data_8V4W
# 
_entry.id   8V4W 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   8V4W         pdb_00008v4w 10.2210/pdb8v4w/pdb 
WWPDB D_1000279433 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8V4W 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 l.zhang@unsw.edu.au          Li   Zhang        ? 'principal investigator/group leader' 0000-0001-7506-8278 
4 anna.roujeinikova@monash.edu Anna Roujeinikova ? 'principal investigator/group leader' 0000-0001-7506-8278 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Anna, R.'     1 0000-0001-8478-4751 
'Xiaotian, Z.' 2 0000-0001-9660-6637 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of Campylobacter concisus Csep1' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Anna, R.'     1 0000-0001-8478-4751 
primary 'Xiaotian, Z.' 2 0000-0001-9660-6637 
# 
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 'Secreted protein 1' 24386.799 1   ? ? ? ? 
2 non-polymer syn 'ACETIC ACID'        60.052    1   ? ? ? ? 
3 water       nat water                18.015    225 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GIDPFTWGFGGSSKEKPNYDYSADKKLIEINTRPISTDNAKYWCFDKGNDLGCLSLEKLEALESKDLKKVVKFYEKTIPE
YCYDKKFAPACNIPAIDLIQQKLSYYVRNDIDNKTIKTFYSDYAKALSESKADVKMLEYGCNELKSAYICRDLRDMYKYL
GDKEKTKEYNDKMKNGDEKWNSVLYDYKHMRYIHGGYSSWWLLEKIK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GIDPFTWGFGGSSKEKPNYDYSADKKLIEINTRPISTDNAKYWCFDKGNDLGCLSLEKLEALESKDLKKVVKFYEKTIPE
YCYDKKFAPACNIPAIDLIQQKLSYYVRNDIDNKTIKTFYSDYAKALSESKADVKMLEYGCNELKSAYICRDLRDMYKYL
GDKEKTKEYNDKMKNGDEKWNSVLYDYKHMRYIHGGYSSWWLLEKIK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ACETIC ACID' ACY 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ILE n 
1 3   ASP n 
1 4   PRO n 
1 5   PHE n 
1 6   THR n 
1 7   TRP n 
1 8   GLY n 
1 9   PHE n 
1 10  GLY n 
1 11  GLY n 
1 12  SER n 
1 13  SER n 
1 14  LYS n 
1 15  GLU n 
1 16  LYS n 
1 17  PRO n 
1 18  ASN n 
1 19  TYR n 
1 20  ASP n 
1 21  TYR n 
1 22  SER n 
1 23  ALA n 
1 24  ASP n 
1 25  LYS n 
1 26  LYS n 
1 27  LEU n 
1 28  ILE n 
1 29  GLU n 
1 30  ILE n 
1 31  ASN n 
1 32  THR n 
1 33  ARG n 
1 34  PRO n 
1 35  ILE n 
1 36  SER n 
1 37  THR n 
1 38  ASP n 
1 39  ASN n 
1 40  ALA n 
1 41  LYS n 
1 42  TYR n 
1 43  TRP n 
1 44  CYS n 
1 45  PHE n 
1 46  ASP n 
1 47  LYS n 
1 48  GLY n 
1 49  ASN n 
1 50  ASP n 
1 51  LEU n 
1 52  GLY n 
1 53  CYS n 
1 54  LEU n 
1 55  SER n 
1 56  LEU n 
1 57  GLU n 
1 58  LYS n 
1 59  LEU n 
1 60  GLU n 
1 61  ALA n 
1 62  LEU n 
1 63  GLU n 
1 64  SER n 
1 65  LYS n 
1 66  ASP n 
1 67  LEU n 
1 68  LYS n 
1 69  LYS n 
1 70  VAL n 
1 71  VAL n 
1 72  LYS n 
1 73  PHE n 
1 74  TYR n 
1 75  GLU n 
1 76  LYS n 
1 77  THR n 
1 78  ILE n 
1 79  PRO n 
1 80  GLU n 
1 81  TYR n 
1 82  CYS n 
1 83  TYR n 
1 84  ASP n 
1 85  LYS n 
1 86  LYS n 
1 87  PHE n 
1 88  ALA n 
1 89  PRO n 
1 90  ALA n 
1 91  CYS n 
1 92  ASN n 
1 93  ILE n 
1 94  PRO n 
1 95  ALA n 
1 96  ILE n 
1 97  ASP n 
1 98  LEU n 
1 99  ILE n 
1 100 GLN n 
1 101 GLN n 
1 102 LYS n 
1 103 LEU n 
1 104 SER n 
1 105 TYR n 
1 106 TYR n 
1 107 VAL n 
1 108 ARG n 
1 109 ASN n 
1 110 ASP n 
1 111 ILE n 
1 112 ASP n 
1 113 ASN n 
1 114 LYS n 
1 115 THR n 
1 116 ILE n 
1 117 LYS n 
1 118 THR n 
1 119 PHE n 
1 120 TYR n 
1 121 SER n 
1 122 ASP n 
1 123 TYR n 
1 124 ALA n 
1 125 LYS n 
1 126 ALA n 
1 127 LEU n 
1 128 SER n 
1 129 GLU n 
1 130 SER n 
1 131 LYS n 
1 132 ALA n 
1 133 ASP n 
1 134 VAL n 
1 135 LYS n 
1 136 MET n 
1 137 LEU n 
1 138 GLU n 
1 139 TYR n 
1 140 GLY n 
1 141 CYS n 
1 142 ASN n 
1 143 GLU n 
1 144 LEU n 
1 145 LYS n 
1 146 SER n 
1 147 ALA n 
1 148 TYR n 
1 149 ILE n 
1 150 CYS n 
1 151 ARG n 
1 152 ASP n 
1 153 LEU n 
1 154 ARG n 
1 155 ASP n 
1 156 MET n 
1 157 TYR n 
1 158 LYS n 
1 159 TYR n 
1 160 LEU n 
1 161 GLY n 
1 162 ASP n 
1 163 LYS n 
1 164 GLU n 
1 165 LYS n 
1 166 THR n 
1 167 LYS n 
1 168 GLU n 
1 169 TYR n 
1 170 ASN n 
1 171 ASP n 
1 172 LYS n 
1 173 MET n 
1 174 LYS n 
1 175 ASN n 
1 176 GLY n 
1 177 ASP n 
1 178 GLU n 
1 179 LYS n 
1 180 TRP n 
1 181 ASN n 
1 182 SER n 
1 183 VAL n 
1 184 LEU n 
1 185 TYR n 
1 186 ASP n 
1 187 TYR n 
1 188 LYS n 
1 189 HIS n 
1 190 MET n 
1 191 ARG n 
1 192 TYR n 
1 193 ILE n 
1 194 HIS n 
1 195 GLY n 
1 196 GLY n 
1 197 TYR n 
1 198 SER n 
1 199 SER n 
1 200 TRP n 
1 201 TRP n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 LYS n 
1 206 ILE n 
1 207 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   207 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CCS77_2074 
_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      'Campylobacter concisus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     199 
_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      'Campylobacter concisus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     199 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACY non-polymer         . 'ACETIC ACID'   ? 'C2 H4 O2'       60.052  
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   GLY 1   16  16  GLY GLY A . n 
A 1 2   ILE 2   17  17  ILE ILE A . n 
A 1 3   ASP 3   18  18  ASP ASP A . n 
A 1 4   PRO 4   19  19  PRO PRO A . n 
A 1 5   PHE 5   20  20  PHE PHE A . n 
A 1 6   THR 6   21  21  THR THR A . n 
A 1 7   TRP 7   22  22  TRP TRP A . n 
A 1 8   GLY 8   23  23  GLY GLY A . n 
A 1 9   PHE 9   24  24  PHE PHE A . n 
A 1 10  GLY 10  25  25  GLY GLY A . n 
A 1 11  GLY 11  26  26  GLY GLY A . n 
A 1 12  SER 12  27  27  SER SER A . n 
A 1 13  SER 13  28  28  SER SER A . n 
A 1 14  LYS 14  29  29  LYS LYS A . n 
A 1 15  GLU 15  30  30  GLU GLU A . n 
A 1 16  LYS 16  31  31  LYS LYS A . n 
A 1 17  PRO 17  32  32  PRO PRO A . n 
A 1 18  ASN 18  33  33  ASN ASN A . n 
A 1 19  TYR 19  34  34  TYR TYR A . n 
A 1 20  ASP 20  35  35  ASP ASP A . n 
A 1 21  TYR 21  36  36  TYR TYR A . n 
A 1 22  SER 22  37  37  SER SER A . n 
A 1 23  ALA 23  38  38  ALA ALA A . n 
A 1 24  ASP 24  39  39  ASP ASP A . n 
A 1 25  LYS 25  40  40  LYS LYS A . n 
A 1 26  LYS 26  41  41  LYS LYS A . n 
A 1 27  LEU 27  42  42  LEU LEU A . n 
A 1 28  ILE 28  43  43  ILE ILE A . n 
A 1 29  GLU 29  44  44  GLU GLU A . n 
A 1 30  ILE 30  45  45  ILE ILE A . n 
A 1 31  ASN 31  46  46  ASN ASN A . n 
A 1 32  THR 32  47  47  THR THR A . n 
A 1 33  ARG 33  48  48  ARG ARG A . n 
A 1 34  PRO 34  49  49  PRO PRO A . n 
A 1 35  ILE 35  50  50  ILE ILE A . n 
A 1 36  SER 36  51  51  SER SER A . n 
A 1 37  THR 37  52  52  THR THR A . n 
A 1 38  ASP 38  53  53  ASP ASP A . n 
A 1 39  ASN 39  54  54  ASN ASN A . n 
A 1 40  ALA 40  55  55  ALA ALA A . n 
A 1 41  LYS 41  56  56  LYS LYS A . n 
A 1 42  TYR 42  57  57  TYR TYR A . n 
A 1 43  TRP 43  58  58  TRP TRP A . n 
A 1 44  CYS 44  59  59  CYS CYS A . n 
A 1 45  PHE 45  60  60  PHE PHE A . n 
A 1 46  ASP 46  61  61  ASP ASP A . n 
A 1 47  LYS 47  62  62  LYS LYS A . n 
A 1 48  GLY 48  63  63  GLY GLY A . n 
A 1 49  ASN 49  64  64  ASN ASN A . n 
A 1 50  ASP 50  65  65  ASP ASP A . n 
A 1 51  LEU 51  66  66  LEU LEU A . n 
A 1 52  GLY 52  67  67  GLY GLY A . n 
A 1 53  CYS 53  68  68  CYS CYS A . n 
A 1 54  LEU 54  69  69  LEU LEU A . n 
A 1 55  SER 55  70  70  SER SER A . n 
A 1 56  LEU 56  71  71  LEU LEU A . n 
A 1 57  GLU 57  72  72  GLU GLU A . n 
A 1 58  LYS 58  73  73  LYS LYS A . n 
A 1 59  LEU 59  74  74  LEU LEU A . n 
A 1 60  GLU 60  75  75  GLU GLU A . n 
A 1 61  ALA 61  76  76  ALA ALA A . n 
A 1 62  LEU 62  77  77  LEU LEU A . n 
A 1 63  GLU 63  78  78  GLU GLU A . n 
A 1 64  SER 64  79  79  SER SER A . n 
A 1 65  LYS 65  80  80  LYS LYS A . n 
A 1 66  ASP 66  81  81  ASP ASP A . n 
A 1 67  LEU 67  82  82  LEU LEU A . n 
A 1 68  LYS 68  83  83  LYS LYS A . n 
A 1 69  LYS 69  84  84  LYS LYS A . n 
A 1 70  VAL 70  85  85  VAL VAL A . n 
A 1 71  VAL 71  86  86  VAL VAL A . n 
A 1 72  LYS 72  87  87  LYS LYS A . n 
A 1 73  PHE 73  88  88  PHE PHE A . n 
A 1 74  TYR 74  89  89  TYR TYR A . n 
A 1 75  GLU 75  90  90  GLU GLU A . n 
A 1 76  LYS 76  91  91  LYS LYS A . n 
A 1 77  THR 77  92  92  THR THR A . n 
A 1 78  ILE 78  93  93  ILE ILE A . n 
A 1 79  PRO 79  94  94  PRO PRO A . n 
A 1 80  GLU 80  95  95  GLU GLU A . n 
A 1 81  TYR 81  96  96  TYR TYR A . n 
A 1 82  CYS 82  97  97  CYS CYS A . n 
A 1 83  TYR 83  98  98  TYR TYR A . n 
A 1 84  ASP 84  99  99  ASP ASP A . n 
A 1 85  LYS 85  100 100 LYS LYS A . n 
A 1 86  LYS 86  101 101 LYS LYS A . n 
A 1 87  PHE 87  102 102 PHE PHE A . n 
A 1 88  ALA 88  103 103 ALA ALA A . n 
A 1 89  PRO 89  104 104 PRO PRO A . n 
A 1 90  ALA 90  105 105 ALA ALA A . n 
A 1 91  CYS 91  106 106 CYS CYS A . n 
A 1 92  ASN 92  107 107 ASN ASN A . n 
A 1 93  ILE 93  108 108 ILE ILE A . n 
A 1 94  PRO 94  109 109 PRO PRO A . n 
A 1 95  ALA 95  110 110 ALA ALA A . n 
A 1 96  ILE 96  111 111 ILE ILE A . n 
A 1 97  ASP 97  112 112 ASP ASP A . n 
A 1 98  LEU 98  113 113 LEU LEU A . n 
A 1 99  ILE 99  114 114 ILE ILE A . n 
A 1 100 GLN 100 115 115 GLN GLN A . n 
A 1 101 GLN 101 116 116 GLN GLN A . n 
A 1 102 LYS 102 117 117 LYS LYS A . n 
A 1 103 LEU 103 118 118 LEU LEU A . n 
A 1 104 SER 104 119 119 SER SER A . n 
A 1 105 TYR 105 120 120 TYR TYR A . n 
A 1 106 TYR 106 121 121 TYR TYR A . n 
A 1 107 VAL 107 122 122 VAL VAL A . n 
A 1 108 ARG 108 123 123 ARG ARG A . n 
A 1 109 ASN 109 124 124 ASN ASN A . n 
A 1 110 ASP 110 125 125 ASP ASP A . n 
A 1 111 ILE 111 126 126 ILE ILE A . n 
A 1 112 ASP 112 127 127 ASP ASP A . n 
A 1 113 ASN 113 128 128 ASN ASN A . n 
A 1 114 LYS 114 129 129 LYS LYS A . n 
A 1 115 THR 115 130 130 THR THR A . n 
A 1 116 ILE 116 131 131 ILE ILE A . n 
A 1 117 LYS 117 132 132 LYS LYS A . n 
A 1 118 THR 118 133 133 THR THR A . n 
A 1 119 PHE 119 134 134 PHE PHE A . n 
A 1 120 TYR 120 135 135 TYR TYR A . n 
A 1 121 SER 121 136 136 SER SER A . n 
A 1 122 ASP 122 137 137 ASP ASP A . n 
A 1 123 TYR 123 138 138 TYR TYR A . n 
A 1 124 ALA 124 139 139 ALA ALA A . n 
A 1 125 LYS 125 140 140 LYS LYS A . n 
A 1 126 ALA 126 141 141 ALA ALA A . n 
A 1 127 LEU 127 142 142 LEU LEU A . n 
A 1 128 SER 128 143 143 SER SER A . n 
A 1 129 GLU 129 144 144 GLU GLU A . n 
A 1 130 SER 130 145 145 SER SER A . n 
A 1 131 LYS 131 146 146 LYS LYS A . n 
A 1 132 ALA 132 147 147 ALA ALA A . n 
A 1 133 ASP 133 148 148 ASP ASP A . n 
A 1 134 VAL 134 149 149 VAL VAL A . n 
A 1 135 LYS 135 150 150 LYS LYS A . n 
A 1 136 MET 136 151 151 MET MET A . n 
A 1 137 LEU 137 152 152 LEU LEU A . n 
A 1 138 GLU 138 153 153 GLU GLU A . n 
A 1 139 TYR 139 154 154 TYR TYR A . n 
A 1 140 GLY 140 155 155 GLY GLY A . n 
A 1 141 CYS 141 156 156 CYS CYS A . n 
A 1 142 ASN 142 157 157 ASN ASN A . n 
A 1 143 GLU 143 158 158 GLU GLU A . n 
A 1 144 LEU 144 159 159 LEU LEU A . n 
A 1 145 LYS 145 160 160 LYS LYS A . n 
A 1 146 SER 146 161 161 SER SER A . n 
A 1 147 ALA 147 162 162 ALA ALA A . n 
A 1 148 TYR 148 163 163 TYR TYR A . n 
A 1 149 ILE 149 164 164 ILE ILE A . n 
A 1 150 CYS 150 165 165 CYS CYS A . n 
A 1 151 ARG 151 166 166 ARG ARG A . n 
A 1 152 ASP 152 167 167 ASP ASP A . n 
A 1 153 LEU 153 168 168 LEU LEU A . n 
A 1 154 ARG 154 169 169 ARG ARG A . n 
A 1 155 ASP 155 170 170 ASP ASP A . n 
A 1 156 MET 156 171 171 MET MET A . n 
A 1 157 TYR 157 172 172 TYR TYR A . n 
A 1 158 LYS 158 173 173 LYS LYS A . n 
A 1 159 TYR 159 174 174 TYR TYR A . n 
A 1 160 LEU 160 175 175 LEU LEU A . n 
A 1 161 GLY 161 176 176 GLY GLY A . n 
A 1 162 ASP 162 177 177 ASP ASP A . n 
A 1 163 LYS 163 178 178 LYS LYS A . n 
A 1 164 GLU 164 179 179 GLU GLU A . n 
A 1 165 LYS 165 180 180 LYS LYS A . n 
A 1 166 THR 166 181 181 THR THR A . n 
A 1 167 LYS 167 182 182 LYS LYS A . n 
A 1 168 GLU 168 183 183 GLU GLU A . n 
A 1 169 TYR 169 184 184 TYR TYR A . n 
A 1 170 ASN 170 185 185 ASN ASN A . n 
A 1 171 ASP 171 186 186 ASP ASP A . n 
A 1 172 LYS 172 187 187 LYS LYS A . n 
A 1 173 MET 173 188 188 MET MET A . n 
A 1 174 LYS 174 189 189 LYS LYS A . n 
A 1 175 ASN 175 190 190 ASN ASN A . n 
A 1 176 GLY 176 191 191 GLY GLY A . n 
A 1 177 ASP 177 192 192 ASP ASP A . n 
A 1 178 GLU 178 193 193 GLU GLU A . n 
A 1 179 LYS 179 194 194 LYS LYS A . n 
A 1 180 TRP 180 195 195 TRP TRP A . n 
A 1 181 ASN 181 196 196 ASN ASN A . n 
A 1 182 SER 182 197 197 SER SER A . n 
A 1 183 VAL 183 198 198 VAL VAL A . n 
A 1 184 LEU 184 199 199 LEU LEU A . n 
A 1 185 TYR 185 200 200 TYR TYR A . n 
A 1 186 ASP 186 201 201 ASP ASP A . n 
A 1 187 TYR 187 202 202 TYR TYR A . n 
A 1 188 LYS 188 203 203 LYS LYS A . n 
A 1 189 HIS 189 204 204 HIS HIS A . n 
A 1 190 MET 190 205 205 MET MET A . n 
A 1 191 ARG 191 206 206 ARG ARG A . n 
A 1 192 TYR 192 207 207 TYR TYR A . n 
A 1 193 ILE 193 208 208 ILE ILE A . n 
A 1 194 HIS 194 209 209 HIS HIS A . n 
A 1 195 GLY 195 210 210 GLY GLY A . n 
A 1 196 GLY 196 211 211 GLY GLY A . n 
A 1 197 TYR 197 212 212 TYR TYR A . n 
A 1 198 SER 198 213 213 SER SER A . n 
A 1 199 SER 199 214 214 SER SER A . n 
A 1 200 TRP 200 215 215 TRP TRP A . n 
A 1 201 TRP 201 216 216 TRP TRP A . n 
A 1 202 LEU 202 217 217 LEU LEU A . n 
A 1 203 LEU 203 218 218 LEU LEU A . n 
A 1 204 GLU 204 219 219 GLU GLU A . n 
A 1 205 LYS 205 220 220 LYS LYS A . n 
A 1 206 ILE 206 221 221 ILE ILE A . n 
A 1 207 LYS 207 222 222 LYS LYS A . 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 
B 2 ACY 1   301 425 ACY ACY A . 
C 3 HOH 1   401 203 HOH HOH A . 
C 3 HOH 2   402 148 HOH HOH A . 
C 3 HOH 3   403 145 HOH HOH A . 
C 3 HOH 4   404 205 HOH HOH A . 
C 3 HOH 5   405 207 HOH HOH A . 
C 3 HOH 6   406 217 HOH HOH A . 
C 3 HOH 7   407 131 HOH HOH A . 
C 3 HOH 8   408 97  HOH HOH A . 
C 3 HOH 9   409 187 HOH HOH A . 
C 3 HOH 10  410 17  HOH HOH A . 
C 3 HOH 11  411 158 HOH HOH A . 
C 3 HOH 12  412 93  HOH HOH A . 
C 3 HOH 13  413 32  HOH HOH A . 
C 3 HOH 14  414 114 HOH HOH A . 
C 3 HOH 15  415 220 HOH HOH A . 
C 3 HOH 16  416 58  HOH HOH A . 
C 3 HOH 17  417 184 HOH HOH A . 
C 3 HOH 18  418 112 HOH HOH A . 
C 3 HOH 19  419 64  HOH HOH A . 
C 3 HOH 20  420 86  HOH HOH A . 
C 3 HOH 21  421 43  HOH HOH A . 
C 3 HOH 22  422 57  HOH HOH A . 
C 3 HOH 23  423 71  HOH HOH A . 
C 3 HOH 24  424 113 HOH HOH A . 
C 3 HOH 25  425 138 HOH HOH A . 
C 3 HOH 26  426 99  HOH HOH A . 
C 3 HOH 27  427 2   HOH HOH A . 
C 3 HOH 28  428 109 HOH HOH A . 
C 3 HOH 29  429 9   HOH HOH A . 
C 3 HOH 30  430 212 HOH HOH A . 
C 3 HOH 31  431 84  HOH HOH A . 
C 3 HOH 32  432 151 HOH HOH A . 
C 3 HOH 33  433 224 HOH HOH A . 
C 3 HOH 34  434 30  HOH HOH A . 
C 3 HOH 35  435 98  HOH HOH A . 
C 3 HOH 36  436 196 HOH HOH A . 
C 3 HOH 37  437 102 HOH HOH A . 
C 3 HOH 38  438 15  HOH HOH A . 
C 3 HOH 39  439 77  HOH HOH A . 
C 3 HOH 40  440 115 HOH HOH A . 
C 3 HOH 41  441 22  HOH HOH A . 
C 3 HOH 42  442 20  HOH HOH A . 
C 3 HOH 43  443 28  HOH HOH A . 
C 3 HOH 44  444 11  HOH HOH A . 
C 3 HOH 45  445 87  HOH HOH A . 
C 3 HOH 46  446 111 HOH HOH A . 
C 3 HOH 47  447 10  HOH HOH A . 
C 3 HOH 48  448 85  HOH HOH A . 
C 3 HOH 49  449 51  HOH HOH A . 
C 3 HOH 50  450 69  HOH HOH A . 
C 3 HOH 51  451 143 HOH HOH A . 
C 3 HOH 52  452 27  HOH HOH A . 
C 3 HOH 53  453 14  HOH HOH A . 
C 3 HOH 54  454 47  HOH HOH A . 
C 3 HOH 55  455 186 HOH HOH A . 
C 3 HOH 56  456 68  HOH HOH A . 
C 3 HOH 57  457 107 HOH HOH A . 
C 3 HOH 58  458 29  HOH HOH A . 
C 3 HOH 59  459 83  HOH HOH A . 
C 3 HOH 60  460 8   HOH HOH A . 
C 3 HOH 61  461 105 HOH HOH A . 
C 3 HOH 62  462 6   HOH HOH A . 
C 3 HOH 63  463 46  HOH HOH A . 
C 3 HOH 64  464 146 HOH HOH A . 
C 3 HOH 65  465 19  HOH HOH A . 
C 3 HOH 66  466 33  HOH HOH A . 
C 3 HOH 67  467 4   HOH HOH A . 
C 3 HOH 68  468 126 HOH HOH A . 
C 3 HOH 69  469 73  HOH HOH A . 
C 3 HOH 70  470 31  HOH HOH A . 
C 3 HOH 71  471 55  HOH HOH A . 
C 3 HOH 72  472 48  HOH HOH A . 
C 3 HOH 73  473 34  HOH HOH A . 
C 3 HOH 74  474 65  HOH HOH A . 
C 3 HOH 75  475 42  HOH HOH A . 
C 3 HOH 76  476 24  HOH HOH A . 
C 3 HOH 77  477 67  HOH HOH A . 
C 3 HOH 78  478 36  HOH HOH A . 
C 3 HOH 79  479 92  HOH HOH A . 
C 3 HOH 80  480 26  HOH HOH A . 
C 3 HOH 81  481 5   HOH HOH A . 
C 3 HOH 82  482 7   HOH HOH A . 
C 3 HOH 83  483 56  HOH HOH A . 
C 3 HOH 84  484 119 HOH HOH A . 
C 3 HOH 85  485 128 HOH HOH A . 
C 3 HOH 86  486 62  HOH HOH A . 
C 3 HOH 87  487 52  HOH HOH A . 
C 3 HOH 88  488 40  HOH HOH A . 
C 3 HOH 89  489 3   HOH HOH A . 
C 3 HOH 90  490 137 HOH HOH A . 
C 3 HOH 91  491 91  HOH HOH A . 
C 3 HOH 92  492 70  HOH HOH A . 
C 3 HOH 93  493 118 HOH HOH A . 
C 3 HOH 94  494 90  HOH HOH A . 
C 3 HOH 95  495 185 HOH HOH A . 
C 3 HOH 96  496 95  HOH HOH A . 
C 3 HOH 97  497 37  HOH HOH A . 
C 3 HOH 98  498 173 HOH HOH A . 
C 3 HOH 99  499 41  HOH HOH A . 
C 3 HOH 100 500 202 HOH HOH A . 
C 3 HOH 101 501 79  HOH HOH A . 
C 3 HOH 102 502 54  HOH HOH A . 
C 3 HOH 103 503 78  HOH HOH A . 
C 3 HOH 104 504 164 HOH HOH A . 
C 3 HOH 105 505 18  HOH HOH A . 
C 3 HOH 106 506 35  HOH HOH A . 
C 3 HOH 107 507 108 HOH HOH A . 
C 3 HOH 108 508 110 HOH HOH A . 
C 3 HOH 109 509 38  HOH HOH A . 
C 3 HOH 110 510 76  HOH HOH A . 
C 3 HOH 111 511 1   HOH HOH A . 
C 3 HOH 112 512 61  HOH HOH A . 
C 3 HOH 113 513 13  HOH HOH A . 
C 3 HOH 114 514 213 HOH HOH A . 
C 3 HOH 115 515 23  HOH HOH A . 
C 3 HOH 116 516 154 HOH HOH A . 
C 3 HOH 117 517 210 HOH HOH A . 
C 3 HOH 118 518 104 HOH HOH A . 
C 3 HOH 119 519 16  HOH HOH A . 
C 3 HOH 120 520 12  HOH HOH A . 
C 3 HOH 121 521 206 HOH HOH A . 
C 3 HOH 122 522 188 HOH HOH A . 
C 3 HOH 123 523 49  HOH HOH A . 
C 3 HOH 124 524 63  HOH HOH A . 
C 3 HOH 125 525 72  HOH HOH A . 
C 3 HOH 126 526 44  HOH HOH A . 
C 3 HOH 127 527 53  HOH HOH A . 
C 3 HOH 128 528 60  HOH HOH A . 
C 3 HOH 129 529 96  HOH HOH A . 
C 3 HOH 130 530 189 HOH HOH A . 
C 3 HOH 131 531 81  HOH HOH A . 
C 3 HOH 132 532 75  HOH HOH A . 
C 3 HOH 133 533 191 HOH HOH A . 
C 3 HOH 134 534 155 HOH HOH A . 
C 3 HOH 135 535 209 HOH HOH A . 
C 3 HOH 136 536 117 HOH HOH A . 
C 3 HOH 137 537 45  HOH HOH A . 
C 3 HOH 138 538 129 HOH HOH A . 
C 3 HOH 139 539 80  HOH HOH A . 
C 3 HOH 140 540 88  HOH HOH A . 
C 3 HOH 141 541 74  HOH HOH A . 
C 3 HOH 142 542 152 HOH HOH A . 
C 3 HOH 143 543 168 HOH HOH A . 
C 3 HOH 144 544 163 HOH HOH A . 
C 3 HOH 145 545 94  HOH HOH A . 
C 3 HOH 146 546 140 HOH HOH A . 
C 3 HOH 147 547 194 HOH HOH A . 
C 3 HOH 148 548 66  HOH HOH A . 
C 3 HOH 149 549 89  HOH HOH A . 
C 3 HOH 150 550 197 HOH HOH A . 
C 3 HOH 151 551 59  HOH HOH A . 
C 3 HOH 152 552 157 HOH HOH A . 
C 3 HOH 153 553 39  HOH HOH A . 
C 3 HOH 154 554 193 HOH HOH A . 
C 3 HOH 155 555 116 HOH HOH A . 
C 3 HOH 156 556 221 HOH HOH A . 
C 3 HOH 157 557 156 HOH HOH A . 
C 3 HOH 158 558 106 HOH HOH A . 
C 3 HOH 159 559 179 HOH HOH A . 
C 3 HOH 160 560 101 HOH HOH A . 
C 3 HOH 161 561 103 HOH HOH A . 
C 3 HOH 162 562 170 HOH HOH A . 
C 3 HOH 163 563 198 HOH HOH A . 
C 3 HOH 164 564 135 HOH HOH A . 
C 3 HOH 165 565 182 HOH HOH A . 
C 3 HOH 166 566 21  HOH HOH A . 
C 3 HOH 167 567 141 HOH HOH A . 
C 3 HOH 168 568 50  HOH HOH A . 
C 3 HOH 169 569 211 HOH HOH A . 
C 3 HOH 170 570 144 HOH HOH A . 
C 3 HOH 171 571 136 HOH HOH A . 
C 3 HOH 172 572 82  HOH HOH A . 
C 3 HOH 173 573 25  HOH HOH A . 
C 3 HOH 174 574 172 HOH HOH A . 
C 3 HOH 175 575 149 HOH HOH A . 
C 3 HOH 176 576 100 HOH HOH A . 
C 3 HOH 177 577 166 HOH HOH A . 
C 3 HOH 178 578 195 HOH HOH A . 
C 3 HOH 179 579 215 HOH HOH A . 
C 3 HOH 180 580 165 HOH HOH A . 
C 3 HOH 181 581 127 HOH HOH A . 
C 3 HOH 182 582 124 HOH HOH A . 
C 3 HOH 183 583 201 HOH HOH A . 
C 3 HOH 184 584 176 HOH HOH A . 
C 3 HOH 185 585 133 HOH HOH A . 
C 3 HOH 186 586 134 HOH HOH A . 
C 3 HOH 187 587 167 HOH HOH A . 
C 3 HOH 188 588 130 HOH HOH A . 
C 3 HOH 189 589 159 HOH HOH A . 
C 3 HOH 190 590 181 HOH HOH A . 
C 3 HOH 191 591 162 HOH HOH A . 
C 3 HOH 192 592 147 HOH HOH A . 
C 3 HOH 193 593 214 HOH HOH A . 
C 3 HOH 194 594 121 HOH HOH A . 
C 3 HOH 195 595 190 HOH HOH A . 
C 3 HOH 196 596 218 HOH HOH A . 
C 3 HOH 197 597 122 HOH HOH A . 
C 3 HOH 198 598 120 HOH HOH A . 
C 3 HOH 199 599 139 HOH HOH A . 
C 3 HOH 200 600 180 HOH HOH A . 
C 3 HOH 201 601 204 HOH HOH A . 
C 3 HOH 202 602 199 HOH HOH A . 
C 3 HOH 203 603 169 HOH HOH A . 
C 3 HOH 204 604 225 HOH HOH A . 
C 3 HOH 205 605 175 HOH HOH A . 
C 3 HOH 206 606 153 HOH HOH A . 
C 3 HOH 207 607 132 HOH HOH A . 
C 3 HOH 208 608 150 HOH HOH A . 
C 3 HOH 209 609 160 HOH HOH A . 
C 3 HOH 210 610 123 HOH HOH A . 
C 3 HOH 211 611 161 HOH HOH A . 
C 3 HOH 212 612 208 HOH HOH A . 
C 3 HOH 213 613 177 HOH HOH A . 
C 3 HOH 214 614 192 HOH HOH A . 
C 3 HOH 215 615 222 HOH HOH A . 
C 3 HOH 216 616 219 HOH HOH A . 
C 3 HOH 217 617 171 HOH HOH A . 
C 3 HOH 218 618 216 HOH HOH A . 
C 3 HOH 219 619 178 HOH HOH A . 
C 3 HOH 220 620 223 HOH HOH A . 
C 3 HOH 221 621 200 HOH HOH A . 
C 3 HOH 222 622 125 HOH HOH A . 
C 3 HOH 223 623 142 HOH HOH A . 
C 3 HOH 224 624 183 HOH HOH A . 
C 3 HOH 225 625 174 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .        1 
? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless   ? ? ? .        2 
? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .        3 
? refinement     ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? 5.8.0419 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8V4W 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.792 
_cell.length_a_esd                 ? 
_cell.length_b                     85.792 
_cell.length_b_esd                 ? 
_cell.length_c                     55.194 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8V4W 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                172 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 64' 
_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                   8V4W 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.40 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.84 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '25% w/v PEG 4000, 100 mM ammonium acetate, 80 mM sodium acetate trihydrate (pH 4.6)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-08-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.07 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.07 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8V4W 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.40 
_reflns.d_resolution_low                               25.00 
_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                                     43067 
_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                           94.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.030 
_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                                    1.40 
_reflns_shell.d_res_low                                     1.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             43067 
_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                                  0.99 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.18 
_refine.aniso_B[1][2]                            0.09 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.18 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.58 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.505 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.982 
_refine.correlation_coeff_Fo_to_Fc_free          0.971 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8V4W 
_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                            1.40 
_refine.ls_d_res_low                             25.00 
_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                     40838 
_refine.ls_number_reflns_R_free                  2218 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.18 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.12852 
_refine.ls_R_factor_R_free                       0.16679 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.12639 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'AB INITIO PHASING' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.053 
_refine.pdbx_overall_ESU_R_Free                  0.053 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.971 
_refine.overall_SU_ML                            0.034 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        25.00 
_refine_hist.number_atoms_solvent             225 
_refine_hist.number_atoms_total               1943 
_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        1714 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_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' ? 0.012  0.012  1762 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1641 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.769  1.853  2369 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.618  1.813  3817 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.683  5.000  206  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 3.337  5.000  5    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.264 10.000 337  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.098  0.200  238  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  2003 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  391  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 7.457  2.649  828  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 7.385  2.645  827  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 9.972  4.770  1032 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 9.979  4.777  1033 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.471 3.084  934  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 10.467 3.086  935  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 14.408 5.447  1338 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 19.535 32.08  2181 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 18.521 29.30  2130 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 4.165  3.000  3403 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.40 
_refine_ls_shell.d_res_low                        1.42 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             110 
_refine_ls_shell.number_reflns_R_work             2056 
_refine_ls_shell.percent_reflns_obs               64.56 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.295 
_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                  0.333 
# 
_struct.entry_id                     8V4W 
_struct.title                        'Crystal structure of Campylobacter concisus Csep1' 
_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        8V4W 
_struct_keywords.text            'cysteine rich protein, UNKNOWN FUNCTION' 
_struct_keywords.pdbx_keywords   'UNKNOWN FUNCTION' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2R4P333_9BACT 
_struct_ref.pdbx_db_accession          A0A2R4P333 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;WGFGGSSKEKPNYDYSADKKLIEINTRPISTDNAKYWCFDKGNDLGCLSLEKLEALESKDLKKVVKFYEKTIPEYCYDKK
FAPACNIPAIDLIQQKLSYYVRNDIDNKTIKTFYSDYAKALSESKADVKMLEYGCNELKSAYICRDLRDMYKYLGDKEKT
KEYNDKMKNGDEKWNSVLYDYKHMRYIHGGYSSWWLLEKIK
;
_struct_ref.pdbx_align_begin           22 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8V4W 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 7 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 207 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A2R4P333 
_struct_ref_seq.db_align_beg                  22 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  222 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       22 
_struct_ref_seq.pdbx_auth_seq_align_end       222 
# 
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 8V4W GLY A 1 ? UNP A0A2R4P333 ? ? 'expression tag' 16 1 
1 8V4W ILE A 2 ? UNP A0A2R4P333 ? ? 'expression tag' 17 2 
1 8V4W ASP A 3 ? UNP A0A2R4P333 ? ? 'expression tag' 18 3 
1 8V4W PRO A 4 ? UNP A0A2R4P333 ? ? 'expression tag' 19 4 
1 8V4W PHE A 5 ? UNP A0A2R4P333 ? ? 'expression tag' 20 5 
1 8V4W THR A 6 ? UNP A0A2R4P333 ? ? 'expression tag' 21 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  11870 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 ASP A 3   ? PHE A 9   ? ASP A 18  PHE A 24  5 ? 7  
HELX_P HELX_P2  AA2 TYR A 21  ? ASN A 31  ? TYR A 36  ASN A 46  1 ? 11 
HELX_P HELX_P3  AA3 THR A 37  ? PHE A 45  ? THR A 52  PHE A 60  1 ? 9  
HELX_P HELX_P4  AA4 ASN A 49  ? LYS A 65  ? ASN A 64  LYS A 80  1 ? 17 
HELX_P HELX_P5  AA5 ASP A 66  ? LYS A 76  ? ASP A 81  LYS A 91  1 ? 11 
HELX_P HELX_P6  AA6 LYS A 76  ? TYR A 83  ? LYS A 91  TYR A 98  1 ? 8  
HELX_P HELX_P7  AA7 PHE A 87  ? CYS A 91  ? PHE A 102 CYS A 106 5 ? 5  
HELX_P HELX_P8  AA8 ASN A 92  ? ILE A 99  ? ASN A 107 ILE A 114 1 ? 8  
HELX_P HELX_P9  AA9 ILE A 99  ? ASN A 109 ? ILE A 114 ASN A 124 1 ? 11 
HELX_P HELX_P10 AB1 THR A 115 ? SER A 130 ? THR A 130 SER A 145 1 ? 16 
HELX_P HELX_P11 AB2 SER A 130 ? GLU A 143 ? SER A 145 GLU A 158 1 ? 14 
HELX_P HELX_P12 AB3 SER A 146 ? GLY A 161 ? SER A 161 GLY A 176 1 ? 16 
HELX_P HELX_P13 AB4 ASP A 162 ? LYS A 174 ? ASP A 177 LYS A 189 1 ? 13 
HELX_P HELX_P14 AB5 ASN A 175 ? GLY A 176 ? ASN A 190 GLY A 191 5 ? 2  
HELX_P HELX_P15 AB6 ASP A 177 ? ASN A 181 ? ASP A 192 ASN A 196 5 ? 5  
HELX_P HELX_P16 AB7 SER A 182 ? ASP A 186 ? SER A 197 ASP A 201 5 ? 5  
HELX_P HELX_P17 AB8 SER A 198 ? LEU A 203 ? SER A 213 LEU A 218 1 ? 6  
HELX_P HELX_P18 AB9 GLU A 204 ? ILE A 206 ? GLU A 219 ILE A 221 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 44  SG ? ? ? 1_555 A CYS 53  SG ? ? A CYS 59  A CYS 68  1_555 ? ? ? ? ? ? ? 2.255 ? ? 
disulf2 disulf ? ? A CYS 82  SG ? ? ? 1_555 A CYS 91  SG ? ? A CYS 97  A CYS 106 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
disulf3 disulf ? ? A CYS 141 SG ? ? ? 1_555 A CYS 150 SG ? ? A CYS 156 A CYS 165 1_555 ? ? ? ? ? ? ? 2.246 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 44  ? CYS A 53  ? CYS A 59  ? 1_555 CYS A 68  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 82  ? CYS A 91  ? CYS A 97  ? 1_555 CYS A 106 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 141 ? CYS A 150 ? CYS A 156 ? 1_555 CYS A 165 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_pdbx_entry_details.entry_id                   8V4W 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 SD A MET 205 ? ? O A HOH 616 ? ? 1.83 
2 1 O  A HOH 419 ? ? O A HOH 587 ? ? 1.91 
3 1 CG A ASN 185 ? ? O A HOH 401 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLU 
_pdbx_validate_symm_contact.auth_seq_id_1     144 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OE2 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    GLU 
_pdbx_validate_symm_contact.auth_seq_id_2     144 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_455 
_pdbx_validate_symm_contact.dist              2.16 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ILE 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     114 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -122.93 
_pdbx_validate_torsion.psi             -63.62 
# 
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 
ACY C    C N N 1   
ACY O    O N N 2   
ACY OXT  O N N 3   
ACY CH3  C N N 4   
ACY HXT  H N N 5   
ACY H1   H N N 6   
ACY H2   H N N 7   
ACY H3   H N N 8   
ALA N    N N N 9   
ALA CA   C N S 10  
ALA C    C N N 11  
ALA O    O N N 12  
ALA CB   C N N 13  
ALA OXT  O N N 14  
ALA H    H N N 15  
ALA H2   H N N 16  
ALA HA   H N N 17  
ALA HB1  H N N 18  
ALA HB2  H N N 19  
ALA HB3  H N N 20  
ALA HXT  H N N 21  
ARG N    N N N 22  
ARG CA   C N S 23  
ARG C    C N N 24  
ARG O    O N N 25  
ARG CB   C N N 26  
ARG CG   C N N 27  
ARG CD   C N N 28  
ARG NE   N N N 29  
ARG CZ   C N N 30  
ARG NH1  N N N 31  
ARG NH2  N N N 32  
ARG OXT  O N N 33  
ARG H    H N N 34  
ARG H2   H N N 35  
ARG HA   H N N 36  
ARG HB2  H N N 37  
ARG HB3  H N N 38  
ARG HG2  H N N 39  
ARG HG3  H N N 40  
ARG HD2  H N N 41  
ARG HD3  H N N 42  
ARG HE   H N N 43  
ARG HH11 H N N 44  
ARG HH12 H N N 45  
ARG HH21 H N N 46  
ARG HH22 H N N 47  
ARG HXT  H N N 48  
ASN N    N N N 49  
ASN CA   C N S 50  
ASN C    C N N 51  
ASN O    O N N 52  
ASN CB   C N N 53  
ASN CG   C N N 54  
ASN OD1  O N N 55  
ASN ND2  N N N 56  
ASN OXT  O N N 57  
ASN H    H N N 58  
ASN H2   H N N 59  
ASN HA   H N N 60  
ASN HB2  H N N 61  
ASN HB3  H N N 62  
ASN HD21 H N N 63  
ASN HD22 H N N 64  
ASN HXT  H N N 65  
ASP N    N N N 66  
ASP CA   C N S 67  
ASP C    C N N 68  
ASP O    O N N 69  
ASP CB   C N N 70  
ASP CG   C N N 71  
ASP OD1  O N N 72  
ASP OD2  O N N 73  
ASP OXT  O N N 74  
ASP H    H N N 75  
ASP H2   H N N 76  
ASP HA   H N N 77  
ASP HB2  H N N 78  
ASP HB3  H N N 79  
ASP HD2  H N N 80  
ASP HXT  H N N 81  
CYS N    N N N 82  
CYS CA   C N R 83  
CYS C    C N N 84  
CYS O    O N N 85  
CYS CB   C N N 86  
CYS SG   S N N 87  
CYS OXT  O N N 88  
CYS H    H N N 89  
CYS H2   H N N 90  
CYS HA   H N N 91  
CYS HB2  H N N 92  
CYS HB3  H N N 93  
CYS HG   H N N 94  
CYS HXT  H N N 95  
GLN N    N N N 96  
GLN CA   C N S 97  
GLN C    C N N 98  
GLN O    O N N 99  
GLN CB   C N N 100 
GLN CG   C N N 101 
GLN CD   C N N 102 
GLN OE1  O N N 103 
GLN NE2  N N N 104 
GLN OXT  O N N 105 
GLN H    H N N 106 
GLN H2   H N N 107 
GLN HA   H N N 108 
GLN HB2  H N N 109 
GLN HB3  H N N 110 
GLN HG2  H N N 111 
GLN HG3  H N N 112 
GLN HE21 H N N 113 
GLN HE22 H N N 114 
GLN HXT  H N N 115 
GLU N    N N N 116 
GLU CA   C N S 117 
GLU C    C N N 118 
GLU O    O N N 119 
GLU CB   C N N 120 
GLU CG   C N N 121 
GLU CD   C N N 122 
GLU OE1  O N N 123 
GLU OE2  O N N 124 
GLU OXT  O N N 125 
GLU H    H N N 126 
GLU H2   H N N 127 
GLU HA   H N N 128 
GLU HB2  H N N 129 
GLU HB3  H N N 130 
GLU HG2  H N N 131 
GLU HG3  H N N 132 
GLU HE2  H N N 133 
GLU HXT  H N N 134 
GLY N    N N N 135 
GLY CA   C N N 136 
GLY C    C N N 137 
GLY O    O N N 138 
GLY OXT  O N N 139 
GLY H    H N N 140 
GLY H2   H N N 141 
GLY HA2  H N N 142 
GLY HA3  H N N 143 
GLY HXT  H N N 144 
HIS N    N N N 145 
HIS CA   C N S 146 
HIS C    C N N 147 
HIS O    O N N 148 
HIS CB   C N N 149 
HIS CG   C Y N 150 
HIS ND1  N Y N 151 
HIS CD2  C Y N 152 
HIS CE1  C Y N 153 
HIS NE2  N Y N 154 
HIS OXT  O N N 155 
HIS H    H N N 156 
HIS H2   H N N 157 
HIS HA   H N N 158 
HIS HB2  H N N 159 
HIS HB3  H N N 160 
HIS HD1  H N N 161 
HIS HD2  H N N 162 
HIS HE1  H N N 163 
HIS HE2  H N N 164 
HIS HXT  H N N 165 
HOH O    O N N 166 
HOH H1   H N N 167 
HOH H2   H N N 168 
ILE N    N N N 169 
ILE CA   C N S 170 
ILE C    C N N 171 
ILE O    O N N 172 
ILE CB   C N S 173 
ILE CG1  C N N 174 
ILE CG2  C N N 175 
ILE CD1  C N N 176 
ILE OXT  O N N 177 
ILE H    H N N 178 
ILE H2   H N N 179 
ILE HA   H N N 180 
ILE HB   H N N 181 
ILE HG12 H N N 182 
ILE HG13 H N N 183 
ILE HG21 H N N 184 
ILE HG22 H N N 185 
ILE HG23 H N N 186 
ILE HD11 H N N 187 
ILE HD12 H N N 188 
ILE HD13 H N N 189 
ILE HXT  H N N 190 
LEU N    N N N 191 
LEU CA   C N S 192 
LEU C    C N N 193 
LEU O    O N N 194 
LEU CB   C N N 195 
LEU CG   C N N 196 
LEU CD1  C N N 197 
LEU CD2  C N N 198 
LEU OXT  O N N 199 
LEU H    H N N 200 
LEU H2   H N N 201 
LEU HA   H N N 202 
LEU HB2  H N N 203 
LEU HB3  H N N 204 
LEU HG   H N N 205 
LEU HD11 H N N 206 
LEU HD12 H N N 207 
LEU HD13 H N N 208 
LEU HD21 H N N 209 
LEU HD22 H N N 210 
LEU HD23 H N N 211 
LEU HXT  H N N 212 
LYS N    N N N 213 
LYS CA   C N S 214 
LYS C    C N N 215 
LYS O    O N N 216 
LYS CB   C N N 217 
LYS CG   C N N 218 
LYS CD   C N N 219 
LYS CE   C N N 220 
LYS NZ   N N N 221 
LYS OXT  O N N 222 
LYS H    H N N 223 
LYS H2   H N N 224 
LYS HA   H N N 225 
LYS HB2  H N N 226 
LYS HB3  H N N 227 
LYS HG2  H N N 228 
LYS HG3  H N N 229 
LYS HD2  H N N 230 
LYS HD3  H N N 231 
LYS HE2  H N N 232 
LYS HE3  H N N 233 
LYS HZ1  H N N 234 
LYS HZ2  H N N 235 
LYS HZ3  H N N 236 
LYS HXT  H N N 237 
MET N    N N N 238 
MET CA   C N S 239 
MET C    C N N 240 
MET O    O N N 241 
MET CB   C N N 242 
MET CG   C N N 243 
MET SD   S N N 244 
MET CE   C N N 245 
MET OXT  O N N 246 
MET H    H N N 247 
MET H2   H N N 248 
MET HA   H N N 249 
MET HB2  H N N 250 
MET HB3  H N N 251 
MET HG2  H N N 252 
MET HG3  H N N 253 
MET HE1  H N N 254 
MET HE2  H N N 255 
MET HE3  H N N 256 
MET HXT  H N N 257 
PHE N    N N N 258 
PHE CA   C N S 259 
PHE C    C N N 260 
PHE O    O N N 261 
PHE CB   C N N 262 
PHE CG   C Y N 263 
PHE CD1  C Y N 264 
PHE CD2  C Y N 265 
PHE CE1  C Y N 266 
PHE CE2  C Y N 267 
PHE CZ   C Y N 268 
PHE OXT  O N N 269 
PHE H    H N N 270 
PHE H2   H N N 271 
PHE HA   H N N 272 
PHE HB2  H N N 273 
PHE HB3  H N N 274 
PHE HD1  H N N 275 
PHE HD2  H N N 276 
PHE HE1  H N N 277 
PHE HE2  H N N 278 
PHE HZ   H N N 279 
PHE HXT  H N N 280 
PRO N    N N N 281 
PRO CA   C N S 282 
PRO C    C N N 283 
PRO O    O N N 284 
PRO CB   C N N 285 
PRO CG   C N N 286 
PRO CD   C N N 287 
PRO OXT  O N N 288 
PRO H    H N N 289 
PRO HA   H N N 290 
PRO HB2  H N N 291 
PRO HB3  H N N 292 
PRO HG2  H N N 293 
PRO HG3  H N N 294 
PRO HD2  H N N 295 
PRO HD3  H N N 296 
PRO HXT  H N N 297 
SER N    N N N 298 
SER CA   C N S 299 
SER C    C N N 300 
SER O    O N N 301 
SER CB   C N N 302 
SER OG   O N N 303 
SER OXT  O N N 304 
SER H    H N N 305 
SER H2   H N N 306 
SER HA   H N N 307 
SER HB2  H N N 308 
SER HB3  H N N 309 
SER HG   H N N 310 
SER HXT  H N N 311 
THR N    N N N 312 
THR CA   C N S 313 
THR C    C N N 314 
THR O    O N N 315 
THR CB   C N R 316 
THR OG1  O N N 317 
THR CG2  C N N 318 
THR OXT  O N N 319 
THR H    H N N 320 
THR H2   H N N 321 
THR HA   H N N 322 
THR HB   H N N 323 
THR HG1  H N N 324 
THR HG21 H N N 325 
THR HG22 H N N 326 
THR HG23 H N N 327 
THR HXT  H N N 328 
TRP N    N N N 329 
TRP CA   C N S 330 
TRP C    C N N 331 
TRP O    O N N 332 
TRP CB   C N N 333 
TRP CG   C Y N 334 
TRP CD1  C Y N 335 
TRP CD2  C Y N 336 
TRP NE1  N Y N 337 
TRP CE2  C Y N 338 
TRP CE3  C Y N 339 
TRP CZ2  C Y N 340 
TRP CZ3  C Y N 341 
TRP CH2  C Y N 342 
TRP OXT  O N N 343 
TRP H    H N N 344 
TRP H2   H N N 345 
TRP HA   H N N 346 
TRP HB2  H N N 347 
TRP HB3  H N N 348 
TRP HD1  H N N 349 
TRP HE1  H N N 350 
TRP HE3  H N N 351 
TRP HZ2  H N N 352 
TRP HZ3  H N N 353 
TRP HH2  H N N 354 
TRP HXT  H N N 355 
TYR N    N N N 356 
TYR CA   C N S 357 
TYR C    C N N 358 
TYR O    O N N 359 
TYR CB   C N N 360 
TYR CG   C Y N 361 
TYR CD1  C Y N 362 
TYR CD2  C Y N 363 
TYR CE1  C Y N 364 
TYR CE2  C Y N 365 
TYR CZ   C Y N 366 
TYR OH   O N N 367 
TYR OXT  O N N 368 
TYR H    H N N 369 
TYR H2   H N N 370 
TYR HA   H N N 371 
TYR HB2  H N N 372 
TYR HB3  H N N 373 
TYR HD1  H N N 374 
TYR HD2  H N N 375 
TYR HE1  H N N 376 
TYR HE2  H N N 377 
TYR HH   H N N 378 
TYR HXT  H N N 379 
VAL N    N N N 380 
VAL CA   C N S 381 
VAL C    C N N 382 
VAL O    O N N 383 
VAL CB   C N N 384 
VAL CG1  C N N 385 
VAL CG2  C N N 386 
VAL OXT  O N N 387 
VAL H    H N N 388 
VAL H2   H N N 389 
VAL HA   H N N 390 
VAL HB   H N N 391 
VAL HG11 H N N 392 
VAL HG12 H N N 393 
VAL HG13 H N N 394 
VAL HG21 H N N 395 
VAL HG22 H N N 396 
VAL HG23 H N N 397 
VAL HXT  H N N 398 
# 
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 
ACY C   O    doub N N 1   
ACY C   OXT  sing N N 2   
ACY C   CH3  sing N N 3   
ACY OXT HXT  sing N N 4   
ACY CH3 H1   sing N N 5   
ACY CH3 H2   sing N N 6   
ACY CH3 H3   sing N N 7   
ALA N   CA   sing N N 8   
ALA N   H    sing N N 9   
ALA N   H2   sing N N 10  
ALA CA  C    sing N N 11  
ALA CA  CB   sing N N 12  
ALA CA  HA   sing N N 13  
ALA C   O    doub N N 14  
ALA C   OXT  sing N N 15  
