 ? 216 HOH A O   1 
HETATM 2118 O O   . HOH C 3 .   ? 19.61500 -6.34600  23.12500 1.000 54.11157 ? 217 HOH A O   1 
HETATM 2119 O O   . HOH C 3 .   ? 23.12100 -9.44400  -4.15800 1.000 40.15713 ? 218 HOH A O   1 
HETATM 2120 O O   . HOH C 3 .   ? 35.71100 -17.55700 -0.16200 1.000 61.22049 ? 219 HOH A O   1 
HETATM 2121 O O   . HOH C 3 .   ? 33.98100 -14.34600 18.92300 1.000 54.64833 ? 220 HOH A O   1 
HETATM 2122 O O   . HOH C 3 .   ? 19.20000 -28.51800 13.89600 1.000 54.97438 ? 221 HOH A O   1 
HETATM 2123 O O   . HOH C 3 .   ? 18.67400 -0.88100  0.16600  1.000 51.43701 ? 222 HOH A O   1 
HETATM 2124 O O   . HOH C 3 .   ? 24.75900 -34.16500 6.76300  1.000 51.41575 ? 223 HOH A O   1 
HETATM 2125 O O   . HOH C 3 .   ? 18.91800 -17.36000 3.77600  1.000 38.90610 ? 224 HOH A O   1 
HETATM 2126 O O   . HOH C 3 .   ? 31.27000 -25.35600 15.50400 1.000 48.77366 ? 225 HOH A O   1 
HETATM 2127 O O   . HOH C 3 .   ? 19.84400 -2.11200  17.96000 1.000 50.72445 ? 226 HOH A O   1 
HETATM 2128 O O   . HOH C 3 .   ? 14.94900 -10.60700 -8.50700 1.000 52.16380 ? 227 HOH A O   1 
HETATM 2129 O O   . HOH C 3 .   ? 16.27100 -6.40100  3.62400  1.000 40.78178 ? 228 HOH A O   1 
HETATM 2130 O O   . HOH C 3 .   ? 13.97200 -9.30000  -2.04100 1.000 51.48685 ? 229 HOH A O   1 
HETATM 2131 O O   . HOH C 3 .   ? 23.44800 -2.31800  1.76600  1.000 34.99932 ? 230 HOH A O   1 
HETATM 2132 O O   . HOH C 3 .   ? 25.88600 -1.38800  8.84000  1.000 35.06876 ? 231 HOH A O   1 
HETATM 2133 O O   . HOH C 3 .   ? 23.68200 1.45100   19.98200 1.000 54.25021 ? 232 HOH A O   1 
HETATM 2134 O O   . HOH C 3 .   ? 18.93700 -23.30100 13.00700 1.000 45.96606 ? 233 HOH A O   1 
HETATM 2135 O O   . HOH C 3 .   ? 12.33200 -20.13700 13.33100 1.000 51.25972 ? 234 HOH A O   1 
HETATM 2136 O O   . HOH C 3 .   ? 23.05400 -6.50000  -4.45900 1.000 43.19118 ? 235 HOH A O   1 
HETATM 2137 O O   . HOH C 3 .   ? 10.13300 -10.74500 7.52900  1.000 53.43067 ? 236 HOH A O   1 
HETATM 2138 O O   . HOH C 3 .   ? 25.98000 -25.61500 18.56200 1.000 43.44554 ? 237 HOH A O   1 
HETATM 2139 O O   . HOH C 3 .   ? 35.01700 -23.62700 5.11100  1.000 42.11879 ? 238 HOH A O   1 
HETATM 2140 O O   . HOH C 3 .   ? 13.26500 -17.09000 5.47900  1.000 43.38074 ? 239 HOH A O   1 
HETATM 2141 O O   . HOH C 3 .   ? 25.00300 -30.80200 20.90100 1.000 54.27291 ? 240 HOH A O   1 
HETATM 2142 O O   . HOH C 3 .   ? 19.17400 -21.02200 11.37200 1.000 39.63726 ? 241 HOH A O   1 
HETATM 2143 O O   . HOH C 3 .   ? 22.55300 -1.27100  15.13900 1.000 46.53367 ? 242 HOH A O   1 
HETATM 2144 O O   . HOH C 3 .   ? 29.96400 -20.09900 -2.26600 1.000 39.49749 ? 243 HOH A O   1 
HETATM 2145 O O   . HOH C 3 .   ? 16.96300 -12.87800 -2.40100 1.000 37.39130 ? 244 HOH A O   1 
HETATM 2146 O O   . HOH C 3 .   ? 42.74500 -23.02900 8.89200  1.000 47.70388 ? 245 HOH A O   1 
HETATM 2147 O O   . HOH C 3 .   ? 14.40500 -13.58100 2.17800  1.000 45.66106 ? 246 HOH A O   1 
HETATM 2148 O O   . HOH C 3 .   ? 16.69900 -25.18900 11.46200 1.000 56.42089 ? 247 HOH A O   1 
HETATM 2149 O O   . HOH C 3 .   ? 12.68200 -12.59600 6.88600  1.000 50.61160 ? 248 HOH A O   1 
HETATM 2150 O O   . HOH C 3 .   ? 17.57800 -1.62400  -2.74700 1.000 55.67708 ? 249 HOH A O   1 
HETATM 2151 O O   . HOH C 3 .   ? 18.40400 -25.84100 16.81200 1.000 56.10939 ? 250 HOH A O   1 
HETATM 2152 O O   . HOH C 3 .   ? 13.97500 -18.74500 16.72900 1.000 44.01348 ? 251 HOH A O   1 
HETATM 2153 O O   . HOH C 3 .   ? 36.18100 -25.95100 8.48000  1.000 48.03820 ? 252 HOH A O   1 
HETATM 2154 O O   . HOH C 3 .   ? 20.18700 -28.97700 9.41400  1.000 54.44505 ? 253 HOH A O   1 
HETATM 2155 O O   . HOH C 3 .   ? 21.83100 -29.79700 7.96100  1.000 61.40348 ? 254 HOH A O   1 
HETATM 2156 O O   . HOH C 3 .   ? 17.74300 1.11000   17.11600 1.000 46.87907 ? 255 HOH A O   1 
HETATM 2157 O O   . HOH C 3 .   ? 25.39000 -40.01200 22.97700 1.000 65.77076 ? 256 HOH A O   1 
HETATM 2158 O O   . HOH C 3 .   ? 37.27100 -24.24600 3.56200  1.000 52.58143 ? 257 HOH A O   1 
HETATM 2159 O O   . HOH C 3 .   ? 50.73700 -22.56200 10.95500 1.000 54.11066 ? 258 HOH A O   1 
HETATM 2160 O O   . HOH C 3 .   ? 34.71600 -16.99100 20.07600 1.000 49.08279 ? 259 HOH A O   1 
HETATM 2161 O O   . HOH C 3 .   ? 39.36500 -15.33000 -1.00300 1.000 55.39382 ? 260 HOH A O   1 
HETATM 2162 O O   . HOH C 3 .   ? 5.77800  -12.92000 13.01600 1.000 54.98388 ? 261 HOH A O   1 
HETATM 2163 O O   . HOH C 3 .   ? 33.85700 -26.64500 14.28700 1.000 59.96939 ? 262 HOH A O   1 
HETATM 2164 O O   . HOH C 3 .   ? 41.85600 -19.72300 2.02600  1.000 57.18669 ? 263 HOH A O   1 
HETATM 2165 O O   . HOH C 3 .   ? 27.67000 -40.65200 21.32700 1.000 52.46558 ? 264 HOH A O   1 
HETATM 2166 O O   . HOH C 3 .   ? 34.05600 -6.42500  4.36600  1.000 55.33616 ? 265 HOH A O   1 
HETATM 2167 O O   . HOH C 3 .   ? 17.57100 -25.95500 4.07800  1.000 45.95172 ? 266 HOH A O   1 
HETATM 2168 O O   . HOH C 3 .   ? 11.00900 -16.65500 21.82100 1.000 55.09451 ? 267 HOH A O   1 
HETATM 2169 O O   . HOH C 3 .   ? 12.34700 -19.35300 9.77400  1.000 50.47149 ? 268 HOH A O   1 
HETATM 2170 O O   . HOH C 3 .   ? 31.08400 -2.99900  -2.14800 1.000 58.54745 ? 269 HOH A O   1 
HETATM 2171 O O   . HOH C 3 .   ? 28.59800 -18.69500 -4.19700 1.000 52.68287 ? 270 HOH A O   1 
HETATM 2172 O O   . HOH C 3 .   ? 24.54000 -1.65300  11.56300 1.000 45.23884 ? 271 HOH A O   1 
HETATM 2173 O O   . HOH C 3 .   ? 36.05500 -7.81400  14.28500 1.000 57.23277 ? 272 HOH A O   1 
HETATM 2174 O O   . HOH C 3 .   ? 26.19700 -8.83200  -4.04000 1.000 51.89222 ? 273 HOH A O   1 
HETATM 2175 O O   . HOH C 3 .   ? 33.15600 -7.03600  17.12900 1.000 56.72412 ? 274 HOH A O   1 
HETATM 2176 O O   . HOH C 3 .   ? 33.88900 -19.30600 -0.26400 1.000 53.19490 ? 275 HOH A O   1 
HETATM 2177 O O   . HOH C 3 .   ? 24.941   -29.173   1.829    1.000 47.22463 ? 276 HOH A O   1 
HETATM 2178 O O   . HOH C 3 .   ? 31.376   -40.988   9.197    1.000 59.18265 ? 277 HOH A O   1 
HETATM 2179 O O   . HOH C 3 .   ? 29.54400 -9.15500  -6.00600 1.000 48.16628 ? 278 HOH A O   1 
HETATM 2180 O O   . HOH C 3 .   ? 23.30100 -10.84000 -6.55200 1.000 53.07856 ? 279 HOH A O   1 
HETATM 2181 O O   . HOH C 3 .   ? 28.780   -17.722   -8.182   1.000 57.94150 ? 280 HOH A O   1 
HETATM 2182 O O   . HOH C 3 .   ? 12.42100 -14.20300 5.33100  1.000 53.84216 ? 281 HOH A O   1 
HETATM 2183 O O   . HOH C 3 .   ? 11.01700 -8.51900  3.68700  1.000 61.86065 ? 282 HOH A O   1 
HETATM 2184 O O   . HOH C 3 .   ? 41.904   -29.682   2.737    1.000 45.01905 ? 283 HOH A O   1 
HETATM 2185 O O   . HOH C 3 .   ? 12.07800 -8.88500  6.20500  1.000 56.09728 ? 284 HOH A O   1 
HETATM 2186 O O   . HOH C 3 .   ? 35.10700 -5.83200  15.26400 1.000 57.41313 ? 285 HOH A O   1 
HETATM 2187 O O   . HOH C 3 .   ? 10.45700 -20.09300 11.66400 1.000 62.24701 ? 286 HOH A O   1 
HETATM 2188 O O   . HOH C 3 .   ? 32.36100 -18.89400 -2.03900 1.000 54.20016 ? 287 HOH A O   1 
HETATM 2189 O O   . HOH C 3 .   ? 13.39300 2.80400   13.61200 1.000 48.38339 ? 288 HOH A O   1 
HETATM 2190 O O   . HOH D 3 .   ? 11.71300 26.96700  22.47600 1.000 60.71788 ? 201 HOH B O   1 
HETATM 2191 O O   . HOH D 3 .   ? 22.81200 11.26600  27.07500 1.000 57.42612 ? 202 HOH B O   1 
HETATM 2192 O O   . HOH D 3 .   ? 36.69700 9.45800   7.81600  1.000 44.92700 ? 203 HOH B O   1 
HETATM 2193 O O   . HOH D 3 .   ? 30.61300 8.25100   9.70900  1.000 36.96062 ? 204 HOH B O   1 
HETATM 2194 O O   . HOH D 3 .   ? 29.20500 9.10200   19.55400 1.000 48.03905 ? 205 HOH B O   1 
HETATM 2195 O O   . HOH D 3 .   ? 20.13600 -0.66600  20.45000 1.000 58.78595 ? 206 HOH B O   1 
HETATM 2196 O O   . HOH D 3 .   ? 20.43400 -0.00400  -1.55800 1.000 47.36861 ? 207 HOH B O   1 
HETATM 2197 O O   . HOH D 3 .   ? 31.71000 17.63200  5.27800  1.000 33.61935 ? 208 HOH B O   1 
HETATM 2198 O O   . HOH D 3 .   ? 11.80200 -0.60500  0.92600  1.000 45.65467 ? 209 HOH B O   1 
HETATM 2199 O O   . HOH D 3 .   ? 20.50200 1.21400   18.34900 1.000 52.29790 ? 210 HOH B O   1 
HETATM 2200 O O   . HOH D 3 .   ? 30.35700 2.69700   6.75200  1.000 34.21823 ? 211 HOH B O   1 
HETATM 2201 O O   . HOH D 3 .   ? 18.89300 16.78000  2.10500  1.000 31.05739 ? 212 HOH B O   1 
HETATM 2202 O O   . HOH D 3 .   ? 34.08800 7.08200   15.11300 1.000 48.97680 ? 213 HOH B O   1 
HETATM 2203 O O   . HOH D 3 .   ? 22.90400 14.07000  23.12700 1.000 42.26279 ? 214 HOH B O   1 
HETATM 2204 O O   . HOH D 3 .   ? 20.78300 18.21500  -1.52000 1.000 37.26793 ? 215 HOH B O   1 
HETATM 2205 O O   . HOH D 3 .   ? 13.93100 5.86900   16.43100 1.000 46.07554 ? 216 HOH B O   1 
HETATM 2206 O O   . HOH D 3 .   ? 12.93700 25.02500  11.04800 1.000 34.55644 ? 217 HOH B O   1 
HETATM 2207 O O   . HOH D 3 .   ? 26.88500 19.53700  -8.01500 1.000 43.86338 ? 218 HOH B O   1 
HETATM 2208 O O   . HOH D 3 .   ? 34.00700 18.54600  10.02800 1.000 47.22523 ? 219 HOH B O   1 
HETATM 2209 O O   . HOH D 3 .   ? 13.72400 9.44900   19.33700 1.000 50.94615 ? 220 HOH B O   1 
HETATM 2210 O O   . HOH D 3 .   ? 15.91200 12.08500  -1.23600 1.000 41.84390 ? 221 HOH B O   1 
HETATM 2211 O O   . HOH D 3 .   ? 15.26400 4.54200   14.55600 1.000 39.59155 ? 222 HOH B O   1 
HETATM 2212 O O   . HOH D 3 .   ? 26.43500 21.36200  5.76400  1.000 38.40728 ? 223 HOH B O   1 
HETATM 2213 O O   . HOH D 3 .   ? 11.61800 3.26300   3.02400  1.000 47.17771 ? 224 HOH B O   1 
HETATM 2214 O O   . HOH D 3 .   ? 13.18400 19.35500  3.52000  1.000 34.92078 ? 225 HOH B O   1 
HETATM 2215 O O   . HOH D 3 .   ? 10.60200 14.31100  5.59200  1.000 44.40494 ? 226 HOH B O   1 
HETATM 2216 O O   . HOH D 3 .   ? 26.60800 19.89700  23.14000 1.000 45.95775 ? 227 HOH B O   1 
HETATM 2217 O O   . HOH D 3 .   ? 13.89700 18.50600  6.12500  1.000 40.75686 ? 228 HOH B O   1 
HETATM 2218 O O   . HOH D 3 .   ? 27.84400 14.64100  22.56800 1.000 42.98444 ? 229 HOH B O   1 
HETATM 2219 O O   . HOH D 3 .   ? 23.27900 6.50800   -1.51200 1.000 34.71780 ? 230 HOH B O   1 
HETATM 2220 O O   . HOH D 3 .   ? 29.07900 5.66900   17.14900 1.000 53.27684 ? 231 HOH B O   1 
HETATM 2221 O O   . HOH D 3 .   ? 22.11400 20.14400  0.01400  1.000 43.59710 ? 232 HOH B O   1 
HETATM 2222 O O   . HOH D 3 .   ? 10.74400 19.43000  22.46200 1.000 55.81293 ? 233 HOH B O   1 
HETATM 2223 O O   . HOH D 3 .   ? 21.21100 9.20800   -8.13100 1.000 45.16562 ? 234 HOH B O   1 
HETATM 2224 O O   . HOH D 3 .   ? 12.75700 28.32900  20.40800 1.000 47.58886 ? 235 HOH B O   1 
HETATM 2225 O O   . HOH D 3 .   ? 33.45100 14.16600  -1.40200 1.000 39.70216 ? 236 HOH B O   1 
HETATM 2226 O O   . HOH D 3 .   ? 29.08400 21.76600  6.09900  1.000 39.56629 ? 237 HOH B O   1 
HETATM 2227 O O   . HOH D 3 .   ? 40.49300 6.76700   6.35500  1.000 57.94586 ? 238 HOH B O   1 
HETATM 2228 O O   . HOH D 3 .   ? 13.73700 13.51000  17.85300 1.000 42.53194 ? 239 HOH B O   1 
HETATM 2229 O O   . HOH D 3 .   ? 19.26400 12.84500  19.99000 1.000 45.03047 ? 240 HOH B O   1 
HETATM 2230 O O   . HOH D 3 .   ? 31.27200 18.40200  -0.16200 1.000 53.31951 ? 241 HOH B O   1 
HETATM 2231 O O   . HOH D 3 .   ? 30.84700 16.71100  20.23700 1.000 52.37912 ? 242 HOH B O   1 
HETATM 2232 O O   . HOH D 3 .   ? 17.61300 3.18800   15.63200 1.000 36.38132 ? 243 HOH B O   1 
HETATM 2233 O O   . HOH D 3 .   ? 27.25700 0.97600   8.96200  1.000 39.29156 ? 244 HOH B O   1 
HETATM 2234 O O   . HOH D 3 .   ? 14.54000 10.63300  -3.35600 1.000 49.18854 ? 245 HOH B O   1 
HETATM 2235 O O   . HOH D 3 .   ? 19.97600 20.35300  24.28200 1.000 48.76248 ? 246 HOH B O   1 
HETATM 2236 O O   . HOH D 3 .   ? 9.30400  14.10900  13.46900 1.000 44.98709 ? 247 HOH B O   1 
HETATM 2237 O O   . HOH D 3 .   ? 24.62900 23.80700  8.83200  1.000 48.12490 ? 248 HOH B O   1 
HETATM 2238 O O   . HOH D 3 .   ? 19.838   24.451    3.947    1.000 44.23786 ? 249 HOH B O   1 
HETATM 2239 O O   . HOH D 3 .   ? 21.17100 8.43300   20.99600 1.000 43.44843 ? 250 HOH B O   1 
HETATM 2240 O O   . HOH D 3 .   ? 19.19700 4.31600   24.39000 1.000 64.36296 ? 251 HOH B O   1 
HETATM 2241 O O   . HOH D 3 .   ? 29.35000 1.60000   10.35100 1.000 49.87227 ? 252 HOH B O   1 
HETATM 2242 O O   . HOH D 3 .   ? 33.76000 0.11800   -0.59400 1.000 51.61370 ? 253 HOH B O   1 
HETATM 2243 O O   . HOH D 3 .   ? 28.11200 20.79500  -0.52900 1.000 47.28990 ? 254 HOH B O   1 
HETATM 2244 O O   . HOH D 3 .   ? 10.45000 8.12000   2.27100  1.000 46.27567 ? 255 HOH B O   1 
HETATM 2245 O O   . HOH D 3 .   ? 10.83800 4.38300   13.18500 1.000 39.88459 ? 256 HOH B O   1 
HETATM 2246 O O   . HOH D 3 .   ? 26.91100 26.78300  15.83700 1.000 47.37737 ? 257 HOH B O   1 
HETATM 2247 O O   . HOH D 3 .   ? 13.16900 29.06300  16.14100 1.000 52.46392 ? 258 HOH B O   1 
HETATM 2248 O O   . HOH D 3 .   ? 37.03500 9.27500   -3.91400 1.000 53.01779 ? 259 HOH B O   1 
HETATM 2249 O O   . HOH D 3 .   ? 31.33300 18.44000  15.69700 1.000 47.89590 ? 260 HOH B O   1 
HETATM 2250 O O   . HOH D 3 .   ? 18.07400 23.31800  26.14400 1.000 45.62348 ? 261 HOH B O   1 
HETATM 2251 O O   . HOH D 3 .   ? 19.76600 -0.44900  -4.53300 1.000 49.01073 ? 262 HOH B O   1 
HETATM 2252 O O   . HOH D 3 .   ? 27.35500 22.27500  19.60600 1.000 47.00605 ? 263 HOH B O   1 
HETATM 2253 O O   . HOH D 3 .   ? 21.31000 27.28700  11.61800 1.000 54.75676 ? 264 HOH B O   1 
HETATM 2254 O O   . HOH D 3 .   ? 17.75900 28.09800  12.08500 1.000 38.53885 ? 265 HOH B O   1 
HETATM 2255 O O   . HOH D 3 .   ? 27.89400 10.82400  21.51100 1.000 48.92753 ? 266 HOH B O   1 
HETATM 2256 O O   . HOH D 3 .   ? 11.41600 6.58000   15.73900 1.000 43.76532 ? 267 HOH B O   1 
HETATM 2257 O O   . HOH D 3 .   ? 16.08700 11.50100  21.41900 1.000 54.75304 ? 268 HOH B O   1 
HETATM 2258 O O   . HOH D 3 .   ? 10.33900 5.89700   5.61700  1.000 44.63429 ? 269 HOH B O   1 
HETATM 2259 O O   . HOH D 3 .   ? 25.20600 15.46700  22.71500 1.000 39.40935 ? 270 HOH B O   1 
HETATM 2260 O O   . HOH D 3 .   ? 10.08700 4.00600   9.90700  1.000 55.26188 ? 271 HOH B O   1 
HETATM 2261 O O   . HOH D 3 .   ? 19.59100 29.32300  15.78800 1.000 43.42924 ? 272 HOH B O   1 
HETATM 2262 O O   . HOH D 3 .   ? 22.78100 24.89700  7.72900  1.000 44.72389 ? 273 HOH B O   1 
HETATM 2263 O O   . HOH D 3 .   ? 11.39500 6.99500   -1.43300 1.000 45.83015 ? 274 HOH B O   1 
HETATM 2264 O O   . HOH D 3 .   ? 10.16700 5.63200   0.31800  1.000 58.13966 ? 275 HOH B O   1 
HETATM 2265 O O   . HOH D 3 .   ? 9.23300  12.12400  6.20700  1.000 49.28348 ? 276 HOH B O   1 
HETATM 2266 O O   . HOH D 3 .   ? 32.57500 14.82300  16.77400 1.000 51.86296 ? 277 HOH B O   1 
HETATM 2267 O O   . HOH D 3 .   ? 11.45100 13.25900  18.10100 1.000 50.83024 ? 278 HOH B O   1 
HETATM 2268 O O   . HOH D 3 .   ? 18.305   32.074    19.493   1.000 55.73707 ? 279 HOH B O   1 
HETATM 2269 O O   . HOH D 3 .   ? 19.36200 9.97200   20.16600 1.000 46.56656 ? 280 HOH B O   1 
HETATM 2270 O O   . HOH D 3 .   ? 10.61300 9.32900   -1.62000 1.000 51.73144 ? 281 HOH B O   1 
HETATM 2271 O O   . HOH D 3 .   ? 14.06300 11.42500  20.35100 1.000 56.85225 ? 282 HOH B O   1 
HETATM 2272 O O   . HOH D 3 .   ? 20.67100 -2.46700  -6.43800 1.000 53.16957 ? 283 HOH B O   1 
HETATM 2273 O O   . HOH D 3 .   ? 20.03900 19.21500  2.08800  1.000 44.10143 ? 284 HOH B O   1 
HETATM 2274 O O   . HOH D 3 .   ? 16.27700 29.25700  27.77900 1.000 54.24732 ? 285 HOH B O   1 
HETATM 2275 O O   . HOH D 3 .   ? 25.65000 17.54000  24.45700 1.000 47.59230 ? 286 HOH B O   1 
HETATM 2276 O O   . HOH D 3 .   ? 9.77000  6.96000   17.65900 1.000 55.22055 ? 287 HOH B O   1 
HETATM 2277 O O   . HOH D 3 .   ? 9.86800  3.85500   4.44900  1.000 50.44433 ? 288 HOH B O   1 
HETATM 2278 O O   . HOH D 3 .   ? 29.00200 26.00400  15.98600 1.000 58.09451 ? 289 HOH B O   1 
HETATM 2279 O O   . HOH D 3 .   ? 29.71700 24.08100  7.31000  1.000 52.91825 ? 290 HOH B O   1 
HETATM 2280 O O   . HOH D 3 .   ? 21.459   13.990    25.302   1.000 51.83311 ? 291 HOH B O   1 
HETATM 2281 O O   . HOH D 3 .   ? 32.10000 16.50000  18.18900 1.000 57.78536 ? 292 HOH B O   1 
HETATM 2282 O O   . HOH D 3 .   ? 16.58500 21.45900  26.77900 1.000 52.71233 ? 293 HOH B O   1 
HETATM 2283 O O   . HOH D 3 .   ? 34.89300 16.60500  -0.82500 1.000 51.98324 ? 294 HOH B O   1 
HETATM 2284 O O   . HOH D 3 .   ? 15.57500 30.11600  12.73700 1.000 55.84875 ? 295 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . VAL A 12  ? 0.79338 0.95341 0.71750 0.28105  -0.04563 -0.20009 12  VAL A N   
2    C CA  . VAL A 12  ? 0.62598 0.84034 0.61679 0.24067  -0.00463 -0.17805 12  VAL A CA  
3    C C   . VAL A 12  ? 0.66527 0.89310 0.65176 0.24513  -0.00623 -0.16821 12  VAL A C   
4    O O   . VAL A 12  ? 0.77453 0.93954 0.75622 0.24946  -0.04311 -0.18195 12  VAL A O   
5    C CB  . VAL A 12  ? 0.62573 0.79441 0.68890 0.19529  -0.00215 -0.17805 12  VAL A CB  
6    C CG1 . VAL A 12  ? 0.56584 0.77336 0.68724 0.14735  0.03232  -0.14826 12  VAL A CG1 
7    C CG2 . VAL A 12  ? 0.63789 0.79034 0.69444 0.19332  0.00198  -0.18084 12  VAL A CG2 
8    N N   . ALA A 13  ? 0.61794 0.92460 0.60565 0.23877  0.03110  -0.13917 13  ALA A N   
9    C CA  . ALA A 13  ? 0.57957 0.89615 0.55900 0.23728  0.03602  -0.11826 13  ALA A CA  
10   C C   . ALA A 13  ? 0.52892 0.81780 0.57467 0.17841  0.04883  -0.09764 13  ALA A C   
11   O O   . ALA A 13  ? 0.50314 0.79090 0.60034 0.13756  0.06616  -0.09140 13  ALA A O   
12   C CB  . ALA A 13  ? 0.60575 1.01802 0.55536 0.25587  0.07301  -0.08883 13  ALA A CB  
13   N N   . VAL A 14  ? 0.52772 0.79369 0.56376 0.18185  0.03898  -0.08805 14  VAL A N   
14   C CA  . VAL A 14  ? 0.53590 0.77649 0.61848 0.13850  0.05122  -0.06633 14  VAL A CA  
15   C C   . VAL A 14  ? 0.49866 0.78294 0.56428 0.12977  0.08776  -0.02859 14  VAL A C   
16   O O   . VAL A 14  ? 0.55639 0.86648 0.56916 0.16776  0.08852  -0.01959 14  VAL A O   
17   C CB  . VAL A 14  ? 0.60018 0.78529 0.68583 0.14914  0.01313  -0.08033 14  VAL A CB  
18   C CG1 . VAL A 14  ? 0.58032 0.74246 0.71167 0.11140  0.02659  -0.05840 14  VAL A CG1 
19   C CG2 . VAL A 14  ? 0.61518 0.75797 0.71628 0.15598  -0.02712 -0.11465 14  VAL A CG2 
20   N N   . SER A 15  ? 0.47884 0.76742 0.58529 0.08135  0.11675  -0.00533 15  SER A N   
21   C CA  . SER A 15  ? 0.47242 0.79740 0.56739 0.06344  0.15101  0.03417  15  SER A CA  
22   C C   . SER A 15  ? 0.58644 0.87199 0.65239 0.07398  0.14897  0.05397  15  SER A C   
23   O O   . SER A 15  ? 0.60302 0.83282 0.67422 0.08217  0.12348  0.03851  15  SER A O   
24   C CB  . SER A 15  ? 0.50942 0.83311 0.65224 0.00628  0.17382  0.04972  15  SER A CB  
25   O OG  . SER A 15  ? 0.50274 0.75232 0.66533 -0.01583 0.16576  0.05026  15  SER A OG  
26   N N   . ASP A 16  ? 0.58990 0.91116 0.62672 0.07393  0.17792  0.09222  16  ASP A N   
27   C CA  . ASP A 16  ? 0.63959 0.92136 0.64220 0.08292  0.18317  0.11878  16  ASP A CA  
28   C C   . ASP A 16  ? 0.64795 0.85275 0.67967 0.04621  0.17900  0.12134  16  ASP A C   
29   O O   . ASP A 16  ? 0.69185 0.84815 0.70216 0.06828  0.16266  0.11908  16  ASP A O   
30   C CB  . ASP A 16  ? 0.70146 1.03087 0.67987 0.07290  0.22336  0.16983  16  ASP A CB  
31   C CG  . ASP A 16  ? 0.73624 1.14773 0.66906 0.12704  0.23078  0.17510  16  ASP A CG  
32   O OD1 . ASP A 16  ? 0.74878 1.16131 0.65356 0.17934  0.19850  0.13531  16  ASP A OD1 
33   O OD2 . ASP A 16  ? 0.71907 1.19262 0.64345 0.11746  0.26743  0.22017  16  ASP A OD2 
34   N N   . GLY A 17  ? 0.63283 0.82828 0.70864 -0.00448 0.19218  0.12538  17  GLY A N   
35   C CA  . GLY A 17  ? 0.62276 0.74239 0.71491 -0.03242 0.18915  0.12864  17  GLY A CA  
36   C C   . GLY A 17  ? 0.58670 0.67065 0.69370 -0.00761 0.15866  0.09741  17  GLY A C   
37   O O   . GLY A 17  ? 0.60725 0.63867 0.70068 0.00164  0.15163  0.10435  17  GLY A O   
38   N N   . VAL A 18  ? 0.53342 0.64742 0.66884 0.00395  0.14019  0.06530  18  VAL A N   
39   C CA  . VAL A 18  ? 0.56639 0.65681 0.72600 0.02234  0.11003  0.04006  18  VAL A CA  
40   C C   . VAL A 18  ? 0.59240 0.67505 0.71802 0.06173  0.08837  0.03861  18  VAL A C   
41   O O   . VAL A 18  ? 0.60034 0.65566 0.74003 0.07110  0.07083  0.03493  18  VAL A O   
42   C CB  . VAL A 18  ? 0.53112 0.64848 0.72123 0.02535  0.09424  0.01004  18  VAL A CB  
43   C CG1 . VAL A 18  ? 0.53093 0.62730 0.75415 0.03708  0.06207  -0.01034 18  VAL A CG1 
44   C CG2 . VAL A 18  ? 0.47932 0.60598 0.69937 -0.00823 0.11528  0.01086  18  VAL A CG2 
45   N N   . ILE A 19  ? 0.60230 0.71510 0.68072 0.09006  0.08912  0.04229  19  ILE A N   
46   C CA  . ILE A 19  ? 0.61792 0.72373 0.65375 0.13505  0.06613  0.03869  19  ILE A CA  
47   C C   . ILE A 19  ? 0.60542 0.67244 0.61718 0.13515  0.08097  0.06870  19  ILE A C   
48   O O   . ILE A 19  ? 0.60830 0.65487 0.61510 0.16043  0.05644  0.06067  19  ILE A O   
49   C CB  . ILE A 19  ? 0.62489 0.77242 0.60272 0.17382  0.06873  0.04017  19  ILE A CB  
50   C CG1 . ILE A 19  ? 0.73807 0.91704 0.72644 0.18128  0.05387  0.00982  19  ILE A CG1 
51   C CG2 . ILE A 19  ? 0.62814 0.76547 0.55425 0.22786  0.04039  0.03220  19  ILE A CG2 
52   C CD1 . ILE A 19  ? 0.72345 0.87366 0.74888 0.18320  0.00890  -0.03011 19  ILE A CD1 
53   N N   . LYS A 20  ? 0.56445 0.61994 0.55946 0.10732  0.11913  0.10418  20  LYS A N   
54   C CA  . LYS A 20  ? 0.62893 0.63014 0.59040 0.10634  0.13418  0.13537  20  LYS A CA  
55   C C   . LYS A 20  ? 0.64094 0.59489 0.63472 0.09615  0.12115  0.12501  20  LYS A C   
56   O O   . LYS A 20  ? 0.66905 0.59013 0.63684 0.12457  0.11072  0.13076  20  LYS A O   
57   C CB  . LYS A 20  ? 0.70386 0.69475 0.64959 0.06684  0.17389  0.17540  20  LYS A CB  
58   C CG  . LYS A 20  ? 0.82069 0.73506 0.72536 0.05941  0.18955  0.21018  20  LYS A CG  
59   C CD  . LYS A 20  ? 0.85331 0.75437 0.74992 0.00988  0.22461  0.25174  20  LYS A CD  
60   C CE  . LYS A 20  ? 0.96675 0.78072 0.80395 0.00927  0.23967  0.29229  20  LYS A CE  
61   N NZ  . LYS A 20  ? 1.03017 0.76465 0.85504 0.02623  0.21897  0.27528  20  LYS A NZ  
62   N N   . VAL A 21  ? 0.60043 0.55433 0.64645 0.06130  0.12329  0.11170  21  VAL A N   
63   C CA  . VAL A 21  ? 0.62250 0.53687 0.69370 0.05719  0.11625  0.10688  21  VAL A CA  
64   C C   . VAL A 21  ? 0.55801 0.49587 0.65525 0.09143  0.08389  0.08587  21  VAL A C   
65   O O   . VAL A 21  ? 0.59608 0.50904 0.68639 0.11213  0.07707  0.09253  21  VAL A O   
66   C CB  . VAL A 21  ? 0.57516 0.49068 0.69229 0.01994  0.12514  0.09649  21  VAL A CB  
67   C CG1 . VAL A 21  ? 0.60171 0.50165 0.75356 0.02911  0.11357  0.08593  21  VAL A CG1 
68   C CG2 . VAL A 21  ? 0.67552 0.54896 0.76647 -0.01584 0.15069  0.11976  21  VAL A CG2 
69   N N   . PHE A 22  ? 0.55608 0.54199 0.68257 0.09885  0.06085  0.06055  22  PHE A N   
70   C CA  . PHE A 22  ? 0.58880 0.59793 0.74747 0.12364  0.02399  0.04100  22  PHE A CA  
71   C C   . PHE A 22  ? 0.60878 0.60864 0.71807 0.16465  0.01166  0.04957  22  PHE A C   
72   O O   . PHE A 22  ? 0.63618 0.63875 0.76300 0.18328  -0.00428 0.05002  22  PHE A O   
73   C CB  . PHE A 22  ? 0.55428 0.59867 0.73889 0.12493  -0.00482 0.01120  22  PHE A CB  
74   C CG  . PHE A 22  ? 0.60354 0.66831 0.81517 0.14807  -0.05077 -0.00938 22  PHE A CG  
75   C CD1 . PHE A 22  ? 0.61477 0.69601 0.89666 0.13575  -0.06538 -0.01065 22  PHE A CD1 
76   C CD2 . PHE A 22  ? 0.66300 0.73553 0.83064 0.18385  -0.08075 -0.02604 22  PHE A CD2 
77   C CE1 . PHE A 22  ? 0.62311 0.73318 0.94185 0.15036  -0.11112 -0.02741 22  PHE A CE1 
78   C CE2 . PHE A 22  ? 0.68031 0.77079 0.87512 0.20274  -0.13045 -0.04846 22  PHE A CE2 
79   C CZ  . PHE A 22  ? 0.68855 0.80017 0.96444 0.18171  -0.14668 -0.04882 22  PHE A CZ  
80   N N   . ASN A 23  ? 0.60656 0.60239 0.65226 0.18388  0.01999  0.05848  23  ASN A N   
81   C CA  . ASN A 23  ? 0.66428 0.65058 0.65373 0.23008  0.00869  0.06698  23  ASN A CA  
82   C C   . ASN A 23  ? 0.67586 0.61230 0.63605 0.23517  0.03023  0.09612  23  ASN A C   
83   O O   . ASN A 23  ? 0.74262 0.67556 0.67986 0.27520  0.01256  0.09696  23  ASN A O   
84   C CB  . ASN A 23  ? 0.73546 0.72963 0.65755 0.25270  0.02049  0.07707  23  ASN A CB  
85   C CG  . ASN A 23  ? 0.79961 0.83595 0.72904 0.27270  -0.01453 0.04139  23  ASN A CG  
86   O OD1 . ASN A 23  ? 0.85813 0.90836 0.80701 0.29672  -0.06042 0.01154  23  ASN A OD1 
87   N ND2 . ASN A 23  ? 0.81772 0.87442 0.73118 0.26379  0.00377  0.04357  23  ASN A ND2 
88   N N   . ASP A 24  ? 0.67303 0.56741 0.63048 0.19812  0.06422  0.11772  24  ASP A N   
89   C CA  . ASP A 24  ? 0.76063 0.59135 0.68339 0.20565  0.07901  0.14123  24  ASP A CA  
90   C C   . ASP A 24  ? 0.70375 0.55005 0.67550 0.21940  0.05894  0.12622  24  ASP A C   
91   O O   . ASP A 24  ? 0.73942 0.55504 0.67620 0.25384  0.05690  0.13828  24  ASP A O   
92   C CB  . ASP A 24  ? 0.78842 0.56170 0.69557 0.16047  0.11228  0.16366  24  ASP A CB  
93   C CG  . ASP A 24  ? 0.88695 0.64279 0.74165 0.14707  0.13786  0.19291  24  ASP A CG  
94   O OD1 . ASP A 24  ? 0.94393 0.70671 0.74820 0.18513  0.13646  0.20509  24  ASP A OD1 
95   O OD2 . ASP A 24  ? 0.95869 0.69941 0.82434 0.09907  0.15957  0.20565  24  ASP A OD2 
96   N N   . MET A 25  ? 0.67223 0.56832 0.72242 0.19606  0.04595  0.10355  25  MET A N   
97   C CA  . MET A 25  ? 0.64971 0.57467 0.75614 0.20626  0.03192  0.09660  25  MET A CA  
98   C C   . MET A 25  ? 0.63593 0.62298 0.77471 0.23940  -0.00610 0.08184  25  MET A C   
99   O O   . MET A 25  ? 0.65838 0.67553 0.83219 0.25922  -0.01613 0.08526  25  MET A O   
100  C CB  . MET A 25  ? 0.57162 0.52332 0.74900 0.16737  0.03651  0.08463  25  MET A CB  
101  C CG  . MET A 25  ? 0.53477 0.42985 0.68739 0.13779  0.06863  0.09589  25  MET A CG  
102  S SD  . MET A 25  ? 0.44970 0.37633 0.67570 0.10200  0.07473  0.08153  25  MET A SD  
103  C CE  . MET A 25  ? 0.41664 0.36099 0.67950 0.13044  0.07326  0.09057  25  MET A CE  
104  N N   . LYS A 26  ? 0.56002 0.80218 0.83550 0.12754  0.05439  -0.02390 26  LYS A N   
105  C CA  . LYS A 26  ? 0.53936 0.76889 0.79945 0.14994  0.04029  -0.03938 26  LYS A CA  
106  C C   . LYS A 26  ? 0.55077 0.76800 0.76156 0.16483  0.02615  -0.05915 26  LYS A C   
107  O O   . LYS A 26  ? 0.64739 0.85985 0.86799 0.15509  0.01398  -0.06281 26  LYS A O   
108  C CB  . LYS A 26  ? 0.56100 0.78966 0.80492 0.17477  0.04015  -0.05544 26  LYS A CB  
109  C CG  . LYS A 26  ? 0.59657 0.83284 0.88615 0.16827  0.04520  -0.04470 26  LYS A CG  
110  N N   . THR A 32  ? 0.79253 0.71435 0.67229 0.18869  0.14753  0.14660  32  THR A N   
111  C CA  . THR A 32  ? 0.74276 0.62367 0.66335 0.15580  0.13934  0.15804  32  THR A CA  
112  C C   . THR A 32  ? 0.63080 0.52926 0.59027 0.11978  0.09781  0.12249  32  THR A C   
113  O O   . THR A 32  ? 0.60687 0.55335 0.59710 0.10670  0.08947  0.11036  32  THR A O   
114  C CB  . THR A 32  ? 0.74810 0.61827 0.73857 0.13743  0.17476  0.21045  32  THR A CB  
115  O OG1 . THR A 32  ? 0.72408 0.61760 0.80272 0.09010  0.15765  0.20623  32  THR A OG1 
116  C CG2 . THR A 32  ? 0.93312 0.83145 0.90183 0.17369  0.21802  0.24449  32  THR A CG2 
117  N N   . PRO A 33  ? 0.61903 0.47974 0.57148 0.11015  0.07146  0.10515  33  PRO A N   
118  C CA  . PRO A 33  ? 0.59866 0.47954 0.57636 0.08779  0.03128  0.07083  33  PRO A CA  
119  C C   . PRO A 33  ? 0.54604 0.45840 0.60788 0.05253  0.02688  0.07780  33  PRO A C   
120  O O   . PRO A 33  ? 0.52070 0.47830 0.59689 0.04563  0.00728  0.05669  33  PRO A O   
121  C CB  . PRO A 33  ? 0.64003 0.46543 0.59831 0.08830  0.00778  0.05688  33  PRO A CB  
122  C CG  . PRO A 33  ? 0.66211 0.44983 0.55445 0.12152  0.03182  0.07253  33  PRO A CG  
123  C CD  . PRO A 33  ? 0.65571 0.45629 0.56681 0.12770  0.07601  0.11348  33  PRO A CD  
124  N N   . GLU A 34  ? 0.56397 0.45612 0.68742 0.03189  0.04592  0.10959  34  GLU A N   
125  C CA  . GLU A 34  ? 0.54253 0.46829 0.75390 -0.00163 0.03983  0.11525  34  GLU A CA  
126  C C   . GLU A 34  ? 0.52709 0.51169 0.74369 0.00272  0.06169  0.12667  34  GLU A C   
127  O O   . GLU A 34  ? 0.53990 0.56868 0.79771 -0.01437 0.04526  0.11340  34  GLU A O   
128  C CB  . GLU A 34  ? 0.61120 0.50298 0.90226 -0.02491 0.05795  0.15128  34  GLU A CB  
129  C CG  . GLU A 34  ? 0.69800 0.53491 1.01530 -0.03884 0.02342  0.13048  34  GLU A CG  
130  C CD  . GLU A 34  ? 0.75350 0.61286 1.08293 -0.05003 -0.03174 0.07865  34  GLU A CD  
131  O OE1 . GLU A 34  ? 0.82764 0.73281 1.22107 -0.07095 -0.04198 0.07453  34  GLU A OE1 
132  O OE2 . GLU A 34  ? 0.75404 0.58907 1.02526 -0.03266 -0.06367 0.04338  34  GLU A OE2 
133  N N   . GLU A 35  ? 0.54671 0.53332 0.72002 0.03013  0.09726  0.14953  35  GLU A N   
134  C CA  . GLU A 35  ? 0.55066 0.58940 0.72712 0.03867  0.11444  0.15540  35  GLU A CA  
135  C C   . GLU A 35  ? 0.55459 0.62609 0.70079 0.04702  0.08775  0.11662  35  GLU A C   
136  O O   . GLU A 35  ? 0.48362 0.60147 0.66261 0.03871  0.08733  0.11362  35  GLU A O   
137  C CB  . GLU A 35  ? 0.62339 0.65634 0.75444 0.07567  0.15444  0.18378  35  GLU A CB  
138  C CG  . GLU A 35  ? 0.73521 0.75545 0.91513 0.07000  0.19339  0.23706  35  GLU A CG  
139  C CD  . GLU A 35  ? 0.79561 0.85926 1.06219 0.03922  0.20135  0.25561  35  GLU A CD  
140  O OE1 . GLU A 35  ? 0.83845 0.94733 1.09716 0.04833  0.20414  0.24660  35  GLU A OE1 
141  O OE2 . GLU A 35  ? 0.90298 0.95536 1.25154 0.00620  0.20303  0.27784  35  GLU A OE2 
142  N N   . VAL A 36  ? 0.47469 0.52447 0.56547 0.06403  0.06726  0.09028  36  VAL A N   
143  C CA  . VAL A 36  ? 0.52591 0.60926 0.60039 0.07372  0.04657  0.06076  36  VAL A CA  
144  C C   . VAL A 36  ? 0.47221 0.58571 0.59308 0.05044  0.02253  0.04922  36  VAL A C   
145  O O   . VAL A 36  ? 0.43400 0.59279 0.57429 0.05193  0.01866  0.04180  36  VAL A O   
146  C CB  . VAL A 36  ? 0.57103 0.62725 0.58098 0.09941  0.03219  0.03920  36  VAL A CB  
147  C CG1 . VAL A 36  ? 0.60838 0.69939 0.62055 0.10449  0.00905  0.01433  36  VAL A CG1 
148  C CG2 . VAL A 36  ? 0.65321 0.69729 0.61555 0.13205  0.05258  0.04348  36  VAL A CG2 
149  N N   . LYS A 37  ? 0.42134 0.51112 0.56453 0.03205  0.00540  0.04730  37  LYS A N   
150  C CA  . LYS A 37  ? 0.37396 0.49435 0.55626 0.01791  -0.02220 0.03172  37  LYS A CA  
151  C C   . LYS A 37  ? 0.40990 0.57902 0.65296 0.00073  -0.01016 0.04640  37  LYS A C   
152  O O   . LYS A 37  ? 0.33023 0.53950 0.59699 -0.00117 -0.02926 0.03383  37  LYS A O   
153  C CB  . LYS A 37  ? 0.41833 0.50086 0.62270 0.00297  -0.04805 0.02110  37  LYS A CB  
154  C CG  . LYS A 37  ? 0.47577 0.51091 0.62254 0.02089  -0.06765 0.00152  37  LYS A CG  
155  C CD  . LYS A 37  ? 0.58038 0.57735 0.76341 0.00517  -0.09830 -0.01358 37  LYS A CD  
156  C CE  . LYS A 37  ? 0.66883 0.61087 0.79391 0.02436  -0.11674 -0.03202 37  LYS A CE  
157  N NZ  . LYS A 37  ? 0.77910 0.67826 0.94686 0.01041  -0.15184 -0.05222 37  LYS A NZ  
158  N N   . LYS A 38  ? 0.34153 0.51014 0.60784 -0.00710 0.02179  0.07441  38  LYS A N   
159  C CA  . LYS A 38  ? 0.32021 0.53556 0.64337 -0.02154 0.03549  0.09058  38  LYS A CA  
160  C C   . LYS A 38  ? 0.33418 0.58786 0.64176 -0.00410 0.05077  0.09092  38  LYS A C   
161  O O   . LYS A 38  ? 0.34303 0.63838 0.69371 -0.01257 0.06065  0.10200  38  LYS A O   
162  C CB  . LYS A 38  ? 0.37003 0.57153 0.73365 -0.03539 0.06499  0.12550  38  LYS A CB  
163  C CG  . LYS A 38  ? 0.42422 0.59147 0.83543 -0.05899 0.05086  0.12941  38  LYS A CG  
164  C CD  . LYS A 38  ? 0.51047 0.66914 0.97480 -0.07069 0.08797  0.17446  38  LYS A CD  
165  C CE  . LYS A 38  ? 0.63617 0.73432 1.11539 -0.07804 0.08864  0.18671  38  LYS A CE  
166  N NZ  . LYS A 38  ? 0.75790 0.84537 1.27212 -0.07597 0.13770  0.24198  38  LYS A NZ  
167  N N   . ARG A 39  ? 0.38589 0.62605 0.64042 0.02012  0.05150  0.07816  39  ARG A N   
168  C CA  . ARG A 39  ? 0.39978 0.67287 0.65401 0.03614  0.05913  0.07253  39  ARG A CA  
169  C C   . ARG A 39  ? 0.31243 0.62865 0.60070 0.03038  0.04457  0.06539  39  ARG A C   
170  O O   . ARG A 39  ? 0.28068 0.60117 0.56755 0.02828  0.02273  0.05562  39  ARG A O   
171  C CB  . ARG A 39  ? 0.37011 0.62037 0.57309 0.06215  0.05415  0.05434  39  ARG A CB  
172  C CG  . ARG A 39  ? 0.52274 0.73830 0.68310 0.08075  0.07233  0.06117  39  ARG A CG  
173  C CD  . ARG A 39  ? 0.62466 0.81804 0.73254 0.10887  0.06159  0.03835  39  ARG A CD  
174  N NE  . ARG A 39  ? 0.73100 0.89311 0.79012 0.13367  0.07904  0.04653  39  ARG A NE  
175  C CZ  . ARG A 39  ? 0.79095 0.92958 0.79506 0.16399  0.07236  0.02908  39  ARG A CZ  
176  N NH1 . ARG A 39  ? 0.78962 0.93166 0.78624 0.17001  0.04807  0.00202  39  ARG A NH1 
177  N NH2 . ARG A 39  ? 0.88471 0.99946 0.84142 0.19280  0.09214  0.04177  39  ARG A NH2 
178  N N   . LYS A 40  ? 0.75395 0.30880 0.57800 0.18199  0.02259  0.07364  40  LYS A N   
179  C CA  . LYS A 40  ? 0.68158 0.28310 0.56512 0.16485  0.01133  0.06099  40  LYS A CA  
180  C C   . LYS A 40  ? 0.67974 0.34011 0.57100 0.19657  -0.01370 0.04376  40  LYS A C   
181  O O   . LYS A 40  ? 0.70512 0.39867 0.57831 0.22501  -0.02470 0.03980  40  LYS A O   
182  C CB  . LYS A 40  ? 0.66001 0.29710 0.58612 0.13822  0.01878  0.06438  40  LYS A CB  
183  C CG  . LYS A 40  ? 0.78017 0.37683 0.70050 0.11424  0.04557  0.08072  40  LYS A CG  
184  C CD  . LYS A 40  ? 0.81231 0.37425 0.74788 0.08139  0.05887  0.07978  40  LYS A CD  
185  C CE  . LYS A 40  ? 0.80240 0.36617 0.76606 0.04671  0.08392  0.08764  40  LYS A CE  
186  N NZ  . LYS A 40  ? 0.81037 0.33202 0.77252 0.01695  0.10115  0.08557  40  LYS A NZ  
187  N N   . LYS A 41  ? 0.65353 0.33633 0.57571 0.18829  -0.02263 0.03004  41  LYS A N   
188  C CA  . LYS A 41  ? 0.59512 0.35596 0.54579 0.20143  -0.04059 0.00971  41  LYS A CA  
189  C C   . LYS A 41  ? 0.51544 0.33560 0.52061 0.16519  -0.03929 0.00259  41  LYS A C   
190  O O   . LYS A 41  ? 0.45224 0.33530 0.47746 0.16723  -0.04590 -0.01046 41  LYS A O   
191  C CB  . LYS A 41  ? 0.62841 0.37677 0.57203 0.21579  -0.04712 -0.00131 41  LYS A CB  
192  C CG  . LYS A 41  ? 0.56558 0.39611 0.54379 0.22376  -0.05915 -0.02380 41  LYS A CG  
193  C CD  . LYS A 41  ? 0.56684 0.45481 0.53773 0.26291  -0.07219 -0.03597 41  LYS A CD  
194  C CE  . LYS A 41  ? 0.55457 0.52250 0.55971 0.27304  -0.07971 -0.06201 41  LYS A CE  
195  N NZ  . LYS A 41  ? 0.50603 0.54672 0.51301 0.29929  -0.09209 -0.07825 41  LYS A NZ  
196  N N   . ALA A 42  ? 0.46743 0.26668 0.49412 0.13234  -0.02993 0.00958  42  ALA A N   
197  C CA  . ALA A 42  ? 0.42980 0.26972 0.49549 0.10431  -0.02705 0.00672  42  ALA A CA  
198  C C   . ALA A 42  ? 0.44219 0.25248 0.51995 0.08017  -0.01540 0.01984  42  ALA A C   
199  O O   . ALA A 42  ? 0.44663 0.21262 0.51496 0.07473  -0.01067 0.02426  42  ALA A O   
200  C CB  . ALA A 42  ? 0.41372 0.28066 0.49937 0.09642  -0.03318 -0.00687 42  ALA A CB  
201  N N   . VAL A 43  ? 0.44092 0.27676 0.54007 0.06514  -0.00924 0.02349  43  VAL A N   
202  C CA  . VAL A 43  ? 0.44379 0.26971 0.56376 0.04516  0.00184  0.03285  43  VAL A CA  
203  C C   . VAL A 43  ? 0.39871 0.26076 0.54294 0.03579  0.00129  0.03008  43  VAL A C   
204  O O   . VAL A 43  ? 0.37396 0.25432 0.51017 0.04038  0.00175  0.02667  43  VAL A O   
205  C CB  . VAL A 43  ? 0.48503 0.28399 0.58725 0.04691  0.01848  0.04728  43  VAL A CB  
206  C CG1 . VAL A 43  ? 0.61707 0.36213 0.68576 0.05511  0.02499  0.05371  43  VAL A CG1 
207  C CG2 . VAL A 43  ? 0.51027 0.32756 0.59346 0.06158  0.01737  0.04719  43  VAL A CG2 
208  N N   . LEU A 44  ? 0.35815 0.22882 0.52922 0.02343  0.00085  0.02975  44  LEU A N   
209  C CA  . LEU A 44  ? 0.37579 0.27219 0.56055 0.02279  0.00025  0.02916  44  LEU A CA  
210  C C   . LEU A 44  ? 0.35035 0.25506 0.55413 0.01826  0.01370  0.03824  44  LEU A C   
211  O O   . LEU A 44  ? 0.35476 0.25390 0.57595 0.00740  0.02157  0.04097  44  LEU A O   
212  C CB  . LEU A 44  ? 0.34601 0.25589 0.54380 0.02173  -0.01455 0.01935  44  LEU A CB  
213  C CG  . LEU A 44  ? 0.39309 0.30014 0.56781 0.02949  -0.02355 0.01096  44  LEU A CG  
214  C CD1 . LEU A 44  ? 0.42908 0.32065 0.59039 0.03193  -0.02699 0.00527  44  LEU A CD1 
215  C CD2 . LEU A 44  ? 0.38613 0.30371 0.56548 0.03295  -0.03799 0.00287  44  LEU A CD2 
216  N N   . PHE A 45  ? 0.34297 0.25669 0.54013 0.02584  0.01987  0.04200  45  PHE A N   
217  C CA  . PHE A 45  ? 0.34781 0.27379 0.56065 0.02819  0.03317  0.04937  45  PHE A CA  
218  C C   . PHE A 45  ? 0.30190 0.24871 0.52312 0.04071  0.02653  0.04657  45  PHE A C   
219  O O   . PHE A 45  ? 0.33561 0.26864 0.52852 0.04916  0.02077  0.04401  45  PHE A O   
220  C CB  . PHE A 45  ? 0.38773 0.29475 0.57145 0.03344  0.04835  0.05642  45  PHE A CB  
221  C CG  . PHE A 45  ? 0.40219 0.28780 0.56321 0.03103  0.05078  0.05817  45  PHE A CG  
222  C CD1 . PHE A 45  ? 0.51321 0.38592 0.68054 0.02514  0.05542  0.06315  45  PHE A CD1 
223  C CD2 . PHE A 45  ? 0.52634 0.40355 0.65628 0.03573  0.04869  0.05285  45  PHE A CD2 
224  C CE1 . PHE A 45  ? 0.58339 0.42750 0.71599 0.03232  0.05697  0.06660  45  PHE A CE1 
225  C CE2 . PHE A 45  ? 0.51362 0.37898 0.62002 0.04182  0.04605  0.05222  45  PHE A CE2 
226  C CZ  . PHE A 45  ? 0.52179 0.36745 0.62488 0.04412  0.04961  0.06080  45  PHE A CZ  
227  N N   . CYS A 46  ? 0.34037 0.31922 0.59620 0.04442  0.03029  0.04702  46  CYS A N   
228  C CA  . CYS A 46  ? 0.31766 0.32088 0.57853 0.06621  0.02130  0.04395  46  CYS A CA  
229  C C   . CYS A 46  ? 0.32397 0.35200 0.60525 0.07862  0.03686  0.04909  46  CYS A C   
230  O O   . CYS A 46  ? 0.32183 0.35090 0.61806 0.06576  0.05558  0.05424  46  CYS A O   
231  C CB  . CYS A 46  ? 0.35892 0.40031 0.65239 0.06502  -0.00192 0.02976  46  CYS A CB  
232  S SG  . CYS A 46  ? 0.32472 0.41376 0.68826 0.03660  0.00162  0.01848  46  CYS A SG  
233  N N   . LEU A 47  ? 0.33403 0.37868 0.60941 0.10824  0.03024  0.04807  47  LEU A N   
234  C CA  . LEU A 47  ? 0.37928 0.46000 0.67983 0.12786  0.04224  0.04986  47  LEU A CA  
235  C C   . LEU A 47  ? 0.36939 0.52844 0.74770 0.11530  0.03674  0.03602  47  LEU A C   
236  O O   . LEU A 47  ? 0.39284 0.58424 0.79896 0.10663  0.01400  0.02165  47  LEU A O   
237  C CB  . LEU A 47  ? 0.42103 0.49298 0.68489 0.17118  0.03496  0.05217  47  LEU A CB  
238  C CG  . LEU A 47  ? 0.52285 0.51182 0.70859 0.18099  0.05082  0.06441  47  LEU A CG  
239  C CD1 . LEU A 47  ? 0.52422 0.49182 0.66415 0.22746  0.04742  0.06820  47  LEU A CD1 
240  C CD2 . LEU A 47  ? 0.54191 0.51278 0.72386 0.17084  0.07748  0.07141  47  LEU A CD2 
241  N N   . SER A 48  ? 0.30086 0.49076 0.71396 0.11193  0.05974  0.03793  48  SER A N   
242  C CA  . SER A 48  ? 0.29185 0.56754 0.78637 0.09935  0.06075  0.02124  48  SER A CA  
243  C C   . SER A 48  ? 0.34875 0.69464 0.87077 0.13820  0.03567  0.00655  48  SER A C   
244  O O   . SER A 48  ? 0.37978 0.69407 0.84701 0.17901  0.02344  0.01435  48  SER A O   
245  C CB  . SER A 48  ? 0.32852 0.61807 0.84721 0.09004  0.09738  0.02793  48  SER A CB  
246  O OG  . SER A 48  ? 0.38506 0.66811 0.87383 0.13152  0.10681  0.03738  48  SER A OG  
247  N N   . GLU A 49  ? 0.29119 0.73349 0.89699 0.12620  0.02948  -0.01656 49  GLU A N   
248  C CA  . GLU A 49  ? 0.30039 0.82525 0.93806 0.16659  -0.00116 -0.03597 49  GLU A CA  
249  C C   . GLU A 49  ? 0.36807 0.89801 0.97790 0.22396  0.00667  -0.02479 49  GLU A C   
250  O O   . GLU A 49  ? 0.43679 0.94928 0.99656 0.26759  -0.01689 -0.02160 49  GLU A O   
251  C CB  . GLU A 49  ? 0.29455 0.92830 1.02641 0.13640  -0.00585 -0.06536 49  GLU A CB  
252  N N   . ASP A 50  ? 0.35269 0.88243 0.97553 0.21947  0.04299  -0.01474 50  ASP A N   
253  C CA  . ASP A 50  ? 0.41646 0.93057 1.00009 0.26858  0.05196  -0.00689 50  ASP A CA  
254  C C   . ASP A 50  ? 0.42253 0.81312 0.89565 0.28907  0.05980  0.01904  50  ASP A C   
255  O O   . ASP A 50  ? 0.52300 0.87339 0.94300 0.32092  0.06788  0.02525  50  ASP A O   
256  C CB  . ASP A 50  ? 0.38501 0.94701 1.01749 0.25630  0.08704  -0.01227 50  ASP A CB  
257  C CG  . ASP A 50  ? 0.39873 0.89563 1.01001 0.21777  0.12668  0.01063  50  ASP A CG  
258  O OD1 . ASP A 50  ? 0.42590 0.83509 0.98191 0.19795  0.12395  0.02583  50  ASP A OD1 
259  O OD2 . ASP A 50  ? 0.46455 0.98893 1.10264 0.20429  0.15811  0.00878  50  ASP A OD2 
260  N N   . LYS A 51  ? 0.47435 0.79699 0.90906 0.26218  0.05660  0.03027  51  LYS A N   
261  C CA  . LYS A 51  ? 0.55758 0.76693 0.89564 0.26933  0.06416  0.04910  51  LYS A CA  
262  C C   . LYS A 51  ? 0.55807 0.71560 0.86270 0.26589  0.09903  0.06268  51  LYS A C   
263  O O   . LYS A 51  ? 0.55656 0.62938 0.78037 0.27874  0.10712  0.07261  51  LYS A O   
264  C CB  . LYS A 51  ? 0.60326 0.77354 0.87285 0.31228  0.04442  0.04935  51  LYS A CB  
265  C CG  . LYS A 51  ? 0.62875 0.81390 0.89817 0.31565  0.01159  0.04081  51  LYS A CG  
266  C CD  . LYS A 51  ? 0.72835 0.87762 0.92828 0.35433  -0.00278 0.04208  51  LYS A CD  
267  C CE  . LYS A 51  ? 0.77288 0.92008 0.95127 0.35964  -0.03141 0.03641  51  LYS A CE  
268  N NZ  . LYS A 51  ? 0.89787 0.99948 0.99333 0.40039  -0.03765 0.04154  51  LYS A NZ  
269  N N   . LYS A 52  ? 0.50017 0.70088 0.85808 0.24245  0.12033  0.06057  52  LYS A N   
270  C CA  . LYS A 52  ? 0.51064 0.66509 0.83468 0.24043  0.15325  0.07211  52  LYS A CA  
271  C C   . LYS A 52  ? 0.49996 0.61064 0.81084 0.19360  0.16536  0.07838  52  LYS A C   
272  O O   . LYS A 52  ? 0.50801 0.57718 0.78389 0.19106  0.19031  0.08683  52  LYS A O   
273  C CB  . LYS A 52  ? 0.49219 0.72003 0.86977 0.25535  0.17330  0.06587  52  LYS A CB  
274  C CG  . LYS A 52  ? 0.55648 0.82640 0.93403 0.29840  0.15268  0.05286  52  LYS A CG  
275  C CD  . LYS A 52  ? 0.67896 0.85197 0.95393 0.32812  0.14832  0.06315  52  LYS A CD  
276  C CE  . LYS A 52  ? 0.68022 0.88044 0.94573 0.37283  0.13398  0.05445  52  LYS A CE  
277  N NZ  . LYS A 52  ? 0.78523 0.96486 1.01969 0.39459  0.15849  0.05876  52  LYS A NZ  
278  N N   . ASN A 53  ? 0.42673 0.54347 0.75886 0.16130  0.14761  0.07373  53  ASN A N   
279  C CA  . ASN A 53  ? 0.45710 0.53618 0.77647 0.12381  0.15658  0.07910  53  ASN A CA  
280  C C   . ASN A 53  ? 0.43269 0.48334 0.73257 0.10838  0.13015  0.07589  53  ASN A C   
281  O O   . ASN A 53  ? 0.35786 0.43964 0.68115 0.11385  0.10695  0.06683  53  ASN A O   
282  C CB  . ASN A 53  ? 0.36787 0.49335 0.74834 0.09478  0.17326  0.07537  53  ASN A CB  
283  C CG  . ASN A 53  ? 0.45294 0.62109 0.86535 0.10642  0.20385  0.07599  53  ASN A CG  
284  O OD1 . ASN A 53  ? 0.60556 0.73409 0.98210 0.10607  0.23155  0.08731  53  ASN A OD1 
285  N ND2 . ASN A 53  ? 0.46283 0.71738 0.94315 0.11899  0.19854  0.06176  53  ASN A ND2 
286  N N   . ILE A 54  ? 0.43743 0.43309 0.69340 0.09215  0.13341  0.08170  54  ILE A N   
287  C CA  . ILE A 54  ? 0.43171 0.40520 0.67302 0.07603  0.11288  0.07784  54  ILE A CA  
288  C C   . ILE A 54  ? 0.44295 0.42084 0.70853 0.05025  0.11814  0.07852  54  ILE A C   
289  O O   . ILE A 54  ? 0.44542 0.39983 0.69337 0.04429  0.13891  0.08689  54  ILE A O   
290  C CB  . ILE A 54  ? 0.45792 0.37724 0.63844 0.07709  0.11205  0.07934  54  ILE A CB  
291  C CG1 . ILE A 54  ? 0.57041 0.46914 0.71851 0.09755  0.11139  0.07785  54  ILE A CG1 
292  C CG2 . ILE A 54  ? 0.44527 0.35345 0.61903 0.06044  0.09386  0.07378  54  ILE A CG2 
293  C CD1 . ILE A 54  ? 0.62027 0.46615 0.71040 0.09542  0.12195  0.07608  54  ILE A CD1 
294  N N   . ILE A 55  ? 0.35056 0.35032 0.64841 0.03643  0.10126  0.06964  55  ILE A N   
295  C CA  . ILE A 55  ? 0.37348 0.37161 0.69484 0.01015  0.10942  0.06810  55  ILE A CA  
296  C C   . ILE A 55  ? 0.38402 0.35445 0.68612 0.00169  0.08857  0.06303  55  ILE A C   
297  O O   . ILE A 55  ? 0.37069 0.34002 0.65639 0.01342  0.06742  0.05810  55  ILE A O   
298  C CB  . ILE A 55  ? 0.38779 0.44839 0.77930 -0.00406 0.11431  0.05602  55  ILE A CB  
299  C CG1 . ILE A 55  ? 0.33951 0.44493 0.75870 0.00598  0.08221  0.04007  55  ILE A CG1 
300  C CG2 . ILE A 55  ? 0.32333 0.41954 0.73915 0.00646  0.13956  0.06004  55  ILE A CG2 
301  C CD1 . ILE A 55  ? 0.31109 0.49184 0.80488 -0.00829 0.07953  0.02074  55  ILE A CD1 
302  N N   . LEU A 56  ? 0.42942 0.37075 0.72763 -0.01766 0.09860  0.06480  56  LEU A N   
303  C CA  . LEU A 56  ? 0.41638 0.33326 0.70137 -0.02468 0.08085  0.05776  56  LEU A CA  
304  C C   . LEU A 56  ? 0.42733 0.38860 0.75878 -0.03453 0.06178  0.03997  56  LEU A C   
305  O O   . LEU A 56  ? 0.38400 0.38640 0.76604 -0.05089 0.06984  0.03092  56  LEU A O   
306  C CB  . LEU A 56  ? 0.52023 0.38465 0.78350 -0.04085 0.09988  0.06394  56  LEU A CB  
307  C CG  . LEU A 56  ? 0.63672 0.44864 0.84144 -0.02619 0.11643  0.08109  56  LEU A CG  
308  C CD1 . LEU A 56  ? 0.65433 0.40512 0.83278 -0.04173 0.14272  0.08943  56  LEU A CD1 
309  C CD2 . LEU A 56  ? 0.53432 0.33232 0.69832 -0.00250 0.09286  0.07978  56  LEU A CD2 
310  N N   . GLU A 57  ? 0.38137 0.33854 0.69638 -0.02486 0.03694  0.03246  57  GLU A N   
311  C CA  . GLU A 57  ? 0.37671 0.36919 0.72432 -0.03121 0.01572  0.01399  57  GLU A CA  
312  C C   . GLU A 57  ? 0.39209 0.35596 0.74403 -0.05700 0.01741  0.00390  57  GLU A C   
313  O O   . GLU A 57  ? 0.43739 0.35083 0.74752 -0.05296 0.01471  0.00745  57  GLU A O   
314  C CB  . GLU A 57  ? 0.31785 0.31105 0.63783 -0.00911 -0.00760 0.01054  57  GLU A CB  
315  C CG  . GLU A 57  ? 0.35717 0.39116 0.70518 -0.00867 -0.03132 -0.00868 57  GLU A CG  
316  C CD  . GLU A 57  ? 0.33614 0.36482 0.64803 0.01593  -0.05049 -0.01042 57  GLU A CD  
317  O OE1 . GLU A 57  ? 0.36504 0.35508 0.63422 0.02353  -0.04501 -0.00094 57  GLU A OE1 
318  O OE2 . GLU A 57  ? 0.34698 0.41279 0.67292 0.02789  -0.07019 -0.02293 57  GLU A OE2 
319  N N   . GLU A 58  ? 0.38931 0.38649 0.79200 -0.08338 0.02281  -0.01116 58  GLU A N   
320  C CA  . GLU A 58  ? 0.45534 0.41411 0.86068 -0.11630 0.03371  -0.02180 58  GLU A CA  
321  C C   . GLU A 58  ? 0.55217 0.47552 0.92436 -0.11140 0.01059  -0.03253 58  GLU A C   
322  O O   . GLU A 58  ? 0.44050 0.40198 0.82330 -0.09963 -0.01792 -0.04701 58  GLU A O   
323  C CB  . GLU A 58  ? 0.50774 0.52704 0.98483 -0.14983 0.03889  -0.04526 58  GLU A CB  
324  C CG  . GLU A 58  ? 0.65601 0.62795 1.13552 -0.19298 0.05629  -0.05966 58  GLU A CG  
325  C CD  . GLU A 58  ? 0.92248 0.81634 1.36278 -0.20653 0.09925  -0.03717 58  GLU A CD  
326  O OE1 . GLU A 58  ? 0.86570 0.76963 1.30238 -0.19136 0.11733  -0.01682 58  GLU A OE1 
327  O OE2 . GLU A 58  ? 0.98333 0.80508 1.37242 -0.22181 0.11090  -0.03780 58  GLU A OE2 
328  N N   . GLY A 59  ? 0.51197 0.35766 0.83668 -0.11590 0.02401  -0.02489 59  GLY A N   
329  C CA  . GLY A 59  ? 0.60113 0.40683 0.89153 -0.11033 0.00679  -0.03579 59  GLY A CA  
330  C C   . GLY A 59  ? 0.50532 0.31302 0.75966 -0.07285 -0.01343 -0.02868 59  GLY A C   
331  O O   . GLY A 59  ? 0.55414 0.32623 0.77514 -0.06384 -0.02426 -0.03641 59  GLY A O   
332  N N   . LYS A 60  ? 0.41842 0.26369 0.67673 -0.05246 -0.01588 -0.01607 60  LYS A N   
333  C CA  . LYS A 60  ? 0.42396 0.27668 0.65423 -0.02484 -0.03052 -0.01316 60  LYS A CA  
334  C C   . LYS A 60  ? 0.43250 0.25341 0.62509 -0.00773 -0.01883 0.00204  60  LYS A C   
335  O O   . LYS A 60  ? 0.39337 0.23202 0.58194 0.00330  -0.01363 0.01225  60  LYS A O   
336  C CB  . LYS A 60  ? 0.39017 0.29392 0.63973 -0.01453 -0.03882 -0.01200 60  LYS A CB  
337  C CG  . LYS A 60  ? 0.36863 0.31260 0.65281 -0.02267 -0.05565 -0.02936 60  LYS A CG  
338  C CD  . LYS A 60  ? 0.41619 0.34702 0.68286 -0.02149 -0.07525 -0.04666 60  LYS A CD  
339  C CE  . LYS A 60  ? 0.39758 0.37781 0.69892 -0.02689 -0.09636 -0.06749 60  LYS A CE  
340  N NZ  . LYS A 60  ? 0.46912 0.43319 0.75977 -0.03587 -0.11366 -0.08984 60  LYS A NZ  
341  N N   . GLU A 61  ? 0.32526 0.35944 0.57128 -0.05885 -0.03749 0.02962  61  GLU A N   
342  C CA  . GLU A 61  ? 0.35656 0.40164 0.60599 -0.04500 -0.02860 0.03435  61  GLU A CA  
343  C C   . GLU A 61  ? 0.33228 0.33102 0.57271 -0.04191 -0.02798 0.03134  61  GLU A C   
344  O O   . GLU A 61  ? 0.39251 0.34917 0.62473 -0.05237 -0.03659 0.02864  61  GLU A O   
345  C CB  . GLU A 61  ? 0.32507 0.40828 0.59285 -0.04451 -0.02713 0.05895  61  GLU A CB  
346  C CG  . GLU A 61  ? 0.35130 0.41121 0.63215 -0.06060 -0.03448 0.08037  61  GLU A CG  
347  C CD  . GLU A 61  ? 0.47959 0.58437 0.78196 -0.06236 -0.03152 0.11276  61  GLU A CD  
348  O OE1 . GLU A 61  ? 0.46454 0.62106 0.76593 -0.04725 -0.02302 0.11514  61  GLU A OE1 
349  O OE2 . GLU A 61  ? 0.47432 0.56126 0.79301 -0.07877 -0.03858 0.13659  61  GLU A OE2 
350  N N   . ILE A 62  ? 0.32542 0.33292 0.56705 -0.02595 -0.01941 0.03157  62  ILE A N   
351  C CA  . ILE A 62  ? 0.35509 0.32764 0.59194 -0.01468 -0.01623 0.03318  62  ILE A CA  
352  C C   . ILE A 62  ? 0.33373 0.33081 0.58773 -0.00638 -0.01391 0.05595  62  ILE A C   
353  O O   . ILE A 62  ? 0.30419 0.34934 0.56600 0.00074  -0.01011 0.05936  62  ILE A O   
354  C CB  . ILE A 62  ? 0.36239 0.33418 0.58870 0.00110  -0.00629 0.01692  62  ILE A CB  
355  C CG1 . ILE A 62  ? 0.38235 0.33687 0.58923 -0.00593 -0.00717 -0.00161 62  ILE A CG1 
356  C CG2 . ILE A 62  ? 0.38593 0.32632 0.60733 0.02092  -0.00054 0.01917  62  ILE A CG2 
357  C CD1 . ILE A 62  ? 0.38190 0.35104 0.58381 0.00681  0.00464  -0.01079 62  ILE A CD1 
358  N N   . LEU A 63  ? 0.32631 0.28748 0.58398 -0.00699 -0.01815 0.07147  63  LEU A N   
359  C CA  . LEU A 63  ? 0.32138 0.30217 0.59397 0.00312  -0.01573 0.09746  63  LEU A CA  
360  C C   . LEU A 63  ? 0.38917 0.35156 0.65788 0.02831  -0.00903 0.09405  63  LEU A C   
361  O O   . LEU A 63  ? 0.38641 0.30444 0.63942 0.03730  -0.00702 0.07517  63  LEU A O   
362  C CB  . LEU A 63  ? 0.36197 0.31643 0.64658 -0.01278 -0.02490 0.12439  63  LEU A CB  
363  C CG  . LEU A 63  ? 0.40932 0.38884 0.70505 -0.03818 -0.03138 0.13432  63  LEU A CG  
364  C CD1 . LEU A 63  ? 0.44260 0.40566 0.75937 -0.05571 -0.04014 0.17097  63  LEU A CD1 
365  C CD2 . LEU A 63  ? 0.38082 0.43598 0.67969 -0.03131 -0.02287 0.13513  63  LEU A CD2 
366  N N   . VAL A 64  ? 0.32856 0.33079 0.61040 0.04249  -0.00536 0.11343  64  VAL A N   
367  C CA  . VAL A 64  ? 0.33910 0.33484 0.62384 0.06927  0.00061  0.11702  64  VAL A CA  
368  C C   . VAL A 64  ? 0.42207 0.34054 0.69822 0.07741  -0.00229 0.12001  64  VAL A C   
369  O O   . VAL A 64  ? 0.46602 0.35577 0.73197 0.10055  0.00418  0.10581  64  VAL A O   
370  C CB  . VAL A 64  ? 0.35994 0.41242 0.66020 0.08045  0.00072  0.14267  64  VAL A CB  
371  C CG1 . VAL A 64  ? 0.39681 0.44039 0.70498 0.11008  0.00488  0.15595  64  VAL A CG1 
372  C CG2 . VAL A 64  ? 0.37701 0.49573 0.67899 0.07668  0.00062  0.12893  64  VAL A CG2 
373  N N   . GLY A 65  ? 0.43690 0.31972 0.71672 0.05894  -0.01275 0.13841  65  GLY A N   
374  C CA  . GLY A 65  ? 0.51224 0.30898 0.78259 0.06255  -0.02112 0.13974  65  GLY A CA  
375  C C   . GLY A 65  ? 0.53163 0.26899 0.77454 0.05763  -0.02608 0.10424  65  GLY A C   
376  O O   . GLY A 65  ? 0.65005 0.30836 0.87562 0.06850  -0.03339 0.09559  65  GLY A O   
377  N N   . ASP A 66  ? 0.50536 0.27572 0.74066 0.04335  -0.02366 0.08333  66  ASP A N   
378  C CA  . ASP A 66  ? 0.57825 0.30300 0.78302 0.04202  -0.02707 0.04988  66  ASP A CA  
379  C C   . ASP A 66  ? 0.61504 0.33370 0.80016 0.07832  -0.01172 0.02968  66  ASP A C   
380  O O   . ASP A 66  ? 0.65163 0.31297 0.80362 0.08995  -0.01385 0.00451  66  ASP A O   
381  C CB  . ASP A 66  ? 0.55251 0.32021 0.75635 0.01975  -0.02765 0.03800  66  ASP A CB  
382  C CG  . ASP A 66  ? 0.53743 0.31635 0.75978 -0.01387 -0.04177 0.05587  66  ASP A CG  
383  O OD1 . ASP A 66  ? 0.56135 0.29562 0.79085 -0.02747 -0.05570 0.07142  66  ASP A OD1 
384  O OD2 . ASP A 66  ? 0.51279 0.34606 0.74411 -0.02581 -0.03904 0.05578  66  ASP A OD2 
385  N N   . VAL A 67  ? 0.55152 0.33302 0.75598 0.09693  0.00311  0.04057  67  VAL A N   
386  C CA  . VAL A 67  ? 0.60230 0.40327 0.79773 0.12791  0.02011  0.02635  67  VAL A CA  
387  C C   . VAL A 67  ? 0.66179 0.40838 0.84476 0.16369  0.02357  0.02618  67  VAL A C   
388  O O   . VAL A 67  ? 0.68284 0.42368 0.88433 0.17298  0.02008  0.04988  67  VAL A O   
389  C CB  . VAL A 67  ? 0.52297 0.41280 0.74912 0.13092  0.03023  0.04011  67  VAL A CB  
390  C CG1 . VAL A 67  ? 0.59245 0.51263 0.81725 0.15881  0.04792  0.03079  67  VAL A CG1 
391  C CG2 . VAL A 67  ? 0.43690 0.36767 0.67132 0.09834  0.02413  0.03811  67  VAL A CG2 
392  N N   . GLY A 68  ? 0.68003 0.38379 0.82797 0.18660  0.03014  -0.00039 68  GLY A N   
393  C CA  . GLY A 68  ? 0.71378 0.34640 0.83884 0.22330  0.03067  -0.00815 68  GLY A CA  