ALA CB  HB1  sing N N 16  
ALA CB  HB2  sing N N 17  
ALA CB  HB3  sing N N 18  
ALA OXT HXT  sing N N 19  
ARG N   CA   sing N N 20  
ARG N   H    sing N N 21  
ARG N   H2   sing N N 22  
ARG CA  C    sing N N 23  
ARG CA  CB   sing N N 24  
ARG CA  HA   sing N N 25  
ARG C   O    doub N N 26  
ARG C   OXT  sing N N 27  
ARG CB  CG   sing N N 28  
ARG CB  HB2  sing N N 29  
ARG CB  HB3  sing N N 30  
ARG CG  CD   sing N N 31  
ARG CG  HG2  sing N N 32  
ARG CG  HG3  sing N N 33  
ARG CD  NE   sing N N 34  
ARG CD  HD2  sing N N 35  
ARG CD  HD3  sing N N 36  
ARG NE  CZ   sing N N 37  
ARG NE  HE   sing N N 38  
ARG CZ  NH1  sing N N 39  
ARG CZ  NH2  doub N N 40  
ARG NH1 HH11 sing N N 41  
ARG NH1 HH12 sing N N 42  
ARG NH2 HH21 sing N N 43  
ARG NH2 HH22 sing N N 44  
ARG OXT HXT  sing N N 45  
ASN N   CA   sing N N 46  
ASN N   H    sing N N 47  
ASN N   H2   sing N N 48  
ASN CA  C    sing N N 49  
ASN CA  CB   sing N N 50  
ASN CA  HA   sing N N 51  
ASN C   O    doub N N 52  
ASN C   OXT  sing N N 53  
ASN CB  CG   sing N N 54  
ASN CB  HB2  sing N N 55  
ASN CB  HB3  sing N N 56  
ASN CG  OD1  doub N N 57  
ASN CG  ND2  sing N N 58  
ASN ND2 HD21 sing N N 59  
ASN ND2 HD22 sing N N 60  
ASN OXT HXT  sing N N 61  
ASP N   CA   sing N N 62  
ASP N   H    sing N N 63  
ASP N   H2   sing N N 64  
ASP CA  C    sing N N 65  
ASP CA  CB   sing N N 66  
ASP CA  HA   sing N N 67  
ASP C   O    doub N N 68  
ASP C   OXT  sing N N 69  
ASP CB  CG   sing N N 70  
ASP CB  HB2  sing N N 71  
ASP CB  HB3  sing N N 72  
ASP CG  OD1  doub N N 73  
ASP CG  OD2  sing N N 74  
ASP OD2 HD2  sing N N 75  
ASP OXT HXT  sing N N 76  
CYS N   CA   sing N N 77  
CYS N   H    sing N N 78  
CYS N   H2   sing N N 79  
CYS CA  C    sing N N 80  
CYS CA  CB   sing N N 81  
CYS CA  HA   sing N N 82  
CYS C   O    doub N N 83  
CYS C   OXT  sing N N 84  
CYS CB  SG   sing N N 85  
CYS CB  HB2  sing N N 86  
CYS CB  HB3  sing N N 87  
CYS SG  HG   sing N N 88  
CYS OXT HXT  sing N N 89  
GLN N   CA   sing N N 90  
GLN N   H    sing N N 91  
GLN N   H2   sing N N 92  
GLN CA  C    sing N N 93  
GLN CA  CB   sing N N 94  
GLN CA  HA   sing N N 95  
GLN C   O    doub N N 96  
GLN C   OXT  sing N N 97  
GLN CB  CG   sing N N 98  
GLN CB  HB2  sing N N 99  
GLN CB  HB3  sing N N 100 
GLN CG  CD   sing N N 101 
GLN CG  HG2  sing N N 102 
GLN CG  HG3  sing N N 103 
GLN CD  OE1  doub N N 104 
GLN CD  NE2  sing N N 105 
GLN NE2 HE21 sing N N 106 
GLN NE2 HE22 sing N N 107 
GLN OXT HXT  sing N N 108 
GLU N   CA   sing N N 109 
GLU N   H    sing N N 110 
GLU N   H2   sing N N 111 
GLU CA  C    sing N N 112 
GLU CA  CB   sing N N 113 
GLU CA  HA   sing N N 114 
GLU C   O    doub N N 115 
GLU C   OXT  sing N N 116 
GLU CB  CG   sing N N 117 
GLU CB  HB2  sing N N 118 
GLU CB  HB3  sing N N 119 
GLU CG  CD   sing N N 120 
GLU CG  HG2  sing N N 121 
GLU CG  HG3  sing N N 122 
GLU CD  OE1  doub N N 123 
GLU CD  OE2  sing N N 124 
GLU OE2 HE2  sing N N 125 
GLU OXT HXT  sing N N 126 
GLY N   CA   sing N N 127 
GLY N   H    sing N N 128 
GLY N   H2   sing N N 129 
GLY CA  C    sing N N 130 
GLY CA  HA2  sing N N 131 
GLY CA  HA3  sing N N 132 
GLY C   O    doub N N 133 
GLY C   OXT  sing N N 134 
GLY OXT HXT  sing N N 135 
HIS N   CA   sing N N 136 
HIS N   H    sing N N 137 
HIS N   H2   sing N N 138 
HIS CA  C    sing N N 139 
HIS CA  CB   sing N N 140 
HIS CA  HA   sing N N 141 
HIS C   O    doub N N 142 
HIS C   OXT  sing N N 143 
HIS CB  CG   sing N N 144 
HIS CB  HB2  sing N N 145 
HIS CB  HB3  sing N N 146 
HIS CG  ND1  sing Y N 147 
HIS CG  CD2  doub Y N 148 
HIS ND1 CE1  doub Y N 149 
HIS ND1 HD1  sing N N 150 
HIS CD2 NE2  sing Y N 151 
HIS CD2 HD2  sing N N 152 
HIS CE1 NE2  sing Y N 153 
HIS CE1 HE1  sing N N 154 
HIS NE2 HE2  sing N N 155 
HIS OXT HXT  sing N N 156 
HOH O   H1   sing N N 157 
HOH O   H2   sing N N 158 
ILE N   CA   sing N N 159 
ILE N   H    sing N N 160 
ILE N   H2   sing N N 161 
ILE CA  C    sing N N 162 
ILE CA  CB   sing N N 163 
ILE CA  HA   sing N N 164 
ILE C   O    doub N N 165 
ILE C   OXT  sing N N 166 
ILE CB  CG1  sing N N 167 
ILE CB  CG2  sing N N 168 
ILE CB  HB   sing N N 169 
ILE CG1 CD1  sing N N 170 
ILE CG1 HG12 sing N N 171 
ILE CG1 HG13 sing N N 172 
ILE CG2 HG21 sing N N 173 
ILE CG2 HG22 sing N N 174 
ILE CG2 HG23 sing N N 175 
ILE CD1 HD11 sing N N 176 
ILE CD1 HD12 sing N N 177 
ILE CD1 HD13 sing N N 178 
ILE OXT HXT  sing N N 179 
LEU N   CA   sing N N 180 
LEU N   H    sing N N 181 
LEU N   H2   sing N N 182 
LEU CA  C    sing N N 183 
LEU CA  CB   sing N N 184 
LEU CA  HA   sing N N 185 
LEU C   O    doub N N 186 
LEU C   OXT  sing N N 187 
LEU CB  CG   sing N N 188 
LEU CB  HB2  sing N N 189 
LEU CB  HB3  sing N N 190 
LEU CG  CD1  sing N N 191 
LEU CG  CD2  sing N N 192 
LEU CG  HG   sing N N 193 
LEU CD1 HD11 sing N N 194 
LEU CD1 HD12 sing N N 195 
LEU CD1 HD13 sing N N 196 
LEU CD2 HD21 sing N N 197 
LEU CD2 HD22 sing N N 198 
LEU CD2 HD23 sing N N 199 
LEU OXT HXT  sing N N 200 
LYS N   CA   sing N N 201 
LYS N   H    sing N N 202 
LYS N   H2   sing N N 203 
LYS CA  C    sing N N 204 
LYS CA  CB   sing N N 205 
LYS CA  HA   sing N N 206 
LYS C   O    doub N N 207 
LYS C   OXT  sing N N 208 
LYS CB  CG   sing N N 209 
LYS CB  HB2  sing N N 210 
LYS CB  HB3  sing N N 211 
LYS CG  CD   sing N N 212 
LYS CG  HG2  sing N N 213 
LYS CG  HG3  sing N N 214 
LYS CD  CE   sing N N 215 
LYS CD  HD2  sing N N 216 
LYS CD  HD3  sing N N 217 
LYS CE  NZ   sing N N 218 
LYS CE  HE2  sing N N 219 
LYS CE  HE3  sing N N 220 
LYS NZ  HZ1  sing N N 221 
LYS NZ  HZ2  sing N N 222 
LYS NZ  HZ3  sing N N 223 
LYS OXT HXT  sing N N 224 
MET N   CA   sing N N 225 
MET N   H    sing N N 226 
MET N   H2   sing N N 227 
MET CA  C    sing N N 228 
MET CA  CB   sing N N 229 
MET CA  HA   sing N N 230 
MET C   O    doub N N 231 
MET C   OXT  sing N N 232 
MET CB  CG   sing N N 233 
MET CB  HB2  sing N N 234 
MET CB  HB3  sing N N 235 
MET CG  SD   sing N N 236 
MET CG  HG2  sing N N 237 
MET CG  HG3  sing N N 238 
MET SD  CE   sing N N 239 
MET CE  HE1  sing N N 240 
MET CE  HE2  sing N N 241 
MET CE  HE3  sing N N 242 
MET OXT HXT  sing N N 243 
PHE N   CA   sing N N 244 
PHE N   H    sing N N 245 
PHE N   H2   sing N N 246 
PHE CA  C    sing N N 247 
PHE CA  CB   sing N N 248 
PHE CA  HA   sing N N 249 
PHE C   O    doub N N 250 
PHE C   OXT  sing N N 251 
PHE CB  CG   sing N N 252 
PHE CB  HB2  sing N N 253 
PHE CB  HB3  sing N N 254 
PHE CG  CD1  doub Y N 255 
PHE CG  CD2  sing Y N 256 
PHE CD1 CE1  sing Y N 257 
PHE CD1 HD1  sing N N 258 
PHE CD2 CE2  doub Y N 259 
PHE CD2 HD2  sing N N 260 
PHE CE1 CZ   doub Y N 261 
PHE CE1 HE1  sing N N 262 
PHE CE2 CZ   sing Y N 263 
PHE CE2 HE2  sing N N 264 
PHE CZ  HZ   sing N N 265 
PHE OXT HXT  sing N N 266 
PRO N   CA   sing N N 267 
PRO N   CD   sing N N 268 
PRO N   H    sing N N 269 
PRO CA  C    sing N N 270 
PRO CA  CB   sing N N 271 
PRO CA  HA   sing N N 272 
PRO C   O    doub N N 273 
PRO C   OXT  sing N N 274 
PRO CB  CG   sing N N 275 
PRO CB  HB2  sing N N 276 
PRO CB  HB3  sing N N 277 
PRO CG  CD   sing N N 278 
PRO CG  HG2  sing N N 279 
PRO CG  HG3  sing N N 280 
PRO CD  HD2  sing N N 281 
PRO CD  HD3  sing N N 282 
PRO OXT HXT  sing N N 283 
SER N   CA   sing N N 284 
SER N   H    sing N N 285 
SER N   H2   sing N N 286 
SER CA  C    sing N N 287 
SER CA  CB   sing N N 288 
SER CA  HA   sing N N 289 
SER C   O    doub N N 290 
SER C   OXT  sing N N 291 
SER CB  OG   sing N N 292 
SER CB  HB2  sing N N 293 
SER CB  HB3  sing N N 294 
SER OG  HG   sing N N 295 
SER OXT HXT  sing N N 296 
THR N   CA   sing N N 297 
THR N   H    sing N N 298 
THR N   H2   sing N N 299 
THR CA  C    sing N N 300 
THR CA  CB   sing N N 301 
THR CA  HA   sing N N 302 
THR C   O    doub N N 303 
THR C   OXT  sing N N 304 
THR CB  OG1  sing N N 305 
THR CB  CG2  sing N N 306 
THR CB  HB   sing N N 307 
THR OG1 HG1  sing N N 308 
THR CG2 HG21 sing N N 309 
THR CG2 HG22 sing N N 310 
THR CG2 HG23 sing N N 311 
THR OXT HXT  sing N N 312 
TRP N   CA   sing N N 313 
TRP N   H    sing N N 314 
TRP N   H2   sing N N 315 
TRP CA  C    sing N N 316 
TRP CA  CB   sing N N 317 
TRP CA  HA   sing N N 318 
TRP C   O    doub N N 319 
TRP C   OXT  sing N N 320 
TRP CB  CG   sing N N 321 
TRP CB  HB2  sing N N 322 
TRP CB  HB3  sing N N 323 
TRP CG  CD1  doub Y N 324 
TRP CG  CD2  sing Y N 325 
TRP CD1 NE1  sing Y N 326 
TRP CD1 HD1  sing N N 327 
TRP CD2 CE2  doub Y N 328 
TRP CD2 CE3  sing Y N 329 
TRP NE1 CE2  sing Y N 330 
TRP NE1 HE1  sing N N 331 
TRP CE2 CZ2  sing Y N 332 
TRP CE3 CZ3  doub Y N 333 
TRP CE3 HE3  sing N N 334 
TRP CZ2 CH2  doub Y N 335 
TRP CZ2 HZ2  sing N N 336 
TRP CZ3 CH2  sing Y N 337 
TRP CZ3 HZ3  sing N N 338 
TRP CH2 HH2  sing N N 339 
TRP OXT HXT  sing N N 340 
TYR N   CA   sing N N 341 
TYR N   H    sing N N 342 
TYR N   H2   sing N N 343 
TYR CA  C    sing N N 344 
TYR CA  CB   sing N N 345 
TYR CA  HA   sing N N 346 
TYR C   O    doub N N 347 
TYR C   OXT  sing N N 348 
TYR CB  CG   sing N N 349 
TYR CB  HB2  sing N N 350 
TYR CB  HB3  sing N N 351 
TYR CG  CD1  doub Y N 352 
TYR CG  CD2  sing Y N 353 
TYR CD1 CE1  sing Y N 354 
TYR CD1 HD1  sing N N 355 
TYR CD2 CE2  doub Y N 356 
TYR CD2 HD2  sing N N 357 
TYR CE1 CZ   doub Y N 358 
TYR CE1 HE1  sing N N 359 
TYR CE2 CZ   sing Y N 360 
TYR CE2 HE2  sing N N 361 
TYR CZ  OH   sing N N 362 
TYR OH  HH   sing N N 363 
TYR OXT HXT  sing N N 364 
VAL N   CA   sing N N 365 
VAL N   H    sing N N 366 
VAL N   H2   sing N N 367 
VAL CA  C    sing N N 368 
VAL CA  CB   sing N N 369 
VAL CA  HA   sing N N 370 
VAL C   O    doub N N 371 
VAL C   OXT  sing N N 372 
VAL CB  CG1  sing N N 373 
VAL CB  CG2  sing N N 374 
VAL CB  HB   sing N N 375 
VAL CG1 HG11 sing N N 376 
VAL CG1 HG12 sing N N 377 
VAL CG1 HG13 sing N N 378 
VAL CG2 HG21 sing N N 379 
VAL CG2 HG22 sing N N 380 
VAL CG2 HG23 sing N N 381 
VAL OXT HXT  sing N N 382 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           PS46772 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8V4W 
_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]   0.011656 
_atom_sites.fract_transf_matrix[1][2]   0.006730 
_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]   0.013459 
_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]   0.018118 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY A 1 1   ? -40.062 25.473  4.064   1.00 42.39  ? 16  GLY A N   1 
ATOM   2    C CA  . GLY A 1 1   ? -40.111 25.787  2.621   1.00 38.15  ? 16  GLY A CA  1 
ATOM   3    C C   . GLY A 1 1   ? -41.085 24.859  1.915   1.00 38.27  ? 16  GLY A C   1 
ATOM   4    O O   . GLY A 1 1   ? -41.633 23.964  2.548   1.00 38.70  ? 16  GLY A O   1 
ATOM   5    N N   . ILE A 1 2   ? -41.257 25.066  0.609   1.00 36.45  ? 17  ILE A N   1 
ATOM   6    C CA  . ILE A 1 2   ? -42.189 24.265  -0.167  1.00 35.67  ? 17  ILE A CA  1 
ATOM   7    C C   . ILE A 1 2   ? -41.666 22.845  -0.340  1.00 37.33  ? 17  ILE A C   1 
ATOM   8    O O   . ILE A 1 2   ? -42.465 21.920  -0.325  1.00 36.88  ? 17  ILE A O   1 
ATOM   9    C CB  . ILE A 1 2   ? -42.468 24.920  -1.519  1.00 39.63  ? 17  ILE A CB  1 
ATOM   10   C CG1 . ILE A 1 2   ? -43.328 26.144  -1.309  1.00 44.70  ? 17  ILE A CG1 1 
ATOM   11   C CG2 . ILE A 1 2   ? -43.121 23.929  -2.476  1.00 40.47  ? 17  ILE A CG2 1 
ATOM   12   C CD1 . ILE A 1 2   ? -43.233 27.123  -2.444  1.00 47.26  ? 17  ILE A CD1 1 
ATOM   13   N N   . ASP A 1 3   ? -40.355 22.662  -0.545  1.00 36.11  ? 18  ASP A N   1 
ATOM   14   C CA  . ASP A 1 3   ? -39.793 21.328  -0.677  1.00 33.99  ? 18  ASP A CA  1 
ATOM   15   C C   . ASP A 1 3   ? -39.856 20.635  0.681   1.00 34.06  ? 18  ASP A C   1 
ATOM   16   O O   . ASP A 1 3   ? -39.281 21.121  1.654   1.00 33.38  ? 18  ASP A O   1 
ATOM   17   C CB  . ASP A 1 3   ? -38.364 21.382  -1.197  1.00 36.92  ? 18  ASP A CB  1 
ATOM   18   C CG  . ASP A 1 3   ? -37.711 20.036  -1.475  1.00 39.41  ? 18  ASP A CG  1 
ATOM   19   O OD1 . ASP A 1 3   ? -38.237 19.004  -1.016  1.00 37.07  ? 18  ASP A OD1 1 
ATOM   20   O OD2 . ASP A 1 3   ? -36.656 20.036  -2.114  1.00 46.23  ? 18  ASP A OD2 1 
ATOM   21   N N   . PRO A 1 4   ? -40.561 19.494  0.822   1.00 28.74  ? 19  PRO A N   1 
ATOM   22   C CA  . PRO A 1 4   ? -40.593 18.806  2.106   1.00 29.57  ? 19  PRO A CA  1 
ATOM   23   C C   . PRO A 1 4   ? -39.243 18.416  2.660   1.00 27.30  ? 19  PRO A C   1 
ATOM   24   O O   . PRO A 1 4   ? -39.187 18.144  3.851   1.00 29.79  ? 19  PRO A O   1 
ATOM   25   C CB  . PRO A 1 4   ? -41.447 17.589  1.826   1.00 29.70  ? 19  PRO A CB  1 
ATOM   26   C CG  . PRO A 1 4   ? -42.329 18.047  0.705   1.00 28.58  ? 19  PRO A CG  1 
ATOM   27   C CD  . PRO A 1 4   ? -41.384 18.802  -0.193  1.00 28.67  ? 19  PRO A CD  1 
ATOM   28   N N   . PHE A 1 5   ? -38.193 18.341  1.816   1.00 29.86  ? 20  PHE A N   1 
ATOM   29   C CA  . PHE A 1 5   ? -36.835 18.173  2.335   1.00 33.86  ? 20  PHE A CA  1 
ATOM   30   C C   . PHE A 1 5   ? -36.559 19.160  3.466   1.00 31.63  ? 20  PHE A C   1 
ATOM   31   O O   . PHE A 1 5   ? -35.921 18.813  4.462   1.00 33.99  ? 20  PHE A O   1 
ATOM   32   C CB  . PHE A 1 5   ? -35.808 18.389  1.223   1.00 38.00  ? 20  PHE A CB  1 
ATOM   33   C CG  . PHE A 1 5   ? -34.370 18.298  1.702   1.00 42.54  ? 20  PHE A CG  1 
ATOM   34   C CD1 . PHE A 1 5   ? -33.838 17.077  2.090   1.00 46.78  ? 20  PHE A CD1 1 
ATOM   35   C CD2 . PHE A 1 5   ? -33.567 19.429  1.779   1.00 45.87  ? 20  PHE A CD2 1 
ATOM   36   C CE1 . PHE A 1 5   ? -32.537 16.980  2.532   1.00 49.66  ? 20  PHE A CE1 1 
ATOM   37   C CE2 . PHE A 1 5   ? -32.258 19.334  2.221   1.00 46.74  ? 20  PHE A CE2 1 
ATOM   38   C CZ  . PHE A 1 5   ? -31.753 18.111  2.611   1.00 48.11  ? 20  PHE A CZ  1 
ATOM   39   N N   . THR A 1 6   ? -37.081 20.383  3.313   1.00 28.72  ? 21  THR A N   1 
ATOM   40   C CA  . THR A 1 6   ? -36.787 21.463  4.243   1.00 30.23  ? 21  THR A CA  1 
ATOM   41   C C   . THR A 1 6   ? -37.476 21.208  5.574   1.00 29.44  ? 21  THR A C   1 
ATOM   42   O O   . THR A 1 6   ? -37.034 21.730  6.589   1.00 33.23  ? 21  THR A O   1 
ATOM   43   C CB  . THR A 1 6   ? -37.152 22.850  3.714   1.00 33.70  ? 21  THR A CB  1 
ATOM   44   O OG1 . THR A 1 6   ? -38.578 22.959  3.626   1.00 35.25  ? 21  THR A OG1 1 
ATOM   45   C CG2 . THR A 1 6   ? -36.433 23.141  2.407   1.00 35.98  ? 21  THR A CG2 1 
ATOM   46   N N   . TRP A 1 7   ? -38.592 20.470  5.554   1.00 27.81  ? 22  TRP A N   1 
ATOM   47   C CA  . TRP A 1 7   ? -39.314 20.201  6.783   1.00 27.38  ? 22  TRP A CA  1 
ATOM   48   C C   . TRP A 1 7   ? -38.536 19.283  7.726   1.00 27.24  ? 22  TRP A C   1 
ATOM   49   O O   . TRP A 1 7   ? -38.851 19.260  8.918   1.00 29.50  ? 22  TRP A O   1 
ATOM   50   C CB  . TRP A 1 7   ? -40.667 19.555  6.501   1.00 27.67  ? 22  TRP A CB  1 
ATOM   51   C CG  . TRP A 1 7   ? -41.528 20.254  5.500   1.00 27.52  ? 22  TRP A CG  1 
ATOM   52   C CD1 . TRP A 1 7   ? -41.352 21.486  4.951   1.00 28.84  ? 22  TRP A CD1 1 
ATOM   53   C CD2 . TRP A 1 7   ? -42.746 19.729  4.935   1.00 28.28  ? 22  TRP A CD2 1 
ATOM   54   N NE1 . TRP A 1 7   ? -42.351 21.739  4.055   1.00 30.27  ? 22  TRP A NE1 1 
ATOM   55   C CE2 . TRP A 1 7   ? -43.219 20.679  4.034   1.00 29.71  ? 22  TRP A CE2 1 
ATOM   56   C CE3 . TRP A 1 7   ? -43.462 18.540  5.092   1.00 27.23  ? 22  TRP A CE3 1 
ATOM   57   C CZ2 . TRP A 1 7   ? -44.382 20.478  3.301   1.00 30.86  ? 22  TRP A CZ2 1 
ATOM   58   C CZ3 . TRP A 1 7   ? -44.626 18.343  4.394   1.00 28.55  ? 22  TRP A CZ3 1 
ATOM   59   C CH2 . TRP A 1 7   ? -45.063 19.297  3.493   1.00 29.64  ? 22  TRP A CH2 1 
ATOM   60   N N   . GLY A 1 8   ? -37.595 18.475  7.176   1.00 26.74  ? 23  GLY A N   1 
ATOM   61   C CA  . GLY A 1 8   ? -36.790 17.554  7.970   1.00 28.07  ? 23  GLY A CA  1 
ATOM   62   C C   . GLY A 1 8   ? -35.305 17.915  7.991   1.00 26.25  ? 23  GLY A C   1 
ATOM   63   O O   . GLY A 1 8   ? -34.502 17.142  8.497   1.00 28.73  ? 23  GLY A O   1 
ATOM   64   N N   . PHE A 1 9   ? -34.972 19.106  7.488   1.00 26.59  ? 24  PHE A N   1 
ATOM   65   C CA  . PHE A 1 9   ? -33.605 19.561  7.348   1.00 25.71  ? 24  PHE A CA  1 
ATOM   66   C C   . PHE A 1 9   ? -32.858 19.452  8.675   1.00 27.50  ? 24  PHE A C   1 
ATOM   67   O O   . PHE A 1 9   ? -33.305 19.947  9.701   1.00 25.22  ? 24  PHE A O   1 
ATOM   68   C CB  . PHE A 1 9   ? -33.608 21.023  6.893   1.00 28.23  ? 24  PHE A CB  1 
ATOM   69   C CG  . PHE A 1 9   ? -32.203 21.532  6.614   1.00 30.23  ? 24  PHE A CG  1 
ATOM   70   C CD1 . PHE A 1 9   ? -31.551 21.217  5.438   1.00 32.61  ? 24  PHE A CD1 1 
ATOM   71   C CD2 . PHE A 1 9   ? -31.527 22.303  7.548   1.00 30.16  ? 24  PHE A CD2 1 
ATOM   72   C CE1 . PHE A 1 9   ? -30.273 21.671  5.194   1.00 34.99  ? 24  PHE A CE1 1 
ATOM   73   C CE2 . PHE A 1 9   ? -30.238 22.763  7.289   1.00 32.77  ? 24  PHE A CE2 1 
ATOM   74   C CZ  . PHE A 1 9   ? -29.627 22.456  6.108   1.00 34.36  ? 24  PHE A CZ  1 
ATOM   75   N N   . GLY A 1 10  ? -31.676 18.835  8.645   1.00 27.19  ? 25  GLY A N   1 
ATOM   76   C CA  . GLY A 1 10  ? -30.872 18.668  9.843   1.00 27.09  ? 25  GLY A CA  1 
ATOM   77   C C   . GLY A 1 10  ? -31.407 17.629  10.827  1.00 25.98  ? 25  GLY A C   1 
ATOM   78   O O   . GLY A 1 10  ? -30.862 17.443  11.921  1.00 27.93  ? 25  GLY A O   1 
ATOM   79   N N   . GLY A 1 11  ? -32.437 16.874  10.426  1.00 27.05  ? 26  GLY A N   1 
ATOM   80   C CA  . GLY A 1 11  ? -33.010 15.905  11.347  1.00 29.06  ? 26  GLY A CA  1 
ATOM   81   C C   . GLY A 1 11  ? -32.205 14.611  11.321  1.00 29.83  ? 26  GLY A C   1 
ATOM   82   O O   . GLY A 1 11  ? -31.265 14.481  10.532  1.00 34.02  ? 26  GLY A O   1 
ATOM   83   N N   . SER A 1 12  ? -32.609 13.638  12.142  1.00 33.70  ? 27  SER A N   1 
ATOM   84   C CA  . SER A 1 12  ? -32.075 12.288  12.075  1.00 40.70  ? 27  SER A CA  1 
ATOM   85   C C   . SER A 1 12  ? -32.089 11.705  10.655  1.00 45.71  ? 27  SER A C   1 
ATOM   86   O O   . SER A 1 12  ? -33.171 11.535  10.087  1.00 52.67  ? 27  SER A O   1 
ATOM   87   C CB  . SER A 1 12  ? -32.869 11.339  12.935  1.00 46.01  ? 27  SER A CB  1 
ATOM   88   O OG  . SER A 1 12  ? -32.099 10.147  13.015  1.00 53.61  ? 27  SER A OG  1 
ATOM   89   N N   . SER A 1 13  ? -30.899 11.260  10.192  1.00 47.34  ? 28  SER A N   1 
ATOM   90   C CA  . SER A 1 13  ? -30.639 10.698  8.878   1.00 48.12  ? 28  SER A CA  1 
ATOM   91   C C   . SER A 1 13  ? -30.839 9.173   8.873   1.00 43.55  ? 28  SER A C   1 
ATOM   92   O O   . SER A 1 13  ? -30.801 8.519   7.802   1.00 43.37  ? 28  SER A O   1 
ATOM   93   C CB  . SER A 1 13  ? -29.211 11.094  8.481   1.00 50.56  ? 28  SER A CB  1 
ATOM   94   O OG  . SER A 1 13  ? -28.828 10.583  7.216   1.00 60.33  ? 28  SER A OG  1 
ATOM   95   N N   . LYS A 1 14  ? -31.067 8.612   10.085  1.00 42.65  ? 29  LYS A N   1 
ATOM   96   C CA  . LYS A 1 14  ? -31.195 7.174   10.328  1.00 38.96  ? 29  LYS A CA  1 
ATOM   97   C C   . LYS A 1 14  ? -32.364 6.609   9.519   1.00 43.02  ? 29  LYS A C   1 
ATOM   98   O O   . LYS A 1 14  ? -33.466 7.108   9.603   1.00 49.59  ? 29  LYS A O   1 
ATOM   99   C CB  . LYS A 1 14  ? -31.628 6.732   11.740  1.00 46.04  ? 29  LYS A CB  1 
ATOM   100  C CG  . LYS A 1 14  ? -30.939 7.325   12.958  1.00 52.89  ? 29  LYS A CG  1 
ATOM   101  C CD  . LYS A 1 14  ? -29.591 6.743   13.333  1.00 49.15  ? 29  LYS A CD  1 
ATOM   102  C CE  . LYS A 1 14  ? -29.041 7.269   14.632  1.00 54.68  ? 29  LYS A CE  1 
ATOM   103  N NZ  . LYS A 1 14  ? -27.578 7.110   14.752  1.00 61.29  ? 29  LYS A NZ  1 
ATOM   104  N N   . GLU A 1 15  ? -32.118 5.501   8.817   1.00 38.58  ? 30  GLU A N   1 
ATOM   105  C CA  . GLU A 1 15  ? -33.112 4.804   8.008   1.00 35.86  ? 30  GLU A CA  1 
ATOM   106  C C   . GLU A 1 15  ? -33.299 3.410   8.589   1.00 35.13  ? 30  GLU A C   1 
ATOM   107  O O   . GLU A 1 15  ? -32.388 2.595   8.564   1.00 40.41  ? 30  GLU A O   1 
ATOM   108  C CB  . GLU A 1 15  ? -32.667 4.534   6.569   1.00 35.55  ? 30  GLU A CB  1 
ATOM   109  C CG  . GLU A 1 15  ? -32.681 5.749   5.653   1.00 42.59  ? 30  GLU A CG  1 
ATOM   110  C CD  . GLU A 1 15  ? -34.043 6.279   5.242   1.00 47.96  ? 30  GLU A CD  1 
ATOM   111  O OE1 . GLU A 1 15  ? -35.134 5.744   5.599   1.00 50.81  ? 30  GLU A OE1 1 
ATOM   112  O OE2 . GLU A 1 15  ? -33.955 7.267   4.492   1.00 55.48  ? 30  GLU A OE2 1 
ATOM   113  N N   . LYS A 1 16  ? -34.513 3.112   9.029   1.00 36.84  ? 31  LYS A N   1 
ATOM   114  C CA  . LYS A 1 16  ? -34.784 1.883   9.733   1.00 39.17  ? 31  LYS A CA  1 
ATOM   115  C C   . LYS A 1 16  ? -35.117 0.798   8.710   1.00 34.78  ? 31  LYS A C   1 
ATOM   116  O O   . LYS A 1 16  ? -35.891 0.999   7.779   1.00 39.04  ? 31  LYS A O   1 
ATOM   117  C CB  . LYS A 1 16  ? -35.917 2.047   10.744  1.00 47.00  ? 31  LYS A CB  1 
ATOM   118  C CG  . LYS A 1 16  ? -35.513 2.797   12.001  1.00 57.61  ? 31  LYS A CG  1 
ATOM   119  C CD  . LYS A 1 16  ? -36.484 2.556   13.154  1.00 64.90  ? 31  LYS A CD  1 
ATOM   120  C CE  . LYS A 1 16  ? -36.480 3.631   14.177  1.00 71.03  ? 31  LYS A CE  1 
ATOM   121  N NZ  . LYS A 1 16  ? -37.015 4.882   13.628  1.00 74.32  ? 31  LYS A NZ  1 
ATOM   122  N N   . PRO A 1 17  ? -34.525 -0.392  8.849   1.00 33.47  ? 32  PRO A N   1 
ATOM   123  C CA  . PRO A 1 17  ? -34.800 -1.473  7.914   1.00 32.05  ? 32  PRO A CA  1 
ATOM   124  C C   . PRO A 1 17  ? -36.183 -2.034  8.185   1.00 32.92  ? 32  PRO A C   1 
ATOM   125  O O   . PRO A 1 17  ? -36.604 -2.075  9.307   1.00 36.52  ? 32  PRO A O   1 
ATOM   126  C CB  . PRO A 1 17  ? -33.690 -2.440  8.264   1.00 32.18  ? 32  PRO A CB  1 
ATOM   127  C CG  . PRO A 1 17  ? -33.369 -2.193  9.699   1.00 38.03  ? 32  PRO A CG  1 
ATOM   128  C CD  . PRO A 1 17  ? -33.549 -0.729  9.891   1.00 36.41  ? 32  PRO A CD  1 
ATOM   129  N N   . ASN A 1 18  ? -36.863 -2.504  7.159   1.00 33.46  ? 33  ASN A N   1 
ATOM   130  C CA  . ASN A 1 18  ? -38.123 -3.203  7.353   1.00 34.59  ? 33  ASN A CA  1 
ATOM   131  C C   . ASN A 1 18  ? -37.998 -4.597  6.745   1.00 31.02  ? 33  ASN A C   1 
ATOM   132  O O   . ASN A 1 18  ? -38.644 -4.921  5.764   1.00 33.72  ? 33  ASN A O   1 
ATOM   133  C CB  . ASN A 1 18  ? -39.268 -2.466  6.684   1.00 36.62  ? 33  ASN A CB  1 
ATOM   134  C CG  . ASN A 1 18  ? -40.599 -3.118  6.981   1.00 47.41  ? 33  ASN A CG  1 
ATOM   135  O OD1 . ASN A 1 18  ? -40.781 -3.743  8.036   1.00 51.09  ? 33  ASN A OD1 1 
ATOM   136  N ND2 . ASN A 1 18  ? -41.554 -2.959  6.076   1.00 53.22  ? 33  ASN A ND2 1 
ATOM   137  N N   . TYR A 1 19  ? -37.096 -5.403  7.293   1.00 28.31  ? 34  TYR A N   1 
ATOM   138  C CA  . TYR A 1 19  ? -36.710 -6.636  6.646   1.00 25.95  ? 34  TYR A CA  1 
ATOM   139  C C   . TYR A 1 19  ? -37.681 -7.768  6.953   1.00 25.86  ? 34  TYR A C   1 
ATOM   140  O O   . TYR A 1 19  ? -38.233 -7.875  8.039   1.00 28.90  ? 34  TYR A O   1 
ATOM   141  C CB  . TYR A 1 19  ? -35.287 -6.971  7.103   1.00 27.37  ? 34  TYR A CB  1 
ATOM   142  C CG  . TYR A 1 19  ? -34.178 -6.041  6.631   1.00 26.83  ? 34  TYR A CG  1 
ATOM   143  C CD1 . TYR A 1 19  ? -34.294 -5.199  5.534   1.00 29.50  ? 34  TYR A CD1 1 
ATOM   144  C CD2 . TYR A 1 19  ? -32.979 -6.024  7.300   1.00 24.96  ? 34  TYR A CD2 1 
ATOM   145  C CE1 . TYR A 1 19  ? -33.223 -4.418  5.094   1.00 28.47  ? 34  TYR A CE1 1 
ATOM   146  C CE2 . TYR A 1 19  ? -31.923 -5.234  6.902   1.00 23.94  ? 34  TYR A CE2 1 
ATOM   147  C CZ  . TYR A 1 19  ? -32.038 -4.431  5.790   1.00 23.07  ? 34  TYR A CZ  1 
ATOM   148  O OH  . TYR A 1 19  ? -30.988 -3.684  5.400   1.00 26.10  ? 34  TYR A OH  1 
ATOM   149  N N   . ASP A 1 20  ? -37.842 -8.639  5.955   1.00 25.40  ? 35  ASP A N   1 
ATOM   150  C CA  . ASP A 1 20  ? -38.650 -9.838  6.093   1.00 25.98  ? 35  ASP A CA  1 
ATOM   151  C C   . ASP A 1 20  ? -37.758 -11.003 6.504   1.00 25.85  ? 35  ASP A C   1 
ATOM   152  O O   . ASP A 1 20  ? -37.008 -11.502 5.687   1.00 25.70  ? 35  ASP A O   1 
ATOM   153  C CB  . ASP A 1 20  ? -39.388 -10.151 4.801   1.00 29.02  ? 35  ASP A CB  1 
ATOM   154  C CG  . ASP A 1 20  ? -40.305 -11.364 4.857   1.00 33.00  ? 35  ASP A CG  1 
ATOM   155  O OD1 . ASP A 1 20  ? -40.410 -11.983 5.928   1.00 31.42  ? 35  ASP A OD1 1 
ATOM   156  O OD2 . ASP A 1 20  ? -40.918 -11.669 3.808   1.00 38.78  ? 35  ASP A OD2 1 
ATOM   157  N N   . TYR A 1 21  ? -37.908 -11.463 7.744   1.00 24.78  ? 36  TYR A N   1 
ATOM   158  C CA  . TYR A 1 21  ? -37.160 -12.576 8.298   1.00 25.34  ? 36  TYR A CA  1 
ATOM   159  C C   . TYR A 1 21  ? -37.926 -13.891 8.225   1.00 25.45  ? 36  TYR A C   1 
ATOM   160  O O   . TYR A 1 21  ? -37.448 -14.887 8.794   1.00 26.59  ? 36  TYR A O   1 
ATOM   161  C CB  . TYR A 1 21  ? -36.765 -12.305 9.753   1.00 26.88  ? 36  TYR A CB  1 
ATOM   162  C CG  . TYR A 1 21  ? -35.839 -11.114 9.867   1.00 26.00  ? 36  TYR A CG  1 
ATOM   163  C CD1 . TYR A 1 21  ? -34.520 -11.183 9.434   1.00 26.06  ? 36  TYR A CD1 1 
ATOM   164  C CD2 . TYR A 1 21  ? -36.290 -9.915  10.391  1.00 24.15  ? 36  TYR A CD2 1 
ATOM   165  C CE1 . TYR A 1 21  ? -33.687 -10.086 9.504   1.00 25.96  ? 36  TYR A CE1 1 
ATOM   166  C CE2 . TYR A 1 21  ? -35.458 -8.811  10.460  1.00 23.82  ? 36  TYR A CE2 1 
ATOM   167  C CZ  . TYR A 1 21  ? -34.150 -8.902  10.031  1.00 23.99  ? 36  TYR A CZ  1 
ATOM   168  O OH  . TYR A 1 21  ? -33.278 -7.857  10.135  1.00 26.36  ? 36  TYR A OH  1 
ATOM   169  N N   . SER A 1 22  ? -39.016 -13.952 7.453   1.00 26.72  ? 37  SER A N   1 
ATOM   170  C CA  . SER A 1 22  ? -39.880 -15.129 7.517   1.00 27.88  ? 37  SER A CA  1 
ATOM   171  C C   . SER A 1 22  ? -39.186 -16.418 7.051   1.00 25.59  ? 37  SER A C   1 
ATOM   172  O O   . SER A 1 22  ? -39.401 -17.458 7.659   1.00 26.68  ? 37  SER A O   1 
ATOM   173  C CB  . SER A 1 22  ? -41.178 -14.944 6.791   1.00 32.38  ? 37  SER A CB  1 
ATOM   174  O OG  . SER A 1 22  ? -40.973 -14.611 5.436   1.00 35.96  ? 37  SER A OG  1 
ATOM   175  N N   . ALA A 1 23  ? -38.312 -16.375 6.037   1.00 24.68  ? 38  ALA A N   1 
ATOM   176  C CA  . ALA A 1 23  ? -37.610 -17.583 5.609   1.00 24.81  ? 38  ALA A CA  1 
ATOM   177  C C   . ALA A 1 23  ? -36.535 -18.005 6.620   1.00 24.57  ? 38  ALA A C   1 
ATOM   178  O O   . ALA A 1 23  ? -36.346 -19.196 6.831   1.00 25.56  ? 38  ALA A O   1 
ATOM   179  C CB  . ALA A 1 23  ? -37.026 -17.417 4.214   1.00 25.24  ? 38  ALA A CB  1 
ATOM   180  N N   . ASP A 1 24  ? -35.816 -17.074 7.245   1.00 23.35  ? 39  ASP A N   1 
ATOM   181  C CA  . ASP A 1 24  ? -34.813 -17.422 8.248   1.00 23.91  ? 39  ASP A CA  1 
ATOM   182  C C   . ASP A 1 24  ? -35.489 -18.048 9.481   1.00 25.72  ? 39  ASP A C   1 
ATOM   183  O O   . ASP A 1 24  ? -34.969 -18.997 10.072  1.00 26.13  ? 39  ASP A O   1 
ATOM   184  C CB  . ASP A 1 24  ? -33.944 -16.199 8.568   1.00 24.46  ? 39  ASP A CB  1 
ATOM   185  C CG  . ASP A 1 24  ? -33.081 -15.731 7.396   1.00 26.05  ? 39  ASP A CG  1 
ATOM   186  O OD1 . ASP A 1 24  ? -32.039 -16.419 7.109   1.00 28.93  ? 39  ASP A OD1 1 
ATOM   187  O OD2 . ASP A 1 24  ? -33.507 -14.778 6.679   1.00 27.02  ? 39  ASP A OD2 1 
ATOM   188  N N   . LYS A 1 25  ? -36.627 -17.477 9.898   1.00 24.98  ? 40  LYS A N   1 
ATOM   189  C CA  . LYS A 1 25  ? -37.441 -18.035 10.961  1.00 27.81  ? 40  LYS A CA  1 
ATOM   190  C C   . LYS A 1 25  ? -37.876 -19.461 10.624  1.00 26.32  ? 40  LYS A C   1 
ATOM   191  O O   . LYS A 1 25  ? -37.711 -20.362 11.457  1.00 28.94  ? 40  LYS A O   1 
ATOM   192  C CB  . LYS A 1 25  ? -38.653 -17.152 11.270  1.00 29.61  ? 40  LYS A CB  1 
ATOM   193  C CG  . LYS A 1 25  ? -39.444 -17.600 12.484  1.00 33.25  ? 40  LYS A CG  1 
ATOM   194  C CD  . LYS A 1 25  ? -40.653 -16.710 12.753  1.00 37.53  ? 40  LYS A CD  1 
ATOM   195  C CE  . LYS A 1 25  ? -41.475 -17.237 13.900  1.00 45.39  ? 40  LYS A CE  1 
ATOM   196  N NZ  . LYS A 1 25  ? -42.433 -16.251 14.392  1.00 52.04  ? 40  LYS A NZ  1 
ATOM   197  N N   . LYS A 1 26  ? -38.433 -19.656 9.414   1.00 26.50  ? 41  LYS A N   1 
ATOM   198  C CA  . LYS A 1 26  ? -38.925 -20.955 8.985   1.00 28.84  ? 41  LYS A CA  1 
ATOM   199  C C   . LYS A 1 26  ? -37.779 -21.972 8.977   1.00 26.07  ? 41  LYS A C   1 
ATOM   200  O O   . LYS A 1 26  ? -37.929 -23.090 9.483   1.00 29.91  ? 41  LYS A O   1 
ATOM   201  C CB  . LYS A 1 26  ? -39.571 -20.816 7.598   1.00 29.12  ? 41  LYS A CB  1 
ATOM   202  C CG  . LYS A 1 26  ? -40.129 -22.129 7.030   1.00 31.93  ? 41  LYS A CG  1 
ATOM   203  C CD  . LYS A 1 26  ? -41.130 -22.826 7.932   1.00 37.52  ? 41  LYS A CD  1 
ATOM   204  C CE  . LYS A 1 26  ? -42.397 -22.154 7.963   1.00 39.18  ? 41  LYS A CE  1 
ATOM   205  N NZ  . LYS A 1 26  ? -43.464 -22.974 8.548   1.00 42.33  ? 41  LYS A NZ  1 
ATOM   206  N N   . LEU A 1 27  ? -36.609 -21.563 8.459   1.00 26.56  ? 42  LEU A N   1 
ATOM   207  C CA  . LEU A 1 27  ? -35.480 -22.487 8.368   1.00 29.02  ? 42  LEU A CA  1 
ATOM   208  C C   . LEU A 1 27  ? -35.052 -22.902 9.769   1.00 28.82  ? 42  LEU A C   1 
ATOM   209  O O   . LEU A 1 27  ? -34.836 -24.081 10.038  1.00 32.00  ? 42  LEU A O   1 
ATOM   210  C CB  . LEU A 1 27  ? -34.301 -21.877 7.612   1.00 27.82  ? 42  LEU A CB  1 
ATOM   211  C CG  . LEU A 1 27  ? -33.099 -22.802 7.437   1.00 31.86  ? 42  LEU A CG  1 
ATOM   212  C CD1 . LEU A 1 27  ? -33.313 -23.704 6.215   1.00 35.80  ? 42  LEU A CD1 1 
ATOM   213  C CD2 . LEU A 1 27  ? -31.759 -22.163 7.290   1.00 37.80  ? 42  LEU A CD2 1 
ATOM   214  N N   . ILE A 1 28  ? -34.932 -21.930 10.680  1.00 29.98  ? 43  ILE A N   1 
ATOM   215  C CA  . ILE A 1 28  ? -34.568 -22.243 12.054  1.00 30.98  ? 43  ILE A CA  1 
ATOM   216  C C   . ILE A 1 28  ? -35.554 -23.235 12.687  1.00 35.25  ? 43  ILE A C   1 
ATOM   217  O O   . ILE A 1 28  ? -35.150 -24.070 13.496  1.00 36.43  ? 43  ILE A O   1 
ATOM   218  C CB  . ILE A 1 28  ? -34.460 -20.950 12.883  1.00 32.23  ? 43  ILE A CB  1 
ATOM   219  C CG1 . ILE A 1 28  ? -33.160 -20.238 12.573  1.00 30.85  ? 43  ILE A CG1 1 
ATOM   220  C CG2 . ILE A 1 28  ? -34.609 -21.259 14.381  1.00 38.80  ? 43  ILE A CG2 1 
ATOM   221  C CD1 . ILE A 1 28  ? -33.098 -18.833 13.132  1.00 32.05  ? 43  ILE A CD1 1 
ATOM   222  N N   . GLU A 1 29  ? -36.844 -23.142 12.343  1.00 34.18  ? 44  GLU A N   1 
ATOM   223  C CA  . GLU A 1 29  ? -37.858 -23.985 12.953  1.00 35.98  ? 44  GLU A CA  1 
ATOM   224  C C   . GLU A 1 29  ? -37.865 -25.400 12.393  1.00 34.53  ? 44  GLU A C   1 
ATOM   225  O O   . GLU A 1 29  ? -38.201 -26.322 13.134  1.00 39.06  ? 44  GLU A O   1 
ATOM   226  C CB  . GLU A 1 29  ? -39.251 -23.396 12.752  1.00 35.90  ? 44  GLU A CB  1 
ATOM   227  C CG  . GLU A 1 29  ? -39.454 -22.105 13.532  1.00 40.64  ? 44  GLU A CG  1 
ATOM   228  C CD  . GLU A 1 29  ? -40.672 -21.270 13.167  1.00 40.02  ? 44  GLU A CD  1 
ATOM   229  O OE1 . GLU A 1 29  ? -41.246 -21.512 12.083  1.00 41.25  ? 44  GLU A OE1 1 
ATOM   230  O OE2 . GLU A 1 29  ? -41.045 -20.374 13.972  1.00 47.73  ? 44  GLU A OE2 1 
ATOM   231  N N   . ILE A 1 30  ? -37.549 -25.583 11.099  1.00 31.80  ? 45  ILE A N   1 
ATOM   232  C CA  . ILE A 1 30  ? -37.822 -26.883 10.491  1.00 34.75  ? 45  ILE A CA  1 
ATOM   233  C C   . ILE A 1 30  ? -36.558 -27.605 10.050  1.00 35.07  ? 45  ILE A C   1 
ATOM   234  O O   . ILE A 1 30  ? -36.651 -28.791 9.746   1.00 40.72  ? 45  ILE A O   1 
ATOM   235  C CB  . ILE A 1 30  ? -38.792 -26.778 9.303   1.00 36.16  ? 45  ILE A CB  1 
ATOM   236  C CG1 . ILE A 1 30  ? -38.149 -26.067 8.130   1.00 37.45  ? 45  ILE A CG1 1 
ATOM   237  C CG2 . ILE A 1 30  ? -40.088 -26.098 9.741   1.00 41.50  ? 45  ILE A CG2 1 
ATOM   238  C CD1 . ILE A 1 30  ? -38.926 -26.098 6.838   1.00 37.24  ? 45  ILE A CD1 1 
ATOM   239  N N   . ASN A 1 31  ? -35.424 -26.904 9.919   1.00 37.88  ? 46  ASN A N   1 
ATOM   240  C CA  . ASN A 1 31  ? -34.240 -27.523 9.357   1.00 38.72  ? 46  ASN A CA  1 
ATOM   241  C C   . ASN A 1 31  ? -33.674 -28.546 10.336  1.00 39.96  ? 46  ASN A C   1 
ATOM   242  O O   . ASN A 1 31  ? -33.439 -28.210 11.493  1.00 42.03  ? 46  ASN A O   1 
ATOM   243  C CB  . ASN A 1 31  ? -33.183 -26.495 8.972   1.00 36.59  ? 46  ASN A CB  1 
ATOM   244  C CG  . ASN A 1 31  ? -31.971 -27.183 8.389   1.00 39.08  ? 46  ASN A CG  1 
ATOM   245  O OD1 . ASN A 1 31  ? -32.097 -27.894 7.393   1.00 44.31  ? 46  ASN A OD1 1 
ATOM   246  N ND2 . ASN A 1 31  ? -30.809 -27.020 8.997   1.00 45.90  ? 46  ASN A ND2 1 
ATOM   247  N N   . THR A 1 32  ? -33.419 -29.770 9.852   1.00 46.57  ? 47  THR A N   1 
ATOM   248  C CA  . THR A 1 32  ? -32.819 -30.811 10.685  1.00 51.54  ? 47  THR A CA  1 
ATOM   249  C C   . THR A 1 32  ? -31.432 -31.199 10.166  1.00 56.09  ? 47  THR A C   1 
ATOM   250  O O   . THR A 1 32  ? -30.749 -32.018 10.789  1.00 61.67  ? 47  THR A O   1 
ATOM   251  C CB  . THR A 1 32  ? -33.716 -32.049 10.743  1.00 53.70  ? 47  THR A CB  1 
ATOM   252  O OG1 . THR A 1 32  ? -33.824 -32.489 9.394   1.00 56.66  ? 47  THR A OG1 1 
ATOM   253  C CG2 . THR A 1 32  ? -35.093 -31.785 11.330  1.00 53.68  ? 47  THR A CG2 1 
ATOM   254  N N   . ARG A 1 33  ? -31.033 -30.632 9.020   1.00 51.30  ? 48  ARG A N   1 
ATOM   255  C CA  . ARG A 1 33  ? -29.816 -31.039 8.339   1.00 54.26  ? 48  ARG A CA  1 
ATOM   256  C C   . ARG A 1 33  ? -28.693 -30.075 8.694   1.00 51.93  ? 48  ARG A C   1 
ATOM   257  O O   . ARG A 1 33  ? -28.907 -28.867 8.650   1.00 52.18  ? 48  ARG A O   1 
ATOM   258  C CB  . ARG A 1 33  ? -30.002 -30.976 6.819   1.00 66.14  ? 48  ARG A CB  1 
ATOM   259  C CG  . ARG A 1 33  ? -28.864 -31.641 6.059   1.00 75.36  ? 48  ARG A CG  1 
ATOM   260  C CD  . ARG A 1 33  ? -28.911 -33.158 6.210   1.00 85.33  ? 48  ARG A CD  1 
ATOM   261  N NE  . ARG A 1 33  ? -27.592 -33.774 6.033   1.00 94.08  ? 48  ARG A NE  1 
ATOM   262  C CZ  . ARG A 1 33  ? -26.978 -34.580 6.903   1.00 100.49 ? 48  ARG A CZ  1 
ATOM   263  N NH1 . ARG A 1 33  ? -27.570 -34.941 8.035   1.00 104.05 ? 48  ARG A NH1 1 
ATOM   264  N NH2 . ARG A 1 33  ? -25.762 -35.028 6.633   1.00 96.85  ? 48  ARG A NH2 1 
ATOM   265  N N   . PRO A 1 34  ? -27.476 -30.568 9.037   1.00 47.80  ? 49  PRO A N   1 
ATOM   266  C CA  . PRO A 1 34  ? -26.337 -29.691 9.283   1.00 46.78  ? 49  PRO A CA  1 
ATOM   267  C C   . PRO A 1 34  ? -26.039 -28.789 8.084   1.00 43.22  ? 49  PRO A C   1 
ATOM   268  O O   . PRO A 1 34  ? -26.068 -29.198 6.932   1.00 47.81  ? 49  PRO A O   1 
ATOM   269  C CB  . PRO A 1 34  ? -25.189 -30.682 9.586   1.00 48.37  ? 49  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 34  ? -25.908 -31.865 10.153  1.00 54.17  ? 49  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 34  ? -27.154 -31.978 9.289   1.00 53.32  ? 49  PRO A CD  1 
ATOM   272  N N   . ILE A 1 35  ? -25.753 -27.536 8.346   1.00 38.50  ? 50  ILE A N   1 
ATOM   273  C CA  . ILE A 1 35  ? -25.321 -26.675 7.249   1.00 39.37  ? 50  ILE A CA  1 
ATOM   274  C C   . ILE A 1 35  ? -23.813 -26.479 7.352   1.00 36.78  ? 50  ILE A C   1 
ATOM   275  O O   . ILE A 1 35  ? -23.288 -26.225 8.432   1.00 37.73  ? 50  ILE A O   1 
ATOM   276  C CB  . ILE A 1 35  ? -26.133 -25.373 7.203   1.00 40.97  ? 50  ILE A CB  1 
ATOM   277  C CG1 . ILE A 1 35  ? -27.614 -25.653 6.991   1.00 42.82  ? 50  ILE A CG1 1 
ATOM   278  C CG2 . ILE A 1 35  ? -25.597 -24.471 6.097   1.00 40.22  ? 50  ILE A CG2 1 
ATOM   279  C CD1 . ILE A 1 35  ? -28.522 -24.454 7.164   1.00 44.10  ? 50  ILE A CD1 1 
ATOM   280  N N   . SER A 1 36  ? -23.124 -26.770 6.245   1.00 39.12  ? 51  SER A N   1 
ATOM   281  C CA  . SER A 1 36  ? -21.678 -26.772 6.225   1.00 37.23  ? 51  SER A CA  1 
ATOM   282  C C   . SER A 1 36  ? -21.158 -25.346 6.337   1.00 31.75  ? 51  SER A C   1 
ATOM   283  O O   . SER A 1 36  ? -21.519 -24.493 5.524   1.00 33.17  ? 51  SER A O   1 
ATOM   284  C CB  . SER A 1 36  ? -21.164 -27.424 4.966   1.00 37.36  ? 51  SER A CB  1 
ATOM   285  O OG  . SER A 1 36  ? -19.748 -27.455 4.980   1.00 40.24  ? 51  SER A OG  1 
ATOM   286  N N   . THR A 1 37  ? -20.293 -25.104 7.322   1.00 30.68  ? 52  THR A N   1 
ATOM   287  C CA  . THR A 1 37  ? -19.583 -23.838 7.416   1.00 30.13  ? 52  THR A CA  1 
ATOM   288  C C   . THR A 1 37  ? -18.173 -23.929 6.829   1.00 28.39  ? 52  THR A C   1 
ATOM   289  O O   . THR A 1 37  ? -17.404 -22.968 6.971   1.00 28.43  ? 52  THR A O   1 
ATOM   290  C CB  . THR A 1 37  ? -19.526 -23.376 8.874   1.00 31.58  ? 52  THR A CB  1 
ATOM   291  O OG1 . THR A 1 37  ? -18.916 -24.400 9.658   1.00 35.07  ? 52  THR A OG1 1 
ATOM   292  C CG2 . THR A 1 37  ? -20.892 -23.038 9.445   1.00 33.39  ? 52  THR A CG2 1 
ATOM   293  N N   . ASP A 1 38  ? -17.796 -25.066 6.215   1.00 30.24  ? 53  ASP A N   1 
ATOM   294  C CA  . ASP A 1 38  ? -16.412 -25.272 5.790   1.00 31.50  ? 53  ASP A CA  1 
ATOM   295  C C   . ASP A 1 38  ? -15.967 -24.215 4.786   1.00 28.31  ? 53  ASP A C   1 
ATOM   296  O O   . ASP A 1 38  ? -14.853 -23.685 4.912   1.00 28.37  ? 53  ASP A O   1 
ATOM   297  C CB  . ASP A 1 38  ? -16.194 -26.673 5.250   1.00 33.64  ? 53  ASP A CB  1 
ATOM   298  C CG  . ASP A 1 38  ? -16.288 -27.805 6.267   1.00 43.24  ? 53  ASP A CG  1 
ATOM   299  O OD1 . ASP A 1 38  ? -16.305 -27.512 7.483   1.00 50.62  ? 53  ASP A OD1 1 
ATOM   300  O OD2 . ASP A 1 38  ? -16.318 -28.991 5.842   1.00 50.76  ? 53  ASP A OD2 1 
ATOM   301  N N   . ASN A 1 39  ? -16.814 -23.930 3.776   1.00 27.05  ? 54  ASN A N   1 
ATOM   302  C CA  . ASN A 1 39  ? -16.431 -22.965 2.744   1.00 26.27  ? 54  ASN A CA  1 
ATOM   303  C C   . ASN A 1 39  ? -16.299 -21.575 3.370   1.00 23.53  ? 54  ASN A C   1 
ATOM   304  O O   . ASN A 1 39  ? -15.362 -20.825 3.089   1.00 24.40  ? 54  ASN A O   1 
ATOM   305  C CB  . ASN A 1 39  ? -17.369 -22.993 1.542   1.00 25.95  ? 54  ASN A CB  1 
ATOM   306  C CG  . ASN A 1 39  ? -16.770 -22.265 0.363   1.00 26.69  ? 54  ASN A CG  1 
ATOM   307  O OD1 . ASN A 1 39  ? -16.999 -21.090 0.144   1.00 26.94  ? 54  ASN A OD1 1 
ATOM   308  N ND2 . ASN A 1 39  ? -15.892 -22.923 -0.351  1.00 34.75  ? 54  ASN A ND2 1 
ATOM   309  N N   . ALA A 1 40  ? -17.249 -21.181 4.212   1.00 24.91  ? 55  ALA A N   1 
ATOM   310  C CA  . ALA A 1 40  ? -17.162 -19.871 4.845   1.00 25.08  ? 55  ALA A CA  1 
ATOM   311  C C   . ALA A 1 40  ? -15.926 -19.727 5.724   1.00 24.36  ? 55  ALA A C   1 
ATOM   312  O O   . ALA A 1 40  ? -15.276 -18.671 5.708   1.00 24.31  ? 55  ALA A O   1 
ATOM   313  C CB  . ALA A 1 40  ? -18.446 -19.556 5.592   1.00 26.07  ? 55  ALA A CB  1 
ATOM   314  N N   . LYS A 1 41  ? -15.566 -20.794 6.464   1.00 26.04  ? 56  LYS A N   1 
ATOM   315  C CA  . LYS A 1 41  ? -14.368 -20.784 7.288   1.00 27.48  ? 56  LYS A CA  1 
ATOM   316  C C   . LYS A 1 41  ? -13.101 -20.677 6.431   1.00 25.19  ? 56  LYS A C   1 
ATOM   317  O O   . LYS A 1 41  ? -12.159 -19.974 6.816   1.00 27.40  ? 56  LYS A O   1 
ATOM   318  C CB  . LYS A 1 41  ? -14.322 -22.031 8.161   1.00 30.24  ? 56  LYS A CB  1 
ATOM   319  C CG  . LYS A 1 41  ? -15.280 -22.014 9.339   1.00 33.99  ? 56  LYS A CG  1 
ATOM   320  C CD  . LYS A 1 41  ? -15.147 -23.292 10.183  1.00 36.25  ? 56  LYS A CD  1 
ATOM   321  C CE  . LYS A 1 41  ? -16.102 -23.252 11.336  1.00 42.50  ? 56  LYS A CE  1 
ATOM   322  N NZ  . LYS A 1 41  ? -16.139 -24.492 12.104  1.00 48.00  ? 56  LYS A NZ  1 
ATOM   323  N N   . TYR A 1 42  ? -13.089 -21.368 5.281   1.00 25.76  ? 57  TYR A N   1 
ATOM   324  C CA  . TYR A 1 42  ? -11.990 -21.264 4.326   1.00 25.78  ? 57  TYR A CA  1 
ATOM   325  C C   . TYR A 1 42  ? -11.759 -19.802 3.933   1.00 25.00  ? 57  TYR A C   1 
ATOM   326  O O   . TYR A 1 42  ? -10.630 -19.297 3.986   1.00 25.85  ? 57  TYR A O   1 
ATOM   327  C CB  . TYR A 1 42  ? -12.268 -22.143 3.103   1.00 26.92  ? 57  TYR A CB  1 
ATOM   328  C CG  . TYR A 1 42  ? -11.214 -22.038 2.017   1.00 26.70  ? 57  TYR A CG  1 
ATOM   329  C CD1 . TYR A 1 42  ? -10.026 -22.720 2.158   1.00 26.39  ? 57  TYR A CD1 1 
ATOM   330  C CD2 . TYR A 1 42  ? -11.458 -21.425 0.805   1.00 25.87  ? 57  TYR A CD2 1 
ATOM   331  C CE1 . TYR A 1 42  ? -9.050  -22.669 1.197   1.00 26.62  ? 57  TYR A CE1 1 
ATOM   332  C CE2 . TYR A 1 42  ? -10.501 -21.417 -0.206  1.00 24.67  ? 57  TYR A CE2 1 
ATOM   333  C CZ  . TYR A 1 42  ? -9.291  -22.050 -0.007  1.00 27.37  ? 57  TYR A CZ  1 
ATOM   334  O OH  . TYR A 1 42  ? -8.315  -22.099 -0.962  1.00 28.85  ? 57  TYR A OH  1 
ATOM   335  N N   . TRP A 1 43  ? -12.824 -19.103 3.562   1.00 23.64  ? 58  TRP A N   1 
ATOM   336  C CA  . TRP A 1 43  ? -12.676 -17.725 3.130   1.00 22.38  ? 58  TRP A CA  1 
ATOM   337  C C   . TRP A 1 43  ? -12.357 -16.782 4.292   1.00 22.10  ? 58  TRP A C   1 
ATOM   338  O O   . TRP A 1 43  ? -11.510 -15.896 4.124   1.00 24.93  ? 58  TRP A O   1 
ATOM   339  C CB  . TRP A 1 43  ? -13.908 -17.260 2.340   1.00 22.78  ? 58  TRP A CB  1 
ATOM   340  C CG  . TRP A 1 43  ? -13.877 -17.897 0.988   1.00 23.08  ? 58  TRP A CG  1 
ATOM   341  C CD1 . TRP A 1 43  ? -14.575 -18.976 0.544   1.00 24.58  ? 58  TRP A CD1 1 
ATOM   342  C CD2 . TRP A 1 43  ? -12.967 -17.521 -0.063  1.00 21.88  ? 58  TRP A CD2 1 
ATOM   343  N NE1 . TRP A 1 43  ? -14.170 -19.281 -0.725  1.00 24.54  ? 58  TRP A NE1 1 
ATOM   344  C CE2 . TRP A 1 43  ? -13.185 -18.428 -1.125  1.00 24.02  ? 58  TRP A CE2 1 
ATOM   345  C CE3 . TRP A 1 43  ? -11.993 -16.517 -0.201  1.00 23.70  ? 58  TRP A CE3 1 
ATOM   346  C CZ2 . TRP A 1 43  ? -12.462 -18.374 -2.307  1.00 25.25  ? 58  TRP A CZ2 1 
ATOM   347  C CZ3 . TRP A 1 43  ? -11.277 -16.466 -1.383  1.00 26.41  ? 58  TRP A CZ3 1 
ATOM   348  C CH2 . TRP A 1 43  ? -11.484 -17.406 -2.398  1.00 27.54  ? 58  TRP A CH2 1 
ATOM   349  N N   . CYS A 1 44  ? -12.965 -16.998 5.459   1.00 25.06  ? 59  CYS A N   1 
ATOM   350  C CA  . CYS A 1 44  ? -12.713 -16.139 6.617   1.00 26.51  ? 59  CYS A CA  1 
ATOM   351  C C   . CYS A 1 44  ? -11.310 -16.378 7.188   1.00 29.46  ? 59  CYS A C   1 
ATOM   352  O O   . CYS A 1 44  ? -10.546 -15.414 7.353   1.00 33.18  ? 59  CYS A O   1 
ATOM   353  C CB  . CYS A 1 44  ? -13.762 -16.387 7.691   1.00 28.75  ? 59  CYS A CB  1 
ATOM   354  S SG  . CYS A 1 44  ? -13.538 -15.337 9.163   1.00 33.26  ? 59  CYS A SG  1 
ATOM   355  N N   . PHE A 1 45  ? -10.954 -17.650 7.457   1.00 31.42  ? 60  PHE A N   1 
ATOM   356  C CA  . PHE A 1 45  ? -9.735  -17.976 8.189   1.00 36.21  ? 60  PHE A CA  1 
ATOM   357  C C   . PHE A 1 45  ? -8.564  -18.224 7.245   1.00 32.01  ? 60  PHE A C   1 
ATOM   358  O O   . PHE A 1 45  ? -7.506  -17.635 7.431   1.00 43.27  ? 60  PHE A O   1 
ATOM   359  C CB  . PHE A 1 45  ? -9.981  -19.140 9.156   1.00 35.48  ? 60  PHE A CB  1 
ATOM   360  C CG  . PHE A 1 45  ? -11.035 -18.832 10.209  1.00 38.77  ? 60  PHE A CG  1 
ATOM   361  C CD1 . PHE A 1 45  ? -11.016 -17.622 10.899  1.00 43.70  ? 60  PHE A CD1 1 
ATOM   362  C CD2 . PHE A 1 45  ? -12.057 -19.733 10.491  1.00 40.95  ? 60  PHE A CD2 1 
ATOM   363  C CE1 . PHE A 1 45  ? -11.980 -17.335 11.855  1.00 45.40  ? 60  PHE A CE1 1 
ATOM   364  C CE2 . PHE A 1 45  ? -13.023 -19.429 11.440  1.00 43.05  ? 60  PHE A CE2 1 
ATOM   365  C CZ  . PHE A 1 45  ? -12.979 -18.233 12.120  1.00 43.07  ? 60  PHE A CZ  1 
ATOM   366  N N   . ASP A 1 46  ? -8.712  -19.111 6.264   1.00 33.37  ? 61  ASP A N   1 
ATOM   367  C CA  . ASP A 1 46  ? -7.573  -19.468 5.433   1.00 31.27  ? 61  ASP A CA  1 
ATOM   368  C C   . ASP A 1 46  ? -7.186  -18.299 4.509   1.00 30.63  ? 61  ASP A C   1 
ATOM   369  O O   . ASP A 1 46  ? -5.990  -18.025 4.322   1.00 36.16  ? 61  ASP A O   1 
ATOM   370  C CB  . ASP A 1 46  ? -7.836  -20.760 4.679   1.00 35.50  ? 61  ASP A CB  1 
ATOM   371  C CG  . ASP A 1 46  ? -7.960  -22.007 5.544   1.00 46.90  ? 61  ASP A CG  1 
ATOM   372  O OD1 . ASP A 1 46  ? -8.880  -22.041 6.376   1.00 51.77  ? 61  ASP A OD1 1 
ATOM   373  O OD2 . ASP A 1 46  ? -7.126  -22.922 5.388   1.00 58.88  ? 61  ASP A OD2 1 
ATOM   374  N N   . LYS A 1 47  ? -8.182  -17.628 3.935   1.00 29.70  ? 62  LYS A N   1 
ATOM   375  C CA  . LYS A 1 47  ? -7.944  -16.598 2.938   1.00 29.27  ? 62  LYS A CA  1 
ATOM   376  C C   . LYS A 1 47  ? -8.016  -15.178 3.504   1.00 29.86  ? 62  LYS A C   1 
ATOM   377  O O   . LYS A 1 47  ? -7.639  -14.223 2.814   1.00 35.61  ? 62  LYS A O   1 
ATOM   378  C CB  . LYS A 1 47  ? -8.971  -16.676 1.812   1.00 28.21  ? 62  LYS A CB  1 
ATOM   379  C CG  . LYS A 1 47  ? -8.921  -17.937 0.985   1.00 31.27  ? 62  LYS A CG  1 
ATOM   380  C CD  . LYS A 1 47  ? -7.587  -18.050 0.271   1.00 37.47  ? 62  LYS A CD  1 
ATOM   381  C CE  . LYS A 1 47  ? -7.698  -18.883 -0.908  1.00 40.94  ? 62  LYS A CE  1 
ATOM   382  N NZ  . LYS A 1 47  ? -6.449  -18.816 -1.662  1.00 42.96  ? 62  LYS A NZ  1 
ATOM   383  N N   . GLY A 1 48  ? -8.525  -15.019 4.714   1.00 29.12  ? 63  GLY A N   1 
ATOM   384  C CA  . GLY A 1 48  ? -8.502  -13.717 5.351   1.00 29.91  ? 63  GLY A CA  1 
ATOM   385  C C   . GLY A 1 48  ? -9.511  -12.733 4.777   1.00 29.54  ? 63  GLY A C   1 
ATOM   386  O O   . GLY A 1 48  ? -9.261  -11.538 4.827   1.00 33.79  ? 63  GLY A O   1 
ATOM   387  N N   . ASN A 1 49  ? -10.620 -13.227 4.231   1.00 26.12  ? 64  ASN A N   1 
ATOM   388  C CA  . ASN A 1 49  ? -11.560 -12.374 3.511   1.00 24.95  ? 64  ASN A CA  1 
ATOM   389  C C   . ASN A 1 49  ? -12.787 -12.045 4.364   1.00 24.91  ? 64  ASN A C   1 
ATOM   390  O O   . ASN A 1 49  ? -13.479 -12.942 4.860   1.00 23.97  ? 64  ASN A O   1 
ATOM   391  C CB  . ASN A 1 49  ? -11.982 -13.057 2.222   1.00 24.79  ? 64  ASN A CB  1 
ATOM   392  C CG  . ASN A 1 49  ? -12.663 -12.129 1.269   1.00 25.17  ? 64  ASN A CG  1 
ATOM   393  O OD1 . ASN A 1 49  ? -13.724 -11.591 1.579   1.00 24.70  ? 64  ASN A OD1 1 
ATOM   394  N ND2 . ASN A 1 49  ? -12.073 -11.923 0.109   1.00 30.04  ? 64  ASN A ND2 1 
ATOM   395  N N   . ASP A 1 50  ? -13.029 -10.756 4.593   1.00 23.73  ? 65  ASP A N   1 
ATOM   396  C CA  . ASP A 1 50  ? -14.130 -10.343 5.456   1.00 24.52  ? 65  ASP A CA  1 
ATOM   397  C C   . ASP A 1 50  ? -15.502 -10.790 4.942   1.00 21.96  ? 65  ASP A C   1 
ATOM   398  O O   . ASP A 1 50  ? -16.418 -10.916 5.745   1.00 22.46  ? 65  ASP A O   1 
ATOM   399  C CB  . ASP A 1 50  ? -14.119 -8.841  5.655   1.00 26.25  ? 65  ASP A CB  1 
ATOM   400  C CG  . ASP A 1 50  ? -13.206 -8.346  6.765   1.00 35.38  ? 65  ASP A CG  1 
ATOM   401  O OD1 . ASP A 1 50  ? -12.806 -9.161  7.619   1.00 40.89  ? 65  ASP A OD1 1 
ATOM   402  O OD2 . ASP A 1 50  ? -12.979 -7.143  6.792   1.00 47.16  ? 65  ASP A OD2 1 
ATOM   403  N N   . LEU A 1 51  ? -15.632 -11.042 3.634   1.00 20.93  ? 66  LEU A N   1 
ATOM   404  C CA  . LEU A 1 51  ? -16.905 -11.531 3.143   1.00 20.47  ? 66  LEU A CA  1 
ATOM   405  C C   . LEU A 1 51  ? -17.152 -12.947 3.657   1.00 22.15  ? 66  LEU A C   1 
ATOM   406  O O   . LEU A 1 51  ? -18.269 -13.314 4.006   1.00 21.89  ? 66  LEU A O   1 
ATOM   407  C CB  . LEU A 1 51  ? -17.070 -11.400 1.631   1.00 20.14  ? 66  LEU A CB  1 
ATOM   408  C CG  . LEU A 1 51  ? -18.431 -11.862 1.089   1.00 19.66  ? 66  LEU A CG  1 
ATOM   409  C CD1 . LEU A 1 51  ? -19.579 -11.105 1.734   1.00 19.92  ? 66  LEU A CD1 1 
ATOM   410  C CD2 . LEU A 1 51  ? -18.452 -11.612 -0.423  1.00 20.99  ? 66  LEU A CD2 1 
ATOM   411  N N   . GLY A 1 52  ? -16.094 -13.748 3.771   1.00 21.30  ? 67  GLY A N   1 
ATOM   412  C CA  . GLY A 1 52  ? -16.243 -15.043 4.391   1.00 23.61  ? 67  GLY A CA  1 
ATOM   413  C C   . GLY A 1 52  ? -16.579 -14.945 5.865   1.00 22.67  ? 67  GLY A C   1 
ATOM   414  O O   . GLY A 1 52  ? -17.354 -15.759 6.347   1.00 23.24  ? 67  GLY A O   1 
ATOM   415  N N   . CYS A 1 53  ? -15.995 -13.972 6.585   1.00 22.54  ? 68  CYS A N   1 
ATOM   416  C CA  . CYS A 1 53  ? -16.384 -13.733 7.974   1.00 24.27  ? 68  CYS A CA  1 
ATOM   417  C C   . CYS A 1 53  ? -17.869 -13.411 8.118   1.00 23.45  ? 68  CYS A C   1 
ATOM   418  O O   . CYS A 1 53  ? -18.509 -13.891 9.040   1.00 23.84  ? 68  CYS A O   1 
ATOM   419  C CB  . CYS A 1 53  ? -15.490 -12.696 8.588   1.00 26.98  ? 68  CYS A CB  1 
ATOM   420  S SG  . CYS A 1 53  ? -13.741 -13.193 8.495   1.00 35.19  ? 68  CYS A SG  1 
ATOM   421  N N   . LEU A 1 54  ? -18.400 -12.599 7.221   1.00 22.06  ? 69  LEU A N   1 
ATOM   422  C CA  . LEU A 1 54  ? -19.821 -12.266 7.261   1.00 20.71  ? 69  LEU A CA  1 
ATOM   423  C C   . LEU A 1 54  ? -20.628 -13.533 6.973   1.00 20.87  ? 69  LEU A C   1 
ATOM   424  O O   . LEU A 1 54  ? -21.630 -13.768 7.653   1.00 22.84  ? 69  LEU A O   1 
ATOM   425  C CB  . LEU A 1 54  ? -20.123 -11.155 6.255   1.00 21.02  ? 69  LEU A CB  1 
ATOM   426  C CG  . LEU A 1 54  ? -19.540 -9.792  6.630   1.00 22.55  ? 69  LEU A CG  1 
ATOM   427  C CD1 . LEU A 1 54  ? -19.696 -8.805  5.499   1.00 21.81  ? 69  LEU A CD1 1 
ATOM   428  C CD2 . LEU A 1 54  ? -20.217 -9.263  7.893   1.00 24.32  ? 69  LEU A CD2 1 
ATOM   429  N N   . SER A 1 55  ? -20.247 -14.305 5.944   1.00 20.85  ? 70  SER A N   1 
ATOM   430  C CA  . SER A 1 55  ? -20.986 -15.532 5.667   1.00 20.57  ? 70  SER A CA  1 
ATOM   431  C C   . SER A 1 55  ? -20.994 -16.445 6.890   1.00 23.32  ? 70  SER A C   1 
ATOM   432  O O   . SER A 1 55  ? -22.009 -17.041 7.203   1.00 22.46  ? 70  SER A O   1 
ATOM   433  C CB  . SER A 1 55  ? -20.401 -16.271 4.472   1.00 21.43  ? 70  SER A CB  1 
ATOM   434  O OG  . SER A 1 55  ? -20.495 -15.496 3.294   1.00 21.49  ? 70  SER A OG  1 
ATOM   435  N N   . LEU A 1 56  ? -19.857 -16.554 7.577   1.00 22.47  ? 71  LEU A N   1 
ATOM   436  C CA  . LEU A 1 56  ? -19.774 -17.440 8.732   1.00 24.15  ? 71  LEU A CA  1 
ATOM   437  C C   . LEU A 1 56  ? -20.688 -16.942 9.850   1.00 24.82  ? 71  LEU A C   1 
ATOM   438  O O   . LEU A 1 56  ? -21.377 -17.738 10.466  1.00 25.54  ? 71  LEU A O   1 
ATOM   439  C CB  . LEU A 1 56  ? -18.309 -17.523 9.168   1.00 26.54  ? 71  LEU A CB  1 
ATOM   440  C CG  . LEU A 1 56  ? -18.022 -18.397 10.390  1.00 29.23  ? 71  LEU A CG  1 
ATOM   441  C CD1 . LEU A 1 56  ? -18.530 -19.805 10.109  1.00 29.08  ? 71  LEU A CD1 1 
ATOM   442  C CD2 . LEU A 1 56  ? -16.575 -18.409 10.695  1.00 32.66  ? 71  LEU A CD2 1 
ATOM   443  N N   . GLU A 1 57  ? -20.721 -15.630 10.085  1.00 23.49  ? 72  GLU A N   1 
ATOM   444  C CA  . GLU A 1 57  ? -21.645 -15.063 11.058  1.00 23.51  ? 72  GLU A CA  1 
ATOM   445  C C   . GLU A 1 57  ? -23.107 -15.386 10.724  1.00 22.55  ? 72  GLU A C   1 
ATOM   446  O O   . GLU A 1 57  ? -23.891 -15.762 11.607  1.00 25.36  ? 72  GLU A O   1 
ATOM   447  C CB  . GLU A 1 57  ? -21.499 -13.552 11.178  1.00 24.25  ? 72  GLU A CB  1 
ATOM   448  C CG  . GLU A 1 57  ? -22.517 -13.018 12.184  1.00 32.85  ? 72  GLU A CG  1 
ATOM   449  C CD  . GLU A 1 57  ? -22.335 -11.632 12.743  1.00 37.77  ? 72  GLU A CD  1 
ATOM   450  O OE1 . GLU A 1 57  ? -21.160 -11.192 12.623  1.00 41.83  ? 72  GLU A OE1 1 
ATOM   451  O OE2 . GLU A 1 57  ? -23.345 -11.036 13.245  1.00 28.72  ? 72  GLU A OE2 1 
ATOM   452  N N   . LYS A 1 58  ? -23.486 -15.259 9.447   1.00 22.37  ? 73  LYS A N   1 
ATOM   453  C CA  . LYS A 1 58  ? -24.849 -15.609 9.053   1.00 21.83  ? 73  LYS A CA  1 
ATOM   454  C C   . LYS A 1 58  ? -25.147 -17.068 9.375   1.00 23.36  ? 73  LYS A C   1 
ATOM   455  O O   . LYS A 1 58  ? -26.193 -17.394 9.963   1.00 24.16  ? 73  LYS A O   1 
ATOM   456  C CB  . LYS A 1 58  ? -25.099 -15.285 7.577   1.00 22.49  ? 73  LYS A CB  1 
ATOM   457  C CG  . LYS A 1 58  ? -26.432 -15.821 7.063   1.00 23.73  ? 73  LYS A CG  1 
ATOM   458  C CD  . LYS A 1 58  ? -27.653 -15.188 7.728   1.00 24.31  ? 73  LYS A CD  1 
ATOM   459  C CE  . LYS A 1 58  ? -28.978 -15.894 7.478   1.00 24.17  ? 73  LYS A CE  1 
ATOM   460  N NZ  . LYS A 1 58  ? -29.478 -15.828 6.087   1.00 23.65  ? 73  LYS A NZ  1 
ATOM   461  N N   . LEU A 1 59  ? -24.213 -17.950 9.006   1.00 23.15  ? 74  LEU A N   1 
ATOM   462  C CA  . LEU A 1 59  ? -24.460 -19.375 9.179   1.00 24.59  ? 74  LEU A CA  1 
ATOM   463  C C   . LEU A 1 59  ? -24.482 -19.755 10.651  1.00 23.25  ? 74  LEU A C   1 
ATOM   464  O O   . LEU A 1 59  ? -25.324 -20.545 11.060  1.00 27.86  ? 74  LEU A O   1 
ATOM   465  C CB  . LEU A 1 59  ? -23.408 -20.168 8.414   1.00 25.66  ? 74  LEU A CB  1 
ATOM   466  C CG  . LEU A 1 59  ? -23.496 -20.059 6.899   1.00 25.94  ? 74  LEU A CG  1 
ATOM   467  C CD1 . LEU A 1 59  ? -22.342 -20.787 6.231   1.00 29.73  ? 74  LEU A CD1 1 
ATOM   468  C CD2 . LEU A 1 59  ? -24.812 -20.564 6.367   1.00 28.32  ? 74  LEU A CD2 1 
ATOM   469  N N   . GLU A 1 60  ? -23.638 -19.148 11.466  1.00 25.40  ? 75  GLU A N   1 
ATOM   470  C CA  . GLU A 1 60  ? -23.620 -19.412 12.901  1.00 25.93  ? 75  GLU A CA  1 
ATOM   471  C C   . GLU A 1 60  ? -24.905 -18.885 13.544  1.00 29.05  ? 75  GLU A C   1 
ATOM   472  O O   . GLU A 1 60  ? -25.391 -19.448 14.509  1.00 31.15  ? 75  GLU A O   1 
ATOM   473  C CB  . GLU A 1 60  ? -22.435 -18.734 13.561  1.00 30.08  ? 75  GLU A CB  1 
ATOM   474  C CG  . GLU A 1 60  ? -21.118 -19.439 13.260  1.00 31.13  ? 75  GLU A CG  1 
ATOM   475  C CD  . GLU A 1 60  ? -19.935 -18.564 13.645  1.00 41.05  ? 75  GLU A CD  1 
ATOM   476  O OE1 . GLU A 1 60  ? -20.097 -17.312 13.816  1.00 49.04  ? 75  GLU A OE1 1 
ATOM   477  O OE2 . GLU A 1 60  ? -18.864 -19.154 13.785  1.00 46.16  ? 75  GLU A OE2 1 
ATOM   478  N N   . ALA A 1 61  ? -25.469 -17.787 12.999  1.00 28.26  ? 76  ALA A N   1 
ATOM   479  C CA  . ALA A 1 61  ? -26.710 -17.275 13.534  1.00 29.05  ? 76  ALA A CA  1 
ATOM   480  C C   . ALA A 1 61  ? -27.810 -18.306 13.326  1.00 28.89  ? 76  ALA A C   1 
ATOM   481  O O   . ALA A 1 61  ? -28.635 -18.545 14.212  1.00 31.57  ? 76  ALA A O   1 
ATOM   482  C CB  . ALA A 1 61  ? -27.047 -15.952 12.893  1.00 29.29  ? 76  ALA A CB  1 
ATOM   483  N N   . LEU A 1 62  ? -27.862 -18.908 12.133  1.00 28.03  ? 77  LEU A N   1 
ATOM   484  C CA  . LEU A 1 62  ? -28.840 -19.963 11.880  1.00 29.49  ? 77  LEU A CA  1 
ATOM   485  C C   . LEU A 1 62  ? -28.580 -21.167 12.783  1.00 33.64  ? 77  LEU A C   1 
ATOM   486  O O   . LEU A 1 62  ? -29.533 -21.753 13.295  1.00 38.09  ? 77  LEU A O   1 
ATOM   487  C CB  . LEU A 1 62  ? -28.834 -20.368 10.410  1.00 29.05  ? 77  LEU A CB  1 
ATOM   488  C CG  . LEU A 1 62  ? -29.289 -19.296 9.414   1.00 27.57  ? 77  LEU A CG  1 
ATOM   489  C CD1 . LEU A 1 62  ? -29.044 -19.777 7.988   1.00 29.77  ? 77  LEU A CD1 1 
ATOM   490  C CD2 . LEU A 1 62  ? -30.749 -18.969 9.601   1.00 29.81  ? 77  LEU A CD2 1 
ATOM   491  N N   . GLU A 1 63  ? -27.307 -21.549 12.974  1.00 33.24  ? 78  GLU A N   1 
ATOM   492  C CA  . GLU A 1 63  ? -26.983 -22.693 13.824  1.00 39.10  ? 78  GLU A CA  1 
ATOM   493  C C   . GLU A 1 63  ? -27.511 -22.512 15.244  1.00 43.38  ? 78  GLU A C   1 
ATOM   494  O O   . GLU A 1 63  ? -27.846 -23.494 15.905  1.00 50.65  ? 78  GLU A O   1 
ATOM   495  C CB  . GLU A 1 63  ? -25.475 -22.917 13.937  1.00 42.22  ? 78  GLU A CB  1 
ATOM   496  C CG  . GLU A 1 63  ? -24.855 -23.603 12.725  1.00 45.81  ? 78  GLU A CG  1 
ATOM   497  C CD  . GLU A 1 63  ? -23.371 -23.926 12.894  1.00 53.97  ? 78  GLU A CD  1 
ATOM   498  O OE1 . GLU A 1 63  ? -22.667 -23.234 13.678  1.00 52.28  ? 78  GLU A OE1 1 
ATOM   499  O OE2 . GLU A 1 63  ? -22.915 -24.907 12.260  1.00 55.06  ? 78  GLU A OE2 1 
ATOM   500  N N   . SER A 1 64  ? -27.498 -21.264 15.719  1.00 37.15  ? 79  SER A N   1 
ATOM   501  C CA  . SER A 1 64  ? -27.860 -20.919 17.081  1.00 36.60  ? 79  SER A CA  1 
ATOM   502  C C   . SER A 1 64  ? -29.345 -21.167 17.325  1.00 36.57  ? 79  SER A C   1 
ATOM   503  O O   . SER A 1 64  ? -29.744 -21.305 18.465  1.00 43.72  ? 79  SER A O   1 
ATOM   504  C CB  . SER A 1 64  ? -27.504 -19.487 17.419  1.00 37.68  ? 79  SER A CB  1 
ATOM   505  O OG  . SER A 1 64  ? -28.467 -18.556 16.921  1.00 35.05  ? 79  SER A OG  1 
ATOM   506  N N   . LYS A 1 65  ? -30.134 -21.179 16.246  1.00 38.02  ? 80  LYS A N   1 
ATOM   507  C CA  . LYS A 1 65  ? -31.584 -21.269 16.303  1.00 37.06  ? 80  LYS A CA  1 
ATOM   508  C C   . LYS A 1 65  ? -32.176 -20.085 17.064  1.00 35.21  ? 80  LYS A C   1 
ATOM   509  O O   . LYS A 1 65  ? -33.280 -20.181 17.557  1.00 40.28  ? 80  LYS A O   1 
ATOM   510  C CB  . LYS A 1 65  ? -31.994 -22.581 16.978  1.00 42.31  ? 80  LYS A CB  1 
ATOM   511  C CG  . LYS A 1 65  ? -31.371 -23.818 16.379  1.00 45.83  ? 80  LYS A CG  1 
ATOM   512  C CD  . LYS A 1 65  ? -32.071 -24.278 15.108  1.00 54.41  ? 80  LYS A CD  1 
ATOM   513  C CE  . LYS A 1 65  ? -31.951 -25.748 14.852  1.00 60.73  ? 80  LYS A CE  1 
ATOM   514  N NZ  . LYS A 1 65  ? -32.485 -26.061 13.519  1.00 62.32  ? 80  LYS A NZ  1 
ATOM   515  N N   . ASP A 1 66  ? -31.431 -18.982 17.166  1.00 33.86  ? 81  ASP A N   1 
ATOM   516  C CA  . ASP A 1 66  ? -31.911 -17.759 17.778  1.00 32.78  ? 81  ASP A CA  1 
ATOM   517  C C   . ASP A 1 66  ? -32.107 -16.722 16.681  1.00 31.32  ? 81  ASP A C   1 
ATOM   518  O O   . ASP A 1 66  ? -31.141 -16.143 16.180  1.00 32.76  ? 81  ASP A O   1 
ATOM   519  C CB  . ASP A 1 66  ? -30.976 -17.292 18.887  1.00 37.59  ? 81  ASP A CB  1 
ATOM   520  C CG  . ASP A 1 66  ? -31.468 -16.096 19.685  1.00 40.12  ? 81  ASP A CG  1 
ATOM   521  O OD1 . ASP A 1 66  ? -32.533 -15.589 19.312  1.00 39.91  ? 81  ASP A OD1 1 
ATOM   522  O OD2 . ASP A 1 66  ? -30.791 -15.718 20.680  1.00 45.72  ? 81  ASP A OD2 1 
ATOM   523  N N   . LEU A 1 67  ? -33.360 -16.468 16.319  1.00 29.92  ? 82  LEU A N   1 
ATOM   524  C CA  . LEU A 1 67  ? -33.622 -15.492 15.271  1.00 29.12  ? 82  LEU A CA  1 
ATOM   525  C C   . LEU A 1 67  ? -33.015 -14.129 15.617  1.00 28.74  ? 82  LEU A C   1 
ATOM   526  O O   . LEU A 1 67  ? -32.668 -13.379 14.715  1.00 27.18  ? 82  LEU A O   1 
ATOM   527  C CB  . LEU A 1 67  ? -35.125 -15.383 15.029  1.00 31.09  ? 82  LEU A CB  1 
ATOM   528  C CG  . LEU A 1 67  ? -35.566 -14.587 13.800  1.00 30.88  ? 82  LEU A CG  1 
ATOM   529  C CD1 . LEU A 1 67  ? -35.020 -15.141 12.492  1.00 30.67  ? 82  LEU A CD1 1 
ATOM   530  C CD2 . LEU A 1 67  ? -37.069 -14.513 13.745  1.00 34.21  ? 82  LEU A CD2 1 
ATOM   531  N N   . LYS A 1 68  ? -32.899 -13.796 16.908  1.00 28.41  ? 83  LYS A N   1 
ATOM   532  C CA  . LYS A 1 68  ? -32.317 -12.509 17.263  1.00 31.55  ? 83  LYS A CA  1 
ATOM   533  C C   . LYS A 1 68  ? -30.893 -12.378 16.703  1.00 27.62  ? 83  LYS A C   1 
ATOM   534  O O   . LYS A 1 68  ? -30.462 -11.284 16.412  1.00 27.53  ? 83  LYS A O   1 
ATOM   535  C CB  . LYS A 1 68  ? -32.276 -12.296 18.777  1.00 34.20  ? 83  LYS A CB  1 
ATOM   536  C CG  . LYS A 1 68  ? -33.659 -12.152 19.418  1.00 38.82  ? 83  LYS A CG  1 
ATOM   537  C CD  . LYS A 1 68  ? -33.618 -11.692 20.877  1.00 43.66  ? 83  LYS A CD  1 
ATOM   538  C CE  . LYS A 1 68  ? -34.873 -11.939 21.643  1.00 52.78  ? 83  LYS A CE  1 
ATOM   539  N NZ  . LYS A 1 68  ? -36.088 -11.754 20.834  1.00 60.78  ? 83  LYS A NZ  1 
ATOM   540  N N   . LYS A 1 69  ? -30.145 -13.476 16.563  1.00 27.92  ? 84  LYS A N   1 
ATOM   541  C CA  . LYS A 1 69  ? -28.796 -13.385 16.009  1.00 26.06  ? 84  LYS A CA  1 
ATOM   542  C C   . LYS A 1 69  ? -28.822 -13.103 14.505  1.00 25.97  ? 84  LYS A C   1 
ATOM   543  O O   . LYS A 1 69  ? -27.895 -12.478 13.962  1.00 25.43  ? 84  LYS A O   1 
ATOM   544  C CB  . LYS A 1 69  ? -27.984 -14.638 16.372  1.00 30.85  ? 84  LYS A CB  1 
ATOM   545  C CG  . LYS A 1 69  ? -27.768 -14.809 17.874  1.00 36.15  ? 84  LYS A CG  1 
ATOM   546  C CD  . LYS A 1 69  ? -26.887 -15.965 18.305  1.00 43.44  ? 84  LYS A CD  1 
ATOM   547  C CE  . LYS A 1 69  ? -26.549 -15.830 19.770  1.00 48.43  ? 84  LYS A CE  1 
ATOM   548  N NZ  . LYS A 1 69  ? -25.706 -16.948 20.202  1.00 58.47  ? 84  LYS A NZ  1 
ATOM   549  N N   . VAL A 1 70  ? -29.876 -13.553 13.823  1.00 23.59  ? 85  VAL A N   1 
ATOM   550  C CA  . VAL A 1 70  ? -30.059 -13.280 12.416  1.00 23.76  ? 85  VAL A CA  1 
ATOM   551  C C   . VAL A 1 70  ? -30.381 -11.793 12.250  1.00 23.76  ? 85  VAL A C   1 
ATOM   552  O O   . VAL A 1 70  ? -29.833 -11.115 11.395  1.00 22.30  ? 85  VAL A O   1 
ATOM   553  C CB  . VAL A 1 70  ? -31.154 -14.178 11.809  1.00 23.41  ? 85  VAL A CB  1 
ATOM   554  C CG1 . VAL A 1 70  ? -31.474 -13.767 10.372  1.00 26.51  ? 85  VAL A CG1 1 
ATOM   555  C CG2 . VAL A 1 70  ? -30.758 -15.661 11.884  1.00 26.55  ? 85  VAL A CG2 1 
ATOM   556  N N   . VAL A 1 71  ? -31.257 -11.293 13.107  1.00 23.83  ? 86  VAL A N   1 
ATOM   557  C CA  . VAL A 1 71  ? -31.606 -9.881  13.078  1.00 24.46  ? 86  VAL A CA  1 
ATOM   558  C C   . VAL A 1 71  ? -30.351 -9.041  13.341  1.00 25.07  ? 86  VAL A C   1 
ATOM   559  O O   . VAL A 1 71  ? -30.141 -8.051  12.648  1.00 24.33  ? 86  VAL A O   1 
ATOM   560  C CB  . VAL A 1 71  ? -32.722 -9.556  14.079  1.00 25.28  ? 86  VAL A CB  1 
ATOM   561  C CG1 . VAL A 1 71  ? -32.995 -8.068  14.148  1.00 27.42  ? 86  VAL A CG1 1 
ATOM   562  C CG2 . VAL A 1 71  ? -33.991 -10.303 13.707  1.00 26.08  ? 86  VAL A CG2 1 
ATOM   563  N N   . LYS A 1 72  ? -29.533 -9.446  14.320  1.00 24.22  ? 87  LYS A N   1 
ATOM   564  C CA  . LYS A 1 72  ? -28.323 -8.709  14.616  1.00 25.39  ? 87  LYS A CA  1 
ATOM   565  C C   . LYS A 1 72  ? -27.423 -8.666  13.376  1.00 23.38  ? 87  LYS A C   1 
ATOM   566  O O   . LYS A 1 72  ? -26.750 -7.675  13.111  1.00 23.12  ? 87  LYS A O   1 
ATOM   567  C CB  . LYS A 1 72  ? -27.580 -9.319  15.816  1.00 26.67  ? 87  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 72  ? -26.276 -8.606  16.185  1.00 33.69  ? 87  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 72  ? -25.577 -9.097  17.441  1.00 39.67  ? 87  LYS A CD  1 
ATOM   570  C CE  . LYS A 1 72  ? -24.172 -8.525  17.560  1.00 47.82  ? 87  LYS A CE  1 
ATOM   571  N NZ  . LYS A 1 72  ? -24.158 -7.061  17.680  1.00 47.54  ? 87  LYS A NZ  1 
ATOM   572  N N   . PHE A 1 73  ? -27.267 -9.818  12.719  1.00 22.76  ? 88  PHE A N   1 
ATOM   573  C CA  . PHE A 1 73  ? -26.411 -9.876  11.542  1.00 22.61  ? 88  PHE A CA  1 
ATOM   574  C C   . PHE A 1 73  ? -26.831 -8.821  10.508  1.00 20.64  ? 88  PHE A C   1 
ATOM   575  O O   . PHE A 1 73  ? -26.020 -8.024  10.034  1.00 21.57  ? 88  PHE A O   1 
ATOM   576  C CB  . PHE A 1 73  ? -26.469 -11.280 10.923  1.00 21.73  ? 88  PHE A CB  1 
ATOM   577  C CG  . PHE A 1 73  ? -25.701 -11.369 9.621   1.00 19.95  ? 88  PHE A CG  1 
ATOM   578  C CD1 . PHE A 1 73  ? -24.305 -11.334 9.608   1.00 21.57  ? 88  PHE A CD1 1 
ATOM   579  C CD2 . PHE A 1 73  ? -26.372 -11.430 8.408   1.00 20.21  ? 88  PHE A CD2 1 
ATOM   580  C CE1 . PHE A 1 73  ? -23.631 -11.333 8.413   1.00 22.04  ? 88  PHE A CE1 1 
ATOM   581  C CE2 . PHE A 1 73  ? -25.667 -11.451 7.209   1.00 21.97  ? 88  PHE A CE2 1 
ATOM   582  C CZ  . PHE A 1 73  ? -24.294 -11.427 7.226   1.00 21.46  ? 88  PHE A CZ  1 
ATOM   583  N N   . TYR A 1 74  ? -28.117 -8.798  10.153  1.00 21.21  ? 89  TYR A N   1 
ATOM   584  C CA  . TYR A 1 74  ? -28.579 -7.948  9.065   1.00 20.52  ? 89  TYR A CA  1 
ATOM   585  C C   . TYR A 1 74  ? -28.713 -6.489  9.508   1.00 21.59  ? 89  TYR A C   1 
ATOM   586  O O   . TYR A 1 74  ? -28.536 -5.629  8.657   1.00 21.98  ? 89  TYR A O   1 
ATOM   587  C CB  . TYR A 1 74  ? -29.920 -8.445  8.497   1.00 20.29  ? 89  TYR A CB  1 
ATOM   588  C CG  . TYR A 1 74  ? -29.725 -9.677  7.629   1.00 19.57  ? 89  TYR A CG  1 
ATOM   589  C CD1 . TYR A 1 74  ? -29.128 -9.606  6.386   1.00 21.22  ? 89  TYR A CD1 1 
ATOM   590  C CD2 . TYR A 1 74  ? -30.165 -10.914 8.055   1.00 20.29  ? 89  TYR A CD2 1 
ATOM   591  C CE1 . TYR A 1 74  ? -28.960 -10.733 5.601   1.00 19.62  ? 89  TYR A CE1 1 
ATOM   592  C CE2 . TYR A 1 74  ? -29.996 -12.040 7.282   1.00 20.42  ? 89  TYR A CE2 1 
ATOM   593  C CZ  . TYR A 1 74  ? -29.380 -11.961 6.055   1.00 20.28  ? 89  TYR A CZ  1 
ATOM   594  O OH  . TYR A 1 74  ? -29.167 -13.099 5.313   1.00 20.42  ? 89  TYR A OH  1 
ATOM   595  N N   . GLU A 1 75  ? -29.025 -6.236  10.786  1.00 22.47  ? 90  GLU A N   1 
ATOM   596  C CA  . GLU A 1 75  ? -29.317 -4.873  11.227  1.00 24.02  ? 90  GLU A CA  1 
ATOM   597  C C   . GLU A 1 75  ? -28.160 -4.156  11.912  1.00 24.85  ? 90  GLU A C   1 
ATOM   598  O O   . GLU A 1 75  ? -28.226 -2.929  12.017  1.00 25.34  ? 90  GLU A O   1 
ATOM   599  C CB  . GLU A 1 75  ? -30.560 -4.838  12.108  1.00 24.28  ? 90  GLU A CB  1 
ATOM   600  C CG  . GLU A 1 75  ? -31.775 -5.348  11.342  1.00 25.37  ? 90  GLU A CG  1 
ATOM   601  C CD  . GLU A 1 75  ? -33.119 -5.134  11.982  1.00 27.30  ? 90  GLU A CD  1 
ATOM   602  O OE1 . GLU A 1 75  ? -33.220 -4.372  12.954  1.00 30.54  ? 90  GLU A OE1 1 
ATOM   603  O OE2 . GLU A 1 75  ? -34.074 -5.748  11.479  1.00 30.18  ? 90  GLU A OE2 1 
ATOM   604  N N   . LYS A 1 76  ? -27.209 -4.900  12.475  1.00 23.56  ? 91  LYS A N   1 
ATOM   605  C CA  . LYS A 1 76  ? -26.052 -4.337  13.157  1.00 25.60  ? 91  LYS A CA  1 
ATOM   606  C C   . LYS A 1 76  ? -24.762 -4.692  12.421  1.00 22.36  ? 91  LYS A C   1 
ATOM   607  O O   . LYS A 1 76  ? -24.022 -3.797  12.000  1.00 23.48  ? 91  LYS A O   1 
ATOM   608  C CB  . LYS A 1 76  ? -25.982 -4.801  14.618  1.00 27.70  ? 91  LYS A CB  1 
ATOM   609  C CG  . LYS A 1 76  ? -27.075 -4.190  15.525  1.00 35.01  ? 91  LYS A CG  1 
ATOM   610  C CD  . LYS A 1 76  ? -26.754 -2.790  16.031  1.00 43.97  ? 91  LYS A CD  1 
ATOM   611  C CE  . LYS A 1 76  ? -27.765 -2.189  16.974  1.00 48.50  ? 91  LYS A CE  1 
ATOM   612  N NZ  . LYS A 1 76  ? -27.744 -2.855  18.274  1.00 59.11  ? 91  LYS A NZ  1 
ATOM   613  N N   . THR A 1 77  ? -24.481 -6.008  12.233  1.00 22.46  ? 92  THR A N   1 
ATOM   614  C CA  . THR A 1 77  ? -23.193 -6.388  11.679  1.00 21.91  ? 92  THR A CA  1 
ATOM   615  C C   . THR A 1 77  ? -23.038 -5.856  10.254  1.00 21.75  ? 92  THR A C   1 
ATOM   616  O O   . THR A 1 77  ? -21.997 -5.277  9.897   1.00 22.11  ? 92  THR A O   1 
ATOM   617  C CB  . THR A 1 77  ? -23.050 -7.895  11.728  1.00 23.44  ? 92  THR A CB  1 
ATOM   618  O OG1 . THR A 1 77  ? -23.244 -8.348  13.062  1.00 25.36  ? 92  THR A OG1 1 
ATOM   619  C CG2 . THR A 1 77  ? -21.663 -8.301  11.236  1.00 25.00  ? 92  THR A CG2 1 
ATOM   620  N N   . ILE A 1 78  ? -24.065 -6.018  9.420   1.00 20.92  ? 93  ILE A N   1 
ATOM   621  C CA  . ILE A 1 78  ? -23.949 -5.538  8.050   1.00 21.36  ? 93  ILE A CA  1 
ATOM   622  C C   . ILE A 1 78  ? -23.612 -4.038  7.977   1.00 21.91  ? 93  ILE A C   1 
ATOM   623  O O   . ILE A 1 78  ? -22.663 -3.650  7.290   1.00 22.02  ? 93  ILE A O   1 
ATOM   624  C CB  . ILE A 1 78  ? -25.150 -5.935  7.183   1.00 20.83  ? 93  ILE A CB  1 
ATOM   625  C CG1 . ILE A 1 78  ? -25.070 -7.421  6.854   1.00 22.20  ? 93  ILE A CG1 1 
ATOM   626  C CG2 . ILE A 1 78  ? -25.252 -5.079  5.934   1.00 20.91  ? 93  ILE A CG2 1 
ATOM   627  C CD1 . ILE A 1 78  ? -23.898 -7.828  6.019   1.00 21.24  ? 93  ILE A CD1 1 
ATOM   628  N N   . PRO A 1 79  ? -24.374 -3.118  8.618   1.00 21.95  ? 94  PRO A N   1 
ATOM   629  C CA  . PRO A 1 79  ? -24.029 -1.712  8.523   1.00 22.26  ? 94  PRO A CA  1 
ATOM   630  C C   . PRO A 1 79  ? -22.678 -1.393  9.138   1.00 22.12  ? 94  PRO A C   1 
ATOM   631  O O   . PRO A 1 79  ? -22.034 -0.462  8.665   1.00 23.14  ? 94  PRO A O   1 
ATOM   632  C CB  . PRO A 1 79  ? -25.173 -0.949  9.189   1.00 23.87  ? 94  PRO A CB  1 
ATOM   633  C CG  . PRO A 1 79  ? -26.013 -1.977  9.797   1.00 28.77  ? 94  PRO A CG  1 
ATOM   634  C CD  . PRO A 1 79  ? -25.717 -3.313  9.174   1.00 23.43  ? 94  PRO A CD  1 
ATOM   635  N N   . GLU A 1 80  ? -22.296 -2.117  10.197  1.00 21.68  ? 95  GLU A N   1 
ATOM   636  C CA  . GLU A 1 80  ? -20.988 -1.951  10.792  1.00 23.25  ? 95  GLU A CA  1 
ATOM   637  C C   . GLU A 1 80  ? -19.900 -2.256  9.769   1.00 23.53  ? 95  GLU A C   1 
ATOM   638  O O   . GLU A 1 80  ? -18.905 -1.562  9.712   1.00 26.64  ? 95  GLU A O   1 
ATOM   639  C CB  . GLU A 1 80  ? -20.903 -2.769  12.063  1.00 23.24  ? 95  GLU A CB  1 
ATOM   640  C CG  . GLU A 1 80  ? -21.759 -2.183  13.186  1.00 24.84  ? 95  GLU A CG  1 
ATOM   641  C CD  . GLU A 1 80  ? -22.016 -3.090  14.377  1.00 27.43  ? 95  GLU A CD  1 
ATOM   642  O OE1 . GLU A 1 80  ? -21.375 -4.171  14.528  1.00 31.97  ? 95  GLU A OE1 1 
ATOM   643  O OE2 . GLU A 1 80  ? -22.881 -2.703  15.173  1.00 26.37  ? 95  GLU A OE2 1 
ATOM   644  N N   . TYR A 1 81  ? -20.084 -3.272  8.925   1.00 21.76  ? 96  TYR A N   1 
ATOM   645  C CA  . TYR A 1 81  ? -19.066 -3.587  7.925   1.00 22.43  ? 96  TYR A CA  1 
ATOM   646  C C   . TYR A 1 81  ? -19.138 -2.657  6.725   1.00 19.87  ? 96  TYR A C   1 
ATOM   647  O O   . TYR A 1 81  ? -18.116 -2.145  6.307   1.00 22.88  ? 96  TYR A O   1 
ATOM   648  C CB  . TYR A 1 81  ? -19.149 -5.036  7.461   1.00 21.27  ? 96  TYR A CB  1 
ATOM   649  C CG  . TYR A 1 81  ? -18.377 -5.988  8.341   1.00 23.21  ? 96  TYR A CG  1 
ATOM   650  C CD1 . TYR A 1 81  ? -18.761 -6.249  9.646   1.00 23.36  ? 96  TYR A CD1 1 
ATOM   651  C CD2 . TYR A 1 81  ? -17.227 -6.589  7.874   1.00 27.26  ? 96  TYR A CD2 1 
ATOM   652  C CE1 . TYR A 1 81  ? -18.054 -7.104  10.454  1.00 24.79  ? 96  TYR A CE1 1 
ATOM   653  C CE2 . TYR A 1 81  ? -16.522 -7.478  8.662   1.00 28.29  ? 96  TYR A CE2 1 
ATOM   654  C CZ  . TYR A 1 81  ? -16.916 -7.715  9.961   1.00 28.77  ? 96  TYR A CZ  1 
ATOM   655  O OH  . TYR A 1 81  ? -16.196 -8.547  10.772  1.00 35.11  ? 96  TYR A OH  1 
ATOM   656  N N   . CYS A 1 82  ? -20.346 -2.401  6.184   1.00 21.52  ? 97  CYS A N   1 
ATOM   657  C CA  . CYS A 1 82  ? -20.535 -1.571  5.012   1.00 20.53  ? 97  CYS A CA  1 
ATOM   658  C C   . CYS A 1 82  ? -20.047 -0.163  5.310   1.00 20.37  ? 97  CYS A C   1 
ATOM   659  O O   . CYS A 1 82  ? -19.260 0.387   4.550   1.00 23.20  ? 97  CYS A O   1 
ATOM   660  C CB  . CYS A 1 82  ? -22.013 -1.580  4.564   1.00 21.90  ? 97  CYS A CB  1 
ATOM   661  S SG  . CYS A 1 82  ? -22.437 -0.378  3.269   1.00 22.73  ? 97  CYS A SG  1 
ATOM   662  N N   . TYR A 1 83  ? -20.662 0.463   6.316   1.00 21.82  ? 98  TYR A N   1 
ATOM   663  C CA  . TYR A 1 83  ? -20.383 1.863   6.589   1.00 22.43  ? 98  TYR A CA  1 
ATOM   664  C C   . TYR A 1 83  ? -19.112 2.001   7.404   1.00 22.50  ? 98  TYR A C   1 
ATOM   665  O O   . TYR A 1 83  ? -18.176 2.644   6.939   1.00 25.37  ? 98  TYR A O   1 
ATOM   666  C CB  . TYR A 1 83  ? -21.554 2.503   7.312   1.00 21.67  ? 98  TYR A CB  1 
ATOM   667  C CG  . TYR A 1 83  ? -22.848 2.714   6.547   1.00 22.19  ? 98  TYR A CG  1 
ATOM   668  C CD1 . TYR A 1 83  ? -22.929 3.576   5.478   1.00 22.31  ? 98  TYR A CD1 1 
ATOM   669  C CD2 . TYR A 1 83  ? -24.026 2.131   6.975   1.00 23.67  ? 98  TYR A CD2 1 
ATOM   670  C CE1 . TYR A 1 83  ? -24.121 3.859   4.843   1.00 23.09  ? 98  TYR A CE1 1 
ATOM   671  C CE2 . TYR A 1 83  ? -25.238 2.460   6.391   1.00 24.47  ? 98  TYR A CE2 1 
ATOM   672  C CZ  . TYR A 1 83  ? -25.296 3.296   5.293   1.00 21.22  ? 98  TYR A CZ  1 
ATOM   673  O OH  . TYR A 1 83  ? -26.455 3.640   4.630   1.00 24.39  ? 98  TYR A OH  1 
ATOM   674  N N   . ASP A 1 84  ? -19.131 1.488   8.619   1.00 24.17  ? 99  ASP A N   1 
ATOM   675  C CA  . ASP A 1 84  ? -18.110 1.843   9.601   1.00 27.28  ? 99  ASP A CA  1 
ATOM   676  C C   . ASP A 1 84  ? -16.720 1.319   9.186   1.00 27.28  ? 99  ASP A C   1 
ATOM   677  O O   . ASP A 1 84  ? -15.757 2.051   9.357   1.00 33.04  ? 99  ASP A O   1 
ATOM   678  C CB  . ASP A 1 84  ? -18.478 1.332   10.984  1.00 26.31  ? 99  ASP A CB  1 
ATOM   679  C CG  . ASP A 1 84  ? -19.880 1.640   11.492  1.00 23.30  ? 99  ASP A CG  1 
ATOM   680  O OD1 . ASP A 1 84  ? -20.589 2.446   10.831  1.00 26.03  ? 99  ASP A OD1 1 
ATOM   681  O OD2 . ASP A 1 84  ? -20.247 1.008   12.508  1.00 27.57  ? 99  ASP A OD2 1 
ATOM   682  N N   . LYS A 1 85  ? -16.646 0.100   8.617   1.00 25.52  ? 100 LYS A N   1 
ATOM   683  C CA  . LYS A 1 85  ? -15.394 -0.535  8.248   1.00 26.96  ? 100 LYS A CA  1 
ATOM   684  C C   . LYS A 1 85  ? -15.092 -0.357  6.760   1.00 24.69  ? 100 LYS A C   1 
ATOM   685  O O   . LYS A 1 85  ? -14.043 -0.797  6.308   1.00 26.73  ? 100 LYS A O   1 
ATOM   686  C CB  . LYS A 1 85  ? -15.458 -2.033  8.535   1.00 31.04  ? 100 LYS A CB  1 
ATOM   687  C CG  . LYS A 1 85  ? -14.119 -2.752  8.688   1.00 42.32  ? 100 LYS A CG  1 
ATOM   688  C CD  . LYS A 1 85  ? -14.129 -4.221  9.129   1.00 50.15  ? 100 LYS A CD  1 
ATOM   689  C CE  . LYS A 1 85  ? -12.739 -4.772  9.348   1.00 49.61  ? 100 LYS A CE  1 
ATOM   690  N NZ  . LYS A 1 85  ? -12.743 -6.207  9.698   1.00 53.71  ? 100 LYS A NZ  1 
ATOM   691  N N   . LYS A 1 86  ? -15.996 0.297   6.008   1.00 22.84  ? 101 LYS A N   1 
ATOM   692  C CA  . LYS A 1 86  ? -15.787 0.591   4.603   1.00 22.46  ? 101 LYS A CA  1 
ATOM   693  C C   . LYS A 1 86  ? -15.569 -0.701  3.811   1.00 21.59  ? 101 LYS A C   1 
ATOM   694  O O   . LYS A 1 86  ? -14.795 -0.713  2.842   1.00 23.18  ? 101 LYS A O   1 
ATOM   695  C CB  . LYS A 1 86  ? -14.668 1.617   4.401   1.00 23.86  ? 101 LYS A CB  1 
ATOM   696  C CG  . LYS A 1 86  ? -14.841 2.944   5.129   1.00 25.18  ? 101 LYS A CG  1 
ATOM   697  C CD  . LYS A 1 86  ? -13.776 3.970   4.766   1.00 28.53  ? 101 LYS A CD  1 
ATOM   698  C CE  . LYS A 1 86  ? -13.787 5.198   5.674   1.00 33.34  ? 101 LYS A CE  1 
ATOM   699  N NZ  . LYS A 1 86  ? -15.036 5.946   5.568   1.00 39.57  ? 101 LYS A NZ  1 
ATOM   700  N N   . PHE A 1 87  ? -16.323 -1.763  4.150   1.00 21.78  ? 102 PHE A N   1 
ATOM   701  C CA  . PHE A 1 87  ? -16.212 -3.045  3.463   1.00 20.76  ? 102 PHE A CA  1 
ATOM   702  C C   . PHE A 1 87  ? -17.373 -3.172  2.466   1.00 20.40  ? 102 PHE A C   1 
ATOM   703  O O   . PHE A 1 87  ? -18.480 -3.598  2.803   1.00 20.61  ? 102 PHE A O   1 
ATOM   704  C CB  . PHE A 1 87  ? -16.163 -4.224  4.461   1.00 22.23  ? 102 PHE A CB  1 
ATOM   705  C CG  . PHE A 1 87  ? -15.872 -5.534  3.744   1.00 21.66  ? 102 PHE A CG  1 
ATOM   706  C CD1 . PHE A 1 87  ? -14.652 -5.746  3.137   1.00 22.68  ? 102 PHE A CD1 1 
ATOM   707  C CD2 . PHE A 1 87  ? -16.811 -6.540  3.652   1.00 21.83  ? 102 PHE A CD2 1 
ATOM   708  C CE1 . PHE A 1 87  ? -14.386 -6.895  2.414   1.00 21.56  ? 102 PHE A CE1 1 
ATOM   709  C CE2 . PHE A 1 87  ? -16.549 -7.692  2.942   1.00 23.55  ? 102 PHE A CE2 1 
ATOM   710  C CZ  . PHE A 1 87  ? -15.341 -7.874  2.313   1.00 21.92  ? 102 PHE A CZ  1 
ATOM   711  N N   . ALA A 1 88  ? -17.120 -2.752  1.223   1.00 19.86  ? 103 ALA A N   1 
ATOM   712  C CA  . ALA A 1 88  ? -18.182 -2.580  0.247   1.00 19.07  ? 103 ALA A CA  1 
ATOM   713  C C   . ALA A 1 88  ? -18.973 -3.854  -0.016  1.00 19.26  ? 103 ALA A C   1 
ATOM   714  O O   . ALA A 1 88  ? -20.182 -3.728  -0.245  1.00 19.91  ? 103 ALA A O   1 
ATOM   715  C CB  . ALA A 1 88  ? -17.654 -2.026  -1.040  1.00 20.95  ? 103 ALA A CB  1 
ATOM   716  N N   . PRO A 1 89  ? -18.405 -5.066  0.025   1.00 19.78  ? 104 PRO A N   1 
ATOM   717  C CA  . PRO A 1 89  ? -19.220 -6.259  -0.234  1.00 18.81  ? 104 PRO A CA  1 
ATOM   718  C C   . PRO A 1 89  ? -20.271 -6.549  0.845   1.00 19.72  ? 104 PRO A C   1 
ATOM   719  O O   . PRO A 1 89  ? -21.108 -7.415  0.639   1.00 20.74  ? 104 PRO A O   1 
ATOM   720  C CB  . PRO A 1 89  ? -18.204 -7.366  -0.400  1.00 20.35  ? 104 PRO A CB  1 
ATOM   721  C CG  . PRO A 1 89  ? -16.937 -6.648  -0.804  1.00 19.62  ? 104 PRO A CG  1 
ATOM   722  C CD  . PRO A 1 89  ? -16.974 -5.398  0.034   1.00 18.94  ? 104 PRO A CD  1 
ATOM   723  N N   . ALA A 1 90  ? -20.257 -5.859  1.994   1.00 18.94  ? 105 ALA A N   1 
ATOM   724  C CA  . ALA A 1 90  ? -21.375 -5.994  2.923   1.00 18.03  ? 105 ALA A CA  1 
ATOM   725  C C   . ALA A 1 90  ? -22.627 -5.242  2.455   1.00 18.94  ? 105 ALA A C   1 
ATOM   726  O O   . ALA A 1 90  ? -23.730 -5.568  2.901   1.00 19.02  ? 105 ALA A O   1 
ATOM   727  C CB  . ALA A 1 90  ? -20.984 -5.462  4.279   1.00 19.73  ? 105 ALA A CB  1 
ATOM   728  N N   . CYS A 1 91  ? -22.463 -4.203  1.624   1.00 18.38  ? 106 CYS A N   1 
ATOM   729  C CA  . CYS A 1 91  ? -23.501 -3.207  1.427   1.00 18.05  ? 106 CYS A CA  1 
ATOM   730  C C   . CYS A 1 91  ? -24.763 -3.724  0.758   1.00 18.13  ? 106 CYS A C   1 
ATOM   731  O O   . CYS A 1 91  ? -25.816 -3.126  1.008   1.00 19.87  ? 106 CYS A O   1 
ATOM   732  C CB  . CYS A 1 91  ? -22.934 -2.010  0.664   1.00 20.35  ? 106 CYS A CB  1 
ATOM   733  S SG  . CYS A 1 91  ? -21.557 -1.166  1.503   1.00 21.98  ? 106 CYS A SG  1 
ATOM   734  N N   . ASN A 1 92  ? -24.668 -4.755  -0.093  1.00 18.05  ? 107 ASN A N   1 
ATOM   735  C CA  . ASN A 1 92  ? -25.840 -5.283  -0.792  1.00 18.28  ? 107 ASN A CA  1 
ATOM   736  C C   . ASN A 1 92  ? -26.307 -6.591  -0.170  1.00 17.25  ? 107 ASN A C   1 
ATOM   737  O O   . ASN A 1 92  ? -27.250 -7.154  -0.691  1.00 18.58  ? 107 ASN A O   1 
ATOM   738  C CB  . ASN A 1 92  ? -25.575 -5.422  -2.278  1.00 18.45  ? 107 ASN A CB  1 
ATOM   739  C CG  . ASN A 1 92  ? -24.479 -6.401  -2.602  1.00 18.75  ? 107 ASN A CG  1 
ATOM   740  O OD1 . ASN A 1 92  ? -23.895 -6.985  -1.690  1.00 20.54  ? 107 ASN A OD1 1 
ATOM   741  N ND2 . ASN A 1 92  ? -24.247 -6.576  -3.881  1.00 19.78  ? 107 ASN A ND2 1 
ATOM   742  N N   . ILE A 1 93  ? -25.768 -7.036  0.958   1.00 17.93  ? 108 ILE A N   1 
ATOM   743  C CA  . ILE A 1 93  ? -26.118 -8.357  1.460   1.00 18.22  ? 108 ILE A CA  1 
ATOM   744  C C   . ILE A 1 93  ? -27.593 -8.426  1.851   1.00 18.36  ? 108 ILE A C   1 
ATOM   745  O O   . ILE A 1 93  ? -28.261 -9.403  1.533   1.00 18.57  ? 108 ILE A O   1 
ATOM   746  C CB  . ILE A 1 93  ? -25.141 -8.855  2.552   1.00 17.80  ? 108 ILE A CB  1 
ATOM   747  C CG1 . ILE A 1 93  ? -23.838 -9.260  1.877   1.00 19.30  ? 108 ILE A CG1 1 
ATOM   748  C CG2 . ILE A 1 93  ? -25.744 -9.996  3.378   1.00 19.76  ? 108 ILE A CG2 1 
ATOM   749  C CD1 . ILE A 1 93  ? -22.734 -9.728  2.802   1.00 20.99  ? 108 ILE A CD1 1 
ATOM   750  N N   . PRO A 1 94  ? -28.161 -7.478  2.620   1.00 18.52  ? 109 PRO A N   1 
ATOM   751  C CA  . PRO A 1 94  ? -29.591 -7.596  2.944   1.00 18.40  ? 109 PRO A CA  1 
ATOM   752  C C   . PRO A 1 94  ? -30.469 -7.558  1.711   1.00 18.18  ? 109 PRO A C   1 
ATOM   753  O O   . PRO A 1 94  ? -31.450 -8.306  1.604   1.00 19.33  ? 109 PRO A O   1 
ATOM   754  C CB  . PRO A 1 94  ? -29.833 -6.421  3.895   1.00 19.15  ? 109 PRO A CB  1 
ATOM   755  C CG  . PRO A 1 94  ? -28.484 -6.089  4.489   1.00 19.70  ? 109 PRO A CG  1 
ATOM   756  C CD  . PRO A 1 94  ? -27.520 -6.365  3.336   1.00 19.64  ? 109 PRO A CD  1 
ATOM   757  N N   . ALA A 1 95  ? -30.126 -6.707  0.742   1.00 18.04  ? 110 ALA A N   1 
ATOM   758  C CA  . ALA A 1 95  ? -30.880 -6.640  -0.499  1.00 19.13  ? 110 ALA A CA  1 
ATOM   759  C C   . ALA A 1 95  ? -30.884 -8.004  -1.175  1.00 17.92  ? 110 ALA A C   1 
ATOM   760  O O   . ALA A 1 95  ? -31.906 -8.460  -1.630  1.00 19.67  ? 110 ALA A O   1 