394  C C   . GLY A 68  ? 0.87101 0.39827 0.96632 0.20847  0.00709  -0.02181 68  GLY A C   
395  O O   . GLY A 68  ? 0.92257 0.39298 0.99597 0.23100  0.00821  -0.03455 68  GLY A O   
396  N N   . GLN A 69  ? 0.86988 0.39104 0.97259 0.16194  -0.01135 -0.01758 69  GLN A N   
397  C CA  . GLN A 69  ? 0.95451 0.39764 1.02807 0.13525  -0.03272 -0.02633 69  GLN A CA  
398  C C   . GLN A 69  ? 0.96568 0.39983 1.00963 0.11365  -0.04082 -0.05541 69  GLN A C   
399  O O   . GLN A 69  ? 1.06840 0.45234 1.07132 0.12173  -0.04323 -0.08271 69  GLN A O   
400  C CB  . GLN A 69  ? 0.90415 0.35554 1.01311 0.09756  -0.04878 0.00855  69  GLN A CB  
401  C CG  . GLN A 69  ? 0.91915 0.39116 1.05998 0.11454  -0.04263 0.04388  69  GLN A CG  
402  C CD  . GLN A 69  ? 1.03386 0.44047 1.14467 0.14992  -0.03857 0.04048  69  GLN A CD  
403  O OE1 . GLN A 69  ? 1.08269 0.41465 1.16813 0.13942  -0.04873 0.03301  69  GLN A OE1 
404  N NE2 . GLN A 69  ? 0.99008 0.43158 1.11052 0.19194  -0.02298 0.04736  69  GLN A NE2 
405  N N   . THR A 70  ? 0.81083 0.29713 0.87930 0.08593  -0.04588 -0.04950 70  THR A N   
406  C CA  . THR A 70  ? 0.80318 0.29021 0.84414 0.06861  -0.05295 -0.07364 70  THR A CA  
407  C C   . THR A 70  ? 0.78442 0.34826 0.82862 0.07912  -0.03111 -0.07760 70  THR A C   
408  O O   . THR A 70  ? 0.80138 0.37093 0.82116 0.06932  -0.03424 -0.09520 70  THR A O   
409  C CB  . THR A 70  ? 0.78296 0.28288 0.84345 0.01999  -0.07332 -0.05915 70  THR A CB  
410  O OG1 . THR A 70  ? 0.74681 0.31678 0.85756 0.00636  -0.06704 -0.03006 70  THR A OG1 
411  C CG2 . THR A 70  ? 0.88843 0.33700 0.94460 0.00127  -0.08991 -0.05011 70  THR A CG2 
412  N N   . VAL A 71  ? 0.73117 0.35798 0.80609 0.09524  -0.01075 -0.05870 71  VAL A N   
413  C CA  . VAL A 71  ? 0.60719 0.31071 0.69319 0.09850  0.00775  -0.05679 71  VAL A CA  
414  C C   . VAL A 71  ? 0.68942 0.41765 0.77685 0.13859  0.03025  -0.05531 71  VAL A C   
415  O O   . VAL A 71  ? 0.65132 0.38632 0.76232 0.15370  0.03374  -0.03831 71  VAL A O   
416  C CB  . VAL A 71  ? 0.56664 0.33384 0.69500 0.07227  0.00587  -0.03362 71  VAL A CB  
417  C CG1 . VAL A 71  ? 0.52273 0.35988 0.66432 0.07582  0.02187  -0.03172 71  VAL A CG1 
418  C CG2 . VAL A 71  ? 0.52781 0.28132 0.65607 0.03645  -0.01367 -0.03389 71  VAL A CG2 
419  N N   . ASP A 72  ? 0.66128 0.40580 0.72384 0.15748  0.04558  -0.07034 72  ASP A N   
420  C CA  . ASP A 72  ? 0.71384 0.49234 0.77935 0.19775  0.06945  -0.06700 72  ASP A CA  
421  C C   . ASP A 72  ? 0.59661 0.47011 0.70245 0.18966  0.08433  -0.04692 72  ASP A C   
422  O O   . ASP A 72  ? 0.70716 0.62947 0.84274 0.21083  0.09795  -0.03060 72  ASP A O   
423  C CB  . ASP A 72  ? 0.76172 0.49957 0.77089 0.22847  0.07853  -0.09465 72  ASP A CB  
424  C CG  . ASP A 72  ? 0.86928 0.64821 0.87847 0.27574  0.10669  -0.09088 72  ASP A CG  
425  O OD1 . ASP A 72  ? 0.90053 0.76629 0.94544 0.27244  0.12350  -0.07042 72  ASP A OD1 
426  O OD2 . ASP A 72  ? 1.02324 0.75415 1.00078 0.31056  0.10927  -0.10699 72  ASP A OD2 
427  N N   . ASP A 73  ? 0.49335 0.39189 0.60134 0.15951  0.07997  -0.04734 73  ASP A N   
428  C CA  . ASP A 73  ? 0.48425 0.45966 0.62801 0.14535  0.08862  -0.03014 73  ASP A CA  
429  C C   . ASP A 73  ? 0.39971 0.37728 0.56014 0.10652  0.06951  -0.02624 73  ASP A C   
430  O O   . ASP A 73  ? 0.39811 0.35961 0.53960 0.08760  0.06224  -0.03519 73  ASP A O   
431  C CB  . ASP A 73  ? 0.48740 0.48583 0.60974 0.15385  0.10490  -0.03438 73  ASP A CB  
432  C CG  . ASP A 73  ? 0.52345 0.59786 0.68619 0.13761  0.11313  -0.01275 73  ASP A CG  
433  O OD1 . ASP A 73  ? 0.41613 0.51185 0.61236 0.10997  0.09965  -0.00287 73  ASP A OD1 
434  O OD2 . ASP A 73  ? 0.55615 0.66850 0.71501 0.15331  0.13296  -0.00539 73  ASP A OD2 
435  N N   . PRO A 74  ? 0.37340 0.37213 0.56634 0.09717  0.06100  -0.01282 74  PRO A N   
436  C CA  . PRO A 74  ? 0.34923 0.34720 0.55094 0.06705  0.04428  -0.01135 74  PRO A CA  
437  C C   . PRO A 74  ? 0.32882 0.35913 0.53889 0.04732  0.04297  -0.01151 74  PRO A C   
438  O O   . PRO A 74  ? 0.33962 0.35428 0.54113 0.02846  0.03186  -0.01701 74  PRO A O   
439  C CB  . PRO A 74  ? 0.37002 0.39338 0.60040 0.06813  0.03865  0.00418  74  PRO A CB  
440  C CG  . PRO A 74  ? 0.35195 0.39886 0.59595 0.09568  0.05124  0.01315  74  PRO A CG  
441  C CD  . PRO A 74  ? 0.41177 0.42970 0.62803 0.11780  0.06527  0.00088  74  PRO A CD  
442  N N   . TYR A 75  ? 0.33434 0.40958 0.56370 0.05074  0.05297  -0.00329 75  TYR A N   
443  C CA  . TYR A 75  ? 0.34079 0.43614 0.57876 0.02917  0.04862  -0.00148 75  TYR A CA  
444  C C   . TYR A 75  ? 0.30251 0.36907 0.50809 0.02621  0.05218  -0.00990 75  TYR A C   
445  O O   . TYR A 75  ? 0.31525 0.37184 0.51615 0.00793  0.04193  -0.01264 75  TYR A O   
446  C CB  . TYR A 75  ? 0.33846 0.48890 0.60982 0.02747  0.05555  0.01348  75  TYR A CB  
447  C CG  . TYR A 75  ? 0.35105 0.51117 0.63614 0.00011  0.04305  0.01568  75  TYR A CG  
448  C CD1 . TYR A 75  ? 0.36539 0.52388 0.66091 -0.01353 0.02446  0.01023  75  TYR A CD1 
449  C CD2 . TYR A 75  ? 0.46161 0.62771 0.74465 -0.00958 0.04948  0.02312  75  TYR A CD2 
450  C CE1 . TYR A 75  ? 0.39715 0.55264 0.70004 -0.03451 0.01085  0.00816  75  TYR A CE1 
451  C CE2 . TYR A 75  ? 0.37132 0.53547 0.66695 -0.03438 0.03551  0.02615  75  TYR A CE2 
452  C CZ  . TYR A 75  ? 0.44180 0.59652 0.74643 -0.04573 0.01546  0.01645  75  TYR A CZ  
453  O OH  . TYR A 75  ? 0.45246 0.59467 0.76474 -0.06596 -0.00040 0.01527  75  TYR A OH  
454  N N   . ALA A 76  ? 0.34264 0.39564 0.52241 0.04719  0.06602  -0.01470 76  ALA A N   
455  C CA  . ALA A 76  ? 0.36884 0.39505 0.51028 0.04659  0.06751  -0.02419 76  ALA A CA  
456  C C   . ALA A 76  ? 0.39102 0.36896 0.51098 0.03387  0.04848  -0.03827 76  ALA A C   
457  O O   . ALA A 76  ? 0.37802 0.34504 0.48157 0.02052  0.04052  -0.04154 76  ALA A O   
458  C CB  . ALA A 76  ? 0.43282 0.45286 0.54317 0.07755  0.08581  -0.03049 76  ALA A CB  
459  N N   . THR A 77  ? 0.37490 0.32711 0.49777 0.03718  0.04035  -0.04306 77  THR A N   
460  C CA  . THR A 77  ? 0.41978 0.33546 0.53138 0.02089  0.02145  -0.05057 77  THR A CA  
461  C C   . THR A 77  ? 0.38843 0.33011 0.52549 -0.00068 0.01145  -0.04176 77  THR A C   
462  O O   . THR A 77  ? 0.37822 0.30785 0.50583 -0.01460 -0.00067 -0.04516 77  THR A O   
463  C CB  . THR A 77  ? 0.42866 0.31165 0.54220 0.02706  0.01501  -0.05169 77  THR A CB  
464  O OG1 . THR A 77  ? 0.46018 0.31088 0.54510 0.05273  0.02385  -0.06344 77  THR A OG1 
465  C CG2 . THR A 77  ? 0.45305 0.30333 0.56096 0.00581  -0.00577 -0.05463 77  THR A CG2 
466  N N   . PHE A 78  ? 0.32828 0.30608 0.49612 -0.00141 0.01499  -0.03145 78  PHE A N   
467  C CA  . PHE A 78  ? 0.31904 0.31872 0.50459 -0.01598 0.00614  -0.02741 78  PHE A CA  
468  C C   . PHE A 78  ? 0.34577 0.34375 0.52033 -0.02431 0.00459  -0.02936 78  PHE A C   
469  O O   . PHE A 78  ? 0.34930 0.34073 0.52032 -0.03338 -0.00598 -0.03106 78  PHE A O   
470  C CB  . PHE A 78  ? 0.31382 0.34929 0.52675 -0.01376 0.00848  -0.02026 78  PHE A CB  
471  C CG  . PHE A 78  ? 0.33536 0.38661 0.55968 -0.02518 -0.00076 -0.02117 78  PHE A CG  
472  C CD1 . PHE A 78  ? 0.32732 0.37819 0.55122 -0.02858 -0.01088 -0.02398 78  PHE A CD1 
473  C CD2 . PHE A 78  ? 0.31361 0.37932 0.54929 -0.03143 0.00034  -0.01815 78  PHE A CD2 
474  C CE1 . PHE A 78  ? 0.35165 0.41016 0.58017 -0.03305 -0.01989 -0.02885 78  PHE A CE1 
475  C CE2 . PHE A 78  ? 0.35358 0.42073 0.59690 -0.04168 -0.01190 -0.02161 78  PHE A CE2 
476  C CZ  . PHE A 78  ? 0.32905 0.38935 0.56560 -0.03985 -0.02192 -0.02947 78  PHE A CZ  
477  N N   . VAL A 79  ? 0.32368 0.33137 0.49410 -0.01984 0.01585  -0.02567 79  VAL A N   
478  C CA  . VAL A 79  ? 0.33549 0.34277 0.49635 -0.02792 0.01516  -0.02164 79  VAL A CA  
479  C C   . VAL A 79  ? 0.38416 0.36331 0.51269 -0.02880 0.00796  -0.02948 79  VAL A C   
480  O O   . VAL A 79  ? 0.34599 0.32162 0.47050 -0.03743 -0.00087 -0.02658 79  VAL A O   
481  C CB  . VAL A 79  ? 0.34887 0.37942 0.51264 -0.02269 0.03132  -0.01022 79  VAL A CB  
482  C CG1 . VAL A 79  ? 0.39287 0.42032 0.54122 -0.02995 0.03182  -0.00162 79  VAL A CG1 
483  C CG2 . VAL A 79  ? 0.35615 0.42049 0.56015 -0.02921 0.03209  0.00041  79  VAL A CG2 
484  N N   . LYS A 80  ? 0.37061 0.32671 0.47558 -0.01970 0.00868  -0.03996 80  LYS A N   
485  C CA  . LYS A 80  ? 0.40330 0.33131 0.47631 -0.02336 -0.00331 -0.04958 80  LYS A CA  
486  C C   . LYS A 80  ? 0.38162 0.30816 0.47056 -0.03851 -0.02130 -0.04820 80  LYS A C   
487  O O   . LYS A 80  ? 0.41564 0.33231 0.48792 -0.04578 -0.03417 -0.05090 80  LYS A O   
488  C CB  . LYS A 80  ? 0.46130 0.35493 0.50334 -0.01084 -0.00294 -0.06477 80  LYS A CB  
489  C CG  . LYS A 80  ? 0.52591 0.41899 0.53191 0.00882  0.01290  -0.06985 80  LYS A CG  
490  C CD  . LYS A 80  ? 0.69383 0.54448 0.65927 0.02795  0.01257  -0.09062 80  LYS A CD  
491  C CE  . LYS A 80  ? 0.71368 0.56806 0.63100 0.04823  0.02577  -0.09716 80  LYS A CE  
492  N NZ  . LYS A 80  ? 0.82817 0.64260 0.69602 0.07725  0.03014  -0.12107 80  LYS A NZ  
493  N N   . MET A 81  ? 0.35198 0.29479 0.47247 -0.04173 -0.02219 -0.04237 81  MET A N   
494  C CA  . MET A 81  ? 0.35842 0.31109 0.49568 -0.05190 -0.03540 -0.03780 81  MET A CA  
495  C C   . MET A 81  ? 0.34043 0.31396 0.48954 -0.05261 -0.03753 -0.03237 81  MET A C   
496  O O   . MET A 81  ? 0.38375 0.37070 0.54428 -0.05600 -0.04695 -0.02819 81  MET A O   
497  C CB  . MET A 81  ? 0.37657 0.34026 0.53745 -0.05171 -0.03464 -0.03216 81  MET A CB  
498  C CG  . MET A 81  ? 0.43404 0.36904 0.58739 -0.05424 -0.03902 -0.03397 81  MET A CG  
499  S SD  . MET A 81  ? 0.45273 0.40590 0.63691 -0.05672 -0.03973 -0.01813 81  MET A SD  
500  C CE  . MET A 81  ? 0.38707 0.36120 0.57989 -0.03958 -0.02388 -0.01774 81  MET A CE  
501  N N   . LEU A 82  ? 0.32861 0.30484 0.47665 -0.04900 -0.02970 -0.03070 82  LEU A N   
502  C CA  . LEU A 82  ? 0.34672 0.32963 0.50388 -0.04933 -0.03462 -0.02633 82  LEU A CA  
503  C C   . LEU A 82  ? 0.38276 0.35737 0.52268 -0.05119 -0.04274 -0.02250 82  LEU A C   
504  O O   . LEU A 82  ? 0.42356 0.38743 0.53939 -0.05233 -0.04022 -0.02214 82  LEU A O   
505  C CB  . LEU A 82  ? 0.33066 0.31508 0.49642 -0.05029 -0.02738 -0.02217 82  LEU A CB  
506  C CG  . LEU A 82  ? 0.33639 0.33548 0.52200 -0.04906 -0.02297 -0.02487 82  LEU A CG  
507  C CD1 . LEU A 82  ? 0.36710 0.37338 0.56533 -0.05470 -0.01770 -0.01748 82  LEU A CD1 
508  C CD2 . LEU A 82  ? 0.31450 0.32174 0.51215 -0.04523 -0.03210 -0.03103 82  LEU A CD2 
509  N N   . PRO A 83  ? 0.35826 0.34076 0.50734 -0.04839 -0.05266 -0.01947 83  PRO A N   
510  C CA  . PRO A 83  ? 0.36312 0.34300 0.49835 -0.04845 -0.06217 -0.01296 83  PRO A CA  
511  C C   . PRO A 83  ? 0.39666 0.36215 0.52146 -0.04678 -0.05939 -0.00391 83  PRO A C   
512  O O   . PRO A 83  ? 0.37820 0.33599 0.51667 -0.04503 -0.05641 -0.00171 83  PRO A O   
513  C CB  . PRO A 83  ? 0.37044 0.37064 0.52522 -0.04098 -0.07112 -0.01015 83  PRO A CB  
514  C CG  . PRO A 83  ? 0.36700 0.37002 0.53841 -0.03290 -0.06468 -0.01627 83  PRO A CG  
515  C CD  . PRO A 83  ? 0.34411 0.34262 0.51453 -0.04102 -0.05508 -0.02171 83  PRO A CD  
516  N N   . ASP A 84  ? 0.35529 0.31632 0.45448 -0.04858 -0.06231 0.00248  84  ASP A N   
517  C CA  . ASP A 84  ? 0.39245 0.34373 0.48048 -0.04773 -0.05881 0.01782  84  ASP A CA  
518  C C   . ASP A 84  ? 0.40835 0.35125 0.51279 -0.04138 -0.06797 0.02748  84  ASP A C   
519  O O   . ASP A 84  ? 0.40536 0.33175 0.51485 -0.04325 -0.06536 0.04012  84  ASP A O   
520  C CB  . ASP A 84  ? 0.44028 0.39336 0.49205 -0.04729 -0.06230 0.02348  84  ASP A CB  
521  C CG  . ASP A 84  ? 0.52386 0.47641 0.54955 -0.04760 -0.04931 0.01662  84  ASP A CG  
522  O OD1 . ASP A 84  ? 0.52088 0.47445 0.56161 -0.04835 -0.03690 0.01052  84  ASP A OD1 
523  O OD2 . ASP A 84  ? 0.52768 0.48032 0.51550 -0.04426 -0.05203 0.01708  84  ASP A OD2 
524  N N   . LYS A 85  ? 0.40047 0.35451 0.51362 -0.03315 -0.07947 0.02399  85  LYS A N   
525  C CA  . LYS A 85  ? 0.43192 0.37754 0.55459 -0.01993 -0.08866 0.03332  85  LYS A CA  
526  C C   . LYS A 85  ? 0.40558 0.36302 0.55078 -0.00639 -0.09195 0.02187  85  LYS A C   
527  O O   . LYS A 85  ? 0.37851 0.34722 0.53095 0.01008  -0.10046 0.02701  85  LYS A O   
528  C CB  . LYS A 85  ? 0.45703 0.41399 0.56416 -0.01535 -0.09968 0.04753  85  LYS A CB  
529  C CG  . LYS A 85  ? 0.53126 0.47806 0.60945 -0.02345 -0.09587 0.06169  85  LYS A CG  
530  C CD  . LYS A 85  ? 0.59148 0.55137 0.65075 -0.01721 -0.10944 0.07660  85  LYS A CD  
531  C CE  . LYS A 85  ? 0.67889 0.62921 0.70714 -0.02090 -0.10363 0.09589  85  LYS A CE  
532  N NZ  . LYS A 85  ? 0.80169 0.76827 0.80438 -0.01430 -0.11834 0.11093  85  LYS A NZ  
533  N N   . ASP A 86  ? 0.36571 0.32573 0.52124 -0.00993 -0.08449 0.00782  86  ASP A N   
534  C CA  . ASP A 86  ? 0.35552 0.32704 0.52642 0.00616  -0.08548 -0.00299 86  ASP A CA  
535  C C   . ASP A 86  ? 0.36060 0.31795 0.53541 0.00114  -0.07972 -0.01609 86  ASP A C   
536  O O   . ASP A 86  ? 0.36546 0.31689 0.53763 -0.01566 -0.07327 -0.01539 86  ASP A O   
537  C CB  . ASP A 86  ? 0.35223 0.36851 0.53451 0.00832  -0.08532 -0.00250 86  ASP A CB  
538  C CG  . ASP A 86  ? 0.43428 0.47542 0.63045 0.03314  -0.08564 -0.00608 86  ASP A CG  
539  O OD1 . ASP A 86  ? 0.46268 0.47910 0.65429 0.05315  -0.08826 -0.01319 86  ASP A OD1 
540  O OD2 . ASP A 86  ? 0.44757 0.53336 0.65883 0.03359  -0.08364 -0.00086 86  ASP A OD2 
541  N N   . CYS A 87  ? 0.30950 0.26562 0.48926 0.01840  -0.08247 -0.02855 87  CYS A N   
542  C CA  . CYS A 87  ? 0.30764 0.25294 0.48904 0.01453  -0.08136 -0.04277 87  CYS A CA  
543  C C   . CYS A 87  ? 0.33157 0.31676 0.51866 0.01580  -0.07329 -0.04775 87  CYS A C   
544  O O   . CYS A 87  ? 0.30315 0.32248 0.49548 0.02407  -0.07015 -0.04167 87  CYS A O   
545  C CB  . CYS A 87  ? 0.33000 0.24457 0.50558 0.03381  -0.09203 -0.05791 87  CYS A CB  
546  S SG  . CYS A 87  ? 0.41646 0.27174 0.58793 0.03182  -0.10477 -0.04918 87  CYS A SG  
547  N N   . ARG A 88  ? 0.39179 0.23448 0.43614 0.00958  -0.00247 -0.05090 88  ARG A N   
548  C CA  . ARG A 88  ? 0.35754 0.23216 0.43661 0.00448  0.00542  -0.03867 88  ARG A CA  
549  C C   . ARG A 88  ? 0.37684 0.25792 0.43439 0.00522  0.01875  -0.03954 88  ARG A C   
550  O O   . ARG A 88  ? 0.40054 0.25875 0.42878 0.00199  0.01873  -0.05138 88  ARG A O   
551  C CB  . ARG A 88  ? 0.38093 0.24922 0.48149 -0.00604 -0.00387 -0.03771 88  ARG A CB  
552  C CG  . ARG A 88  ? 0.37055 0.23347 0.50294 -0.00628 -0.02609 -0.04124 88  ARG A CG  
553  C CD  . ARG A 88  ? 0.38571 0.28708 0.58432 -0.00757 -0.02472 -0.02212 88  ARG A CD  
554  N NE  . ARG A 88  ? 0.36039 0.25889 0.60843 -0.01149 -0.05296 -0.02747 88  ARG A NE  
555  C CZ  . ARG A 88  ? 0.36150 0.25884 0.61484 -0.00284 -0.07181 -0.03760 88  ARG A CZ  
556  N NH1 . ARG A 88  ? 0.38143 0.27703 0.59264 0.01067  -0.06271 -0.04096 88  ARG A NH1 
557  N NH2 . ARG A 88  ? 0.40245 0.29806 0.70796 -0.00651 -0.10460 -0.04612 88  ARG A NH2 
558  N N   . TYR A 89  ? 0.35021 0.26369 0.42545 0.01118  0.02923  -0.02537 89  TYR A N   
559  C CA  . TYR A 89  ? 0.34339 0.26478 0.40099 0.01326  0.03520  -0.02624 89  TYR A CA  
560  C C   . TYR A 89  ? 0.37530 0.30465 0.45998 0.00419  0.03637  -0.01210 89  TYR A C   
561  O O   . TYR A 89  ? 0.35141 0.28473 0.47397 -0.00164 0.03407  0.00092  89  TYR A O   
562  C CB  . TYR A 89  ? 0.36434 0.31412 0.40753 0.03515  0.04604  -0.01940 89  TYR A CB  
563  C CG  . TYR A 89  ? 0.41190 0.35716 0.43298 0.05177  0.04545  -0.03206 89  TYR A CG  
564  C CD1 . TYR A 89  ? 0.42680 0.33691 0.41952 0.04952  0.03250  -0.05760 89  TYR A CD1 
565  C CD2 . TYR A 89  ? 0.43086 0.40794 0.46434 0.07154  0.05934  -0.01628 89  TYR A CD2 
566  C CE1 . TYR A 89  ? 0.43857 0.33780 0.41031 0.06816  0.02937  -0.07108 89  TYR A CE1 
567  C CE2 . TYR A 89  ? 0.48501 0.45891 0.49610 0.09308  0.05921  -0.02968 89  TYR A CE2 
568  C CZ  . TYR A 89  ? 0.49965 0.43053 0.47706 0.09179  0.04211  -0.05909 89  TYR A CZ  
569  O OH  . TYR A 89  ? 0.56209 0.48395 0.51788 0.11602  0.03976  -0.07357 89  TYR A OH  
570  N N   . ALA A 90  ? 0.38487 0.31563 0.45589 0.00384  0.03667  -0.01574 90  ALA A N   
571  C CA  . ALA A 90  ? 0.33932 0.27508 0.43381 -0.00051 0.03734  -0.00210 90  ALA A CA  
572  C C   . ALA A 90  ? 0.39362 0.34536 0.46999 0.00961  0.03906  -0.00097 90  ALA A C   
573  O O   . ALA A 90  ? 0.38765 0.34007 0.43715 0.01466  0.03361  -0.01896 90  ALA A O   
574  C CB  . ALA A 90  ? 0.38425 0.29300 0.48577 -0.01274 0.02793  -0.01479 90  ALA A CB  
575  N N   . LEU A 91  ? 0.31918 0.28229 0.41374 0.01410  0.04344  0.02061  91  LEU A N   
576  C CA  . LEU A 91  ? 0.40051 0.37512 0.48104 0.02451  0.03990  0.02106  91  LEU A CA  
577  C C   . LEU A 91  ? 0.37178 0.33055 0.47843 0.01451  0.03424  0.02034  91  LEU A C   
578  O O   . LEU A 91  ? 0.35999 0.30496 0.49737 0.00794  0.03536  0.03422  91  LEU A O   
579  C CB  . LEU A 91  ? 0.37518 0.37506 0.44635 0.04626  0.05133  0.05108  91  LEU A CB  
580  C CG  . LEU A 91  ? 0.44991 0.46973 0.48265 0.06762  0.05852  0.05028  91  LEU A CG  
581  C CD1 . LEU A 91  ? 0.46638 0.51384 0.49174 0.09249  0.07914  0.09095  91  LEU A CD1 
582  C CD2 . LEU A 91  ? 0.50949 0.52866 0.50234 0.07769  0.03905  0.01618  91  LEU A CD2 
583  N N   . TYR A 92  ? 0.33847 0.29973 0.43855 0.01483  0.02646  0.00309  92  TYR A N   
584  C CA  . TYR A 92  ? 0.34781 0.29947 0.46884 0.01295  0.02314  0.00132  92  TYR A CA  
585  C C   . TYR A 92  ? 0.37244 0.34689 0.49143 0.02736  0.01675  0.00396  92  TYR A C   
586  O O   . TYR A 92  ? 0.36532 0.35811 0.47235 0.03011  0.00892  -0.01151 92  TYR A O   
587  C CB  . TYR A 92  ? 0.38446 0.32253 0.50625 0.00209  0.02347  -0.02118 92  TYR A CB  
588  C CG  . TYR A 92  ? 0.40278 0.32838 0.54008 0.00660  0.02272  -0.02422 92  TYR A CG  
589  C CD1 . TYR A 92  ? 0.35863 0.30312 0.50871 0.01593  0.02154  -0.02683 92  TYR A CD1 
590  C CD2 . TYR A 92  ? 0.38229 0.27747 0.52327 0.00560  0.01938  -0.02698 92  TYR A CD2 
591  C CE1 . TYR A 92  ? 0.39736 0.33050 0.55975 0.02591  0.02164  -0.03078 92  TYR A CE1 
592  C CE2 . TYR A 92  ? 0.44326 0.32168 0.59269 0.01606  0.01523  -0.03470 92  TYR A CE2 
593  C CZ  . TYR A 92  ? 0.43045 0.32796 0.58877 0.02725  0.01871  -0.03589 92  TYR A CZ  
594  O OH  . TYR A 92  ? 0.45498 0.33519 0.61929 0.04278  0.01547  -0.04534 92  TYR A OH  
595  N N   . ASP A 93  ? 0.34986 0.32065 0.48423 0.03737  0.01620  0.02239  93  ASP A N   
596  C CA  . ASP A 93  ? 0.38765 0.37928 0.51967 0.05593  0.00772  0.02785  93  ASP A CA  
597  C C   . ASP A 93  ? 0.41249 0.40503 0.56895 0.05407  0.00270  0.00908  93  ASP A C   
598  O O   . ASP A 93  ? 0.38435 0.35480 0.55925 0.05594  0.00486  0.01304  93  ASP A O   
599  C CB  . ASP A 93  ? 0.41910 0.40385 0.55525 0.07069  0.01252  0.06406  93  ASP A CB  
600  C CG  . ASP A 93  ? 0.54725 0.55517 0.66660 0.09709  0.00280  0.07445  93  ASP A CG  
601  O OD1 . ASP A 93  ? 0.57979 0.61139 0.69144 0.10269  -0.01223 0.04933  93  ASP A OD1 
602  O OD2 . ASP A 93  ? 0.62013 0.62308 0.73732 0.11316  0.00884  0.10964  93  ASP A OD2 
603  N N   . ALA A 94  ? 0.34751 0.36562 0.50911 0.05143  -0.00414 -0.01196 94  ALA A N   
604  C CA  . ALA A 94  ? 0.38437 0.41215 0.57638 0.04799  -0.00102 -0.02713 94  ALA A CA  
605  C C   . ALA A 94  ? 0.36472 0.42466 0.58075 0.06562  -0.01418 -0.02802 94  ALA A C   
606  O O   . ALA A 94  ? 0.37569 0.46059 0.58699 0.07342  -0.03188 -0.03134 94  ALA A O   
607  C CB  . ALA A 94  ? 0.36091 0.39775 0.56115 0.02902  0.00409  -0.04451 94  ALA A CB  
608  N N   . THR A 95  ? 0.35683 0.41590 0.59632 0.07601  -0.00850 -0.02782 95  THR A N   
609  C CA  . THR A 95  ? 0.34012 0.43510 0.61300 0.09372  -0.01935 -0.03102 95  THR A CA  
610  C C   . THR A 95  ? 0.32906 0.45774 0.64549 0.08371  -0.00884 -0.04710 95  THR A C   
611  O O   . THR A 95  ? 0.33610 0.44943 0.64962 0.07431  0.01327  -0.05066 95  THR A O   
612  C CB  . THR A 95  ? 0.39555 0.46908 0.67175 0.11637  -0.01852 -0.01934 95  THR A CB  
613  O OG1 . THR A 95  ? 0.55719 0.60297 0.80445 0.12394  -0.02601 0.00400  95  THR A OG1 
614  C CG2 . THR A 95  ? 0.42905 0.54233 0.74309 0.13818  -0.02905 -0.02342 95  THR A CG2 
615  N N   . TYR A 96  ? 0.32004 0.49644 0.67905 0.08704  -0.02506 -0.05497 96  TYR A N   
616  C CA  . TYR A 96  ? 0.30269 0.51942 0.72202 0.07471  -0.01327 -0.06399 96  TYR A CA  
617  C C   . TYR A 96  ? 0.29828 0.57105 0.77821 0.08805  -0.03628 -0.07028 96  TYR A C   
618  O O   . TYR A 96  ? 0.27821 0.55594 0.74200 0.10524  -0.06679 -0.07146 96  TYR A O   
619  C CB  . TYR A 96  ? 0.30009 0.51221 0.72307 0.04433  -0.01055 -0.07085 96  TYR A CB  
620  C CG  . TYR A 96  ? 0.32091 0.53845 0.73646 0.03943  -0.04578 -0.08305 96  TYR A CG  
621  C CD1 . TYR A 96  ? 0.33927 0.52222 0.68617 0.04831  -0.05686 -0.07978 96  TYR A CD1 
622  C CD2 . TYR A 96  ? 0.38254 0.64122 0.86262 0.02868  -0.06902 -0.09850 96  TYR A CD2 
623  C CE1 . TYR A 96  ? 0.42483 0.61329 0.75258 0.05300  -0.08854 -0.09340 96  TYR A CE1 
624  C CE2 . TYR A 96  ? 0.37959 0.63896 0.84633 0.03026  -0.10828 -0.11718 96  TYR A CE2 
625  C CZ  . TYR A 96  ? 0.41951 0.64272 0.80203 0.04538  -0.11687 -0.11550 96  TYR A CZ  
626  O OH  . TYR A 96  ? 0.52699 0.75104 0.88406 0.05562  -0.15538 -0.13657 96  TYR A OH  
627  N N   . GLU A 97  ? 0.24675 0.56496 0.79790 0.08331  -0.02029 -0.07183 97  GLU A N   
628  C CA  . GLU A 97  ? 0.24529 0.61853 0.85823 0.09466  -0.04133 -0.07602 97  GLU A CA  
629  C C   . GLU A 97  ? 0.29719 0.70685 0.97425 0.06604  -0.03591 -0.07680 97  GLU A C   
630  O O   . GLU A 97  ? 0.24263 0.64911 0.93188 0.04906  -0.00003 -0.06632 97  GLU A O   
631  C CB  . GLU A 97  ? 0.26288 0.64671 0.87876 0.12555  -0.02504 -0.06620 97  GLU A CB  
632  C CG  . GLU A 97  ? 0.36559 0.69863 0.91954 0.15185  -0.02863 -0.06167 97  GLU A CG  
633  C CD  . GLU A 97  ? 0.43324 0.75830 0.98028 0.18073  -0.01001 -0.05528 97  GLU A CD  
634  O OE1 . GLU A 97  ? 0.37908 0.74601 0.96652 0.18529  0.00853  -0.05407 97  GLU A OE1 
635  O OE2 . GLU A 97  ? 0.52836 0.80278 1.02925 0.19977  -0.01429 -0.05038 97  GLU A OE2 
636  N N   . THR A 98  ? 0.39520 0.70361 0.91366 0.08641  -0.12713 -0.05475 98  THR A N   
637  C CA  . THR A 98  ? 0.41208 0.75809 0.97775 0.06945  -0.13516 -0.06026 98  THR A CA  
638  C C   . THR A 98  ? 0.40908 0.79124 0.99565 0.08620  -0.13064 -0.05633 98  THR A C   
639  O O   . THR A 98  ? 0.41847 0.79318 0.98385 0.11001  -0.12122 -0.05047 98  THR A O   
640  C CB  . THR A 98  ? 0.42453 0.76778 0.98640 0.06647  -0.16635 -0.07587 98  THR A CB  
641  O OG1 . THR A 98  ? 0.50310 0.85020 1.03879 0.09765  -0.18561 -0.08189 98  THR A OG1 
642  C CG2 . THR A 98  ? 0.42731 0.73222 0.96103 0.05604  -0.17094 -0.08014 98  THR A CG2 
643  N N   . LYS A 99  ? 0.41071 0.83081 1.03997 0.07497  -0.13773 -0.05912 99  LYS A N   
644  C CA  . LYS A 99  ? 0.28706 0.74568 0.93774 0.09315  -0.13535 -0.05541 99  LYS A CA  
645  C C   . LYS A 99  ? 0.33648 0.79049 0.95769 0.12374  -0.15760 -0.06239 99  LYS A C   
646  O O   . LYS A 99  ? 0.35845 0.82861 0.97879 0.14686  -0.15174 -0.05644 99  LYS A O   
647  C CB  . LYS A 99  ? 0.34600 0.84964 1.05447 0.07435  -0.13880 -0.05560 99  LYS A CB  
648  N N   . GLU A 100 ? 0.36210 0.79249 0.95443 0.12730  -0.18189 -0.07388 100 GLU A N   
649  C CA  . GLU A 100 ? 0.46564 0.89446 1.02704 0.15794  -0.20387 -0.07967 100 GLU A CA  
650  C C   . GLU A 100 ? 0.44390 0.82767 0.94113 0.18091  -0.20338 -0.07479 100 GLU A C   
651  O O   . GLU A 100 ? 0.49682 0.87486 0.95968 0.21066  -0.21482 -0.07342 100 GLU A O   
652  C CB  . GLU A 100 ? 0.55758 1.00136 1.13385 0.15181  -0.23650 -0.09856 100 GLU A CB  
653  N N   . SER A 101 ? 0.46932 0.82080 0.94908 0.16924  -0.18880 -0.06960 101 SER A N   
654  C CA  . SER A 101 ? 0.49410 0.80426 0.91571 0.19083  -0.18817 -0.06260 101 SER A CA  
655  C C   . SER A 101 ? 0.38766 0.66443 0.79830 0.17971  -0.15991 -0.04941 101 SER A C   
656  O O   . SER A 101 ? 0.42041 0.70187 0.86025 0.15196  -0.14526 -0.04971 101 SER A O   
657  C CB  . SER A 101 ? 0.50720 0.80448 0.90152 0.19106  -0.21165 -0.07561 101 SER A CB  
658  O OG  . SER A 101 ? 0.57465 0.86408 0.98999 0.16047  -0.20859 -0.08174 101 SER A OG  
659  N N   . LYS A 102 ? 0.42840 0.66552 0.78837 0.19876  -0.14817 -0.03455 102 LYS A N   
660  C CA  . LYS A 102 ? 0.39156 0.58587 0.72847 0.18522  -0.12152 -0.02094 102 LYS A CA  
661  C C   . LYS A 102 ? 0.43625 0.60050 0.72904 0.18831  -0.12412 -0.01615 102 LYS A C   
662  O O   . LYS A 102 ? 0.47147 0.63244 0.73152 0.21637  -0.13603 -0.01223 102 LYS A O   
663  C CB  . LYS A 102 ? 0.42860 0.60059 0.75350 0.20351  -0.10383 -0.00568 102 LYS A CB  
664  C CG  . LYS A 102 ? 0.47863 0.60496 0.78601 0.19009  -0.07999 0.00645  102 LYS A CG  
665  C CD  . LYS A 102 ? 0.51194 0.61563 0.81741 0.20778  -0.06670 0.01748  102 LYS A CD  
666  C CE  . LYS A 102 ? 0.52230 0.58130 0.82034 0.19260  -0.04733 0.02555  102 LYS A CE  
667  N NZ  . LYS A 102 ? 0.55231 0.58607 0.85432 0.20855  -0.03810 0.03180  102 LYS A NZ  
668  N N   . LYS A 103 ? 0.38329 0.52770 0.67304 0.16296  -0.11279 -0.01599 103 LYS A N   
669  C CA  . LYS A 103 ? 0.45096 0.57314 0.70403 0.16462  -0.11547 -0.01385 103 LYS A CA  
670  C C   . LYS A 103 ? 0.49129 0.57792 0.73138 0.15051  -0.08997 0.00081  103 LYS A C   
671  O O   . LYS A 103 ? 0.42124 0.50211 0.68395 0.13319  -0.07544 0.00243  103 LYS A O   
672  C CB  . LYS A 103 ? 0.47347 0.61233 0.74136 0.14741  -0.13561 -0.03423 103 LYS A CB  
673  C CG  . LYS A 103 ? 0.55288 0.72872 0.84292 0.15831  -0.16664 -0.05296 103 LYS A CG  
674  C CD  . LYS A 103 ? 0.55260 0.73722 0.86479 0.13653  -0.18630 -0.07323 103 LYS A CD  
675  C CE  . LYS A 103 ? 0.64883 0.86826 0.98747 0.14677  -0.22291 -0.09550 103 LYS A CE  
676  N NZ  . LYS A 103 ? 0.76487 0.98147 1.11998 0.12730  -0.24393 -0.11570 103 LYS A NZ  
677  N N   . GLU A 104 ? 0.50695 0.57186 0.71057 0.16019  -0.08560 0.01064  104 GLU A N   
678  C CA  . GLU A 104 ? 0.54783 0.58382 0.74477 0.14615  -0.06397 0.02368  104 GLU A CA  
679  C C   . GLU A 104 ? 0.54919 0.57969 0.71954 0.14642  -0.06893 0.02022  104 GLU A C   
680  O O   . GLU A 104 ? 0.56414 0.59887 0.70191 0.17178  -0.08025 0.02024  104 GLU A O   
681  C CB  . GLU A 104 ? 0.58661 0.59750 0.77163 0.16226  -0.04449 0.04883  104 GLU A CB  
682  C CG  . GLU A 104 ? 0.67250 0.65837 0.87264 0.14129  -0.02466 0.05807  104 GLU A CG  
683  C CD  . GLU A 104 ? 0.85193 0.81017 1.04564 0.15443  -0.00517 0.08563  104 GLU A CD  
684  O OE1 . GLU A 104 ? 0.85046 0.80697 1.01435 0.18084  -0.00232 0.10244  104 GLU A OE1 
685  O OE2 . GLU A 104 ? 0.92683 0.86465 1.14653 0.13919  0.00683  0.09061  104 GLU A OE2 
686  N N   . ASP A 105 ? 0.42066 0.44282 0.60219 0.12148  -0.06263 0.01513  105 ASP A N   
687  C CA  . ASP A 105 ? 0.44978 0.46584 0.60712 0.12243  -0.06779 0.01003  105 ASP A CA  
688  C C   . ASP A 105 ? 0.46620 0.46406 0.62983 0.10350  -0.04914 0.01837  105 ASP A C   
689  O O   . ASP A 105 ? 0.37404 0.36916 0.56588 0.08220  -0.04149 0.01687  105 ASP A O   
690  C CB  . ASP A 105 ? 0.48638 0.51819 0.65525 0.11145  -0.09228 -0.01509 105 ASP A CB  
691  C CG  . ASP A 105 ? 0.65116 0.69882 0.80270 0.13639  -0.11756 -0.02749 105 ASP A CG  
692  O OD1 . ASP A 105 ? 0.72310 0.76248 0.83117 0.16275  -0.12135 -0.02450 105 ASP A OD1 
693  O OD2 . ASP A 105 ? 0.57386 0.64434 0.75536 0.13180  -0.13389 -0.04032 105 ASP A OD2 
694  N N   . LEU A 106 ? 0.45546 0.44330 0.59130 0.11406  -0.04336 0.02561  106 LEU A N   
695  C CA  . LEU A 106 ? 0.42778 0.40323 0.57067 0.09774  -0.02949 0.03070  106 LEU A CA  
696  C C   . LEU A 106 ? 0.44894 0.42674 0.60029 0.07811  -0.04336 0.00969  106 LEU A C   
697  O O   . LEU A 106 ? 0.45737 0.44131 0.59635 0.08403  -0.06309 -0.00655 106 LEU A O   
698  C CB  . LEU A 106 ? 0.45006 0.41859 0.56215 0.11852  -0.01684 0.04698  106 LEU A CB  
699  C CG  . LEU A 106 ? 0.56570 0.52800 0.67359 0.13605  0.00529  0.07662  106 LEU A CG  
700  C CD1 . LEU A 106 ? 0.63743 0.59745 0.72210 0.15184  0.02177  0.09337  106 LEU A CD1 
701  C CD2 . LEU A 106 ? 0.50020 0.45252 0.65114 0.11435  0.01857  0.08627  106 LEU A CD2 
702  N N   . VAL A 107 ? 0.38529 0.35644 0.55846 0.05591  -0.03428 0.00990  107 VAL A N   
703  C CA  . VAL A 107 ? 0.41870 0.38780 0.59856 0.03817  -0.04276 -0.00444 107 VAL A CA  
704  C C   . VAL A 107 ? 0.39741 0.35454 0.57063 0.03502  -0.03108 0.00257  107 VAL A C   
705  O O   . VAL A 107 ? 0.36100 0.31414 0.54890 0.02968  -0.01657 0.01408  107 VAL A O   
706  C CB  . VAL A 107 ? 0.41063 0.38608 0.62051 0.01747  -0.04296 -0.01062 107 VAL A CB  
707  C CG1 . VAL A 107 ? 0.37455 0.34712 0.58979 0.00193  -0.05111 -0.02171 107 VAL A CG1 
708  C CG2 . VAL A 107 ? 0.49570 0.48774 0.71799 0.02268  -0.05077 -0.01426 107 VAL A CG2 
709  N N   . PHE A 108 ? 0.37270 0.32415 0.52722 0.03883  -0.03929 -0.00591 108 PHE A N   
710  C CA  . PHE A 108 ? 0.38593 0.32862 0.53587 0.03609  -0.03053 -0.00194 108 PHE A CA  
711  C C   . PHE A 108 ? 0.35465 0.29205 0.52288 0.01348  -0.03457 -0.01098 108 PHE A C   
712  O O   . PHE A 108 ? 0.38589 0.32128 0.55709 0.00525  -0.04801 -0.02324 108 PHE A O   
713  C CB  . PHE A 108 ? 0.41288 0.35007 0.52940 0.05566  -0.03776 -0.00772 108 PHE A CB  
714  C CG  . PHE A 108 ? 0.42771 0.35843 0.53938 0.05612  -0.02887 -0.00395 108 PHE A CG  
715  C CD1 . PHE A 108 ? 0.40950 0.34707 0.52567 0.06433  -0.00854 0.01519  108 PHE A CD1 
716  C CD2 . PHE A 108 ? 0.50978 0.42801 0.61630 0.04885  -0.04085 -0.01847 108 PHE A CD2 
717  C CE1 . PHE A 108 ? 0.47151 0.40842 0.58815 0.06611  -0.00066 0.01871  108 PHE A CE1 
718  C CE2 . PHE A 108 ? 0.56110 0.47444 0.66253 0.05216  -0.03312 -0.01503 108 PHE A CE2 
719  C CZ  . PHE A 108 ? 0.48944 0.41461 0.59640 0.06122  -0.01344 0.00288  108 PHE A CZ  
720  N N   . ILE A 109 ? 0.38368 0.31934 0.56649 0.00425  -0.02335 -0.00417 109 ILE A N   
721  C CA  . ILE A 109 ? 0.34766 0.27897 0.54231 -0.01251 -0.02557 -0.01050 109 ILE A CA  
722  C C   . ILE A 109 ? 0.35912 0.28265 0.54644 -0.01152 -0.02341 -0.00999 109 ILE A C   
723  O O   . ILE A 109 ? 0.35960 0.28686 0.55024 -0.00421 -0.01429 -0.00130 109 ILE A O   
724  C CB  . ILE A 109 ? 0.35487 0.29113 0.57023 -0.02070 -0.01897 -0.00765 109 ILE A CB  
725  C CG1 . ILE A 109 ? 0.37154 0.31668 0.59333 -0.01936 -0.02167 -0.00894 109 ILE A CG1 
726  C CG2 . ILE A 109 ? 0.36838 0.30091 0.58800 -0.03204 -0.02005 -0.01316 109 ILE A CG2 
727  C CD1 . ILE A 109 ? 0.39622 0.34412 0.63445 -0.02278 -0.01616 -0.00798 109 ILE A CD1 
728  N N   . PHE A 110 ? 0.33741 0.25094 0.51837 -0.01838 -0.03097 -0.01753 110 PHE A N   
729  C CA  . PHE A 110 ? 0.37375 0.27919 0.54857 -0.01742 -0.02989 -0.01752 110 PHE A CA  
730  C C   . PHE A 110 ? 0.34710 0.25058 0.53110 -0.02952 -0.02921 -0.01835 110 PHE A C   
731  O O   . PHE A 110 ? 0.35502 0.25329 0.53936 -0.03793 -0.03273 -0.02054 110 PHE A O   
732  C CB  . PHE A 110 ? 0.34016 0.23013 0.49495 -0.01094 -0.03958 -0.02478 110 PHE A CB  
733  C CG  . PHE A 110 ? 0.36733 0.24705 0.51394 -0.00755 -0.03924 -0.02485 110 PHE A CG  
734  C CD1 . PHE A 110 ? 0.37724 0.26854 0.53252 -0.00316 -0.03032 -0.01818 110 PHE A CD1 
735  C CD2 . PHE A 110 ? 0.40721 0.26545 0.54171 -0.00848 -0.04915 -0.03169 110 PHE A CD2 
736  C CE1 . PHE A 110 ? 0.35637 0.24111 0.50508 0.00233  -0.03179 -0.01905 110 PHE A CE1 
737  C CE2 . PHE A 110 ? 0.43153 0.27798 0.55583 -0.00234 -0.04957 -0.03145 110 PHE A CE2 
738  C CZ  . PHE A 110 ? 0.41021 0.27175 0.54000 0.00423  -0.04096 -0.02537 110 PHE A CZ  
739  N N   . TRP A 111 ? 0.31666 0.22574 0.50973 -0.02888 -0.02485 -0.01614 111 TRP A N   
740  C CA  . TRP A 111 ? 0.32049 0.22899 0.51620 -0.03406 -0.02579 -0.01876 111 TRP A CA  
741  C C   . TRP A 111 ? 0.35033 0.25102 0.53497 -0.02929 -0.02925 -0.01952 111 TRP A C   
742  O O   . TRP A 111 ? 0.33711 0.24384 0.52906 -0.02285 -0.02895 -0.01874 111 TRP A O   
743  C CB  . TRP A 111 ? 0.30570 0.22453 0.52132 -0.03441 -0.02396 -0.02024 111 TRP A CB  
744  C CG  . TRP A 111 ? 0.29085 0.20984 0.50658 -0.03376 -0.02894 -0.02720 111 TRP A CG  
745  C CD1 . TRP A 111 ? 0.30334 0.22685 0.53274 -0.03052 -0.03476 -0.03206 111 TRP A CD1 
746  C CD2 . TRP A 111 ? 0.31719 0.23384 0.51857 -0.03349 -0.02930 -0.03048 111 TRP A CD2 
747  N NE1 . TRP A 111 ? 0.30899 0.23101 0.52876 -0.02661 -0.04208 -0.04129 111 TRP A NE1 
748  C CE2 . TRP A 111 ? 0.32015 0.23776 0.51929 -0.02690 -0.03692 -0.03906 111 TRP A CE2 
749  C CE3 . TRP A 111 ? 0.36289 0.27922 0.55493 -0.03677 -0.02351 -0.02620 111 TRP A CE3 
750  C CZ2 . TRP A 111 ? 0.38156 0.29809 0.56044 -0.01968 -0.03793 -0.04336 111 TRP A CZ2 
751  C CZ3 . TRP A 111 ? 0.41316 0.33097 0.59142 -0.03196 -0.02095 -0.02709 111 TRP A CZ3 
752  C CH2 . TRP A 111 ? 0.40278 0.31972 0.57007 -0.02171 -0.02761 -0.03548 111 TRP A CH2 
753  N N   . ALA A 112 ? 0.35339 0.24159 0.52294 -0.03146 -0.03127 -0.01889 112 ALA A N   
754  C CA  . ALA A 112 ? 0.36069 0.23709 0.51570 -0.02476 -0.03494 -0.01820 112 ALA A CA  
755  C C   . ALA A 112 ? 0.36232 0.23267 0.50459 -0.02440 -0.03418 -0.01511 112 ALA A C   
756  O O   . ALA A 112 ? 0.39214 0.24643 0.52318 -0.02709 -0.03204 -0.00825 112 ALA A O   
757  C CB  . ALA A 112 ? 0.40663 0.26499 0.55045 -0.02323 -0.03817 -0.01779 112 ALA A CB  
758  N N   . PRO A 113 ? 0.38316 0.26541 0.52732 -0.01951 -0.03618 -0.01973 113 PRO A N   
759  C CA  . PRO A 113 ? 0.42444 0.30284 0.54848 -0.01317 -0.03489 -0.01688 113 PRO A CA  
760  C C   . PRO A 113 ? 0.44979 0.31346 0.55248 -0.00319 -0.03803 -0.01167 113 PRO A C   
761  O O   . PRO A 113 ? 0.42847 0.29088 0.53450 0.00200  -0.04471 -0.01530 113 PRO A O   
762  C CB  . PRO A 113 ? 0.42553 0.31914 0.55655 -0.00669 -0.04193 -0.02900 113 PRO A CB  
763  C CG  . PRO A 113 ? 0.41218 0.31545 0.57149 -0.00961 -0.04821 -0.03561 113 PRO A CG  
764  C CD  . PRO A 113 ? 0.33618 0.23486 0.50234 -0.01824 -0.04038 -0.02776 113 PRO A CD  
765  N N   . GLU A 114 ? 0.45394 0.30670 0.53470 0.00117  -0.03116 -0.00059 114 GLU A N   
766  C CA  . GLU A 114 ? 0.48410 0.31775 0.54244 0.01160  -0.03230 0.00831  114 GLU A CA  
767  C C   . GLU A 114 ? 0.49193 0.33361 0.53972 0.02897  -0.04547 -0.00192 114 GLU A C   
768  O O   . GLU A 114 ? 0.53750 0.36705 0.57616 0.03750  -0.05043 0.00064  114 GLU A O   
769  C CB  . GLU A 114 ? 0.53934 0.36167 0.57635 0.01561  -0.01921 0.02655  114 GLU A CB  
770  C CG  . GLU A 114 ? 0.53694 0.34987 0.59295 -0.00278 -0.00683 0.03985  114 GLU A CG  
771  C CD  . GLU A 114 ? 0.54280 0.33308 0.61278 -0.01304 -0.01297 0.03946  114 GLU A CD  
772  O OE1 . GLU A 114 ? 0.50539 0.27872 0.56009 -0.00237 -0.02027 0.03867  114 GLU A OE1 
773  O OE2 . GLU A 114 ? 0.54418 0.33397 0.63944 -0.02942 -0.01207 0.03834  114 GLU A OE2 
774  N N   . SER A 115 ? 0.48059 0.34217 0.53201 0.03543  -0.05341 -0.01506 115 SER A N   
775  C CA  . SER A 115 ? 0.52719 0.39818 0.57329 0.05237  -0.06963 -0.02658 115 SER A CA  
776  C C   . SER A 115 ? 0.54040 0.42697 0.62376 0.04680  -0.07914 -0.03762 115 SER A C   
777  O O   . SER A 115 ? 0.53515 0.43459 0.62573 0.05890  -0.09395 -0.04788 115 SER A O   
778  C CB  . SER A 115 ? 0.58271 0.46597 0.61517 0.06552  -0.07855 -0.03892 115 SER A CB  
779  O OG  . SER A 115 ? 0.64821 0.54147 0.70359 0.05271  -0.07588 -0.04685 115 SER A OG  
780  N N   . ALA A 116 ? 0.45121 0.33927 0.55916 0.03088  -0.07075 -0.03473 116 ALA A N   
781  C CA  . ALA A 116 ? 0.42002 0.32316 0.56019 0.02871  -0.07400 -0.03891 116 ALA A CA  
782  C C   . ALA A 116 ? 0.48557 0.38141 0.61352 0.04129  -0.07659 -0.03454 116 ALA A C   
783  O O   . ALA A 116 ? 0.49133 0.36202 0.58994 0.04450  -0.07152 -0.02528 116 ALA A O   
784  C CB  . ALA A 116 ? 0.41546 0.31895 0.57308 0.01465  -0.06245 -0.03382 116 ALA A CB  
785  N N   . PRO A 117 ? 0.43268 0.34960 0.58672 0.04848  -0.08380 -0.04004 117 PRO A N   
786  C CA  . PRO A 117 ? 0.49390 0.40624 0.63654 0.06414  -0.08657 -0.03667 117 PRO A CA  
787  C C   . PRO A 117 ? 0.45638 0.34892 0.58581 0.06283  -0.07498 -0.02824 117 PRO A C   
788  O O   . PRO A 117 ? 0.43159 0.33031 0.57684 0.05336  -0.06603 -0.02665 117 PRO A O   
789  C CB  . PRO A 117 ? 0.49434 0.44248 0.68146 0.06909  -0.09422 -0.04378 117 PRO A CB  
790  C CG  . PRO A 117 ? 0.49152 0.45756 0.71014 0.05669  -0.10097 -0.05347 117 PRO A CG  
791  C CD  . PRO A 117 ? 0.43213 0.37886 0.63265 0.04271  -0.09014 -0.04919 117 PRO A CD  
792  N N   . LEU A 118 ? 0.41880 0.32655 0.72446 -0.02468 -0.01454 0.03135  118 LEU A N   
793  C CA  . LEU A 118 ? 0.40952 0.32763 0.73806 -0.01005 0.00659  0.02668  118 LEU A CA  
794  C C   . LEU A 118 ? 0.39910 0.32495 0.75518 -0.00661 0.02540  0.02327  118 LEU A C   
795  O O   . LEU A 118 ? 0.38233 0.29188 0.71954 0.00248  0.04221  0.01157  118 LEU A O   
796  C CB  . LEU A 118 ? 0.39989 0.33292 0.76121 -0.00406 -0.00095 0.03844  118 LEU A CB  
797  C CG  . LEU A 118 ? 0.33271 0.25151 0.69864 0.00730  0.00959  0.03352  118 LEU A CG  
798  C CD1 . LEU A 118 ? 0.37443 0.28063 0.70456 0.00468  0.01002  0.03128  118 LEU A CD1 
799  C CD2 . LEU A 118 ? 0.34855 0.27090 0.74490 0.01214  -0.00255 0.04733  118 LEU A CD2 
800  N N   . LYS A 119 ? 0.37592 0.32944 0.77634 -0.01378 0.02215  0.03886  119 LYS A N   
801  C CA  . LYS A 119 ? 0.39946 0.37404 0.83471 -0.00230 0.04823  0.04572  119 LYS A CA  
802  C C   . LYS A 119 ? 0.41635 0.37140 0.81521 -0.00660 0.06243  0.03371  119 LYS A C   
803  O O   . LYS A 119 ? 0.45234 0.39412 0.83387 0.01128  0.08804  0.02353  119 LYS A O   
804  C CB  . LYS A 119 ? 0.43454 0.46064 0.93911 -0.01291 0.03929  0.07897  119 LYS A CB  
805  C CG  . LYS A 119 ? 0.58478 0.64902 1.13453 0.00334  0.07263  0.09810  119 LYS A CG  
806  C CD  . LYS A 119 ? 0.56439 0.63763 1.13821 0.04501  0.10289  0.10215  119 LYS A CD  
807  C CE  . LYS A 119 ? 0.61617 0.74490 1.24776 0.06877  0.14055  0.13564  119 LYS A CE  
808  N NZ  . LYS A 119 ? 0.66458 0.78870 1.26846 0.05741  0.15544  0.13167  119 LYS A NZ  
809  N N   . SER A 120 ? 0.36905 0.31086 0.74519 -0.02943 0.04357  0.03453  120 SER A N   
810  C CA  . SER A 120 ? 0.41228 0.33311 0.75561 -0.03306 0.05555  0.02628  120 SER A CA  
811  C C   . SER A 120 ? 0.41417 0.29881 0.70074 -0.02073 0.06152  0.00393  120 SER A C   
812  O O   . SER A 120 ? 0.42239 0.29494 0.68732 -0.01500 0.07798  -0.00307 120 SER A O   
813  C CB  . SER A 120 ? 0.52368 0.42836 0.85605 -0.06195 0.02949  0.03703  120 SER A CB  
814  O OG  . SER A 120 ? 0.62199 0.48616 0.90563 -0.06808 0.00171  0.02694  120 SER A OG  
815  N N   . LYS A 121 ? 0.40014 0.27459 0.66749 -0.01635 0.04856  -0.00077 121 LYS A N   
816  C CA  . LYS A 121 ? 0.42877 0.28899 0.66320 -0.00491 0.05412  -0.00815 121 LYS A CA  
817  C C   . LYS A 121 ? 0.44134 0.30091 0.68310 0.00219  0.06550  -0.01249 121 LYS A C   
818  O O   . LYS A 121 ? 0.42154 0.26652 0.63655 0.00359  0.06939  -0.01594 121 LYS A O   
819  C CB  . LYS A 121 ? 0.40098 0.26575 0.62702 0.00060  0.04240  -0.00147 121 LYS A CB  
820  C CG  . LYS A 121 ? 0.39285 0.26404 0.60829 0.00991  0.04656  0.00595  121 LYS A CG  
821  C CD  . LYS A 121 ? 0.47553 0.36519 0.69555 0.01582  0.03869  0.02224  121 LYS A CD  
822  C CE  . LYS A 121 ? 0.48193 0.35702 0.65504 0.02983  0.04207  0.02471  121 LYS A CE  
823  N NZ  . LYS A 121 ? 0.46687 0.36418 0.63787 0.04098  0.04067  0.04557  121 LYS A NZ  
824  N N   . MET A 122 ? 0.35544 0.22187 0.62523 0.00820  0.06851  -0.01122 122 MET A N   
825  C CA  . MET A 122 ? 0.37805 0.21655 0.62869 0.01892  0.07690  -0.01966 122 MET A CA  
826  C C   . MET A 122 ? 0.41338 0.24064 0.64296 0.02602  0.09977  -0.02582 122 MET A C   
827  O O   . MET A 122 ? 0.44587 0.23353 0.63020 0.03228  0.10344  -0.03611 122 MET A O   
828  C CB  . MET A 122 ? 0.34767 0.18154 0.62142 0.03188  0.07632  -0.01696 122 MET A CB  
829  C CG  . MET A 122 ? 0.39589 0.23436 0.68245 0.02258  0.05098  -0.00785 122 MET A CG  
830  S SD  . MET A 122 ? 0.39712 0.22341 0.65364 0.00629  0.03056  -0.00171 122 MET A SD  
831  C CE  . MET A 122 ? 0.40838 0.17099 0.61049 0.00825  0.02431  -0.01535 122 MET A CE  
832  N N   . ILE A 123 ? 0.38786 0.24570 0.64516 0.02248  0.11181  -0.01601 123 ILE A N   
833  C CA  . ILE A 123 ? 0.43441 0.28821 0.67298 0.02702  0.13439  -0.01509 123 ILE A CA  
834  C C   . ILE A 123 ? 0.44848 0.27755 0.64312 0.01495  0.12478  -0.02316 123 ILE A C   
835  O O   . ILE A 123 ? 0.47269 0.27446 0.62444 0.02081  0.13450  -0.02990 123 ILE A O   
836  C CB  . ILE A 123 ? 0.46399 0.36415 0.75452 0.01905  0.14414  0.00842  123 ILE A CB  
837  C CG1 . ILE A 123 ? 0.47547 0.41433 0.82346 0.03393  0.15439  0.02648  123 ILE A CG1 
838  C CG2 . ILE A 123 ? 0.51765 0.42024 0.79170 0.02298  0.17006  0.01661  123 ILE A CG2 
839  C CD1 . ILE A 123 ? 0.46943 0.46847 0.88727 0.01706  0.15330  0.06283  123 ILE A CD1 
840  N N   . TYR A 124 ? 0.40261 0.23598 0.60029 0.00198  0.10580  -0.02091 124 TYR A N   
841  C CA  . TYR A 124 ? 0.43342 0.24812 0.59529 -0.00139 0.09995  -0.02268 124 TYR A CA  
842  C C   . TYR A 124 ? 0.46588 0.26594 0.60515 0.00178  0.09112  -0.02516 124 TYR A C   
843  O O   . TYR A 124 ? 0.46457 0.24752 0.57266 -0.00041 0.09042  -0.02439 124 TYR A O   
844  C CB  . TYR A 124 ? 0.42560 0.23840 0.58295 -0.00352 0.08678  -0.01868 124 TYR A CB  
845  C CG  . TYR A 124 ? 0.45706 0.25453 0.60741 -0.01398 0.08323  -0.01579 124 TYR A CG  
846  C CD1 . TYR A 124 ? 0.45391 0.22505 0.57284 -0.01511 0.08595  -0.01420 124 TYR A CD1 
847  C CD2 . TYR A 124 ? 0.43167 0.23507 0.60479 -0.02644 0.07041  -0.01079 124 TYR A CD2 
848  C CE1 . TYR A 124 ? 0.48425 0.22641 0.59001 -0.02977 0.07493  -0.00950 124 TYR A CE1 
849  C CE2 . TYR A 124 ? 0.45066 0.22918 0.61292 -0.04510 0.05529  -0.00371 124 TYR A CE2 
850  C CZ  . TYR A 124 ? 0.47730 0.22089 0.60365 -0.04745 0.05696  -0.00392 124 TYR A CZ  
851  O OH  . TYR A 124 ? 0.52177 0.22585 0.63011 -0.07044 0.03451  0.00473  124 TYR A OH  
852  N N   . ALA A 125 ? 0.43039 0.23525 0.58535 0.00250  0.07845  -0.02355 125 ALA A N   
853  C CA  . ALA A 125 ? 0.46851 0.25816 0.60737 -0.00391 0.05884  -0.01746 125 ALA A CA  
854  C C   . ALA A 125 ? 0.53866 0.27919 0.63075 -0.00369 0.05858  -0.03014 125 ALA A C   
855  O O   . ALA A 125 ? 0.55499 0.27147 0.61384 -0.01540 0.03958  -0.02451 125 ALA A O   
856  C CB  . ALA A 125 ? 0.46335 0.26398 0.62969 -0.00645 0.04307  -0.00909 125 ALA A CB  
857  N N   . SER A 126 ? 0.50827 0.23060 0.59256 0.01199  0.07873  -0.04376 126 SER A N   
858  C CA  . SER A 126 ? 0.55040 0.21035 0.56986 0.02357  0.08471  -0.05806 126 SER A CA  
859  C C   . SER A 126 ? 0.63567 0.28800 0.61793 0.02792  0.10495  -0.06038 126 SER A C   
860  O O   . SER A 126 ? 0.73996 0.33020 0.64681 0.03619  0.10623  -0.07164 126 SER A O   
861  C CB  . SER A 126 ? 0.62755 0.27332 0.65008 0.05103  0.10686  -0.06599 126 SER A CB  
862  O OG  . SER A 126 ? 0.61791 0.32141 0.69416 0.06331  0.13954  -0.05599 126 SER A OG  
863  N N   . SER A 127 ? 0.58566 0.28857 0.60817 0.02210  0.11775  -0.04954 127 SER A N   
864  C CA  . SER A 127 ? 0.64080 0.34079 0.63512 0.02288  0.13517  -0.04609 127 SER A CA  
865  C C   . SER A 127 ? 0.67676 0.37225 0.65359 0.00499  0.11219  -0.03847 127 SER A C   
866  O O   . SER A 127 ? 0.69835 0.38579 0.64640 0.00360  0.12165  -0.03385 127 SER A O   
867  C CB  . SER A 127 ? 0.60134 0.35122 0.64916 0.02346  0.15804  -0.03282 127 SER A CB  
868  O OG  . SER A 127 ? 0.60768 0.37740 0.68526 0.04133  0.18112  -0.02889 127 SER A OG  
869  N N   . LYS A 128 ? 0.60362 0.31188 0.60341 -0.00636 0.08471  -0.03060 128 LYS A N   
870  C CA  . LYS A 128 ? 0.66414 0.38562 0.66464 -0.01632 0.06856  -0.01314 128 LYS A CA  
871  C C   . LYS A 128 ? 0.70271 0.38336 0.64359 -0.02660 0.05172  -0.01064 128 LYS A C   
872  O O   . LYS A 128 ? 0.67788 0.36368 0.60754 -0.02995 0.05101  0.00175  128 LYS A O   
873  C CB  . LYS A 128 ? 0.60831 0.36253 0.65016 -0.02079 0.04782  0.00475  128 LYS A CB  
874  C CG  . LYS A 128 ? 0.61291 0.39445 0.66741 -0.02122 0.03848  0.03205  128 LYS A CG  
875  C CD  . LYS A 128 ? 0.59999 0.42705 0.70094 -0.01901 0.02591  0.05983  128 LYS A CD  
876  C CE  . LYS A 128 ? 0.66624 0.48852 0.77143 -0.04362 -0.01048 0.07560  128 LYS A CE  
877  N NZ  . LYS A 128 ? 0.74999 0.55431 0.82832 -0.06478 -0.04058 0.09354  128 LYS A NZ  
878  N N   . ASP A 129 ? 0.75534 0.38471 0.64858 -0.03196 0.03393  -0.02176 129 ASP A N   
879  C CA  . ASP A 129 ? 0.82071 0.39051 0.63549 -0.04511 0.00884  -0.02141 129 ASP A CA  
880  C C   . ASP A 129 ? 0.88300 0.43148 0.64598 -0.03084 0.04017  -0.03093 129 ASP A C   
881  O O   . ASP A 129 ? 0.93956 0.46748 0.65854 -0.04267 0.02394  -0.02035 129 ASP A O   
882  C CB  . ASP A 129 ? 0.88890 0.37947 0.63841 -0.04959 -0.01613 -0.03804 129 ASP A CB  
883  C CG  . ASP A 129 ? 0.94328 0.44308 0.72996 -0.07819 -0.06539 -0.01642 129 ASP A CG  
884  O OD1 . ASP A 129 ? 0.90625 0.47850 0.76442 -0.09270 -0.07952 0.01680  129 ASP A OD1 
885  O OD2 . ASP A 129 ? 1.02353 0.45530 0.76544 -0.08371 -0.08901 -0.02891 129 ASP A OD2 
886  N N   . ALA A 130 ? 0.87944 0.43925 0.65245 -0.00656 0.08412  -0.04402 130 ALA A N   
887  C CA  . ALA A 130 ? 0.96405 0.51328 0.69455 0.00838  0.11866  -0.04450 130 ALA A CA  
888  C C   . ALA A 130 ? 0.87169 0.46820 0.64396 -0.00329 0.12242  -0.02394 130 ALA A C   
889  O O   . ALA A 130 ? 0.89121 0.46814 0.61440 -0.00491 0.12744  -0.01623 130 ALA A O   
890  C CB  . ALA A 130 ? 0.94527 0.51259 0.69529 0.03723  0.16509  -0.05029 130 ALA A CB  
891  N N   . ILE A 131 ? 0.78725 0.43527 0.63859 -0.00934 0.11926  -0.01486 131 ILE A N   
892  C CA  . ILE A 131 ? 0.80147 0.47276 0.67665 -0.01604 0.12069  0.00264  131 ILE A CA  
893  C C   . ILE A 131 ? 0.84290 0.50419 0.69722 -0.02655 0.08999  0.01736  131 ILE A C   
894  O O   . ILE A 131 ? 0.82516 0.48001 0.65824 -0.02988 0.09044  0.03150  131 ILE A O   
895  C CB  . ILE A 131 ? 0.71823 0.42383 0.65867 -0.01539 0.12434  0.00605  131 ILE A CB  
896  C CG1 . ILE A 131 ? 0.72928 0.43337 0.67336 -0.01829 0.11978  0.02229  131 ILE A CG1 
897  C CG2 . ILE A 131 ? 0.70169 0.42185 0.67329 -0.01325 0.10718  0.00103  131 ILE A CG2 
898  C CD1 . ILE A 131 ? 0.74846 0.45556 0.72597 -0.01713 0.12061  0.02363  131 ILE A CD1 
899  N N   . LYS A 132 ? 0.76358 0.42730 0.62762 -0.03386 0.06068  0.02088  132 LYS A N   
900  C CA  . LYS A 132 ? 0.83158 0.50120 0.69196 -0.04662 0.02772  0.04723  132 LYS A CA  
901  C C   . LYS A 132 ? 0.92838 0.54783 0.70860 -0.05923 0.01216  0.04800  132 LYS A C   
902  O O   . LYS A 132 ? 0.97708 0.60428 0.75202 -0.06669 -0.00361 0.07282  132 LYS A O   
903  C CB  . LYS A 132 ? 0.76848 0.45885 0.66344 -0.05780 -0.00442 0.06148  132 LYS A CB  
904  C CG  . LYS A 132 ? 0.72546 0.47928 0.69490 -0.04460 -0.00002 0.08864  132 LYS A CG  
905  C CD  . LYS A 132 ? 0.76280 0.55196 0.77484 -0.05798 -0.03215 0.11724  132 LYS A CD  
906  C CE  . LYS A 132 ? 0.77140 0.58055 0.79112 -0.07780 -0.07102 0.16153  132 LYS A CE  
907  N NZ  . LYS A 132 ? 0.77295 0.62722 0.84718 -0.09767 -0.10741 0.20186  132 LYS A NZ  
908  N N   . LYS A 133 ? 0.99884 0.56122 0.70817 -0.05717 0.01835  0.02233  133 LYS A N   
909  C CA  . LYS A 133 ? 1.00307 0.50122 0.61080 -0.06310 0.00813  0.01937  133 LYS A CA  
910  C C   . LYS A 133 ? 1.04527 0.55863 0.64451 -0.05359 0.03954  0.02943  133 LYS A C   
911  O O   . LYS A 133 ? 1.08676 0.56482 0.61824 -0.06291 0.02384  0.04025  133 LYS A O   
912  C CB  . LYS A 133 ? 1.11067 0.53375 0.63018 -0.04874 0.02036  -0.01230 133 LYS A CB  
913  C CG  . LYS A 133 ? 1.30390 0.66735 0.78089 -0.06840 -0.03085 -0.01941 133 LYS A CG  
914  C CD  . LYS A 133 ? 1.38268 0.65264 0.75825 -0.04466 -0.01510 -0.05426 133 LYS A CD  
915  C CE  . LYS A 133 ? 1.45879 0.66958 0.81043 -0.06625 -0.06831 -0.06081 133 LYS A CE  
916  N NZ  . LYS A 133 ? 1.55394 0.70688 0.84206 -0.11010 -0.14171 -0.04218 133 LYS A NZ  
917  N N   . LYS A 134 ? 1.01859 0.57861 0.68103 -0.03902 0.07879  0.02920  134 LYS A N   
918  C CA  . LYS A 134 ? 1.04963 0.62359 0.71278 -0.03685 0.10096  0.04612  134 LYS A CA  
919  C C   . LYS A 134 ? 1.03931 0.63471 0.73688 -0.04719 0.07498  0.07244  134 LYS A C   
920  O O   . LYS A 134 ? 1.11797 0.70446 0.78882 -0.05079 0.07630  0.09075  134 LYS A O   
921  C CB  . LYS A 134 ? 0.97680 0.58814 0.69863 -0.02676 0.13918  0.04527  134 LYS A CB  
922  C CG  . LYS A 134 ? 0.97425 0.58122 0.67554 -0.00948 0.17440  0.03165  134 LYS A CG  
923  C CD  . LYS A 134 ? 1.08096 0.65629 0.69802 0.00188  0.19913  0.03847  134 LYS A CD  
924  C CE  . LYS A 134 ? 1.07859 0.66648 0.68947 0.03007  0.24858  0.03696  134 LYS A CE  
925  N NZ  . LYS A 134 ? 1.19032 0.74765 0.70935 0.04946  0.28084  0.04779  134 LYS A NZ  
926  N N   . LEU A 135 ? 0.72623 1.11216 0.49577 0.26067  0.02126  0.02463  135 LEU A N   
927  C CA  . LEU A 135 ? 0.76194 1.09077 0.56019 0.22497  0.00499  0.03779  135 LEU A CA  
928  C C   . LEU A 135 ? 0.84952 1.14810 0.61897 0.25428  -0.02891 -0.00546 135 LEU A C   
929  O O   . LEU A 135 ? 0.86816 1.09761 0.67206 0.24262  -0.05238 -0.04122 135 LEU A O   
930  C CB  . LEU A 135 ? 0.76887 1.02916 0.63036 0.18249  0.00490  0.03085  135 LEU A CB  
931  C CG  . LEU A 135 ? 0.76041 1.04565 0.64793 0.16172  0.03092  0.05536  135 LEU A CG  
932  C CD1 . LEU A 135 ? 0.64254 0.86105 0.58061 0.12859  0.02778  0.04083  135 LEU A CD1 
933  C CD2 . LEU A 135 ? 0.72885 1.06816 0.62048 0.13861  0.04928  0.11844  135 LEU A CD2 
934  N N   . THR A 136 ? 0.87058 1.22962 0.57665 0.29393  -0.03171 0.00037  136 THR A N   
935  C CA  . THR A 136 ? 0.94956 1.29045 0.61811 0.32881  -0.06836 -0.04380 136 THR A CA  
936  C C   . THR A 136 ? 0.97076 1.25679 0.67533 0.29701  -0.09052 -0.03331 136 THR A C   
937  O O   . THR A 136 ? 0.98886 1.28733 0.70433 0.27018  -0.07797 0.02223  136 THR A O   
938  C CB  . THR A 136 ? 1.01464 1.44340 0.59967 0.37900  -0.06337 -0.03053 136 THR A CB  
939  O OG1 . THR A 136 ? 1.06745 1.54111 0.64856 0.35586  -0.04313 0.04446  136 THR A OG1 
940  C CG2 . THR A 136 ? 0.93181 1.42559 0.48379 0.41569  -0.03758 -0.04015 136 THR A CG2 
941  N N   . GLY A 137 ? 0.93576 1.16083 0.66558 0.29991  -0.12535 -0.08556 137 GLY A N   
942  C CA  . GLY A 137 ? 0.88046 1.05749 0.65368 0.27312  -0.14677 -0.08086 137 GLY A CA  
943  C C   . GLY A 137 ? 0.87573 0.99539 0.72800 0.22734  -0.13669 -0.07758 137 GLY A C   
944  O O   . GLY A 137 ? 0.90172 0.98694 0.79472 0.20671  -0.15034 -0.07197 137 GLY A O   
945  N N   . ILE A 138 ? 0.82051 0.93380 0.69359 0.21467  -0.11330 -0.08073 138 ILE A N   
946  C CA  . ILE A 138 ? 0.79585 0.86191 0.73543 0.17580  -0.10218 -0.07752 138 ILE A CA  
947  C C   . ILE A 138 ? 0.73607 0.75438 0.72032 0.17536  -0.13015 -0.12140 138 ILE A C   
948  O O   . ILE A 138 ? 0.79784 0.80866 0.77263 0.19931  -0.14968 -0.16083 138 ILE A O   
949  C CB  . ILE A 138 ? 0.79490 0.87465 0.73841 0.16569  -0.07167 -0.06569 138 ILE A CB  
950  C CG1 . ILE A 138 ? 0.74357 0.78518 0.74316 0.12660  -0.05717 -0.05315 138 ILE A CG1 
951  C CG2 . ILE A 138 ? 0.82009 0.90131 0.74859 0.19530  -0.07916 -0.10604 138 ILE A CG2 
952  C CD1 . ILE A 138 ? 0.61109 0.65628 0.61798 0.10090  -0.04517 -0.01093 138 ILE A CD1 
953  N N   . LYS A 139 ? 0.70555 0.69271 0.74298 0.14933  -0.13442 -0.11447 139 LYS A N   
954  C CA  . LYS A 139 ? 0.71314 0.66770 0.80167 0.14716  -0.16314 -0.14744 139 LYS A CA  
955  C C   . LYS A 139 ? 0.64828 0.57394 0.80116 0.11988  -0.14819 -0.14842 139 LYS A C   
956  O O   . LYS A 139 ? 0.62165 0.52475 0.82560 0.11563  -0.17012 -0.17171 139 LYS A O   
957  C CB  . LYS A 139 ? 0.70737 0.65959 0.81509 0.14466  -0.18363 -0.14051 139 LYS A CB  
958  C CG  . LYS A 139 ? 0.77074 0.75215 0.81582 0.17503  -0.20589 -0.14030 139 LYS A CG  
959  C CD  . LYS A 139 ? 0.85659 0.83186 0.92835 0.17760  -0.23756 -0.14366 139 LYS A CD  
960  C CE  . LYS A 139 ? 0.75951 0.72446 0.86696 0.15390  -0.21929 -0.10662 139 LYS A CE  
961  N NZ  . LYS A 139 ? 0.79783 0.76362 0.92423 0.16331  -0.25097 -0.10626 139 LYS A NZ  
962  N N   . HIS A 140 ? 0.49223 0.42110 0.64584 0.10126  -0.11353 -0.12191 140 HIS A N   