ATOM   761  C CB  . ALA A 1 95  ? -30.363 -5.597  -1.428  1.00 19.83  ? 110 ALA A CB  1 
ATOM   762  N N   . ILE A 1 96  ? -29.718 -8.629  -1.294  1.00 18.07  ? 111 ILE A N   1 
ATOM   763  C CA  . ILE A 1 96  ? -29.649 -9.927  -1.954  1.00 18.30  ? 111 ILE A CA  1 
ATOM   764  C C   . ILE A 1 96  ? -30.400 -10.986 -1.133  1.00 17.66  ? 111 ILE A C   1 
ATOM   765  O O   . ILE A 1 96  ? -31.224 -11.719 -1.671  1.00 19.18  ? 111 ILE A O   1 
ATOM   766  C CB  . ILE A 1 96  ? -28.180 -10.323 -2.172  1.00 18.90  ? 111 ILE A CB  1 
ATOM   767  C CG1 . ILE A 1 96  ? -27.488 -9.378  -3.124  1.00 20.43  ? 111 ILE A CG1 1 
ATOM   768  C CG2 . ILE A 1 96  ? -28.070 -11.793 -2.641  1.00 19.75  ? 111 ILE A CG2 1 
ATOM   769  C CD1 . ILE A 1 96  ? -25.974 -9.507  -2.977  1.00 26.67  ? 111 ILE A CD1 1 
ATOM   770  N N   . ASP A 1 97  ? -30.065 -11.112 0.139   1.00 17.45  ? 112 ASP A N   1 
ATOM   771  C CA  . ASP A 1 97  ? -30.549 -12.210 0.951   1.00 18.04  ? 112 ASP A CA  1 
ATOM   772  C C   . ASP A 1 97  ? -32.047 -12.126 1.244   1.00 18.83  ? 112 ASP A C   1 
ATOM   773  O O   . ASP A 1 97  ? -32.719 -13.163 1.391   1.00 21.11  ? 112 ASP A O   1 
ATOM   774  C CB  . ASP A 1 97  ? -29.792 -12.361 2.259   1.00 18.39  ? 112 ASP A CB  1 
ATOM   775  C CG  . ASP A 1 97  ? -28.404 -12.982 2.162   1.00 19.26  ? 112 ASP A CG  1 
ATOM   776  O OD1 . ASP A 1 97  ? -28.023 -13.346 1.029   1.00 22.82  ? 112 ASP A OD1 1 
ATOM   777  O OD2 . ASP A 1 97  ? -27.732 -13.002 3.226   1.00 22.27  ? 112 ASP A OD2 1 
ATOM   778  N N   . LEU A 1 98  ? -32.568 -10.894 1.394   1.00 19.10  ? 113 LEU A N   1 
ATOM   779  C CA  . LEU A 1 98  ? -33.925 -10.686 1.888   1.00 17.89  ? 113 LEU A CA  1 
ATOM   780  C C   . LEU A 1 98  ? -34.890 -10.115 0.851   1.00 19.03  ? 113 LEU A C   1 
ATOM   781  O O   . LEU A 1 98  ? -36.096 -10.060 1.121   1.00 21.70  ? 113 LEU A O   1 
ATOM   782  C CB  . LEU A 1 98  ? -33.880 -9.814  3.148   1.00 20.91  ? 113 LEU A CB  1 
ATOM   783  C CG  . LEU A 1 98  ? -32.989 -10.308 4.287   1.00 21.30  ? 113 LEU A CG  1 
ATOM   784  C CD1 . LEU A 1 98  ? -32.918 -9.362  5.439   1.00 23.90  ? 113 LEU A CD1 1 
ATOM   785  C CD2 . LEU A 1 98  ? -33.405 -11.707 4.727   1.00 22.94  ? 113 LEU A CD2 1 
ATOM   786  N N   . ILE A 1 99  ? -34.401 -9.688  -0.320  1.00 17.77  ? 114 ILE A N   1 
ATOM   787  C CA  . ILE A 1 99  ? -35.251 -9.203  -1.392  1.00 18.48  ? 114 ILE A CA  1 
ATOM   788  C C   . ILE A 1 99  ? -35.029 -10.000 -2.675  1.00 18.01  ? 114 ILE A C   1 
ATOM   789  O O   . ILE A 1 99  ? -35.934 -10.675 -3.159  1.00 20.18  ? 114 ILE A O   1 
ATOM   790  C CB  . ILE A 1 99  ? -35.120 -7.677  -1.621  1.00 20.63  ? 114 ILE A CB  1 
ATOM   791  C CG1 . ILE A 1 99  ? -35.236 -6.876  -0.337  1.00 22.25  ? 114 ILE A CG1 1 
ATOM   792  C CG2 . ILE A 1 99  ? -36.138 -7.222  -2.650  1.00 20.55  ? 114 ILE A CG2 1 
ATOM   793  C CD1 . ILE A 1 99  ? -35.006 -5.373  -0.501  1.00 24.63  ? 114 ILE A CD1 1 
ATOM   794  N N   . GLN A 1 100 ? -33.828 -9.933  -3.234  1.00 18.59  ? 115 GLN A N   1 
ATOM   795  C CA  . GLN A 1 100 ? -33.522 -10.606 -4.486  1.00 17.99  ? 115 GLN A CA  1 
ATOM   796  C C   . GLN A 1 100 ? -33.818 -12.107 -4.377  1.00 17.17  ? 115 GLN A C   1 
ATOM   797  O O   . GLN A 1 100 ? -34.451 -12.688 -5.273  1.00 19.66  ? 115 GLN A O   1 
ATOM   798  C CB  . GLN A 1 100 ? -32.070 -10.348 -4.894  1.00 18.45  ? 115 GLN A CB  1 
ATOM   799  C CG  . GLN A 1 100 ? -31.709 -10.719 -6.328  1.00 19.95  ? 115 GLN A CG  1 
ATOM   800  C CD  . GLN A 1 100 ? -31.388 -12.173 -6.555  1.00 20.86  ? 115 GLN A CD  1 
ATOM   801  O OE1 . GLN A 1 100 ? -31.198 -12.914 -5.594  1.00 21.49  ? 115 GLN A OE1 1 
ATOM   802  N NE2 . GLN A 1 100 ? -31.274 -12.505 -7.834  1.00 23.25  ? 115 GLN A NE2 1 
ATOM   803  N N   . GLN A 1 101 ? -33.373 -12.723 -3.269  1.00 18.29  ? 116 GLN A N   1 
ATOM   804  C CA  . GLN A 1 101 ? -33.490 -14.164 -3.102  1.00 18.87  ? 116 GLN A CA  1 
ATOM   805  C C   . GLN A 1 101 ? -34.937 -14.553 -2.776  1.00 19.63  ? 116 GLN A C   1 
ATOM   806  O O   . GLN A 1 101 ? -35.333 -15.674 -3.053  1.00 20.89  ? 116 GLN A O   1 
ATOM   807  C CB  . GLN A 1 101 ? -32.503 -14.638 -2.039  1.00 19.56  ? 116 GLN A CB  1 
ATOM   808  C CG  . GLN A 1 101 ? -31.088 -14.683 -2.592  1.00 20.38  ? 116 GLN A CG  1 
ATOM   809  C CD  . GLN A 1 101 ? -30.959 -15.881 -3.500  1.00 20.96  ? 116 GLN A CD  1 
ATOM   810  O OE1 . GLN A 1 101 ? -30.928 -17.024 -3.025  1.00 22.85  ? 116 GLN A OE1 1 
ATOM   811  N NE2 . GLN A 1 101 ? -30.870 -15.644 -4.804  1.00 21.76  ? 116 GLN A NE2 1 
ATOM   812  N N   . LYS A 1 102 ? -35.708 -13.658 -2.135  1.00 18.86  ? 117 LYS A N   1 
ATOM   813  C CA  . LYS A 1 102 ? -37.123 -13.878 -1.857  1.00 20.82  ? 117 LYS A CA  1 
ATOM   814  C C   . LYS A 1 102 ? -37.893 -13.903 -3.170  1.00 19.24  ? 117 LYS A C   1 
ATOM   815  O O   . LYS A 1 102 ? -38.625 -14.833 -3.491  1.00 22.06  ? 117 LYS A O   1 
ATOM   816  C CB  . LYS A 1 102 ? -37.656 -12.762 -0.953  1.00 21.23  ? 117 LYS A CB  1 
ATOM   817  C CG  . LYS A 1 102 ? -39.173 -12.865 -0.796  1.00 22.68  ? 117 LYS A CG  1 
ATOM   818  C CD  . LYS A 1 102 ? -39.671 -11.948 0.315   1.00 27.19  ? 117 LYS A CD  1 
ATOM   819  C CE  . LYS A 1 102 ? -41.136 -11.855 0.355   1.00 33.60  ? 117 LYS A CE  1 
ATOM   820  N NZ  . LYS A 1 102 ? -41.578 -10.877 1.369   1.00 40.47  ? 117 LYS A NZ  1 
ATOM   821  N N   . LEU A 1 103 ? -37.683 -12.911 -4.018  1.00 20.06  ? 118 LEU A N   1 
ATOM   822  C CA  . LEU A 1 103 ? -38.371 -12.851 -5.298  1.00 21.14  ? 118 LEU A CA  1 
ATOM   823  C C   . LEU A 1 103 ? -37.940 -14.018 -6.191  1.00 20.30  ? 118 LEU A C   1 
ATOM   824  O O   . LEU A 1 103 ? -38.769 -14.564 -6.931  1.00 23.35  ? 118 LEU A O   1 
ATOM   825  C CB  . LEU A 1 103 ? -38.146 -11.502 -5.978  1.00 21.64  ? 118 LEU A CB  1 
ATOM   826  C CG  . LEU A 1 103 ? -39.002 -10.334 -5.469  1.00 24.00  ? 118 LEU A CG  1 
ATOM   827  C CD1 . LEU A 1 103 ? -39.044 -10.159 -3.976  1.00 30.37  ? 118 LEU A CD1 1 
ATOM   828  C CD2 . LEU A 1 103 ? -38.557 -9.013  -6.067  1.00 24.98  ? 118 LEU A CD2 1 
ATOM   829  N N   . SER A 1 104 ? -36.661 -14.451 -6.078  1.00 21.29  ? 119 SER A N   1 
ATOM   830  C CA  . SER A 1 104 ? -36.211 -15.611 -6.830  1.00 22.22  ? 119 SER A CA  1 
ATOM   831  C C   . SER A 1 104 ? -37.011 -16.856 -6.435  1.00 21.50  ? 119 SER A C   1 
ATOM   832  O O   . SER A 1 104 ? -37.388 -17.674 -7.288  1.00 23.93  ? 119 SER A O   1 
ATOM   833  C CB  . SER A 1 104 ? -34.724 -15.821 -6.645  1.00 22.98  ? 119 SER A CB  1 
ATOM   834  O OG  . SER A 1 104 ? -33.971 -14.797 -7.269  1.00 24.16  ? 119 SER A OG  1 
ATOM   835  N N   . TYR A 1 105 ? -37.192 -17.027 -5.119  1.00 22.05  ? 120 TYR A N   1 
ATOM   836  C CA  . TYR A 1 105 ? -37.949 -18.154 -4.590  1.00 22.89  ? 120 TYR A CA  1 
ATOM   837  C C   . TYR A 1 105 ? -39.369 -18.154 -5.154  1.00 21.55  ? 120 TYR A C   1 
ATOM   838  O O   . TYR A 1 105 ? -39.881 -19.219 -5.521  1.00 23.77  ? 120 TYR A O   1 
ATOM   839  C CB  . TYR A 1 105 ? -37.961 -18.077 -3.075  1.00 22.49  ? 120 TYR A CB  1 
ATOM   840  C CG  . TYR A 1 105 ? -38.713 -19.203 -2.366  1.00 22.49  ? 120 TYR A CG  1 
ATOM   841  C CD1 . TYR A 1 105 ? -40.088 -19.181 -2.234  1.00 23.23  ? 120 TYR A CD1 1 
ATOM   842  C CD2 . TYR A 1 105 ? -38.038 -20.255 -1.745  1.00 25.15  ? 120 TYR A CD2 1 
ATOM   843  C CE1 . TYR A 1 105 ? -40.768 -20.147 -1.525  1.00 27.02  ? 120 TYR A CE1 1 
ATOM   844  C CE2 . TYR A 1 105 ? -38.702 -21.208 -0.991  1.00 27.45  ? 120 TYR A CE2 1 
ATOM   845  C CZ  . TYR A 1 105 ? -40.078 -21.166 -0.874  1.00 27.81  ? 120 TYR A CZ  1 
ATOM   846  O OH  . TYR A 1 105 ? -40.783 -22.145 -0.196  1.00 31.61  ? 120 TYR A OH  1 
ATOM   847  N N   . TYR A 1 106 ? -40.023 -16.985 -5.231  1.00 22.50  ? 121 TYR A N   1 
ATOM   848  C CA  . TYR A 1 106 ? -41.375 -16.911 -5.806  1.00 23.61  ? 121 TYR A CA  1 
ATOM   849  C C   . TYR A 1 106 ? -41.376 -17.317 -7.291  1.00 23.78  ? 121 TYR A C   1 
ATOM   850  O O   . TYR A 1 106 ? -42.316 -17.980 -7.762  1.00 26.67  ? 121 TYR A O   1 
ATOM   851  C CB  . TYR A 1 106 ? -41.988 -15.513 -5.619  1.00 24.22  ? 121 TYR A CB  1 
ATOM   852  C CG  . TYR A 1 106 ? -42.576 -15.240 -4.247  1.00 26.38  ? 121 TYR A CG  1 
ATOM   853  C CD1 . TYR A 1 106 ? -41.840 -15.397 -3.107  1.00 22.82  ? 121 TYR A CD1 1 
ATOM   854  C CD2 . TYR A 1 106 ? -43.949 -15.037 -4.084  1.00 30.84  ? 121 TYR A CD2 1 
ATOM   855  C CE1 . TYR A 1 106 ? -42.363 -15.164 -1.850  1.00 26.38  ? 121 TYR A CE1 1 
ATOM   856  C CE2 . TYR A 1 106 ? -44.501 -14.846 -2.831  1.00 33.86  ? 121 TYR A CE2 1 
ATOM   857  C CZ  . TYR A 1 106 ? -43.702 -14.891 -1.704  1.00 31.15  ? 121 TYR A CZ  1 
ATOM   858  O OH  . TYR A 1 106 ? -44.176 -14.714 -0.423  1.00 36.94  ? 121 TYR A OH  1 
ATOM   859  N N   . VAL A 1 107 ? -40.317 -16.978 -8.042  1.00 23.62  ? 122 VAL A N   1 
ATOM   860  C CA  . VAL A 1 107 ? -40.209 -17.409 -9.433  1.00 25.10  ? 122 VAL A CA  1 
ATOM   861  C C   . VAL A 1 107 ? -40.017 -18.919 -9.535  1.00 24.62  ? 122 VAL A C   1 
ATOM   862  O O   . VAL A 1 107 ? -40.757 -19.573 -10.284 1.00 28.41  ? 122 VAL A O   1 
ATOM   863  C CB  . VAL A 1 107 ? -39.079 -16.682 -10.163 1.00 25.80  ? 122 VAL A CB  1 
ATOM   864  C CG1 . VAL A 1 107 ? -38.827 -17.293 -11.539 1.00 27.74  ? 122 VAL A CG1 1 
ATOM   865  C CG2 . VAL A 1 107 ? -39.375 -15.196 -10.260 1.00 27.72  ? 122 VAL A CG2 1 
ATOM   866  N N   . ARG A 1 108 ? -39.099 -19.489 -8.736  1.00 24.87  ? 123 ARG A N   1 
ATOM   867  C CA  . ARG A 1 108 ? -38.817 -20.924 -8.782  1.00 25.96  ? 123 ARG A CA  1 
ATOM   868  C C   . ARG A 1 108 ? -40.048 -21.772 -8.441  1.00 30.97  ? 123 ARG A C   1 
ATOM   869  O O   . ARG A 1 108 ? -40.243 -22.854 -9.023  1.00 34.61  ? 123 ARG A O   1 
ATOM   870  C CB  . ARG A 1 108 ? -37.714 -21.307 -7.796  1.00 28.55  ? 123 ARG A CB  1 
ATOM   871  C CG  . ARG A 1 108 ? -36.354 -20.796 -8.192  1.00 29.41  ? 123 ARG A CG  1 
ATOM   872  C CD  . ARG A 1 108 ? -35.310 -21.546 -7.404  1.00 26.28  ? 123 ARG A CD  1 
ATOM   873  N NE  . ARG A 1 108 ? -35.358 -21.436 -5.941  1.00 26.50  ? 123 ARG A NE  1 
ATOM   874  C CZ  . ARG A 1 108 ? -34.928 -20.389 -5.242  1.00 26.23  ? 123 ARG A CZ  1 
ATOM   875  N NH1 . ARG A 1 108 ? -34.254 -19.413 -5.824  1.00 26.01  ? 123 ARG A NH1 1 
ATOM   876  N NH2 . ARG A 1 108 ? -35.085 -20.386 -3.950  1.00 25.95  ? 123 ARG A NH2 1 
ATOM   877  N N   . ASN A 1 109 ? -40.856 -21.279 -7.483  1.00 27.27  ? 124 ASN A N   1 
ATOM   878  C CA  . ASN A 1 109 ? -41.952 -22.034 -6.890  1.00 27.91  ? 124 ASN A CA  1 
ATOM   879  C C   . ASN A 1 109 ? -43.317 -21.589 -7.454  1.00 33.20  ? 124 ASN A C   1 
ATOM   880  O O   . ASN A 1 109 ? -44.371 -22.017 -6.969  1.00 35.91  ? 124 ASN A O   1 
ATOM   881  C CB  . ASN A 1 109 ? -41.772 -22.012 -5.380  1.00 28.72  ? 124 ASN A CB  1 
ATOM   882  C CG  . ASN A 1 109 ? -40.479 -22.659 -4.920  1.00 29.64  ? 124 ASN A CG  1 
ATOM   883  O OD1 . ASN A 1 109 ? -39.525 -22.031 -4.397  1.00 30.69  ? 124 ASN A OD1 1 
ATOM   884  N ND2 . ASN A 1 109 ? -40.426 -23.964 -5.080  1.00 30.81  ? 124 ASN A ND2 1 
ATOM   885  N N   . ASP A 1 110 ? -43.313 -20.782 -8.531  1.00 32.78  ? 125 ASP A N   1 
ATOM   886  C CA  . ASP A 1 110 ? -44.535 -20.347 -9.207  1.00 35.57  ? 125 ASP A CA  1 
ATOM   887  C C   . ASP A 1 110 ? -45.546 -19.735 -8.239  1.00 34.66  ? 125 ASP A C   1 
ATOM   888  O O   . ASP A 1 110 ? -46.727 -20.083 -8.259  1.00 40.64  ? 125 ASP A O   1 
ATOM   889  C CB  . ASP A 1 110 ? -45.209 -21.475 -9.968  1.00 41.55  ? 125 ASP A CB  1 
ATOM   890  C CG  . ASP A 1 110 ? -44.248 -22.271 -10.825 1.00 45.18  ? 125 ASP A CG  1 
ATOM   891  O OD1 . ASP A 1 110 ? -43.311 -21.640 -11.352 1.00 49.06  ? 125 ASP A OD1 1 
ATOM   892  O OD2 . ASP A 1 110 ? -44.453 -23.502 -10.974 1.00 57.06  ? 125 ASP A OD2 1 
ATOM   893  N N   . ILE A 1 111 ? -45.084 -18.830 -7.395  1.00 33.70  ? 126 ILE A N   1 
ATOM   894  C CA  . ILE A 1 111 ? -45.932 -18.255 -6.375  1.00 35.86  ? 126 ILE A CA  1 
ATOM   895  C C   . ILE A 1 111 ? -46.429 -16.888 -6.837  1.00 39.07  ? 126 ILE A C   1 
ATOM   896  O O   . ILE A 1 111 ? -45.667 -16.074 -7.332  1.00 38.40  ? 126 ILE A O   1 
ATOM   897  C CB  . ILE A 1 111 ? -45.182 -18.176 -5.035  1.00 39.11  ? 126 ILE A CB  1 
ATOM   898  C CG1 . ILE A 1 111 ? -44.646 -19.541 -4.623  1.00 40.37  ? 126 ILE A CG1 1 
ATOM   899  C CG2 . ILE A 1 111 ? -46.094 -17.593 -3.959  1.00 42.11  ? 126 ILE A CG2 1 
ATOM   900  C CD1 . ILE A 1 111 ? -43.570 -19.486 -3.571  1.00 45.53  ? 126 ILE A CD1 1 
ATOM   901  N N   . ASP A 1 112 ? -47.738 -16.676 -6.687  1.00 42.86  ? 127 ASP A N   1 
ATOM   902  C CA  . ASP A 1 112 ? -48.354 -15.368 -6.877  1.00 44.54  ? 127 ASP A CA  1 
ATOM   903  C C   . ASP A 1 112 ? -48.113 -14.790 -8.275  1.00 45.19  ? 127 ASP A C   1 
ATOM   904  O O   . ASP A 1 112 ? -47.916 -13.589 -8.406  1.00 51.20  ? 127 ASP A O   1 
ATOM   905  C CB  . ASP A 1 112 ? -47.869 -14.402 -5.813  1.00 44.76  ? 127 ASP A CB  1 
ATOM   906  C CG  . ASP A 1 112 ? -48.415 -14.663 -4.419  1.00 54.27  ? 127 ASP A CG  1 
ATOM   907  O OD1 . ASP A 1 112 ? -49.273 -15.566 -4.278  1.00 62.24  ? 127 ASP A OD1 1 
ATOM   908  O OD2 . ASP A 1 112 ? -47.987 -13.946 -3.491  1.00 65.74  ? 127 ASP A OD2 1 
ATOM   909  N N   . ASN A 1 113 ? -48.099 -15.643 -9.307  1.00 47.54  ? 128 ASN A N   1 
ATOM   910  C CA  . ASN A 1 113 ? -47.940 -15.223 -10.694 1.00 50.32  ? 128 ASN A CA  1 
ATOM   911  C C   . ASN A 1 113 ? -46.650 -14.443 -10.932 1.00 47.27  ? 128 ASN A C   1 
ATOM   912  O O   . ASN A 1 113 ? -46.555 -13.686 -11.895 1.00 50.34  ? 128 ASN A O   1 
ATOM   913  C CB  . ASN A 1 113 ? -49.164 -14.462 -11.189 1.00 59.08  ? 128 ASN A CB  1 
ATOM   914  C CG  . ASN A 1 113 ? -50.359 -15.376 -11.254 1.00 64.76  ? 128 ASN A CG  1 
ATOM   915  O OD1 . ASN A 1 113 ? -50.306 -16.406 -11.938 1.00 66.56  ? 128 ASN A OD1 1 
ATOM   916  N ND2 . ASN A 1 113 ? -51.417 -15.045 -10.529 1.00 71.20  ? 128 ASN A ND2 1 
ATOM   917  N N   . LYS A 1 114 ? -45.628 -14.705 -10.117 1.00 40.80  ? 129 LYS A N   1 
ATOM   918  C CA  . LYS A 1 114 ? -44.307 -14.144 -10.362 1.00 37.02  ? 129 LYS A CA  1 
ATOM   919  C C   . LYS A 1 114 ? -43.558 -15.013 -11.369 1.00 32.12  ? 129 LYS A C   1 
ATOM   920  O O   . LYS A 1 114 ? -43.549 -16.242 -11.268 1.00 35.57  ? 129 LYS A O   1 
ATOM   921  C CB  . LYS A 1 114 ? -43.586 -13.985 -9.026  1.00 36.25  ? 129 LYS A CB  1 
ATOM   922  C CG  . LYS A 1 114 ? -44.333 -13.121 -8.025  1.00 39.27  ? 129 LYS A CG  1 
ATOM   923  C CD  . LYS A 1 114 ? -44.591 -11.693 -8.453  1.00 43.70  ? 129 LYS A CD  1 
ATOM   924  C CE  . LYS A 1 114 ? -45.391 -11.015 -7.375  1.00 47.92  ? 129 LYS A CE  1 
ATOM   925  N NZ  . LYS A 1 114 ? -45.444 -9.578  -7.623  1.00 55.23  ? 129 LYS A NZ  1 
ATOM   926  N N   . THR A 1 115 ? -42.922 -14.360 -12.350 1.00 32.24  ? 130 THR A N   1 
ATOM   927  C CA  . THR A 1 115 ? -42.208 -15.064 -13.406 1.00 30.28  ? 130 THR A CA  1 
ATOM   928  C C   . THR A 1 115 ? -40.888 -14.347 -13.695 1.00 31.07  ? 130 THR A C   1 
ATOM   929  O O   . THR A 1 115 ? -40.644 -13.224 -13.237 1.00 31.07  ? 130 THR A O   1 
ATOM   930  C CB  . THR A 1 115 ? -43.046 -15.117 -14.688 1.00 36.60  ? 130 THR A CB  1 
ATOM   931  O OG1 . THR A 1 115 ? -43.138 -13.775 -15.155 1.00 38.40  ? 130 THR A OG1 1 
ATOM   932  C CG2 . THR A 1 115 ? -44.470 -15.606 -14.483 1.00 38.29  ? 130 THR A CG2 1 
ATOM   933  N N   . ILE A 1 116 ? -40.054 -14.983 -14.517 1.00 29.35  ? 131 ILE A N   1 
ATOM   934  C CA  . ILE A 1 116 ? -38.826 -14.334 -14.948 1.00 33.87  ? 131 ILE A CA  1 
ATOM   935  C C   . ILE A 1 116 ? -39.145 -13.049 -15.718 1.00 32.69  ? 131 ILE A C   1 
ATOM   936  O O   . ILE A 1 116 ? -38.326 -12.144 -15.726 1.00 35.24  ? 131 ILE A O   1 
ATOM   937  C CB  . ILE A 1 116 ? -37.913 -15.268 -15.751 1.00 37.75  ? 131 ILE A CB  1 
ATOM   938  C CG1 . ILE A 1 116 ? -38.576 -15.885 -16.968 1.00 39.03  ? 131 ILE A CG1 1 
ATOM   939  C CG2 . ILE A 1 116 ? -37.334 -16.336 -14.840 1.00 42.94  ? 131 ILE A CG2 1 
ATOM   940  C CD1 . ILE A 1 116 ? -37.565 -16.318 -18.017 1.00 48.38  ? 131 ILE A CD1 1 
ATOM   941  N N   . LYS A 1 117 ? -40.309 -13.007 -16.385 1.00 33.61  ? 132 LYS A N   1 
ATOM   942  C CA  . LYS A 1 117 ? -40.737 -11.851 -17.145 1.00 34.75  ? 132 LYS A CA  1 
ATOM   943  C C   . LYS A 1 117 ? -40.858 -10.619 -16.249 1.00 34.20  ? 132 LYS A C   1 
ATOM   944  O O   . LYS A 1 117 ? -40.414 -9.549  -16.651 1.00 39.96  ? 132 LYS A O   1 
ATOM   945  C CB  . LYS A 1 117 ? -42.045 -12.160 -17.875 1.00 39.72  ? 132 LYS A CB  1 
ATOM   946  C CG  . LYS A 1 117 ? -42.846 -10.978 -18.416 1.00 49.85  ? 132 LYS A CG  1 
ATOM   947  C CD  . LYS A 1 117 ? -44.005 -11.466 -19.290 1.00 56.25  ? 132 LYS A CD  1 
ATOM   948  C CE  . LYS A 1 117 ? -45.091 -10.484 -19.623 1.00 62.69  ? 132 LYS A CE  1 
ATOM   949  N NZ  . LYS A 1 117 ? -44.647 -9.372  -20.463 1.00 68.31  ? 132 LYS A NZ  1 
ATOM   950  N N   . THR A 1 118 ? -41.416 -10.783 -15.040 1.00 30.90  ? 133 THR A N   1 
ATOM   951  C CA  . THR A 1 118 ? -41.679 -9.653  -14.158 1.00 33.69  ? 133 THR A CA  1 
ATOM   952  C C   . THR A 1 118 ? -40.555 -9.439  -13.154 1.00 28.93  ? 133 THR A C   1 
ATOM   953  O O   . THR A 1 118 ? -40.497 -8.383  -12.533 1.00 29.35  ? 133 THR A O   1 
ATOM   954  C CB  . THR A 1 118 ? -43.000 -9.789  -13.394 1.00 36.47  ? 133 THR A CB  1 
ATOM   955  O OG1 . THR A 1 118 ? -42.957 -10.949 -12.559 1.00 40.35  ? 133 THR A OG1 1 
ATOM   956  C CG2 . THR A 1 118 ? -44.178 -9.835  -14.343 1.00 44.23  ? 133 THR A CG2 1 
ATOM   957  N N   . PHE A 1 119 ? -39.666 -10.414 -13.013 1.00 26.16  ? 134 PHE A N   1 
ATOM   958  C CA  . PHE A 1 119 ? -38.707 -10.451 -11.923 1.00 25.43  ? 134 PHE A CA  1 
ATOM   959  C C   . PHE A 1 119 ? -37.856 -9.183  -11.839 1.00 23.38  ? 134 PHE A C   1 
ATOM   960  O O   . PHE A 1 119 ? -37.647 -8.669  -10.739 1.00 23.77  ? 134 PHE A O   1 
ATOM   961  C CB  . PHE A 1 119 ? -37.756 -11.648 -12.052 1.00 22.97  ? 134 PHE A CB  1 
ATOM   962  C CG  . PHE A 1 119 ? -36.651 -11.616 -11.027 1.00 22.91  ? 134 PHE A CG  1 
ATOM   963  C CD1 . PHE A 1 119 ? -36.855 -12.041 -9.722  1.00 21.98  ? 134 PHE A CD1 1 
ATOM   964  C CD2 . PHE A 1 119 ? -35.399 -11.155 -11.402 1.00 22.85  ? 134 PHE A CD2 1 
ATOM   965  C CE1 . PHE A 1 119 ? -35.866 -11.925 -8.776  1.00 24.70  ? 134 PHE A CE1 1 
ATOM   966  C CE2 . PHE A 1 119 ? -34.423 -11.071 -10.460 1.00 23.03  ? 134 PHE A CE2 1 
ATOM   967  C CZ  . PHE A 1 119 ? -34.646 -11.489 -9.162  1.00 24.02  ? 134 PHE A CZ  1 
ATOM   968  N N   . TYR A 1 120 ? -37.251 -8.769  -12.941 1.00 23.53  ? 135 TYR A N   1 
ATOM   969  C CA  . TYR A 1 120 ? -36.293 -7.671  -12.845 1.00 23.15  ? 135 TYR A CA  1 
ATOM   970  C C   . TYR A 1 120 ? -36.961 -6.341  -12.448 1.00 23.20  ? 135 TYR A C   1 
ATOM   971  O O   . TYR A 1 120 ? -36.397 -5.585  -11.657 1.00 23.22  ? 135 TYR A O   1 
ATOM   972  C CB  . TYR A 1 120 ? -35.511 -7.544  -14.154 1.00 24.76  ? 135 TYR A CB  1 
ATOM   973  C CG  . TYR A 1 120 ? -34.697 -8.801  -14.411 1.00 27.33  ? 135 TYR A CG  1 
ATOM   974  C CD1 . TYR A 1 120 ? -33.465 -8.990  -13.803 1.00 28.17  ? 135 TYR A CD1 1 
ATOM   975  C CD2 . TYR A 1 120 ? -35.226 -9.847  -15.146 1.00 31.36  ? 135 TYR A CD2 1 
ATOM   976  C CE1 . TYR A 1 120 ? -32.748 -10.177 -13.944 1.00 31.71  ? 135 TYR A CE1 1 
ATOM   977  C CE2 . TYR A 1 120 ? -34.511 -11.012 -15.336 1.00 33.48  ? 135 TYR A CE2 1 
ATOM   978  C CZ  . TYR A 1 120 ? -33.281 -11.188 -14.728 1.00 34.30  ? 135 TYR A CZ  1 
ATOM   979  O OH  . TYR A 1 120 ? -32.681 -12.407 -14.947 1.00 42.67  ? 135 TYR A OH  1 
ATOM   980  N N   . SER A 1 121 ? -38.140 -6.074  -13.012 1.00 24.30  ? 136 SER A N   1 
ATOM   981  C CA  . SER A 1 121 ? -38.984 -4.960  -12.631 1.00 25.39  ? 136 SER A CA  1 
ATOM   982  C C   . SER A 1 121 ? -39.426 -5.102  -11.167 1.00 23.43  ? 136 SER A C   1 
ATOM   983  O O   . SER A 1 121 ? -39.442 -4.145  -10.402 1.00 23.61  ? 136 SER A O   1 
ATOM   984  C CB  . SER A 1 121 ? -40.201 -4.908  -13.587 1.00 33.00  ? 136 SER A CB  1 
ATOM   985  O OG  . SER A 1 121 ? -41.088 -3.912  -13.146 1.00 46.37  ? 136 SER A OG  1 
ATOM   986  N N   . ASP A 1 122 ? -39.851 -6.301  -10.773 1.00 24.80  ? 137 ASP A N   1 
ATOM   987  C CA  . ASP A 1 122 ? -40.330 -6.550  -9.430  1.00 23.17  ? 137 ASP A CA  1 
ATOM   988  C C   . ASP A 1 122 ? -39.208 -6.266  -8.416  1.00 22.21  ? 137 ASP A C   1 
ATOM   989  O O   . ASP A 1 122 ? -39.440 -5.702  -7.350  1.00 22.33  ? 137 ASP A O   1 
ATOM   990  C CB  . ASP A 1 122 ? -40.809 -7.987  -9.307  1.00 25.79  ? 137 ASP A CB  1 
ATOM   991  C CG  . ASP A 1 122 ? -42.054 -8.361  -10.095 1.00 34.19  ? 137 ASP A CG  1 
ATOM   992  O OD1 . ASP A 1 122 ? -42.852 -7.430  -10.390 1.00 36.51  ? 137 ASP A OD1 1 
ATOM   993  O OD2 . ASP A 1 122 ? -42.174 -9.593  -10.442 1.00 38.43  ? 137 ASP A OD2 1 
ATOM   994  N N   . TYR A 1 123 ? -38.004 -6.756  -8.713  1.00 20.96  ? 138 TYR A N   1 
ATOM   995  C CA  . TYR A 1 123 ? -36.878 -6.566  -7.815  1.00 19.24  ? 138 TYR A CA  1 
ATOM   996  C C   . TYR A 1 123 ? -36.500 -5.089  -7.743  1.00 19.84  ? 138 TYR A C   1 
ATOM   997  O O   . TYR A 1 123 ? -36.255 -4.587  -6.639  1.00 20.53  ? 138 TYR A O   1 
ATOM   998  C CB  . TYR A 1 123 ? -35.704 -7.444  -8.240  1.00 20.59  ? 138 TYR A CB  1 
ATOM   999  C CG  . TYR A 1 123 ? -34.429 -7.297  -7.401  1.00 20.76  ? 138 TYR A CG  1 
ATOM   1000 C CD1 . TYR A 1 123 ? -34.500 -7.074  -6.050  1.00 21.65  ? 138 TYR A CD1 1 
ATOM   1001 C CD2 . TYR A 1 123 ? -33.163 -7.398  -7.964  1.00 22.01  ? 138 TYR A CD2 1 
ATOM   1002 C CE1 . TYR A 1 123 ? -33.380 -6.898  -5.275  1.00 21.45  ? 138 TYR A CE1 1 
ATOM   1003 C CE2 . TYR A 1 123 ? -32.018 -7.199  -7.202  1.00 21.46  ? 138 TYR A CE2 1 
ATOM   1004 C CZ  . TYR A 1 123 ? -32.126 -6.957  -5.851  1.00 21.03  ? 138 TYR A CZ  1 
ATOM   1005 O OH  . TYR A 1 123 ? -31.047 -6.780  -5.030  1.00 22.68  ? 138 TYR A OH  1 
ATOM   1006 N N   . ALA A 1 124 ? -36.482 -4.393  -8.887  1.00 19.78  ? 139 ALA A N   1 
ATOM   1007 C CA  . ALA A 1 124 ? -36.167 -2.974  -8.831  1.00 20.98  ? 139 ALA A CA  1 
ATOM   1008 C C   . ALA A 1 124 ? -37.172 -2.217  -7.952  1.00 20.52  ? 139 ALA A C   1 
ATOM   1009 O O   . ALA A 1 124 ? -36.772 -1.336  -7.184  1.00 21.17  ? 139 ALA A O   1 
ATOM   1010 C CB  . ALA A 1 124 ? -36.155 -2.422  -10.242 1.00 21.79  ? 139 ALA A CB  1 
ATOM   1011 N N   . LYS A 1 125 ? -38.477 -2.538  -8.099  1.00 21.15  ? 140 LYS A N   1 
ATOM   1012 C CA  . LYS A 1 125 ? -39.525 -1.888  -7.330  1.00 20.97  ? 140 LYS A CA  1 
ATOM   1013 C C   . LYS A 1 125 ? -39.329 -2.172  -5.847  1.00 21.31  ? 140 LYS A C   1 
ATOM   1014 O O   . LYS A 1 125 ? -39.307 -1.260  -5.020  1.00 22.25  ? 140 LYS A O   1 
ATOM   1015 C CB  . LYS A 1 125 ? -40.881 -2.366  -7.842  1.00 24.48  ? 140 LYS A CB  1 
ATOM   1016 C CG  . LYS A 1 125 ? -41.295 -1.813  -9.201  1.00 32.39  ? 140 LYS A CG  1 
ATOM   1017 C CD  . LYS A 1 125 ? -42.692 -2.305  -9.575  1.00 40.56  ? 140 LYS A CD  1 
ATOM   1018 C CE  . LYS A 1 125 ? -43.287 -1.800  -10.859 1.00 49.89  ? 140 LYS A CE  1 
ATOM   1019 N NZ  . LYS A 1 125 ? -44.517 -2.532  -11.191 1.00 54.28  ? 140 LYS A NZ  1 
ATOM   1020 N N   . ALA A 1 126 ? -39.105 -3.445  -5.483  1.00 21.88  ? 141 ALA A N   1 
ATOM   1021 C CA  . ALA A 1 126 ? -38.945 -3.789  -4.083  1.00 20.85  ? 141 ALA A CA  1 
ATOM   1022 C C   . ALA A 1 126 ? -37.669 -3.190  -3.468  1.00 20.58  ? 141 ALA A C   1 
ATOM   1023 O O   . ALA A 1 126 ? -37.680 -2.734  -2.320  1.00 22.54  ? 141 ALA A O   1 
ATOM   1024 C CB  . ALA A 1 126 ? -38.970 -5.283  -3.906  1.00 22.18  ? 141 ALA A CB  1 
ATOM   1025 N N   . LEU A 1 127 ? -36.563 -3.207  -4.228  1.00 20.52  ? 142 LEU A N   1 
ATOM   1026 C CA  . LEU A 1 127 ? -35.336 -2.652  -3.672  1.00 19.83  ? 142 LEU A CA  1 
ATOM   1027 C C   . LEU A 1 127 ? -35.474 -1.135  -3.464  1.00 19.68  ? 142 LEU A C   1 
ATOM   1028 O O   . LEU A 1 127 ? -35.053 -0.611  -2.433  1.00 20.57  ? 142 LEU A O   1 
ATOM   1029 C CB  . LEU A 1 127 ? -34.196 -2.947  -4.642  1.00 20.77  ? 142 LEU A CB  1 
ATOM   1030 C CG  . LEU A 1 127 ? -32.829 -2.363  -4.277  1.00 18.84  ? 142 LEU A CG  1 
ATOM   1031 C CD1 . LEU A 1 127 ? -32.374 -2.784  -2.899  1.00 20.11  ? 142 LEU A CD1 1 
ATOM   1032 C CD2 . LEU A 1 127 ? -31.831 -2.759  -5.330  1.00 18.96  ? 142 LEU A CD2 1 
ATOM   1033 N N   . SER A 1 128 ? -36.082 -0.438  -4.436  1.00 20.26  ? 143 SER A N   1 
ATOM   1034 C CA  . SER A 1 128 ? -36.238 1.011   -4.349  1.00 21.51  ? 143 SER A CA  1 
ATOM   1035 C C   . SER A 1 128 ? -37.105 1.405   -3.159  1.00 22.62  ? 143 SER A C   1 
ATOM   1036 O O   . SER A 1 128 ? -36.920 2.498   -2.638  1.00 25.86  ? 143 SER A O   1 
ATOM   1037 C CB  . SER A 1 128 ? -36.743 1.527   -5.645  1.00 23.33  ? 143 SER A CB  1 
ATOM   1038 O OG  . SER A 1 128 ? -38.122 1.226   -5.817  1.00 28.09  ? 143 SER A OG  1 
ATOM   1039 N N   . GLU A 1 129 ? -37.991 0.521   -2.691  1.00 22.40  ? 144 GLU A N   1 
ATOM   1040 C CA  . GLU A 1 129 ? -38.833 0.803   -1.528  1.00 24.39  ? 144 GLU A CA  1 
ATOM   1041 C C   . GLU A 1 129 ? -38.115 0.576   -0.193  1.00 23.23  ? 144 GLU A C   1 
ATOM   1042 O O   . GLU A 1 129 ? -38.574 1.040   0.842   1.00 29.22  ? 144 GLU A O   1 
ATOM   1043 C CB  . GLU A 1 129 ? -40.017 -0.159  -1.620  1.00 26.67  ? 144 GLU A CB  1 
ATOM   1044 C CG  . GLU A 1 129 ? -40.971 0.190   -2.744  1.00 35.68  ? 144 GLU A CG  1 
ATOM   1045 C CD  . GLU A 1 129 ? -41.864 -1.039  -3.069  1.00 42.68  ? 144 GLU A CD  1 
ATOM   1046 O OE1 . GLU A 1 129 ? -41.905 -2.023  -2.261  1.00 58.04  ? 144 GLU A OE1 1 
ATOM   1047 O OE2 . GLU A 1 129 ? -42.500 -1.005  -4.156  1.00 65.90  ? 144 GLU A OE2 1 
ATOM   1048 N N   . SER A 1 130 ? -36.962 -0.127  -0.221  1.00 22.67  ? 145 SER A N   1 
ATOM   1049 C CA  . SER A 1 130 ? -36.159 -0.409  0.960   1.00 20.61  ? 145 SER A CA  1 
ATOM   1050 C C   . SER A 1 130 ? -35.079 0.655   1.145   1.00 22.96  ? 145 SER A C   1 
ATOM   1051 O O   . SER A 1 130 ? -33.937 0.504   0.672   1.00 22.77  ? 145 SER A O   1 
ATOM   1052 C CB  . SER A 1 130 ? -35.527 -1.787  0.853   1.00 21.39  ? 145 SER A CB  1 
ATOM   1053 O OG  . SER A 1 130 ? -34.905 -2.130  2.095   1.00 25.64  ? 145 SER A OG  1 
ATOM   1054 N N   . LYS A 1 131 ? -35.433 1.761   1.790   1.00 25.07  ? 146 LYS A N   1 
ATOM   1055 C CA  . LYS A 1 131 ? -34.548 2.915   1.797   1.00 24.42  ? 146 LYS A CA  1 
ATOM   1056 C C   . LYS A 1 131 ? -33.250 2.626   2.550   1.00 22.90  ? 146 LYS A C   1 
ATOM   1057 O O   . LYS A 1 131 ? -32.206 3.180   2.187   1.00 23.66  ? 146 LYS A O   1 
ATOM   1058 C CB  . LYS A 1 131 ? -35.260 4.129   2.381   1.00 28.25  ? 146 LYS A CB  1 
ATOM   1059 C CG  . LYS A 1 131 ? -36.509 4.515   1.595   1.00 34.12  ? 146 LYS A CG  1 
ATOM   1060 C CD  . LYS A 1 131 ? -37.356 5.529   2.357   1.00 45.64  ? 146 LYS A CD  1 
ATOM   1061 C CE  . LYS A 1 131 ? -38.754 5.625   1.805   1.00 55.56  ? 146 LYS A CE  1 
ATOM   1062 N NZ  . LYS A 1 131 ? -39.484 6.736   2.406   1.00 60.34  ? 146 LYS A NZ  1 
ATOM   1063 N N   . ALA A 1 132 ? -33.297 1.789   3.588   1.00 23.76  ? 147 ALA A N   1 
ATOM   1064 C CA  . ALA A 1 132 ? -32.086 1.427   4.299   1.00 22.50  ? 147 ALA A CA  1 
ATOM   1065 C C   . ALA A 1 132 ? -31.091 0.793   3.316   1.00 21.70  ? 147 ALA A C   1 
ATOM   1066 O O   . ALA A 1 132 ? -29.873 1.029   3.402   1.00 22.45  ? 147 ALA A O   1 
ATOM   1067 C CB  . ALA A 1 132 ? -32.371 0.536   5.470   1.00 24.15  ? 147 ALA A CB  1 
ATOM   1068 N N   . ASP A 1 133 ? -31.599 -0.107  2.468   1.00 20.37  ? 148 ASP A N   1 
ATOM   1069 C CA  . ASP A 1 133 ? -30.724 -0.759  1.515   1.00 19.32  ? 148 ASP A CA  1 
ATOM   1070 C C   . ASP A 1 133 ? -30.208 0.194   0.445   1.00 19.53  ? 148 ASP A C   1 
ATOM   1071 O O   . ASP A 1 133 ? -29.010 0.191   0.131   1.00 19.98  ? 148 ASP A O   1 
ATOM   1072 C CB  . ASP A 1 133 ? -31.426 -1.962  0.913   1.00 20.03  ? 148 ASP A CB  1 
ATOM   1073 C CG  . ASP A 1 133 ? -31.672 -3.064  1.923   1.00 22.68  ? 148 ASP A CG  1 
ATOM   1074 O OD1 . ASP A 1 133 ? -30.758 -3.341  2.752   1.00 23.47  ? 148 ASP A OD1 1 
ATOM   1075 O OD2 . ASP A 1 133 ? -32.782 -3.623  1.904   1.00 27.91  ? 148 ASP A OD2 1 
ATOM   1076 N N   . VAL A 1 134 ? -31.077 1.021   -0.119  1.00 19.10  ? 149 VAL A N   1 
ATOM   1077 C CA  . VAL A 1 134 ? -30.673 1.989   -1.140  1.00 19.78  ? 149 VAL A CA  1 
ATOM   1078 C C   . VAL A 1 134 ? -29.551 2.848   -0.558  1.00 20.03  ? 149 VAL A C   1 
ATOM   1079 O O   . VAL A 1 134 ? -28.573 3.137   -1.259  1.00 19.83  ? 149 VAL A O   1 
ATOM   1080 C CB  . VAL A 1 134 ? -31.845 2.834   -1.669  1.00 20.80  ? 149 VAL A CB  1 
ATOM   1081 C CG1 . VAL A 1 134 ? -31.374 3.934   -2.610  1.00 22.92  ? 149 VAL A CG1 1 
ATOM   1082 C CG2 . VAL A 1 134 ? -32.836 1.922   -2.374  1.00 21.97  ? 149 VAL A CG2 1 
ATOM   1083 N N   . LYS A 1 135 ? -29.693 3.327   0.687   1.00 19.44  ? 150 LYS A N   1 
ATOM   1084 C CA  . LYS A 1 135 ? -28.625 4.172   1.215   1.00 21.21  ? 150 LYS A CA  1 
ATOM   1085 C C   . LYS A 1 135 ? -27.296 3.440   1.384   1.00 20.24  ? 150 LYS A C   1 
ATOM   1086 O O   . LYS A 1 135 ? -26.254 4.056   1.171   1.00 19.96  ? 150 LYS A O   1 
ATOM   1087 C CB  . LYS A 1 135 ? -29.096 4.831   2.511   1.00 22.90  ? 150 LYS A CB  1 
ATOM   1088 C CG  . LYS A 1 135 ? -30.103 5.992   2.310   1.00 26.92  ? 150 LYS A CG  1 
ATOM   1089 C CD  . LYS A 1 135 ? -29.341 7.265   1.952   1.00 38.04  ? 150 LYS A CD  1 
ATOM   1090 C CE  . LYS A 1 135 ? -30.140 8.484   1.580   1.00 47.08  ? 150 LYS A CE  1 
ATOM   1091 N NZ  . LYS A 1 135 ? -30.734 8.396   0.236   1.00 49.49  ? 150 LYS A NZ  1 
ATOM   1092 N N   . MET A 1 136 ? -27.305 2.149   1.746   1.00 18.63  ? 151 MET A N   1 
ATOM   1093 C CA  . MET A 1 136 ? -26.054 1.386   1.818   1.00 18.61  ? 151 MET A CA  1 
ATOM   1094 C C   . MET A 1 136 ? -25.457 1.222   0.420   1.00 18.40  ? 151 MET A C   1 
ATOM   1095 O O   . MET A 1 136 ? -24.236 1.278   0.270   1.00 19.09  ? 151 MET A O   1 
ATOM   1096 C CB  . MET A 1 136 ? -26.200 0.017   2.482   1.00 20.02  ? 151 MET A CB  1 
ATOM   1097 C CG  . MET A 1 136 ? -26.307 0.147   3.964   1.00 22.12  ? 151 MET A CG  1 
ATOM   1098 S SD  . MET A 1 136 ? -26.156 -1.389  4.874   1.00 25.21  ? 151 MET A SD  1 
ATOM   1099 C CE  . MET A 1 136 ? -27.676 -2.116  4.275   1.00 25.41  ? 151 MET A CE  1 
ATOM   1100 N N   . LEU A 1 137 ? -26.285 1.027   -0.599  1.00 18.27  ? 152 LEU A N   1 
ATOM   1101 C CA  . LEU A 1 137 ? -25.784 0.918   -1.962  1.00 18.90  ? 152 LEU A CA  1 
ATOM   1102 C C   . LEU A 1 137 ? -25.161 2.251   -2.370  1.00 19.04  ? 152 LEU A C   1 
ATOM   1103 O O   . LEU A 1 137 ? -24.116 2.285   -3.013  1.00 19.42  ? 152 LEU A O   1 
ATOM   1104 C CB  . LEU A 1 137 ? -26.867 0.498   -2.952  1.00 18.85  ? 152 LEU A CB  1 
ATOM   1105 C CG  . LEU A 1 137 ? -27.555 -0.853  -2.697  1.00 19.53  ? 152 LEU A CG  1 
ATOM   1106 C CD1 . LEU A 1 137 ? -28.678 -1.023  -3.712  1.00 20.74  ? 152 LEU A CD1 1 
ATOM   1107 C CD2 . LEU A 1 137 ? -26.616 -2.017  -2.697  1.00 18.66  ? 152 LEU A CD2 1 
ATOM   1108 N N   . GLU A 1 138 ? -25.819 3.364   -2.053  1.00 19.77  ? 153 GLU A N   1 
ATOM   1109 C CA  . GLU A 1 138 ? -25.283 4.652   -2.450  1.00 20.52  ? 153 GLU A CA  1 
ATOM   1110 C C   . GLU A 1 138 ? -23.910 4.869   -1.805  1.00 19.99  ? 153 GLU A C   1 
ATOM   1111 O O   . GLU A 1 138 ? -22.999 5.382   -2.444  1.00 22.04  ? 153 GLU A O   1 
ATOM   1112 C CB  . GLU A 1 138 ? -26.303 5.724   -2.090  1.00 21.01  ? 153 GLU A CB  1 
ATOM   1113 C CG  . GLU A 1 138 ? -27.509 5.792   -3.005  1.00 22.08  ? 153 GLU A CG  1 
ATOM   1114 C CD  . GLU A 1 138 ? -28.608 6.713   -2.549  1.00 24.18  ? 153 GLU A CD  1 
ATOM   1115 O OE1 . GLU A 1 138 ? -28.558 7.220   -1.412  1.00 27.79  ? 153 GLU A OE1 1 
ATOM   1116 O OE2 . GLU A 1 138 ? -29.534 6.898   -3.367  1.00 27.91  ? 153 GLU A OE2 1 
ATOM   1117 N N   . TYR A 1 139 ? -23.733 4.448   -0.561  1.00 19.64  ? 154 TYR A N   1 
ATOM   1118 C CA  . TYR A 1 139 ? -22.444 4.525   0.090   1.00 20.61  ? 154 TYR A CA  1 
ATOM   1119 C C   . TYR A 1 139 ? -21.407 3.648   -0.594  1.00 20.12  ? 154 TYR A C   1 
ATOM   1120 O O   . TYR A 1 139 ? -20.281 4.077   -0.880  1.00 20.97  ? 154 TYR A O   1 
ATOM   1121 C CB  . TYR A 1 139 ? -22.573 4.229   1.578   1.00 21.11  ? 154 TYR A CB  1 
ATOM   1122 C CG  . TYR A 1 139 ? -21.302 4.499   2.359   1.00 21.42  ? 154 TYR A CG  1 
ATOM   1123 C CD1 . TYR A 1 139 ? -20.956 5.790   2.721   1.00 22.48  ? 154 TYR A CD1 1 
ATOM   1124 C CD2 . TYR A 1 139 ? -20.504 3.460   2.826   1.00 20.89  ? 154 TYR A CD2 1 
ATOM   1125 C CE1 . TYR A 1 139 ? -19.819 6.044   3.456   1.00 23.58  ? 154 TYR A CE1 1 
ATOM   1126 C CE2 . TYR A 1 139 ? -19.349 3.722   3.544   1.00 23.37  ? 154 TYR A CE2 1 
ATOM   1127 C CZ  . TYR A 1 139 ? -19.007 5.017   3.860   1.00 24.56  ? 154 TYR A CZ  1 
ATOM   1128 O OH  . TYR A 1 139 ? -17.857 5.281   4.545   1.00 28.91  ? 154 TYR A OH  1 
ATOM   1129 N N   . GLY A 1 140 ? -21.762 2.372   -0.807  1.00 19.47  ? 155 GLY A N   1 
ATOM   1130 C CA  . GLY A 1 140 ? -20.814 1.426   -1.385  1.00 19.55  ? 155 GLY A CA  1 
ATOM   1131 C C   . GLY A 1 140 ? -20.353 1.807   -2.776  1.00 19.73  ? 155 GLY A C   1 
ATOM   1132 O O   . GLY A 1 140 ? -19.225 1.481   -3.148  1.00 20.89  ? 155 GLY A O   1 
ATOM   1133 N N   . CYS A 1 141 ? -21.239 2.472   -3.535  1.00 19.40  ? 156 CYS A N   1 
ATOM   1134 C CA  . CYS A 1 141 ? -20.915 2.991   -4.846  1.00 19.12  ? 156 CYS A CA  1 
ATOM   1135 C C   . CYS A 1 141 ? -20.219 4.348   -4.743  1.00 20.34  ? 156 CYS A C   1 
ATOM   1136 O O   . CYS A 1 141 ? -19.086 4.496   -5.242  1.00 23.57  ? 156 CYS A O   1 
ATOM   1137 C CB  . CYS A 1 141 ? -22.154 3.069   -5.730  1.00 22.17  ? 156 CYS A CB  1 
ATOM   1138 S SG  . CYS A 1 141 ? -21.835 3.860   -7.326  1.00 25.26  ? 156 CYS A SG  1 
ATOM   1139 N N   . ASN A 1 142 ? -20.877 5.351   -4.153  1.00 21.40  ? 157 ASN A N   1 
ATOM   1140 C CA  . ASN A 1 142 ? -20.411 6.735   -4.303  1.00 22.28  ? 157 ASN A CA  1 
ATOM   1141 C C   . ASN A 1 142 ? -19.210 7.035   -3.420  1.00 23.19  ? 157 ASN A C   1 
ATOM   1142 O O   . ASN A 1 142 ? -18.335 7.855   -3.804  1.00 26.73  ? 157 ASN A O   1 
ATOM   1143 C CB  . ASN A 1 142 ? -21.566 7.692   -4.054  1.00 22.75  ? 157 ASN A CB  1 
ATOM   1144 C CG  . ASN A 1 142 ? -22.683 7.532   -5.059  1.00 27.40  ? 157 ASN A CG  1 
ATOM   1145 O OD1 . ASN A 1 142 ? -22.444 7.326   -6.243  1.00 30.12  ? 157 ASN A OD1 1 
ATOM   1146 N ND2 . ASN A 1 142 ? -23.913 7.698   -4.627  1.00 28.80  ? 157 ASN A ND2 1 
ATOM   1147 N N   . GLU A 1 143 ? -19.163 6.398   -2.245  1.00 21.75  ? 158 GLU A N   1 
ATOM   1148 C CA  . GLU A 1 143 ? -18.029 6.598   -1.357  1.00 22.78  ? 158 GLU A CA  1 
ATOM   1149 C C   . GLU A 1 143 ? -16.947 5.549   -1.547  1.00 22.90  ? 158 GLU A C   1 
ATOM   1150 O O   . GLU A 1 143 ? -15.767 5.885   -1.559  1.00 26.48  ? 158 GLU A O   1 
ATOM   1151 C CB  . GLU A 1 143 ? -18.451 6.655   0.115   1.00 24.14  ? 158 GLU A CB  1 
ATOM   1152 C CG  . GLU A 1 143 ? -17.320 7.036   1.039   1.00 29.82  ? 158 GLU A CG  1 
ATOM   1153 C CD  . GLU A 1 143 ? -16.943 8.513   1.001   1.00 35.15  ? 158 GLU A CD  1 
ATOM   1154 O OE1 . GLU A 1 143 ? -17.566 9.352   0.288   1.00 36.40  ? 158 GLU A OE1 1 
ATOM   1155 O OE2 . GLU A 1 143 ? -15.978 8.815   1.730   1.00 43.08  ? 158 GLU A OE2 1 
ATOM   1156 N N   . LEU A 1 144 ? -17.335 4.266   -1.572  1.00 21.59  ? 159 LEU A N   1 
ATOM   1157 C CA  . LEU A 1 144 ? -16.350 3.201   -1.566  1.00 21.81  ? 159 LEU A CA  1 
ATOM   1158 C C   . LEU A 1 144 ? -15.922 2.811   -2.986  1.00 21.06  ? 159 LEU A C   1 
ATOM   1159 O O   . LEU A 1 144 ? -14.949 2.077   -3.133  1.00 23.91  ? 159 LEU A O   1 
ATOM   1160 C CB  . LEU A 1 144 ? -16.881 2.006   -0.789  1.00 21.68  ? 159 LEU A CB  1 
ATOM   1161 C CG  . LEU A 1 144 ? -17.374 2.298   0.620   1.00 22.04  ? 159 LEU A CG  1 
ATOM   1162 C CD1 . LEU A 1 144 ? -17.778 0.986   1.299   1.00 21.63  ? 159 LEU A CD1 1 
ATOM   1163 C CD2 . LEU A 1 144 ? -16.314 2.972   1.459   1.00 24.03  ? 159 LEU A CD2 1 
ATOM   1164 N N   . LYS A 1 145 ? -16.669 3.217   -4.017  1.00 21.60  ? 160 LYS A N   1 
ATOM   1165 C CA  . LYS A 1 145 ? -16.291 2.998   -5.397  1.00 21.29  ? 160 LYS A CA  1 
ATOM   1166 C C   . LYS A 1 145 ? -16.231 1.502   -5.724  1.00 21.38  ? 160 LYS A C   1 
ATOM   1167 O O   . LYS A 1 145 ? -15.382 1.046   -6.491  1.00 23.89  ? 160 LYS A O   1 
ATOM   1168 C CB  . LYS A 1 145 ? -14.952 3.660   -5.701  1.00 23.86  ? 160 LYS A CB  1 
ATOM   1169 C CG  . LYS A 1 145 ? -14.821 5.069   -5.238  1.00 27.92  ? 160 LYS A CG  1 
ATOM   1170 C CD  . LYS A 1 145 ? -15.786 6.034   -5.842  1.00 31.40  ? 160 LYS A CD  1 
ATOM   1171 C CE  . LYS A 1 145 ? -15.431 7.429   -5.407  1.00 37.14  ? 160 LYS A CE  1 
ATOM   1172 N NZ  . LYS A 1 145 ? -16.376 8.345   -6.036  1.00 43.28  ? 160 LYS A NZ  1 
ATOM   1173 N N   . SER A 1 146 ? -17.184 0.717   -5.209  1.00 19.38  ? 161 SER A N   1 
ATOM   1174 C CA  . SER A 1 146 ? -17.347 -0.666  -5.652  1.00 18.97  ? 161 SER A CA  1 
ATOM   1175 C C   . SER A 1 146 ? -18.202 -0.735  -6.905  1.00 19.38  ? 161 SER A C   1 
ATOM   1176 O O   . SER A 1 146 ? -19.389 -0.456  -6.865  1.00 21.08  ? 161 SER A O   1 
ATOM   1177 C CB  . SER A 1 146 ? -17.972 -1.525  -4.613  1.00 21.16  ? 161 SER A CB  1 
ATOM   1178 O OG  . SER A 1 146 ? -18.252 -2.813  -5.187  1.00 22.16  ? 161 SER A OG  1 
ATOM   1179 N N   . ALA A 1 147 ? -17.622 -1.139  -8.038  1.00 21.01  ? 162 ALA A N   1 
ATOM   1180 C CA  . ALA A 1 147 ? -18.379 -1.247  -9.268  1.00 21.54  ? 162 ALA A CA  1 
ATOM   1181 C C   . ALA A 1 147 ? -19.540 -2.232  -9.129  1.00 18.65  ? 162 ALA A C   1 
ATOM   1182 O O   . ALA A 1 147 ? -20.573 -1.977  -9.737  1.00 20.35  ? 162 ALA A O   1 
ATOM   1183 C CB  . ALA A 1 147 ? -17.498 -1.666  -10.408 1.00 24.75  ? 162 ALA A CB  1 
ATOM   1184 N N   . TYR A 1 148 ? -19.414 -3.306  -8.339  1.00 20.00  ? 163 TYR A N   1 
ATOM   1185 C CA  . TYR A 1 148 ? -20.542 -4.220  -8.175  1.00 19.44  ? 163 TYR A CA  1 
ATOM   1186 C C   . TYR A 1 148 ? -21.699 -3.580  -7.404  1.00 18.20  ? 163 TYR A C   1 
ATOM   1187 O O   . TYR A 1 148 ? -22.857 -3.821  -7.726  1.00 19.33  ? 163 TYR A O   1 
ATOM   1188 C CB  . TYR A 1 148 ? -20.114 -5.528  -7.519  1.00 21.08  ? 163 TYR A CB  1 
ATOM   1189 C CG  . TYR A 1 148 ? -19.293 -6.407  -8.432  1.00 20.93  ? 163 TYR A CG  1 
ATOM   1190 C CD1 . TYR A 1 148 ? -19.747 -6.796  -9.666  1.00 21.52  ? 163 TYR A CD1 1 
ATOM   1191 C CD2 . TYR A 1 148 ? -18.076 -6.860  -8.000  1.00 21.00  ? 163 TYR A CD2 1 
ATOM   1192 C CE1 . TYR A 1 148 ? -18.985 -7.621  -10.473 1.00 22.68  ? 163 TYR A CE1 1 
ATOM   1193 C CE2 . TYR A 1 148 ? -17.280 -7.656  -8.804  1.00 22.95  ? 163 TYR A CE2 1 
ATOM   1194 C CZ  . TYR A 1 148 ? -17.754 -8.056  -10.028 1.00 22.94  ? 163 TYR A CZ  1 
ATOM   1195 O OH  . TYR A 1 148 ? -17.021 -8.876  -10.809 1.00 27.11  ? 163 TYR A OH  1 
ATOM   1196 N N   . ILE A 1 149 ? -21.412 -2.665  -6.489  1.00 19.21  ? 164 ILE A N   1 
ATOM   1197 C CA  . ILE A 1 149 ? -22.475 -1.957  -5.788  1.00 18.60  ? 164 ILE A CA  1 
ATOM   1198 C C   . ILE A 1 149 ? -23.101 -0.912  -6.722  1.00 17.22  ? 164 ILE A C   1 