963  C CA  . HIS A 140 ? 0.55610 0.46551 0.76361 0.07741  -0.09639 -0.11678 140 HIS A CA  
964  C C   . HIS A 140 ? 0.52235 0.43944 0.70813 0.07133  -0.06794 -0.10231 140 HIS A C   
965  O O   . HIS A 140 ? 0.45727 0.39626 0.60147 0.07301  -0.05381 -0.08330 140 HIS A O   
966  C CB  . HIS A 140 ? 0.55186 0.45718 0.79298 0.05995  -0.08640 -0.09909 140 HIS A CB  
967  C CG  . HIS A 140 ? 0.60127 0.50562 0.86520 0.06746  -0.11404 -0.10880 140 HIS A CG  
968  N ND1 . HIS A 140 ? 0.66859 0.57992 0.90698 0.07443  -0.12106 -0.09485 140 HIS A ND1 
969  C CD2 . HIS A 140 ? 0.56572 0.46421 0.87901 0.06907  -0.14011 -0.12938 140 HIS A CD2 
970  C CE1 . HIS A 140 ? 0.64837 0.55987 0.91528 0.08276  -0.14934 -0.10775 140 HIS A CE1 
971  N NE2 . HIS A 140 ? 0.64457 0.55015 0.95893 0.07882  -0.16205 -0.12996 140 HIS A NE2 
972  N N   . GLU A 141 ? 0.52803 0.42965 0.74786 0.06275  -0.06121 -0.10726 141 GLU A N   
973  C CA  . GLU A 141 ? 0.49687 0.40483 0.70253 0.05832  -0.03784 -0.09475 141 GLU A CA  
974  C C   . GLU A 141 ? 0.54218 0.43805 0.79369 0.03738  -0.02130 -0.08219 141 GLU A C   
975  O O   . GLU A 141 ? 0.53471 0.41562 0.83690 0.03098  -0.03157 -0.08804 141 GLU A O   
976  C CB  . GLU A 141 ? 0.54882 0.45370 0.73758 0.08028  -0.04973 -0.11428 141 GLU A CB  
977  C CG  . GLU A 141 ? 0.54996 0.46389 0.72820 0.07891  -0.02788 -0.10064 141 GLU A CG  
978  C CD  . GLU A 141 ? 0.63765 0.54885 0.79793 0.10775  -0.04122 -0.12260 141 GLU A CD  
979  O OE1 . GLU A 141 ? 0.72244 0.63486 0.85904 0.13372  -0.06414 -0.14931 141 GLU A OE1 
980  O OE2 . GLU A 141 ? 0.70090 0.60893 0.86831 0.10838  -0.03057 -0.11507 141 GLU A OE2 
981  N N   . LEU A 142 ? 0.43096 0.33835 0.66638 0.02695  0.00335  -0.06306 142 LEU A N   
982  C CA  . LEU A 142 ? 0.45063 0.35523 0.71513 0.01345  0.02166  -0.04996 142 LEU A CA  
983  C C   . LEU A 142 ? 0.41014 0.32265 0.65040 0.01625  0.03334  -0.04092 142 LEU A C   
984  O O   . LEU A 142 ? 0.40578 0.33562 0.60824 0.01805  0.03938  -0.03539 142 LEU A O   
985  C CB  . LEU A 142 ? 0.41465 0.32641 0.68002 0.00283  0.03697  -0.04014 142 LEU A CB  
986  C CG  . LEU A 142 ? 0.40327 0.32378 0.68114 -0.00521 0.05990  -0.02655 142 LEU A CG  
987  C CD1 . LEU A 142 ? 0.52220 0.44504 0.85599 -0.00890 0.06241  -0.02123 142 LEU A CD1 
988  C CD2 . LEU A 142 ? 0.44494 0.36943 0.70365 -0.00753 0.06930  -0.02674 142 LEU A CD2 
989  N N   . GLN A 143 ? 0.36527 0.26682 0.63222 0.01627  0.03419  -0.03641 143 GLN A N   
990  C CA  . GLN A 143 ? 0.36538 0.27514 0.61453 0.01945  0.04584  -0.02375 143 GLN A CA  
991  C C   . GLN A 143 ? 0.40792 0.32538 0.67287 0.00569  0.06666  -0.00116 143 GLN A C   
992  O O   . GLN A 143 ? 0.39861 0.31086 0.70498 -0.00283 0.06981  0.00665  143 GLN A O   
993  C CB  . GLN A 143 ? 0.38877 0.27811 0.65175 0.03471  0.02937  -0.03277 143 GLN A CB  
994  C CG  . GLN A 143 ? 0.40855 0.29454 0.64894 0.05690  0.00764  -0.06085 143 GLN A CG  
995  C CD  . GLN A 143 ? 0.43271 0.30007 0.67562 0.07960  -0.00801 -0.07437 143 GLN A CD  
996  O OE1 . GLN A 143 ? 0.47018 0.34275 0.71017 0.08249  0.00299  -0.05900 143 GLN A OE1 
997  N NE2 . GLN A 143 ? 0.51344 0.35642 0.76201 0.09867  -0.03746 -0.10575 143 GLN A NE2 
998  N N   . ALA A 144 ? 0.34329 0.27950 0.57642 0.00500  0.08033  0.01063  144 ALA A N   
999  C CA  . ALA A 144 ? 0.35072 0.30019 0.58615 -0.00215 0.09941  0.03041  144 ALA A CA  
1000 C C   . ALA A 144 ? 0.35942 0.32202 0.57003 0.00333  0.10412  0.04419  144 ALA A C   
1001 O O   . ALA A 144 ? 0.34369 0.31703 0.52663 0.00833  0.09760  0.03696  144 ALA A O   
1002 C CB  . ALA A 144 ? 0.37579 0.33784 0.59116 -0.00782 0.10872  0.02414  144 ALA A CB  
1003 N N   . ASN A 145 ? 0.40010 0.36867 0.62273 0.00254  0.11611  0.06819  145 ASN A N   
1004 C CA  . ASN A 145 ? 0.38119 0.36469 0.58024 0.00936  0.11962  0.08494  145 ASN A CA  
1005 C C   . ASN A 145 ? 0.43570 0.44763 0.60760 0.00740  0.13708  0.09992  145 ASN A C   
1006 O O   . ASN A 145 ? 0.46438 0.49169 0.61968 0.01375  0.14082  0.12023  145 ASN A O   
1007 C CB  . ASN A 145 ? 0.39636 0.35894 0.62850 0.01634  0.11254  0.10346  145 ASN A CB  
1008 C CG  . ASN A 145 ? 0.47556 0.42197 0.76034 0.00625  0.11672  0.12275  145 ASN A CG  
1009 O OD1 . ASN A 145 ? 0.51755 0.48628 0.80783 -0.00261 0.13545  0.13653  145 ASN A OD1 
1010 N ND2 . ASN A 145 ? 0.53555 0.44498 0.86345 0.00892  0.09753  0.12392  145 ASN A ND2 
1011 N N   . CYS A 146 ? 0.41268 0.43304 0.57574 0.00302  0.14572  0.08789  146 CYS A N   
1012 C CA  . CYS A 146 ? 0.44978 0.49836 0.57863 0.00822  0.16025  0.09246  146 CYS A CA  
1013 C C   . CYS A 146 ? 0.47843 0.52464 0.59989 0.00784  0.16146  0.06604  146 CYS A C   
1014 O O   . CYS A 146 ? 0.42631 0.45334 0.57852 0.00225  0.15589  0.05449  146 CYS A O   
1015 C CB  . CYS A 146 ? 0.47103 0.54162 0.61628 0.01281  0.18144  0.12861  146 CYS A CB  
1016 S SG  . CYS A 146 ? 0.48482 0.55705 0.69449 0.00566  0.19631  0.14154  146 CYS A SG  
1017 N N   . TYR A 147 ? 0.49009 0.55448 0.56946 0.01703  0.16578  0.05452  147 TYR A N   
1018 C CA  . TYR A 147 ? 0.47586 0.53079 0.54592 0.02128  0.16199  0.02455  147 TYR A CA  
1019 C C   . TYR A 147 ? 0.45745 0.52538 0.56142 0.02872  0.18186  0.02989  147 TYR A C   
1020 O O   . TYR A 147 ? 0.49382 0.54445 0.61394 0.02920  0.17504  0.00884  147 TYR A O   
1021 C CB  . TYR A 147 ? 0.54601 0.61263 0.56166 0.03418  0.15656  0.00401  147 TYR A CB  
1022 C CG  . TYR A 147 ? 0.52514 0.57317 0.52086 0.02167  0.12807  -0.01051 147 TYR A CG  
1023 C CD1 . TYR A 147 ? 0.50490 0.52034 0.51692 0.00757  0.10755  -0.02792 147 TYR A CD1 
1024 C CD2 . TYR A 147 ? 0.57298 0.64122 0.53939 0.02293  0.12127  -0.00126 147 TYR A CD2 
1025 C CE1 . TYR A 147 ? 0.51427 0.52139 0.51890 -0.00761 0.08279  -0.03283 147 TYR A CE1 
1026 C CE2 . TYR A 147 ? 0.52620 0.58634 0.48581 0.00904  0.09451  -0.01063 147 TYR A CE2 
1027 C CZ  . TYR A 147 ? 0.54249 0.57397 0.52382 -0.00748 0.07633  -0.02488 147 TYR A CZ  
1028 O OH  . TYR A 147 ? 0.50874 0.54121 0.49296 -0.02448 0.05126  -0.02613 147 TYR A OH  
1029 N N   . GLU A 148 ? 0.44566 0.54804 0.56477 0.03457  0.20598  0.06150  148 GLU A N   
1030 C CA  . GLU A 148 ? 0.46593 0.59340 0.62868 0.03971  0.22679  0.07335  148 GLU A CA  
1031 C C   . GLU A 148 ? 0.42296 0.52030 0.64394 0.02374  0.21246  0.06889  148 GLU A C   
1032 O O   . GLU A 148 ? 0.48114 0.58410 0.73002 0.02849  0.21530  0.05669  148 GLU A O   
1033 C CB  . GLU A 148 ? 0.47929 0.65171 0.66090 0.04214  0.25407  0.12069  148 GLU A CB  
1034 C CG  . GLU A 148 ? 0.57205 0.78686 0.80679 0.04651  0.27947  0.14109  148 GLU A CG  
1035 C CD  . GLU A 148 ? 0.75071 1.01786 1.00884 0.04643  0.30868  0.19836  148 GLU A CD  
1036 O OE1 . GLU A 148 ? 0.79282 1.04218 1.05991 0.03240  0.30124  0.22808  148 GLU A OE1 
1037 O OE2 . GLU A 148 ? 0.82462 1.14727 1.08854 0.06108  0.33285  0.21219  148 GLU A OE2 
1038 N N   . GLU A 149 ? 0.41100 0.47748 0.64722 0.00881  0.19448  0.07499  149 GLU A N   
1039 C CA  . GLU A 149 ? 0.46605 0.50415 0.74804 -0.00206 0.17635  0.06582  149 GLU A CA  
1040 C C   . GLU A 149 ? 0.50350 0.51725 0.76238 -0.00008 0.15825  0.03189  149 GLU A C   
1041 O O   . GLU A 149 ? 0.50332 0.51046 0.79296 -0.00018 0.15124  0.02075  149 GLU A O   
1042 C CB  . GLU A 149 ? 0.44076 0.45319 0.73777 -0.01099 0.16042  0.07615  149 GLU A CB  
1043 C CG  . GLU A 149 ? 0.48181 0.50584 0.82105 -0.01675 0.17130  0.11428  149 GLU A CG  
1044 C CD  . GLU A 149 ? 0.51826 0.50621 0.87483 -0.02093 0.14943  0.11783  149 GLU A CD  
1045 O OE1 . GLU A 149 ? 0.49483 0.46014 0.82122 -0.01550 0.13095  0.09064  149 GLU A OE1 
1046 O OE2 . GLU A 149 ? 0.58735 0.57121 0.98972 -0.02807 0.15036  0.14911  149 GLU A OE2 
1047 N N   . VAL A 150 ? 0.42676 0.42852 0.63669 0.00044  0.14841  0.01898  150 VAL A N   
1048 C CA  . VAL A 150 ? 0.48091 0.45757 0.67752 -0.00247 0.12867  -0.00358 150 VAL A CA  
1049 C C   . VAL A 150 ? 0.48748 0.46273 0.68120 0.00740  0.13070  -0.02162 150 VAL A C   
1050 O O   . VAL A 150 ? 0.56563 0.51888 0.76815 0.00624  0.11516  -0.03480 150 VAL A O   
1051 C CB  . VAL A 150 ? 0.46542 0.43550 0.62313 -0.00853 0.11635  -0.00628 150 VAL A CB  
1052 C CG1 . VAL A 150 ? 0.44584 0.42056 0.56655 -0.00416 0.11640  -0.01788 150 VAL A CG1 
1053 C CG2 . VAL A 150 ? 0.44615 0.39738 0.60534 -0.01606 0.09673  -0.01317 150 VAL A CG2 
1054 N N   . LYS A 151 ? 0.49158 0.49172 0.67171 0.02101  0.14910  -0.02224 151 LYS A N   
1055 C CA  . LYS A 151 ? 0.53634 0.54034 0.71345 0.03910  0.15322  -0.04307 151 LYS A CA  
1056 C C   . LYS A 151 ? 0.54842 0.57879 0.77886 0.04695  0.16893  -0.03413 151 LYS A C   
1057 O O   . LYS A 151 ? 0.58356 0.62459 0.81739 0.06704  0.17468  -0.05114 151 LYS A O   
1058 C CB  . LYS A 151 ? 0.50419 0.53198 0.63519 0.05781  0.16633  -0.05184 151 LYS A CB  
1059 C CG  . LYS A 151 ? 0.55930 0.56314 0.64112 0.05173  0.14514  -0.06659 151 LYS A CG  
1060 C CD  . LYS A 151 ? 0.69323 0.72234 0.72498 0.07536  0.15395  -0.08115 151 LYS A CD  
1061 C CE  . LYS A 151 ? 0.79199 0.80321 0.78062 0.06610  0.12897  -0.09274 151 LYS A CE  
1062 N NZ  . LYS A 151 ? 0.82871 0.86066 0.76035 0.09230  0.12923  -0.11509 151 LYS A NZ  
1063 N N   . ASP A 152 ? 0.51848 0.56092 0.79461 0.03311  0.17385  -0.00893 152 ASP A N   
1064 C CA  . ASP A 152 ? 0.51297 0.58753 0.85203 0.03604  0.18664  0.00450  152 ASP A CA  
1065 C C   . ASP A 152 ? 0.53348 0.58214 0.89879 0.03586  0.16344  -0.01523 152 ASP A C   
1066 O O   . ASP A 152 ? 0.43324 0.45653 0.81798 0.02103  0.14195  -0.01411 152 ASP A O   
1067 C CB  . ASP A 152 ? 0.50753 0.59565 0.89382 0.01788  0.19192  0.03819  152 ASP A CB  
1068 C CG  . ASP A 152 ? 0.56234 0.69733 1.02355 0.01743  0.20873  0.06146  152 ASP A CG  
1069 O OD1 . ASP A 152 ? 0.51531 0.67581 0.99108 0.03413  0.21696  0.04891  152 ASP A OD1 
1070 O OD2 . ASP A 152 ? 0.59022 0.73807 1.10117 0.00055  0.21265  0.09428  152 ASP A OD2 
1071 N N   . ARG A 153 ? 0.50711 0.56275 0.87055 0.05648  0.16600  -0.03473 153 ARG A N   
1072 C CA  . ARG A 153 ? 0.49641 0.52601 0.88253 0.05870  0.14179  -0.05072 153 ARG A CA  
1073 C C   . ARG A 153 ? 0.50528 0.55796 0.96344 0.04934  0.13778  -0.03522 153 ARG A C   
1074 O O   . ARG A 153 ? 0.54157 0.56780 1.01475 0.04230  0.11051  -0.04228 153 ARG A O   
1075 C CB  . ARG A 153 ? 0.56487 0.59542 0.93972 0.08710  0.14390  -0.07515 153 ARG A CB  
1076 C CG  . ARG A 153 ? 0.67648 0.67480 0.98395 0.09542  0.13816  -0.09633 153 ARG A CG  
1077 C CD  . ARG A 153 ? 0.78285 0.72490 1.07568 0.09906  0.10632  -0.11830 153 ARG A CD  
1078 N NE  . ARG A 153 ? 0.85519 0.76058 1.09365 0.09977  0.09336  -0.13653 153 ARG A NE  
1079 C CZ  . ARG A 153 ? 0.82088 0.67586 1.04547 0.10747  0.06623  -0.15831 153 ARG A CZ  
1080 N NH1 . ARG A 153 ? 0.71712 0.55171 0.97297 0.11822  0.05085  -0.16357 153 ARG A NH1 
1081 N NH2 . ARG A 153 ? 0.77888 0.60145 0.96126 0.10402  0.05068  -0.17426 153 ARG A NH2 
1082 N N   . CYS A 154 ? 0.44982 0.55436 0.95469 0.04836  0.16268  -0.01165 154 CYS A N   
1083 C CA  . CYS A 154 ? 0.47381 0.60027 1.05901 0.03353  0.15445  0.00631  154 CYS A CA  
1084 C C   . CYS A 154 ? 0.48438 0.56920 1.07011 0.00999  0.12763  0.00907  154 CYS A C   
1085 O O   . CYS A 154 ? 0.51114 0.58556 1.14181 0.00106  0.10064  0.00452  154 CYS A O   
1086 C CB  . CYS A 154 ? 0.41266 0.60650 1.05141 0.03261  0.18828  0.04054  154 CYS A CB  
1087 S SG  . CYS A 154 ? 0.58913 0.84953 1.24082 0.06906  0.22004  0.03485  154 CYS A SG  
1088 N N   . THR A 155 ? 0.49126 0.55368 1.02637 0.00340  0.13227  0.01352  155 THR A N   
1089 C CA  . THR A 155 ? 0.58185 0.60768 1.11497 -0.01186 0.10805  0.01296  155 THR A CA  
1090 C C   . THR A 155 ? 0.50381 0.49072 0.99568 -0.00695 0.07954  -0.01417 155 THR A C   
1091 O O   . THR A 155 ? 0.50270 0.47137 1.01485 -0.01126 0.05171  -0.02349 155 THR A O   
1092 C CB  . THR A 155 ? 0.56369 0.58380 1.05979 -0.01674 0.12232  0.02836  155 THR A CB  
1093 O OG1 . THR A 155 ? 0.56721 0.62522 1.10956 -0.02338 0.14603  0.06222  155 THR A OG1 
1094 C CG2 . THR A 155 ? 0.60146 0.58180 1.08754 -0.02446 0.09600  0.02103  155 THR A CG2 
1095 N N   . LEU A 156 ? 0.53917 0.51443 0.97427 0.00271  0.08399  -0.02595 156 LEU A N   
1096 C CA  . LEU A 156 ? 0.52497 0.47134 0.92857 0.00640  0.05930  -0.04209 156 LEU A CA  
1097 C C   . LEU A 156 ? 0.48904 0.43927 0.93588 0.01214  0.04009  -0.05008 156 LEU A C   
1098 O O   . LEU A 156 ? 0.42683 0.36192 0.87109 0.01212  0.01358  -0.05813 156 LEU A O   
1099 C CB  . LEU A 156 ? 0.51307 0.44542 0.86577 0.01220  0.06449  -0.04841 156 LEU A CB  
1100 C CG  . LEU A 156 ? 0.50604 0.41166 0.83137 0.01343  0.04074  -0.05460 156 LEU A CG  
1101 C CD1 . LEU A 156 ? 0.49474 0.39537 0.80095 0.00770  0.02682  -0.05106 156 LEU A CD1 
1102 C CD2 . LEU A 156 ? 0.53406 0.42071 0.82027 0.01326  0.04191  -0.05677 156 LEU A CD2 
1103 N N   . ALA A 157 ? 0.46283 0.43968 0.95023 0.02041  0.05288  -0.04829 157 ALA A N   
1104 C CA  . ALA A 157 ? 0.41830 0.40562 0.95436 0.02749  0.03381  -0.05461 157 ALA A CA  
1105 C C   . ALA A 157 ? 0.45395 0.44641 1.04000 0.01479  0.01169  -0.05241 157 ALA A C   
1106 O O   . ALA A 157 ? 0.45586 0.43843 1.05300 0.01869  -0.01963 -0.06424 157 ALA A O   
1107 C CB  . ALA A 157 ? 0.41308 0.44069 0.99199 0.04159  0.05592  -0.05116 157 ALA A CB  
1108 N N   . GLU A 158 ? 0.45873 0.46390 1.07548 0.00035  0.02373  -0.03746 158 GLU A N   
1109 C CA  . GLU A 158 ? 0.51565 0.51507 1.18517 -0.01320 -0.00392 -0.03803 158 GLU A CA  
1110 C C   . GLU A 158 ? 0.51378 0.47003 1.12916 -0.01052 -0.03241 -0.05822 158 GLU A C   
1111 O O   . GLU A 158 ? 0.52296 0.46665 1.16042 -0.00978 -0.06892 -0.07494 158 GLU A O   
1112 C CB  . GLU A 158 ? 0.52522 0.54566 1.24827 -0.03059 0.01526  -0.01057 158 GLU A CB  
1113 C CG  . GLU A 158 ? 0.58905 0.66834 1.38531 -0.03238 0.03888  0.01269  158 GLU A CG  
1114 C CD  . GLU A 158 ? 0.70611 0.81596 1.55706 -0.05049 0.06247  0.05103  158 GLU A CD  
1115 O OE1 . GLU A 158 ? 0.71525 0.79838 1.52976 -0.05728 0.06878  0.05991  158 GLU A OE1 
1116 O OE2 . GLU A 158 ? 0.66257 0.81838 1.57442 -0.05384 0.07297  0.07467  158 GLU A OE2 
1117 N N   . LYS A 159 ? 0.50002 0.43850 1.04406 -0.00610 -0.01795 -0.05854 159 LYS A N   
1118 C CA  . LYS A 159 ? 0.57107 0.48165 1.06247 0.00211  -0.04177 -0.07650 159 LYS A CA  
1119 C C   . LYS A 159 ? 0.59067 0.49892 1.05671 0.01567  -0.06452 -0.09047 159 LYS A C   
1120 O O   . LYS A 159 ? 0.61799 0.51402 1.05736 0.02618  -0.09199 -0.10767 159 LYS A O   
1121 C CB  . LYS A 159 ? 0.53890 0.44155 0.96583 0.00421  -0.02154 -0.07026 159 LYS A CB  
1122 C CG  . LYS A 159 ? 0.56530 0.46772 1.00760 -0.00535 -0.00378 -0.05569 159 LYS A CG  
1123 C CD  . LYS A 159 ? 0.59085 0.47267 1.06861 -0.00698 -0.02957 -0.06486 159 LYS A CD  
1124 C CE  . LYS A 159 ? 0.61606 0.49203 1.10768 -0.01516 -0.01462 -0.04582 159 LYS A CE  
1125 N NZ  . LYS A 159 ? 0.63895 0.48325 1.16564 -0.01481 -0.04590 -0.05771 159 LYS A NZ  
1126 N N   . LEU A 160 ? 0.49566 0.41551 0.96745 0.01900  -0.05477 -0.08360 160 LEU A N   
1127 C CA  . LEU A 160 ? 0.46774 0.38270 0.91387 0.03219  -0.07549 -0.08958 160 LEU A CA  
1128 C C   . LEU A 160 ? 0.56865 0.49390 1.06664 0.03743  -0.10743 -0.10147 160 LEU A C   
1129 O O   . LEU A 160 ? 0.62622 0.54573 1.09600 0.05013  -0.13682 -0.11190 160 LEU A O   
1130 C CB  . LEU A 160 ? 0.47286 0.38692 0.90686 0.03595  -0.05713 -0.07888 160 LEU A CB  
1131 C CG  . LEU A 160 ? 0.47111 0.36921 0.84435 0.03241  -0.04045 -0.06934 160 LEU A CG  
1132 C CD1 . LEU A 160 ? 0.47212 0.36396 0.84742 0.03481  -0.02360 -0.06554 160 LEU A CD1 
1133 C CD2 . LEU A 160 ? 0.54170 0.42995 0.86714 0.03878  -0.06036 -0.06447 160 LEU A CD2 
1134 N N   . GLY A 161 ? 0.49461 0.44146 1.06923 0.02867  -0.10272 -0.09760 161 GLY A N   
1135 C CA  . GLY A 161 ? 0.52152 0.48554 1.15758 0.03187  -0.13415 -0.10638 161 GLY A CA  
1136 C C   . GLY A 161 ? 0.50920 0.50224 1.24067 0.01480  -0.12927 -0.09691 161 GLY A C   
1137 O O   . GLY A 161 ? 0.52987 0.55080 1.33178 0.01470  -0.14846 -0.09767 161 GLY A O   
1138 N N   . GLY A 162 ? 0.51913 0.51059 1.25811 -0.00028 -0.10363 -0.08322 162 GLY A N   
1139 C CA  . GLY A 162 ? 0.52827 0.54825 1.36172 -0.02033 -0.09951 -0.06527 162 GLY A CA  
1140 C C   . GLY A 162 ? 0.49585 0.57129 1.38374 -0.01820 -0.06628 -0.04243 162 GLY A C   
1141 O O   . GLY A 162 ? 0.48500 0.56822 1.32651 -0.00091 -0.03840 -0.04155 162 GLY A O   
1142 N N   . SER A 163 ? 0.50935 0.62427 1.49782 -0.03429 -0.07129 -0.02408 163 SER A N   
1143 C CA  . SER A 163 ? 0.43614 0.60825 1.46367 -0.02961 -0.03418 0.00336  163 SER A CA  
1144 C C   . SER A 163 ? 0.41883 0.61904 1.45850 -0.00650 -0.03997 -0.00994 163 SER A C   
1145 O O   . SER A 163 ? 0.40998 0.65914 1.46683 0.00596  -0.00675 0.00598  163 SER A O   
1146 C CB  . SER A 163 ? 0.45659 0.64641 1.54919 -0.05065 -0.03889 0.03234  163 SER A CB  
1147 O OG  . SER A 163 ? 0.51802 0.69741 1.65242 -0.05399 -0.08560 0.01641  163 SER A OG  
1148 N N   . ALA A 164 ? 0.41737 0.58967 1.44385 0.00289  -0.08266 -0.03789 164 ALA A N   
1149 C CA  . ALA A 164 ? 0.40918 0.60000 1.43883 0.02762  -0.09083 -0.04779 164 ALA A CA  
1150 C C   . ALA A 164 ? 0.40602 0.58093 1.36440 0.05460  -0.06484 -0.05569 164 ALA A C   
1151 O O   . ALA A 164 ? 0.36482 0.55680 1.33045 0.07882  -0.06334 -0.06032 164 ALA A O   
1152 C CB  . ALA A 164 ? 0.45887 0.62222 1.48435 0.03126  -0.14719 -0.07112 164 ALA A CB  
1153 N N   . VAL A 165 ? 0.53473 0.47778 1.23366 -0.05695 0.17495  -0.13252 165 VAL A N   
1154 C CA  . VAL A 165 ? 0.48884 0.44538 1.16867 -0.04283 0.14759  -0.11256 165 VAL A CA  
1155 C C   . VAL A 165 ? 0.52287 0.44363 1.16935 -0.04056 0.15818  -0.07862 165 VAL A C   
1156 O O   . VAL A 165 ? 0.52933 0.38633 1.14623 -0.03724 0.17731  -0.05398 165 VAL A O   
1157 C CB  . VAL A 165 ? 0.49026 0.43162 1.17400 -0.02306 0.13260  -0.10737 165 VAL A CB  
1158 C CG1 . VAL A 165 ? 0.42668 0.38733 1.07254 -0.00669 0.10568  -0.08797 165 VAL A CG1 
1159 C CG2 . VAL A 165 ? 0.39562 0.37855 1.11445 -0.03286 0.13055  -0.14994 165 VAL A CG2 
1160 N N   . ILE A 166 ? 0.43967 0.39636 1.07723 -0.04264 0.14552  -0.07687 166 ILE A N   
1161 C CA  . ILE A 166 ? 0.48104 0.41258 1.08892 -0.04574 0.16223  -0.05380 166 ILE A CA  
1162 C C   . ILE A 166 ? 0.47442 0.41112 1.03301 -0.02961 0.14078  -0.03102 166 ILE A C   
1163 O O   . ILE A 166 ? 0.50453 0.41286 1.02079 -0.03262 0.15614  -0.01039 166 ILE A O   
1164 C CB  . ILE A 166 ? 0.46888 0.43923 1.09910 -0.05669 0.17292  -0.07741 166 ILE A CB  
1165 C CG1 . ILE A 166 ? 0.45780 0.48412 1.09818 -0.04845 0.13504  -0.09573 166 ILE A CG1 
1166 C CG2 . ILE A 166 ? 0.49023 0.44989 1.14126 -0.07270 0.19908  -0.09907 166 ILE A CG2 
1167 C CD1 . ILE A 166 ? 0.46405 0.52157 1.12769 -0.05138 0.13415  -0.11332 166 ILE A CD1 
1168 N N   . SER A 167 ? 0.40234 0.37533 0.95454 -0.01772 0.10963  -0.03808 167 SER A N   
1169 C CA  . SER A 167 ? 0.40079 0.37869 0.89760 -0.00573 0.09215  -0.02038 167 SER A CA  
1170 C C   . SER A 167 ? 0.40739 0.40942 0.90469 0.00456  0.06813  -0.03078 167 SER A C   
1171 O O   . SER A 167 ? 0.35775 0.37913 0.89612 -0.00111 0.06501  -0.05644 167 SER A O   
1172 C CB  . SER A 167 ? 0.39711 0.40186 0.88156 -0.01117 0.08679  -0.02656 167 SER A CB  
1173 O OG  . SER A 167 ? 0.49759 0.53751 0.98660 -0.01333 0.06161  -0.04481 167 SER A OG  
1174 N N   . LEU A 168 ? 0.36481 0.37171 0.81826 0.01519  0.05395  -0.01649 168 LEU A N   
1175 C CA  . LEU A 168 ? 0.35489 0.39152 0.81918 0.02669  0.03466  -0.02973 168 LEU A CA  
1176 C C   . LEU A 168 ? 0.33959 0.40447 0.75200 0.02336  0.02056  -0.02658 168 LEU A C   
1177 O O   . LEU A 168 ? 0.34607 0.39041 0.71214 0.02530  0.02236  -0.00066 168 LEU A O   
1178 C CB  . LEU A 168 ? 0.38980 0.39368 0.87461 0.05243  0.03144  -0.01246 168 LEU A CB  
1179 C CG  . LEU A 168 ? 0.41169 0.45162 0.92380 0.07554  0.00817  -0.02503 168 LEU A CG  
1180 C CD1 . LEU A 168 ? 0.33655 0.41906 0.90508 0.06455  0.01333  -0.07286 168 LEU A CD1 
1181 C CD2 . LEU A 168 ? 0.51149 0.49856 1.03761 0.10914  -0.00011 0.00425  168 LEU A CD2 
1182 N N   . GLU A 169 ? 0.24203 0.35069 0.65499 0.01085  0.01123  -0.05612 169 GLU A N   
1183 C CA  . GLU A 169 ? 0.28050 0.41853 0.64567 0.00110  0.00215  -0.06096 169 GLU A CA  
1184 C C   . GLU A 169 ? 0.30447 0.41175 0.60897 -0.01035 0.01205  -0.04015 169 GLU A C   
1185 O O   . GLU A 169 ? 0.31896 0.43031 0.57956 -0.01281 0.01001  -0.02897 169 GLU A O   
1186 C CB  . GLU A 169 ? 0.28851 0.45497 0.66837 0.02345  -0.01534 -0.05584 169 GLU A CB  
1187 C CG  . GLU A 169 ? 0.23784 0.45061 0.68718 0.03384  -0.02332 -0.09113 169 GLU A CG  
1188 C CD  . GLU A 169 ? 0.24434 0.51065 0.68170 0.00127  -0.01892 -0.13470 169 GLU A CD  
1189 O OE1 . GLU A 169 ? 0.26794 0.57661 0.68205 -0.00561 -0.02799 -0.14368 169 GLU A OE1 
1190 O OE2 . GLU A 169 ? 0.26753 0.53110 0.70928 -0.02320 -0.00553 -0.16028 169 GLU A OE2 
1191 N N   . GLY A 170 ? 0.28498 0.36480 0.59259 -0.01722 0.02271  -0.03822 170 GLY A N   
1192 C CA  . GLY A 170 ? 0.33074 0.38249 0.59629 -0.02534 0.03476  -0.02751 170 GLY A CA  
1193 C C   . GLY A 170 ? 0.36484 0.38698 0.62298 -0.01929 0.05357  -0.00500 170 GLY A C   
1194 O O   . GLY A 170 ? 0.38307 0.38394 0.61003 -0.02766 0.06982  -0.00231 170 GLY A O   
1195 N N   . LYS A 171 ? 0.35480 0.36635 0.63657 -0.00825 0.05603  0.00944  171 LYS A N   
1196 C CA  . LYS A 171 ? 0.40547 0.37897 0.66417 -0.01231 0.07853  0.03053  171 LYS A CA  
1197 C C   . LYS A 171 ? 0.40675 0.35697 0.71610 -0.00912 0.09388  0.03280  171 LYS A C   
1198 O O   . LYS A 171 ? 0.41762 0.37392 0.76781 0.00169  0.08195  0.02788  171 LYS A O   
1199 C CB  . LYS A 171 ? 0.49795 0.46403 0.70192 -0.00980 0.06625  0.05393  171 LYS A CB  
1200 C CG  . LYS A 171 ? 0.53726 0.53069 0.68521 -0.02257 0.05752  0.04754  171 LYS A CG  
1201 C CD  . LYS A 171 ? 0.72124 0.73314 0.83308 -0.01484 0.02941  0.06511  171 LYS A CD  
1202 C CE  . LYS A 171 ? 0.80393 0.85117 0.85902 -0.03663 0.02495  0.05203  171 LYS A CE  
1203 N NZ  . LYS A 171 ? 0.84855 0.92217 0.86139 -0.03300 -0.00604 0.06996  171 LYS A NZ  
1204 N N   . PRO A 172 ? 0.40211 0.32698 0.71400 -0.02248 0.12546  0.03384  172 PRO A N   
1205 C CA  . PRO A 172 ? 0.41979 0.32057 0.77328 -0.02845 0.14705  0.03260  172 PRO A CA  
1206 C C   . PRO A 172 ? 0.54851 0.40127 0.86568 -0.02354 0.14281  0.06126  172 PRO A C   
1207 O O   . PRO A 172 ? 0.50552 0.33933 0.75597 -0.02023 0.12981  0.08670  172 PRO A O   
1208 C CB  . PRO A 172 ? 0.46987 0.35547 0.82034 -0.05007 0.18756  0.02487  172 PRO A CB  
1209 C CG  . PRO A 172 ? 0.44751 0.35762 0.78162 -0.04713 0.18252  0.01468  172 PRO A CG  
1210 C CD  . PRO A 172 ? 0.41647 0.33445 0.69761 -0.03684 0.14898  0.02913  172 PRO A CD  
1211 N N   . LEU A 173 ? 0.55103 0.38031 0.91066 -0.02363 0.15284  0.05719  173 LEU A N   
1212 C CA  . LEU A 173 ? 0.64057 0.40142 0.96467 -0.01742 0.15288  0.08763  173 LEU A CA  
1213 C C   . LEU A 173 ? 0.82784 0.52074 1.09547 -0.04848 0.19325  0.10567  173 LEU A C   
1214 O O   . LEU A 173 ? 0.78345 0.49200 1.07764 -0.07574 0.22989  0.08054  173 LEU A O   
1215 C CB  . LEU A 173 ? 0.69125 0.44105 1.07950 -0.00815 0.15318  0.07264  173 LEU A CB  
1216 C CG  . LEU A 173 ? 0.61643 0.42009 1.05816 0.01576  0.12146  0.05062  173 LEU A CG  
1217 C CD1 . LEU A 173 ? 0.64800 0.41855 1.14237 0.01658  0.13546  0.03579  173 LEU A CD1 
1218 C CD2 . LEU A 173 ? 0.58124 0.39400 0.98937 0.04470  0.08469  0.07179  173 LEU A CD2 
1219 O OXT . LEU A 173 ? 0.96819 0.58822 1.16242 -0.04848 0.19011  0.14413  173 LEU A OXT 
1220 N N   . GLN B 3   ? 0.79420 0.89241 1.43369 0.20778  0.07417  -0.05311 3   GLN B N   
1221 C CA  . GLN B 3   ? 0.69444 0.80038 1.32097 0.18835  0.12162  -0.03866 3   GLN B CA  
1222 C C   . GLN B 3   ? 0.53231 0.60013 1.10449 0.16783  0.12485  -0.03118 3   GLN B C   
1223 O O   . GLN B 3   ? 0.53532 0.61892 1.12201 0.14406  0.14972  -0.02178 3   GLN B O   
1224 C CB  . GLN B 3   ? 0.80172 0.89688 1.37716 0.20710  0.15004  -0.03413 3   GLN B CB  
1225 C CG  . GLN B 3   ? 0.69443 0.79303 1.23818 0.19056  0.19309  -0.01966 3   GLN B CG  
1226 C CD  . GLN B 3   ? 0.75475 0.90372 1.36873 0.17925  0.21812  -0.01205 3   GLN B CD  
1227 O OE1 . GLN B 3   ? 0.82188 1.00965 1.50536 0.18915  0.21018  -0.01948 3   GLN B OE1 
1228 N NE2 . GLN B 3   ? 0.78498 0.92955 1.37691 0.15930  0.24728  0.00268  3   GLN B NE2 
1229 N N   . VAL B 4   ? 0.46254 0.47564 0.95702 0.17235  0.09754  -0.03384 4   VAL B N   
1230 C CA  . VAL B 4   ? 0.41161 0.38664 0.82611 0.14695  0.09763  -0.02631 4   VAL B CA  
1231 C C   . VAL B 4   ? 0.40956 0.39785 0.85147 0.12465  0.07026  -0.02792 4   VAL B C   
1232 O O   . VAL B 4   ? 0.40649 0.39880 0.87413 0.13176  0.02900  -0.03734 4   VAL B O   
1233 C CB  . VAL B 4   ? 0.56583 0.47784 0.88053 0.15246  0.07781  -0.02732 4   VAL B CB  
1234 C CG1 . VAL B 4   ? 0.53825 0.41926 0.78375 0.12559  0.06786  -0.02216 4   VAL B CG1 
1235 C CG2 . VAL B 4   ? 0.54176 0.43628 0.81855 0.16887  0.10983  -0.02739 4   VAL B CG2 
1236 N N   . GLN B 5   ? 0.36551 0.35832 0.79679 0.10064  0.09126  -0.02008 5   GLN B N   
1237 C CA  . GLN B 5   ? 0.34804 0.34693 0.79346 0.07941  0.06503  -0.02253 5   GLN B CA  
1238 C C   . GLN B 5   ? 0.37213 0.33637 0.72848 0.05983  0.07199  -0.01486 5   GLN B C   
1239 O O   . GLN B 5   ? 0.37470 0.33015 0.69238 0.05771  0.10977  -0.00710 5   GLN B O   
1240 C CB  . GLN B 5   ? 0.32599 0.37617 0.87678 0.06821  0.08165  -0.02327 5   GLN B CB  
1241 C CG  . GLN B 5   ? 0.33080 0.42351 0.98185 0.08341  0.06309  -0.03635 5   GLN B CG  
1242 C CD  . GLN B 5   ? 0.37348 0.51366 1.13238 0.06559  0.06755  -0.04138 5   GLN B CD  
1243 O OE1 . GLN B 5   ? 0.37097 0.54104 1.18661 0.06279  0.09687  -0.03789 5   GLN B OE1 
1244 N NE2 . GLN B 5   ? 0.34435 0.47706 1.09937 0.04820  0.03495  -0.04844 5   GLN B NE2 
1245 N N   . LEU B 6   ? 0.34268 0.29026 0.66674 0.04871  0.03441  -0.01861 6   LEU B N   
1246 C CA  . LEU B 6   ? 0.33483 0.25550 0.57957 0.02993  0.03462  -0.01359 6   LEU B CA  
1247 C C   . LEU B 6   ? 0.38628 0.32496 0.66793 0.01610  0.00820  -0.01879 6   LEU B C   