ATOM   1199 O O   . ILE A 1 149 ? -24.330 -0.730  -6.746  1.00 19.73  ? 164 ILE A O   1 
ATOM   1200 C CB  . ILE A 1 149 ? -22.012 -1.380  -4.444  1.00 19.63  ? 164 ILE A CB  1 
ATOM   1201 C CG1 . ILE A 1 149 ? -21.416 -2.444  -3.510  1.00 19.99  ? 164 ILE A CG1 1 
ATOM   1202 C CG2 . ILE A 1 149 ? -23.175 -0.659  -3.775  1.00 19.61  ? 164 ILE A CG2 1 
ATOM   1203 C CD1 . ILE A 1 149 ? -22.353 -3.582  -3.134  1.00 21.18  ? 164 ILE A CD1 1 
ATOM   1204 N N   . CYS A 1 150 ? -22.284 -0.182  -7.480  1.00 19.77  ? 165 CYS A N   1 
ATOM   1205 C CA  . CYS A 1 150 ? -22.790 0.687   -8.533  1.00 20.77  ? 165 CYS A CA  1 
ATOM   1206 C C   . CYS A 1 150 ? -23.728 -0.051  -9.466  1.00 20.30  ? 165 CYS A C   1 
ATOM   1207 O O   . CYS A 1 150 ? -24.760 0.497   -9.886  1.00 20.83  ? 165 CYS A O   1 
ATOM   1208 C CB  . CYS A 1 150 ? -21.655 1.326   -9.332  1.00 22.56  ? 165 CYS A CB  1 
ATOM   1209 S SG  . CYS A 1 150 ? -20.525 2.339   -8.333  1.00 25.89  ? 165 CYS A SG  1 
ATOM   1210 N N   . ARG A 1 151 ? -23.368 -1.299  -9.817  1.00 19.81  ? 166 ARG A N   1 
ATOM   1211 C CA  . ARG A 1 151 ? -24.179 -2.105  -10.724 1.00 19.32  ? 166 ARG A CA  1 
ATOM   1212 C C   . ARG A 1 151 ? -25.548 -2.403  -10.116 1.00 18.28  ? 166 ARG A C   1 
ATOM   1213 O O   . ARG A 1 151 ? -26.544 -2.449  -10.834 1.00 19.65  ? 166 ARG A O   1 
ATOM   1214 C CB  . ARG A 1 151 ? -23.424 -3.404  -11.061 1.00 18.80  ? 166 ARG A CB  1 
ATOM   1215 C CG  . ARG A 1 151 ? -24.074 -4.150  -12.212 1.00 19.98  ? 166 ARG A CG  1 
ATOM   1216 C CD  . ARG A 1 151 ? -23.476 -5.521  -12.376 1.00 21.58  ? 166 ARG A CD  1 
ATOM   1217 N NE  . ARG A 1 151 ? -23.708 -6.357  -11.186 1.00 21.53  ? 166 ARG A NE  1 
ATOM   1218 C CZ  . ARG A 1 151 ? -23.164 -7.565  -10.963 1.00 20.91  ? 166 ARG A CZ  1 
ATOM   1219 N NH1 . ARG A 1 151 ? -22.380 -8.134  -11.875 1.00 21.72  ? 166 ARG A NH1 1 
ATOM   1220 N NH2 . ARG A 1 151 ? -23.410 -8.143  -9.823  1.00 21.05  ? 166 ARG A NH2 1 
ATOM   1221 N N   . ASP A 1 152 ? -25.625 -2.580  -8.801  1.00 18.87  ? 167 ASP A N   1 
ATOM   1222 C CA  . ASP A 1 152 ? -26.904 -2.781  -8.137  1.00 18.87  ? 167 ASP A CA  1 
ATOM   1223 C C   . ASP A 1 152 ? -27.843 -1.602  -8.376  1.00 18.87  ? 167 ASP A C   1 
ATOM   1224 O O   . ASP A 1 152 ? -29.030 -1.776  -8.663  1.00 19.16  ? 167 ASP A O   1 
ATOM   1225 C CB  . ASP A 1 152 ? -26.756 -3.075  -6.656  1.00 18.92  ? 167 ASP A CB  1 
ATOM   1226 C CG  . ASP A 1 152 ? -26.017 -4.355  -6.340  1.00 21.80  ? 167 ASP A CG  1 
ATOM   1227 O OD1 . ASP A 1 152 ? -26.254 -5.372  -7.078  1.00 23.69  ? 167 ASP A OD1 1 
ATOM   1228 O OD2 . ASP A 1 152 ? -25.302 -4.370  -5.295  1.00 21.78  ? 167 ASP A OD2 1 
ATOM   1229 N N   . LEU A 1 153 ? -27.322 -0.378  -8.275  1.00 19.01  ? 168 LEU A N   1 
ATOM   1230 C CA  . LEU A 1 153 ? -28.134 0.813   -8.516  1.00 18.70  ? 168 LEU A CA  1 
ATOM   1231 C C   . LEU A 1 153 ? -28.410 0.975   -9.997  1.00 18.15  ? 168 LEU A C   1 
ATOM   1232 O O   . LEU A 1 153 ? -29.527 1.315   -10.386 1.00 20.22  ? 168 LEU A O   1 
ATOM   1233 C CB  . LEU A 1 153 ? -27.414 2.029   -7.913  1.00 21.14  ? 168 LEU A CB  1 
ATOM   1234 C CG  . LEU A 1 153 ? -27.418 2.059   -6.390  1.00 21.12  ? 168 LEU A CG  1 
ATOM   1235 C CD1 . LEU A 1 153 ? -26.433 3.103   -5.872  1.00 22.92  ? 168 LEU A CD1 1 
ATOM   1236 C CD2 . LEU A 1 153 ? -28.797 2.328   -5.836  1.00 22.73  ? 168 LEU A CD2 1 
ATOM   1237 N N   . ARG A 1 154 ? -27.412 0.699   -10.857 1.00 19.40  ? 169 ARG A N   1 
ATOM   1238 C CA  . ARG A 1 154 ? -27.645 0.714   -12.292 1.00 20.12  ? 169 ARG A CA  1 
ATOM   1239 C C   . ARG A 1 154 ? -28.825 -0.179  -12.658 1.00 20.38  ? 169 ARG A C   1 
ATOM   1240 O O   . ARG A 1 154 ? -29.708 0.266   -13.404 1.00 21.07  ? 169 ARG A O   1 
ATOM   1241 C CB  . ARG A 1 154 ? -26.347 0.303   -12.990 1.00 21.33  ? 169 ARG A CB  1 
ATOM   1242 C CG  . ARG A 1 154 ? -26.303 0.465   -14.494 1.00 21.99  ? 169 ARG A CG  1 
ATOM   1243 C CD  . ARG A 1 154 ? -27.061 -0.577  -15.315 1.00 24.22  ? 169 ARG A CD  1 
ATOM   1244 N NE  . ARG A 1 154 ? -26.689 -1.962  -15.012 1.00 25.23  ? 169 ARG A NE  1 
ATOM   1245 C CZ  . ARG A 1 154 ? -25.738 -2.664  -15.620 1.00 25.55  ? 169 ARG A CZ  1 
ATOM   1246 N NH1 . ARG A 1 154 ? -24.904 -2.078  -16.455 1.00 26.63  ? 169 ARG A NH1 1 
ATOM   1247 N NH2 . ARG A 1 154 ? -25.576 -3.925  -15.311 1.00 24.23  ? 169 ARG A NH2 1 
ATOM   1248 N N   . ASP A 1 155 ? -28.815 -1.429  -12.171 1.00 19.62  ? 170 ASP A N   1 
ATOM   1249 C CA  . ASP A 1 155 ? -29.870 -2.377  -12.485 1.00 21.19  ? 170 ASP A CA  1 
ATOM   1250 C C   . ASP A 1 155 ? -31.217 -1.868  -11.959 1.00 18.74  ? 170 ASP A C   1 
ATOM   1251 O O   . ASP A 1 155 ? -32.219 -1.963  -12.641 1.00 21.41  ? 170 ASP A O   1 
ATOM   1252 C CB  . ASP A 1 155 ? -29.549 -3.740  -11.911 1.00 21.83  ? 170 ASP A CB  1 
ATOM   1253 C CG  . ASP A 1 155 ? -28.405 -4.518  -12.532 1.00 22.84  ? 170 ASP A CG  1 
ATOM   1254 O OD1 . ASP A 1 155 ? -28.003 -4.145  -13.636 1.00 23.51  ? 170 ASP A OD1 1 
ATOM   1255 O OD2 . ASP A 1 155 ? -27.952 -5.494  -11.884 1.00 25.02  ? 170 ASP A OD2 1 
ATOM   1256 N N   . MET A 1 156 ? -31.243 -1.373  -10.729 1.00 18.85  ? 171 MET A N   1 
ATOM   1257 C CA  . MET A 1 156 ? -32.461 -0.863  -10.130 1.00 18.69  ? 171 MET A CA  1 
ATOM   1258 C C   . MET A 1 156 ? -33.048 0.250   -11.009 1.00 19.76  ? 171 MET A C   1 
ATOM   1259 O O   . MET A 1 156 ? -34.225 0.198   -11.421 1.00 21.99  ? 171 MET A O   1 
ATOM   1260 C CB  . MET A 1 156 ? -32.195 -0.346  -8.713  1.00 20.32  ? 171 MET A CB  1 
ATOM   1261 C CG  . MET A 1 156 ? -33.439 0.033   -7.951  1.00 21.45  ? 171 MET A CG  1 
ATOM   1262 S SD  . MET A 1 156 ? -33.096 0.874   -6.406  1.00 22.65  ? 171 MET A SD  1 
ATOM   1263 C CE  . MET A 1 156 ? -32.547 2.504   -6.928  1.00 25.48  ? 171 MET A CE  1 
ATOM   1264 N N   . TYR A 1 157 ? -32.247 1.261   -11.332 1.00 20.91  ? 172 TYR A N   1 
ATOM   1265 C CA  . TYR A 1 157 ? -32.780 2.358   -12.129 1.00 21.49  ? 172 TYR A CA  1 
ATOM   1266 C C   . TYR A 1 157 ? -33.140 1.919   -13.541 1.00 22.58  ? 172 TYR A C   1 
ATOM   1267 O O   . TYR A 1 157 ? -34.084 2.436   -14.115 1.00 24.81  ? 172 TYR A O   1 
ATOM   1268 C CB  . TYR A 1 157 ? -31.764 3.512   -12.119 1.00 22.61  ? 172 TYR A CB  1 
ATOM   1269 C CG  . TYR A 1 157 ? -31.728 4.205   -10.771 1.00 21.86  ? 172 TYR A CG  1 
ATOM   1270 C CD1 . TYR A 1 157 ? -32.851 4.855   -10.287 1.00 23.94  ? 172 TYR A CD1 1 
ATOM   1271 C CD2 . TYR A 1 157 ? -30.577 4.260   -10.005 1.00 22.85  ? 172 TYR A CD2 1 
ATOM   1272 C CE1 . TYR A 1 157 ? -32.831 5.494   -9.069  1.00 25.77  ? 172 TYR A CE1 1 
ATOM   1273 C CE2 . TYR A 1 157 ? -30.525 4.923   -8.791  1.00 23.28  ? 172 TYR A CE2 1 
ATOM   1274 C CZ  . TYR A 1 157 ? -31.668 5.541   -8.322  1.00 24.52  ? 172 TYR A CZ  1 
ATOM   1275 O OH  . TYR A 1 157 ? -31.696 6.170   -7.111  1.00 29.70  ? 172 TYR A OH  1 
ATOM   1276 N N   . LYS A 1 158 ? -32.415 0.965   -14.126 1.00 21.25  ? 173 LYS A N   1 
ATOM   1277 C CA  . LYS A 1 158 ? -32.729 0.484   -15.466 1.00 22.90  ? 173 LYS A CA  1 
ATOM   1278 C C   . LYS A 1 158 ? -34.138 -0.107  -15.522 1.00 23.89  ? 173 LYS A C   1 
ATOM   1279 O O   . LYS A 1 158 ? -34.934 0.213   -16.427 1.00 26.94  ? 173 LYS A O   1 
ATOM   1280 C CB  . LYS A 1 158 ? -31.717 -0.582  -15.884 1.00 25.09  ? 173 LYS A CB  1 
ATOM   1281 C CG  . LYS A 1 158 ? -32.031 -1.282  -17.192 1.00 29.18  ? 173 LYS A CG  1 
ATOM   1282 C CD  . LYS A 1 158 ? -30.896 -2.234  -17.562 1.00 34.14  ? 173 LYS A CD  1 
ATOM   1283 C CE  . LYS A 1 158 ? -31.209 -3.260  -18.596 1.00 43.78  ? 173 LYS A CE  1 
ATOM   1284 N NZ  . LYS A 1 158 ? -30.303 -4.406  -18.442 1.00 49.26  ? 173 LYS A NZ  1 
ATOM   1285 N N   . TYR A 1 159 ? -34.458 -0.954  -14.538 1.00 23.60  ? 174 TYR A N   1 
ATOM   1286 C CA  . TYR A 1 159 ? -35.749 -1.610  -14.540 1.00 24.32  ? 174 TYR A CA  1 
ATOM   1287 C C   . TYR A 1 159 ? -36.864 -0.775  -13.916 1.00 24.95  ? 174 TYR A C   1 
ATOM   1288 O O   . TYR A 1 159 ? -38.025 -1.151  -14.102 1.00 31.54  ? 174 TYR A O   1 
ATOM   1289 C CB  . TYR A 1 159 ? -35.655 -3.005  -13.915 1.00 24.72  ? 174 TYR A CB  1 
ATOM   1290 C CG  . TYR A 1 159 ? -34.771 -3.907  -14.753 1.00 25.82  ? 174 TYR A CG  1 
ATOM   1291 C CD1 . TYR A 1 159 ? -35.215 -4.359  -15.979 1.00 29.05  ? 174 TYR A CD1 1 
ATOM   1292 C CD2 . TYR A 1 159 ? -33.530 -4.337  -14.314 1.00 28.61  ? 174 TYR A CD2 1 
ATOM   1293 C CE1 . TYR A 1 159 ? -34.418 -5.135  -16.791 1.00 30.52  ? 174 TYR A CE1 1 
ATOM   1294 C CE2 . TYR A 1 159 ? -32.742 -5.171  -15.092 1.00 31.63  ? 174 TYR A CE2 1 
ATOM   1295 C CZ  . TYR A 1 159 ? -33.182 -5.557  -16.341 1.00 34.48  ? 174 TYR A CZ  1 
ATOM   1296 O OH  . TYR A 1 159 ? -32.429 -6.378  -17.140 1.00 42.14  ? 174 TYR A OH  1 
ATOM   1297 N N   . LEU A 1 160 ? -36.535 0.336   -13.253 1.00 24.67  ? 175 LEU A N   1 
ATOM   1298 C CA  . LEU A 1 160 ? -37.509 1.394   -12.935 1.00 27.34  ? 175 LEU A CA  1 
ATOM   1299 C C   . LEU A 1 160 ? -37.805 2.281   -14.151 1.00 28.54  ? 175 LEU A C   1 
ATOM   1300 O O   . LEU A 1 160 ? -38.767 3.061   -14.118 1.00 35.29  ? 175 LEU A O   1 
ATOM   1301 C CB  . LEU A 1 160 ? -37.081 2.277   -11.763 1.00 27.94  ? 175 LEU A CB  1 
ATOM   1302 C CG  . LEU A 1 160 ? -36.954 1.616   -10.387 1.00 28.44  ? 175 LEU A CG  1 
ATOM   1303 C CD1 . LEU A 1 160 ? -36.335 2.580   -9.400  1.00 28.39  ? 175 LEU A CD1 1 
ATOM   1304 C CD2 . LEU A 1 160 ? -38.293 1.144   -9.807  1.00 30.51  ? 175 LEU A CD2 1 
ATOM   1305 N N   . GLY A 1 161 ? -36.927 2.263   -15.168 1.00 29.35  ? 176 GLY A N   1 
ATOM   1306 C CA  . GLY A 1 161 ? -37.105 3.079   -16.354 1.00 30.47  ? 176 GLY A CA  1 
ATOM   1307 C C   . GLY A 1 161 ? -36.534 4.493   -16.221 1.00 31.56  ? 176 GLY A C   1 
ATOM   1308 O O   . GLY A 1 161 ? -36.879 5.353   -17.021 1.00 35.92  ? 176 GLY A O   1 
ATOM   1309 N N   . ASP A 1 162 ? -35.641 4.726   -15.254 1.00 29.17  ? 177 ASP A N   1 
ATOM   1310 C CA  . ASP A 1 162 ? -35.036 6.031   -15.057 1.00 28.20  ? 177 ASP A CA  1 
ATOM   1311 C C   . ASP A 1 162 ? -33.723 6.136   -15.839 1.00 28.33  ? 177 ASP A C   1 
ATOM   1312 O O   . ASP A 1 162 ? -32.676 5.687   -15.380 1.00 27.96  ? 177 ASP A O   1 
ATOM   1313 C CB  . ASP A 1 162 ? -34.785 6.275   -13.587 1.00 28.18  ? 177 ASP A CB  1 
ATOM   1314 C CG  . ASP A 1 162 ? -34.341 7.693   -13.247 1.00 31.58  ? 177 ASP A CG  1 
ATOM   1315 O OD1 . ASP A 1 162 ? -33.642 8.347   -14.084 1.00 31.45  ? 177 ASP A OD1 1 
ATOM   1316 O OD2 . ASP A 1 162 ? -34.621 8.110   -12.115 1.00 34.78  ? 177 ASP A OD2 1 
ATOM   1317 N N   . LYS A 1 163 ? -33.784 6.695   -17.042 1.00 29.37  ? 178 LYS A N   1 
ATOM   1318 C CA  . LYS A 1 163 ? -32.674 6.610   -17.973 1.00 31.24  ? 178 LYS A CA  1 
ATOM   1319 C C   . LYS A 1 163 ? -31.478 7.443   -17.494 1.00 29.11  ? 178 LYS A C   1 
ATOM   1320 O O   . LYS A 1 163 ? -30.332 6.996   -17.620 1.00 30.37  ? 178 LYS A O   1 
ATOM   1321 C CB  . LYS A 1 163 ? -33.155 7.010   -19.365 1.00 35.51  ? 178 LYS A CB  1 
ATOM   1322 C CG  . LYS A 1 163 ? -34.168 6.077   -20.000 1.00 40.49  ? 178 LYS A CG  1 
ATOM   1323 C CD  . LYS A 1 163 ? -34.765 6.703   -21.251 1.00 47.18  ? 178 LYS A CD  1 
ATOM   1324 C CE  . LYS A 1 163 ? -35.914 5.925   -21.772 1.00 58.26  ? 178 LYS A CE  1 
ATOM   1325 N NZ  . LYS A 1 163 ? -35.475 4.551   -22.007 1.00 64.41  ? 178 LYS A NZ  1 
ATOM   1326 N N   . GLU A 1 164 ? -31.732 8.631   -16.927 1.00 30.02  ? 179 GLU A N   1 
ATOM   1327 C CA  . GLU A 1 164 ? -30.673 9.510   -16.452 1.00 29.49  ? 179 GLU A CA  1 
ATOM   1328 C C   . GLU A 1 164 ? -29.893 8.833   -15.314 1.00 28.27  ? 179 GLU A C   1 
ATOM   1329 O O   . GLU A 1 164 ? -28.662 8.826   -15.281 1.00 26.58  ? 179 GLU A O   1 
ATOM   1330 C CB  . GLU A 1 164 ? -31.267 10.832  -15.963 1.00 35.06  ? 179 GLU A CB  1 
ATOM   1331 C CG  . GLU A 1 164 ? -30.215 11.928  -15.796 1.00 42.57  ? 179 GLU A CG  1 
ATOM   1332 C CD  . GLU A 1 164 ? -30.668 13.344  -15.381 1.00 47.61  ? 179 GLU A CD  1 
ATOM   1333 O OE1 . GLU A 1 164 ? -31.761 13.528  -14.789 1.00 56.47  ? 179 GLU A OE1 1 
ATOM   1334 O OE2 . GLU A 1 164 ? -29.924 14.304  -15.691 1.00 55.03  ? 179 GLU A OE2 1 
ATOM   1335 N N   . LYS A 1 165 ? -30.608 8.262   -14.349 1.00 26.23  ? 180 LYS A N   1 
ATOM   1336 C CA  . LYS A 1 165 ? -29.947 7.619   -13.227 1.00 25.90  ? 180 LYS A CA  1 
ATOM   1337 C C   . LYS A 1 165 ? -29.268 6.322   -13.675 1.00 23.82  ? 180 LYS A C   1 
ATOM   1338 O O   . LYS A 1 165 ? -28.224 5.967   -13.142 1.00 24.98  ? 180 LYS A O   1 
ATOM   1339 C CB  . LYS A 1 165 ? -30.884 7.392   -12.043 1.00 25.16  ? 180 LYS A CB  1 
ATOM   1340 C CG  . LYS A 1 165 ? -31.455 8.644   -11.415 1.00 30.78  ? 180 LYS A CG  1 
ATOM   1341 C CD  . LYS A 1 165 ? -30.466 9.486   -10.662 1.00 39.75  ? 180 LYS A CD  1 
ATOM   1342 C CE  . LYS A 1 165 ? -30.035 8.836   -9.418  1.00 37.97  ? 180 LYS A CE  1 
ATOM   1343 N NZ  . LYS A 1 165 ? -29.256 9.864   -8.704  1.00 42.82  ? 180 LYS A NZ  1 
ATOM   1344 N N   . THR A 1 166 ? -29.820 5.613   -14.655 1.00 24.38  ? 181 THR A N   1 
ATOM   1345 C CA  . THR A 1 166 ? -29.169 4.425   -15.173 1.00 24.45  ? 181 THR A CA  1 
ATOM   1346 C C   . THR A 1 166 ? -27.821 4.820   -15.782 1.00 25.72  ? 181 THR A C   1 
ATOM   1347 O O   . THR A 1 166 ? -26.808 4.151   -15.567 1.00 24.91  ? 181 THR A O   1 
ATOM   1348 C CB  . THR A 1 166 ? -30.024 3.726   -16.232 1.00 24.90  ? 181 THR A CB  1 
ATOM   1349 O OG1 . THR A 1 166 ? -31.279 3.374   -15.671 1.00 25.57  ? 181 THR A OG1 1 
ATOM   1350 C CG2 . THR A 1 166 ? -29.366 2.441   -16.702 1.00 25.66  ? 181 THR A CG2 1 
ATOM   1351 N N   . LYS A 1 167 ? -27.793 5.916   -16.527 1.00 24.68  ? 182 LYS A N   1 
ATOM   1352 C CA  . LYS A 1 167 ? -26.556 6.384   -17.133 1.00 25.65  ? 182 LYS A CA  1 
ATOM   1353 C C   . LYS A 1 167 ? -25.550 6.758   -16.044 1.00 26.52  ? 182 LYS A C   1 
ATOM   1354 O O   . LYS A 1 167 ? -24.361 6.448   -16.145 1.00 25.65  ? 182 LYS A O   1 
ATOM   1355 C CB  . LYS A 1 167 ? -26.811 7.560   -18.083 1.00 28.33  ? 182 LYS A CB  1 
ATOM   1356 C CG  . LYS A 1 167 ? -25.450 8.109   -18.609 1.00 33.82  ? 182 LYS A CG  1 
ATOM   1357 C CD  . LYS A 1 167 ? -25.428 9.119   -19.734 1.00 45.35  ? 182 LYS A CD  1 
ATOM   1358 C CE  . LYS A 1 167 ? -24.001 9.499   -20.104 1.00 48.52  ? 182 LYS A CE  1 
ATOM   1359 N NZ  . LYS A 1 167 ? -23.091 8.357   -20.273 1.00 51.21  ? 182 LYS A NZ  1 
ATOM   1360 N N   . GLU A 1 168 ? -26.015 7.491   -15.037 1.00 24.75  ? 183 GLU A N   1 
ATOM   1361 C CA  . GLU A 1 168 ? -25.161 7.888   -13.931 1.00 24.35  ? 183 GLU A CA  1 
ATOM   1362 C C   . GLU A 1 168 ? -24.429 6.689   -13.340 1.00 24.79  ? 183 GLU A C   1 
ATOM   1363 O O   . GLU A 1 168 ? -23.215 6.754   -13.091 1.00 24.81  ? 183 GLU A O   1 
ATOM   1364 C CB  . GLU A 1 168 ? -26.009 8.585   -12.871 1.00 24.99  ? 183 GLU A CB  1 
ATOM   1365 C CG  . GLU A 1 168 ? -25.224 9.004   -11.643 1.00 27.70  ? 183 GLU A CG  1 
ATOM   1366 C CD  . GLU A 1 168 ? -26.069 9.572   -10.518 1.00 30.17  ? 183 GLU A CD  1 
ATOM   1367 O OE1 . GLU A 1 168 ? -27.228 9.948   -10.825 1.00 35.02  ? 183 GLU A OE1 1 
ATOM   1368 O OE2 . GLU A 1 168 ? -25.574 9.652   -9.369  1.00 31.19  ? 183 GLU A OE2 1 
ATOM   1369 N N   . TYR A 1 169 ? -25.172 5.624   -13.025 1.00 22.67  ? 184 TYR A N   1 
ATOM   1370 C CA  . TYR A 1 169 ? -24.565 4.501   -12.325 1.00 23.07  ? 184 TYR A CA  1 
ATOM   1371 C C   . TYR A 1 169 ? -23.769 3.616   -13.295 1.00 24.31  ? 184 TYR A C   1 
ATOM   1372 O O   . TYR A 1 169 ? -22.809 2.992   -12.890 1.00 24.83  ? 184 TYR A O   1 
ATOM   1373 C CB  . TYR A 1 169 ? -25.583 3.778   -11.433 1.00 22.89  ? 184 TYR A CB  1 
ATOM   1374 C CG  . TYR A 1 169 ? -25.822 4.623   -10.202 1.00 22.18  ? 184 TYR A CG  1 
ATOM   1375 C CD1 . TYR A 1 169 ? -24.851 4.675   -9.219  1.00 22.86  ? 184 TYR A CD1 1 
ATOM   1376 C CD2 . TYR A 1 169 ? -26.912 5.479   -10.087 1.00 23.91  ? 184 TYR A CD2 1 
ATOM   1377 C CE1 . TYR A 1 169 ? -24.989 5.473   -8.097  1.00 25.01  ? 184 TYR A CE1 1 
ATOM   1378 C CE2 . TYR A 1 169 ? -27.031 6.305   -8.982  1.00 24.92  ? 184 TYR A CE2 1 
ATOM   1379 C CZ  . TYR A 1 169 ? -26.056 6.323   -8.002  1.00 25.39  ? 184 TYR A CZ  1 
ATOM   1380 O OH  . TYR A 1 169 ? -26.055 7.136   -6.890  1.00 28.11  ? 184 TYR A OH  1 
ATOM   1381 N N   . ASN A 1 170 ? -24.171 3.550   -14.548 1.00 23.97  ? 185 ASN A N   1 
ATOM   1382 C CA  . ASN A 1 170 ? -23.338 2.915   -15.561 1.00 26.48  ? 185 ASN A CA  1 
ATOM   1383 C C   . ASN A 1 170 ? -21.967 3.569   -15.644 1.00 27.22  ? 185 ASN A C   1 
ATOM   1384 O O   . ASN A 1 170 ? -20.960 2.885   -15.790 1.00 29.80  ? 185 ASN A O   1 
ATOM   1385 C CB  . ASN A 1 170 ? -23.954 3.003   -16.937 1.00 30.30  ? 185 ASN A CB  1 
ATOM   1386 C CG  . ASN A 1 170 ? -23.666 1.749   -17.695 1.00 38.38  ? 185 ASN A CG  1 
ATOM   1387 O OD1 . ASN A 1 170 ? -22.935 1.780   -18.699 1.00 53.40  ? 185 ASN A OD1 1 
ATOM   1388 N ND2 . ASN A 1 170 ? -24.208 0.669   -17.176 1.00 28.52  ? 185 ASN A ND2 1 
ATOM   1389 N N   . ASP A 1 171 ? -21.937 4.904   -15.652 1.00 26.48  ? 186 ASP A N   1 
ATOM   1390 C CA  . ASP A 1 171 ? -20.659 5.596   -15.720 1.00 28.17  ? 186 ASP A CA  1 
ATOM   1391 C C   . ASP A 1 171 ? -19.834 5.325   -14.456 1.00 28.74  ? 186 ASP A C   1 
ATOM   1392 O O   . ASP A 1 171 ? -18.627 5.166   -14.525 1.00 31.44  ? 186 ASP A O   1 
ATOM   1393 C CB  . ASP A 1 171 ? -20.890 7.077   -15.949 1.00 28.51  ? 186 ASP A CB  1 
ATOM   1394 C CG  . ASP A 1 171 ? -21.337 7.459   -17.355 1.00 33.70  ? 186 ASP A CG  1 
ATOM   1395 O OD1 . ASP A 1 171 ? -21.223 6.626   -18.261 1.00 37.25  ? 186 ASP A OD1 1 
ATOM   1396 O OD2 . ASP A 1 171 ? -21.819 8.591   -17.533 1.00 43.23  ? 186 ASP A OD2 1 
ATOM   1397 N N   . LYS A 1 172 ? -20.474 5.304   -13.283 1.00 26.68  ? 187 LYS A N   1 
ATOM   1398 C CA  . LYS A 1 172 ? -19.774 5.052   -12.022 1.00 27.06  ? 187 LYS A CA  1 
ATOM   1399 C C   . LYS A 1 172 ? -19.179 3.647   -11.961 1.00 26.92  ? 187 LYS A C   1 
ATOM   1400 O O   . LYS A 1 172 ? -18.106 3.428   -11.387 1.00 28.75  ? 187 LYS A O   1 
ATOM   1401 C CB  . LYS A 1 172 ? -20.687 5.381   -10.843 1.00 25.79  ? 187 LYS A CB  1 
ATOM   1402 C CG  . LYS A 1 172 ? -20.905 6.867   -10.633 1.00 27.70  ? 187 LYS A CG  1 
ATOM   1403 C CD  . LYS A 1 172 ? -22.009 7.144   -9.607  1.00 26.81  ? 187 LYS A CD  1 
ATOM   1404 C CE  . LYS A 1 172 ? -22.098 8.634   -9.321  1.00 29.23  ? 187 LYS A CE  1 
ATOM   1405 N NZ  . LYS A 1 172 ? -23.157 8.959   -8.350  1.00 30.07  ? 187 LYS A NZ  1 
ATOM   1406 N N   . MET A 1 173 ? -19.867 2.694   -12.575 1.00 27.09  ? 188 MET A N   1 
ATOM   1407 C CA  . MET A 1 173 ? -19.341 1.351   -12.718 1.00 28.70  ? 188 MET A CA  1 
ATOM   1408 C C   . MET A 1 173 ? -17.984 1.298   -13.403 1.00 32.56  ? 188 MET A C   1 
ATOM   1409 O O   . MET A 1 173 ? -17.176 0.411   -13.105 1.00 33.52  ? 188 MET A O   1 
ATOM   1410 C CB  . MET A 1 173 ? -20.284 0.518   -13.581 1.00 30.55  ? 188 MET A CB  1 
ATOM   1411 C CG  . MET A 1 173 ? -21.438 0.045   -12.806 1.00 29.43  ? 188 MET A CG  1 
ATOM   1412 S SD  . MET A 1 173 ? -22.614 -0.835  -13.855 1.00 32.16  ? 188 MET A SD  1 
ATOM   1413 C CE  . MET A 1 173 ? -21.576 -2.243  -14.141 1.00 25.70  ? 188 MET A CE  1 
ATOM   1414 N N   . LYS A 1 174 ? -17.745 2.218   -14.341 1.00 35.59  ? 189 LYS A N   1 
ATOM   1415 C CA  . LYS A 1 174 ? -16.516 2.191   -15.125 1.00 40.22  ? 189 LYS A CA  1 
ATOM   1416 C C   . LYS A 1 174 ? -15.329 2.751   -14.329 1.00 41.37  ? 189 LYS A C   1 
ATOM   1417 O O   . LYS A 1 174 ? -14.190 2.632   -14.789 1.00 46.07  ? 189 LYS A O   1 
ATOM   1418 C CB  . LYS A 1 174 ? -16.769 2.859   -16.486 1.00 45.72  ? 189 LYS A CB  1 
ATOM   1419 C CG  . LYS A 1 174 ? -17.677 1.987   -17.375 1.00 51.45  ? 189 LYS A CG  1 
ATOM   1420 C CD  . LYS A 1 174 ? -18.226 2.577   -18.673 1.00 56.60  ? 189 LYS A CD  1 
ATOM   1421 C CE  . LYS A 1 174 ? -18.872 1.508   -19.512 1.00 64.03  ? 189 LYS A CE  1 
ATOM   1422 N NZ  . LYS A 1 174 ? -19.878 2.016   -20.448 1.00 73.03  ? 189 LYS A NZ  1 
ATOM   1423 N N   . ASN A 1 175 ? -15.608 3.379   -13.171 1.00 37.72  ? 190 ASN A N   1 
ATOM   1424 C CA  . ASN A 1 175 ? -14.599 4.065   -12.370 1.00 41.72  ? 190 ASN A CA  1 
ATOM   1425 C C   . ASN A 1 175 ? -14.435 3.436   -10.980 1.00 35.80  ? 190 ASN A C   1 
ATOM   1426 O O   . ASN A 1 175 ? -14.135 4.112   -9.998  1.00 40.33  ? 190 ASN A O   1 
ATOM   1427 C CB  . ASN A 1 175 ? -14.946 5.539   -12.208 1.00 45.93  ? 190 ASN A CB  1 
ATOM   1428 C CG  . ASN A 1 175 ? -14.833 6.313   -13.500 1.00 54.15  ? 190 ASN A CG  1 
ATOM   1429 O OD1 . ASN A 1 175 ? -15.611 7.246   -13.740 1.00 68.12  ? 190 ASN A OD1 1 
ATOM   1430 N ND2 . ASN A 1 175 ? -13.834 5.988   -14.308 1.00 60.59  ? 190 ASN A ND2 1 
ATOM   1431 N N   . GLY A 1 176 ? -14.624 2.122   -10.877 1.00 33.29  ? 191 GLY A N   1 
ATOM   1432 C CA  . GLY A 1 176 ? -14.525 1.452   -9.596  1.00 29.61  ? 191 GLY A CA  1 
ATOM   1433 C C   . GLY A 1 176 ? -13.080 1.268   -9.154  1.00 28.61  ? 191 GLY A C   1 
ATOM   1434 O O   . GLY A 1 176 ? -12.150 1.302   -9.977  1.00 35.01  ? 191 GLY A O   1 
ATOM   1435 N N   . ASP A 1 177 ? -12.940 1.072   -7.832  1.00 25.90  ? 192 ASP A N   1 
ATOM   1436 C CA  . ASP A 1 177 ? -11.687 0.733   -7.184  1.00 27.47  ? 192 ASP A CA  1 
ATOM   1437 C C   . ASP A 1 177 ? -11.386 -0.735  -7.444  1.00 26.41  ? 192 ASP A C   1 
ATOM   1438 O O   . ASP A 1 177 ? -12.233 -1.590  -7.209  1.00 26.26  ? 192 ASP A O   1 
ATOM   1439 C CB  . ASP A 1 177 ? -11.783 1.014   -5.687  1.00 31.94  ? 192 ASP A CB  1 
ATOM   1440 C CG  . ASP A 1 177 ? -10.527 0.848   -4.839  1.00 37.11  ? 192 ASP A CG  1 
ATOM   1441 O OD1 . ASP A 1 177 ? -9.593  0.137   -5.285  1.00 37.88  ? 192 ASP A OD1 1 
ATOM   1442 O OD2 . ASP A 1 177 ? -10.479 1.450   -3.720  1.00 46.12  ? 192 ASP A OD2 1 
ATOM   1443 N N   . GLU A 1 178 ? -10.168 -1.025  -7.925  1.00 29.19  ? 193 GLU A N   1 
ATOM   1444 C CA  . GLU A 1 178 ? -9.747  -2.367  -8.282  1.00 29.94  ? 193 GLU A CA  1 
ATOM   1445 C C   . GLU A 1 178 ? -9.827  -3.320  -7.090  1.00 29.11  ? 193 GLU A C   1 
ATOM   1446 O O   . GLU A 1 178 ? -9.996  -4.517  -7.296  1.00 30.00  ? 193 GLU A O   1 
ATOM   1447 C CB  . GLU A 1 178 ? -8.325  -2.273  -8.842  1.00 35.05  ? 193 GLU A CB  1 
ATOM   1448 C CG  . GLU A 1 178 ? -7.789  -3.570  -9.444  1.00 42.11  ? 193 GLU A CG  1 
ATOM   1449 C CD  . GLU A 1 178 ? -8.587  -4.265  -10.553 1.00 45.53  ? 193 GLU A CD  1 
ATOM   1450 O OE1 . GLU A 1 178 ? -9.445  -3.647  -11.245 1.00 51.10  ? 193 GLU A OE1 1 
ATOM   1451 O OE2 . GLU A 1 178 ? -8.306  -5.483  -10.718 1.00 57.29  ? 193 GLU A OE2 1 
ATOM   1452 N N   . LYS A 1 179 ? -9.792  -2.804  -5.842  1.00 29.26  ? 194 LYS A N   1 
ATOM   1453 C CA  . LYS A 1 179 ? -9.810  -3.669  -4.670  1.00 28.73  ? 194 LYS A CA  1 
ATOM   1454 C C   . LYS A 1 179 ? -11.116 -4.463  -4.613  1.00 28.56  ? 194 LYS A C   1 
ATOM   1455 O O   . LYS A 1 179 ? -11.164 -5.529  -3.989  1.00 30.31  ? 194 LYS A O   1 
ATOM   1456 C CB  . LYS A 1 179 ? -9.549  -2.973  -3.331  1.00 34.93  ? 194 LYS A CB  1 
ATOM   1457 C CG  . LYS A 1 179 ? -10.644 -2.124  -2.760  1.00 40.20  ? 194 LYS A CG  1 
ATOM   1458 C CD  . LYS A 1 179 ? -10.309 -1.257  -1.537  1.00 45.59  ? 194 LYS A CD  1 
ATOM   1459 C CE  . LYS A 1 179 ? -10.140 -2.028  -0.252  1.00 50.92  ? 194 LYS A CE  1 
ATOM   1460 N NZ  . LYS A 1 179 ? -10.022 -1.176  0.942   1.00 56.07  ? 194 LYS A NZ  1 
ATOM   1461 N N   . TRP A 1 180 ? -12.178 -3.941  -5.265  1.00 25.48  ? 195 TRP A N   1 
ATOM   1462 C CA  . TRP A 1 180 ? -13.473 -4.606  -5.233  1.00 23.94  ? 195 TRP A CA  1 
ATOM   1463 C C   . TRP A 1 180 ? -13.769 -5.399  -6.510  1.00 22.41  ? 195 TRP A C   1 
ATOM   1464 O O   . TRP A 1 180 ? -14.858 -5.973  -6.652  1.00 23.60  ? 195 TRP A O   1 
ATOM   1465 C CB  . TRP A 1 180 ? -14.591 -3.577  -5.000  1.00 23.42  ? 195 TRP A CB  1 
ATOM   1466 C CG  . TRP A 1 180 ? -14.389 -2.665  -3.817  1.00 24.76  ? 195 TRP A CG  1 
ATOM   1467 C CD1 . TRP A 1 180 ? -14.410 -1.309  -3.845  1.00 26.69  ? 195 TRP A CD1 1 
ATOM   1468 C CD2 . TRP A 1 180 ? -14.138 -3.039  -2.455  1.00 26.26  ? 195 TRP A CD2 1 
ATOM   1469 N NE1 . TRP A 1 180 ? -14.259 -0.804  -2.586  1.00 28.01  ? 195 TRP A NE1 1 
ATOM   1470 C CE2 . TRP A 1 180 ? -14.056 -1.835  -1.710  1.00 26.25  ? 195 TRP A CE2 1 
ATOM   1471 C CE3 . TRP A 1 180 ? -13.971 -4.262  -1.789  1.00 27.45  ? 195 TRP A CE3 1 
ATOM   1472 C CZ2 . TRP A 1 180 ? -13.821 -1.830  -0.339  1.00 29.01  ? 195 TRP A CZ2 1 
ATOM   1473 C CZ3 . TRP A 1 180 ? -13.668 -4.244  -0.435  1.00 28.20  ? 195 TRP A CZ3 1 
ATOM   1474 C CH2 . TRP A 1 180 ? -13.654 -3.045  0.280   1.00 28.61  ? 195 TRP A CH2 1 
ATOM   1475 N N   . ASN A 1 181 ? -12.841 -5.388  -7.468  1.00 23.68  ? 196 ASN A N   1 
ATOM   1476 C CA  . ASN A 1 181 ? -13.060 -5.985  -8.787  1.00 23.23  ? 196 ASN A CA  1 
ATOM   1477 C C   . ASN A 1 181 ? -12.627 -7.460  -8.817  1.00 24.83  ? 196 ASN A C   1 
ATOM   1478 O O   . ASN A 1 181 ? -11.593 -7.854  -9.383  1.00 27.21  ? 196 ASN A O   1 
ATOM   1479 C CB  . ASN A 1 181 ? -12.268 -5.182  -9.796  1.00 26.39  ? 196 ASN A CB  1 
ATOM   1480 C CG  . ASN A 1 181 ? -12.526 -5.623  -11.205 1.00 32.89  ? 196 ASN A CG  1 
ATOM   1481 O OD1 . ASN A 1 181 ? -13.582 -6.171  -11.499 1.00 37.22  ? 196 ASN A OD1 1 
ATOM   1482 N ND2 . ASN A 1 181 ? -11.623 -5.283  -12.104 1.00 41.52  ? 196 ASN A ND2 1 
ATOM   1483 N N   . SER A 1 182 ? -13.419 -8.295  -8.142  1.00 22.76  ? 197 SER A N   1 
ATOM   1484 C CA  . SER A 1 182 ? -13.252 -9.742  -8.138  1.00 23.42  ? 197 SER A CA  1 
ATOM   1485 C C   . SER A 1 182 ? -14.605 -10.429 -8.152  1.00 20.88  ? 197 SER A C   1 
ATOM   1486 O O   . SER A 1 182 ? -15.497 -9.950  -7.448  1.00 20.28  ? 197 SER A O   1 
ATOM   1487 C CB  . SER A 1 182 ? -12.511 -10.194 -6.934  1.00 27.22  ? 197 SER A CB  1 
ATOM   1488 O OG  . SER A 1 182 ? -12.419 -11.602 -6.843  1.00 31.66  ? 197 SER A OG  1 
ATOM   1489 N N   . VAL A 1 183 ? -14.729 -11.536 -8.898  1.00 20.97  ? 198 VAL A N   1 
ATOM   1490 C CA  . VAL A 1 183 ? -16.014 -12.244 -8.957  1.00 19.52  ? 198 VAL A CA  1 
ATOM   1491 C C   . VAL A 1 183 ? -16.385 -12.859 -7.596  1.00 20.08  ? 198 VAL A C   1 
ATOM   1492 O O   . VAL A 1 183 ? -17.548 -13.215 -7.384  1.00 20.00  ? 198 VAL A O   1 
ATOM   1493 C CB  . VAL A 1 183 ? -16.119 -13.305 -10.063 1.00 24.92  ? 198 VAL A CB  1 
ATOM   1494 C CG1 . VAL A 1 183 ? -16.235 -12.682 -11.436 1.00 27.07  ? 198 VAL A CG1 1 
ATOM   1495 C CG2 . VAL A 1 183 ? -14.975 -14.299 -9.992  1.00 25.88  ? 198 VAL A CG2 1 
ATOM   1496 N N   . LEU A 1 184 ? -15.441 -12.913 -6.653  1.00 19.52  ? 199 LEU A N   1 
ATOM   1497 C CA  . LEU A 1 184 ? -15.731 -13.271 -5.274  1.00 20.16  ? 199 LEU A CA  1 
ATOM   1498 C C   . LEU A 1 184 ? -16.837 -12.381 -4.692  1.00 19.01  ? 199 LEU A C   1 
ATOM   1499 O O   . LEU A 1 184 ? -17.459 -12.762 -3.715  1.00 19.32  ? 199 LEU A O   1 
ATOM   1500 C CB  . LEU A 1 184 ? -14.483 -13.183 -4.402  1.00 20.65  ? 199 LEU A CB  1 
ATOM   1501 C CG  . LEU A 1 184 ? -13.400 -14.211 -4.704  1.00 20.94  ? 199 LEU A CG  1 
ATOM   1502 C CD1 . LEU A 1 184 ? -12.128 -13.916 -3.957  1.00 23.27  ? 199 LEU A CD1 1 
ATOM   1503 C CD2 . LEU A 1 184 ? -13.828 -15.621 -4.370  1.00 22.53  ? 199 LEU A CD2 1 
ATOM   1504 N N   . TYR A 1 185 ? -16.930 -11.159 -5.212  1.00 18.53  ? 200 TYR A N   1 
ATOM   1505 C CA  . TYR A 1 185 ? -17.854 -10.128 -4.746  1.00 17.69  ? 200 TYR A CA  1 
ATOM   1506 C C   . TYR A 1 185 ? -19.034 -9.885  -5.678  1.00 18.29  ? 200 TYR A C   1 
ATOM   1507 O O   . TYR A 1 185 ? -19.792 -8.944  -5.469  1.00 19.83  ? 200 TYR A O   1 
ATOM   1508 C CB  . TYR A 1 185 ? -17.101 -8.804  -4.514  1.00 18.96  ? 200 TYR A CB  1 
ATOM   1509 C CG  . TYR A 1 185 ? -15.878 -8.898  -3.623  1.00 18.76  ? 200 TYR A CG  1 
ATOM   1510 C CD1 . TYR A 1 185 ? -15.875 -9.687  -2.481  1.00 20.46  ? 200 TYR A CD1 1 
ATOM   1511 C CD2 . TYR A 1 185 ? -14.786 -8.093  -3.842  1.00 23.96  ? 200 TYR A CD2 1 
ATOM   1512 C CE1 . TYR A 1 185 ? -14.781 -9.766  -1.632  1.00 22.21  ? 200 TYR A CE1 1 
ATOM   1513 C CE2 . TYR A 1 185 ? -13.699 -8.144  -3.003  1.00 28.63  ? 200 TYR A CE2 1 
ATOM   1514 C CZ  . TYR A 1 185 ? -13.687 -8.971  -1.893  1.00 27.66  ? 200 TYR A CZ  1 
ATOM   1515 O OH  . TYR A 1 185 ? -12.600 -9.006  -1.065  1.00 35.91  ? 200 TYR A OH  1 
ATOM   1516 N N   . ASP A 1 186 ? -19.230 -10.743 -6.684  1.00 17.90  ? 201 ASP A N   1 
ATOM   1517 C CA  . ASP A 1 186 ? -20.277 -10.619 -7.677  1.00 18.20  ? 201 ASP A CA  1 
ATOM   1518 C C   . ASP A 1 186 ? -21.411 -11.597 -7.356  1.00 18.40  ? 201 ASP A C   1 
ATOM   1519 O O   . ASP A 1 186 ? -21.247 -12.807 -7.613  1.00 19.45  ? 201 ASP A O   1 
ATOM   1520 C CB  . ASP A 1 186 ? -19.723 -10.911 -9.075  1.00 19.34  ? 201 ASP A CB  1 
ATOM   1521 C CG  . ASP A 1 186 ? -20.748 -10.761 -10.193 1.00 21.48  ? 201 ASP A CG  1 
ATOM   1522 O OD1 . ASP A 1 186 ? -21.938 -10.582 -9.860  1.00 20.26  ? 201 ASP A OD1 1 
ATOM   1523 O OD2 . ASP A 1 186 ? -20.368 -10.848 -11.365 1.00 25.13  ? 201 ASP A OD2 1 
ATOM   1524 N N   . TYR A 1 187 ? -22.537 -11.108 -6.811  1.00 18.27  ? 202 TYR A N   1 
ATOM   1525 C CA  . TYR A 1 187 ? -23.582 -12.020 -6.361  1.00 18.53  ? 202 TYR A CA  1 
ATOM   1526 C C   . TYR A 1 187 ? -24.165 -12.839 -7.512  1.00 20.39  ? 202 TYR A C   1 
ATOM   1527 O O   . TYR A 1 187 ? -24.827 -13.859 -7.251  1.00 22.12  ? 202 TYR A O   1 
ATOM   1528 C CB  . TYR A 1 187 ? -24.722 -11.309 -5.619  1.00 19.52  ? 202 TYR A CB  1 
ATOM   1529 C CG  . TYR A 1 187 ? -25.798 -10.652 -6.471  1.00 18.73  ? 202 TYR A CG  1 
ATOM   1530 C CD1 . TYR A 1 187 ? -26.936 -11.333 -6.829  1.00 20.62  ? 202 TYR A CD1 1 
ATOM   1531 C CD2 . TYR A 1 187 ? -25.712 -9.340  -6.892  1.00 21.23  ? 202 TYR A CD2 1 
ATOM   1532 C CE1 . TYR A 1 187 ? -27.949 -10.748 -7.564  1.00 21.25  ? 202 TYR A CE1 1 
ATOM   1533 C CE2 . TYR A 1 187 ? -26.710 -8.731  -7.631  1.00 20.83  ? 202 TYR A CE2 1 
ATOM   1534 C CZ  . TYR A 1 187 ? -27.846 -9.439  -7.971  1.00 21.03  ? 202 TYR A CZ  1 
ATOM   1535 O OH  . TYR A 1 187 ? -28.860 -8.866  -8.692  1.00 21.99  ? 202 TYR A OH  1 
ATOM   1536 N N   . LYS A 1 188 ? -24.023 -12.363 -8.751  1.00 19.49  ? 203 LYS A N   1 
ATOM   1537 C CA  . LYS A 1 188 ? -24.553 -13.040 -9.918  1.00 21.36  ? 203 LYS A CA  1 
ATOM   1538 C C   . LYS A 1 188 ? -23.641 -14.187 -10.370 1.00 23.57  ? 203 LYS A C   1 
ATOM   1539 O O   . LYS A 1 188 ? -24.016 -14.975 -11.218 1.00 27.68  ? 203 LYS A O   1 
ATOM   1540 C CB  . LYS A 1 188 ? -24.794 -12.095 -11.101 1.00 21.30  ? 203 LYS A CB  1 
ATOM   1541 C CG  . LYS A 1 188 ? -25.728 -10.948 -10.791 1.00 22.14  ? 203 LYS A CG  1 
ATOM   1542 C CD  . LYS A 1 188 ? -25.982 -10.003 -11.972 1.00 22.13  ? 203 LYS A CD  1 
ATOM   1543 C CE  . LYS A 1 188 ? -26.740 -8.781  -11.599 1.00 23.40  ? 203 LYS A CE  1 
ATOM   1544 N NZ  . LYS A 1 188 ? -27.069 -7.995  -12.802 1.00 25.97  ? 203 LYS A NZ  1 
ATOM   1545 N N   . HIS A 1 189 ? -22.436 -14.270 -9.797  1.00 20.25  ? 204 HIS A N   1 
ATOM   1546 C CA  . HIS A 1 189 ? -21.442 -15.237 -10.227 1.00 22.04  ? 204 HIS A CA  1 
ATOM   1547 C C   . HIS A 1 189 ? -21.355 -16.409 -9.245  1.00 20.73  ? 204 HIS A C   1 
ATOM   1548 O O   . HIS A 1 189 ? -21.488 -16.262 -8.040  1.00 20.92  ? 204 HIS A O   1 
ATOM   1549 C CB  . HIS A 1 189 ? -20.094 -14.534 -10.381 1.00 23.70  ? 204 HIS A CB  1 
ATOM   1550 C CG  . HIS A 1 189 ? -19.108 -15.332 -11.153 1.00 25.91  ? 204 HIS A CG  1 
ATOM   1551 N ND1 . HIS A 1 189 ? -18.809 -15.131 -12.481 1.00 30.90  ? 204 HIS A ND1 1 
ATOM   1552 C CD2 . HIS A 1 189 ? -18.364 -16.362 -10.730 1.00 22.40  ? 204 HIS A CD2 1 
ATOM   1553 C CE1 . HIS A 1 189 ? -17.888 -16.044 -12.866 1.00 27.91  ? 204 HIS A CE1 1 
ATOM   1554 N NE2 . HIS A 1 189 ? -17.635 -16.814 -11.792 1.00 32.28  ? 204 HIS A NE2 1 
ATOM   1555 N N   . MET A 1 190 ? -21.025 -17.584 -9.791  1.00 23.57  ? 205 MET A N   1 
ATOM   1556 C CA  . MET A 1 190 ? -20.853 -18.778 -8.990  1.00 24.73  ? 205 MET A CA  1 
ATOM   1557 C C   . MET A 1 190 ? -19.779 -18.646 -7.916  1.00 21.79  ? 205 MET A C   1 
ATOM   1558 O O   . MET A 1 190 ? -19.902 -19.317 -6.878  1.00 24.95  ? 205 MET A O   1 
ATOM   1559 C CB  . MET A 1 190 ? -20.498 -19.974 -9.891  1.00 26.17  ? 205 MET A CB  1 
ATOM   1560 C CG  . MET A 1 190 ? -19.068 -20.011 -10.479 1.00 31.95  ? 205 MET A CG  1 
ATOM   1561 S SD  . MET A 1 190 ? -18.456 -21.627 -11.050 1.00 34.33  ? 205 MET A SD  1 
ATOM   1562 C CE  . MET A 1 190 ? -19.953 -22.021 -11.951 1.00 40.32  ? 205 MET A CE  1 
ATOM   1563 N N   . ARG A 1 191 ? -18.771 -17.795 -8.121  1.00 21.94  ? 206 ARG A N   1 
ATOM   1564 C CA  . ARG A 1 191 ? -17.695 -17.655 -7.159  1.00 21.85  ? 206 ARG A CA  1 
ATOM   1565 C C   . ARG A 1 191 ? -18.044 -16.760 -5.960  1.00 20.50  ? 206 ARG A C   1 
ATOM   1566 O O   . ARG A 1 191 ? -17.272 -16.639 -5.033  1.00 21.25  ? 206 ARG A O   1 
ATOM   1567 C CB  . ARG A 1 191 ? -16.433 -17.076 -7.823  1.00 24.25  ? 206 ARG A CB  1 
ATOM   1568 C CG  . ARG A 1 191 ? -15.834 -18.053 -8.824  1.00 26.49  ? 206 ARG A CG  1 
ATOM   1569 C CD  . ARG A 1 191 ? -15.202 -19.257 -8.177  1.00 25.68  ? 206 ARG A CD  1 
ATOM   1570 N NE  . ARG A 1 191 ? -14.019 -18.967 -7.342  1.00 25.45  ? 206 ARG A NE  1 
ATOM   1571 C CZ  . ARG A 1 191 ? -13.440 -19.885 -6.583  1.00 24.56  ? 206 ARG A CZ  1 
ATOM   1572 N NH1 . ARG A 1 191 ? -13.908 -21.135 -6.551  1.00 25.61  ? 206 ARG A NH1 1 
ATOM   1573 N NH2 . ARG A 1 191 ? -12.389 -19.562 -5.876  1.00 24.52  ? 206 ARG A NH2 1 
ATOM   1574 N N   . TYR A 1 192 ? -19.227 -16.154 -5.951  1.00 19.10  ? 207 TYR A N   1 
ATOM   1575 C CA  . TYR A 1 192 ? -19.601 -15.238 -4.864  1.00 18.49  ? 207 TYR A CA  1 
ATOM   1576 C C   . TYR A 1 192 ? -19.431 -15.919 -3.510  1.00 19.14  ? 207 TYR A C   1 
ATOM   1577 O O   . TYR A 1 192 ? -20.022 -16.966 -3.293  1.00 19.49  ? 207 TYR A O   1 
ATOM   1578 C CB  . TYR A 1 192 ? -21.070 -14.847 -5.021  1.00 18.80  ? 207 TYR A CB  1 
ATOM   1579 C CG  . TYR A 1 192 ? -21.551 -13.794 -4.043  1.00 18.07  ? 207 TYR A CG  1 
ATOM   1580 C CD1 . TYR A 1 192 ? -20.879 -12.618 -3.773  1.00 18.27  ? 207 TYR A CD1 1 
ATOM   1581 C CD2 . TYR A 1 192 ? -22.791 -13.954 -3.483  1.00 18.87  ? 207 TYR A CD2 1 
ATOM   1582 C CE1 . TYR A 1 192 ? -21.403 -11.667 -2.923  1.00 18.74  ? 207 TYR A CE1 1 
ATOM   1583 C CE2 . TYR A 1 192 ? -23.348 -12.996 -2.655  1.00 19.04  ? 207 TYR A CE2 1 
ATOM   1584 C CZ  . TYR A 1 192 ? -22.642 -11.854 -2.359  1.00 18.92  ? 207 TYR A CZ  1 
ATOM   1585 O OH  . TYR A 1 192 ? -23.165 -10.908 -1.517  1.00 20.16  ? 207 TYR A OH  1 
ATOM   1586 N N   . ILE A 1 193 ? -18.650 -15.328 -2.604  1.00 18.95  ? 208 ILE A N   1 
ATOM   1587 C CA  . ILE A 1 193 ? -18.328 -16.002 -1.362  1.00 18.65  ? 208 ILE A CA  1 
ATOM   1588 C C   . ILE A 1 193 ? -19.586 -16.272 -0.551  1.00 18.45  ? 208 ILE A C   1 
ATOM   1589 O O   . ILE A 1 193 ? -19.701 -17.306 0.122   1.00 21.01  ? 208 ILE A O   1 
ATOM   1590 C CB  . ILE A 1 193 ? -17.287 -15.220 -0.539  1.00 20.60  ? 208 ILE A CB  1 
ATOM   1591 C CG1 . ILE A 1 193 ? -15.927 -15.256 -1.232  1.00 20.16  ? 208 ILE A CG1 1 
ATOM   1592 C CG2 . ILE A 1 193 ? -17.219 -15.753 0.890   1.00 21.08  ? 208 ILE A CG2 1 
ATOM   1593 C CD1 . ILE A 1 193 ? -14.908 -14.288 -0.685  1.00 21.29  ? 208 ILE A CD1 1 
ATOM   1594 N N   . HIS A 1 194 ? -20.513 -15.308 -0.598  1.00 18.81  ? 209 HIS A N   1 
ATOM   1595 C CA  . HIS A 1 194 ? -21.722 -15.385 0.209   1.00 18.57  ? 209 HIS A CA  1 
ATOM   1596 C C   . HIS A 1 194 ? -22.843 -16.108 -0.530  1.00 18.70  ? 209 HIS A C   1 
ATOM   1597 O O   . HIS A 1 194 ? -24.006 -16.101 -0.064  1.00 19.85  ? 209 HIS A O   1 
ATOM   1598 C CB  . HIS A 1 194 ? -22.110 -13.966 0.664   1.00 18.92  ? 209 HIS A CB  1 
ATOM   1599 C CG  . HIS A 1 194 ? -23.212 -13.877 1.666   1.00 17.80  ? 209 HIS A CG  1 
ATOM   1600 N ND1 . HIS A 1 194 ? -23.042 -14.378 2.930   1.00 19.95  ? 209 HIS A ND1 1 
ATOM   1601 C CD2 . HIS A 1 194 ? -24.469 -13.333 1.617   1.00 19.21  ? 209 HIS A CD2 1 
ATOM   1602 C CE1 . HIS A 1 194 ? -24.179 -14.171 3.622   1.00 20.80  ? 209 HIS A CE1 1 
ATOM   1603 N NE2 . HIS A 1 194 ? -25.063 -13.543 2.828   1.00 20.14  ? 209 HIS A NE2 1 
ATOM   1604 N N   . GLY A 1 195 ? -22.538 -16.761 -1.642  1.00 19.02  ? 210 GLY A N   1 
ATOM   1605 C CA  . GLY A 1 195 ? -23.597 -17.349 -2.442  1.00 20.00  ? 210 GLY A CA  1 
ATOM   1606 C C   . GLY A 1 195 ? -24.258 -18.521 -1.724  1.00 20.01  ? 210 GLY A C   1 
ATOM   1607 O O   . GLY A 1 195 ? -23.612 -19.349 -1.084  1.00 23.00  ? 210 GLY A O   1 
ATOM   1608 N N   . GLY A 1 196 ? -25.595 -18.539 -1.773  1.00 20.72  ? 211 GLY A N   1 
ATOM   1609 C CA  . GLY A 1 196 ? -26.371 -19.678 -1.276  1.00 22.45  ? 211 GLY A CA  1 
ATOM   1610 C C   . GLY A 1 196 ? -26.655 -19.625 0.220   1.00 21.43  ? 211 GLY A C   1 
ATOM   1611 O O   . GLY A 1 196 ? -27.115 -20.630 0.795   1.00 24.91  ? 211 GLY A O   1 
ATOM   1612 N N   . TYR A 1 197 ? -26.424 -18.460 0.863   1.00 21.14  ? 212 TYR A N   1 
ATOM   1613 C CA  . TYR A 1 197 ? -26.638 -18.377 2.322   1.00 21.47  ? 212 TYR A CA  1 
ATOM   1614 C C   . TYR A 1 197 ? -27.902 -17.607 2.743   1.00 23.17  ? 212 TYR A C   1 
ATOM   1615 O O   . TYR A 1 197 ? -28.098 -17.395 3.944   1.00 24.31  ? 212 TYR A O   1 
ATOM   1616 C CB  . TYR A 1 197 ? -25.376 -17.836 3.008   1.00 23.07  ? 212 TYR A CB  1 
ATOM   1617 C CG  . TYR A 1 197 ? -24.126 -18.673 2.771   1.00 21.25  ? 212 TYR A CG  1 
ATOM   1618 C CD1 . TYR A 1 197 ? -24.177 -20.072 2.707   1.00 23.67  ? 212 TYR A CD1 1 
ATOM   1619 C CD2 . TYR A 1 197 ? -22.909 -18.064 2.592   1.00 21.50  ? 212 TYR A CD2 1 
ATOM   1620 C CE1 . TYR A 1 197 ? -23.025 -20.797 2.465   1.00 24.11  ? 212 TYR A CE1 1 
ATOM   1621 C CE2 . TYR A 1 197 ? -21.749 -18.781 2.408   1.00 22.16  ? 212 TYR A CE2 1 
ATOM   1622 C CZ  . TYR A 1 197 ? -21.804 -20.148 2.347   1.00 24.36  ? 212 TYR A CZ  1 
ATOM   1623 O OH  . TYR A 1 197 ? -20.651 -20.849 2.171   1.00 24.26  ? 212 TYR A OH  1 
ATOM   1624 N N   . SER A 1 198 ? -28.728 -17.208 1.787   1.00 20.54  ? 213 SER A N   1 
ATOM   1625 C CA  . SER A 1 198 ? -30.075 -16.754 2.101   1.00 21.40  ? 213 SER A CA  1 
ATOM   1626 C C   . SER A 1 198 ? -30.888 -17.953 2.551   1.00 21.41  ? 213 SER A C   1 
ATOM   1627 O O   . SER A 1 198 ? -30.810 -18.979 1.892   1.00 22.26  ? 213 SER A O   1 
ATOM   1628 C CB  . SER A 1 198 ? -30.730 -16.135 0.912   1.00 21.07  ? 213 SER A CB  1 
ATOM   1629 O OG  . SER A 1 198 ? -32.077 -15.803 1.208   1.00 22.27  ? 213 SER A OG  1 
ATOM   1630 N N   . SER A 1 199 ? -31.725 -17.811 3.577   1.00 20.36  ? 214 SER A N   1 
ATOM   1631 C CA  . SER A 1 199 ? -32.637 -18.891 3.916   1.00 23.98  ? 214 SER A CA  1 
ATOM   1632 C C   . SER A 1 199 ? -33.646 -19.172 2.787   1.00 21.65  ? 214 SER A C   1 
ATOM   1633 O O   . SER A 1 199 ? -34.169 -20.295 2.713   1.00 24.74  ? 214 SER A O   1 
ATOM   1634 C CB  . SER A 1 199 ? -33.310 -18.689 5.242   1.00 24.79  ? 214 SER A CB  1 
ATOM   1635 O OG  . SER A 1 199 ? -32.387 -18.835 6.309   1.00 27.35  ? 214 SER A OG  1 
ATOM   1636 N N   . TRP A 1 200 ? -33.913 -18.221 1.889   1.00 21.95  ? 215 TRP A N   1 