1248 O O   . LEU B 6   ? 0.43269 0.36741 0.71575 0.02210  -0.03511 -0.02690 6   LEU B O   
1249 C CB  . LEU B 6   ? 0.36477 0.24031 0.51847 0.03343  0.01257  -0.01305 6   LEU B CB  
1250 C CG  . LEU B 6   ? 0.43614 0.28874 0.55468 0.04657  0.03473  -0.01116 6   LEU B CG  
1251 C CD1 . LEU B 6   ? 0.52643 0.33287 0.57387 0.05021  0.00829  -0.01056 6   LEU B CD1 
1252 C CD2 . LEU B 6   ? 0.49986 0.35063 0.58102 0.03796  0.07498  -0.00774 6   LEU B CD2 
1253 N N   . VAL B 7   ? 0.29608 0.25239 0.60693 0.00054  0.03283  -0.01488 7   VAL B N   
1254 C CA  . VAL B 7   ? 0.30591 0.28166 0.67034 -0.01202 0.00879  -0.02246 7   VAL B CA  
1255 C C   . VAL B 7   ? 0.34718 0.30050 0.63855 -0.02819 0.00830  -0.01854 7   VAL B C   
1256 O O   . VAL B 7   ? 0.33180 0.28434 0.61373 -0.03812 0.04490  -0.00978 7   VAL B O   
1257 C CB  . VAL B 7   ? 0.27460 0.28981 0.75022 -0.01765 0.03495  -0.02236 7   VAL B CB  
1258 C CG1 . VAL B 7   ? 0.26767 0.30071 0.80567 -0.03133 0.00340  -0.03492 7   VAL B CG1 
1259 C CG2 . VAL B 7   ? 0.28271 0.32555 0.82932 0.00121  0.03878  -0.02699 7   VAL B CG2 
1260 N N   . GLU B 8   ? 0.32040 0.25646 0.55974 -0.02810 -0.03336 -0.02504 8   GLU B N   
1261 C CA  . GLU B 8   ? 0.40541 0.32450 0.57650 -0.04116 -0.03906 -0.02364 8   GLU B CA  
1262 C C   . GLU B 8   ? 0.37343 0.30999 0.60167 -0.05209 -0.05435 -0.03172 8   GLU B C   
1263 O O   . GLU B 8   ? 0.33885 0.29811 0.64853 -0.04857 -0.08125 -0.04382 8   GLU B O   
1264 C CB  . GLU B 8   ? 0.42517 0.31931 0.51325 -0.03551 -0.07468 -0.02571 8   GLU B CB  
1265 C CG  . GLU B 8   ? 0.43904 0.30816 0.46782 -0.02712 -0.06398 -0.01854 8   GLU B CG  
1266 C CD  . GLU B 8   ? 0.46742 0.33533 0.53110 -0.00782 -0.08625 -0.02162 8   GLU B CD  
1267 O OE1 . GLU B 8   ? 0.45033 0.34432 0.59423 0.00057  -0.10536 -0.03076 8   GLU B OE1 
1268 O OE2 . GLU B 8   ? 0.48629 0.32619 0.49726 -0.00025 -0.08514 -0.01608 8   GLU B OE2 
1269 N N   . SER B 9   ? 0.33362 0.25890 0.51878 -0.06444 -0.03850 -0.02718 9   SER B N   
1270 C CA  . SER B 9   ? 0.37480 0.30758 0.60139 -0.07558 -0.05233 -0.03461 9   SER B CA  
1271 C C   . SER B 9   ? 0.38843 0.29889 0.52279 -0.08191 -0.04924 -0.03135 9   SER B C   
1272 O O   . SER B 9   ? 0.40338 0.29840 0.45419 -0.07914 -0.03181 -0.02394 9   SER B O   
1273 C CB  . SER B 9   ? 0.34692 0.29852 0.66289 -0.08311 -0.01566 -0.02893 9   SER B CB  
1274 O OG  . SER B 9   ? 0.39878 0.33772 0.67567 -0.08513 0.03644  -0.01227 9   SER B OG  
1275 N N   . GLY B 10  ? 0.36792 0.27144 0.59920 -0.05192 0.03879  -0.07466 10  GLY B N   
1276 C CA  . GLY B 10  ? 0.38051 0.27279 0.57392 -0.05058 0.02870  -0.08221 10  GLY B CA  
1277 C C   . GLY B 10  ? 0.47499 0.35366 0.66510 -0.04917 0.02178  -0.07246 10  GLY B C   
1278 O O   . GLY B 10  ? 0.44737 0.31857 0.61024 -0.04420 0.01565  -0.07741 10  GLY B O   
1279 N N   . GLY B 11  ? 0.41755 0.29708 0.63719 -0.05358 0.02315  -0.05749 11  GLY B N   
1280 C CA  . GLY B 11  ? 0.38743 0.26197 0.59952 -0.05643 0.01749  -0.04746 11  GLY B CA  
1281 C C   . GLY B 11  ? 0.45644 0.31129 0.62081 -0.06238 0.00781  -0.03654 11  GLY B C   
1282 O O   . GLY B 11  ? 0.46352 0.30774 0.60333 -0.06615 0.00218  -0.03147 11  GLY B O   
1283 N N   . GLY B 12  ? 0.46721 0.31710 0.61509 -0.06511 0.00583  -0.03318 12  GLY B N   
1284 C CA  . GLY B 12  ? 0.49901 0.32252 0.59438 -0.07043 -0.00121 -0.02954 12  GLY B CA  
1285 C C   . GLY B 12  ? 0.45578 0.28023 0.53407 -0.06777 0.00351  -0.03617 12  GLY B C   
1286 O O   . GLY B 12  ? 0.45455 0.30615 0.56499 -0.06556 0.00971  -0.03719 12  GLY B O   
1287 N N   . LEU B 13  ? 0.54000 0.33352 0.56559 -0.06906 0.00081  -0.04126 13  LEU B N   
1288 C CA  . LEU B 13  ? 0.53850 0.33150 0.53901 -0.06441 0.00976  -0.05262 13  LEU B CA  
1289 C C   . LEU B 13  ? 0.55149 0.33503 0.54416 -0.03533 0.01653  -0.07397 13  LEU B C   
1290 O O   . LEU B 13  ? 0.57201 0.32124 0.54092 -0.02743 0.00942  -0.07898 13  LEU B O   
1291 C CB  . LEU B 13  ? 0.59022 0.35117 0.53543 -0.08431 0.00499  -0.04897 13  LEU B CB  
1292 C CG  . LEU B 13  ? 0.63570 0.38954 0.54201 -0.07942 0.01800  -0.06741 13  LEU B CG  
1293 C CD1 . LEU B 13  ? 0.61401 0.42079 0.55102 -0.08624 0.02749  -0.06052 13  LEU B CD1 
1294 C CD2 . LEU B 13  ? 0.71902 0.43072 0.56054 -0.10386 0.01152  -0.06741 13  LEU B CD2 
1295 N N   . VAL B 14  ? 0.47197 0.28892 0.48803 -0.02184 0.02793  -0.08154 14  VAL B N   
1296 C CA  . VAL B 14  ? 0.48022 0.30067 0.50291 0.00667  0.03355  -0.09548 14  VAL B CA  
1297 C C   . VAL B 14  ? 0.51973 0.35870 0.53475 0.02038  0.05011  -0.10633 14  VAL B C   
1298 O O   . VAL B 14  ? 0.50096 0.37122 0.52338 0.00542  0.05636  -0.10023 14  VAL B O   
1299 C CB  . VAL B 14  ? 0.52413 0.38045 0.59427 0.01059  0.03037  -0.09141 14  VAL B CB  
1300 C CG1 . VAL B 14  ? 0.55365 0.41782 0.63222 0.03513  0.03144  -0.09851 14  VAL B CG1 
1301 C CG2 . VAL B 14  ? 0.60018 0.44663 0.67994 -0.00404 0.01964  -0.08403 14  VAL B CG2 
1302 N N   . GLN B 15  ? 0.53735 0.35957 0.54096 0.04813  0.05685  -0.12009 15  GLN B N   
1303 C CA  . GLN B 15  ? 0.52335 0.36970 0.52614 0.06794  0.07737  -0.13265 15  GLN B CA  
1304 C C   . GLN B 15  ? 0.50242 0.41737 0.55947 0.07392  0.08154  -0.12231 15  GLN B C   
1305 O O   . GLN B 15  ? 0.46098 0.38833 0.54942 0.07795  0.07017  -0.11368 15  GLN B O   
1306 C CB  . GLN B 15  ? 0.56271 0.37135 0.54963 0.10157  0.08424  -0.14886 15  GLN B CB  
1307 C CG  . GLN B 15  ? 0.65881 0.48762 0.64193 0.12637  0.11077  -0.16645 15  GLN B CG  
1308 C CD  . GLN B 15  ? 0.80916 0.63193 0.74555 0.10554  0.12435  -0.17900 15  GLN B CD  
1309 O OE1 . GLN B 15  ? 0.82920 0.59522 0.71386 0.08590  0.11691  -0.18592 15  GLN B OE1 
1310 N NE2 . GLN B 15  ? 0.73683 0.62308 0.68964 0.10505  0.14262  -0.17905 15  GLN B NE2 
1311 N N   . ALA B 16  ? 0.46522 0.42480 0.52877 0.07075  0.09655  -0.12246 16  ALA B N   
1312 C CA  . ALA B 16  ? 0.43169 0.45877 0.54548 0.07474  0.09929  -0.11020 16  ALA B CA  
1313 C C   . ALA B 16  ? 0.42682 0.46293 0.56649 0.10668  0.10006  -0.11152 16  ALA B C   
1314 O O   . ALA B 16  ? 0.46746 0.47557 0.59047 0.13533  0.11065  -0.12540 16  ALA B O   
1315 C CB  . ALA B 16  ? 0.43651 0.51550 0.54997 0.07140  0.11846  -0.11047 16  ALA B CB  
1316 N N   . GLY B 17  ? 0.38617 0.46030 0.56759 0.10005  0.08765  -0.09583 17  GLY B N   
1317 C CA  . GLY B 17  ? 0.38433 0.47402 0.59398 0.12150  0.08196  -0.08931 17  GLY B CA  
1318 C C   . GLY B 17  ? 0.37921 0.42399 0.57813 0.11573  0.06250  -0.08839 17  GLY B C   
1319 O O   . GLY B 17  ? 0.37312 0.43678 0.59656 0.12346  0.05213  -0.07766 17  GLY B O   
1320 N N   . GLY B 18  ? 0.38352 0.37591 0.54706 0.09989  0.05665  -0.09630 18  GLY B N   
1321 C CA  . GLY B 18  ? 0.40811 0.36312 0.55850 0.09157  0.03976  -0.09472 18  GLY B CA  
1322 C C   . GLY B 18  ? 0.38922 0.36579 0.55900 0.06625  0.02796  -0.08832 18  GLY B C   
1323 O O   . GLY B 18  ? 0.33689 0.35211 0.53246 0.05390  0.02984  -0.08415 18  GLY B O   
1324 N N   . SER B 19  ? 0.36937 0.31818 0.52419 0.05727  0.01567  -0.08846 19  SER B N   
1325 C CA  . SER B 19  ? 0.36178 0.32497 0.52777 0.03545  0.00693  -0.08812 19  SER B CA  
1326 C C   . SER B 19  ? 0.36716 0.29584 0.51238 0.02054  0.00523  -0.09308 19  SER B C   
1327 O O   . SER B 19  ? 0.41693 0.30985 0.53479 0.02551  0.00345  -0.09203 19  SER B O   
1328 C CB  . SER B 19  ? 0.35160 0.32997 0.52152 0.03651  -0.00610 -0.08086 19  SER B CB  
1329 O OG  . SER B 19  ? 0.33914 0.35608 0.53539 0.05106  -0.00623 -0.07039 19  SER B OG  
1330 N N   . LEU B 20  ? 0.41711 0.27421 0.56381 0.03468  -0.02936 -0.06162 20  LEU B N   
1331 C CA  . LEU B 20  ? 0.42165 0.27484 0.61739 0.00590  -0.01484 -0.07745 20  LEU B CA  
1332 C C   . LEU B 20  ? 0.41648 0.26906 0.58531 0.01609  -0.01960 -0.04690 20  LEU B C   
1333 O O   . LEU B 20  ? 0.38952 0.27470 0.51827 0.03157  -0.04913 -0.02803 20  LEU B O   
1334 C CB  . LEU B 20  ? 0.45485 0.38473 0.70093 -0.02167 -0.04801 -0.11415 20  LEU B CB  
1335 C CG  . LEU B 20  ? 0.50763 0.46545 0.81798 -0.05332 -0.03476 -0.14965 20  LEU B CG  
1336 C CD1 . LEU B 20  ? 0.45608 0.37560 0.78707 -0.06824 0.01275  -0.17165 20  LEU B CD1 
1337 C CD2 . LEU B 20  ? 0.45009 0.49940 0.75562 -0.05109 -0.06938 -0.15625 20  LEU B CD2 
1338 N N   . ARG B 21  ? 0.37467 0.19285 0.56633 0.00475  0.01191  -0.04570 21  ARG B N   
1339 C CA  . ARG B 21  ? 0.38658 0.21182 0.56012 0.01109  0.00648  -0.02330 21  ARG B CA  
1340 C C   . ARG B 21  ? 0.32475 0.18488 0.55402 -0.01658 0.00003  -0.04749 21  ARG B C   
1341 O O   . ARG B 21  ? 0.39186 0.23754 0.66818 -0.03867 0.02936  -0.07147 21  ARG B O   
1342 C CB  . ARG B 21  ? 0.44253 0.20318 0.58300 0.03161  0.05021  0.00677  21  ARG B CB  
1343 C CG  . ARG B 21  ? 0.46302 0.23820 0.58011 0.04031  0.04429  0.02773  21  ARG B CG  
1344 C CD  . ARG B 21  ? 0.61117 0.33119 0.70817 0.05458  0.09224  0.05195  21  ARG B CD  
1345 N NE  . ARG B 21  ? 0.73241 0.44181 0.87812 0.02288  0.11810  0.02973  21  ARG B NE  
1346 C CZ  . ARG B 21  ? 0.75437 0.44919 0.90122 0.01944  0.14805  0.03878  21  ARG B CZ  
1347 N NH1 . ARG B 21  ? 0.79668 0.48631 0.89978 0.04475  0.15500  0.06881  21  ARG B NH1 
1348 N NH2 . ARG B 21  ? 0.85618 0.54885 1.05055 -0.00956 0.17332  0.01457  21  ARG B NH2 
1349 N N   . LEU B 22  ? 0.33000 0.23786 0.55419 -0.01503 -0.03514 -0.04346 22  LEU B N   
1350 C CA  . LEU B 22  ? 0.30290 0.24755 0.57082 -0.02943 -0.04153 -0.05938 22  LEU B CA  
1351 C C   . LEU B 22  ? 0.32405 0.24003 0.57786 -0.02309 -0.02236 -0.03972 22  LEU B C   
1352 O O   . LEU B 22  ? 0.33095 0.22139 0.53463 -0.00585 -0.02055 -0.01350 22  LEU B O   
1353 C CB  . LEU B 22  ? 0.28679 0.28873 0.55149 -0.02447 -0.08409 -0.06079 22  LEU B CB  
1354 C CG  . LEU B 22  ? 0.31811 0.35452 0.57852 -0.02466 -0.10470 -0.07335 22  LEU B CG  
1355 C CD1 . LEU B 22  ? 0.32787 0.39672 0.54278 -0.01282 -0.11759 -0.05868 22  LEU B CD1 
1356 C CD2 . LEU B 22  ? 0.26752 0.32195 0.56605 -0.03939 -0.08484 -0.10454 22  LEU B CD2 
1357 N N   . SER B 23  ? 0.31978 0.25354 0.61916 -0.03666 -0.00989 -0.05611 23  SER B N   
1358 C CA  . SER B 23  ? 0.31050 0.22760 0.60460 -0.03212 0.00710  -0.04249 23  SER B CA  
1359 C C   . SER B 23  ? 0.28813 0.25907 0.61432 -0.03247 -0.01296 -0.05553 23  SER B C   
1360 O O   . SER B 23  ? 0.31252 0.33731 0.68341 -0.04181 -0.02463 -0.08207 23  SER B O   
1361 C CB  . SER B 23  ? 0.35405 0.23421 0.67396 -0.04688 0.05480  -0.04883 23  SER B CB  
1362 O OG  . SER B 23  ? 0.44306 0.26638 0.73111 -0.04028 0.08009  -0.03343 23  SER B OG  
1363 N N   . CYS B 24  ? 0.24862 0.20911 0.55224 -0.01974 -0.01365 -0.03848 24  CYS B N   
1364 C CA  . CYS B 24  ? 0.24660 0.24655 0.57755 -0.01336 -0.02303 -0.04684 24  CYS B CA  
1365 C C   . CYS B 24  ? 0.30483 0.28339 0.64095 -0.01471 0.00667  -0.04250 24  CYS B C   
1366 O O   . CYS B 24  ? 0.32894 0.27003 0.62249 -0.00547 0.01425  -0.02217 24  CYS B O   
1367 C CB  . CYS B 24  ? 0.27013 0.27130 0.56563 0.00542  -0.05001 -0.03113 24  CYS B CB  
1368 S SG  . CYS B 24  ? 0.32946 0.36882 0.65221 0.02452  -0.05526 -0.03566 24  CYS B SG  
1369 N N   . ALA B 25  ? 0.26569 0.27804 0.65460 -0.02704 0.02353  -0.06494 25  ALA B N   
1370 C CA  . ALA B 25  ? 0.27285 0.27448 0.67239 -0.02962 0.05263  -0.06356 25  ALA B CA  
1371 C C   . ALA B 25  ? 0.31316 0.35426 0.72295 -0.00963 0.03595  -0.06597 25  ALA B C   
1372 O O   . ALA B 25  ? 0.27537 0.38115 0.72533 -0.00513 0.02084  -0.08623 25  ALA B O   
1373 C CB  . ALA B 25  ? 0.29090 0.30938 0.74424 -0.05803 0.08565  -0.09044 25  ALA B CB  
1374 N N   . ALA B 26  ? 0.27168 0.27860 0.64437 0.00516  0.04027  -0.04687 26  ALA B N   
1375 C CA  . ALA B 26  ? 0.29013 0.31498 0.66246 0.02824  0.02930  -0.04573 26  ALA B CA  
1376 C C   . ALA B 26  ? 0.31980 0.35828 0.71643 0.02825  0.05494  -0.05377 26  ALA B C   
1377 O O   . ALA B 26  ? 0.31749 0.32988 0.70800 0.01326  0.08214  -0.04969 26  ALA B O   
1378 C CB  . ALA B 26  ? 0.33925 0.31481 0.65367 0.04118  0.01957  -0.02588 26  ALA B CB  
1379 N N   . SER B 27  ? 0.28729 0.36795 0.70797 0.04960  0.04776  -0.06271 27  SER B N   
1380 C CA  . SER B 27  ? 0.30229 0.39937 0.74224 0.05496  0.06949  -0.07034 27  SER B CA  
1381 C C   . SER B 27  ? 0.33006 0.42900 0.75655 0.09181  0.05833  -0.06426 27  SER B C   
1382 O O   . SER B 27  ? 0.34049 0.44582 0.75713 0.11405  0.03597  -0.05722 27  SER B O   
1383 C CB  . SER B 27  ? 0.38331 0.55339 0.88839 0.03853  0.08357  -0.09903 27  SER B CB  
1384 O OG  . SER B 27  ? 0.38985 0.63559 0.92863 0.05734  0.06007  -0.11507 27  SER B OG  
1385 N N   . GLY B 28  ? 0.33669 0.42575 0.76013 0.10012  0.07787  -0.06564 28  GLY B N   
1386 C CA  . GLY B 28  ? 0.36400 0.44423 0.77439 0.13643  0.07608  -0.06154 28  GLY B CA  
1387 C C   . GLY B 28  ? 0.38951 0.38891 0.74216 0.13988  0.07995  -0.04752 28  GLY B C   
1388 O O   . GLY B 28  ? 0.43877 0.41425 0.77741 0.16686  0.08739  -0.04629 28  GLY B O   
1389 N N   . PHE B 29  ? 0.39122 0.35162 0.71080 0.11380  0.07795  -0.04012 29  PHE B N   
1390 C CA  . PHE B 29  ? 0.46062 0.36018 0.72786 0.10952  0.08193  -0.03504 29  PHE B CA  
1391 C C   . PHE B 29  ? 0.40274 0.29382 0.64540 0.08145  0.08294  -0.03090 29  PHE B C   
1392 O O   . PHE B 29  ? 0.40379 0.31694 0.66414 0.06947  0.07655  -0.02640 29  PHE B O   
1393 C CB  . PHE B 29  ? 0.45600 0.32163 0.70003 0.12355  0.06697  -0.02562 29  PHE B CB  
1394 C CG  . PHE B 29  ? 0.42986 0.30599 0.67039 0.10976  0.04454  -0.01694 29  PHE B CG  
1395 C CD1 . PHE B 29  ? 0.39944 0.32916 0.67882 0.11775  0.02835  -0.01665 29  PHE B CD1 
1396 C CD2 . PHE B 29  ? 0.42487 0.26901 0.62586 0.08759  0.04041  -0.01396 29  PHE B CD2 
1397 C CE1 . PHE B 29  ? 0.33950 0.28141 0.61717 0.10388  0.00903  -0.01252 29  PHE B CE1 
1398 C CE2 . PHE B 29  ? 0.43616 0.29223 0.63386 0.07680  0.02056  -0.00706 29  PHE B CE2 
1399 C CZ  . PHE B 29  ? 0.40878 0.30951 0.64446 0.08465  0.00522  -0.00586 29  PHE B CZ  
1400 N N   . PRO B 30  ? 0.47232 0.33534 0.67284 0.07244  0.09268  -0.03432 30  PRO B N   
1401 C CA  . PRO B 30  ? 0.43285 0.30065 0.60499 0.05530  0.09287  -0.02813 30  PRO B CA  
1402 C C   . PRO B 30  ? 0.41960 0.27150 0.56379 0.04649  0.07297  -0.02412 30  PRO B C   
1403 O O   . PRO B 30  ? 0.45260 0.27793 0.57380 0.04417  0.07080  -0.03267 30  PRO B O   
1404 C CB  . PRO B 30  ? 0.48391 0.35322 0.62693 0.05301  0.11293  -0.03925 30  PRO B CB  
1405 C CG  . PRO B 30  ? 0.51109 0.36569 0.66972 0.06556  0.12413  -0.05378 30  PRO B CG  
1406 C CD  . PRO B 30  ? 0.54642 0.38242 0.72574 0.07839  0.10845  -0.04793 30  PRO B CD  
1407 N N   . VAL B 31  ? 0.40500 0.26967 0.55087 0.04021  0.06222  -0.01263 31  VAL B N   
1408 C CA  . VAL B 31  ? 0.41486 0.27164 0.53702 0.03280  0.04188  -0.00951 31  VAL B CA  
1409 C C   . VAL B 31  ? 0.40809 0.26346 0.48287 0.02285  0.04570  -0.01901 31  VAL B C   
1410 O O   . VAL B 31  ? 0.44272 0.28812 0.49646 0.01311  0.03381  -0.02418 31  VAL B O   
1411 C CB  . VAL B 31  ? 0.43037 0.30118 0.56243 0.02945  0.03218  0.00193  31  VAL B CB  
1412 C CG1 . VAL B 31  ? 0.41341 0.29826 0.59759 0.03243  0.02726  0.00047  31  VAL B CG1 
1413 C CG2 . VAL B 31  ? 0.39260 0.27087 0.50685 0.03068  0.05052  0.01151  31  VAL B CG2 
1414 N N   . ASN B 32  ? 0.44473 0.31849 0.50214 0.02404  0.06374  -0.02428 32  ASN B N   
1415 C CA  . ASN B 32  ? 0.44607 0.34020 0.46064 0.01353  0.06658  -0.04078 32  ASN B CA  
1416 C C   . ASN B 32  ? 0.51934 0.38934 0.52787 0.00128  0.07751  -0.06731 32  ASN B C   
1417 O O   . ASN B 32  ? 0.54537 0.43575 0.52294 -0.01514 0.08369  -0.09157 32  ASN B O   
1418 C CB  . ASN B 32  ? 0.48012 0.41778 0.47170 0.02381  0.08169  -0.03699 32  ASN B CB  
1419 C CG  . ASN B 32  ? 0.54665 0.48228 0.55799 0.03310  0.10298  -0.03660 32  ASN B CG  
1420 O OD1 . ASN B 32  ? 0.60306 0.51564 0.65226 0.03848  0.10568  -0.02501 32  ASN B OD1 
1421 N ND2 . ASN B 32  ? 0.56545 0.53636 0.55230 0.03476  0.11873  -0.05204 32  ASN B ND2 
1422 N N   . HIS B 33  ? 0.46686 0.29683 0.50372 0.00959  0.08294  -0.06575 33  HIS B N   
1423 C CA  . HIS B 33  ? 0.53762 0.32570 0.56708 0.00263  0.09941  -0.08736 33  HIS B CA  
1424 C C   . HIS B 33  ? 0.51658 0.25436 0.54636 0.00287  0.09227  -0.07914 33  HIS B C   
1425 O O   . HIS B 33  ? 0.56601 0.25118 0.58658 0.00038  0.11197  -0.09190 33  HIS B O   
1426 C CB  . HIS B 33  ? 0.57433 0.35144 0.62807 0.02031  0.11730  -0.09080 33  HIS B CB  
1427 C CG  . HIS B 33  ? 0.62170 0.44219 0.66684 0.01766  0.13212  -0.10462 33  HIS B CG  
1428 N ND1 . HIS B 33  ? 0.66453 0.48385 0.72558 0.02928  0.15141  -0.11456 33  HIS B ND1 
1429 C CD2 . HIS B 33  ? 0.60851 0.48149 0.62765 0.00921  0.13123  -0.10884 33  HIS B CD2 
1430 C CE1 . HIS B 33  ? 0.71050 0.57909 0.75607 0.02561  0.16188  -0.12433 33  HIS B CE1 
1431 N NE2 . HIS B 33  ? 0.68756 0.59064 0.70608 0.01584  0.15021  -0.11973 33  HIS B NE2 
1432 N N   . ARG B 34  ? 0.52425 0.27409 0.56192 0.00719  0.06828  -0.05785 34  ARG B N   
1433 C CA  . ARG B 34  ? 0.51205 0.22573 0.54610 0.01018  0.05970  -0.04615 34  ARG B CA  
1434 C C   . ARG B 34  ? 0.48466 0.21988 0.49643 -0.01038 0.04246  -0.04604 34  ARG B C   
1435 O O   . ARG B 34  ? 0.48405 0.26663 0.49113 -0.01656 0.03168  -0.04705 34  ARG B O   
1436 C CB  . ARG B 34  ? 0.48848 0.21082 0.55885 0.04008  0.04487  -0.02252 34  ARG B CB  
1437 C CG  . ARG B 34  ? 0.52089 0.23762 0.61731 0.06481  0.06017  -0.02334 34  ARG B CG  
1438 C CD  . ARG B 34  ? 0.63005 0.28092 0.70810 0.07660  0.08591  -0.02823 34  ARG B CD  
1439 N NE  . ARG B 34  ? 0.71806 0.37659 0.82332 0.10647  0.09659  -0.02729 34  ARG B NE  
1440 C CZ  . ARG B 34  ? 0.71676 0.38427 0.82928 0.10232  0.11365  -0.04525 34  ARG B CZ  
1441 N NH1 . ARG B 34  ? 0.70683 0.37975 0.79769 0.07145  0.12262  -0.06598 34  ARG B NH1 
1442 N NH2 . ARG B 34  ? 0.78231 0.46588 0.92238 0.13121  0.12080  -0.04348 34  ARG B NH2 
1443 N N   . THR B 35  ? 0.52099 0.22005 0.51694 -0.01717 0.04239  -0.04226 35  THR B N   
1444 C CA  . THR B 35  ? 0.51432 0.23582 0.49276 -0.03397 0.02424  -0.04000 35  THR B CA  
1445 C C   . THR B 35  ? 0.49024 0.23304 0.49403 -0.01179 -0.00226 -0.01395 35  THR B C   
1446 O O   . THR B 35  ? 0.52367 0.24051 0.53704 0.00768  -0.00335 0.00248  35  THR B O   
1447 C CB  . THR B 35  ? 0.55728 0.22863 0.50667 -0.05507 0.04196  -0.04933 35  THR B CB  
1448 O OG1 . THR B 35  ? 0.60964 0.26332 0.54131 -0.08012 0.07157  -0.08245 35  THR B OG1 
1449 C CG2 . THR B 35  ? 0.57202 0.27504 0.50353 -0.07452 0.02325  -0.04913 35  THR B CG2 
1450 N N   . MET B 36  ? 0.38139 0.23847 0.52573 0.04555  0.02438  -0.05791 36  MET B N   
1451 C CA  . MET B 36  ? 0.40581 0.26675 0.55953 0.04174  0.02334  -0.03410 36  MET B CA  
1452 C C   . MET B 36  ? 0.40591 0.26150 0.57102 0.03839  0.00793  -0.02907 36  MET B C   
1453 O O   . MET B 36  ? 0.38162 0.23205 0.53848 0.03717  -0.00491 -0.04099 36  MET B O   
1454 C CB  . MET B 36  ? 0.37439 0.23583 0.49427 0.03609  0.02737  -0.02154 36  MET B CB  
1455 C CG  . MET B 36  ? 0.38493 0.25288 0.48721 0.03291  0.05326  -0.03010 36  MET B CG  
1456 S SD  . MET B 36  ? 0.38868 0.27970 0.55822 0.03661  0.07302  -0.04144 36  MET B SD  
1457 C CE  . MET B 36  ? 0.35414 0.25342 0.55709 0.03508  0.06460  -0.02058 36  MET B CE  
1458 N N   . ALA B 37  ? 0.35570 0.21440 0.54092 0.03703  0.00841  -0.01601 37  ALA B N   
1459 C CA  . ALA B 37  ? 0.33452 0.19447 0.52155 0.02882  0.00163  -0.01475 37  ALA B CA  
1460 C C   . ALA B 37  ? 0.37274 0.24489 0.56621 0.02726  -0.00328 -0.00180 37  ALA B C   
1461 O O   . ALA B 37  ? 0.36637 0.24484 0.56851 0.03403  -0.00223 0.00734  37  ALA B O   
1462 C CB  . ALA B 37  ? 0.36632 0.21443 0.55529 0.02493  0.00949  -0.01480 37  ALA B CB  
1463 N N   . TRP B 38  ? 0.33577 0.21547 0.53501 0.01894  -0.00985 -0.00811 38  TRP B N   
1464 C CA  . TRP B 38  ? 0.35159 0.24829 0.55998 0.01595  -0.01488 -0.00388 38  TRP B CA  
1465 C C   . TRP B 38  ? 0.34644 0.23763 0.54070 0.00702  -0.00780 -0.00428 38  TRP B C   
1466 O O   . TRP B 38  ? 0.34124 0.22352 0.53641 -0.00407 0.00182  -0.01702 38  TRP B O   
1467 C CB  . TRP B 38  ? 0.31150 0.22319 0.54070 0.01114  -0.02593 -0.01518 38  TRP B CB  
1468 C CG  . TRP B 38  ? 0.33474 0.24439 0.56608 0.01633  -0.03107 -0.00573 38  TRP B CG  
1469 C CD1 . TRP B 38  ? 0.35854 0.24918 0.57125 0.01896  -0.03653 -0.00388 38  TRP B CD1 
1470 C CD2 . TRP B 38  ? 0.32066 0.24202 0.57250 0.01758  -0.03014 0.00235  38  TRP B CD2 
1471 N NE1 . TRP B 38  ? 0.32771 0.20979 0.53826 0.01918  -0.03494 0.01107  38  TRP B NE1 
1472 C CE2 . TRP B 38  ? 0.31759 0.22092 0.55939 0.01707  -0.02829 0.01321  38  TRP B CE2 
1473 C CE3 . TRP B 38  ? 0.28935 0.23445 0.56621 0.01888  -0.03120 -0.00053 38  TRP B CE3 
1474 C CZ2 . TRP B 38  ? 0.33032 0.23697 0.59305 0.01366  -0.02012 0.02209  38  TRP B CZ2 
1475 C CZ3 . TRP B 38  ? 0.28238 0.23816 0.59039 0.01913  -0.02859 0.00174  38  TRP B CZ3 
1476 C CH2 . TRP B 38  ? 0.32060 0.25646 0.62528 0.01460  -0.01941 0.01343  38  TRP B CH2 
1477 N N   . TYR B 39  ? 0.34999 0.24434 0.52948 0.01126  -0.01220 0.00829  39  TYR B N   
1478 C CA  . TYR B 39  ? 0.33703 0.22428 0.48425 0.00014  -0.00594 0.01127  39  TYR B CA  
1479 C C   . TYR B 39  ? 0.35749 0.27459 0.50346 0.00267  -0.01941 0.00636  39  TYR B C   
1480 O O   . TYR B 39  ? 0.32520 0.26341 0.50228 0.01480  -0.03330 0.00361  39  TYR B O   
1481 C CB  . TYR B 39  ? 0.41625 0.26300 0.52679 0.00385  -0.00233 0.03507  39  TYR B CB  
1482 C CG  . TYR B 39  ? 0.44395 0.28227 0.55094 0.02604  -0.02393 0.05301  39  TYR B CG  
1483 C CD1 . TYR B 39  ? 0.45078 0.30084 0.53606 0.03473  -0.04438 0.05860  39  TYR B CD1 
1484 C CD2 . TYR B 39  ? 0.46663 0.28600 0.59630 0.03915  -0.02596 0.05867  39  TYR B CD2 
1485 C CE1 . TYR B 39  ? 0.46088 0.30365 0.55425 0.05854  -0.07075 0.06890  39  TYR B CE1 
1486 C CE2 . TYR B 39  ? 0.52991 0.34275 0.67186 0.06070  -0.04770 0.06788  39  TYR B CE2 
1487 C CZ  . TYR B 39  ? 0.51075 0.33516 0.63742 0.07127  -0.07192 0.07271  39  TYR B CZ  
1488 O OH  . TYR B 39  ? 0.54161 0.36179 0.69316 0.09581  -0.09949 0.07509  39  TYR B OH  
1489 N N   . ARG B 40  ? 0.36687 0.28724 0.47877 -0.01132 -0.01183 0.00113  40  ARG B N   
1490 C CA  . ARG B 40  ? 0.36932 0.32371 0.47861 -0.00989 -0.02499 -0.01172 40  ARG B CA  
1491 C C   . ARG B 40  ? 0.43504 0.36863 0.46722 -0.01284 -0.02614 0.00476  40  ARG B C   
1492 O O   . ARG B 40  ? 0.46547 0.35906 0.44804 -0.02641 -0.00617 0.02194  40  ARG B O   
1493 C CB  . ARG B 40  ? 0.30653 0.29780 0.45570 -0.02671 -0.01562 -0.04726 40  ARG B CB  
1494 C CG  . ARG B 40  ? 0.35488 0.33767 0.48126 -0.05219 0.01328  -0.06105 40  ARG B CG  
1495 C CD  . ARG B 40  ? 0.34865 0.37263 0.53890 -0.06581 0.01833  -0.10565 40  ARG B CD  
1496 N NE  . ARG B 40  ? 0.38446 0.40750 0.57464 -0.09233 0.04997  -0.13022 40  ARG B NE  
1497 C CZ  . ARG B 40  ? 0.39323 0.44934 0.65168 -0.10462 0.05532  -0.17566 40  ARG B CZ  
1498 N NH1 . ARG B 40  ? 0.31393 0.39263 0.61867 -0.07963 0.02882  -0.18100 40  ARG B NH1 
1499 N NH2 . ARG B 40  ? 0.39445 0.45534 0.65659 -0.13124 0.08988  -0.20423 40  ARG B NH2 
1500 N N   . GLN B 41  ? 0.43387 0.39040 0.45412 0.00051  -0.05115 0.00041  41  GLN B N   
1501 C CA  . GLN B 41  ? 0.50316 0.43561 0.43479 0.00219  -0.06174 0.01875  41  GLN B CA  
1502 C C   . GLN B 41  ? 0.52015 0.50111 0.44181 0.00021  -0.07405 -0.01148 41  GLN B C   
1503 O O   . GLN B 41  ? 0.48779 0.51034 0.47144 0.01755  -0.09880 -0.03313 41  GLN B O   
1504 C CB  . GLN B 41  ? 0.55758 0.45641 0.47352 0.03170  -0.09550 0.04827  41  GLN B CB  
1505 C CG  . GLN B 41  ? 0.71002 0.56007 0.51540 0.03457  -0.11049 0.07963  41  GLN B CG  
1506 C CD  . GLN B 41  ? 0.71532 0.51148 0.51218 0.05975  -0.13764 0.11426  41  GLN B CD  
1507 O OE1 . GLN B 41  ? 0.90498 0.71627 0.78383 0.07991  -0.15233 0.10537  41  GLN B OE1 
1508 N NE2 . GLN B 41  ? 0.94368 0.67385 0.64387 0.05707  -0.14211 0.15295  41  GLN B NE2 
1509 N N   . ALA B 42  ? 0.58250 0.55900 0.43092 -0.02263 -0.05358 -0.01622 42  ALA B N   
1510 C CA  . ALA B 42  ? 0.62443 0.64123 0.43516 -0.02731 -0.06253 -0.04475 42  ALA B CA  
1511 C C   . ALA B 42  ? 0.77211 0.75137 0.47402 -0.00935 -0.09541 -0.01310 42  ALA B C   
1512 O O   . ALA B 42  ? 0.82128 0.73187 0.45330 -0.00834 -0.09331 0.03332  42  ALA B O   
1513 C CB  . ALA B 42  ? 0.65244 0.68389 0.43454 -0.06656 -0.01564 -0.07111 42  ALA B CB  
1514 N N   . PRO B 43  ? 0.76104 0.78110 0.45101 0.00756  -0.13099 -0.03808 43  PRO B N   
1515 C CA  . PRO B 43  ? 0.88009 0.86255 0.46251 0.03058  -0.17431 -0.00966 43  PRO B CA  
1516 C C   . PRO B 43  ? 1.01847 0.93975 0.44816 0.00368  -0.14635 0.02552  43  PRO B C   
1517 O O   . PRO B 43  ? 1.03892 0.98086 0.43502 -0.03358 -0.09909 0.00233  43  PRO B O   
1518 C CB  . PRO B 43  ? 0.87490 0.92870 0.48257 0.04667  -0.20986 -0.05982 43  PRO B CB  
1519 C CG  . PRO B 43  ? 0.72827 0.84261 0.49475 0.04653  -0.19866 -0.10011 43  PRO B CG  
1520 C CD  . PRO B 43  ? 0.67894 0.77835 0.46858 0.01281  -0.14227 -0.09352 43  PRO B CD  
1521 N N   . GLY B 44  ? 1.13433 0.97626 0.47784 0.02113  -0.17323 0.08121  44  GLY B N   
1522 C CA  . GLY B 44  ? 1.28689 1.05100 0.47628 -0.00412 -0.14743 0.12716  44  GLY B CA  
1523 C C   . GLY B 44  ? 1.28290 1.00881 0.48266 -0.04394 -0.07908 0.14478  44  GLY B C   
1524 O O   . GLY B 44  ? 1.49274 1.15549 0.57049 -0.07414 -0.04378 0.17858  44  GLY B O   
1525 N N   . LYS B 45  ? 1.15695 0.91662 0.49499 -0.04608 -0.05866 0.12205  45  LYS B N   
1526 C CA  . LYS B 45  ? 1.14478 0.87861 0.50985 -0.08121 0.00156  0.12716  45  LYS B CA  
1527 C C   . LYS B 45  ? 1.03025 0.72622 0.46975 -0.06072 -0.01098 0.15386  45  LYS B C   
1528 O O   . LYS B 45  ? 0.98982 0.69757 0.48659 -0.02262 -0.05891 0.15626  45  LYS B O   
1529 C CB  . LYS B 45  ? 1.03587 0.84800 0.49747 -0.10683 0.04083  0.06574  45  LYS B CB  
1530 C CG  . LYS B 45  ? 1.07345 0.92713 0.47241 -0.13450 0.06515  0.02948  45  LYS B CG  
1531 C CD  . LYS B 45  ? 1.12157 1.03697 0.61869 -0.16598 0.11226  -0.02992 45  LYS B CD  
1532 C CE  . LYS B 45  ? 1.18540 1.13497 0.61330 -0.20256 0.15083  -0.06842 45  LYS B CE  