ATOM   1637 C CA  . TRP A 1 200 ? -34.757 -18.462 0.735   1.00 21.51  ? 215 TRP A CA  1 
ATOM   1638 C C   . TRP A 1 200 ? -34.173 -19.534 -0.198  1.00 21.99  ? 215 TRP A C   1 
ATOM   1639 O O   . TRP A 1 200 ? -34.890 -20.242 -0.868  1.00 25.70  ? 215 TRP A O   1 
ATOM   1640 C CB  . TRP A 1 200 ? -35.049 -17.166 -0.042  1.00 21.42  ? 215 TRP A CB  1 
ATOM   1641 C CG  . TRP A 1 200 ? -35.928 -16.221 0.704   1.00 22.05  ? 215 TRP A CG  1 
ATOM   1642 C CD1 . TRP A 1 200 ? -35.500 -15.111 1.348   1.00 21.48  ? 215 TRP A CD1 1 
ATOM   1643 C CD2 . TRP A 1 200 ? -37.349 -16.343 0.936   1.00 20.92  ? 215 TRP A CD2 1 
ATOM   1644 N NE1 . TRP A 1 200 ? -36.570 -14.523 1.954   1.00 21.31  ? 215 TRP A NE1 1 
ATOM   1645 C CE2 . TRP A 1 200 ? -37.720 -15.220 1.708   1.00 22.04  ? 215 TRP A CE2 1 
ATOM   1646 C CE3 . TRP A 1 200 ? -38.339 -17.240 0.536   1.00 23.49  ? 215 TRP A CE3 1 
ATOM   1647 C CZ2 . TRP A 1 200 ? -39.034 -14.997 2.131   1.00 22.53  ? 215 TRP A CZ2 1 
ATOM   1648 C CZ3 . TRP A 1 200 ? -39.616 -17.019 0.974   1.00 23.91  ? 215 TRP A CZ3 1 
ATOM   1649 C CH2 . TRP A 1 200 ? -39.963 -15.924 1.745   1.00 23.63  ? 215 TRP A CH2 1 
ATOM   1650 N N   . TRP A 1 201 ? -32.849 -19.672 -0.203  1.00 22.38  ? 216 TRP A N   1 
ATOM   1651 C CA  . TRP A 1 201 ? -32.189 -20.761 -0.896  1.00 23.16  ? 216 TRP A CA  1 
ATOM   1652 C C   . TRP A 1 201 ? -32.043 -21.991 0.013   1.00 22.68  ? 216 TRP A C   1 
ATOM   1653 O O   . TRP A 1 201 ? -32.310 -23.113 -0.445  1.00 27.06  ? 216 TRP A O   1 
ATOM   1654 C CB  . TRP A 1 201 ? -30.831 -20.319 -1.458  1.00 23.20  ? 216 TRP A CB  1 
ATOM   1655 C CG  . TRP A 1 201 ? -30.126 -21.445 -2.146  1.00 23.92  ? 216 TRP A CG  1 
ATOM   1656 C CD1 . TRP A 1 201 ? -29.024 -22.080 -1.692  1.00 24.45  ? 216 TRP A CD1 1 
ATOM   1657 C CD2 . TRP A 1 201 ? -30.595 -22.166 -3.296  1.00 26.31  ? 216 TRP A CD2 1 
ATOM   1658 N NE1 . TRP A 1 201 ? -28.738 -23.136 -2.524  1.00 27.62  ? 216 TRP A NE1 1 
ATOM   1659 C CE2 . TRP A 1 201 ? -29.651 -23.187 -3.537  1.00 26.80  ? 216 TRP A CE2 1 
ATOM   1660 C CE3 . TRP A 1 201 ? -31.692 -22.047 -4.158  1.00 28.21  ? 216 TRP A CE3 1 
ATOM   1661 C CZ2 . TRP A 1 201 ? -29.790 -24.096 -4.585  1.00 28.25  ? 216 TRP A CZ2 1 
ATOM   1662 C CZ3 . TRP A 1 201 ? -31.825 -22.939 -5.199  1.00 28.77  ? 216 TRP A CZ3 1 
ATOM   1663 C CH2 . TRP A 1 201 ? -30.891 -23.952 -5.407  1.00 31.25  ? 216 TRP A CH2 1 
ATOM   1664 N N   . LEU A 1 202 ? -31.567 -21.800 1.258   1.00 22.73  ? 217 LEU A N   1 
ATOM   1665 C CA  . LEU A 1 202 ? -31.315 -22.892 2.193   1.00 23.82  ? 217 LEU A CA  1 
ATOM   1666 C C   . LEU A 1 202 ? -32.560 -23.753 2.420   1.00 24.69  ? 217 LEU A C   1 
ATOM   1667 O O   . LEU A 1 202 ? -32.444 -24.979 2.554   1.00 27.32  ? 217 LEU A O   1 
ATOM   1668 C CB  . LEU A 1 202 ? -30.691 -22.455 3.513   1.00 24.72  ? 217 LEU A CB  1 
ATOM   1669 C CG  . LEU A 1 202 ? -29.305 -21.848 3.408   1.00 25.13  ? 217 LEU A CG  1 
ATOM   1670 C CD1 . LEU A 1 202 ? -28.927 -21.119 4.682   1.00 28.94  ? 217 LEU A CD1 1 
ATOM   1671 C CD2 . LEU A 1 202 ? -28.279 -22.916 3.026   1.00 27.18  ? 217 LEU A CD2 1 
ATOM   1672 N N   . LEU A 1 203 ? -33.761 -23.148 2.332   1.00 25.90  ? 218 LEU A N   1 
ATOM   1673 C CA  . LEU A 1 203 ? -34.980 -23.909 2.497   1.00 26.72  ? 218 LEU A CA  1 
ATOM   1674 C C   . LEU A 1 203 ? -35.141 -24.951 1.400   1.00 27.10  ? 218 LEU A C   1 
ATOM   1675 O O   . LEU A 1 203 ? -35.749 -25.990 1.642   1.00 32.70  ? 218 LEU A O   1 
ATOM   1676 C CB  . LEU A 1 203 ? -36.174 -22.959 2.469   1.00 26.98  ? 218 LEU A CB  1 
ATOM   1677 C CG  . LEU A 1 203 ? -36.470 -22.219 3.764   1.00 29.44  ? 218 LEU A CG  1 
ATOM   1678 C CD1 . LEU A 1 203 ? -37.496 -21.131 3.502   1.00 28.77  ? 218 LEU A CD1 1 
ATOM   1679 C CD2 . LEU A 1 203 ? -36.967 -23.155 4.831   1.00 31.51  ? 218 LEU A CD2 1 
ATOM   1680 N N   . GLU A 1 204 ? -34.574 -24.691 0.216   1.00 29.32  ? 219 GLU A N   1 
ATOM   1681 C CA  . GLU A 1 204 ? -34.653 -25.594 -0.921  1.00 29.45  ? 219 GLU A CA  1 
ATOM   1682 C C   . GLU A 1 204 ? -33.838 -26.886 -0.706  1.00 32.26  ? 219 GLU A C   1 
ATOM   1683 O O   . GLU A 1 204 ? -34.093 -27.869 -1.363  1.00 38.03  ? 219 GLU A O   1 
ATOM   1684 C CB  . GLU A 1 204 ? -34.130 -24.998 -2.229  1.00 31.16  ? 219 GLU A CB  1 
ATOM   1685 C CG  . GLU A 1 204 ? -34.833 -23.737 -2.735  1.00 31.30  ? 219 GLU A CG  1 
ATOM   1686 C CD  . GLU A 1 204 ? -36.246 -23.908 -3.299  1.00 33.32  ? 219 GLU A CD  1 
ATOM   1687 O OE1 . GLU A 1 204 ? -36.767 -25.056 -3.345  1.00 43.16  ? 219 GLU A OE1 1 
ATOM   1688 O OE2 . GLU A 1 204 ? -36.800 -22.886 -3.788  1.00 30.53  ? 219 GLU A OE2 1 
ATOM   1689 N N   . LYS A 1 205 ? -32.932 -26.910 0.273   1.00 33.01  ? 220 LYS A N   1 
ATOM   1690 C CA  . LYS A 1 205 ? -31.947 -27.956 0.436   1.00 39.90  ? 220 LYS A CA  1 
ATOM   1691 C C   . LYS A 1 205 ? -32.306 -28.856 1.605   1.00 44.48  ? 220 LYS A C   1 
ATOM   1692 O O   . LYS A 1 205 ? -31.573 -29.814 1.875   1.00 54.08  ? 220 LYS A O   1 
ATOM   1693 C CB  . LYS A 1 205 ? -30.565 -27.315 0.619   1.00 41.30  ? 220 LYS A CB  1 
ATOM   1694 C CG  . LYS A 1 205 ? -30.132 -26.387 -0.527  1.00 48.72  ? 220 LYS A CG  1 
ATOM   1695 C CD  . LYS A 1 205 ? -30.215 -26.960 -1.947  1.00 51.80  ? 220 LYS A CD  1 
ATOM   1696 C CE  . LYS A 1 205 ? -29.183 -27.986 -2.277  1.00 60.59  ? 220 LYS A CE  1 
ATOM   1697 N NZ  . LYS A 1 205 ? -29.148 -28.290 -3.713  1.00 63.69  ? 220 LYS A NZ  1 
ATOM   1698 N N   . ILE A 1 206 ? -33.430 -28.556 2.262   1.00 45.51  ? 221 ILE A N   1 
ATOM   1699 C CA  . ILE A 1 206 ? -33.943 -29.357 3.360   1.00 52.96  ? 221 ILE A CA  1 
ATOM   1700 C C   . ILE A 1 206 ? -34.260 -30.763 2.866   1.00 63.08  ? 221 ILE A C   1 
ATOM   1701 O O   . ILE A 1 206 ? -34.001 -31.727 3.580   1.00 71.39  ? 221 ILE A O   1 
ATOM   1702 C CB  . ILE A 1 206 ? -35.149 -28.643 3.981   1.00 48.40  ? 221 ILE A CB  1 
ATOM   1703 C CG1 . ILE A 1 206 ? -34.637 -27.410 4.733   1.00 45.15  ? 221 ILE A CG1 1 
ATOM   1704 C CG2 . ILE A 1 206 ? -35.987 -29.580 4.853   1.00 55.71  ? 221 ILE A CG2 1 
ATOM   1705 C CD1 . ILE A 1 206 ? -35.661 -26.759 5.620   1.00 50.66  ? 221 ILE A CD1 1 
ATOM   1706 N N   . LYS A 1 207 ? -34.813 -30.866 1.649   1.00 67.19  ? 222 LYS A N   1 
ATOM   1707 C CA  . LYS A 1 207 ? -34.939 -32.145 0.960   1.00 74.60  ? 222 LYS A CA  1 
ATOM   1708 C C   . LYS A 1 207 ? -35.859 -33.079 1.764   1.00 78.22  ? 222 LYS A C   1 
ATOM   1709 O O   . LYS A 1 207 ? -36.585 -32.561 2.633   1.00 81.02  ? 222 LYS A O   1 
ATOM   1710 C CB  . LYS A 1 207 ? -33.580 -32.820 0.729   1.00 76.58  ? 222 LYS A CB  1 
ATOM   1711 C CG  . LYS A 1 207 ? -33.213 -33.957 1.682   1.00 84.00  ? 222 LYS A CG  1 
ATOM   1712 C CD  . LYS A 1 207 ? -31.717 -34.217 1.790   1.00 87.57  ? 222 LYS A CD  1 
ATOM   1713 C CE  . LYS A 1 207 ? -31.019 -33.164 2.597   1.00 90.00  ? 222 LYS A CE  1 
ATOM   1714 N NZ  . LYS A 1 207 ? -29.612 -33.501 2.829   1.00 91.29  ? 222 LYS A NZ  1 
HETATM 1715 C C   . ACY B 2 .   ? -43.859 25.706  4.089   1.00 51.81  ? 301 ACY A C   1 
HETATM 1716 O O   . ACY B 2 .   ? -44.207 26.694  3.424   1.00 60.13  ? 301 ACY A O   1 
HETATM 1717 O OXT . ACY B 2 .   ? -42.809 25.656  4.809   1.00 61.12  ? 301 ACY A OXT 1 
HETATM 1718 C CH3 . ACY B 2 .   ? -44.753 24.484  4.016   1.00 51.70  ? 301 ACY A CH3 1 
HETATM 1719 O O   . HOH C 3 .   ? -25.804 1.978   -18.058 1.00 41.86  ? 401 HOH A O   1 
HETATM 1720 O O   . HOH C 3 .   ? -10.448 -23.062 7.646   1.00 68.53  ? 402 HOH A O   1 
HETATM 1721 O O   . HOH C 3 .   ? -44.917 -12.152 -12.985 1.00 57.81  ? 403 HOH A O   1 
HETATM 1722 O O   . HOH C 3 .   ? -16.920 -26.294 9.385   1.00 66.37  ? 404 HOH A O   1 
HETATM 1723 O O   . HOH C 3 .   ? -27.022 9.113   13.546  1.00 53.19  ? 405 HOH A O   1 
HETATM 1724 O O   . HOH C 3 .   ? -12.390 -4.963  5.936   1.00 57.51  ? 406 HOH A O   1 
HETATM 1725 O O   . HOH C 3 .   ? -22.348 10.233  -15.800 1.00 42.80  ? 407 HOH A O   1 
HETATM 1726 O O   . HOH C 3 .   ? -19.745 9.832   -0.863  1.00 44.32  ? 408 HOH A O   1 
HETATM 1727 O O   . HOH C 3 .   ? -34.353 9.455   9.315   1.00 64.87  ? 409 HOH A O   1 
HETATM 1728 O O   . HOH C 3 .   ? -29.456 6.434   -5.957  1.00 32.63  ? 410 HOH A O   1 
HETATM 1729 O O   . HOH C 3 .   ? -32.373 9.185   15.353  1.00 43.19  ? 411 HOH A O   1 
HETATM 1730 O O   . HOH C 3 .   ? -31.240 12.063  14.480  1.00 67.61  ? 412 HOH A O   1 
HETATM 1731 O O   . HOH C 3 .   ? -18.245 -9.996  -12.774 1.00 29.64  ? 413 HOH A O   1 
HETATM 1732 O O   . HOH C 3 .   ? -35.159 16.446  5.127   1.00 44.36  ? 414 HOH A O   1 
HETATM 1733 O O   . HOH C 3 .   ? -14.001 -9.647  9.871   1.00 53.25  ? 415 HOH A O   1 
HETATM 1734 O O   . HOH C 3 .   ? -42.523 -23.678 11.402  1.00 41.24  ? 416 HOH A O   1 
HETATM 1735 O O   . HOH C 3 .   ? -41.174 -11.998 -10.585 1.00 41.78  ? 417 HOH A O   1 
HETATM 1736 O O   . HOH C 3 .   ? -40.413 2.871   1.109   1.00 55.78  ? 418 HOH A O   1 
HETATM 1737 O O   . HOH C 3 .   ? -28.199 8.782   -6.576  1.00 37.45  ? 419 HOH A O   1 
HETATM 1738 O O   . HOH C 3 .   ? -14.627 -0.011  -12.703 1.00 43.38  ? 420 HOH A O   1 
HETATM 1739 O O   . HOH C 3 .   ? -14.738 8.097   7.033   1.00 32.92  ? 421 HOH A O   1 
HETATM 1740 O O   . HOH C 3 .   ? -42.426 -19.455 10.963  1.00 37.68  ? 422 HOH A O   1 
HETATM 1741 O O   . HOH C 3 .   ? -9.852  -11.652 -6.306  1.00 36.23  ? 423 HOH A O   1 
HETATM 1742 O O   . HOH C 3 .   ? -39.746 -24.423 0.613   1.00 47.98  ? 424 HOH A O   1 
HETATM 1743 O O   . HOH C 3 .   ? -12.414 2.615   -2.371  1.00 52.62  ? 425 HOH A O   1 
HETATM 1744 O O   . HOH C 3 .   ? -42.977 -5.399  -12.072 1.00 41.77  ? 426 HOH A O   1 
HETATM 1745 O O   . HOH C 3 .   ? -21.780 -8.558  -1.660  1.00 20.38  ? 427 HOH A O   1 
HETATM 1746 O O   . HOH C 3 .   ? -39.427 24.274  6.330   1.00 43.80  ? 428 HOH A O   1 
HETATM 1747 O O   . HOH C 3 .   ? -23.852 -6.428  -7.453  1.00 20.21  ? 429 HOH A O   1 
HETATM 1748 O O   . HOH C 3 .   ? -36.583 -2.392  4.131   1.00 61.16  ? 430 HOH A O   1 
HETATM 1749 O O   . HOH C 3 .   ? -29.703 5.313   -19.575 1.00 41.28  ? 431 HOH A O   1 
HETATM 1750 O O   . HOH C 3 .   ? -33.493 -14.129 -16.805 1.00 63.88  ? 432 HOH A O   1 
HETATM 1751 O O   . HOH C 3 .   ? -45.374 -13.077 -16.426 1.00 55.31  ? 433 HOH A O   1 
HETATM 1752 O O   . HOH C 3 .   ? -21.738 -11.811 -13.439 1.00 33.21  ? 434 HOH A O   1 
HETATM 1753 O O   . HOH C 3 .   ? -37.607 16.453  -1.482  1.00 42.81  ? 435 HOH A O   1 
HETATM 1754 O O   . HOH C 3 .   ? -26.369 -15.060 -12.476 1.00 52.23  ? 436 HOH A O   1 
HETATM 1755 O O   . HOH C 3 .   ? -34.616 1.982   -18.401 1.00 52.46  ? 437 HOH A O   1 
HETATM 1756 O O   . HOH C 3 .   ? -18.486 -19.370 1.655   1.00 24.89  ? 438 HOH A O   1 
HETATM 1757 O O   . HOH C 3 .   ? -30.167 -1.260  11.250  1.00 36.10  ? 439 HOH A O   1 
HETATM 1758 O O   . HOH C 3 .   ? -34.077 14.516  8.761   1.00 88.68  ? 440 HOH A O   1 
HETATM 1759 O O   . HOH C 3 .   ? -29.346 -6.472  -9.823  1.00 24.81  ? 441 HOH A O   1 
HETATM 1760 O O   . HOH C 3 .   ? -28.982 -5.970  -6.534  1.00 27.22  ? 442 HOH A O   1 
HETATM 1761 O O   . HOH C 3 .   ? -26.588 -15.241 -0.211  1.00 27.82  ? 443 HOH A O   1 
HETATM 1762 O O   . HOH C 3 .   ? -28.740 2.490   5.441   1.00 24.91  ? 444 HOH A O   1 
HETATM 1763 O O   . HOH C 3 .   ? -31.026 8.783   5.139   1.00 52.23  ? 445 HOH A O   1 
HETATM 1764 O O   . HOH C 3 .   ? -46.827 -15.038 -0.141  1.00 47.25  ? 446 HOH A O   1 
HETATM 1765 O O   . HOH C 3 .   ? -20.160 -7.141  -3.512  1.00 23.17  ? 447 HOH A O   1 
HETATM 1766 O O   . HOH C 3 .   ? -39.141 -3.411  -0.168  1.00 38.00  ? 448 HOH A O   1 
HETATM 1767 O O   . HOH C 3 .   ? -38.453 -6.560  10.383  1.00 39.22  ? 449 HOH A O   1 
HETATM 1768 O O   . HOH C 3 .   ? -19.477 -5.768  13.459  1.00 38.58  ? 450 HOH A O   1 
HETATM 1769 O O   . HOH C 3 .   ? -23.679 -16.835 -6.564  1.00 46.02  ? 451 HOH A O   1 
HETATM 1770 O O   . HOH C 3 .   ? -18.427 -0.492  13.832  1.00 31.46  ? 452 HOH A O   1 
HETATM 1771 O O   . HOH C 3 .   ? -32.059 -15.046 4.406   1.00 24.77  ? 453 HOH A O   1 
HETATM 1772 O O   . HOH C 3 .   ? -19.037 -25.692 3.039   1.00 35.12  ? 454 HOH A O   1 
HETATM 1773 O O   . HOH C 3 .   ? -17.237 6.325   -16.553 1.00 68.36  ? 455 HOH A O   1 
HETATM 1774 O O   . HOH C 3 .   ? -26.598 8.582   -0.109  1.00 33.31  ? 456 HOH A O   1 
HETATM 1775 O O   . HOH C 3 .   ? -31.990 7.785   -2.598  1.00 61.88  ? 457 HOH A O   1 
HETATM 1776 O O   . HOH C 3 .   ? -29.155 -3.248  7.371   1.00 30.17  ? 458 HOH A O   1 
HETATM 1777 O O   . HOH C 3 .   ? -14.351 6.904   2.798   1.00 39.81  ? 459 HOH A O   1 
HETATM 1778 O O   . HOH C 3 .   ? -26.030 -5.767  -9.778  1.00 22.79  ? 460 HOH A O   1 
HETATM 1779 O O   . HOH C 3 .   ? -42.372 -18.671 -12.311 1.00 47.60  ? 461 HOH A O   1 
HETATM 1780 O O   . HOH C 3 .   ? -30.237 -4.221  -8.346  1.00 21.11  ? 462 HOH A O   1 
HETATM 1781 O O   . HOH C 3 .   ? -33.539 -6.190  2.529   1.00 30.22  ? 463 HOH A O   1 
HETATM 1782 O O   . HOH C 3 .   ? -36.249 6.807   -10.315 1.00 45.29  ? 464 HOH A O   1 
HETATM 1783 O O   . HOH C 3 .   ? -20.871 -19.631 -1.050  1.00 24.94  ? 465 HOH A O   1 
HETATM 1784 O O   . HOH C 3 .   ? -30.948 -10.184 -9.916  1.00 27.81  ? 466 HOH A O   1 
HETATM 1785 O O   . HOH C 3 .   ? -36.979 -11.920 2.962   1.00 22.34  ? 467 HOH A O   1 
HETATM 1786 O O   . HOH C 3 .   ? -12.439 0.396   1.929   1.00 38.36  ? 468 HOH A O   1 
HETATM 1787 O O   . HOH C 3 .   ? -24.001 -14.963 14.248  1.00 38.33  ? 469 HOH A O   1 
HETATM 1788 O O   . HOH C 3 .   ? -24.608 -0.660  14.477  1.00 28.17  ? 470 HOH A O   1 
HETATM 1789 O O   . HOH C 3 .   ? -40.969 20.621  10.066  1.00 35.90  ? 471 HOH A O   1 
HETATM 1790 O O   . HOH C 3 .   ? -25.219 -12.478 14.690  1.00 30.36  ? 472 HOH A O   1 
HETATM 1791 O O   . HOH C 3 .   ? -18.729 -4.792  -3.302  1.00 29.09  ? 473 HOH A O   1 
HETATM 1792 O O   . HOH C 3 .   ? -38.855 -7.532  -15.553 1.00 35.29  ? 474 HOH A O   1 
HETATM 1793 O O   . HOH C 3 .   ? -36.269 -4.851  10.032  1.00 31.77  ? 475 HOH A O   1 
HETATM 1794 O O   . HOH C 3 .   ? -16.521 4.732   7.733   1.00 28.27  ? 476 HOH A O   1 
HETATM 1795 O O   . HOH C 3 .   ? -25.921 5.487   16.285  1.00 40.51  ? 477 HOH A O   1 
HETATM 1796 O O   . HOH C 3 .   ? -31.317 -8.876  17.531  1.00 36.25  ? 478 HOH A O   1 
HETATM 1797 O O   . HOH C 3 .   ? -15.977 -18.858 -3.944  1.00 42.54  ? 479 HOH A O   1 
HETATM 1798 O O   . HOH C 3 .   ? -25.781 -23.065 0.460   1.00 32.42  ? 480 HOH A O   1 
HETATM 1799 O O   . HOH C 3 .   ? -33.644 -17.862 -3.488  1.00 23.23  ? 481 HOH A O   1 
HETATM 1800 O O   . HOH C 3 .   ? -14.774 -1.907  -8.345  1.00 23.84  ? 482 HOH A O   1 
HETATM 1801 O O   . HOH C 3 .   ? -27.025 -0.624  13.067  1.00 30.67  ? 483 HOH A O   1 
HETATM 1802 O O   . HOH C 3 .   ? -45.371 -8.638  -10.622 1.00 45.92  ? 484 HOH A O   1 
HETATM 1803 O O   . HOH C 3 .   ? -35.248 4.669   -3.230  1.00 43.56  ? 485 HOH A O   1 
HETATM 1804 O O   . HOH C 3 .   ? -16.386 -4.152  -8.139  1.00 35.70  ? 486 HOH A O   1 
HETATM 1805 O O   . HOH C 3 .   ? -41.993 -5.845  -6.198  1.00 33.51  ? 487 HOH A O   1 
HETATM 1806 O O   . HOH C 3 .   ? -25.805 6.759   1.771   1.00 29.82  ? 488 HOH A O   1 
HETATM 1807 O O   . HOH C 3 .   ? -22.508 -8.299  -5.842  1.00 20.26  ? 489 HOH A O   1 
HETATM 1808 O O   . HOH C 3 .   ? -11.220 -8.862  3.537   1.00 41.73  ? 490 HOH A O   1 
HETATM 1809 O O   . HOH C 3 .   ? -12.612 -24.837 6.190   1.00 40.67  ? 491 HOH A O   1 
HETATM 1810 O O   . HOH C 3 .   ? -41.852 -17.617 9.059   1.00 37.35  ? 492 HOH A O   1 
HETATM 1811 O O   . HOH C 3 .   ? -42.360 -2.283  -15.078 1.00 66.77  ? 493 HOH A O   1 
HETATM 1812 O O   . HOH C 3 .   ? -22.641 -6.647  15.241  1.00 38.93  ? 494 HOH A O   1 
HETATM 1813 O O   . HOH C 3 .   ? -10.588 -10.919 7.779   1.00 57.95  ? 495 HOH A O   1 
HETATM 1814 O O   . HOH C 3 .   ? -32.261 -1.716  13.219  1.00 48.10  ? 496 HOH A O   1 
HETATM 1815 O O   . HOH C 3 .   ? -16.979 7.975   4.406   1.00 39.56  ? 497 HOH A O   1 
HETATM 1816 O O   . HOH C 3 .   ? -30.769 -26.375 4.370   1.00 50.73  ? 498 HOH A O   1 
HETATM 1817 O O   . HOH C 3 .   ? -23.519 -22.179 -0.895  1.00 31.11  ? 499 HOH A O   1 
HETATM 1818 O O   . HOH C 3 .   ? -17.444 -14.417 11.622  1.00 51.88  ? 500 HOH A O   1 
HETATM 1819 O O   . HOH C 3 .   ? -28.708 -5.650  -15.945 1.00 40.60  ? 501 HOH A O   1 
HETATM 1820 O O   . HOH C 3 .   ? -12.857 -2.908  4.802   1.00 38.24  ? 502 HOH A O   1 
HETATM 1821 O O   . HOH C 3 .   ? -35.590 0.712   4.957   1.00 39.20  ? 503 HOH A O   1 
HETATM 1822 O O   . HOH C 3 .   ? -23.105 -24.471 3.152   1.00 45.67  ? 504 HOH A O   1 
HETATM 1823 O O   . HOH C 3 .   ? -19.779 -22.645 4.214   1.00 26.21  ? 505 HOH A O   1 
HETATM 1824 O O   . HOH C 3 .   ? -21.801 9.235   -13.201 1.00 34.88  ? 506 HOH A O   1 
HETATM 1825 O O   . HOH C 3 .   ? -30.845 17.284  6.388   1.00 44.55  ? 507 HOH A O   1 
HETATM 1826 O O   . HOH C 3 .   ? -20.776 0.433   -17.387 1.00 61.63  ? 508 HOH A O   1 
HETATM 1827 O O   . HOH C 3 .   ? -40.019 -10.659 9.504   1.00 36.28  ? 509 HOH A O   1 
HETATM 1828 O O   . HOH C 3 .   ? -14.492 -21.438 -2.581  1.00 40.73  ? 510 HOH A O   1 
HETATM 1829 O O   . HOH C 3 .   ? -28.550 -4.149  1.110   1.00 21.68  ? 511 HOH A O   1 
HETATM 1830 O O   . HOH C 3 .   ? -26.469 -24.891 -2.299  1.00 44.03  ? 512 HOH A O   1 
HETATM 1831 O O   . HOH C 3 .   ? -28.696 -17.527 -1.271  1.00 25.60  ? 513 HOH A O   1 
HETATM 1832 O O   . HOH C 3 .   ? -26.561 4.789   13.375  1.00 63.86  ? 514 HOH A O   1 
HETATM 1833 O O   . HOH C 3 .   ? -24.890 -7.830  -14.685 1.00 31.00  ? 515 HOH A O   1 
HETATM 1834 O O   . HOH C 3 .   ? -28.894 -9.739  -14.209 1.00 52.06  ? 516 HOH A O   1 
HETATM 1835 O O   . HOH C 3 .   ? -40.056 -8.441  1.695   1.00 54.74  ? 517 HOH A O   1 
HETATM 1836 O O   . HOH C 3 .   ? -19.581 -27.532 8.723   1.00 55.16  ? 518 HOH A O   1 
HETATM 1837 O O   . HOH C 3 .   ? -33.598 -5.406  -10.948 1.00 25.76  ? 519 HOH A O   1 
HETATM 1838 O O   . HOH C 3 .   ? -36.142 -14.331 5.567   1.00 26.11  ? 520 HOH A O   1 
HETATM 1839 O O   . HOH C 3 .   ? -10.935 -6.635  -1.021  1.00 47.86  ? 521 HOH A O   1 
HETATM 1840 O O   . HOH C 3 .   ? -38.711 4.576   -1.701  1.00 63.72  ? 522 HOH A O   1 
HETATM 1841 O O   . HOH C 3 .   ? -30.787 15.557  14.126  1.00 36.37  ? 523 HOH A O   1 
HETATM 1842 O O   . HOH C 3 .   ? -21.597 -7.369  -14.565 1.00 37.95  ? 524 HOH A O   1 
HETATM 1843 O O   . HOH C 3 .   ? -31.854 -4.619  15.508  1.00 42.04  ? 525 HOH A O   1 
HETATM 1844 O O   . HOH C 3 .   ? -20.907 -22.592 -0.143  1.00 35.77  ? 526 HOH A O   1 
HETATM 1845 O O   . HOH C 3 .   ? -37.306 -8.180  2.987   1.00 32.36  ? 527 HOH A O   1 
HETATM 1846 O O   . HOH C 3 .   ? -18.786 5.926   -7.764  1.00 33.08  ? 528 HOH A O   1 
HETATM 1847 O O   . HOH C 3 .   ? -22.860 -3.692  -17.764 1.00 46.93  ? 529 HOH A O   1 
HETATM 1848 O O   . HOH C 3 .   ? -42.880 -3.901  -4.310  1.00 50.61  ? 530 HOH A O   1 
HETATM 1849 O O   . HOH C 3 .   ? -22.249 11.226  -6.733  1.00 62.95  ? 531 HOH A O   1 
HETATM 1850 O O   . HOH C 3 .   ? -36.082 8.308   -17.884 1.00 37.92  ? 532 HOH A O   1 
HETATM 1851 O O   . HOH C 3 .   ? -36.203 -6.221  13.444  1.00 57.01  ? 533 HOH A O   1 
HETATM 1852 O O   . HOH C 3 .   ? -29.625 1.724   8.057   1.00 43.18  ? 534 HOH A O   1 
HETATM 1853 O O   . HOH C 3 .   ? -35.570 -18.113 17.350  1.00 50.21  ? 535 HOH A O   1 
HETATM 1854 O O   . HOH C 3 .   ? -23.888 -20.669 16.724  1.00 47.90  ? 536 HOH A O   1 
HETATM 1855 O O   . HOH C 3 .   ? -20.924 -18.005 -12.717 1.00 35.56  ? 537 HOH A O   1 
HETATM 1856 O O   . HOH C 3 .   ? -22.914 -17.883 20.548  1.00 40.55  ? 538 HOH A O   1 
HETATM 1857 O O   . HOH C 3 .   ? -23.086 -5.384  -16.042 1.00 40.67  ? 539 HOH A O   1 
HETATM 1858 O O   . HOH C 3 .   ? -8.297  1.224   -8.479  1.00 41.05  ? 540 HOH A O   1 
HETATM 1859 O O   . HOH C 3 .   ? -9.418  -13.180 -0.387  1.00 45.11  ? 541 HOH A O   1 
HETATM 1860 O O   . HOH C 3 .   ? -11.198 -2.899  3.072   1.00 65.64  ? 542 HOH A O   1 
HETATM 1861 O O   . HOH C 3 .   ? -28.664 12.635  5.046   1.00 58.47  ? 543 HOH A O   1 
HETATM 1862 O O   . HOH C 3 .   ? -33.999 -8.512  -18.537 1.00 63.23  ? 544 HOH A O   1 
HETATM 1863 O O   . HOH C 3 .   ? -40.826 -17.889 -14.723 1.00 37.55  ? 545 HOH A O   1 
HETATM 1864 O O   . HOH C 3 .   ? -38.208 24.795  -0.288  1.00 58.34  ? 546 HOH A O   1 
HETATM 1865 O O   . HOH C 3 .   ? -26.885 -15.113 -5.390  1.00 59.45  ? 547 HOH A O   1 
HETATM 1866 O O   . HOH C 3 .   ? -36.626 2.617   -19.956 1.00 52.29  ? 548 HOH A O   1 
HETATM 1867 O O   . HOH C 3 .   ? -37.838 2.113   3.631   1.00 39.80  ? 549 HOH A O   1 
HETATM 1868 O O   . HOH C 3 .   ? -31.047 12.520  -11.999 1.00 58.09  ? 550 HOH A O   1 
HETATM 1869 O O   . HOH C 3 .   ? -29.356 -14.845 -8.340  1.00 38.26  ? 551 HOH A O   1 
HETATM 1870 O O   . HOH C 3 .   ? -34.383 10.154  -16.667 1.00 49.92  ? 552 HOH A O   1 
HETATM 1871 O O   . HOH C 3 .   ? -24.223 8.894   -1.806  1.00 31.98  ? 553 HOH A O   1 
HETATM 1872 O O   . HOH C 3 .   ? -8.370  -11.586 1.391   1.00 70.05  ? 554 HOH A O   1 
HETATM 1873 O O   . HOH C 3 .   ? -22.725 -14.169 -13.904 1.00 43.93  ? 555 HOH A O   1 
HETATM 1874 O O   . HOH C 3 .   ? -44.279 -24.748 -5.518  1.00 59.19  ? 556 HOH A O   1 
HETATM 1875 O O   . HOH C 3 .   ? -22.273 9.388   -23.083 1.00 53.30  ? 557 HOH A O   1 
HETATM 1876 O O   . HOH C 3 .   ? -27.472 -3.128  -18.646 1.00 51.77  ? 558 HOH A O   1 
HETATM 1877 O O   . HOH C 3 .   ? -45.746 -4.498  -9.082  1.00 44.45  ? 559 HOH A O   1 
HETATM 1878 O O   . HOH C 3 .   ? -30.122 -7.843  -13.516 1.00 47.28  ? 560 HOH A O   1 
HETATM 1879 O O   . HOH C 3 .   ? -15.602 -22.804 -8.621  1.00 42.76  ? 561 HOH A O   1 
HETATM 1880 O O   . HOH C 3 .   ? -21.800 -21.382 16.104  1.00 53.69  ? 562 HOH A O   1 
HETATM 1881 O O   . HOH C 3 .   ? -10.399 -10.230 -3.028  1.00 56.22  ? 563 HOH A O   1 
HETATM 1882 O O   . HOH C 3 .   ? -32.178 3.006   -18.721 1.00 53.02  ? 564 HOH A O   1 
HETATM 1883 O O   . HOH C 3 .   ? -17.758 -2.467  -14.463 1.00 50.65  ? 565 HOH A O   1 
HETATM 1884 O O   . HOH C 3 .   ? -26.967 -15.873 -2.998  1.00 36.77  ? 566 HOH A O   1 
HETATM 1885 O O   . HOH C 3 .   ? -28.956 10.739  13.552  1.00 55.08  ? 567 HOH A O   1 
HETATM 1886 O O   . HOH C 3 .   ? -29.229 -0.159  19.476  1.00 42.17  ? 568 HOH A O   1 
HETATM 1887 O O   . HOH C 3 .   ? -27.131 -26.274 -5.523  1.00 63.23  ? 569 HOH A O   1 
HETATM 1888 O O   . HOH C 3 .   ? -14.806 -6.049  12.633  1.00 58.55  ? 570 HOH A O   1 
HETATM 1889 O O   . HOH C 3 .   ? -21.270 -15.990 -14.820 1.00 48.46  ? 571 HOH A O   1 
HETATM 1890 O O   . HOH C 3 .   ? -18.633 -16.528 -15.688 1.00 39.29  ? 572 HOH A O   1 
HETATM 1891 O O   . HOH C 3 .   ? -32.972 -4.107  -8.543  1.00 22.12  ? 573 HOH A O   1 
HETATM 1892 O O   . HOH C 3 .   ? -22.811 -30.429 6.277   1.00 69.60  ? 574 HOH A O   1 
HETATM 1893 O O   . HOH C 3 .   ? -26.113 -7.045  -16.913 1.00 54.29  ? 575 HOH A O   1 
HETATM 1894 O O   . HOH C 3 .   ? -27.144 4.032   -19.473 1.00 35.38  ? 576 HOH A O   1 
HETATM 1895 O O   . HOH C 3 .   ? -15.734 -3.081  10.476  1.00 54.71  ? 577 HOH A O   1 
HETATM 1896 O O   . HOH C 3 .   ? -39.880 3.958   -4.250  1.00 55.79  ? 578 HOH A O   1 
HETATM 1897 O O   . HOH C 3 .   ? -35.955 -11.905 16.470  1.00 49.71  ? 579 HOH A O   1 
HETATM 1898 O O   . HOH C 3 .   ? -15.955 10.443  -2.920  1.00 56.30  ? 580 HOH A O   1 
HETATM 1899 O O   . HOH C 3 .   ? -19.015 -12.486 -14.975 1.00 49.21  ? 581 HOH A O   1 
HETATM 1900 O O   . HOH C 3 .   ? -40.168 -13.217 10.844  1.00 42.92  ? 582 HOH A O   1 
HETATM 1901 O O   . HOH C 3 .   ? -21.249 -24.423 1.575   1.00 53.67  ? 583 HOH A O   1 
HETATM 1902 O O   . HOH C 3 .   ? -45.608 -9.794  -16.928 1.00 66.38  ? 584 HOH A O   1 
HETATM 1903 O O   . HOH C 3 .   ? -38.879 -2.198  2.597   1.00 49.80  ? 585 HOH A O   1 
HETATM 1904 O O   . HOH C 3 .   ? -11.224 4.188   -6.795  1.00 62.97  ? 586 HOH A O   1 
HETATM 1905 O O   . HOH C 3 .   ? -28.353 9.968   -5.089  1.00 68.79  ? 587 HOH A O   1 
HETATM 1906 O O   . HOH C 3 .   ? -22.516 8.112   0.041   1.00 46.71  ? 588 HOH A O   1 
HETATM 1907 O O   . HOH C 3 .   ? -30.218 -6.478  16.471  1.00 40.26  ? 589 HOH A O   1 
HETATM 1908 O O   . HOH C 3 .   ? -17.088 -26.899 1.509   1.00 57.89  ? 590 HOH A O   1 
HETATM 1909 O O   . HOH C 3 .   ? -39.607 -8.501  11.494  1.00 58.11  ? 591 HOH A O   1 
HETATM 1910 O O   . HOH C 3 .   ? -19.101 -19.515 -13.988 1.00 54.59  ? 592 HOH A O   1 
HETATM 1911 O O   . HOH C 3 .   ? -33.820 -9.488  16.882  1.00 75.96  ? 593 HOH A O   1 
HETATM 1912 O O   . HOH C 3 .   ? -27.462 -0.594  -18.964 1.00 41.50  ? 594 HOH A O   1 
HETATM 1913 O O   . HOH C 3 .   ? -23.537 -10.326 -14.900 1.00 49.11  ? 595 HOH A O   1 
HETATM 1914 O O   . HOH C 3 .   ? -35.284 -2.427  -19.306 1.00 66.57  ? 596 HOH A O   1 
HETATM 1915 O O   . HOH C 3 .   ? -13.955 -2.038  -10.996 1.00 37.92  ? 597 HOH A O   1 
HETATM 1916 O O   . HOH C 3 .   ? -31.512 -7.438  -11.226 1.00 30.30  ? 598 HOH A O   1 
HETATM 1917 O O   . HOH C 3 .   ? -9.640  -9.091  -4.912  1.00 57.31  ? 599 HOH A O   1 
HETATM 1918 O O   . HOH C 3 .   ? -24.436 11.341  -16.306 1.00 48.08  ? 600 HOH A O   1 
HETATM 1919 O O   . HOH C 3 .   ? -41.546 16.355  8.434   1.00 61.04  ? 601 HOH A O   1 
HETATM 1920 O O   . HOH C 3 .   ? -18.889 -8.054  -14.266 1.00 55.52  ? 602 HOH A O   1 
HETATM 1921 O O   . HOH C 3 .   ? -36.559 -35.491 -0.164  1.00 53.53  ? 603 HOH A O   1 
HETATM 1922 O O   . HOH C 3 .   ? -28.696 -0.067  15.364  1.00 66.43  ? 604 HOH A O   1 
HETATM 1923 O O   . HOH C 3 .   ? -30.838 -2.118  15.521  1.00 60.20  ? 605 HOH A O   1 
HETATM 1924 O O   . HOH C 3 .   ? -12.857 4.984   1.304   1.00 56.15  ? 606 HOH A O   1 
HETATM 1925 O O   . HOH C 3 .   ? -27.388 10.850  1.006   1.00 63.41  ? 607 HOH A O   1 
HETATM 1926 O O   . HOH C 3 .   ? -38.591 5.967   -11.060 1.00 46.07  ? 608 HOH A O   1 
HETATM 1927 O O   . HOH C 3 .   ? -10.701 1.451   4.192   1.00 52.72  ? 609 HOH A O   1 
HETATM 1928 O O   . HOH C 3 .   ? -29.748 -11.531 -12.015 1.00 43.67  ? 610 HOH A O   1 
HETATM 1929 O O   . HOH C 3 .   ? -12.550 2.672   0.342   1.00 48.99  ? 611 HOH A O   1 
HETATM 1930 O O   . HOH C 3 .   ? -42.507 -14.504 9.972   1.00 62.65  ? 612 HOH A O   1 
HETATM 1931 O O   . HOH C 3 .   ? -22.344 11.620  -11.751 1.00 54.94  ? 613 HOH A O   1 
HETATM 1932 O O   . HOH C 3 .   ? -36.944 26.982  1.264   1.00 45.64  ? 614 HOH A O   1 
HETATM 1933 O O   . HOH C 3 .   ? -16.918 -4.693  12.910  1.00 55.58  ? 615 HOH A O   1 
HETATM 1934 O O   . HOH C 3 .   ? -19.090 -22.741 -9.738  1.00 45.60  ? 616 HOH A O   1 
HETATM 1935 O O   . HOH C 3 .   ? -24.470 -12.484 17.405  1.00 48.04  ? 617 HOH A O   1 
HETATM 1936 O O   . HOH C 3 .   ? -37.961 -17.666 15.960  1.00 54.90  ? 618 HOH A O   1 
HETATM 1937 O O   . HOH C 3 .   ? -25.777 12.227  -20.364 1.00 67.69  ? 619 HOH A O   1 
HETATM 1938 O O   . HOH C 3 .   ? -28.069 -26.673 3.390   1.00 59.93  ? 620 HOH A O   1 
HETATM 1939 O O   . HOH C 3 .   ? -8.395  -14.427 -2.607  1.00 50.32  ? 621 HOH A O   1 
HETATM 1940 O O   . HOH C 3 .   ? -37.770 -8.345  13.518  1.00 53.15  ? 622 HOH A O   1 
HETATM 1941 O O   . HOH C 3 .   ? -25.689 -25.234 2.105   1.00 50.62  ? 623 HOH A O   1 
HETATM 1942 O O   . HOH C 3 .   ? -25.783 -11.791 19.565  1.00 58.78  ? 624 HOH A O   1 
HETATM 1943 O O   . HOH C 3 .   ? -28.857 18.058  4.346   1.00 56.50  ? 625 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 1   ? 0.3454 0.5014 0.7640 -0.1048 -0.0504 -0.0146 16  GLY A N   
2    C CA  . GLY A 1   ? 0.4384 0.3138 0.6972 -0.1196 -0.0725 -0.0128 16  GLY A CA  
3    C C   . GLY A 1   ? 0.4708 0.3992 0.5842 -0.0973 -0.1178 -0.0081 16  GLY A C   
4    O O   . GLY A 1   ? 0.4780 0.4238 0.5686 -0.1106 -0.1255 0.0135  16  GLY A O   
5    N N   . ILE A 2   ? 0.4868 0.3247 0.5733 -0.0956 -0.1709 -0.0444 17  ILE A N   
6    C CA  . ILE A 2   ? 0.4496 0.3546 0.5511 -0.0681 -0.1766 -0.0442 17  ILE A CA  
7    C C   . ILE A 2   ? 0.4391 0.3824 0.5967 -0.0388 -0.1227 -0.0430 17  ILE A C   
8    O O   . ILE A 2   ? 0.3505 0.3697 0.6810 -0.0690 -0.1822 -0.0522 17  ILE A O   
9    C CB  . ILE A 2   ? 0.5136 0.4100 0.5820 -0.0281 -0.1377 0.0170  17  ILE A CB  
10   C CG1 . ILE A 2   ? 0.5677 0.4567 0.6739 -0.0379 -0.1693 0.0134  17  ILE A CG1 
11   C CG2 . ILE A 2   ? 0.5082 0.4432 0.5862 -0.0039 -0.1492 0.0167  17  ILE A CG2 
12   C CD1 . ILE A 2   ? 0.6422 0.4838 0.6695 -0.0848 -0.1866 0.0492  17  ILE A CD1 
13   N N   . ASP A 3   ? 0.4221 0.3887 0.5614 -0.0559 -0.1450 -0.0284 18  ASP A N   
14   C CA  . ASP A 3   ? 0.3312 0.4253 0.5349 -0.0661 -0.1561 -0.0217 18  ASP A CA  
15   C C   . ASP A 3   ? 0.3566 0.4065 0.5312 -0.0248 -0.1066 -0.0375 18  ASP A C   
16   O O   . ASP A 3   ? 0.3348 0.4224 0.5111 -0.0898 -0.1235 -0.0201 18  ASP A O   
17   C CB  . ASP A 3   ? 0.3192 0.4853 0.5982 -0.0766 -0.1309 0.0296  18  ASP A CB  
18   C CG  . ASP A 3   ? 0.3078 0.5967 0.5929 -0.0607 -0.0757 -0.0309 18  ASP A CG  
19   O OD1 . ASP A 3   ? 0.3309 0.5995 0.4780 -0.0661 -0.0946 -0.0185 18  ASP A OD1 
20   O OD2 . ASP A 3   ? 0.3725 0.6563 0.7277 -0.1403 0.0528  -0.0477 18  ASP A OD2 
21   N N   . PRO A 4   ? 0.2851 0.3725 0.4345 -0.0285 -0.0902 -0.0547 19  PRO A N   
22   C CA  . PRO A 4   ? 0.2858 0.3816 0.4562 -0.0332 -0.0558 -0.0648 19  PRO A CA  
23   C C   . PRO A 4   ? 0.3298 0.3219 0.3854 -0.0058 -0.0599 -0.0454 19  PRO A C   
24   O O   . PRO A 4   ? 0.3506 0.3876 0.3938 -0.0172 -0.0880 -0.0642 19  PRO A O   
25   C CB  . PRO A 4   ? 0.3495 0.3110 0.4680 -0.0273 -0.0478 -0.0557 19  PRO A CB  
26   C CG  . PRO A 4   ? 0.2933 0.3395 0.4532 -0.0334 -0.0575 -0.0593 19  PRO A CG  
27   C CD  . PRO A 4   ? 0.2997 0.3700 0.4196 -0.0245 -0.0737 -0.0590 19  PRO A CD  
28   N N   . PHE A 5   ? 0.3002 0.4373 0.3969 0.0033  -0.0645 -0.1002 20  PHE A N   
29   C CA  . PHE A 5   ? 0.3298 0.5253 0.4314 0.0329  -0.0938 -0.0868 20  PHE A CA  
30   C C   . PHE A 5   ? 0.3096 0.4716 0.4205 0.0246  -0.0772 -0.0643 20  PHE A C   
31   O O   . PHE A 5   ? 0.3744 0.5010 0.4160 0.0326  -0.0788 -0.0973 20  PHE A O   
32   C CB  . PHE A 5   ? 0.3457 0.6175 0.4807 -0.0130 -0.0671 -0.0752 20  PHE A CB  
33   C CG  . PHE A 5   ? 0.3709 0.7323 0.5131 0.0343  -0.0376 -0.0963 20  PHE A CG  
34   C CD1 . PHE A 5   ? 0.3806 0.8209 0.5758 0.0678  -0.0859 -0.0587 20  PHE A CD1 
35   C CD2 . PHE A 5   ? 0.3717 0.8560 0.5150 0.0086  -0.0640 -0.0921 20  PHE A CD2 
36   C CE1 . PHE A 5   ? 0.3472 0.8745 0.6653 0.1188  -0.0444 -0.0558 20  PHE A CE1 
37   C CE2 . PHE A 5   ? 0.3798 0.8872 0.5089 0.0377  -0.0393 -0.1306 20  PHE A CE2 
38   C CZ  . PHE A 5   ? 0.3127 0.9288 0.5866 0.0681  -0.1221 -0.1046 20  PHE A CZ  
39   N N   . THR A 6   ? 0.2793 0.4146 0.3974 -0.0291 -0.0688 -0.0563 21  THR A N   
40   C CA  . THR A 6   ? 0.2480 0.4662 0.4345 -0.0722 -0.0869 -0.0756 21  THR A CA  
41   C C   . THR A 6   ? 0.2505 0.4364 0.4315 -0.0726 -0.0632 -0.0783 21  THR A C   
42   O O   . THR A 6   ? 0.3188 0.4775 0.4663 -0.0996 -0.1039 -0.0612 21  THR A O   
43   C CB  . THR A 6   ? 0.3023 0.4975 0.4807 -0.0885 -0.0898 -0.0459 21  THR A CB  
44   O OG1 . THR A 6   ? 0.3450 0.4803 0.5139 -0.0521 -0.1023 -0.0608 21  THR A OG1 
45   C CG2 . THR A 6   ? 0.3337 0.5142 0.5190 -0.1432 -0.0533 -0.0415 21  THR A CG2 
46   N N   . TRP A 7   ? 0.2520 0.3903 0.4142 -0.0415 -0.0845 -0.0745 22  TRP A N   
47   C CA  . TRP A 7   ? 0.2571 0.3797 0.4036 -0.0428 -0.0744 -0.0790 22  TRP A CA  
48   C C   . TRP A 7   ? 0.2647 0.4057 0.3645 -0.0323 -0.0686 -0.0745 22  TRP A C   
49   O O   . TRP A 7   ? 0.2823 0.4702 0.3685 0.0034  -0.0792 -0.0708 22  TRP A O   
50   C CB  . TRP A 7   ? 0.2771 0.3670 0.4072 -0.0287 -0.0917 -0.0817 22  TRP A CB  
51   C CG  . TRP A 7   ? 0.2705 0.3704 0.4047 -0.0225 -0.0989 -0.0789 22  TRP A CG  
52   C CD1 . TRP A 7   ? 0.2435 0.3726 0.4797 -0.0341 -0.0914 -0.0742 22  TRP A CD1 
53   C CD2 . TRP A 7   ? 0.2771 0.3356 0.4618 -0.0380 -0.1043 -0.0736 22  TRP A CD2 
54   N NE1 . TRP A 7   ? 0.2837 0.3771 0.4894 -0.0541 -0.0840 -0.0481 22  TRP A NE1 
55   C CE2 . TRP A 7   ? 0.2569 0.3320 0.5400 -0.0319 -0.1153 -0.0606 22  TRP A CE2 
56   C CE3 . TRP A 7   ? 0.2814 0.3093 0.4438 -0.0220 -0.1281 -0.0340 22  TRP A CE3 
57   C CZ2 . TRP A 7   ? 0.2739 0.3819 0.5169 -0.0320 -0.1470 -0.0388 22  TRP A CZ2 
58   C CZ3 . TRP A 7   ? 0.2666 0.3465 0.4716 -0.0298 -0.0995 -0.0310 22  TRP A CZ3 
59   C CH2 . TRP A 7   ? 0.2834 0.3481 0.4946 -0.0019 -0.1801 -0.0453 22  TRP A CH2 
60   N N   . GLY A 8   ? 0.2627 0.3855 0.3678 -0.0280 -0.0772 -0.0993 23  GLY A N   
61   C CA  . GLY A 8   ? 0.2728 0.3736 0.4200 -0.0276 -0.0754 -0.1167 23  GLY A CA  
62   C C   . GLY A 8   ? 0.2466 0.3078 0.4429 -0.0046 -0.0918 -0.0987 23  GLY A C   
63   O O   . GLY A 8   ? 0.2861 0.3400 0.4655 0.0207  -0.1157 -0.1199 23  GLY A O   
64   N N   . PHE A 9   ? 0.2157 0.3496 0.4451 0.0111  -0.0703 -0.0969 24  PHE A N   
65   C CA  . PHE A 9   ? 0.2373 0.3194 0.4200 0.0073  -0.0395 -0.1348 24  PHE A CA  
66   C C   . PHE A 9   ? 0.2669 0.3330 0.4450 0.0190  -0.0589 -0.1419 24  PHE A C   
67   O O   . PHE A 9   ? 0.2265 0.3325 0.3994 -0.0030 -0.0685 -0.1181 24  PHE A O   
68   C CB  . PHE A 9   ? 0.2661 0.3762 0.4302 -0.0341 -0.0706 -0.0970 24  PHE A CB  
69   C CG  . PHE A 9   ? 0.2747 0.4295 0.4445 -0.0144 -0.0527 -0.1497 24  PHE A CG  
70   C CD1 . PHE A 9   ? 0.2956 0.5018 0.4417 -0.0595 -0.0604 -0.2019 24  PHE A CD1 
71   C CD2 . PHE A 9   ? 0.3131 0.3817 0.4511 -0.0583 -0.0722 -0.1397 24  PHE A CD2 
72   C CE1 . PHE A 9   ? 0.3483 0.5138 0.4673 -0.0850 0.0367  -0.1848 24  PHE A CE1 
73   C CE2 . PHE A 9   ? 0.3250 0.4552 0.4649 -0.0718 -0.0313 -0.1874 24  PHE A CE2 
74   C CZ  . PHE A 9   ? 0.3476 0.4867 0.4712 -0.1091 0.0000  -0.1614 24  PHE A CZ  
75   N N   . GLY A 10  ? 0.2505 0.3475 0.4350 0.0319  -0.0409 -0.1575 25  GLY A N   
76   C CA  . GLY A 10  ? 0.2341 0.3542 0.4410 0.0342  -0.0581 -0.1549 25  GLY A CA  
77   C C   . GLY A 10  ? 0.2482 0.3674 0.3714 0.0253  -0.0538 -0.1442 25  GLY A C   
78   O O   . GLY A 10  ? 0.2890 0.3586 0.4137 0.0155  -0.0895 -0.1492 25  GLY A O   
79   N N   . GLY A 11  ? 0.2764 0.3530 0.3983 0.0142  -0.0655 -0.1241 26  GLY A N   
80   C CA  . GLY A 11  ? 0.2495 0.4133 0.4415 -0.0038 -0.0850 -0.1197 26  GLY A CA  
81   C C   . GLY A 11  ? 0.2995 0.3750 0.4588 -0.0037 -0.0553 -0.1405 26  GLY A C   
82   O O   . GLY A 11  ? 0.3633 0.4126 0.5167 -0.0082 0.0116  -0.1090 26  GLY A O   
83   N N   . SER A 12  ? 0.3640 0.4062 0.5103 -0.0183 -0.0242 -0.1414 27  SER A N   
84   C CA  . SER A 12  ? 0.5075 0.4018 0.6370 0.0853  -0.0036 -0.1524 27  SER A CA  
85   C C   . SER A 12  ? 0.5319 0.4889 0.7159 0.0463  -0.0574 -0.1797 27  SER A C   
86   O O   . SER A 12  ? 0.4351 0.5589 1.0073 -0.0488 -0.0747 -0.2148 27  SER A O   
87   C CB  . SER A 12  ? 0.6982 0.4422 0.6078 0.1192  0.0651  -0.1733 27  SER A CB  
88   O OG  . SER A 12  ? 0.8175 0.4827 0.7366 0.1848  0.1544  -0.0898 27  SER A OG  
89   N N   . SER A 13  ? 0.6030 0.4116 0.7841 0.0081  0.0527  -0.2364 28  SER A N   
90   C CA  . SER A 13  ? 0.5994 0.4407 0.7883 -0.0424 0.1158  -0.1128 28  SER A CA  
91   C C   . SER A 13  ? 0.4805 0.4391 0.7351 -0.0202 0.0915  -0.1292 28  SER A C   
92   O O   . SER A 13  ? 0.5209 0.4008 0.7262 -0.0920 0.0462  -0.1351 28  SER A O   
93   C CB  . SER A 13  ? 0.6582 0.3965 0.8663 -0.0617 0.1678  -0.0601 28  SER A CB  
94   O OG  . SER A 13  ? 0.7947 0.5923 0.9051 0.0290  0.1695  0.0387  28  SER A OG  
95   N N   . LYS A 14  ? 0.5101 0.4204 0.6900 0.0494  0.1340  -0.1409 29  LYS A N   
96   C CA  . LYS A 14  ? 0.4420 0.3236 0.7147 0.0212  0.1058  -0.2364 29  LYS A CA  
97   C C   . LYS A 14  ? 0.4891 0.4040 0.7413 0.0830  -0.0042 -0.2194 29  LYS A C   
98   O O   . LYS A 14  ? 0.5124 0.6141 0.7578 0.0977  0.1127  -0.2415 29  LYS A O   
99   C CB  . LYS A 14  ? 0.5412 0.4896 0.7187 0.0191  0.0865  -0.1984 29  LYS A CB  
100  C CG  . LYS A 14  ? 0.6257 0.5362 0.8476 0.0291  0.0199  -0.2239 29  LYS A CG  
101  C CD  . LYS A 14  ? 0.4925 0.5020 0.8729 0.0352  0.0338  -0.3744 29  LYS A CD  
102  C CE  . LYS A 14  ? 0.5140 0.6953 0.8682 0.0109  -0.0064 -0.3961 29  LYS A CE  
103  N NZ  . LYS A 14  ? 0.6370 0.8322 0.8597 0.0382  -0.0496 -0.3743 29  LYS A NZ  
104  N N   . GLU A 15  ? 0.4800 0.3527 0.6330 0.0058  -0.0281 -0.1976 30  GLU A N   
105  C CA  . GLU A 15  ? 0.3760 0.4516 0.5350 0.0193  -0.0107 -0.1633 30  GLU A CA  
106  C C   . GLU A 15  ? 0.3852 0.3943 0.5553 0.0221  0.0504  -0.1311 30  GLU A C   
107  O O   . GLU A 15  ? 0.4869 0.4468 0.6016 0.0704  0.0072  -0.0860 30  GLU A O   
108  C CB  . GLU A 15  ? 0.4012 0.4537 0.4960 0.0320  0.0241  -0.1852 30  GLU A CB  
109  C CG  . GLU A 15  ? 0.4651 0.5384 0.6148 0.0262  0.0060  -0.1134 30  GLU A CG  
110  C CD  . GLU A 15  ? 0.6092 0.5662 0.6470 0.0786  -0.0580 -0.0985 30  GLU A CD  
111  O OE1 . GLU A 15  ? 0.7940 0.4948 0.6417 -0.0583 -0.0579 -0.1257 30  GLU A OE1 
112  O OE2 . GLU A 15  ? 0.8434 0.4907 0.7737 0.0850  -0.0605 -0.1097 30  GLU A OE2 
113  N N   . LYS A 16  ? 0.4352 0.3728 0.5917 0.0515  0.1113  -0.0955 31  LYS A N   
114  C CA  . LYS A 16  ? 0.5496 0.3391 0.5995 0.0206  0.0898  -0.1100 31  LYS A CA  
115  C C   . LYS A 16  ? 0.4899 0.3134 0.5180 0.0252  0.0661  -0.0860 31  LYS A C   
116  O O   . LYS A 16  ? 0.5582 0.3533 0.5719 0.1102  0.0069  -0.0610 31  LYS A O   
117  C CB  . LYS A 16  ? 0.6683 0.4748 0.6427 -0.0115 0.1826  -0.1150 31  LYS A CB  
118  C CG  . LYS A 16  ? 0.8002 0.6110 0.7777 -0.0237 0.1100  -0.1108 31  LYS A CG  
119  C CD  . LYS A 16  ? 0.8853 0.7003 0.8803 0.0444  0.1571  -0.0755 31  LYS A CD  
120  C CE  . LYS A 16  ? 0.9834 0.7399 0.9755 0.0202  0.1091  -0.1176 31  LYS A CE  
121  N NZ  . LYS A 16  ? 0.9993 0.7838 1.0408 0.1057  0.0973  -0.1163 31  LYS A NZ  
122  N N   . PRO A 17  ? 0.4260 0.3225 0.5231 0.0403  0.0841  -0.0819 32  PRO A N   
123  C CA  . PRO A 17  ? 0.4265 0.3404 0.4509 0.0252  0.1459  -0.0554 32  PRO A CA  
124  C C   . PRO A 17  ? 0.4179 0.3694 0.4634 0.0638  0.0903  -0.0506 32  PRO A C   
125  O O   . PRO A 17  ? 0.4344 0.4528 0.5003 0.0160  0.1461  -0.0195 32  PRO A O   
126  C CB  . PRO A 17  ? 0.3680 0.3389 0.5159 0.0440  0.1316  -0.0363 32  PRO A CB  
127  C CG  . PRO A 17  ? 0.4614 0.3796 0.6038 0.0478  0.0842  -0.0217 32  PRO A CG  
128  C CD  . PRO A 17  ? 0.4660 0.3921 0.5253 0.0468  0.0872  -0.0745 32  PRO A CD  
129  N N   . ASN A 18  ? 0.4259 0.3329 0.5124 0.1050  0.0082  -0.0325 33  ASN A N   
130  C CA  . ASN A 18  ? 0.3984 0.3918 0.5239 0.0989  0.0489  -0.0233 33  ASN A CA  
131  C C   . ASN A 18  ? 0.3788 0.3357 0.4640 0.0455  0.0273  0.0131  33  ASN A C   
132  O O   . ASN A 18  ? 0.3932 0.3759 0.5121 0.1380  0.0045  -0.0248 33  ASN A O   
133  C CB  . ASN A 18  ? 0.4913 0.3373 0.5627 0.1359  0.0433  -0.0555 33  ASN A CB  
134  C CG  . ASN A 18  ? 0.5416 0.5524 0.7073 0.0844  -0.0122 -0.0430 33  ASN A CG  
135  O OD1 . ASN A 18  ? 0.5045 0.6666 0.7700 0.1053  0.0486  -0.0189 33  ASN A OD1 
136  N ND2 . ASN A 18  ? 0.5760 0.6490 0.7972 0.1079  -0.0698 -0.0874 33  ASN A ND2 
137  N N   . TYR A 19  ? 0.2957 0.3487 0.4311 0.0510  0.0913  -0.0268 34  TYR A N   
138  C CA  . TYR A 19  ? 0.2941 0.2997 0.3923 0.0736  0.1265  0.0083  34  TYR A CA  
139  C C   . TYR A 19  ? 0.3060 0.3111 0.3653 0.0692  0.0866  -0.0013 34  TYR A C   
140  O O   . TYR A 19  ? 0.3477 0.3628 0.3877 0.0480  0.1127  -0.0317 34  TYR A O   
141  C CB  . TYR A 19  ? 0.3133 0.3127 0.4140 0.1051  0.1144  0.0249  34  TYR A CB  
142  C CG  . TYR A 19  ? 0.3106 0.3424 0.3664 0.0860  0.1046  0.0043  34  TYR A CG  
143  C CD1 . TYR A 19  ? 0.2889 0.4216 0.4105 0.0239  0.0700  0.0599  34  TYR A CD1 
144  C CD2 . TYR A 19  ? 0.3512 0.2496 0.3474 0.0684  0.0661  -0.0256 34  TYR A CD2 
145  C CE1 . TYR A 19  ? 0.2581 0.4631 0.3605 -0.0004 0.0596  0.0149  34  TYR A CE1 
146  C CE2 . TYR A 19  ? 0.3094 0.2678 0.3325 0.0433  0.0495  -0.0460 34  TYR A CE2 
147  C CZ  . TYR A 19  ? 0.2928 0.2536 0.3303 0.0338  0.0400  -0.0404 34  TYR A CZ  
148  O OH  . TYR A 19  ? 0.3132 0.2779 0.4007 0.0383  0.0722  -0.0184 34  TYR A OH  
149  N N   . ASP A 20  ? 0.3056 0.3167 0.3428 0.0673  0.1100  0.0013  35  ASP A N   
150  C CA  . ASP A 20  ? 0.3007 0.2978 0.3888 0.0725  0.1042  -0.0207 35  ASP A CA  
151  C C   . ASP A 20  ? 0.3226 0.2995 0.3599 0.0667  0.1066  -0.0177 35  ASP A C   
152  O O   . ASP A 20  ? 0.3416 0.2994 0.3356 0.0941  0.0871  0.0116  35  ASP A O   
153  C CB  . ASP A 20  ? 0.3068 0.3815 0.4144 0.1358  0.1040  -0.0360 35  ASP A CB  
154  C CG  . ASP A 20  ? 0.3771 0.4299 0.4467 0.1153  0.0746  -0.0568 35  ASP A CG  
155  O OD1 . ASP A 20  ? 0.3446 0.3562 0.4931 0.0865  0.0451  0.0016  35  ASP A OD1 
156  O OD2 . ASP A 20  ? 0.4057 0.5748 0.4928 0.0820  0.0646  -0.0825 35  ASP A OD2 
157  N N   . TYR A 21  ? 0.3285 0.2830 0.3300 0.0498  0.0921  -0.0387 36  TYR A N   
158  C CA  . TYR A 21  ? 0.3034 0.2983 0.3612 0.0344  0.0947  -0.0255 36  TYR A CA  
159  C C   . TYR A 21  ? 0.2986 0.2744 0.3938 0.0294  0.1017  -0.0388 36  TYR A C   
160  O O   . TYR A 21  ? 0.3461 0.2784 0.3859 0.0286  0.1200  -0.0020 36  TYR A O   
161  C CB  . TYR A 21  ? 0.3025 0.3361 0.3826 0.0442  0.0803  -0.0258 36  TYR A CB  
162  C CG  . TYR A 21  ? 0.2974 0.3127 0.3776 0.0336  0.1009  -0.0182 36  TYR A CG  
163  C CD1 . TYR A 21  ? 0.3004 0.2870 0.4028 0.0442  0.0973  -0.0442 36  TYR A CD1 
164  C CD2 . TYR A 21  ? 0.2489 0.3061 0.3626 0.0435  0.0995  -0.0191 36  TYR A CD2 
165  C CE1 . TYR A 21  ? 0.2568 0.3257 0.4037 0.0472  0.0705  -0.0486 36  TYR A CE1 
166  C CE2 . TYR A 21  ? 0.3010 0.2672 0.3368 0.0424  0.0964  -0.0349 36  TYR A CE2 
167  C CZ  . TYR A 21  ? 0.2664 0.2750 0.3702 0.0213  0.0831  -0.0346 36  TYR A CZ  
168  O OH  . TYR A 21  ? 0.3019 0.3307 0.3689 -0.0071 0.0700  -0.0267 36  TYR A OH  
169  N N   . SER A 22  ? 0.3092 0.3039 0.4023 0.0496  0.1010  -0.0202 37  SER A N   
170  C CA  . SER A 22  ? 0.3335 0.2973 0.4287 0.0257  0.1085  -0.0324 37  SER A CA  
171  C C   . SER A 22  ? 0.2987 0.2824 0.3913 -0.0046 0.1014  -0.0202 37  SER A C   
172  O O   . SER A 22  ? 0.3140 0.2837 0.4162 -0.0062 0.1293  -0.0053 37  SER A O   
173  C CB  . SER A 22  ? 0.3728 0.3999 0.4577 -0.0523 0.0465  -0.0303 37  SER A CB  
174  O OG  . SER A 22  ? 0.3874 0.4832 0.4959 0.0944  0.0538  -0.0449 37  SER A OG  
175  N N   . ALA A 23  ? 0.3020 0.2487 0.3871 -0.0052 0.1021  -0.0219 38  ALA A N   
176  C CA  . ALA A 23  ? 0.3087 0.2312 0.4027 -0.0257 0.1029  -0.0193 38  ALA A CA  
177  C C   . ALA A 23  ? 0.3155 0.2593 0.3588 -0.0128 0.1117  0.0017  38  ALA A C   
178  O O   . ALA A 23  ? 0.2862 0.2545 0.4305 0.0109  0.1146  0.0399  38  ALA A O   
179  C CB  . ALA A 23  ? 0.3250 0.2421 0.3918 -0.0010 0.1245  -0.0030 38  ALA A CB  
180  N N   . ASP A 24  ? 0.2880 0.2405 0.3586 0.0033  0.0936  0.0069  39  ASP A N   
181  C CA  . ASP A 24  ? 0.2984 0.2543 0.3556 0.0321  0.0868  -0.0124 39  ASP A CA  
182  C C   . ASP A 24  ? 0.3008 0.3101 0.3665 0.0465  0.0928  0.0128  39  ASP A C   
183  O O   . ASP A 24  ? 0.2880 0.2883 0.4167 0.0117  0.1139  0.0200  39  ASP A O   
184  C CB  . ASP A 24  ? 0.3013 0.2634 0.3647 0.0313  0.0754  -0.0294 39  ASP A CB  
185  C CG  . ASP A 24  ? 0.3273 0.2759 0.3865 0.0142  0.0812  0.0086  39  ASP A CG  
186  O OD1 . ASP A 24  ? 0.3219 0.2990 0.4784 0.0082  0.0887  0.0316  39  ASP A OD1 
187  O OD2 . ASP A 24  ? 0.3512 0.2757 0.3997 0.0105  0.0679  0.0030  39  ASP A OD2 
188  N N   . LYS A 25  ? 0.2910 0.2836 0.3744 0.0216  0.1282  0.0004  40  LYS A N   
189  C CA  . LYS A 25  ? 0.3393 0.3421 0.3753 0.0237  0.1491  -0.0145 40  LYS A CA  
190  C C   . LYS A 25  ? 0.3199 0.3226 0.3574 0.0050  0.1357  0.0244  40  LYS A C   
191  O O   . LYS A 25  ? 0.3013 0.3661 0.4320 0.0042  0.1235  0.0797  40  LYS A O   
192  C CB  . LYS A 25  ? 0.3262 0.3765 0.4222 0.0255  0.1612  -0.0192 40  LYS A CB  
193  C CG  . LYS A 25  ? 0.3730 0.4467 0.4437 0.0145  0.1764  -0.0061 40  LYS A CG  
194  C CD  . LYS A 25  ? 0.4598 0.4843 0.4820 0.0646  0.1454  -0.0618 40  LYS A CD  
195  C CE  . LYS A 25  ? 0.5141 0.6340 0.5764 0.0695  0.1709  -0.0574 40  LYS A CE  
196  N NZ  . LYS A 25  ? 0.6402 0.7265 0.6104 0.0660  0.0893  -0.0870 40  LYS A NZ  
197  N N   . LYS A 26  ? 0.2722 0.3456 0.3890 -0.0159 0.1275  0.0218  41  LYS A N   
198  C CA  . LYS A 26  ? 0.2894 0.3620 0.4445 -0.0434 0.1338  0.0049  41  LYS A CA  
199  C C   . LYS A 26  ? 0.3118 0.2400 0.4389 -0.0702 0.0731  0.0123  41  LYS A C   
200  O O   . LYS A 26  ? 0.3564 0.2695 0.5107 -0.0369 0.1422  0.0454  41  LYS A O   
201  C CB  . LYS A 26  ? 0.3023 0.3621 0.4420 -0.0198 0.1099  0.0037  41  LYS A CB  
202  C CG  . LYS A 26  ? 0.3271 0.4191 0.4671 -0.0227 0.1286  0.0258  41  LYS A CG  
203  C CD  . LYS A 26  ? 0.4026 0.5159 0.5072 -0.0581 0.0922  0.0992  41  LYS A CD  
204  C CE  . LYS A 26  ? 0.4191 0.5440 0.5255 -0.0006 0.1356  0.1786  41  LYS A CE  
205  N NZ  . LYS A 26  ? 0.3348 0.6515 0.6221 0.0038  0.1635  0.2028  41  LYS A NZ  
206  N N   . LEU A 27  ? 0.3350 0.2414 0.4327 -0.0151 0.1314  0.0585  42  LEU A N   
207  C CA  . LEU A 27  ? 0.3325 0.2702 0.4999 -0.0154 0.1418  0.0325  42  LEU A CA  
208  C C   . LEU A 27  ? 0.3486 0.2779 0.4686 -0.0344 0.1250  0.0245  42  LEU A C   
209  O O   . LEU A 27  ? 0.3683 0.2870 0.5604 -0.0528 0.1331  0.0767  42  LEU A O   
210  C CB  . LEU A 27  ? 0.3388 0.2322 0.4859 -0.0009 0.1604  0.0414  42  LEU A CB  
211  C CG  . LEU A 27  ? 0.3533 0.2666 0.5906 0.0224  0.2196  0.0299  42  LEU A CG  
212  C CD1 . LEU A 27  ? 0.4313 0.3672 0.5618 0.0389  0.1562  0.0899  42  LEU A CD1 
213  C CD2 . LEU A 27  ? 0.4166 0.3588 0.6608 0.0038  0.2096  -0.0087 42  LEU A CD2 
214  N N   . ILE A 28  ? 0.3338 0.3489 0.4563 -0.0378 0.1166  0.0324  43  ILE A N   
215  C CA  . ILE A 28  ? 0.3110 0.3955 0.4706 -0.0292 0.1167  0.0365  43  ILE A CA  
216  C C   . ILE A 28  ? 0.3662 0.4390 0.5340 -0.0411 0.1007  0.1207  43  ILE A C   
217  O O   . ILE A 28  ? 0.4095 0.4325 0.5422 -0.0407 0.0989  0.1281  43  ILE A O   
218  C CB  . ILE A 28  ? 0.3516 0.4435 0.4294 -0.0318 0.0933  0.0134  43  ILE A CB  
219  C CG1 . ILE A 28  ? 0.3019 0.4079 0.4625 0.0104  0.0724  0.0292  43  ILE A CG1 
220  C CG2 . ILE A 28  ? 0.4206 0.5611 0.4924 -0.0395 0.1058  -0.0274 43  ILE A CG2 
221  C CD1 . ILE A 28  ? 0.3503 0.3967 0.4709 0.0404  0.0773  0.0227  43  ILE A CD1 
222  N N   . GLU A 29  ? 0.3370 0.4445 0.5172 -0.0602 0.0895  0.1440  44  GLU A N   
223  C CA  . GLU A 29  ? 0.4296 0.4225 0.5150 -0.0460 0.1150  0.1500  44  GLU A CA  
224  C C   . GLU A 29  ? 0.3849 0.4309 0.4962 -0.0409 0.0976  0.1414  44  GLU A C   
225  O O   . GLU A 29  ? 0.4772 0.4137 0.5932 0.0037  0.1225  0.1741  44  GLU A O   
226  C CB  . GLU A 29  ? 0.3785 0.4413 0.5442 -0.0649 0.1141  0.1481  44  GLU A CB  
227  C CG  . GLU A 29  ? 0.4197 0.5126 0.6118 -0.0674 0.1085  0.0809  44  GLU A CG  
228  C CD  . GLU A 29  ? 0.4149 0.5063 0.5994 -0.0171 0.1253  0.0701  44  GLU A CD  
229  O OE1 . GLU A 29  ? 0.3968 0.5311 0.6395 -0.0388 0.0607  0.0081  44  GLU A OE1 
230  O OE2 . GLU A 29  ? 0.5094 0.6342 0.6701 0.0820  0.1806  0.0214  44  GLU A OE2 
231  N N   . ILE A 30  ? 0.3780 0.3371 0.4932 -0.0441 0.1120  0.1235  45  ILE A N   
232  C CA  . ILE A 30  ? 0.4071 0.3142 0.5990 -0.0917 0.0842  0.1023  45  ILE A CA  
233  C C   . ILE A 30  ? 0.4149 0.3047 0.6129 -0.0544 0.1021  0.0902  45  ILE A C   
234  O O   . ILE A 30  ? 0.4447 0.3384 0.7640 0.0013  0.0793  0.0654  45  ILE A O   
235  C CB  . ILE A 30  ? 0.3917 0.3578 0.6243 -0.0913 0.0524  0.1056  45  ILE A CB  
236  C CG1 . ILE A 30  ? 0.4233 0.3670 0.6326 -0.0621 0.0533  0.0717  45  ILE A CG1 
237  C CG2 . ILE A 30  ? 0.4706 0.4597 0.6465 -0.0421 0.0710  0.0634  45  ILE A CG2 
238  C CD1 . ILE A 30  ? 0.4196 0.3740 0.6215 -0.0713 0.0608  0.0276  45  ILE A CD1 
239  N N   . ASN A 31  ? 0.4466 0.3251 0.6674 -0.0150 0.1019  0.1174  46  ASN A N   
240  C CA  . ASN A 31  ? 0.4289 0.3535 0.6886 -0.0220 0.0916  0.1111  46  ASN A CA  
241  C C   . ASN A 31  ? 0.4314 0.4062 0.6806 -0.0186 0.1013  0.1445  46  ASN A C   
242  O O   . ASN A 31  ? 0.4636 0.4197 0.7138 -0.0144 0.0763  0.1315  46  ASN A O   
243  C CB  . ASN A 31  ? 0.3723 0.3418 0.6762 0.0180  0.1212  0.1358  46  ASN A CB  
244  C CG  . ASN A 31  ? 0.4115 0.3489 0.7245 0.0649  0.0874  0.0489  46  ASN A CG  
245  O OD1 . ASN A 31  ? 0.4358 0.4158 0.8320 0.0821  0.1514  -0.0535 46  ASN A OD1 
246  N ND2 . ASN A 31  ? 0.4852 0.4789 0.7799 0.0792  0.0480  0.0779  46  ASN A ND2 
247  N N   . THR A 32  ? 0.4719 0.4771 0.8204 -0.0336 0.0689  0.1229  47  THR A N   
248  C CA  . THR A 32  ? 0.5789 0.4899 0.8893 0.0130  0.0901  0.1513  47  THR A CA  
249  C C   . THR A 32  ? 0.5864 0.4665 1.0784 0.0415  0.0951  0.1144  47  THR A C   
250  O O   . THR A 32  ? 0.6288 0.4634 1.2510 0.0885  0.0591  0.1511  47  THR A O   
251  C CB  . THR A 32  ? 0.6630 0.5297 0.8478 -0.0482 0.0822  0.1108  47  THR A CB  
252  O OG1 . THR A 32  ? 0.7258 0.5628 0.8642 -0.0052 0.1188  0.0525  47  THR A OG1 
253  C CG2 . THR A 32  ? 0.6895 0.5423 0.8078 -0.0142 0.0938  0.1627  47  THR A CG2 
254  N N   . ARG A 33  ? 0.4632 0.3433 1.1426 0.0402  0.1570  0.0269  48  ARG A N   
255  C CA  . ARG A 33  ? 0.4970 0.3902 1.1744 0.0151  0.1734  -0.0075 48  ARG A CA  
256  C C   . ARG A 33  ? 0.3662 0.4620 1.1449 0.0342  0.1811  0.0505  48  ARG A C   
257  O O   . ARG A 33  ? 0.4605 0.3880 1.1341 0.0567  0.1418  0.0844  48  ARG A O   
258  C CB  . ARG A 33  ? 0.7099 0.5648 1.2383 0.0434  0.1431  -0.0382 48  ARG A CB  
259  C CG  . ARG A 33  ? 0.7555 0.7862 1.3217 0.0001  0.2046  -0.0210 48  ARG A CG  
260  C CD  . ARG A 33  ? 0.9815 0.8474 1.4132 0.1085  0.1282  0.0282  48  ARG A CD  
261  N NE  . ARG A 33  ? 1.0472 1.0313 1.4962 0.1526  0.1090  0.0406  48  ARG A NE  
262  C CZ  . ARG A 33  ? 1.1657 1.0430 1.6095 0.1407  0.0360  0.0358  48  ARG A CZ  
263  N NH1 . ARG A 33  ? 1.2363 1.0649 1.6523 0.1011  0.0369  0.0391  48  ARG A NH1 
264  N NH2 . ARG A 33  ? 1.0733 1.0220 1.5847 0.1028  0.0142  0.0250  48  ARG A NH2 
265  N N   . PRO A 34  ? 0.4381 0.3274 1.0508 0.0807  0.0909  0.0961  49  PRO A N   
266  C CA  . PRO A 34  ? 0.4768 0.4090 0.8917 0.0285  0.1057  0.1594  49  PRO A CA  
267  C C   . PRO A 34  ? 0.4956 0.3837 0.7627 -0.0402 0.1009  0.1190  49  PRO A C   
268  O O   . PRO A 34  ? 0.6004 0.4687 0.7473 -0.0583 0.0931  0.0862  49  PRO A O   
269  C CB  . PRO A 34  ? 0.4488 0.4541 0.9349 0.0472  0.0730  0.1535  49  PRO A CB  
270  C CG  . PRO A 34  ? 0.5457 0.4785 1.0339 0.0469  0.0495  0.1370  49  PRO A CG  
271  C CD  . PRO A 34  ? 0.5498 0.3926 1.0834 0.0482  0.0650  0.1448  49  PRO A CD  
272  N N   . ILE A 35  ? 0.3951 0.3689 0.6990 -0.0295 0.0981  0.1037  50  ILE A N   
273  C CA  . ILE A 35  ? 0.4185 0.3680 0.7093 -0.0271 0.0836  0.1271  50  ILE A CA  
274  C C   . ILE A 35  ? 0.4402 0.3395 0.6179 -0.0198 0.1016  0.0550  50  ILE A C   
275  O O   . ILE A 35  ? 0.3869 0.4901 0.5566 0.0054  0.1395  0.0130  50  ILE A O   
276  C CB  . ILE A 35  ? 0.4076 0.3392 0.8097 -0.0651 0.1111  0.1238  50  ILE A CB  
277  C CG1 . ILE A 35  ? 0.4209 0.4233 0.7827 -0.0242 0.0772  0.1046  50  ILE A CG1 
278  C CG2 . ILE A 35  ? 0.3953 0.3425 0.7905 -0.0018 0.1193  0.1667  50  ILE A CG2 
279  C CD1 . ILE A 35  ? 0.4749 0.4378 0.7628 -0.0173 0.0916  0.1463  50  ILE A CD1 
280  N N   . SER A 36  ? 0.5002 0.3957 0.5903 0.0305  0.0615  0.1328  51  SER A N   
281  C CA  . SER A 36  ? 0.5017 0.3151 0.5978 0.0611  0.1453  0.0772  51  SER A CA  
282  C C   . SER A 36  ? 0.3980 0.3401 0.4682 0.0340  0.1132  0.0463  51  SER A C   
283  O O   . SER A 36  ? 0.4307 0.3449 0.4846 0.0222  0.1174  0.0442  51  SER A O   
284  C CB  . SER A 36  ? 0.4817 0.3076 0.6301 0.0419  0.1649  0.0442  51  SER A CB  
285  O OG  . SER A 36  ? 0.4713 0.3834 0.6743 0.0486  0.1901  0.0156  51  SER A OG  
286  N N   . THR A 37  ? 0.3709 0.3615 0.4333 0.0632  0.1350  0.0754  52  THR A N   
287  C CA  . THR A 37  ? 0.3716 0.3377 0.4354 0.0393  0.0861  0.1081  52  THR A CA  
288  C C   . THR A 37  ? 0.3531 0.3419 0.3836 0.0263  0.0746  0.0532  52  THR A C   
289  O O   . THR A 37  ? 0.3327 0.3268 0.4207 0.0465  0.0883  0.0652  52  THR A O   
290  C CB  . THR A 37  ? 0.3550 0.3984 0.4465 0.0657  0.0883  0.1063  52  THR A CB  
291  O OG1 . THR A 37  ? 0.4409 0.4340 0.4577 0.0663  0.0759  0.1100  52  THR A OG1 
292  C CG2 . THR A 37  ? 0.4132 0.4078 0.4477 0.0801  0.1336  0.1181  52  THR A CG2 
293  N N   . ASP A 38  ? 0.3614 0.3661 0.4215 0.0347  0.1150  0.0867  53  ASP A N   
294  C CA  . ASP A 38  ? 0.4167 0.3390 0.4413 0.0436  0.1148  0.0671  53  ASP A CA  
295  C C   . ASP A 38  ? 0.3667 0.3208 0.3883 0.0475  0.0758  0.0612  53  ASP A C   
296  O O   . ASP A 38  ? 0.3641 0.3278 0.3861 0.0584  0.0695  0.0618  53  ASP A O   
297  C CB  . ASP A 38  ? 0.4078 0.3567 0.5137 0.1237  0.1488  0.0565  53  ASP A CB  
298  C CG  . ASP A 38  ? 0.5907 0.4408 0.6114 0.1226  0.1303  0.0819  53  ASP A CG  
299  O OD1 . ASP A 38  ? 0.7702 0.5084 0.6448 0.1116  0.0654  0.1567  53  ASP A OD1 
300  O OD2 . ASP A 38  ? 0.7246 0.4490 0.7551 0.0928  0.0943  0.0921  53  ASP A OD2 
301  N N   . ASN A 39  ? 0.3295 0.2882 0.4100 0.0506  0.0955  0.0317  54  ASN A N   
302  C CA  . ASN A 39  ? 0.3288 0.3114 0.3580 0.0730  0.0943  0.0314  54  ASN A CA  
303  C C   . ASN A 39  ? 0.2773 0.3025 0.3143 0.0461  0.0737  0.0347  54  ASN A C   
304  O O   . ASN A 39  ? 0.2814 0.3173 0.3283 0.0561  0.0765  0.0198  54  ASN A O   
305  C CB  . ASN A 39  ? 0.3638 0.2713 0.3510 0.0587  0.0764  -0.0212 54  ASN A CB  
306  C CG  . ASN A 39  ? 0.3695 0.2660 0.3786 0.0550  0.0640  -0.0080 54  ASN A CG  
307  O OD1 . ASN A 39  ? 0.3600 0.2669 0.3966 0.0491  0.0841  0.0172  54  ASN A OD1 
308  N ND2 . ASN A 39  ? 0.5148 0.3623 0.4433 0.0866  0.1775  0.0105  54  ASN A ND2 
309  N N   . ALA A 40  ? 0.2984 0.3075 0.3406 0.0603  0.1146  0.0363  55  ALA A N   
310  C CA  . ALA A 40  ? 0.3226 0.3147 0.3156 0.0752  0.0896  0.0069  55  ALA A CA  
311  C C   . ALA A 40  ? 0.3458 0.3036 0.2762 0.0486  0.0861  0.0154  55  ALA A C   
312  O O   . ALA A 40  ? 0.2538 0.3371 0.3326 0.0661  0.0424  0.0069  55  ALA A O   
313  C CB  . ALA A 40  ? 0.3392 0.3260 0.3252 0.1070  0.0843  -0.0088 55  ALA A CB  
314  N N   . LYS A 41  ? 0.3311 0.3385 0.3197 0.0578  0.0683  0.0314  56  LYS A N   
315  C CA  . LYS A 41  ? 0.3547 0.3880 0.3014 0.0509  0.0767  0.0724  56  LYS A CA  
316  C C   . LYS A 41  ? 0.3049 0.3598 0.2925 0.0453  0.0522  0.0460  56  LYS A C   
317  O O   . LYS A 41  ? 0.3030 0.3875 0.3506 0.0765  0.0442  0.0442  56  LYS A O   
318  C CB  . LYS A 41  ? 0.3792 0.4366 0.3331 0.0824  0.0826  0.1054  56  LYS A CB  
319  C CG  . LYS A 41  ? 0.4440 0.4807 0.3667 0.0987  0.1205  0.1234  56  LYS A CG  
320  C CD  . LYS A 41  ? 0.4428 0.5292 0.4054 0.0948  0.1213  0.1627  56  LYS A CD  
321  C CE  . LYS A 41  ? 0.5388 0.6573 0.4188 0.0300  0.1289  0.1789  56  LYS A CE  
322  N NZ  . LYS A 41  ? 0.6023 0.7249 0.4966 0.0443  0.0891  0.2029  56  LYS A NZ  
323  N N   . TYR A 42  ? 0.2917 0.3564 0.3308 0.0671  0.0597  0.0442  57  TYR A N   
324  C CA  . TYR A 42  ? 0.2796 0.3710 0.3291 0.0885  0.0558  0.0243  57  TYR A CA  
325  C C   . TYR A 42  ? 0.2432 0.3427 0.3640 0.0904  0.0913  -0.0059 57  TYR A C   
326  O O   . TYR A 42  ? 0.2573 0.3754 0.3496 0.0632  0.0381  0.0278  57  TYR A O   
327  C CB  . TYR A 42  ? 0.3370 0.3277 0.3582 0.1121  0.0860  0.0381  57  TYR A CB  
328  C CG  . TYR A 42  ? 0.3011 0.3671 0.3462 0.1181  0.0817  0.0403  57  TYR A CG  
329  C CD1 . TYR A 42  ? 0.2964 0.3870 0.3194 0.1149  0.0826  0.0732  57  TYR A CD1 
330  C CD2 . TYR A 42  ? 0.3135 0.3281 0.3412 0.0812  0.0561  0.0577  57  TYR A CD2 
331  C CE1 . TYR A 42  ? 0.2502 0.4165 0.3446 0.0916  0.0806  0.0247  57  TYR A CE1 
332  C CE2 . TYR A 42  ? 0.2789 0.3403 0.3183 0.0478  0.0455  0.0485  57  TYR A CE2 
333  C CZ  . TYR A 42  ? 0.2856 0.4084 0.3461 0.0477  0.0700  0.0471  57  TYR A CZ  
334  O OH  . TYR A 42  ? 0.3105 0.4351 0.3507 0.0469  0.0783  0.0318  57  TYR A OH  
335  N N   . TRP A 43  ? 0.2541 0.3318 0.3125 0.0671  0.0564  0.0010  58  TRP A N   
336  C CA  . TRP A 43  ? 0.2519 0.3180 0.2805 0.0458  0.0730  0.0066  58  TRP A CA  
337  C C   . TRP A 43  ? 0.2957 0.3021 0.2419 0.0330  0.0365  0.0125  58  TRP A C   
338  O O   . TRP A 43  ? 0.2920 0.3148 0.3404 0.0045  0.0359  0.0016  58  TRP A O   
339  C CB  . TRP A 43  ? 0.2748 0.3204 0.2702 0.0350  0.0438  0.0253  58  TRP A CB  
340  C CG  . TRP A 43  ? 0.2731 0.3233 0.2805 0.0573  0.0417  0.0146  58  TRP A CG  
341  C CD1 . TRP A 43  ? 0.3022 0.3332 0.2987 0.0399  0.0340  0.0067  58  TRP A CD1 
342  C CD2 . TRP A 43  ? 0.2558 0.3094 0.2660 0.0547  0.0558  0.0045  58  TRP A CD2 
343  N NE1 . TRP A 43  ? 0.3421 0.2794 0.3108 0.0339  0.0284  -0.0166 58  TRP A NE1 
344  C CE2 . TRP A 43  ? 0.3307 0.2978 0.2840 0.0572  0.0606  0.0002  58  TRP A CE2 
345  C CE3 . TRP A 43  ? 0.2579 0.3445 0.2981 0.0547  0.0437  0.0179  58  TRP A CE3 
346  C CZ2 . TRP A 43  ? 0.3083 0.3576 0.2934 0.0858  0.0626  -0.0146 58  TRP A CZ2 
347  C CZ3 . TRP A 43  ? 0.2625 0.4094 0.3316 0.0494  0.0504  0.0230  58  TRP A CZ3 
348  C CH2 . TRP A 43  ? 0.2834 0.4061 0.3568 0.0911  0.0552  -0.0003 58  TRP A CH2 
349  N N   . CYS A 44  ? 0.3147 0.3743 0.2632 0.0668  0.0389  -0.0095 59  CYS A N   
350  C CA  . CYS A 44  ? 0.3145 0.3751 0.3177 0.0820  0.0064  -0.0199 59  CYS A CA  
351  C C   . CYS A 44  ? 0.3252 0.4627 0.3316 0.0425  -0.0028 -0.0031 59  CYS A C   
352  O O   . CYS A 44  ? 0.3518 0.4962 0.4125 0.0471  -0.0402 -0.0112 59  CYS A O   
353  C CB  . CYS A 44  ? 0.3427 0.4850 0.2647 0.0864  -0.0018 -0.0207 59  CYS A CB  
354  S SG  . CYS A 44  ? 0.3754 0.5371 0.3512 0.1035  0.0055  -0.0175 59  CYS A SG  
355  N N   . PHE A 45  ? 0.3463 0.4770 0.3704 0.0730  -0.0411 -0.0361 60  PHE A N   
356  C CA  . PHE A 45  ? 0.3770 0.5788 0.4202 0.1126  -0.0082 -0.0172 60  PHE A CA  
357  C C   . PHE A 45  ? 0.2906 0.4968 0.4288 0.0969  -0.0184 -0.0316 60  PHE A C   
358  O O   . PHE A 45  ? 0.3819 0.6236 0.6385 0.0653  -0.0018 -0.1354 60  PHE A O   
359  C CB  . PHE A 45  ? 0.3889 0.5667 0.3925 0.1515  -0.0011 -0.0043 60  PHE A CB  
360  C CG  . PHE A 45  ? 0.5069 0.6213 0.3448 0.1433  0.0075  0.0069  60  PHE A CG  
361  C CD1 . PHE A 45  ? 0.5826 0.6249 0.4530 0.1363  0.0820  -0.0425 60  PHE A CD1 
362  C CD2 . PHE A 45  ? 0.4449 0.7038 0.4072 0.1407  0.0132  -0.0251 60  PHE A CD2 
363  C CE1 . PHE A 45  ? 0.5848 0.6422 0.4981 0.1229  0.0791  0.0241  60  PHE A CE1 
364  C CE2 . PHE A 45  ? 0.4857 0.7289 0.4212 0.1449  0.0095  -0.0293 60  PHE A CE2 
365  C CZ  . PHE A 45  ? 0.4324 0.7080 0.4959 0.1602  0.0038  0.0301  60  PHE A CZ  
366  N N   . ASP A 46  ? 0.3568 0.4858 0.4254 0.1123  0.0061  0.0136  61  ASP A N   
367  C CA  . ASP A 46  ? 0.3030 0.4496 0.4356 0.1052  0.0211  0.0281  61  ASP A CA  
368  C C   . ASP A 46  ? 0.2736 0.4363 0.4539 0.1317  0.0417  0.0265  61  ASP A C   
369  O O   . ASP A 46  ? 0.2981 0.5381 0.5378 0.0711  0.0503  0.0347  61  ASP A O   
370  C CB  . ASP A 46  ? 0.3645 0.4682 0.5160 0.1697  0.0676  0.0277  61  ASP A CB  
371  C CG  . ASP A 46  ? 0.5202 0.6126 0.6493 0.1388  0.0387  0.0823  61  ASP A CG  
372  O OD1 . ASP A 46  ? 0.5772 0.7424 0.6475 0.0917  -0.0080 0.1677  61  ASP A OD1 
373  O OD2 . ASP A 46  ? 0.6671 0.7174 0.8527 0.1724  0.0975  0.0049  61  ASP A OD2 
374  N N   . LYS A 47  ? 0.2633 0.4573 0.4078 0.1002  0.0307  0.0387  62  LYS A N   
375  C CA  . LYS A 47  ? 0.2616 0.4580 0.3924 0.0758  0.0575  0.0199  62  LYS A CA  
376  C C   . LYS A 47  ? 0.2371 0.4711 0.4265 0.0648  0.0373  0.0000  62  LYS A C   
377  O O   . LYS A 47  ? 0.3735 0.4283 0.5511 0.0076  0.0573  -0.0082 62  LYS A O   
378  C CB  . LYS A 47  ? 0.2783 0.4622 0.3315 0.0863  0.0602  0.0148  62  LYS A CB  
379  C CG  . LYS A 47  ? 0.3543 0.4583 0.3755 0.1134  0.0862  0.0102  62  LYS A CG  
380  C CD  . LYS A 47  ? 0.3521 0.6202 0.4513 0.0994  0.0557  -0.0527 62  LYS A CD  
381  C CE  . LYS A 47  ? 0.3744 0.7142 0.4671 0.0315  0.0610  -0.0820 62  LYS A CE  
382  N NZ  . LYS A 47  ? 0.4063 0.7488 0.4772 0.0124  0.0977  -0.0927 62  LYS A NZ  
383  N N   . GLY A 48  ? 0.2860 0.4318 0.3887 0.0355  0.0009  -0.0101 63  GLY A N   
384  C CA  . GLY A 48  ? 0.2986 0.4548 0.3830 0.0772  -0.0345 -0.0513 63  GLY A CA  
385  C C   . GLY A 48  ? 0.3084 0.4093 0.4048 0.0467  -0.0433 -0.0325 63  GLY A C   
386  O O   . GLY A 48  ? 0.2938 0.4196 0.5703 0.0387  -0.0484 -0.0502 63  GLY A O   
387  N N   . ASN A 49  ? 0.2622 0.3613 0.3689 0.0167  0.0124  -0.0260 64  ASN A N   
388  C CA  . ASN A 49  ? 0.2475 0.3470 0.3536 -0.0056 0.0089  0.0013  64  ASN A CA  
389  C C   . ASN A 49  ? 0.2853 0.3292 0.3321 0.0543  0.0187  0.0257  64  ASN A C   
390  O O   . ASN A 49  ? 0.2798 0.3224 0.3087 0.0266  0.0036  0.0142  64  ASN A O   
391  C CB  . ASN A 49  ? 0.2591 0.3456 0.3373 0.0062  0.0209  -0.0129 64  ASN A CB  
392  C CG  . ASN A 49  ? 0.2183 0.3905 0.3475 0.0257  0.0496  0.0064  64  ASN A CG  
393  O OD1 . ASN A 49  ? 0.2277 0.3833 0.3275 0.0365  0.0621  -0.0286 64  ASN A OD1 
394  N ND2 . ASN A 49  ? 0.2727 0.4967 0.3718 0.0332  0.0399  0.0447  64  ASN A ND2 
395  N N   . ASP A 50  ? 0.2570 0.3349 0.3098 0.0068  0.0051  -0.0085 65  ASP A N   
396  C CA  . ASP A 50  ? 0.2857 0.3513 0.2948 -0.0136 0.0059  -0.0286 65  ASP A CA  
397  C C   . ASP A 50  ? 0.2836 0.2883 0.2624 -0.0030 0.0270  -0.0270 65  ASP A C   
398  O O   . ASP A 50  ? 0.2620 0.3304 0.2611 -0.0016 0.0337  -0.0372 65  ASP A O   
399  C CB  . ASP A 50  ? 0.2871 0.3686 0.3418 -0.0167 0.0061  -0.0698 65  ASP A CB  
400  C CG  . ASP A 50  ? 0.3962 0.5016 0.4465 -0.0426 -0.0650 -0.0431 65  ASP A CG  
401  O OD1 . ASP A 50  ? 0.4636 0.6355 0.4544 0.0293  -0.1365 -0.0894 65  ASP A OD1 
402  O OD2 . ASP A 50  ? 0.5340 0.5261 0.7316 -0.1092 -0.1411 -0.0636 65  ASP A OD2 
403  N N   . LEU A 51  ? 0.2304 0.3045 0.2603 -0.0077 0.0262  -0.0315 66  LEU A N   
404  C CA  . LEU A 51  ? 0.2324 0.2762 0.2692 0.0016  0.0269  -0.0372 66  LEU A CA  
405  C C   . LEU A 51  ? 0.2716 0.2978 0.2721 0.0394  0.0487  -0.0292 66  LEU A C   
406  O O   . LEU A 51  ? 0.2671 0.2833 0.2814 0.0231  0.0472  -0.0129 66  LEU A O   
407  C CB  . LEU A 51  ? 0.2346 0.2658 0.2648 0.0140  0.0346  -0.0385 66  LEU A CB  
408  C CG  . LEU A 51  ? 0.2322 0.2464 0.2684 0.0158  0.0439  -0.0409 66  LEU A CG  
409  C CD1 . LEU A 51  ? 0.2479 0.2493 0.2595 0.0261  0.0484  -0.0298 66  LEU A CD1 
410  C CD2 . LEU A 51  ? 0.2597 0.2692 0.2687 0.0130  0.0275  -0.0459 66  LEU A CD2 
411  N N   . GLY A 52  ? 0.2437 0.2935 0.2720 0.0473  0.0702  0.0009  67  GLY A N   
412  C CA  . GLY A 52  ? 0.2784 0.3088 0.3100 0.0340  0.0518  -0.0086 67  GLY A CA  
413  C C   . GLY A 52  ? 0.2352 0.3156 0.3105 0.0395  0.0280  -0.0065 67  GLY A C   
414  O O   . GLY A 52  ? 0.2563 0.3079 0.3188 0.0366  0.0474  0.0163  67  GLY A O   
415  N N   . CYS A 53  ? 0.2542 0.3392 0.2629 0.0148  0.0468  0.0109  68  CYS A N   
416  C CA  . CYS A 53  ? 0.2960 0.3593 0.2669 0.0281  0.0088  0.0000  68  CYS A CA  
417  C C   . CYS A 53  ? 0.3039 0.3175 0.2695 0.0127  0.0301  -0.0126 68  CYS A C   
418  O O   . CYS A 53  ? 0.2831 0.3259 0.2969 0.0420  0.0316  0.0198  68  CYS A O   
419  C CB  . CYS A 53  ? 0.2826 0.4782 0.2644 -0.0235 0.0204  -0.0066 68  CYS A CB  
420  S SG  . CYS A 53  ? 0.3528 0.5689 0.4153 0.0156  -0.0187 0.0375  68  CYS A SG  
421  N N   . LEU A 54  ? 0.2791 0.3060 0.2532 0.0056  0.0473  -0.0224 69  LEU A N   
422  C CA  . LEU A 54  ? 0.2521 0.2749 0.2600 0.0191  0.0256  -0.0224 69  LEU A CA  
423  C C   . LEU A 54  ? 0.2786 0.2689 0.2456 0.0335  0.0207  -0.0208 69  LEU A C   
424  O O   . LEU A 54  ? 0.2840 0.2796 0.3042 0.0451  0.0675  0.0040  69  LEU A O   
425  C CB  . LEU A 54  ? 0.2671 0.2709 0.2606 0.0029  0.0500  -0.0328 69  LEU A CB  
426  C CG  . LEU A 54  ? 0.2893 0.2699 0.2977 -0.0010 0.0579  -0.0325 69  LEU A CG  
427  C CD1 . LEU A 54  ? 0.2743 0.2659 0.2886 -0.0047 0.0574  -0.0251 69  LEU A CD1 
428  C CD2 . LEU A 54  ? 0.3185 0.2989 0.3066 0.0084  0.0384  -0.0306 69  LEU A CD2 
429  N N   . SER A 55  ? 0.2539 0.2734 0.2650 0.0115  0.0551  -0.0216 70  SER A N   
430  C CA  . SER A 55  ? 0.2240 0.2891 0.2683 0.0262  0.0515  -0.0050 70  SER A CA  
431  C C   . SER A 55  ? 0.2929 0.3164 0.2768 0.0390  0.0446  -0.0087 70  SER A C   
432  O O   . SER A 55  ? 0.2809 0.2550 0.3176 0.0364  0.0535  0.0139  70  SER A O   
433  C CB  . SER A 55  ? 0.2504 0.2681 0.2957 0.0342  0.0561  -0.0211 70  SER A CB  
434  O OG  . SER A 55  ? 0.2621 0.2636 0.2907 0.0203  0.0531  -0.0070 70  SER A OG  
435  N N   . LEU A 56  ? 0.2714 0.3030 0.2793 0.0192  0.0679  0.0297  71  LEU A N   
436  C CA  . LEU A 56  ? 0.3123 0.3214 0.2840 0.0414  0.0565  0.0217  71  LEU A CA  
437  C C   . LEU A 56  ? 0.3323 0.3274 0.2834 0.0301  0.0525  0.0074  71  LEU A C   
438  O O   . LEU A 56  ? 0.3084 0.3308 0.3311 0.0521  0.0822  0.0403  71  LEU A O   
439  C CB  . LEU A 56  ? 0.2930 0.3682 0.3473 0.0775  0.0766  0.0448  71  LEU A CB  
440  C CG  . LEU A 56  ? 0.3299 0.4147 0.3660 0.0781  0.0719  0.0656  71  LEU A CG  
441  C CD1 . LEU A 56  ? 0.3148 0.3712 0.4189 0.1047  0.0739  0.0913  71  LEU A CD1 
442  C CD2 . LEU A 56  ? 0.3744 0.4802 0.3863 0.0690  0.0402  0.0814  71  LEU A CD2 
443  N N   . GLU A 57  ? 0.2885 0.3109 0.2932 0.0269  0.0625  0.0173  72  GLU A N   
444  C CA  . GLU A 57  ? 0.3105 0.3245 0.2584 0.0597  0.0357  0.0227  72  GLU A CA  
445  C C   . GLU A 57  ? 0.3312 0.2775 0.2481 0.0024  0.0519  0.0329  72  GLU A C   
446  O O   . GLU A 57  ? 0.3605 0.3129 0.2903 0.0558  0.0943  0.0662  72  GLU A O   
447  C CB  . GLU A 57  ? 0.3241 0.3255 0.2718 0.0557  0.0394  0.0199  72  GLU A CB  
448  C CG  . GLU A 57  ? 0.4329 0.4266 0.3885 0.1009  0.0261  0.0123  72  GLU A CG  
449  C CD  . GLU A 57  ? 0.4531 0.4585 0.5236 0.0687  0.0517  -0.0125 72  GLU A CD  
450  O OE1 . GLU A 57  ? 0.4169 0.5302 0.6421 0.0721  0.1185  -0.0594 72  GLU A OE1 
451  O OE2 . GLU A 57  ? 0.3369 0.3582 0.3960 0.0591  0.0465  0.0214  72  GLU A OE2 
452  N N   . LYS A 58  ? 0.2845 0.2887 0.2767 0.0440  0.0360  0.0218  73  LYS A N   
453  C CA  . LYS A 58  ? 0.2786 0.2589 0.2918 0.0239  0.0457  -0.0089 73  LYS A CA  
454  C C   . LYS A 58  ? 0.3055 0.2866 0.2955 0.0362  0.0823  -0.0162 73  LYS A C   
455  O O   . LYS A 58  ? 0.2870 0.2842 0.3468 0.0594  0.0890  0.0297  73  LYS A O   
456  C CB  . LYS A 58  ? 0.2925 0.2738 0.2883 0.0249  0.0416  0.0016  73  LYS A CB  
457  C CG  . LYS A 58  ? 0.2978 0.2937 0.3101 0.0164  0.0707  0.0014  73  LYS A CG  
458  C CD  . LYS A 58  ? 0.3109 0.2948 0.3180 0.0344  0.0522  -0.0174 73  LYS A CD  
459  C CE  . LYS A 58  ? 0.3081 0.2653 0.3449 0.0358  0.0611  -0.0062 73  LYS A CE  
460  N NZ  . LYS A 58  ? 0.2783 0.2686 0.3518 0.0000  0.0817  -0.0261 73  LYS A NZ  
461  N N   . LEU A 59  ? 0.2727 0.2664 0.3405 0.0348  0.1082  0.0164  74  LEU A N   
462  C CA  . LEU A 59  ? 0.3045 0.2703 0.3596 0.0054  0.1165  -0.0065 74  LEU A CA  
463  C C   . LEU A 59  ? 0.3163 0.2190 0.3481 0.0457  0.0803  0.0046  74  LEU A C   
464  O O   . LEU A 59  ? 0.3604 0.2692 0.4290 0.0543  0.1233  0.0675  74  LEU A O   
465  C CB  . LEU A 59  ? 0.3172 0.2708 0.3868 0.0187  0.1177  -0.0049 74  LEU A CB  
466  C CG  . LEU A 59  ? 0.3372 0.2628 0.3856 0.0288  0.1076  -0.0275 74  LEU A CG  
467  C CD1 . LEU A 59  ? 0.3522 0.3722 0.4051 0.0519  0.1233  -0.0525 74  LEU A CD1 
468  C CD2 . LEU A 59  ? 0.3625 0.3079 0.4056 0.0041  0.1071  -0.0128 74  LEU A CD2 
469  N N   . GLU A 60  ? 0.3093 0.3064 0.3492 0.0199  0.0991  0.0438  75  GLU A N   
470  C CA  . GLU A 60  ? 0.3421 0.2961 0.3470 0.0151  0.1065  0.0422  75  GLU A CA  
471  C C   . GLU A 60  ? 0.3854 0.3662 0.3523 0.0820  0.1071  0.0952  75  GLU A C   
472  O O   . GLU A 60  ? 0.4317 0.3779 0.3739 0.1097  0.1190  0.1129  75  GLU A O   
473  C CB  . GLU A 60  ? 0.3603 0.4055 0.3772 0.0045  0.1236  0.0885  75  GLU A CB  
474  C CG  . GLU A 60  ? 0.3722 0.4101 0.4006 0.0185  0.1146  0.1339  75  GLU A CG  
475  C CD  . GLU A 60  ? 0.5112 0.5999 0.4487 -0.0303 0.0923  0.1096  75  GLU A CD  
476  O OE1 . GLU A 60  ? 0.6620 0.6829 0.5185 -0.0197 0.0035  0.0868  75  GLU A OE1 
477  O OE2 . GLU A 60  ? 0.5676 0.7463 0.4398 0.0300  -0.0131 0.1076  75  GLU A OE2 
478  N N   . ALA A 61  ? 0.3760 0.3354 0.3622 0.0685  0.1265  0.0863  76  ALA A N   
479  C CA  . ALA A 61  ? 0.3643 0.3951 0.3444 0.0957  0.1147  0.0982  76  ALA A CA  
480  C C   . ALA A 61  ? 0.4045 0.3470 0.3461 0.0743  0.1330  0.0809  76  ALA A C   
481  O O   . ALA A 61  ? 0.4128 0.4113 0.3756 0.0554  0.1560  0.1049  76  ALA A O   
482  C CB  . ALA A 61  ? 0.3526 0.3597 0.4005 0.0881  0.1669  0.0862  76  ALA A CB  
483  N N   . LEU A 62  ? 0.3478 0.3174 0.3998 0.0788  0.1653  0.0870  77  LEU A N   
484  C CA  . LEU A 62  ? 0.3476 0.3153 0.4575 0.0187  0.1550  0.1200  77  LEU A CA  
485  C C   . LEU A 62  ? 0.4288 0.3334 0.5161 0.0416  0.1449  0.1543  77  LEU A C   
486  O O   . LEU A 62  ? 0.4450 0.3853 0.6171 0.0475  0.1915  0.1663  77  LEU A O   
487  C CB  . LEU A 62  ? 0.3545 0.2690 0.4802 0.0062  0.1664  0.0855  77  LEU A CB  
488  C CG  . LEU A 62  ? 0.3351 0.2684 0.4441 -0.0394 0.1473  0.0640  77  LEU A CG  
489  C CD1 . LEU A 62  ? 0.3603 0.2944 0.4765 -0.0479 0.1702  0.0406  77  LEU A CD1 
490  C CD2 . LEU A 62  ? 0.3669 0.3383 0.4274 -0.0248 0.1666  0.0267  77  LEU A CD2 
491  N N   . GLU A 63  ? 0.4479 0.2901 0.5248 0.0599  0.1941  0.1488  78  GLU A N   
492  C CA  . GLU A 63  ? 0.5459 0.3287 0.6111 0.0701  0.1605  0.2016  78  GLU A CA  
493  C C   . GLU A 63  ? 0.5990 0.4404 0.6087 0.0983  0.1619  0.1537  78  GLU A C   
494  O O   . GLU A 63  ? 0.7172 0.5187 0.6884 0.0777  0.2688  0.2071  78  GLU A O   
495  C CB  . GLU A 63  ? 0.5321 0.3307 0.7413 0.1236  0.1673  0.1481  78  GLU A CB  
496  C CG  . GLU A 63  ? 0.5815 0.3909 0.7680 0.1054  0.1698  0.1089  78  GLU A CG  
497  C CD  . GLU A 63  ? 0.6175 0.5897 0.8436 0.1621  0.1284  0.0545  78  GLU A CD  
498  O OE1 . GLU A 63  ? 0.4805 0.5979 0.9081 0.1078  0.0272  0.2121  78  GLU A OE1 
499  O OE2 . GLU A 63  ? 0.6669 0.6862 0.7390 0.1860  0.2502  0.1226  78  GLU A OE2 
500  N N   . SER A 64  ? 0.4719 0.4729 0.4666 0.1185  0.1400  0.1974  79  SER A N   
501  C CA  . SER A 64  ? 0.4486 0.4719 0.4703 0.1145  0.1424  0.1396  79  SER A CA  
502  C C   . SER A 64  ? 0.4562 0.4258 0.5075 0.0743  0.1896  0.1345  79  SER A C   
503  O O   . SER A 64  ? 0.6357 0.4798 0.5458 0.0366  0.2212  0.1488  79  SER A O   
504  C CB  . SER A 64  ? 0.4307 0.5149 0.4859 0.0744  0.0854  0.1710  79  SER A CB  
505  O OG  . SER A 64  ? 0.4095 0.4522 0.4700 0.0737  0.0913  0.1205  79  SER A OG  
506  N N   . LYS A 65  ? 0.4697 0.4371 0.5376 0.0581  0.2087  0.1282  80  LYS A N   
507  C CA  . LYS A 65  ? 0.5003 0.3722 0.5356 -0.0089 0.2031  0.0657  80  LYS A CA  
508  C C   . LYS A 65  ? 0.4216 0.3978 0.5186 -0.0160 0.1241  0.0541  80  LYS A C   
509  O O   . LYS A 65  ? 0.4138 0.4901 0.6267 0.0196  0.1350  0.1004  80  LYS A O   
510  C CB  . LYS A 65  ? 0.5795 0.4208 0.6072 -0.0277 0.2066  0.0784  80  LYS A CB  
511  C CG  . LYS A 65  ? 0.6201 0.4259 0.6952 -0.0808 0.1748  -0.0233 80  LYS A CG  
512  C CD  . LYS A 65  ? 0.7129 0.6073 0.7473 -0.1027 0.1408  -0.0671 80  LYS A CD  
513  C CE  . LYS A 65  ? 0.8183 0.5981 0.8912 -0.1931 0.1255  -0.0996 80  LYS A CE  
514  N NZ  . LYS A 65  ? 0.8779 0.5558 0.9342 -0.2127 0.1752  -0.1586 80  LYS A NZ  
515  N N   . ASP A 66  ? 0.3824 0.4141 0.4901 0.0018  0.1266  0.0858  81  ASP A N   
516  C CA  . ASP A 66  ? 0.3214 0.4580 0.4662 0.0191  0.1003  0.0594  81  ASP A CA  
517  C C   . ASP A 66  ? 0.3509 0.3745 0.4648 0.0092  0.0672  0.0550  81  ASP A C   
518  O O   . ASP A 66  ? 0.3503 0.4005 0.4939 0.0322  0.0702  0.0496  81  ASP A O   
519  C CB  . ASP A 66  ? 0.4320 0.4939 0.5023 0.0046  0.1073  0.0251  81  ASP A CB  
520  C CG  . ASP A 66  ? 0.4993 0.4935 0.5316 0.0081  0.1233  0.0490  81  ASP A CG  
521  O OD1 . ASP A 66  ? 0.5431 0.4944 0.4788 0.0948  0.1187  0.0996  81  ASP A OD1 
522  O OD2 . ASP A 66  ? 0.6069 0.5101 0.6203 0.1146  0.0398  -0.0266 81  ASP A OD2 
523  N N   . LEU A 67  ? 0.3546 0.3824 0.4000 0.0196  0.0824  0.0605  82  LEU A N   
524  C CA  . LEU A 67  ? 0.3331 0.3826 0.3909 0.0291  0.1018  0.0528  82  LEU A CA  
525  C C   . LEU A 67  ? 0.3287 0.3866 0.3768 0.0760  0.1224  0.0247  82  LEU A C   
526  O O   . LEU A 67  ? 0.3147 0.3884 0.3298 0.0165  0.1114  0.0319  82  LEU A O   
527  C CB  . LEU A 67  ? 0.3237 0.4239 0.4338 -0.0013 0.1489  0.0573  82  LEU A CB  
528  C CG  . LEU A 67  ? 0.3270 0.4165 0.4299 0.0069  0.1135  0.0479  82  LEU A CG  
529  C CD1 . LEU A 67  ? 0.3311 0.4248 0.4096 -0.0063 0.1039  0.0630  82  LEU A CD1 
530  C CD2 . LEU A 67  ? 0.3721 0.4758 0.4518 0.0215  0.1099  -0.0059 82  LEU A CD2 
531  N N   . LYS A 68  ? 0.2964 0.4094 0.3738 -0.0079 0.1209  0.0202  83  LYS A N   
532  C CA  . LYS A 68  ? 0.3805 0.4242 0.3940 0.0143  0.1092  -0.0241 83  LYS A CA  
533  C C   . LYS A 68  ? 0.3451 0.3774 0.3270 0.0053  0.1060  -0.0080 83  LYS A C   
534  O O   . LYS A 68  ? 0.3561 0.3742 0.3157 0.0169  0.0658  0.0118  83  LYS A O   
535  C CB  . LYS A 68  ? 0.4458 0.4768 0.3767 -0.0077 0.1107  -0.0041 83  LYS A CB  
536  C CG  . LYS A 68  ? 0.4646 0.5454 0.4650 0.0114  0.0927  0.0072  83  LYS A CG  
537  C CD  . LYS A 68  ? 0.5322 0.6111 0.5157 0.0901  0.1405  -0.0198 83  LYS A CD  
538  C CE  . LYS A 68  ? 0.5991 0.7348 0.6714 0.0573  0.1361  0.0023  83  LYS A CE  
539  N NZ  . LYS A 68  ? 0.7556 0.8118 0.7420 0.0961  0.0680  0.0168  83  LYS A NZ  
540  N N   . LYS A 69  ? 0.3248 0.3964 0.3398 0.0195  0.0830  0.0261  84  LYS A N   
541  C CA  . LYS A 69  ? 0.2780 0.3596 0.3527 0.0072  0.0580  0.0160  84  LYS A CA  
542  C C   . LYS A 69  ? 0.2785 0.3459 0.3622 0.0102  0.0582  0.0223  84  LYS A C   
543  O O   . LYS A 69  ? 0.2961 0.3349 0.3354 0.0284  0.0767  0.0022  84  LYS A O   
544  C CB  . LYS A 69  ? 0.3558 0.4040 0.4125 0.0509  0.0686  0.0459  84  LYS A CB  
545  C CG  . LYS A 69  ? 0.4322 0.4804 0.4611 0.0896  0.0497  0.0806  84  LYS A CG  
546  C CD  . LYS A 69  ? 0.4648 0.5865 0.5992 0.0970  0.0295  0.1134  84  LYS A CD  
547  C CE  . LYS A 69  ? 0.4977 0.7073 0.6351 0.1190  0.0017  0.1651  84  LYS A CE  
548  N NZ  . LYS A 69  ? 0.6255 0.8068 0.7894 0.1185  -0.0130 0.1449  84  LYS A NZ  
549  N N   . VAL A 70  ? 0.2911 0.3104 0.2947 0.0103  0.0736  0.0091  85  VAL A N   
550  C CA  . VAL A 70  ? 0.2900 0.3052 0.3077 0.0107  0.0889  -0.0038 85  VAL A CA  
551  C C   . VAL A 70  ? 0.3236 0.3140 0.2652 0.0281  0.0930  0.0019  85  VAL A C   
552  O O   . VAL A 70  ? 0.2908 0.2769 0.2796 0.0148  0.0819  -0.0055 85  VAL A O   
553  C CB  . VAL A 70  ? 0.2934 0.2761 0.3200 0.0029  0.0786  -0.0117 85  VAL A CB  
554  C CG1 . VAL A 70  ? 0.3328 0.3242 0.3504 -0.0521 0.0870  -0.0082 85  VAL A CG1 
555  C CG2 . VAL A 70  ? 0.3426 0.2938 0.3722 -0.0048 0.1058  0.0078  85  VAL A CG2 
556  N N   . VAL A 71  ? 0.2945 0.3004 0.3106 0.0181  0.0918  -0.0188 86  VAL A N   
557  C CA  . VAL A 71  ? 0.3206 0.3017 0.3070 0.0451  0.0994  -0.0178 86  VAL A CA  
558  C C   . VAL A 71  ? 0.3053 0.3160 0.3314 0.0547  0.1053  -0.0333 86  VAL A C   
559  O O   . VAL A 71  ? 0.3045 0.2895 0.3303 0.0356  0.0830  -0.0204 86  VAL A O   
560  C CB  . VAL A 71  ? 0.3189 0.3151 0.3267 0.0280  0.1264  0.0008  86  VAL A CB  
561  C CG1 . VAL A 71  ? 0.3064 0.3555 0.3800 0.0688  0.1562  -0.0154 86  VAL A CG1 
562  C CG2 . VAL A 71  ? 0.3262 0.3194 0.3455 0.0436  0.0843  0.0126  86  VAL A CG2 
563  N N   . LYS A 72  ? 0.3133 0.3010 0.3059 0.0162  0.0831  -0.0312 87  LYS A N   
564  C CA  . LYS A 72  ? 0.3511 0.3114 0.3023 0.0071  0.0752  -0.0500 87  LYS A CA  
565  C C   . LYS A 72  ? 0.3166 0.2769 0.2950 -0.0074 0.0877  -0.0494 87  LYS A C   
566  O O   . LYS A 72  ? 0.2867 0.2929 0.2987 -0.0172 0.0684  -0.0583 87  LYS A O   
567  C CB  . LYS A 72  ? 0.3903 0.3476 0.2756 -0.0118 0.0720  -0.0355 87  LYS A CB  
568  C CG  . LYS A 72  ? 0.4514 0.4642 0.3646 -0.0664 0.0073  -0.0443 87  LYS A CG  
569  C CD  . LYS A 72  ? 0.5643 0.4825 0.4604 -0.0502 -0.0088 -0.0489 87  LYS A CD  
570  C CE  . LYS A 72  ? 0.6146 0.5880 0.6143 -0.0260 -0.0445 -0.0664 87  LYS A CE  
571  N NZ  . LYS A 72  ? 0.6706 0.5704 0.5652 0.0335  -0.0290 -0.1193 87  LYS A NZ  
572  N N   . PHE A 73  ? 0.3174 0.2787 0.2686 0.0045  0.0626  -0.0434 88  PHE A N   
573  C CA  . PHE A 73  ? 0.2919 0.2729 0.2942 0.0167  0.0658  -0.0406 88  PHE A CA  
574  C C   . PHE A 73  ? 0.2545 0.2307 0.2992 0.0129  0.0569  -0.0402 88  PHE A C   
575  O O   . PHE A 73  ? 0.2846 0.2386 0.2965 -0.0103 0.0553  -0.0275 88  PHE A O   
576  C CB  . PHE A 73  ? 0.2590 0.2712 0.2953 0.0065  0.0769  -0.0404 88  PHE A CB  
577  C CG  . PHE A 73  ? 0.2273 0.2513 0.2794 0.0187  0.0622  -0.0318 88  PHE A CG  
578  C CD1 . PHE A 73  ? 0.2319 0.2818 0.3058 0.0278  0.0605  -0.0409 88  PHE A CD1 
579  C CD2 . PHE A 73  ? 0.2240 0.2593 0.2844 0.0248  0.0586  -0.0150 88  PHE A CD2 
580  C CE1 . PHE A 73  ? 0.2362 0.2870 0.3143 0.0133  0.0663  -0.0186 88  PHE A CE1 
581  C CE2 . PHE A 73  ? 0.2601 0.2935 0.2810 0.0235  0.0588  0.0011  88  PHE A CE2 
582  C CZ  . PHE A 73  ? 0.2500 0.2722 0.2930 0.0412  0.0710  -0.0211 88  PHE A CZ  
583  N N   . TYR A 74  ? 0.2608 0.2672 0.2777 0.0045  0.0707  -0.0403 89  TYR A N   
584  C CA  . TYR A 74  ? 0.2630 0.2586 0.2580 -0.0035 0.0608  -0.0526 89  TYR A CA  
585  C C   . TYR A 74  ? 0.2771 0.2537 0.2896 -0.0026 0.0560  -0.0304 89  TYR A C   
586  O O   . TYR A 74  ? 0.2941 0.2475 0.2935 0.0167  0.0669  -0.0444 89  TYR A O   
587  C CB  . TYR A 74  ? 0.2386 0.2392 0.2932 -0.0020 0.0531  -0.0299 89  TYR A CB  
588  C CG  . TYR A 74  ? 0.2428 0.2480 0.2527 -0.0013 0.0533  -0.0307 89  TYR A CG  
589  C CD1 . TYR A 74  ? 0.2655 0.2418 0.2991 0.0168  0.0837  -0.0235 89  TYR A CD1 
590  C CD2 . TYR A 74  ? 0.2696 0.2415 0.2597 0.0101  0.0829  -0.0242 89  TYR A CD2 
591  C CE1 . TYR A 74  ? 0.2470 0.2372 0.2612 0.0061  0.0743  -0.0143 89  TYR A CE1 
592  C CE2 . TYR A 74  ? 0.2965 0.2288 0.2506 0.0228  0.0793  -0.0158 89  TYR A CE2 
593  C CZ  . TYR A 74  ? 0.2654 0.2310 0.2741 0.0209  0.0850  -0.0227 89  TYR A CZ  
594  O OH  . TYR A 74  ? 0.2633 0.2100 0.3027 0.0136  0.0690  -0.0319 89  TYR A OH  
595  N N   . GLU A 75  ? 0.2971 0.2537 0.3031 0.0047  0.0755  -0.0336 90  GLU A N   
596  C CA  . GLU A 75  ? 0.2945 0.2884 0.3296 0.0114  0.0858  -0.0560 90  GLU A CA  