1533 N NZ  . LYS B 45  ? 1.18564 1.18775 0.71519 -0.23659 0.20125  -0.12905 45  LYS B NZ  
1534 N N   . GLU B 46  ? 1.07048 0.72329 0.51307 -0.08836 0.03566  0.16846  46  GLU B N   
1535 C CA  . GLU B 46  ? 1.02920 0.65211 0.54805 -0.07375 0.03102  0.18440  46  GLU B CA  
1536 C C   . GLU B 46  ? 0.89388 0.58816 0.54453 -0.06506 0.03040  0.13874  46  GLU B C   
1537 O O   . GLU B 46  ? 0.83430 0.58750 0.52354 -0.08190 0.04994  0.09650  46  GLU B O   
1538 C CB  . GLU B 46  ? 1.05161 0.61073 0.54089 -0.10814 0.08292  0.20651  46  GLU B CB  
1539 C CG  . GLU B 46  ? 1.34371 0.82258 0.68606 -0.12516 0.09319  0.25617  46  GLU B CG  
1540 C CD  . GLU B 46  ? 1.48108 0.90423 0.80445 -0.16745 0.15658  0.27094  46  GLU B CD  
1541 O OE1 . GLU B 46  ? 1.46014 0.89786 0.88826 -0.17695 0.18318  0.24567  46  GLU B OE1 
1542 O OE2 . GLU B 46  ? 1.65638 1.04794 0.89301 -0.18383 0.17313  0.29646  46  GLU B OE2 
1543 N N   . ARG B 47  ? 0.79559 0.48154 0.51362 -0.03851 0.00677  0.14696  47  ARG B N   
1544 C CA  . ARG B 47  ? 0.71188 0.45099 0.53623 -0.03194 0.00829  0.11181  47  ARG B CA  
1545 C C   . ARG B 47  ? 0.66585 0.41353 0.52429 -0.06279 0.05274  0.08703  47  ARG B C   
1546 O O   . ARG B 47  ? 0.69679 0.39775 0.52720 -0.08366 0.08339  0.10149  47  ARG B O   
1547 C CB  . ARG B 47  ? 0.74836 0.46980 0.62647 -0.00518 -0.01335 0.12395  47  ARG B CB  
1548 C CG  . ARG B 47  ? 0.81175 0.52861 0.68634 0.02820  -0.05894 0.13890  47  ARG B CG  
1549 C CD  . ARG B 47  ? 0.75269 0.45621 0.69242 0.04855  -0.06979 0.14122  47  ARG B CD  
1550 N NE  . ARG B 47  ? 0.78150 0.48813 0.73830 0.08113  -0.11390 0.14541  47  ARG B NE  
1551 C CZ  . ARG B 47  ? 0.84658 0.50114 0.75982 0.09944  -0.14592 0.17519  47  ARG B CZ  
1552 N NH1 . ARG B 47  ? 0.99416 0.57968 0.83717 0.08631  -0.13449 0.21110  47  ARG B NH1 
1553 N NH2 . ARG B 47  ? 0.98142 0.65249 0.92552 0.13096  -0.19004 0.16725  47  ARG B NH2 
1554 N N   . GLU B 48  ? 0.50211 0.34323 0.53498 -0.03325 0.03159  0.05727  48  GLU B N   
1555 C CA  . GLU B 48  ? 0.50127 0.34634 0.55459 -0.04195 0.04842  0.05175  48  GLU B CA  
1556 C C   . GLU B 48  ? 0.40860 0.27042 0.49857 -0.03183 0.04423  0.04377  48  GLU B C   
1557 O O   . GLU B 48  ? 0.39499 0.27622 0.49868 -0.02778 0.04181  0.03641  48  GLU B O   
1558 C CB  . GLU B 48  ? 0.50188 0.36172 0.55169 -0.04974 0.06577  0.04279  48  GLU B CB  
1559 C CG  . GLU B 48  ? 0.48522 0.36459 0.56216 -0.05473 0.08197  0.03857  48  GLU B CG  
1560 C CD  . GLU B 48  ? 0.50676 0.40648 0.58266 -0.05101 0.10005  0.02692  48  GLU B CD  
1561 O OE1 . GLU B 48  ? 0.53166 0.41816 0.58202 -0.04495 0.09814  0.01903  48  GLU B OE1 
1562 O OE2 . GLU B 48  ? 0.50494 0.43496 0.60403 -0.05327 0.11520  0.02477  48  GLU B OE2 
1563 N N   . TRP B 49  ? 0.43907 0.28785 0.53750 -0.03105 0.04234  0.04576  49  TRP B N   
1564 C CA  . TRP B 49  ? 0.38069 0.24366 0.50657 -0.02225 0.03917  0.03769  49  TRP B CA  
1565 C C   . TRP B 49  ? 0.37414 0.25925 0.52368 -0.03058 0.05034  0.03081  49  TRP B C   
1566 O O   . TRP B 49  ? 0.40072 0.28939 0.55239 -0.04381 0.05978  0.03280  49  TRP B O   
1567 C CB  . TRP B 49  ? 0.40004 0.23135 0.51549 -0.01805 0.03099  0.03960  49  TRP B CB  
1568 C CG  . TRP B 49  ? 0.43616 0.24336 0.52710 0.00113  0.01825  0.04519  49  TRP B CG  
1569 C CD1 . TRP B 49  ? 0.49302 0.27122 0.55138 0.00045  0.01276  0.05699  49  TRP B CD1 
1570 C CD2 . TRP B 49  ? 0.45788 0.27222 0.55317 0.02868  0.00887  0.03972  49  TRP B CD2 
1571 N NE1 . TRP B 49  ? 0.52576 0.29076 0.56979 0.02949  -0.00244 0.05949  49  TRP B NE1 
1572 C CE2 . TRP B 49  ? 0.43845 0.22978 0.50722 0.04856  -0.00343 0.04787  49  TRP B CE2 
1573 C CE3 . TRP B 49  ? 0.44412 0.28540 0.56070 0.04028  0.01039  0.02912  49  TRP B CE3 
1574 C CZ2 . TRP B 49  ? 0.49130 0.29323 0.56042 0.08456  -0.01346 0.04395  49  TRP B CZ2 
1575 C CZ3 . TRP B 49  ? 0.46258 0.31501 0.57658 0.07173  0.00343  0.02509  49  TRP B CZ3 
1576 C CH2 . TRP B 49  ? 0.47970 0.31601 0.57320 0.09585  -0.00798 0.03159  49  TRP B CH2 
1577 N N   . VAL B 50  ? 0.35181 0.25477 0.51820 -0.02303 0.04885  0.02430  50  VAL B N   
1578 C CA  . VAL B 50  ? 0.36928 0.28789 0.55228 -0.02347 0.05673  0.01865  50  VAL B CA  
1579 C C   . VAL B 50  ? 0.34391 0.27308 0.54670 -0.01890 0.05108  0.01563  50  VAL B C   
1580 O O   . VAL B 50  ? 0.32674 0.27319 0.54701 -0.01776 0.05450  0.01297  50  VAL B O   
1581 C CB  . VAL B 50  ? 0.37580 0.29023 0.54718 -0.01948 0.05935  0.01409  50  VAL B CB  
1582 C CG1 . VAL B 50  ? 0.41477 0.31971 0.56100 -0.02480 0.06597  0.01479  50  VAL B CG1 
1583 C CG2 . VAL B 50  ? 0.36148 0.27224 0.52748 -0.01997 0.04865  0.01524  50  VAL B CG2 
1584 N N   . ALA B 51  ? 0.34222 0.26756 0.54194 -0.01420 0.04256  0.01589  51  ALA B N   
1585 C CA  . ALA B 51  ? 0.32395 0.25749 0.53380 -0.01068 0.03729  0.01318  51  ALA B CA  
1586 C C   . ALA B 51  ? 0.33033 0.25960 0.53037 -0.00469 0.03147  0.01160  51  ALA B C   
1587 O O   . ALA B 51  ? 0.31189 0.24362 0.50397 0.00137  0.03145  0.01334  51  ALA B O   
1588 C CB  . ALA B 51  ? 0.32363 0.26021 0.53357 -0.00704 0.03662  0.01397  51  ALA B CB  
1589 N N   . ALA B 52  ? 0.32342 0.25021 0.52282 -0.00406 0.02585  0.00715  52  ALA B N   
1590 C CA  . ALA B 52  ? 0.30184 0.22277 0.48491 0.00699  0.02238  0.00192  52  ALA B CA  
1591 C C   . ALA B 52  ? 0.32473 0.25045 0.50297 0.00656  0.01679  -0.00248 52  ALA B C   
1592 O O   . ALA B 52  ? 0.30881 0.23707 0.49709 -0.00293 0.01102  -0.00211 52  ALA B O   
1593 C CB  . ALA B 52  ? 0.33483 0.22089 0.49865 0.01122  0.01797  -0.00259 52  ALA B CB  
1594 N N   . ILE B 53  ? 0.33353 0.26643 0.49550 0.01833  0.01835  -0.00677 53  ILE B N   
1595 C CA  . ILE B 53  ? 0.32047 0.25589 0.46696 0.01861  0.01338  -0.01113 53  ILE B CA  
1596 C C   . ILE B 53  ? 0.40189 0.32172 0.51856 0.03550  0.01364  -0.02481 53  ILE B C   
1597 O O   . ILE B 53  ? 0.37079 0.30494 0.48390 0.05336  0.02260  -0.02708 53  ILE B O   
1598 C CB  . ILE B 53  ? 0.31507 0.27696 0.46265 0.01426  0.01780  -0.00068 53  ILE B CB  
1599 C CG1 . ILE B 53  ? 0.34821 0.30923 0.47298 0.01324  0.01081  -0.00232 53  ILE B CG1 
1600 C CG2 . ILE B 53  ? 0.33125 0.32330 0.47893 0.01936  0.03004  0.00293  53  ILE B CG2 
1601 C CD1 . ILE B 53  ? 0.39074 0.36236 0.50880 0.00416  0.01114  0.01269  53  ILE B CD1 
1602 N N   . GLU B 54  ? 0.38116 0.27209 0.47453 0.03176  0.00242  -0.03533 54  GLU B N   
1603 C CA  . GLU B 54  ? 0.42532 0.28289 0.47909 0.05063  0.00098  -0.05237 54  GLU B CA  
1604 C C   . GLU B 54  ? 0.44765 0.33872 0.48344 0.07016  0.01300  -0.05724 54  GLU B C   
1605 O O   . GLU B 54  ? 0.43804 0.36783 0.48394 0.05999  0.01799  -0.04630 54  GLU B O   
1606 C CB  . GLU B 54  ? 0.53203 0.34356 0.55674 0.03558  -0.01700 -0.06397 54  GLU B CB  
1607 C CG  . GLU B 54  ? 0.60659 0.44088 0.62227 0.02670  -0.02360 -0.06414 54  GLU B CG  
1608 C CD  . GLU B 54  ? 0.64830 0.44340 0.62821 0.01138  -0.04460 -0.07805 54  GLU B CD  
1609 O OE1 . GLU B 54  ? 0.74197 0.47772 0.68410 0.01309  -0.05221 -0.09381 54  GLU B OE1 
1610 O OE2 . GLU B 54  ? 0.69427 0.51455 0.67922 -0.00261 -0.05601 -0.07272 54  GLU B OE2 
1611 N N   . SER B 55  ? 0.47476 0.34742 0.47830 0.09915  0.01766  -0.07375 55  SER B N   
1612 C CA  . SER B 55  ? 0.49827 0.40697 0.47869 0.12042  0.03162  -0.08224 55  SER B CA  
1613 C C   . SER B 55  ? 0.60267 0.48800 0.54130 0.11017  0.02263  -0.09226 55  SER B C   
1614 O O   . SER B 55  ? 0.58295 0.41418 0.50280 0.09411  0.00289  -0.09947 55  SER B O   
1615 C CB  . SER B 55  ? 0.54623 0.44329 0.50298 0.16391  0.03958  -0.09997 55  SER B CB  
1616 O OG  . SER B 55  ? 0.64039 0.44832 0.54844 0.17315  0.02353  -0.11943 55  SER B OG  
1617 N N   . HIS B 56  ? 0.56618 0.49700 0.48749 0.11724  0.03695  -0.09209 56  HIS B N   
1618 C CA  . HIS B 56  ? 0.61515 0.53407 0.48968 0.10952  0.03077  -0.09952 56  HIS B CA  
1619 C C   . HIS B 56  ? 0.69162 0.60143 0.58215 0.07397  0.01039  -0.08261 56  HIS B C   
1620 O O   . HIS B 56  ? 0.69822 0.64607 0.60281 0.05906  0.01496  -0.06199 56  HIS B O   
1621 C CB  . HIS B 56  ? 0.68173 0.53639 0.49612 0.13171  0.02235  -0.13020 56  HIS B CB  
1622 C CG  . HIS B 56  ? 0.71302 0.58006 0.50831 0.17778  0.04334  -0.14808 56  HIS B CG  
1623 N ND1 . HIS B 56  ? 0.75186 0.57925 0.55122 0.20349  0.04065  -0.15808 56  HIS B ND1 
1624 C CD2 . HIS B 56  ? 0.73493 0.66111 0.51274 0.20458  0.06865  -0.15468 56  HIS B CD2 
1625 C CE1 . HIS B 56  ? 0.76422 0.62322 0.54930 0.25024  0.06109  -0.17229 56  HIS B CE1 
1626 N NE2 . HIS B 56  ? 0.85809 0.78325 0.63233 0.25133  0.08008  -0.17146 56  HIS B NE2 
1627 N N   . GLY B 57  ? 0.71406 0.57615 0.60287 0.05999  -0.01266 -0.08954 57  GLY B N   
1628 C CA  . GLY B 57  ? 0.55906 0.42920 0.48006 0.03246  -0.03089 -0.07264 57  GLY B CA  
1629 C C   . GLY B 57  ? 0.62698 0.53026 0.60401 0.02621  -0.02212 -0.05079 57  GLY B C   
1630 O O   . GLY B 57  ? 0.63474 0.55806 0.62793 0.03747  -0.00319 -0.04665 57  GLY B O   
1631 N N   . GLN B 58  ? 0.51001 0.42174 0.51642 0.01020  -0.03644 -0.03767 58  GLN B N   
1632 C CA  . GLN B 58  ? 0.45857 0.38981 0.50956 0.00774  -0.02817 -0.02146 58  GLN B CA  
1633 C C   . GLN B 58  ? 0.51425 0.44369 0.60277 -0.00254 -0.03852 -0.02048 58  GLN B C   
1634 O O   . GLN B 58  ? 0.49206 0.43932 0.61166 -0.00397 -0.03939 -0.00785 58  GLN B O   
1635 C CB  . GLN B 58  ? 0.44648 0.39393 0.49458 0.00494  -0.02900 -0.00278 58  GLN B CB  
1636 C CG  . GLN B 58  ? 0.47169 0.43299 0.49276 0.00728  -0.01151 0.00242  58  GLN B CG  
1637 C CD  . GLN B 58  ? 0.51878 0.48166 0.53026 -0.00276 -0.01357 0.02471  58  GLN B CD  
1638 O OE1 . GLN B 58  ? 0.53691 0.48477 0.55763 -0.00360 -0.03030 0.03465  58  GLN B OE1 
1639 N NE2 . GLN B 58  ? 0.49555 0.47633 0.48461 -0.00986 0.00232  0.03337  58  GLN B NE2 
1640 N N   . GLU B 59  ? 0.49377 0.40023 0.57563 -0.01034 -0.04602 -0.03362 59  GLU B N   
1641 C CA  . GLU B 59  ? 0.45024 0.36288 0.56754 -0.02594 -0.05156 -0.03056 59  GLU B CA  
1642 C C   . GLU B 59  ? 0.43142 0.35135 0.57579 -0.01913 -0.03342 -0.02203 59  GLU B C   
1643 O O   . GLU B 59  ? 0.40295 0.30963 0.53360 -0.00642 -0.02062 -0.02406 59  GLU B O   
1644 C CB  . GLU B 59  ? 0.50849 0.38137 0.60197 -0.04248 -0.06251 -0.04437 59  GLU B CB  
1645 C CG  . GLU B 59  ? 0.54726 0.43241 0.67495 -0.06744 -0.06677 -0.03841 59  GLU B CG  
1646 C CD  . GLU B 59  ? 0.72189 0.55409 0.81669 -0.09233 -0.07921 -0.04903 59  GLU B CD  
1647 O OE1 . GLU B 59  ? 0.77939 0.56177 0.82197 -0.08790 -0.08890 -0.06445 59  GLU B OE1 
1648 O OE2 . GLU B 59  ? 0.80130 0.63748 0.91670 -0.11767 -0.07912 -0.04197 59  GLU B OE2 
1649 N N   . THR B 60  ? 0.33216 0.27909 0.51438 -0.02546 -0.03270 -0.01311 60  THR B N   
1650 C CA  . THR B 60  ? 0.29709 0.24855 0.49849 -0.02023 -0.01691 -0.00643 60  THR B CA  
1651 C C   . THR B 60  ? 0.33078 0.28588 0.55125 -0.03612 -0.01423 -0.00591 60  THR B C   
1652 O O   . THR B 60  ? 0.33784 0.30577 0.56847 -0.05468 -0.02484 -0.00775 60  THR B O   
1653 C CB  . THR B 60  ? 0.30079 0.27350 0.51947 -0.00908 -0.01378 0.00303  60  THR B CB  
1654 O OG1 . THR B 60  ? 0.30369 0.30639 0.54545 -0.00910 -0.02577 0.00521  60  THR B OG1 
1655 C CG2 . THR B 60  ? 0.35715 0.31890 0.54966 -0.00044 -0.01296 0.00738  60  THR B CG2 
1656 N N   . TRP B 61  ? 0.32169 0.26840 0.54447 -0.03235 -0.00049 -0.00205 61  TRP B N   
1657 C CA  . TRP B 61  ? 0.35324 0.30223 0.58707 -0.04746 0.00637  0.00168  61  TRP B CA  
1658 C C   . TRP B 61  ? 0.31193 0.27670 0.55875 -0.03660 0.02059  0.00681  61  TRP B C   
1659 O O   . TRP B 61  ? 0.28966 0.24184 0.52440 -0.02302 0.02417  0.00735  61  TRP B O   
1660 C CB  . TRP B 61  ? 0.35739 0.25686 0.55881 -0.05459 0.00498  0.00000  61  TRP B CB  
1661 C CG  . TRP B 61  ? 0.36961 0.26088 0.57023 -0.07194 0.01300  0.00811  61  TRP B CG  
1662 C CD1 . TRP B 61  ? 0.42348 0.31061 0.62291 -0.10325 0.00972  0.01232  61  TRP B CD1 
1663 C CD2 . TRP B 61  ? 0.35334 0.23956 0.54847 -0.06319 0.02467  0.01435  61  TRP B CD2 
1664 N NE1 . TRP B 61  ? 0.41479 0.29354 0.60609 -0.11395 0.02112  0.02231  61  TRP B NE1 
1665 C CE2 . TRP B 61  ? 0.38207 0.25958 0.56982 -0.08746 0.02967  0.02280  61  TRP B CE2 
1666 C CE3 . TRP B 61  ? 0.38181 0.27257 0.57541 -0.04163 0.03018  0.01448  61  TRP B CE3 
1667 C CZ2 . TRP B 61  ? 0.42826 0.29732 0.60249 -0.08641 0.03998  0.03079  61  TRP B CZ2 
1668 C CZ3 . TRP B 61  ? 0.40972 0.29386 0.59304 -0.04186 0.03790  0.02097  61  TRP B CZ3 
1669 C CH2 . TRP B 61  ? 0.40828 0.28047 0.58038 -0.06197 0.04288  0.02873  61  TRP B CH2 
1670 N N   . TYR B 62  ? 0.30581 0.30085 0.57487 -0.04441 0.02886  0.00983  62  TYR B N   
1671 C CA  . TYR B 62  ? 0.31063 0.31380 0.58266 -0.03288 0.04301  0.01126  62  TYR B CA  
1672 C C   . TYR B 62  ? 0.29539 0.31025 0.56916 -0.05020 0.05547  0.01549  62  TYR B C   
1673 O O   . TYR B 62  ? 0.29303 0.33753 0.58478 -0.07031 0.05548  0.01822  62  TYR B O   
1674 C CB  . TYR B 62  ? 0.29265 0.32684 0.58605 -0.01306 0.04417  0.00868  62  TYR B CB  
1675 C CG  . TYR B 62  ? 0.30583 0.32117 0.58855 0.00123  0.03200  0.00843  62  TYR B CG  
1676 C CD1 . TYR B 62  ? 0.29662 0.27741 0.55398 0.00855  0.03347  0.00940  62  TYR B CD1 
1677 C CD2 . TYR B 62  ? 0.28690 0.32115 0.58184 0.00305  0.01772  0.00880  62  TYR B CD2 
1678 C CE1 . TYR B 62  ? 0.29603 0.25984 0.53892 0.01518  0.02352  0.01253  62  TYR B CE1 
1679 C CE2 . TYR B 62  ? 0.29700 0.31101 0.57414 0.01392  0.00689  0.01124  62  TYR B CE2 
1680 C CZ  . TYR B 62  ? 0.31039 0.28894 0.56118 0.01869  0.01119  0.01394  62  TYR B CZ  
1681 O OH  . TYR B 62  ? 0.28218 0.24203 0.51171 0.02319  0.00156  0.01950  62  TYR B OH  
1682 N N   . ALA B 63  ? 0.31823 0.31260 0.57080 -0.04622 0.06523  0.01721  63  ALA B N   
1683 C CA  . ALA B 63  ? 0.36773 0.37494 0.61503 -0.06089 0.08006  0.02229  63  ALA B CA  
1684 C C   . ALA B 63  ? 0.33345 0.40013 0.61175 -0.05288 0.09434  0.01797  63  ALA B C   
1685 O O   . ALA B 63  ? 0.30945 0.38826 0.60044 -0.02668 0.09317  0.01009  63  ALA B O   
1686 C CB  . ALA B 63  ? 0.34639 0.32008 0.55953 -0.05486 0.08483  0.02392  63  ALA B CB  
1687 N N   . ASP B 64  ? 0.31642 0.42024 0.60396 -0.07461 0.10809  0.02399  64  ASP B N   
1688 C CA  . ASP B 64  ? 0.35506 0.53155 0.67541 -0.06308 0.12598  0.01919  64  ASP B CA  
1689 C C   . ASP B 64  ? 0.32961 0.49384 0.63067 -0.02847 0.13858  0.00792  64  ASP B C   
1690 O O   . ASP B 64  ? 0.34424 0.54920 0.66811 0.00168  0.14615  -0.00203 64  ASP B O   
1691 C CB  . ASP B 64  ? 0.34646 0.56759 0.67294 -0.09860 0.14279  0.02990  64  ASP B CB  
1692 C CG  . ASP B 64  ? 0.44664 0.70168 0.80276 -0.13422 0.13079  0.03834  64  ASP B CG  
1693 O OD1 . ASP B 64  ? 0.45196 0.70771 0.82881 -0.12536 0.11063  0.03336  64  ASP B OD1 
1694 O OD2 . ASP B 64  ? 0.49770 0.77659 0.85151 -0.17497 0.14045  0.05066  64  ASP B OD2 
1695 N N   . SER B 65  ? 0.37605 0.48134 0.63169 -0.03044 0.13838  0.00848  65  SER B N   
1696 C CA  . SER B 65  ? 0.41520 0.49825 0.64099 -0.00505 0.14782  -0.00336 65  SER B CA  
1697 C C   . SER B 65  ? 0.40560 0.45874 0.63040 0.02453  0.13439  -0.01386 65  SER B C   
1698 O O   . SER B 65  ? 0.42025 0.45241 0.61996 0.04873  0.14107  -0.02643 65  SER B O   
1699 C CB  . SER B 65  ? 0.42811 0.45800 0.60509 -0.01968 0.14472  0.00151  65  SER B CB  
1700 O OG  . SER B 65  ? 0.47987 0.47029 0.65224 -0.02815 0.12262  0.00832  65  SER B OG  
1701 N N   . VAL B 66  ? 0.35729 0.39930 0.59940 0.02175  0.11520  -0.00895 66  VAL B N   
1702 C CA  . VAL B 66  ? 0.37448 0.38263 0.60844 0.04328  0.10150  -0.01431 66  VAL B CA  
1703 C C   . VAL B 66  ? 0.40294 0.44502 0.67371 0.05644  0.09184  -0.01271 66  VAL B C   
1704 O O   . VAL B 66  ? 0.35663 0.36715 0.61690 0.07273  0.07831  -0.01359 66  VAL B O   
1705 C CB  . VAL B 66  ? 0.38608 0.34431 0.59441 0.02796  0.08610  -0.00885 66  VAL B CB  
1706 C CG1 . VAL B 66  ? 0.37350 0.30503 0.54698 0.01524  0.09064  -0.00926 66  VAL B CG1 
1707 C CG2 . VAL B 66  ? 0.36297 0.33428 0.59150 0.01099  0.07556  0.00036  66  VAL B CG2 
1708 N N   . LYS B 67  ? 0.44531 0.40306 0.64317 -0.05566 0.11704  -0.05257 67  LYS B N   
1709 C CA  . LYS B 67  ? 0.42751 0.44497 0.64933 -0.07892 0.11148  -0.08451 67  LYS B CA  
1710 C C   . LYS B 67  ? 0.39188 0.46669 0.61303 -0.06063 0.08012  -0.08352 67  LYS B C   
1711 O O   . LYS B 67  ? 0.39355 0.46815 0.60687 -0.04717 0.07655  -0.07191 67  LYS B O   
1712 C CB  . LYS B 67  ? 0.43075 0.45720 0.67460 -0.11544 0.15041  -0.11435 67  LYS B CB  
1713 C CG  . LYS B 67  ? 0.53640 0.51947 0.78660 -0.14033 0.18438  -0.12882 67  LYS B CG  
1714 C CD  . LYS B 67  ? 0.51644 0.50637 0.79349 -0.18595 0.23154  -0.16854 67  LYS B CD  
1715 C CE  . LYS B 67  ? 0.55165 0.46261 0.81031 -0.19186 0.27046  -0.16909 67  LYS B CE  
1716 N NZ  . LYS B 67  ? 0.68608 0.58968 0.94693 -0.21919 0.31281  -0.20553 67  LYS B NZ  
1717 N N   . GLY B 68  ? 0.36397 0.48708 0.59008 -0.05617 0.06108  -0.09425 68  GLY B N   
1718 C CA  . GLY B 68  ? 0.32046 0.49012 0.53847 -0.02960 0.03802  -0.08767 68  GLY B CA  
1719 C C   . GLY B 68  ? 0.36327 0.48788 0.55784 -0.00069 0.02169  -0.05858 68  GLY B C   
1720 O O   . GLY B 68  ? 0.34762 0.49434 0.53079 0.02413  0.01070  -0.05030 68  GLY B O   
1721 N N   . ARG B 69  ? 0.30578 0.37133 0.49259 -0.00232 0.02389  -0.04517 69  ARG B N   
1722 C CA  . ARG B 69  ? 0.34284 0.37613 0.51382 0.01697  0.01207  -0.02831 69  ARG B CA  
1723 C C   . ARG B 69  ? 0.33791 0.34479 0.50695 0.01486  0.00913  -0.02388 69  ARG B C   
1724 O O   . ARG B 69  ? 0.34204 0.33348 0.50288 0.02587  0.00296  -0.01727 69  ARG B O   
1725 C CB  . ARG B 69  ? 0.35308 0.36137 0.51624 0.02224  0.01445  -0.02026 69  ARG B CB  
1726 C CG  . ARG B 69  ? 0.37437 0.40507 0.53731 0.02688  0.01748  -0.02237 69  ARG B CG  
1727 C CD  . ARG B 69  ? 0.37247 0.38423 0.52402 0.03726  0.01839  -0.01408 69  ARG B CD  
1728 N NE  . ARG B 69  ? 0.35433 0.34476 0.50209 0.03490  0.03124  -0.00654 69  ARG B NE  
1729 C CZ  . ARG B 69  ? 0.36859 0.34766 0.50530 0.04744  0.02719  0.00057  69  ARG B CZ  
1730 N NH1 . ARG B 69  ? 0.37622 0.36208 0.51039 0.05374  0.01146  -0.00594 69  ARG B NH1 
1731 N NH2 . ARG B 69  ? 0.35497 0.31863 0.48223 0.05514  0.04366  0.01277  69  ARG B NH2 
1732 N N   . PHE B 70  ? 0.33841 0.33470 0.51446 0.00019  0.01838  -0.02823 70  PHE B N   
1733 C CA  . PHE B 70  ? 0.35960 0.33414 0.53371 -0.00027 0.01622  -0.02365 70  PHE B CA  
1734 C C   . PHE B 70  ? 0.31925 0.31311 0.50189 -0.01105 0.01877  -0.03502 70  PHE B C   
1735 O O   . PHE B 70  ? 0.30569 0.32531 0.49932 -0.02588 0.02870  -0.05177 70  PHE B O   
1736 C CB  . PHE B 70  ? 0.37427 0.31925 0.54351 0.00013  0.02758  -0.01603 70  PHE B CB  
1737 C CG  . PHE B 70  ? 0.37396 0.31454 0.53234 0.01630  0.02340  -0.00622 70  PHE B CG  
1738 C CD1 . PHE B 70  ? 0.38627 0.34004 0.54268 0.02233  0.01299  -0.00860 70  PHE B CD1 
1739 C CD2 . PHE B 70  ? 0.42207 0.35028 0.56964 0.02942  0.03309  0.00481  70  PHE B CD2 
1740 C CE1 . PHE B 70  ? 0.39384 0.35391 0.54165 0.03538  0.00953  -0.00614 70  PHE B CE1 
1741 C CE2 . PHE B 70  ? 0.39570 0.33965 0.53187 0.04917  0.02831  0.01083  70  PHE B CE2 
1742 C CZ  . PHE B 70  ? 0.35376 0.31602 0.49209 0.04903  0.01555  0.00240  70  PHE B CZ  
1743 N N   . THR B 71  ? 0.33388 0.32022 0.51317 -0.00585 0.01210  -0.02992 71  THR B N   
1744 C CA  . THR B 71  ? 0.28938 0.29500 0.47428 -0.01321 0.01401  -0.04003 71  THR B CA  
1745 C C   . THR B 71  ? 0.30142 0.27469 0.48427 -0.01478 0.01606  -0.03304 71  THR B C   
1746 O O   . THR B 71  ? 0.30466 0.26117 0.48192 -0.00528 0.00948  -0.02158 71  THR B O   
1747 C CB  . THR B 71  ? 0.28353 0.32278 0.46128 0.00409  0.00518  -0.03671 71  THR B CB  
1748 O OG1 . THR B 71  ? 0.31705 0.39715 0.49325 0.01416  0.00282  -0.04090 71  THR B OG1 
1749 C CG2 . THR B 71  ? 0.31920 0.38990 0.50144 -0.00085 0.00625  -0.04908 71  THR B CG2 
1750 N N   . ILE B 72  ? 0.28009 0.24865 0.46866 -0.02795 0.02789  -0.04361 72  ILE B N   
1751 C CA  . ILE B 72  ? 0.29662 0.24079 0.48198 -0.02602 0.03103  -0.03720 72  ILE B CA  
1752 C C   . ILE B 72  ? 0.30449 0.27484 0.49301 -0.02859 0.02631  -0.04631 72  ILE B C   
1753 O O   . ILE B 72  ? 0.32326 0.33276 0.51849 -0.03703 0.02799  -0.06503 72  ILE B O   
1754 C CB  . ILE B 72  ? 0.33987 0.24841 0.52293 -0.03224 0.05481  -0.03824 72  ILE B CB  
1755 C CG1 . ILE B 72  ? 0.30829 0.19575 0.48371 -0.02088 0.05734  -0.02668 72  ILE B CG1 
1756 C CG2 . ILE B 72  ? 0.32211 0.23547 0.51642 -0.05713 0.07686  -0.06450 72  ILE B CG2 
1757 C CD1 . ILE B 72  ? 0.36129 0.20301 0.52499 -0.01484 0.08889  -0.01947 72  ILE B CD1 
1758 N N   . SER B 73  ? 0.31217 0.27103 0.49638 -0.02039 0.02106  -0.03547 73  SER B N   
1759 C CA  . SER B 73  ? 0.30296 0.28411 0.48656 -0.01833 0.01834  -0.03985 73  SER B CA  
1760 C C   . SER B 73  ? 0.31677 0.27410 0.49888 -0.01586 0.02028  -0.03108 73  SER B C   
1761 O O   . SER B 73  ? 0.31496 0.25017 0.49644 -0.01260 0.02134  -0.02225 73  SER B O   
1762 C CB  . SER B 73  ? 0.31141 0.31553 0.48653 -0.00128 0.01036  -0.02993 73  SER B CB  
1763 O OG  . SER B 73  ? 0.31880 0.29095 0.48956 0.00575  0.01011  -0.01369 73  SER B OG  
1764 N N   . ARG B 74  ? 0.29968 0.27254 0.48054 -0.01421 0.02032  -0.03439 74  ARG B N   
1765 C CA  . ARG B 74  ? 0.31003 0.26686 0.49031 -0.01078 0.02191  -0.02594 74  ARG B CA  
1766 C C   . ARG B 74  ? 0.34071 0.31637 0.51583 -0.00194 0.01988  -0.02059 74  ARG B C   
1767 O O   . ARG B 74  ? 0.30990 0.31799 0.47923 0.00489  0.01821  -0.02563 74  ARG B O   
1768 C CB  . ARG B 74  ? 0.32436 0.26502 0.50544 -0.01708 0.03414  -0.03483 74  ARG B CB  
1769 C CG  . ARG B 74  ? 0.38526 0.34625 0.56869 -0.02810 0.04166  -0.05678 74  ARG B CG  
1770 C CD  . ARG B 74  ? 0.38381 0.31166 0.56630 -0.03651 0.06422  -0.06782 74  ARG B CD  
1771 N NE  . ARG B 74  ? 0.40081 0.35627 0.58815 -0.05009 0.07138  -0.09529 74  ARG B NE  
1772 C CZ  . ARG B 74  ? 0.40590 0.35799 0.60097 -0.07312 0.09375  -0.12654 74  ARG B CZ  
1773 N NH1 . ARG B 74  ? 0.43830 0.34629 0.63413 -0.08332 0.11632  -0.12888 74  ARG B NH1 
1774 N NH2 . ARG B 74  ? 0.43555 0.43182 0.63796 -0.08712 0.09736  -0.15883 74  ARG B NH2 
1775 N N   . ASP B 75  ? 0.33885 0.30105 0.51520 0.00060  0.02227  -0.01057 75  ASP B N   
1776 C CA  . ASP B 75  ? 0.33389 0.30462 0.50384 0.00953  0.02725  -0.00261 75  ASP B CA  
1777 C C   . ASP B 75  ? 0.31661 0.28790 0.49129 0.00530  0.02906  -0.00747 75  ASP B C   
1778 O O   . ASP B 75  ? 0.31576 0.27657 0.49855 0.00137  0.03035  -0.00516 75  ASP B O   
1779 C CB  . ASP B 75  ? 0.31226 0.26074 0.48141 0.01207  0.03735  0.01079  75  ASP B CB  
1780 C CG  . ASP B 75  ? 0.42863 0.37543 0.58650 0.02488  0.05161  0.02413  75  ASP B CG  
1781 O OD1 . ASP B 75  ? 0.39229 0.35010 0.55240 0.02395  0.05181  0.02223  75  ASP B OD1 
1782 O OD2 . ASP B 75  ? 0.50998 0.44172 0.65296 0.04019  0.06633  0.03919  75  ASP B OD2 
1783 N N   . ASN B 76  ? 0.32383 0.31611 0.49343 0.00760  0.02982  -0.01712 76  ASN B N   
1784 C CA  . ASN B 76  ? 0.33234 0.32097 0.50407 0.00471  0.03458  -0.02362 76  ASN B CA  
1785 C C   . ASN B 76  ? 0.36556 0.35169 0.53859 0.01057  0.03773  -0.00985 76  ASN B C   
1786 O O   . ASN B 76  ? 0.37264 0.35235 0.55099 0.00988  0.04042  -0.00974 76  ASN B O   
1787 C CB  . ASN B 76  ? 0.33834 0.35669 0.50556 0.00326  0.03714  -0.04299 76  ASN B CB  
1788 C CG  . ASN B 76  ? 0.35042 0.37659 0.52272 -0.01139 0.04058  -0.06714 76  ASN B CG  
1789 O OD1 . ASN B 76  ? 0.34837 0.34991 0.52478 -0.01756 0.04173  -0.06424 76  ASN B OD1 
1790 N ND2 . ASN B 76  ? 0.32311 0.39038 0.49650 -0.01849 0.04424  -0.09467 76  ASN B ND2 
1791 N N   . ALA B 77  ? 0.33525 0.32689 0.50195 0.01875  0.04191  0.00250  77  ALA B N   
1792 C CA  . ALA B 77  ? 0.38559 0.37270 0.55403 0.02102  0.05271  0.01324  77  ALA B CA  
1793 C C   . ALA B 77  ? 0.42135 0.39497 0.60716 0.00696  0.05656  0.01208  77  ALA B C   
1794 O O   . ALA B 77  ? 0.43435 0.41720 0.63078 0.00184  0.06198  0.00992  77  ALA B O   
1795 C CB  . ALA B 77  ? 0.39313 0.37953 0.54454 0.03803  0.06630  0.03053  77  ALA B CB  
1796 N N   . LYS B 78  ? 0.36448 0.32644 0.55460 0.00052  0.05404  0.00980  78  LYS B N   
1797 C CA  . LYS B 78  ? 0.34645 0.31190 0.55471 -0.01391 0.05584  0.00032  78  LYS B CA  
1798 C C   . LYS B 78  ? 0.37093 0.35760 0.58439 -0.01056 0.04181  -0.00779 78  LYS B C   
1799 O O   . LYS B 78  ? 0.34884 0.36032 0.57642 -0.01639 0.04048  -0.01808 78  LYS B O   
1800 C CB  . LYS B 78  ? 0.36396 0.30845 0.57228 -0.02029 0.06186  -0.00021 78  LYS B CB  
1801 C CG  . LYS B 78  ? 0.40073 0.31250 0.60055 -0.01932 0.08813  0.01136  78  LYS B CG  
1802 C CD  . LYS B 78  ? 0.49341 0.37693 0.68990 -0.02251 0.09806  0.01104  78  LYS B CD  
1803 C CE  . LYS B 78  ? 0.60958 0.44519 0.79214 -0.01677 0.13586  0.02632  78  LYS B CE  
1804 N NZ  . LYS B 78  ? 0.64679 0.44747 0.82699 -0.02191 0.15150  0.02280  78  LYS B NZ  
1805 N N   . ASN B 79  ? 0.32682 0.30698 0.52803 0.00012  0.03606  -0.00505 79  ASN B N   
1806 C CA  . ASN B 79  ? 0.33545 0.31814 0.53305 0.01009  0.03326  -0.00630 79  ASN B CA  
1807 C C   . ASN B 79  ? 0.34499 0.33380 0.54625 0.00994  0.02794  -0.00829 79  ASN B C   
1808 O O   . ASN B 79  ? 0.31824 0.33393 0.52171 0.02127  0.02626  -0.00929 79  ASN B O   
1809 C CB  . ASN B 79  ? 0.31519 0.32187 0.51557 0.02134  0.03648  -0.00549 79  ASN B CB  
1810 C CG  . ASN B 79  ? 0.39443 0.38273 0.57840 0.04038  0.04490  0.00013  79  ASN B CG  
1811 O OD1 . ASN B 79  ? 0.38826 0.34319 0.56265 0.03606  0.05242  -0.00259 79  ASN B OD1 
1812 N ND2 . ASN B 79  ? 0.36190 0.37459 0.54161 0.06292  0.04813  0.00611  79  ASN B ND2 
1813 N N   . THR B 80  ? 0.30043 0.27249 0.50033 0.00137  0.02546  -0.00886 80  THR B N   
1814 C CA  . THR B 80  ? 0.31101 0.28775 0.51429 -0.00057 0.02082  -0.01221 80  THR B CA  
1815 C C   . THR B 80  ? 0.35816 0.31220 0.55107 0.00117  0.01980  -0.00908 80  THR B C   
1816 O O   . THR B 80  ? 0.33356 0.27714 0.52174 -0.00256 0.02138  -0.00941 80  THR B O   
1817 C CB  . THR B 80  ? 0.34615 0.32391 0.56076 -0.01571 0.02486  -0.01918 80  THR B CB  
1818 O OG1 . THR B 80  ? 0.34768 0.35338 0.57743 -0.02348 0.03014  -0.02928 80  THR B OG1 
1819 C CG2 . THR B 80  ? 0.35314 0.33533 0.57140 -0.01988 0.02143  -0.02704 80  THR B CG2 
1820 N N   . VAL B 81  ? 0.27985 0.23592 0.46959 0.00796  0.01824  -0.00813 81  VAL B N   
1821 C CA  . VAL B 81  ? 0.32276 0.25973 0.50564 0.00669  0.02019  -0.00708 81  VAL B CA  
1822 C C   . VAL B 81  ? 0.30260 0.24821 0.48967 0.00330  0.01278  -0.00993 81  VAL B C   
1823 O O   . VAL B 81  ? 0.29226 0.26127 0.48556 0.00532  0.00892  -0.01493 81  VAL B O   
1824 C CB  . VAL B 81  ? 0.31923 0.24000 0.49001 0.02069  0.03305  -0.00012 81  VAL B CB  
1825 C CG1 . VAL B 81  ? 0.33467 0.23300 0.50163 0.01328  0.04153  -0.00269 81  VAL B CG1 
1826 C CG2 . VAL B 81  ? 0.30583 0.21097 0.47037 0.02633  0.04674  0.00196  81  VAL B CG2 
1827 N N   . TYR B 82  ? 0.30719 0.24199 0.49186 -0.00192 0.01189  -0.01067 82  TYR B N   
1828 C CA  . TYR B 82  ? 0.31401 0.25064 0.50018 -0.00361 0.00788  -0.01293 82  TYR B CA  
1829 C C   . TYR B 82  ? 0.31508 0.24799 0.49576 -0.00029 0.00779  -0.01161 82  TYR B C   
1830 O O   . TYR B 82  ? 0.30969 0.23566 0.48754 -0.00240 0.01401  -0.01187 82  TYR B O   
1831 C CB  . TYR B 82  ? 0.30453 0.23233 0.48874 -0.00572 0.01091  -0.01105 82  TYR B CB  
1832 C CG  . TYR B 82  ? 0.31482 0.23837 0.50196 -0.00852 0.01778  -0.00960 82  TYR B CG  
1833 C CD1 . TYR B 82  ? 0.33778 0.25835 0.53469 -0.01826 0.02549  -0.01764 82  TYR B CD1 
1834 C CD2 . TYR B 82  ? 0.35625 0.28395 0.53830 -0.00389 0.01921  -0.00446 82  TYR B CD2 
1835 C CE1 . TYR B 82  ? 0.40003 0.31394 0.60159 -0.02423 0.03761  -0.01770 82  TYR B CE1 
1836 C CE2 . TYR B 82  ? 0.38584 0.30863 0.56896 -0.00455 0.02796  -0.00076 82  TYR B CE2 
1837 C CZ  . TYR B 82  ? 0.39830 0.31054 0.59119 -0.01511 0.03844  -0.00596 82  TYR B CZ  
1838 O OH  . TYR B 82  ? 0.43464 0.33955 0.63064 -0.01922 0.05258  -0.00384 82  TYR B OH  
1839 N N   . LEU B 83  ? 0.29842 0.23731 0.47930 0.00188  0.00405  -0.01409 83  LEU B N   
1840 C CA  . LEU B 83  ? 0.31863 0.25470 0.49419 0.00517  0.00457  -0.01221 83  LEU B CA  
1841 C C   . LEU B 83  ? 0.33038 0.26550 0.50643 0.00345  0.00155  -0.01628 83  LEU B C   
1842 O O   . LEU B 83  ? 0.33346 0.27476 0.51276 0.00199  0.00052  -0.02435 83  LEU B O   
1843 C CB  . LEU B 83  ? 0.30021 0.24420 0.46886 0.01800  0.00724  -0.00765 83  LEU B CB  
1844 C CG  . LEU B 83  ? 0.34148 0.27641 0.50362 0.02076  0.01344  -0.00348 83  LEU B CG  
1845 C CD1 . LEU B 83  ? 0.34518 0.26021 0.50848 0.01020  0.02792  -0.00399 83  LEU B CD1 
1846 C CD2 . LEU B 83  ? 0.34809 0.29277 0.49722 0.04214  0.01916  0.00595  83  LEU B CD2 
1847 N N   . GLN B 84  ? 0.31039 0.24283 0.48273 0.00501  0.00296  -0.01335 84  GLN B N   
1848 C CA  . GLN B 84  ? 0.29789 0.22339 0.46439 0.01134  0.00557  -0.01238 84  GLN B CA  
1849 C C   . GLN B 84  ? 0.32005 0.25433 0.48474 0.01419  0.00215  -0.01419 84  GLN B C   
1850 O O   . GLN B 84  ? 0.33848 0.28662 0.50436 0.01306  0.00173  -0.01386 84  GLN B O   
1851 C CB  . GLN B 84  ? 0.33692 0.26900 0.49469 0.02314  0.00961  -0.00459 84  GLN B CB  
1852 C CG  . GLN B 84  ? 0.35247 0.27393 0.49657 0.04037  0.01822  0.00260  84  GLN B CG  
1853 C CD  . GLN B 84  ? 0.39858 0.27586 0.53817 0.03901  0.03572  0.00327  84  GLN B CD  
1854 O OE1 . GLN B 84  ? 0.42727 0.28524 0.56307 0.04072  0.04841  0.00930  84  GLN B OE1 
1855 N NE2 . GLN B 84  ? 0.41450 0.27527 0.55505 0.03396  0.04073  -0.00591 84  GLN B NE2 
1856 N N   . MET B 85  ? 0.32583 0.25378 0.48911 0.01520  0.00303  -0.01974 85  MET B N   
1857 C CA  . MET B 85  ? 0.33847 0.27646 0.49824 0.02029  0.00013  -0.02096 85  MET B CA  
1858 C C   . MET B 85  ? 0.34344 0.26957 0.49556 0.02797  0.00584  -0.02154 85  MET B C   
1859 O O   . MET B 85  ? 0.38661 0.28926 0.53697 0.02571  0.01624  -0.02759 85  MET B O   
1860 C CB  . MET B 85  ? 0.34579 0.29919 0.50752 0.02034  -0.00364 -0.02898 85  MET B CB  
1861 C CG  . MET B 85  ? 0.36386 0.32626 0.52633 0.02290  -0.00416 -0.02232 85  MET B CG  
1862 S SD  . MET B 85  ? 0.49882 0.50039 0.65601 0.03867  -0.00767 -0.02665 85  MET B SD  
1863 C CE  . MET B 85  ? 0.27930 0.30082 0.45120 0.02288  -0.01157 -0.05381 85  MET B CE  
1864 N N   . ASN B 86  ? 0.32797 0.33600 0.40506 0.00468  -0.00497 -0.01100 86  ASN B N   
1865 C CA  . ASN B 86  ? 0.33161 0.34791 0.41000 0.02251  -0.01008 -0.01706 86  ASN B CA  
1866 C C   . ASN B 86  ? 0.34214 0.39779 0.44736 0.02868  0.00561  -0.01390 86  ASN B C   
1867 O O   . ASN B 86  ? 0.32039 0.39500 0.44406 0.01742  0.01704  -0.00644 86  ASN B O   
1868 C CB  . ASN B 86  ? 0.33725 0.35067 0.42699 0.02941  -0.02993 -0.02201 86  ASN B CB  
1869 C CG  . ASN B 86  ? 0.40368 0.35945 0.44571 0.02670  -0.04437 -0.02602 86  ASN B CG  
1870 O OD1 . ASN B 86  ? 0.39534 0.31671 0.39820 0.03199  -0.04389 -0.03065 86  ASN B OD1 
1871 N ND2 . ASN B 86  ? 0.39010 0.32770 0.42899 0.01803  -0.05680 -0.02456 86  ASN B ND2 
1872 N N   . SER B 87  ? 0.32043 0.38076 0.42069 0.04688  0.00814  -0.01982 87  SER B N   
1873 C CA  . SER B 87  ? 0.35036 0.44201 0.47083 0.05534  0.02886  -0.01845 87  SER B CA  
1874 C C   . SER B 87  ? 0.35117 0.43513 0.45113 0.04444  0.04561  -0.00975 87  SER B C   
1875 O O   . SER B 87  ? 0.33615 0.44103 0.45486 0.03783  0.06453  -0.00365 87  SER B O   
1876 C CB  . SER B 87  ? 0.32908 0.46578 0.51045 0.05427  0.03267  -0.01925 87  SER B CB  
1877 O OG  . SER B 87  ? 0.39507 0.53589 0.59533 0.06951  0.01112  -0.02960 87  SER B OG  
1878 N N   . LEU B 88  ? 0.36110 0.41073 0.42118 0.04279  0.03766  -0.01022 88  LEU B N   
1879 C CA  . LEU B 88  ? 0.36112 0.39539 0.39869 0.03531  0.04367  -0.00412 88  LEU B CA  
1880 C C   . LEU B 88  ? 0.41556 0.44402 0.42825 0.04674  0.06227  -0.00232 88  LEU B C   
1881 O O   . LEU B 88  ? 0.42633 0.45402 0.42897 0.06331  0.06843  -0.00811 88  LEU B O   
1882 C CB  . LEU B 88  ? 0.43487 0.43792 0.44760 0.03244  0.02717  -0.00849 88  LEU B CB  
1883 C CG  . LEU B 88  ? 0.40398 0.40579 0.43607 0.01751  0.01790  -0.00897 88  LEU B CG  
1884 C CD1 . LEU B 88  ? 0.42857 0.40503 0.44716 0.01525  0.00753  -0.01691 88  LEU B CD1 
1885 C CD2 . LEU B 88  ? 0.39068 0.39657 0.43298 0.00623  0.02002  -0.00205 88  LEU B CD2 
1886 N N   . LYS B 89  ? 0.38014 0.39704 0.37588 0.03883  0.07210  0.00548  89  LYS B N   
1887 C CA  . LYS B 89  ? 0.46545 0.46276 0.42348 0.04627  0.09469  0.00925  89  LYS B CA  
1888 C C   . LYS B 89  ? 0.52668 0.47422 0.42959 0.04602  0.08062  0.01183  89  LYS B C   
1889 O O   . LYS B 89  ? 0.45641 0.39947 0.36933 0.03642  0.05931  0.01230  89  LYS B O   
1890 C CB  . LYS B 89  ? 0.51650 0.53904 0.50207 0.03443  0.12311  0.01701  89  LYS B CB  
1891 C CG  . LYS B 89  ? 0.56518 0.64193 0.62064 0.03215  0.12840  0.01304  89  LYS B CG  
1892 C CD  . LYS B 89  ? 0.57653 0.68132 0.67024 0.01561  0.15483  0.01969  89  LYS B CD  
1893 C CE  . LYS B 89  ? 0.58175 0.74238 0.75501 0.01469  0.14923  0.01270  89  LYS B CE  
1894 N NZ  . LYS B 89  ? 0.53887 0.73570 0.76798 -0.00425 0.17084  0.01665  89  LYS B NZ  
1895 N N   . PRO B 90  ? 0.52730 0.43245 0.36953 0.05819  0.09092  0.01239  90  PRO B N   
1896 C CA  . PRO B 90  ? 0.61478 0.46275 0.39734 0.05995  0.07180  0.01428  90  PRO B CA  
1897 C C   . PRO B 90  ? 0.63967 0.48221 0.42583 0.04521  0.06979  0.02269  90  PRO B C   
1898 O O   . PRO B 90  ? 0.63877 0.45322 0.40881 0.04521  0.03961  0.02077  90  PRO B O   
1899 C CB  . PRO B 90  ? 0.69543 0.49376 0.40431 0.07443  0.09404  0.01577  90  PRO B CB  
1900 C CG  . PRO B 90  ? 0.69607 0.52590 0.42955 0.08557  0.11293  0.00968  90  PRO B CG  
1901 C CD  . PRO B 90  ? 0.56524 0.46676 0.38708 0.07386  0.11713  0.00933  90  PRO B CD  
1902 N N   . GLU B 91  ? 0.59239 0.46139 0.40363 0.03281  0.09947  0.03073  91  GLU B N   
1903 C CA  . GLU B 91  ? 0.62800 0.48717 0.43835 0.01748  0.09877  0.03930  91  GLU B CA  
1904 C C   . GLU B 91  ? 0.56471 0.45106 0.42508 0.00954  0.07007  0.03621  91  GLU B C   
1905 O O   . GLU B 91  ? 0.57210 0.44292 0.42638 0.00040  0.06277  0.04162  91  GLU B O   
1906 C CB  . GLU B 91  ? 0.61780 0.50368 0.45345 0.00256  0.13828  0.04735  91  GLU B CB  
1907 C CG  . GLU B 91  ? 0.76914 0.61927 0.54988 0.00628  0.17745  0.05180  91  GLU B CG  
1908 C CD  . GLU B 91  ? 0.82714 0.69745 0.61718 0.02296  0.19623  0.04371  91  GLU B CD  
1909 O OE1 . GLU B 91  ? 0.68315 0.60147 0.52954 0.03007  0.18000  0.03511  91  GLU B OE1 
1910 O OE2 . GLU B 91  ? 0.90982 0.73952 0.64231 0.02994  0.22877  0.04584  91  GLU B OE2 
1911 N N   . ASP B 92  ? 0.52377 0.44389 0.42765 0.01278  0.05640  0.02762  92  ASP B N   
1912 C CA  . ASP B 92  ? 0.45150 0.38953 0.39564 0.00581  0.03525  0.02346  92  ASP B CA  
1913 C C   . ASP B 92  ? 0.48431 0.39560 0.41533 0.01338  0.00615  0.01546  92  ASP B C   
1914 O O   . ASP B 92  ? 0.45732 0.38216 0.42454 0.00804  -0.00727 0.01044  92  ASP B O   
1915 C CB  . ASP B 92  ? 0.39727 0.37317 0.38597 0.00420  0.03653  0.01766  92  ASP B CB  
1916 C CG  . ASP B 92  ? 0.43602 0.44467 0.45430 -0.00241 0.05635  0.02236  92  ASP B CG  
1917 O OD1 . ASP B 92  ? 0.41650 0.43075 0.44477 -0.01500 0.06572  0.03018  92  ASP B OD1 
1918 O OD2 . ASP B 92  ? 0.42523 0.45314 0.45919 0.00535  0.06043  0.01712  92  ASP B OD2 
1919 N N   . THR B 93  ? 0.49767 0.37084 0.38094 0.02597  -0.00395 0.01260  93  THR B N   
1920 C CA  . THR B 93  ? 0.51297 0.36093 0.39064 0.03358  -0.03780 0.00283  93  THR B CA  
1921 C C   . THR B 93  ? 0.56075 0.39321 0.44118 0.03173  -0.05458 0.00415  93  THR B C   
1922 O O   . THR B 93  ? 0.54996 0.34702 0.38204 0.03301  -0.04935 0.01316  93  THR B O   
1923 C CB  . THR B 93  ? 0.54971 0.34745 0.36209 0.04845  -0.04847 0.00036  93  THR B CB  
1924 O OG1 . THR B 93  ? 0.53697 0.34920 0.35094 0.05214  -0.03558 -0.00297 93  THR B OG1 
1925 C CG2 . THR B 93  ? 0.55692 0.32302 0.36396 0.05723  -0.09210 -0.01140 93  THR B CG2 
1926 N N   . ALA B 94  ? 0.47460 0.32956 0.40937 0.02902  -0.07254 -0.00549 94  ALA B N   
1927 C CA  . ALA B 94  ? 0.47000 0.31592 0.41831 0.03001  -0.08877 -0.00674 94  ALA B CA  
1928 C C   . ALA B 94  ? 0.43443 0.31446 0.45569 0.02738  -0.10078 -0.02091 94  ALA B C   
1929 O O   . ALA B 94  ? 0.41522 0.32288 0.46963 0.02051  -0.09062 -0.02673 94  ALA B O   
1930 C CB  . ALA B 94  ? 0.47368 0.32624 0.41630 0.01900  -0.06506 0.00628  94  ALA B CB  
1931 N N   . VAL B 95  ? 0.46879 0.34273 0.51299 0.03323  -0.12060 -0.02709 95  VAL B N   
1932 C CA  . VAL B 95  ? 0.41243 0.32245 0.53193 0.02901  -0.12012 -0.03947 95  VAL B CA  
1933 C C   . VAL B 95  ? 0.39208 0.31816 0.51910 0.01755  -0.09100 -0.03019 95  VAL B C   
1934 O O   . VAL B 95  ? 0.38703 0.29130 0.47761 0.01842  -0.08938 -0.01932 95  VAL B O   
1935 C CB  . VAL B 95  ? 0.43571 0.33424 0.58453 0.04412  -0.15616 -0.05317 95  VAL B CB  
1936 C CG1 . VAL B 95  ? 0.37161 0.31306 0.60906 0.03952  -0.14786 -0.06819 95  VAL B CG1 
1937 C CG2 . VAL B 95  ? 0.47348 0.34760 0.60893 0.05615  -0.19302 -0.06321 95  VAL B CG2 
1938 N N   . TYR B 96  ? 0.33319 0.28893 0.50087 0.00614  -0.06912 -0.03468 96  TYR B N   
1939 C CA  . TYR B 96  ? 0.31524 0.27759 0.48241 -0.00450 -0.04436 -0.02694 96  TYR B CA  
1940 C C   . TYR B 96  ? 0.31938 0.29134 0.53460 -0.00388 -0.03951 -0.03809 96  TYR B C   
1941 O O   . TYR B 96  ? 0.30244 0.29210 0.56743 -0.00411 -0.03851 -0.05285 96  TYR B O   
1942 C CB  . TYR B 96  ? 0.33711 0.31082 0.49770 -0.01624 -0.02244 -0.02313 96  TYR B CB  
1943 C CG  . TYR B 96  ? 0.30903 0.27787 0.42746 -0.01649 -0.01994 -0.01122 96  TYR B CG  
1944 C CD1 . TYR B 96  ? 0.36414 0.32391 0.46015 -0.00780 -0.03214 -0.01185 96  TYR B CD1 
1945 C CD2 . TYR B 96  ? 0.34468 0.31635 0.44771 -0.02468 -0.00571 -0.00074 96  TYR B CD2 
1946 C CE1 . TYR B 96  ? 0.35265 0.30795 0.41218 -0.00672 -0.02343 -0.00231 96  TYR B CE1 
1947 C CE2 . TYR B 96  ? 0.34738 0.32248 0.42616 -0.02467 -0.00004 0.00786  96  TYR B CE2 
1948 C CZ  . TYR B 96  ? 0.36587 0.33346 0.42330 -0.01531 -0.00573 0.00695  96  TYR B CZ  
1949 O OH  . TYR B 96  ? 0.38296 0.35352 0.41870 -0.01399 0.00585  0.01397  96  TYR B OH  
1950 N N   . TYR B 97  ? 0.30973 0.26868 0.51117 -0.00385 -0.03431 -0.03173 97  TYR B N   
1951 C CA  . TYR B 97  ? 0.30522 0.26650 0.54408 0.00029  -0.02797 -0.04182 97  TYR B CA  
1952 C C   . TYR B 97  ? 0.28155 0.23119 0.49834 -0.01141 -0.00244 -0.03409 97  TYR B C   
1953 O O   . TYR B 97  ? 0.33045 0.26535 0.50279 -0.01825 -0.00229 -0.01961 97  TYR B O   
1954 C CB  . TYR B 97  ? 0.30537 0.24654 0.53607 0.01579  -0.05210 -0.04236 97  TYR B CB  
1955 C CG  . TYR B 97  ? 0.34445 0.28351 0.58699 0.03097  -0.08594 -0.05103 97  TYR B CG  
1956 C CD1 . TYR B 97  ? 0.36255 0.27828 0.54947 0.03235  -0.10180 -0.04034 97  TYR B CD1 
1957 C CD2 . TYR B 97  ? 0.33499 0.29232 0.64460 0.04437  -0.10210 -0.07118 97  TYR B CD2 
1958 C CE1 . TYR B 97  ? 0.38452 0.28420 0.56830 0.04789  -0.13711 -0.04867 97  TYR B CE1 
1959 C CE2 . TYR B 97  ? 0.40636 0.35606 0.72663 0.06022  -0.14233 -0.08107 97  TYR B CE2 
1960 C CZ  . TYR B 97  ? 0.39394 0.30982 0.64408 0.06197  -0.16083 -0.06912 97  TYR B CZ  
1961 O OH  . TYR B 97  ? 0.46868 0.36325 0.71447 0.07865  -0.20351 -0.07870 97  TYR B OH  
1962 N N   . CYS B 98  ? 0.30973 0.26193 0.55765 -0.01329 0.01853  -0.04479 98  CYS B N   
1963 C CA  . CYS B 98  ? 0.34329 0.27039 0.56065 -0.02181 0.04044  -0.03929 98  CYS B CA  
1964 C C   . CYS B 98  ? 0.33373 0.24773 0.56681 -0.01103 0.04428  -0.04666 98  CYS B C   
1965 O O   . CYS B 98  ? 0.29925 0.23110 0.58839 -0.00289 0.05295  -0.06323 98  CYS B O   
1966 C CB  . CYS B 98  ? 0.33323 0.25757 0.55388 -0.03350 0.06793  -0.04505 98  CYS B CB  
1967 S SG  . CYS B 98  ? 0.43074 0.30570 0.59214 -0.04285 0.08894  -0.03770 98  CYS B SG  
1968 N N   . VAL B 99  ? 0.33802 0.22187 0.52667 -0.01047 0.03696  -0.03565 99  VAL B N   
1969 C CA  . VAL B 99  ? 0.38948 0.25485 0.58475 0.00336  0.03468  -0.04185 99  VAL B CA  
1970 C C   . VAL B 99  ? 0.44889 0.27199 0.59670 -0.00346 0.05133  -0.03574 99  VAL B C   
1971 O O   . VAL B 99  ? 0.42071 0.22663 0.52556 -0.01869 0.05433  -0.02418 99  VAL B O   
1972 C CB  . VAL B 99  ? 0.43494 0.28986 0.61300 0.01456  0.00162  -0.03563 99  VAL B CB  
1973 C CG1 . VAL B 99  ? 0.43630 0.32062 0.65318 0.02512  -0.02054 -0.04378 99  VAL B CG1 
1974 C CG2 . VAL B 99  ? 0.42945 0.26083 0.54489 -0.00064 -0.00629 -0.01520 99  VAL B CG2 
1975 N N   . ARG B 100 ? 0.38957 0.19302 0.54589 0.01012  0.05923  -0.04508 100 ARG B N   
1976 C CA  . ARG B 100 ? 0.46905 0.22021 0.56916 0.00781  0.06671  -0.03885 100 ARG B CA  
1977 C C   . ARG B 100 ? 0.51109 0.23877 0.57312 0.01001  0.03600  -0.02642 100 ARG B C   
1978 O O   . ARG B 100 ? 0.48754 0.22054 0.57001 0.02682  0.01781  -0.03170 100 ARG B O   
1979 C CB  . ARG B 100 ? 0.47359 0.20830 0.59516 0.02305  0.09328  -0.05541 100 ARG B CB  
1980 C CG  . ARG B 100 ? 0.48027 0.23479 0.64377 0.01911  0.13189  -0.06974 100 ARG B CG  
1981 C CD  . ARG B 100 ? 0.61987 0.37952 0.83586 0.03836  0.15604  -0.09004 100 ARG B CD  
1982 N NE  . ARG B 100 ? 0.57528 0.38185 0.86187 0.05644  0.12700  -0.09988 100 ARG B NE  
1983 C CZ  . ARG B 100 ? 0.48969 0.30982 0.82881 0.07930  0.12730  -0.11654 100 ARG B CZ  
1984 N NH1 . ARG B 100 ? 0.54953 0.34707 0.87288 0.08516  0.15629  -0.12207 100 ARG B NH1 
1985 N NH2 . ARG B 100 ? 0.62436 0.48278 1.02075 0.09552  0.09139  -0.12487 100 ARG B NH2 
1986 N N   . VAL B 101 ? 0.41844 0.35408 0.45634 0.04968  0.06420  0.01194  101 VAL B N   
1987 C CA  . VAL B 101 ? 0.42106 0.34010 0.42980 0.04920  0.04027  0.01833  101 VAL B CA  
1988 C C   . VAL B 101 ? 0.38530 0.31215 0.44336 0.05747  0.03025  0.01055  101 VAL B C   
1989 O O   . VAL B 101 ? 0.42956 0.37446 0.51690 0.06537  0.05442  0.00182  101 VAL B O   
1990 C CB  . VAL B 101 ? 0.43390 0.34825 0.38512 0.04901  0.05790  0.02496  101 VAL B CB  
1991 C CG1 . VAL B 101 ? 0.45996 0.35771 0.38959 0.04886  0.03832  0.03024  101 VAL B CG1 
1992 C CG2 . VAL B 101 ? 0.46669 0.37036 0.37265 0.03965  0.06370  0.03241  101 VAL B CG2 
1993 N N   . GLY B 102 ? 0.41332 0.32370 0.47926 0.05611  -0.00515 0.01341  102 GLY B N   
1994 C CA  . GLY B 102 ? 0.39064 0.30768 0.50892 0.06386  -0.01768 0.00566  102 GLY B CA  
1995 C C   . GLY B 102 ? 0.39262 0.32290 0.58826 0.06671  -0.02622 -0.00673 102 GLY B C   
1996 O O   . GLY B 102 ? 0.36881 0.30955 0.61907 0.07373  -0.02923 -0.01624 102 GLY B O   
1997 N N   . ALA B 103 ? 0.36670 0.29743 0.57389 0.06144  -0.02899 -0.00848 103 ALA B N   
1998 C CA  . ALA B 103 ? 0.36986 0.30985 0.65650 0.06325  -0.04393 -0.02130 103 ALA B CA  
1999 C C   . ALA B 103 ? 0.43657 0.35472 0.70782 0.05698  -0.08230 -0.01717 103 ALA B C   
2000 O O   . ALA B 103 ? 0.44891 0.35593 0.66157 0.04983  -0.07696 -0.00842 103 ALA B O   
2001 C CB  . ALA B 103 ? 0.45187 0.41708 0.78458 0.06451  -0.00227 -0.03240 103 ALA B CB  
2002 N N   . GLU B 104 ? 0.44698 0.36037 0.77772 0.06042  -0.11894 -0.02597 104 GLU B N   
2003 C CA  A GLU B 104 ? 0.48540 0.37225 0.80829 0.05771  -0.16725 -0.02473 104 GLU B CA  
2004 C CA  B GLU B 104 ? 0.49016 0.37531 0.80162 0.05692  -0.16519 -0.02282 104 GLU B CA  
2005 C C   . GLU B 104 ? 0.49907 0.39277 0.84013 0.05229  -0.16241 -0.03183 104 GLU B C   
2006 O O   . GLU B 104 ? 0.55101 0.41942 0.84431 0.04719  -0.18860 -0.02620 104 GLU B O   
2007 C CB  A GLU B 104 ? 0.46976 0.35405 0.86853 0.06549  -0.20675 -0.03592 104 GLU B CB  
2008 C CB  B GLU B 104 ? 0.48185 0.35342 0.84118 0.06405  -0.21222 -0.02847 104 GLU B CB  
2009 C CG  A GLU B 104 ? 0.47117 0.39259 0.98443 0.07094  -0.18379 -0.05661 104 GLU B CG  
2010 C CG  B GLU B 104 ? 0.51360 0.38088 0.85308 0.06887  -0.20862 -0.02076 104 GLU B CG  
2011 C CD  A GLU B 104 ? 0.45651 0.40353 0.97938 0.07421  -0.13194 -0.05840 104 GLU B CD  
2012 C CD  B GLU B 104 ? 0.51242 0.37613 0.91591 0.07631  -0.24432 -0.02908 104 GLU B CD  
2013 O OE1 A GLU B 104 ? 0.40224 0.34134 0.86430 0.07537  -0.12343 -0.04656 104 GLU B OE1 
2014 O OE1 B GLU B 104 ? 0.55649 0.40065 0.96529 0.07280  -0.28721 -0.03265 104 GLU B OE1 
2015 O OE2 A GLU B 104 ? 0.42866 0.40292 1.01075 0.07220  -0.09679 -0.07188 104 GLU B OE2 
2016 O OE2 B GLU B 104 ? 0.40253 0.28720 0.83769 0.07866  -0.22312 -0.03443 104 GLU B OE2 
2017 N N   . TYR B 105 ? 0.41308 0.33823 0.82485 0.05345  -0.12897 -0.04510 105 TYR B N   
2018 C CA  . TYR B 105 ? 0.47602 0.40853 0.93125 0.04947  -0.13038 -0.05584 105 TYR B CA  
2019 C C   . TYR B 105 ? 0.45555 0.38092 0.83648 0.04099  -0.11034 -0.04514 105 TYR B C   
2020 O O   . TYR B 105 ? 0.48412 0.41343 0.80713 0.03904  -0.07447 -0.03392 105 TYR B O   
2021 C CB  . TYR B 105 ? 0.50379 0.46918 1.05638 0.05245  -0.09317 -0.07256 105 TYR B CB  
2022 C CG  . TYR B 105 ? 0.46361 0.43952 1.06821 0.04767  -0.08451 -0.08430 105 TYR B CG  
2023 C CD1 . TYR B 105 ? 0.48035 0.45328 1.15907 0.04893  -0.12662 -0.09999 105 TYR B CD1 
2024 C CD2 . TYR B 105 ? 0.49099 0.47804 1.07121 0.04251  -0.03595 -0.08005 105 TYR B CD2 
2025 C CE1 . TYR B 105 ? 0.48920 0.47280 1.22394 0.04456  -0.11867 -0.11284 105 TYR B CE1 
2026 C CE2 . TYR B 105 ? 0.40347 0.39933 1.03380 0.03775  -0.02635 -0.09067 105 TYR B CE2 
2027 C CZ  . TYR B 105 ? 0.45592 0.45118 1.16567 0.03859  -0.06690 -0.10756 105 TYR B CZ  
2028 O OH  . TYR B 105 ? 0.46845 0.47326 1.23633 0.03404  -0.05829 -0.12020 105 TYR B OH  
2029 N N   . VAL B 106 ? 0.43815 0.35078 0.81938 0.03636  -0.13687 -0.04936 106 VAL B N   
2030 C CA  . VAL B 106 ? 0.44534 0.35031 0.76333 0.02790  -0.12090 -0.04143 106 VAL B CA  
2031 C C   . VAL B 106 ? 0.44820 0.36540 0.83329 0.02517  -0.12224 -0.05685 106 VAL B C   
2032 O O   . VAL B 106 ? 0.43449 0.35007 0.88862 0.02880  -0.15912 -0.07159 106 VAL B O   
2033 C CB  . VAL B 106 ? 0.54855 0.41372 0.77103 0.02370  -0.15623 -0.02824 106 VAL B CB  
2034 C CG1 . VAL B 106 ? 0.66287 0.50294 0.90703 0.02755  -0.21594 -0.03587 106 VAL B CG1 
2035 C CG2 . VAL B 106 ? 0.57460 0.43116 0.73985 0.01457  -0.14139 -0.02291 106 VAL B CG2 
2036 N N   . GLY B 107 ? 0.37720 0.30577 0.74563 0.01917  -0.08351 -0.05425 107 GLY B N   
2037 C CA  . GLY B 107 ? 0.37050 0.30819 0.79420 0.01520  -0.08221 -0.06752 107 GLY B CA  
2038 C C   . GLY B 107 ? 0.41196 0.32165 0.79059 0.01019  -0.12568 -0.06792 107 GLY B C   
2039 O O   . GLY B 107 ? 0.46508 0.34438 0.77918 0.01091  -0.16368 -0.05982 107 GLY B O   
2040 N N   . GLN B 108 ? 0.38953 0.30662 0.80074 0.00514  -0.11854 -0.07776 108 GLN B N   
2041 C CA  . GLN B 108 ? 0.42648 0.31702 0.80264 0.00081  -0.15989 -0.08199 108 GLN B CA  
2042 C C   . GLN B 108 ? 0.43288 0.30750 0.70788 -0.00766 -0.14046 -0.06701 108 GLN B C   
2043 O O   . GLN B 108 ? 0.47119 0.31633 0.69434 -0.01160 -0.17361 -0.06790 108 GLN B O   
2044 C CB  . GLN B 108 ? 0.42335 0.32938 0.89683 -0.00000 -0.16779 -0.10391 108 GLN B CB  
2045 C CG  . GLN B 108 ? 0.43099 0.34942 1.01149 0.00818  -0.19371 -0.12186 108 GLN B CG  
2046 C CD  . GLN B 108 ? 0.49054 0.37656 1.04222 0.01464  -0.25988 -0.12275 108 GLN B CD  
2047 O OE1 . GLN B 108 ? 0.58393 0.43714 1.07838 0.01316  -0.30244 -0.12309 108 GLN B OE1 
2048 N NE2 . GLN B 108 ? 0.54349 0.43529 1.13190 0.02220  -0.26867 -0.12324 108 GLN B NE2 
2049 N N   . GLY B 109 ? 0.41231 0.30370 0.65996 -0.01011 -0.08860 -0.05484 109 GLY B N   
2050 C CA  . GLY B 109 ? 0.41673 0.29445 0.57477 -0.01758 -0.06903 -0.04121 109 GLY B CA  
2051 C C   . GLY B 109 ? 0.39834 0.28333 0.57202 -0.02449 -0.05210 -0.04796 109 GLY B C   
2052 O O   . GLY B 109 ? 0.39349 0.29268 0.64751 -0.02394 -0.05728 -0.06379 109 GLY B O   
2053 N N   . THR B 110 ? 0.31578 0.37940 0.53211 -0.01991 -0.04934 -0.04014 110 THR B N   
2054 C CA  . THR B 110 ? 0.34725 0.41419 0.56086 -0.03107 -0.05051 -0.03890 110 THR B CA  
2055 C C   . THR B 110 ? 0.34121 0.38729 0.52770 -0.02977 -0.05720 -0.03363 110 THR B C   
2056 O O   . THR B 110 ? 0.31307 0.34673 0.48577 -0.02865 -0.05129 -0.03024 110 THR B O   
2057 C CB  . THR B 110 ? 0.32247 0.38563 0.52529 -0.03756 -0.03421 -0.03529 110 THR B CB  
2058 O OG1 . THR B 110 ? 0.38631 0.43502 0.58368 -0.04565 -0.02809 -0.03150 110 THR B OG1 
2059 C CG2 . THR B 110 ? 0.33984 0.39880 0.51857 -0.03183 -0.03540 -0.03380 110 THR B CG2 
2060 N N   . GLN B 111 ? 0.35160 0.39670 0.53449 -0.03275 -0.06632 -0.03825 111 GLN B N   
2061 C CA  . GLN B 111 ? 0.36315 0.38533 0.51263 -0.02936 -0.06873 -0.03575 111 GLN B CA  
2062 C C   . GLN B 111 ? 0.39088 0.39971 0.53326 -0.03404 -0.05445 -0.03287 111 GLN B C   
2063 O O   . GLN B 111 ? 0.36131 0.36488 0.51156 -0.04030 -0.04771 -0.03478 111 GLN B O   
2064 C CB  . GLN B 111 ? 0.37761 0.40480 0.51795 -0.02868 -0.08703 -0.04899 111 GLN B CB  
2065 C CG  . GLN B 111 ? 0.42508 0.42206 0.51749 -0.02437 -0.08516 -0.04952 111 GLN B CG  
2066 C CD  . GLN B 111 ? 0.49885 0.47228 0.54713 -0.00635 -0.08265 -0.03423 111 GLN B CD  
2067 O OE1 . GLN B 111 ? 0.50278 0.48014 0.53842 0.01111  -0.09895 -0.02942 111 GLN B OE1 
2068 N NE2 . GLN B 111 ? 0.47473 0.42118 0.50033 -0.00814 -0.05800 -0.02598 111 GLN B NE2 
2069 N N   . VAL B 112 ? 0.34454 0.34541 0.47367 -0.02902 -0.04585 -0.02819 112 VAL B N   
2070 C CA  . VAL B 112 ? 0.34347 0.34195 0.47192 -0.02430 -0.03485 -0.02752 112 VAL B CA  
2071 C C   . VAL B 112 ? 0.35601 0.33305 0.45836 -0.02166 -0.02610 -0.03074 112 VAL B C   
2072 O O   . VAL B 112 ? 0.38056 0.34954 0.46773 -0.02234 -0.01879 -0.02788 112 VAL B O   
2073 C CB  . VAL B 112 ? 0.36304 0.39112 0.51498 -0.02116 -0.03078 -0.02809 112 VAL B CB  
2074 C CG1 . VAL B 112 ? 0.35226 0.39377 0.51383 -0.00805 -0.02315 -0.03012 112 VAL B CG1 
2075 C CG2 . VAL B 112 ? 0.31937 0.36374 0.47926 -0.02004 -0.03926 -0.02697 112 VAL B CG2 
2076 N N   . THR B 113 ? 0.38765 0.34493 0.47714 -0.01784 -0.02087 -0.03633 113 THR B N   
2077 C CA  . THR B 113 ? 0.39272 0.32573 0.44936 -0.01355 -0.00870 -0.04355 113 THR B CA  
2078 C C   . THR B 113 ? 0.40513 0.33524 0.47492 0.00028  0.00983  -0.04471 113 THR B C   
2079 O O   . THR B 113 ? 0.47073 0.38588 0.54682 0.00677  0.00973  -0.04353 113 THR B O   
2080 C CB  . THR B 113 ? 0.46082 0.36932 0.48426 -0.02035 -0.02195 -0.05925 113 THR B CB  
2081 O OG1 . THR B 113 ? 0.49998 0.42716 0.52391 -0.02464 -0.04530 -0.05868 113 THR B OG1 
2082 C CG2 . THR B 113 ? 0.48367 0.36363 0.45435 -0.01327 -0.01009 -0.06888 113 THR B CG2 
2083 N N   . VAL B 114 ? 0.39367 0.33578 0.46918 0.00721  0.03012  -0.04611 114 VAL B N   
2084 C CA  . VAL B 114 ? 0.38442 0.34072 0.48655 0.02764  0.04737  -0.04952 114 VAL B CA  
2085 C C   . VAL B 114 ? 0.44593 0.36577 0.51054 0.03254  0.07256  -0.06100 114 VAL B C   
2086 O O   . VAL B 114 ? 0.49489 0.41042 0.53719 0.02376  0.09055  -0.06293 114 VAL B O   
2087 C CB  . VAL B 114 ? 0.35783 0.37826 0.51871 0.03022  0.05367  -0.05116 114 VAL B CB  
2088 C CG1 . VAL B 114 ? 0.35239 0.40552 0.55266 0.06111  0.06485  -0.05755 114 VAL B CG1 
2089 C CG2 . VAL B 114 ? 0.33374 0.38595 0.51818 0.02263  0.02760  -0.04586 114 VAL B CG2 
2090 N N   . SER B 115 ? 0.46456 0.34752 0.51332 0.04720  0.07926  -0.06844 115 SER B N   
2091 C CA  . SER B 115 ? 0.52869 0.37035 0.53384 0.05228  0.10456  -0.08543 115 SER B CA  
2092 C C   . SER B 115 ? 0.58757 0.45618 0.63240 0.07925  0.13600  -0.08828 115 SER B C   
2093 O O   . SER B 115 ? 0.55222 0.44745 0.64504 0.10479  0.13176  -0.08101 115 SER B O   
2094 C CB  . SER B 115 ? 0.58862 0.36750 0.55606 0.04909  0.10032  -0.10099 115 SER B CB  
2095 O OG  . SER B 115 ? 0.75487 0.51768 0.75142 0.07149  0.10814  -0.09279 115 SER B OG  
2096 N N   . ALA B 116 ? 0.58005 0.44362 0.60213 0.07762  0.16868  -0.09883 116 ALA B N   
2097 C CA  . ALA B 116 ? 0.58918 0.49614 0.66555 0.09884  0.20549  -0.10586 116 ALA B CA  
2098 C C   . ALA B 116 ? 0.69198 0.57944 0.78234 0.13689  0.21733  -0.11461 116 ALA B C   
2099 O O   . ALA B 116 ? 0.76040 0.57224 0.79258 0.14033  0.21644  -0.12292 116 ALA B O   
2100 C CB  . ALA B 116 ? 0.65448 0.54324 0.68860 0.08694  0.24900  -0.11463 116 ALA B CB  
2101 O OXT . ALA B 116 ? 0.72715 0.67525 0.89102 0.16654  0.23032  -0.11663 116 ALA B OXT 
# 