597  C C   . GLU A 75  ? 0.3225 0.2979 0.3237 0.0085  0.0720  -0.0560 90  GLU A C   
598  O O   . GLU A 75  ? 0.3270 0.2825 0.3533 0.0154  0.0847  -0.0558 90  GLU A O   
599  C CB  . GLU A 75  ? 0.3160 0.2658 0.3407 0.0268  0.0846  -0.0664 90  GLU A CB  
600  C CG  . GLU A 75  ? 0.3099 0.2882 0.3659 0.0177  0.0558  -0.0352 90  GLU A CG  
601  C CD  . GLU A 75  ? 0.3538 0.2853 0.3980 0.0313  0.0926  -0.0579 90  GLU A CD  
602  O OE1 . GLU A 75  ? 0.3627 0.3370 0.4607 0.0333  0.1180  -0.1002 90  GLU A OE1 
603  O OE2 . GLU A 75  ? 0.3294 0.3297 0.4876 0.0296  0.0531  -0.0310 90  GLU A OE2 
604  N N   . LYS A 76  ? 0.3031 0.2688 0.3231 -0.0030 0.0797  -0.0643 91  LYS A N   
605  C CA  . LYS A 76  ? 0.3175 0.2925 0.3627 0.0029  0.0667  -0.0800 91  LYS A CA  
606  C C   . LYS A 76  ? 0.3013 0.2567 0.2914 -0.0109 0.0428  -0.0592 91  LYS A C   
607  O O   . LYS A 76  ? 0.2982 0.2699 0.3242 -0.0334 0.0447  -0.0756 91  LYS A O   
608  C CB  . LYS A 76  ? 0.3381 0.3711 0.3431 0.0199  0.0590  -0.0590 91  LYS A CB  
609  C CG  . LYS A 76  ? 0.4272 0.5090 0.3942 0.0412  0.0750  -0.0911 91  LYS A CG  
610  C CD  . LYS A 76  ? 0.5011 0.6335 0.5361 0.0246  0.1210  -0.1033 91  LYS A CD  
611  C CE  . LYS A 76  ? 0.6823 0.7488 0.4118 0.0064  0.1206  -0.1887 91  LYS A CE  
612  N NZ  . LYS A 76  ? 0.7870 0.8864 0.5724 -0.0117 0.1050  -0.0872 91  LYS A NZ  
613  N N   . THR A 77  ? 0.2964 0.2667 0.2903 -0.0024 0.0421  -0.0645 92  THR A N   
614  C CA  . THR A 77  ? 0.2694 0.2636 0.2996 0.0070  0.0069  -0.0576 92  THR A CA  
615  C C   . THR A 77  ? 0.2682 0.2649 0.2932 -0.0260 0.0241  -0.0457 92  THR A C   
616  O O   . THR A 77  ? 0.2655 0.2682 0.3065 -0.0171 0.0308  -0.0663 92  THR A O   
617  C CB  . THR A 77  ? 0.2908 0.2849 0.3150 0.0097  0.0422  -0.0471 92  THR A CB  
618  O OG1 . THR A 77  ? 0.3283 0.3308 0.3044 0.0038  0.0580  -0.0338 92  THR A OG1 
619  C CG2 . THR A 77  ? 0.2974 0.3229 0.3295 0.0016  0.0449  -0.0602 92  THR A CG2 
620  N N   . ILE A 78  ? 0.2769 0.2510 0.2669 -0.0080 0.0293  -0.0482 93  ILE A N   
621  C CA  . ILE A 78  ? 0.2518 0.2756 0.2843 -0.0134 0.0346  -0.0547 93  ILE A CA  
622  C C   . ILE A 78  ? 0.2654 0.2717 0.2954 -0.0214 0.0491  -0.0684 93  ILE A C   
623  O O   . ILE A 78  ? 0.2821 0.2663 0.2881 -0.0348 0.0413  -0.0812 93  ILE A O   
624  C CB  . ILE A 78  ? 0.2562 0.2600 0.2754 -0.0188 0.0481  -0.0794 93  ILE A CB  
625  C CG1 . ILE A 78  ? 0.2781 0.2784 0.2870 -0.0387 0.0669  -0.0684 93  ILE A CG1 
626  C CG2 . ILE A 78  ? 0.2639 0.2576 0.2731 -0.0103 0.0315  -0.0882 93  ILE A CG2 
627  C CD1 . ILE A 78  ? 0.2707 0.2310 0.3052 -0.0193 0.0403  -0.0817 93  ILE A CD1 
628  N N   . PRO A 79  ? 0.2714 0.2583 0.3042 -0.0177 0.0488  -0.0790 94  PRO A N   
629  C CA  . PRO A 79  ? 0.3015 0.2441 0.3002 -0.0009 0.0473  -0.0803 94  PRO A CA  
630  C C   . PRO A 79  ? 0.3351 0.2448 0.2606 -0.0048 0.0432  -0.0704 94  PRO A C   
631  O O   . PRO A 79  ? 0.3426 0.2502 0.2865 -0.0387 0.0590  -0.0597 94  PRO A O   
632  C CB  . PRO A 79  ? 0.2870 0.2646 0.3554 -0.0144 0.0291  -0.1025 94  PRO A CB  
633  C CG  . PRO A 79  ? 0.3701 0.2841 0.4388 0.0116  0.1004  -0.0456 94  PRO A CG  
634  C CD  . PRO A 79  ? 0.2886 0.2653 0.3365 -0.0180 0.0495  -0.0490 94  PRO A CD  
635  N N   . GLU A 80  ? 0.2864 0.2528 0.2844 -0.0214 0.0233  -0.0629 95  GLU A N   
636  C CA  . GLU A 80  ? 0.2805 0.3082 0.2948 -0.0273 0.0276  -0.0898 95  GLU A CA  
637  C C   . GLU A 80  ? 0.2974 0.3055 0.2912 -0.0475 0.0375  -0.0743 95  GLU A C   
638  O O   . GLU A 80  ? 0.3026 0.3472 0.3623 -0.0854 0.0638  -0.1222 95  GLU A O   
639  C CB  . GLU A 80  ? 0.2825 0.2901 0.3106 -0.0235 0.0322  -0.0717 95  GLU A CB  
640  C CG  . GLU A 80  ? 0.3267 0.2940 0.3230 -0.0346 0.0381  -0.0750 95  GLU A CG  
641  C CD  . GLU A 80  ? 0.3559 0.3333 0.3532 -0.0200 0.0484  -0.0439 95  GLU A CD  
642  O OE1 . GLU A 80  ? 0.4869 0.3874 0.3403 0.0243  0.0435  -0.0365 95  GLU A OE1 
643  O OE2 . GLU A 80  ? 0.3735 0.2843 0.3440 -0.0063 0.0634  -0.0493 95  GLU A OE2 
644  N N   . TYR A 81  ? 0.2727 0.2722 0.2820 -0.0284 0.0105  -0.0622 96  TYR A N   
645  C CA  . TYR A 81  ? 0.2661 0.2819 0.3044 -0.0142 0.0345  -0.0673 96  TYR A CA  
646  C C   . TYR A 81  ? 0.2408 0.2561 0.2580 -0.0433 0.0097  -0.0941 96  TYR A C   
647  O O   . TYR A 81  ? 0.2537 0.3221 0.2937 -0.0385 0.0272  -0.0677 96  TYR A O   
648  C CB  . TYR A 81  ? 0.2275 0.2993 0.2813 0.0043  0.0436  -0.0600 96  TYR A CB  
649  C CG  . TYR A 81  ? 0.2849 0.2996 0.2975 0.0170  0.0088  -0.0678 96  TYR A CG  
650  C CD1 . TYR A 81  ? 0.2631 0.3117 0.3126 0.0289  -0.0039 -0.0334 96  TYR A CD1 
651  C CD2 . TYR A 81  ? 0.2982 0.4023 0.3354 0.0431  0.0184  -0.0600 96  TYR A CD2 
652  C CE1 . TYR A 81  ? 0.3108 0.3327 0.2984 0.0276  0.0151  -0.0120 96  TYR A CE1 
653  C CE2 . TYR A 81  ? 0.2811 0.4332 0.3605 0.0619  0.0102  -0.0339 96  TYR A CE2 
654  C CZ  . TYR A 81  ? 0.3135 0.4199 0.3596 0.0909  -0.0100 0.0024  96  TYR A CZ  
655  O OH  . TYR A 81  ? 0.3906 0.5494 0.3940 0.1233  -0.0322 0.0523  96  TYR A OH  
656  N N   . CYS A 82  ? 0.2519 0.2706 0.2950 -0.0169 -0.0003 -0.0852 97  CYS A N   
657  C CA  . CYS A 82  ? 0.2703 0.2453 0.2646 -0.0283 0.0041  -0.0873 97  CYS A CA  
658  C C   . CYS A 82  ? 0.2358 0.2564 0.2819 -0.0365 0.0117  -0.0616 97  CYS A C   
659  O O   . CYS A 82  ? 0.3037 0.2550 0.3228 -0.0434 0.0569  -0.0871 97  CYS A O   
660  C CB  . CYS A 82  ? 0.3163 0.2662 0.2495 -0.0220 -0.0274 -0.0798 97  CYS A CB  
661  S SG  . CYS A 82  ? 0.2780 0.2422 0.3435 -0.0122 0.0202  -0.0596 97  CYS A SG  
662  N N   . TYR A 83  ? 0.2547 0.2600 0.3144 -0.0427 0.0227  -0.0846 98  TYR A N   
663  C CA  . TYR A 83  ? 0.2812 0.2796 0.2916 -0.0302 0.0203  -0.0619 98  TYR A CA  
664  C C   . TYR A 83  ? 0.2873 0.2778 0.2899 -0.0185 0.0090  -0.0895 98  TYR A C   
665  O O   . TYR A 83  ? 0.2917 0.3421 0.3301 -0.0440 0.0168  -0.0635 98  TYR A O   
666  C CB  . TYR A 83  ? 0.3040 0.2436 0.2759 -0.0240 0.0347  -0.0915 98  TYR A CB  
667  C CG  . TYR A 83  ? 0.3152 0.2467 0.2812 -0.0042 0.0302  -0.0881 98  TYR A CG  
668  C CD1 . TYR A 83  ? 0.3041 0.2466 0.2971 -0.0164 0.0272  -0.0886 98  TYR A CD1 
669  C CD2 . TYR A 83  ? 0.3422 0.2356 0.3214 -0.0396 0.0376  -0.0700 98  TYR A CD2 
670  C CE1 . TYR A 83  ? 0.3223 0.2299 0.3253 -0.0041 0.0446  -0.0730 98  TYR A CE1 
671  C CE2 . TYR A 83  ? 0.3604 0.2629 0.3063 -0.0343 0.0158  -0.0846 98  TYR A CE2 
672  C CZ  . TYR A 83  ? 0.2848 0.2303 0.2913 0.0019  0.0353  -0.0888 98  TYR A CZ  
673  O OH  . TYR A 83  ? 0.3124 0.2954 0.3188 0.0367  0.0056  -0.0762 98  TYR A OH  
674  N N   . ASP A 84  ? 0.2841 0.3169 0.3173 -0.0547 -0.0213 -0.0826 99  ASP A N   
675  C CA  . ASP A 84  ? 0.3191 0.4052 0.3123 -0.0656 -0.0098 -0.0980 99  ASP A CA  
676  C C   . ASP A 84  ? 0.2651 0.4321 0.3394 -0.0831 -0.0194 -0.1290 99  ASP A C   
677  O O   . ASP A 84  ? 0.3061 0.4726 0.4768 -0.1201 -0.0019 -0.1587 99  ASP A O   
678  C CB  . ASP A 84  ? 0.3348 0.3552 0.3098 -0.0699 -0.0086 -0.1012 99  ASP A CB  
679  C CG  . ASP A 84  ? 0.3496 0.2876 0.2482 -0.0374 -0.0090 -0.1106 99  ASP A CG  
680  O OD1 . ASP A 84  ? 0.3637 0.3204 0.3051 -0.0408 -0.0002 -0.0961 99  ASP A OD1 
681  O OD2 . ASP A 84  ? 0.4197 0.3334 0.2945 -0.0511 0.0546  -0.1122 99  ASP A OD2 
682  N N   . LYS A 85  ? 0.2699 0.4143 0.2856 -0.0650 -0.0185 -0.0741 100 LYS A N   
683  C CA  . LYS A 85  ? 0.2731 0.4304 0.3208 -0.0681 -0.0467 -0.0725 100 LYS A CA  
684  C C   . LYS A 85  ? 0.2607 0.3612 0.3161 -0.0620 -0.0231 -0.0434 100 LYS A C   
685  O O   . LYS A 85  ? 0.2797 0.3843 0.3518 -0.0425 -0.0030 -0.0801 100 LYS A O   
686  C CB  . LYS A 85  ? 0.3388 0.4609 0.3798 -0.0237 -0.0165 -0.0196 100 LYS A CB  
687  C CG  . LYS A 85  ? 0.4792 0.5658 0.5629 0.0353  -0.0571 -0.0209 100 LYS A CG  
688  C CD  . LYS A 85  ? 0.6215 0.6067 0.6771 0.0431  -0.1033 0.0067  100 LYS A CD  
689  C CE  . LYS A 85  ? 0.6006 0.5648 0.7197 0.0400  -0.1617 -0.0252 100 LYS A CE  
690  N NZ  . LYS A 85  ? 0.7572 0.5668 0.7169 -0.0018 -0.1412 -0.0209 100 LYS A NZ  
691  N N   . LYS A 86  ? 0.2614 0.3063 0.3001 -0.0461 0.0168  -0.0720 101 LYS A N   
692  C CA  . LYS A 86  ? 0.2451 0.2825 0.3256 -0.0573 0.0233  -0.0807 101 LYS A CA  
693  C C   . LYS A 86  ? 0.2214 0.3047 0.2941 -0.0209 0.0099  -0.0719 101 LYS A C   
694  O O   . LYS A 86  ? 0.2647 0.2958 0.3201 -0.0503 0.0292  -0.0820 101 LYS A O   
695  C CB  . LYS A 86  ? 0.2601 0.2941 0.3525 -0.0478 0.0297  -0.0868 101 LYS A CB  
696  C CG  . LYS A 86  ? 0.2687 0.3102 0.3777 -0.0509 0.0606  -0.1122 101 LYS A CG  
697  C CD  . LYS A 86  ? 0.3329 0.3176 0.4334 -0.0644 0.0874  -0.1075 101 LYS A CD  
698  C CE  . LYS A 86  ? 0.4059 0.3403 0.5206 -0.0597 0.0932  -0.1238 101 LYS A CE  
699  N NZ  . LYS A 86  ? 0.4794 0.4352 0.5889 -0.0851 0.0559  -0.0938 101 LYS A NZ  
700  N N   . PHE A 87  ? 0.2427 0.2860 0.2990 -0.0017 0.0401  -0.0724 102 PHE A N   
701  C CA  . PHE A 87  ? 0.2115 0.2823 0.2949 0.0096  0.0157  -0.0487 102 PHE A CA  
702  C C   . PHE A 87  ? 0.2469 0.2700 0.2582 0.0110  0.0125  -0.0550 102 PHE A C   
703  O O   . PHE A 87  ? 0.2587 0.2643 0.2601 -0.0146 0.0293  -0.0577 102 PHE A O   
704  C CB  . PHE A 87  ? 0.2411 0.2921 0.3116 -0.0200 0.0190  -0.0431 102 PHE A CB  
705  C CG  . PHE A 87  ? 0.2409 0.2821 0.2999 0.0168  0.0156  -0.0237 102 PHE A CG  
706  C CD1 . PHE A 87  ? 0.2300 0.2881 0.3435 -0.0030 0.0233  -0.0652 102 PHE A CD1 
707  C CD2 . PHE A 87  ? 0.2525 0.2907 0.2863 -0.0058 0.0256  -0.0377 102 PHE A CD2 
708  C CE1 . PHE A 87  ? 0.2327 0.2605 0.3258 0.0238  0.0336  -0.0428 102 PHE A CE1 
709  C CE2 . PHE A 87  ? 0.2700 0.3180 0.3069 -0.0038 0.0302  -0.0490 102 PHE A CE2 
710  C CZ  . PHE A 87  ? 0.2566 0.2696 0.3066 -0.0015 0.0294  -0.0673 102 PHE A CZ  
711  N N   . ALA A 88  ? 0.2350 0.2566 0.2630 -0.0095 0.0158  -0.0527 103 ALA A N   
712  C CA  . ALA A 88  ? 0.2540 0.2296 0.2409 -0.0074 -0.0011 -0.0606 103 ALA A CA  
713  C C   . ALA A 88  ? 0.2523 0.2122 0.2674 -0.0094 0.0067  -0.0519 103 ALA A C   
714  O O   . ALA A 88  ? 0.2450 0.2285 0.2830 -0.0019 0.0052  -0.0431 103 ALA A O   
715  C CB  . ALA A 88  ? 0.2657 0.2625 0.2677 -0.0033 0.0099  -0.0457 103 ALA A CB  
716  N N   . PRO A 89  ? 0.2165 0.2506 0.2846 -0.0238 0.0362  -0.0334 104 PRO A N   
717  C CA  . PRO A 89  ? 0.2017 0.2277 0.2854 -0.0098 0.0287  -0.0434 104 PRO A CA  
718  C C   . PRO A 89  ? 0.2381 0.2422 0.2688 -0.0046 0.0293  -0.0419 104 PRO A C   
719  O O   . PRO A 89  ? 0.2450 0.2526 0.2905 -0.0333 0.0306  -0.0786 104 PRO A O   
720  C CB  . PRO A 89  ? 0.2208 0.2628 0.2895 0.0079  0.0428  -0.0628 104 PRO A CB  
721  C CG  . PRO A 89  ? 0.2075 0.2517 0.2864 0.0269  0.0429  -0.0550 104 PRO A CG  
722  C CD  . PRO A 89  ? 0.2020 0.2186 0.2990 -0.0045 0.0253  -0.0564 104 PRO A CD  
723  N N   . ALA A 90  ? 0.2291 0.2227 0.2678 -0.0415 0.0238  -0.0449 105 ALA A N   
724  C CA  . ALA A 90  ? 0.2397 0.2054 0.2399 -0.0307 0.0200  -0.0090 105 ALA A CA  
725  C C   . ALA A 90  ? 0.2632 0.2042 0.2521 0.0002  0.0289  -0.0333 105 ALA A C   
726  O O   . ALA A 90  ? 0.2438 0.2285 0.2503 -0.0100 0.0393  -0.0486 105 ALA A O   
727  C CB  . ALA A 90  ? 0.2411 0.2522 0.2563 -0.0219 0.0116  -0.0198 105 ALA A CB  
728  N N   . CYS A 91  ? 0.2291 0.2097 0.2594 -0.0100 0.0266  -0.0494 106 CYS A N   
729  C CA  . CYS A 91  ? 0.2245 0.1810 0.2804 -0.0055 0.0208  -0.0678 106 CYS A CA  
730  C C   . CYS A 91  ? 0.2105 0.1977 0.2806 0.0072  0.0115  -0.0567 106 CYS A C   
731  O O   . CYS A 91  ? 0.2215 0.1982 0.3354 0.0030  0.0140  -0.0723 106 CYS A O   
732  C CB  . CYS A 91  ? 0.2539 0.2006 0.3186 -0.0018 0.0196  -0.0481 106 CYS A CB  
733  S SG  . CYS A 91  ? 0.2532 0.2296 0.3524 -0.0251 0.0327  -0.0637 106 CYS A SG  
734  N N   . ASN A 92  ? 0.2285 0.2009 0.2564 0.0146  0.0107  -0.0553 107 ASN A N   
735  C CA  . ASN A 92  ? 0.2268 0.2028 0.2651 0.0152  0.0248  -0.0410 107 ASN A CA  
736  C C   . ASN A 92  ? 0.2000 0.2076 0.2478 0.0038  0.0171  -0.0684 107 ASN A C   
737  O O   . ASN A 92  ? 0.2248 0.2072 0.2740 -0.0136 0.0143  -0.0631 107 ASN A O   
738  C CB  . ASN A 92  ? 0.2298 0.1911 0.2803 -0.0068 0.0189  -0.0577 107 ASN A CB  
739  C CG  . ASN A 92  ? 0.2452 0.1884 0.2789 0.0121  0.0150  -0.0227 107 ASN A CG  
740  O OD1 . ASN A 92  ? 0.2849 0.1997 0.2959 0.0393  0.0267  -0.0449 107 ASN A OD1 
741  N ND2 . ASN A 92  ? 0.2783 0.1968 0.2763 0.0208  0.0193  -0.0406 107 ASN A ND2 
742  N N   . ILE A 93  ? 0.2407 0.1775 0.2630 -0.0212 0.0283  -0.0539 108 ILE A N   
743  C CA  . ILE A 93  ? 0.2289 0.1955 0.2677 0.0000  0.0559  -0.0489 108 ILE A CA  
744  C C   . ILE A 93  ? 0.2257 0.1782 0.2938 -0.0130 0.0568  -0.0599 108 ILE A C   
745  O O   . ILE A 93  ? 0.2181 0.1953 0.2922 -0.0045 0.0462  -0.0523 108 ILE A O   
746  C CB  . ILE A 93  ? 0.2356 0.1760 0.2649 0.0003  0.0585  -0.0472 108 ILE A CB  
747  C CG1 . ILE A 93  ? 0.2456 0.2283 0.2595 0.0024  0.0584  -0.0350 108 ILE A CG1 
748  C CG2 . ILE A 93  ? 0.2364 0.2352 0.2790 0.0055  0.0488  -0.0270 108 ILE A CG2 
749  C CD1 . ILE A 93  ? 0.2642 0.2313 0.3019 0.0043  0.0557  -0.0352 108 ILE A CD1 
750  N N   . PRO A 94  ? 0.2076 0.2069 0.2892 -0.0029 0.0513  -0.0779 109 PRO A N   
751  C CA  . PRO A 94  ? 0.2295 0.1919 0.2779 0.0190  0.0537  -0.0311 109 PRO A CA  
752  C C   . PRO A 94  ? 0.2235 0.1903 0.2770 0.0108  0.0367  -0.0616 109 PRO A C   
753  O O   . PRO A 94  ? 0.2099 0.2040 0.3206 -0.0027 0.0427  -0.0463 109 PRO A O   
754  C CB  . PRO A 94  ? 0.2378 0.2203 0.2694 0.0167  0.0394  -0.0577 109 PRO A CB  
755  C CG  . PRO A 94  ? 0.2401 0.2198 0.2888 0.0044  0.0393  -0.0797 109 PRO A CG  
756  C CD  . PRO A 94  ? 0.2297 0.2351 0.2813 -0.0093 0.0269  -0.0650 109 PRO A CD  
757  N N   . ALA A 95  ? 0.2140 0.1904 0.2811 -0.0077 0.0233  -0.0497 110 ALA A N   
758  C CA  . ALA A 95  ? 0.2137 0.2150 0.2981 0.0227  0.0337  -0.0446 110 ALA A CA  
759  C C   . ALA A 95  ? 0.1827 0.2155 0.2828 -0.0141 0.0151  -0.0619 110 ALA A C   
760  O O   . ALA A 95  ? 0.2005 0.2118 0.3352 0.0059  0.0059  -0.0685 110 ALA A O   
761  C CB  . ALA A 95  ? 0.2475 0.1842 0.3216 -0.0025 0.0126  -0.0450 110 ALA A CB  
762  N N   . ILE A 96  ? 0.1964 0.2028 0.2873 -0.0139 0.0264  -0.0489 111 ILE A N   
763  C CA  . ILE A 96  ? 0.2272 0.1830 0.2851 -0.0049 0.0387  -0.0468 111 ILE A CA  
764  C C   . ILE A 96  ? 0.1947 0.2008 0.2755 0.0119  0.0360  -0.0576 111 ILE A C   
765  O O   . ILE A 96  ? 0.2214 0.1944 0.3130 -0.0256 0.0262  -0.0606 111 ILE A O   
766  C CB  . ILE A 96  ? 0.2283 0.1831 0.3069 -0.0145 0.0457  -0.0602 111 ILE A CB  
767  C CG1 . ILE A 96  ? 0.2479 0.1976 0.3306 -0.0315 0.1020  -0.0869 111 ILE A CG1 
768  C CG2 . ILE A 96  ? 0.2240 0.2099 0.3165 0.0000  0.0579  -0.0637 111 ILE A CG2 
769  C CD1 . ILE A 96  ? 0.3280 0.3008 0.3846 -0.0030 0.0818  -0.0348 111 ILE A CD1 
770  N N   . ASP A 97  ? 0.2051 0.1754 0.2825 -0.0097 0.0511  -0.0452 112 ASP A N   
771  C CA  . ASP A 97  ? 0.2063 0.1739 0.3051 0.0025  0.0596  -0.0378 112 ASP A CA  
772  C C   . ASP A 97  ? 0.2051 0.1963 0.3140 -0.0119 0.0679  -0.0656 112 ASP A C   
773  O O   . ASP A 97  ? 0.2183 0.1974 0.3863 -0.0109 0.0605  -0.0660 112 ASP A O   
774  C CB  . ASP A 97  ? 0.2127 0.1777 0.3082 0.0100  0.0435  -0.0471 112 ASP A CB  
775  C CG  . ASP A 97  ? 0.2203 0.2045 0.3069 0.0096  0.0460  -0.0124 112 ASP A CG  
776  O OD1 . ASP A 97  ? 0.2718 0.2651 0.3301 0.0001  0.0533  -0.0322 112 ASP A OD1 
777  O OD2 . ASP A 97  ? 0.2598 0.2507 0.3358 0.0130  0.0642  -0.0361 112 ASP A OD2 
778  N N   . LEU A 98  ? 0.2073 0.1930 0.3253 0.0095  0.0768  -0.0401 113 LEU A N   
779  C CA  . LEU A 98  ? 0.2090 0.1776 0.2931 0.0073  0.0602  -0.0332 113 LEU A CA  
780  C C   . LEU A 98  ? 0.2144 0.1946 0.3141 -0.0118 0.0304  -0.0302 113 LEU A C   
781  O O   . LEU A 98  ? 0.2191 0.2430 0.3623 -0.0047 0.0543  -0.0378 113 LEU A O   
782  C CB  . LEU A 98  ? 0.2559 0.2252 0.3135 0.0031  0.0606  -0.0531 113 LEU A CB  
783  C CG  . LEU A 98  ? 0.2369 0.2546 0.3177 -0.0106 0.0519  -0.0636 113 LEU A CG  
784  C CD1 . LEU A 98  ? 0.2944 0.2824 0.3313 -0.0137 0.0413  -0.0636 113 LEU A CD1 
785  C CD2 . LEU A 98  ? 0.2540 0.2745 0.3430 0.0301  0.0441  -0.0274 113 LEU A CD2 
786  N N   . ILE A 99  ? 0.2118 0.1916 0.2719 -0.0077 0.0274  -0.0330 114 ILE A N   
787  C CA  . ILE A 99  ? 0.2191 0.2094 0.2737 -0.0181 0.0394  -0.0299 114 ILE A CA  
788  C C   . ILE A 99  ? 0.2182 0.1879 0.2782 -0.0011 0.0358  -0.0437 114 ILE A C   
789  O O   . ILE A 99  ? 0.2118 0.2192 0.3358 -0.0222 0.0253  -0.0486 114 ILE A O   
790  C CB  . ILE A 99  ? 0.2594 0.2036 0.3208 0.0157  0.0508  -0.0230 114 ILE A CB  
791  C CG1 . ILE A 99  ? 0.2855 0.2064 0.3536 0.0096  0.0570  -0.0198 114 ILE A CG1 
792  C CG2 . ILE A 99  ? 0.2161 0.2196 0.3450 0.0054  0.0570  -0.0194 114 ILE A CG2 
793  C CD1 . ILE A 99  ? 0.3184 0.2057 0.4119 0.0223  0.0739  -0.0181 114 ILE A CD1 
794  N N   . GLN A 100 ? 0.2118 0.1941 0.3006 -0.0270 0.0381  -0.0435 115 GLN A N   
795  C CA  . GLN A 100 ? 0.2258 0.1783 0.2796 -0.0079 0.0420  -0.0268 115 GLN A CA  
796  C C   . GLN A 100 ? 0.1918 0.1840 0.2765 -0.0142 0.0258  -0.0430 115 GLN A C   
797  O O   . GLN A 100 ? 0.2243 0.2123 0.3105 -0.0263 0.0274  -0.0431 115 GLN A O   
798  C CB  . GLN A 100 ? 0.2278 0.1786 0.2948 -0.0203 0.0274  -0.0410 115 GLN A CB  
799  C CG  . GLN A 100 ? 0.2319 0.2146 0.3114 -0.0219 0.0381  -0.0514 115 GLN A CG  
800  C CD  . GLN A 100 ? 0.2373 0.2460 0.3094 -0.0154 0.0373  -0.0310 115 GLN A CD  
801  O OE1 . GLN A 100 ? 0.2908 0.2052 0.3205 -0.0129 0.0542  -0.0599 115 GLN A OE1 
802  N NE2 . GLN A 100 ? 0.2951 0.2649 0.3235 -0.0528 0.0410  -0.0547 115 GLN A NE2 
803  N N   . GLN A 101 ? 0.2248 0.1875 0.2827 -0.0114 0.0267  -0.0520 116 GLN A N   
804  C CA  . GLN A 101 ? 0.2264 0.1818 0.3087 -0.0217 0.0535  -0.0483 116 GLN A CA  
805  C C   . GLN A 101 ? 0.2381 0.2091 0.2986 -0.0433 0.0625  -0.0536 116 GLN A C   
806  O O   . GLN A 101 ? 0.2418 0.2061 0.3460 -0.0350 0.0376  -0.0484 116 GLN A O   
807  C CB  . GLN A 101 ? 0.2299 0.1909 0.3225 -0.0240 0.0425  -0.0443 116 GLN A CB  
808  C CG  . GLN A 101 ? 0.2590 0.1859 0.3296 -0.0182 0.0481  -0.0394 116 GLN A CG  
809  C CD  . GLN A 101 ? 0.2393 0.2153 0.3419 -0.0167 0.0708  -0.0490 116 GLN A CD  
810  O OE1 . GLN A 101 ? 0.2958 0.1775 0.3948 -0.0069 0.0530  -0.0425 116 GLN A OE1 
811  N NE2 . GLN A 101 ? 0.2735 0.2035 0.3498 0.0069  0.0624  -0.0557 116 GLN A NE2 
812  N N   . LYS A 102 ? 0.2198 0.1986 0.2982 -0.0374 0.0291  -0.0552 117 LYS A N   
813  C CA  . LYS A 102 ? 0.2378 0.2165 0.3369 -0.0311 0.0556  -0.0308 117 LYS A CA  
814  C C   . LYS A 102 ? 0.2214 0.2099 0.2999 -0.0259 0.0481  -0.0370 117 LYS A C   
815  O O   . LYS A 102 ? 0.2369 0.2392 0.3621 -0.0402 0.0440  -0.0661 117 LYS A O   
816  C CB  . LYS A 102 ? 0.2448 0.2336 0.3283 -0.0374 0.0500  -0.0265 117 LYS A CB  
817  C CG  . LYS A 102 ? 0.2368 0.2792 0.3456 -0.0264 0.0497  -0.0425 117 LYS A CG  
818  C CD  . LYS A 102 ? 0.2931 0.3389 0.4010 0.0167  0.0812  -0.0476 117 LYS A CD  
819  C CE  . LYS A 102 ? 0.3426 0.4175 0.5165 0.0170  0.0559  -0.1041 117 LYS A CE  
820  N NZ  . LYS A 102 ? 0.4965 0.4741 0.5672 0.1064  0.0774  -0.0978 117 LYS A NZ  
821  N N   . LEU A 103 ? 0.2338 0.1998 0.3284 -0.0248 0.0308  -0.0322 118 LEU A N   
822  C CA  . LEU A 103 ? 0.2206 0.2375 0.3450 -0.0407 0.0313  -0.0386 118 LEU A CA  
823  C C   . LEU A 103 ? 0.2464 0.2061 0.3189 -0.0434 0.0137  -0.0369 118 LEU A C   
824  O O   . LEU A 103 ? 0.2426 0.2711 0.3736 -0.0528 0.0121  -0.0752 118 LEU A O   
825  C CB  . LEU A 103 ? 0.2260 0.2201 0.3760 -0.0597 0.0181  -0.0559 118 LEU A CB  
826  C CG  . LEU A 103 ? 0.2951 0.2206 0.3963 -0.0318 -0.0074 -0.0610 118 LEU A CG  
827  C CD1 . LEU A 103 ? 0.3741 0.3259 0.4538 -0.0343 -0.0145 -0.0667 118 LEU A CD1 
828  C CD2 . LEU A 103 ? 0.3213 0.2251 0.4026 -0.0258 0.0177  -0.0486 118 LEU A CD2 
829  N N   . SER A 104 ? 0.2585 0.2334 0.3170 -0.0128 0.0177  -0.0403 119 SER A N   
830  C CA  . SER A 104 ? 0.2784 0.2143 0.3516 -0.0259 0.0452  -0.0645 119 SER A CA  
831  C C   . SER A 104 ? 0.2730 0.2361 0.3077 -0.0181 0.0371  -0.0781 119 SER A C   
832  O O   . SER A 104 ? 0.2941 0.2468 0.3684 -0.0496 0.0605  -0.1033 119 SER A O   
833  C CB  . SER A 104 ? 0.2754 0.2090 0.3888 -0.0265 0.0850  -0.0929 119 SER A CB  
834  O OG  . SER A 104 ? 0.3051 0.2638 0.3492 -0.0343 0.0351  -0.0630 119 SER A OG  
835  N N   . TYR A 105 ? 0.2810 0.2300 0.3269 -0.0523 0.0487  -0.0825 120 TYR A N   
836  C CA  . TYR A 105 ? 0.2737 0.2226 0.3735 -0.0176 0.0484  -0.0269 120 TYR A CA  
837  C C   . TYR A 105 ? 0.2409 0.2281 0.3499 -0.0438 0.0540  -0.0611 120 TYR A C   
838  O O   . TYR A 105 ? 0.2772 0.2212 0.4049 -0.0689 0.0407  -0.0827 120 TYR A O   
839  C CB  . TYR A 105 ? 0.2446 0.2354 0.3746 -0.0251 0.0443  -0.0232 120 TYR A CB  
840  C CG  . TYR A 105 ? 0.2564 0.2305 0.3677 -0.0213 0.0915  -0.0264 120 TYR A CG  
841  C CD1 . TYR A 105 ? 0.2741 0.1880 0.4206 -0.0151 0.0903  -0.0459 120 TYR A CD1 
842  C CD2 . TYR A 105 ? 0.3024 0.2363 0.4170 -0.0447 0.0744  -0.0272 120 TYR A CD2 
843  C CE1 . TYR A 105 ? 0.3039 0.2444 0.4785 -0.0356 0.1253  -0.0245 120 TYR A CE1 
844  C CE2 . TYR A 105 ? 0.3272 0.2384 0.4775 -0.0341 0.1145  -0.0253 120 TYR A CE2 
845  C CZ  . TYR A 105 ? 0.3281 0.2246 0.5041 -0.0459 0.1241  -0.0087 120 TYR A CZ  
846  O OH  . TYR A 105 ? 0.3773 0.2722 0.5516 -0.0719 0.1580  0.0417  120 TYR A OH  
847  N N   . TYR A 106 ? 0.2705 0.2379 0.3464 -0.0320 0.0346  -0.0636 121 TYR A N   
848  C CA  . TYR A 106 ? 0.2785 0.2605 0.3581 -0.0444 0.0405  -0.0359 121 TYR A CA  
849  C C   . TYR A 106 ? 0.2749 0.2546 0.3740 -0.0666 0.0496  -0.0606 121 TYR A C   
850  O O   . TYR A 106 ? 0.2753 0.3058 0.4324 -0.0776 0.0570  -0.1076 121 TYR A O   
851  C CB  . TYR A 106 ? 0.2612 0.2801 0.3788 -0.0359 0.0262  -0.0365 121 TYR A CB  
852  C CG  . TYR A 106 ? 0.2735 0.3347 0.3943 -0.0006 0.0337  -0.0612 121 TYR A CG  
853  C CD1 . TYR A 106 ? 0.2215 0.2756 0.3698 -0.0118 0.0405  -0.0604 121 TYR A CD1 
854  C CD2 . TYR A 106 ? 0.3091 0.4253 0.4375 0.0432  0.0278  -0.0546 121 TYR A CD2 
855  C CE1 . TYR A 106 ? 0.2692 0.3382 0.3948 -0.0033 0.0546  -0.0545 121 TYR A CE1 
856  C CE2 . TYR A 106 ? 0.3258 0.5106 0.4501 0.0598  0.0666  -0.0622 121 TYR A CE2 
857  C CZ  . TYR A 106 ? 0.3239 0.4436 0.4161 0.0644  0.0583  -0.0786 121 TYR A CZ  
858  O OH  . TYR A 106 ? 0.4357 0.5499 0.4180 0.0944  0.0932  -0.0500 121 TYR A OH  
859  N N   . VAL A 107 ? 0.2782 0.2924 0.3270 -0.0636 0.0447  -0.0386 122 VAL A N   
860  C CA  . VAL A 107 ? 0.3078 0.3016 0.3444 -0.0676 0.0665  -0.0513 122 VAL A CA  
861  C C   . VAL A 107 ? 0.3142 0.2947 0.3265 -0.0835 0.0209  -0.0736 122 VAL A C   
862  O O   . VAL A 107 ? 0.3368 0.3491 0.3937 -0.1120 0.0144  -0.1325 122 VAL A O   
863  C CB  . VAL A 107 ? 0.3289 0.3395 0.3119 -0.0750 0.0379  -0.0452 122 VAL A CB  
864  C CG1 . VAL A 107 ? 0.3480 0.3645 0.3416 -0.1108 0.0507  -0.0583 122 VAL A CG1 
865  C CG2 . VAL A 107 ? 0.3683 0.3310 0.3541 -0.1088 0.0274  -0.0559 122 VAL A CG2 
866  N N   . ARG A 108 ? 0.2964 0.2718 0.3767 -0.0369 0.0212  -0.1074 123 ARG A N   
867  C CA  . ARG A 108 ? 0.3319 0.2621 0.3922 -0.0036 0.0569  -0.1332 123 ARG A CA  
868  C C   . ARG A 108 ? 0.4044 0.3058 0.4667 -0.0619 0.0541  -0.1195 123 ARG A C   
869  O O   . ARG A 108 ? 0.4597 0.3268 0.5286 -0.0743 0.1148  -0.1612 123 ARG A O   
870  C CB  . ARG A 108 ? 0.3602 0.2454 0.4792 -0.0054 0.0616  -0.0917 123 ARG A CB  
871  C CG  . ARG A 108 ? 0.3683 0.2948 0.4543 -0.0402 0.0676  -0.0879 123 ARG A CG  
872  C CD  . ARG A 108 ? 0.3366 0.2279 0.4341 -0.0233 0.0652  -0.0856 123 ARG A CD  
873  N NE  . ARG A 108 ? 0.3097 0.2708 0.4263 -0.0457 0.0574  -0.0852 123 ARG A NE  
874  C CZ  . ARG A 108 ? 0.3334 0.2650 0.3981 -0.0227 0.0763  -0.0839 123 ARG A CZ  
875  N NH1 . ARG A 108 ? 0.3054 0.2683 0.4146 -0.0054 0.0535  -0.0728 123 ARG A NH1 
876  N NH2 . ARG A 108 ? 0.3169 0.2450 0.4241 -0.0457 0.0642  -0.0748 123 ARG A NH2 
877  N N   . ASN A 109 ? 0.3229 0.2456 0.4676 -0.0837 0.0362  -0.1195 124 ASN A N   
878  C CA  . ASN A 109 ? 0.3464 0.2362 0.4779 -0.0858 0.0285  -0.0850 124 ASN A CA  
879  C C   . ASN A 109 ? 0.3397 0.3831 0.5386 -0.0953 -0.0172 -0.0878 124 ASN A C   
880  O O   . ASN A 109 ? 0.4125 0.3907 0.5612 -0.1518 0.0149  -0.0703 124 ASN A O   
881  C CB  . ASN A 109 ? 0.3506 0.2777 0.4631 -0.0728 0.0718  -0.0813 124 ASN A CB  
882  C CG  . ASN A 109 ? 0.3637 0.2568 0.5057 -0.0170 0.0657  -0.0839 124 ASN A CG  
883  O OD1 . ASN A 109 ? 0.3693 0.3062 0.4907 -0.0605 0.0576  -0.0800 124 ASN A OD1 
884  N ND2 . ASN A 109 ? 0.3362 0.2608 0.5736 -0.0425 0.0403  -0.1128 124 ASN A ND2 
885  N N   . ASP A 110 ? 0.3425 0.3734 0.5297 -0.0798 0.0311  -0.1050 125 ASP A N   
886  C CA  . ASP A 110 ? 0.3443 0.4410 0.5663 -0.0942 0.0167  -0.1054 125 ASP A CA  
887  C C   . ASP A 110 ? 0.2820 0.4812 0.5536 -0.1119 0.0342  -0.0676 125 ASP A C   
888  O O   . ASP A 110 ? 0.2794 0.5992 0.6657 -0.1134 0.0073  0.0089  125 ASP A O   
889  C CB  . ASP A 110 ? 0.4184 0.5117 0.6485 -0.1275 -0.0265 -0.1380 125 ASP A CB  
890  C CG  . ASP A 110 ? 0.5197 0.4519 0.7449 -0.1063 0.0195  -0.1712 125 ASP A CG  
891  O OD1 . ASP A 110 ? 0.6588 0.4896 0.7158 -0.1841 -0.0014 -0.1791 125 ASP A OD1 
892  O OD2 . ASP A 110 ? 0.8058 0.4571 0.9053 -0.1279 0.0411  -0.2161 125 ASP A OD2 
893  N N   . ILE A 111 ? 0.3218 0.4307 0.5280 -0.0228 0.0618  -0.0723 126 ILE A N   
894  C CA  . ILE A 111 ? 0.3198 0.5367 0.5059 0.0051  0.1135  -0.0103 126 ILE A CA  
895  C C   . ILE A 111 ? 0.3535 0.5871 0.5440 0.0602  0.1091  0.0128  126 ILE A C   
896  O O   . ILE A 111 ? 0.3558 0.5348 0.5684 0.0880  0.0959  -0.0028 126 ILE A O   
897  C CB  . ILE A 111 ? 0.4198 0.5873 0.4790 0.0570  0.1315  -0.0224 126 ILE A CB  
898  C CG1 . ILE A 111 ? 0.4500 0.5821 0.5019 0.0724  0.0891  -0.0448 126 ILE A CG1 
899  C CG2 . ILE A 111 ? 0.4133 0.6675 0.5192 0.1297  0.1601  0.0110  126 ILE A CG2 
900  C CD1 . ILE A 111 ? 0.5603 0.5855 0.5842 0.0123  0.0795  -0.0505 126 ILE A CD1 
901  N N   . ASP A 112 ? 0.3706 0.6437 0.6141 0.1018  0.1472  0.0381  127 ASP A N   
902  C CA  . ASP A 112 ? 0.4087 0.6639 0.6199 0.1623  0.1292  0.0516  127 ASP A CA  
903  C C   . ASP A 112 ? 0.3853 0.6635 0.6684 0.1601  0.0867  0.1040  127 ASP A C   
904  O O   . ASP A 112 ? 0.6200 0.6185 0.7070 0.2706  0.1581  0.1205  127 ASP A O   
905  C CB  . ASP A 112 ? 0.4898 0.5386 0.6723 0.1809  0.1264  0.0419  127 ASP A CB  
906  C CG  . ASP A 112 ? 0.6181 0.7288 0.7153 0.1534  0.1729  -0.0308 127 ASP A CG  
907  O OD1 . ASP A 112 ? 0.7559 0.7773 0.8318 0.1405  0.1070  -0.0122 127 ASP A OD1 
908  O OD2 . ASP A 112 ? 0.7840 0.8862 0.8276 0.2065  0.1509  -0.1487 127 ASP A OD2 
909  N N   . ASN A 113 ? 0.4126 0.7964 0.5972 0.1689  -0.0126 0.0879  128 ASN A N   
910  C CA  . ASN A 113 ? 0.4742 0.8221 0.6156 0.1626  0.0246  0.0788  128 ASN A CA  
911  C C   . ASN A 113 ? 0.5115 0.6966 0.5880 0.1802  0.0300  0.1259  128 ASN A C   
912  O O   . ASN A 113 ? 0.5858 0.7995 0.5274 0.1673  0.0303  0.1329  128 ASN A O   
913  C CB  . ASN A 113 ? 0.6137 0.9029 0.7282 0.1842  -0.0162 0.1001  128 ASN A CB  
914  C CG  . ASN A 113 ? 0.6495 0.9857 0.8254 0.1274  -0.0025 0.0880  128 ASN A CG  
915  O OD1 . ASN A 113 ? 0.6802 1.0544 0.7942 0.0929  0.0636  0.1142  128 ASN A OD1 
916  N ND2 . ASN A 113 ? 0.8171 0.9947 0.8936 0.1490  0.0496  0.0283  128 ASN A ND2 
917  N N   . LYS A 114 ? 0.4494 0.6315 0.4693 0.0466  0.0614  0.0515  129 LYS A N   
918  C CA  . LYS A 114 ? 0.4674 0.4650 0.4743 0.0664  0.0832  0.0078  129 LYS A CA  
919  C C   . LYS A 114 ? 0.4209 0.3712 0.4284 0.0519  0.0525  -0.0211 129 LYS A C   
920  O O   . LYS A 114 ? 0.4225 0.4060 0.5230 0.0007  0.0037  -0.0093 129 LYS A O   
921  C CB  . LYS A 114 ? 0.5053 0.3998 0.4724 0.0862  0.0749  0.0246  129 LYS A CB  
922  C CG  . LYS A 114 ? 0.5705 0.3961 0.5254 0.1037  0.1010  0.0196  129 LYS A CG  
923  C CD  . LYS A 114 ? 0.6223 0.4458 0.5924 0.1312  0.1326  0.0310  129 LYS A CD  
924  C CE  . LYS A 114 ? 0.6315 0.4679 0.7215 0.1555  0.1351  -0.0173 129 LYS A CE  
925  N NZ  . LYS A 114 ? 0.7118 0.5384 0.8482 0.0734  0.1012  0.0027  129 LYS A NZ  
926  N N   . THR A 115 ? 0.4912 0.3587 0.3749 0.0035  0.0279  -0.0427 130 THR A N   
927  C CA  . THR A 115 ? 0.3731 0.3519 0.4255 0.0075  0.0140  -0.0814 130 THR A CA  
928  C C   . THR A 115 ? 0.4463 0.3892 0.3452 -0.0141 -0.0038 -0.1002 130 THR A C   
929  O O   . THR A 115 ? 0.4710 0.3288 0.3807 -0.0350 -0.0353 -0.1029 130 THR A O   
930  C CB  . THR A 115 ? 0.4459 0.4420 0.5028 -0.0210 -0.0340 -0.0824 130 THR A CB  
931  O OG1 . THR A 115 ? 0.4892 0.4833 0.4865 -0.0530 -0.0658 -0.0493 130 THR A OG1 
932  C CG2 . THR A 115 ? 0.4137 0.4681 0.5729 0.0255  -0.0466 -0.1032 130 THR A CG2 
933  N N   . ILE A 116 ? 0.4204 0.3425 0.3522 -0.0170 -0.0132 -0.1278 131 ILE A N   
934  C CA  . ILE A 116 ? 0.4542 0.3972 0.4355 -0.0425 0.0023  -0.0967 131 ILE A CA  
935  C C   . ILE A 116 ? 0.4104 0.3914 0.4403 -0.0273 0.0122  -0.1058 131 ILE A C   
936  O O   . ILE A 116 ? 0.4748 0.4282 0.4358 -0.1148 0.0137  -0.0627 131 ILE A O   
937  C CB  . ILE A 116 ? 0.5223 0.4551 0.4570 0.0039  0.0144  -0.1497 131 ILE A CB  
938  C CG1 . ILE A 116 ? 0.5591 0.4304 0.4934 0.0410  0.0020  -0.1240 131 ILE A CG1 
939  C CG2 . ILE A 116 ? 0.6493 0.4714 0.5109 0.0137  0.0188  -0.1128 131 ILE A CG2 
940  C CD1 . ILE A 116 ? 0.6812 0.5359 0.6212 0.0302  0.0434  -0.0969 131 ILE A CD1 
941  N N   . LYS A 117 ? 0.4114 0.4465 0.4191 -0.0358 -0.0094 -0.0916 132 LYS A N   
942  C CA  . LYS A 117 ? 0.4298 0.4686 0.4221 -0.0442 -0.0068 -0.0675 132 LYS A CA  
943  C C   . LYS A 117 ? 0.4002 0.4247 0.4744 -0.0659 -0.0579 -0.0780 132 LYS A C   
944  O O   . LYS A 117 ? 0.5175 0.4667 0.5341 -0.0930 -0.0150 0.0157  132 LYS A O   
945  C CB  . LYS A 117 ? 0.5355 0.5176 0.4560 -0.0581 -0.1245 -0.0699 132 LYS A CB  
946  C CG  . LYS A 117 ? 0.6845 0.6059 0.6037 -0.0324 -0.1382 -0.0623 132 LYS A CG  
947  C CD  . LYS A 117 ? 0.7420 0.7567 0.6387 -0.0232 -0.2033 -0.0115 132 LYS A CD  
948  C CE  . LYS A 117 ? 0.8106 0.7738 0.7977 -0.0051 -0.1190 0.0538  132 LYS A CE  
949  N NZ  . LYS A 117 ? 0.9560 0.8490 0.7905 0.0259  -0.1000 0.0919  132 LYS A NZ  
950  N N   . THR A 118 ? 0.3484 0.3941 0.4315 -0.0251 -0.0899 -0.0784 133 THR A N   
951  C CA  . THR A 118 ? 0.3801 0.4318 0.4683 -0.0282 -0.0740 -0.1321 133 THR A CA  
952  C C   . THR A 118 ? 0.3197 0.3276 0.4520 -0.0005 -0.0736 -0.0712 133 THR A C   
953  O O   . THR A 118 ? 0.3020 0.3287 0.4846 -0.0145 -0.0599 -0.0987 133 THR A O   
954  C CB  . THR A 118 ? 0.2908 0.5620 0.5330 -0.0187 -0.0829 -0.2051 133 THR A CB  
955  O OG1 . THR A 118 ? 0.3301 0.6198 0.5831 -0.1074 -0.0184 -0.2572 133 THR A OG1 
956  C CG2 . THR A 118 ? 0.3865 0.6678 0.6263 -0.0229 -0.1304 -0.1824 133 THR A CG2 
957  N N   . PHE A 119 ? 0.2762 0.2981 0.4196 -0.0342 -0.0715 -0.0601 134 PHE A N   
958  C CA  . PHE A 119 ? 0.2880 0.3120 0.3662 -0.0396 -0.0227 -0.0504 134 PHE A CA  
959  C C   . PHE A 119 ? 0.2563 0.2990 0.3331 -0.0355 -0.0200 -0.0383 134 PHE A C   
960  O O   . PHE A 119 ? 0.2625 0.2849 0.3556 -0.0273 -0.0194 -0.0437 134 PHE A O   
961  C CB  . PHE A 119 ? 0.2498 0.2705 0.3526 -0.0548 0.0026  -0.0547 134 PHE A CB  
962  C CG  . PHE A 119 ? 0.2722 0.2705 0.3278 -0.0266 0.0235  -0.0509 134 PHE A CG  
963  C CD1 . PHE A 119 ? 0.2488 0.2549 0.3314 -0.0215 0.0134  -0.0445 134 PHE A CD1 
964  C CD2 . PHE A 119 ? 0.2475 0.2904 0.3302 -0.0056 0.0260  -0.0249 134 PHE A CD2 
965  C CE1 . PHE A 119 ? 0.2894 0.3318 0.3171 0.0089  0.0373  -0.0470 134 PHE A CE1 
966  C CE2 . PHE A 119 ? 0.2664 0.2736 0.3350 -0.0108 0.0056  -0.0394 134 PHE A CE2 
967  C CZ  . PHE A 119 ? 0.2520 0.3205 0.3401 -0.0101 -0.0047 -0.0466 134 PHE A CZ  
968  N N   . TYR A 120 ? 0.2759 0.2908 0.3275 -0.0282 -0.0295 -0.0656 135 TYR A N   
969  C CA  . TYR A 120 ? 0.2365 0.2945 0.3486 -0.0237 -0.0057 -0.0606 135 TYR A CA  
970  C C   . TYR A 120 ? 0.2762 0.2855 0.3198 -0.0287 0.0085  -0.0379 135 TYR A C   
971  O O   . TYR A 120 ? 0.2469 0.2829 0.3523 -0.0240 -0.0012 -0.0755 135 TYR A O   
972  C CB  . TYR A 120 ? 0.2745 0.3111 0.3553 -0.0401 0.0090  -0.0495 135 TYR A CB  
973  C CG  . TYR A 120 ? 0.2946 0.3508 0.3931 -0.0252 0.0520  -0.0750 135 TYR A CG  
974  C CD1 . TYR A 120 ? 0.2641 0.3642 0.4420 0.0017  0.0800  -0.0195 135 TYR A CD1 
975  C CD2 . TYR A 120 ? 0.3847 0.3673 0.4395 -0.0389 0.0738  -0.0876 135 TYR A CD2 
976  C CE1 . TYR A 120 ? 0.3152 0.3714 0.5184 0.0595  0.0855  -0.0192 135 TYR A CE1 
977  C CE2 . TYR A 120 ? 0.4563 0.3346 0.4810 -0.0064 0.1014  -0.0652 135 TYR A CE2 
978  C CZ  . TYR A 120 ? 0.4133 0.3466 0.5433 0.0621  0.1324  -0.0485 135 TYR A CZ  
979  O OH  . TYR A 120 ? 0.5606 0.4070 0.6536 0.1014  0.2344  -0.0964 135 TYR A OH  
980  N N   . SER A 121 ? 0.2663 0.3045 0.3523 -0.0062 -0.0037 -0.0404 136 SER A N   
981  C CA  . SER A 121 ? 0.2711 0.3354 0.3583 0.0004  0.0096  -0.0415 136 SER A CA  
982  C C   . SER A 121 ? 0.2614 0.2871 0.3419 0.0302  -0.0127 -0.0367 136 SER A C   
983  O O   . SER A 121 ? 0.2503 0.2897 0.3570 -0.0232 0.0027  -0.0507 136 SER A O   
984  C CB  . SER A 121 ? 0.3405 0.5044 0.4090 0.1265  -0.0321 0.0272  136 SER A CB  
985  O OG  . SER A 121 ? 0.5018 0.6317 0.6282 0.0516  -0.0243 -0.0072 136 SER A OG  
986  N N   . ASP A 122 ? 0.2583 0.3201 0.3637 -0.0081 -0.0366 -0.0095 137 ASP A N   
987  C CA  . ASP A 122 ? 0.2338 0.2715 0.3749 -0.0204 -0.0140 -0.0477 137 ASP A CA  
988  C C   . ASP A 122 ? 0.2309 0.2562 0.3567 0.0084  -0.0266 -0.0378 137 ASP A C   
989  O O   . ASP A 122 ? 0.2098 0.2592 0.3793 -0.0048 0.0122  -0.0343 137 ASP A O   
990  C CB  . ASP A 122 ? 0.2529 0.3276 0.3993 -0.0568 0.0023  -0.0370 137 ASP A CB  
991  C CG  . ASP A 122 ? 0.3466 0.4245 0.5278 -0.0426 -0.0950 -0.0486 137 ASP A CG  
992  O OD1 . ASP A 122 ? 0.3047 0.4587 0.6239 -0.0795 -0.0232 -0.0317 137 ASP A OD1 
993  O OD2 . ASP A 122 ? 0.4329 0.4820 0.5454 -0.1279 -0.0124 -0.0843 137 ASP A OD2 
994  N N   . TYR A 123 ? 0.2183 0.2402 0.3379 -0.0213 -0.0042 -0.0465 138 TYR A N   
995  C CA  . TYR A 123 ? 0.1864 0.2277 0.3168 -0.0238 0.0093  -0.0376 138 TYR A CA  
996  C C   . TYR A 123 ? 0.1946 0.2548 0.3045 -0.0164 0.0216  -0.0180 138 TYR A C   
997  O O   . TYR A 123 ? 0.2195 0.2531 0.3075 -0.0036 -0.0015 -0.0229 138 TYR A O   
998  C CB  . TYR A 123 ? 0.2363 0.2204 0.3255 -0.0033 0.0105  -0.0520 138 TYR A CB  
999  C CG  . TYR A 123 ? 0.2175 0.2297 0.3417 -0.0135 0.0097  -0.0226 138 TYR A CG  
1000 C CD1 . TYR A 123 ? 0.2324 0.2625 0.3277 0.0072  0.0030  -0.0205 138 TYR A CD1 
1001 C CD2 . TYR A 123 ? 0.2425 0.2391 0.3548 0.0049  0.0183  -0.0275 138 TYR A CD2 
1002 C CE1 . TYR A 123 ? 0.2603 0.2141 0.3407 0.0119  0.0189  -0.0459 138 TYR A CE1 
1003 C CE2 . TYR A 123 ? 0.2321 0.2346 0.3487 -0.0323 0.0128  -0.0091 138 TYR A CE2 
1004 C CZ  . TYR A 123 ? 0.2361 0.2062 0.3568 -0.0215 0.0164  0.0021  138 TYR A CZ  
1005 O OH  . TYR A 123 ? 0.2405 0.2324 0.3887 -0.0135 -0.0125 -0.0302 138 TYR A OH  
1006 N N   . ALA A 124 ? 0.2188 0.2321 0.3005 -0.0108 0.0026  -0.0339 139 ALA A N   
1007 C CA  . ALA A 124 ? 0.2262 0.2530 0.3181 -0.0193 0.0158  -0.0408 139 ALA A CA  
1008 C C   . ALA A 124 ? 0.2127 0.2503 0.3167 -0.0023 0.0275  -0.0182 139 ALA A C   
1009 O O   . ALA A 124 ? 0.2356 0.2340 0.3346 0.0030  0.0159  -0.0374 139 ALA A O   
1010 C CB  . ALA A 124 ? 0.2424 0.2524 0.3331 -0.0247 0.0195  -0.0134 139 ALA A CB  
1011 N N   . LYS A 125 ? 0.2280 0.2509 0.3248 -0.0013 0.0236  -0.0280 140 LYS A N   
1012 C CA  . LYS A 125 ? 0.2484 0.2192 0.3290 0.0049  0.0219  -0.0475 140 LYS A CA  
1013 C C   . LYS A 125 ? 0.2123 0.2705 0.3270 0.0000  0.0043  -0.0265 140 LYS A C   
1014 O O   . LYS A 125 ? 0.2356 0.2495 0.3604 0.0171  0.0348  -0.0027 140 LYS A O   
1015 C CB  . LYS A 125 ? 0.2472 0.3375 0.3455 -0.0046 0.0114  -0.0369 140 LYS A CB  
1016 C CG  . LYS A 125 ? 0.3633 0.4358 0.4314 0.0247  -0.0235 -0.0166 140 LYS A CG  
1017 C CD  . LYS A 125 ? 0.3871 0.6384 0.5157 0.0104  -0.0494 -0.0248 140 LYS A CD  
1018 C CE  . LYS A 125 ? 0.4876 0.7879 0.6201 0.0348  -0.0690 0.0032  140 LYS A CE  
1019 N NZ  . LYS A 125 ? 0.4264 0.8999 0.7361 0.0440  0.0245  -0.0482 140 LYS A NZ  
1020 N N   . ALA A 126 ? 0.2287 0.2555 0.3471 0.0019  0.0354  -0.0150 141 ALA A N   
1021 C CA  . ALA A 126 ? 0.2126 0.2409 0.3387 0.0164  0.0327  -0.0111 141 ALA A CA  
1022 C C   . ALA A 126 ? 0.2177 0.2358 0.3285 0.0280  0.0357  -0.0214 141 ALA A C   
1023 O O   . ALA A 126 ? 0.2301 0.3085 0.3178 0.0212  0.0227  -0.0290 141 ALA A O   
1024 C CB  . ALA A 126 ? 0.2218 0.2598 0.3612 -0.0277 0.0205  0.0041  141 ALA A CB  
1025 N N   . LEU A 127 ? 0.2063 0.2549 0.3183 -0.0076 0.0313  -0.0490 142 LEU A N   
1026 C CA  . LEU A 127 ? 0.2179 0.2299 0.3058 -0.0124 0.0138  -0.0322 142 LEU A CA  
1027 C C   . LEU A 127 ? 0.2051 0.2403 0.3023 0.0065  0.0246  -0.0168 142 LEU A C   
1028 O O   . LEU A 127 ? 0.2181 0.2327 0.3306 0.0213  0.0212  -0.0332 142 LEU A O   
1029 C CB  . LEU A 127 ? 0.2315 0.2360 0.3218 -0.0009 0.0202  -0.0312 142 LEU A CB  
1030 C CG  . LEU A 127 ? 0.2124 0.2221 0.2812 0.0072  0.0132  -0.0294 142 LEU A CG  
1031 C CD1 . LEU A 127 ? 0.1980 0.2601 0.3061 0.0296  0.0297  -0.0312 142 LEU A CD1 
1032 C CD2 . LEU A 127 ? 0.2016 0.2195 0.2993 0.0075  0.0110  -0.0494 142 LEU A CD2 
1033 N N   . SER A 128 ? 0.2190 0.2277 0.3230 0.0006  0.0105  -0.0373 143 SER A N   
1034 C CA  . SER A 128 ? 0.2700 0.2112 0.3359 0.0128  0.0124  -0.0154 143 SER A CA  
1035 C C   . SER A 128 ? 0.2625 0.2707 0.3264 0.0275  0.0047  -0.0084 143 SER A C   
1036 O O   . SER A 128 ? 0.2940 0.2986 0.3899 0.0109  0.0166  -0.0732 143 SER A O   
1037 C CB  . SER A 128 ? 0.2971 0.1980 0.3915 0.0254  0.0130  -0.0081 143 SER A CB  
1038 O OG  . SER A 128 ? 0.3093 0.2929 0.4652 -0.0082 -0.0343 0.0355  143 SER A OG  
1039 N N   . GLU A 129 ? 0.2534 0.2660 0.3317 0.0387  0.0208  -0.0422 144 GLU A N   
1040 C CA  . GLU A 129 ? 0.2772 0.2942 0.3554 0.0373  0.0291  -0.0499 144 GLU A CA  
1041 C C   . GLU A 129 ? 0.2393 0.2761 0.3672 0.0114  0.0448  -0.0547 144 GLU A C   
1042 O O   . GLU A 129 ? 0.3056 0.4035 0.4012 0.0568  0.0294  -0.0732 144 GLU A O   
1043 C CB  . GLU A 129 ? 0.2833 0.3570 0.3730 0.0421  0.0503  -0.0326 144 GLU A CB  
1044 C CG  . GLU A 129 ? 0.3456 0.5454 0.4646 0.0651  -0.0140 -0.0182 144 GLU A CG  
1045 C CD  . GLU A 129 ? 0.3123 0.7390 0.5704 0.1177  -0.2281 0.0503  144 GLU A CD  
1046 O OE1 . GLU A 129 ? 0.3350 0.8368 1.0335 -0.0310 0.0199  0.0890  144 GLU A OE1 
1047 O OE2 . GLU A 129 ? 0.6287 1.2567 0.6185 -0.1233 -0.1924 0.0401  144 GLU A OE2 
1048 N N   . SER A 130 ? 0.2233 0.2772 0.3608 0.0444  0.0460  -0.0554 145 SER A N   
1049 C CA  . SER A 130 ? 0.2389 0.2210 0.3230 0.0179  0.0493  -0.0524 145 SER A CA  
1050 C C   . SER A 130 ? 0.2741 0.2463 0.3518 -0.0058 0.0749  -0.0608 145 SER A C   
1051 O O   . SER A 130 ? 0.2747 0.2444 0.3462 0.0137  0.0609  -0.0588 145 SER A O   
1052 C CB  . SER A 130 ? 0.2382 0.2403 0.3343 0.0164  0.0512  -0.0370 145 SER A CB  
1053 O OG  . SER A 130 ? 0.2939 0.3130 0.3672 0.0520  0.0096  -0.0246 145 SER A OG  
1054 N N   . LYS A 131 ? 0.3005 0.2506 0.4015 0.0110  0.0615  -0.0548 146 LYS A N   
1055 C CA  . LYS A 131 ? 0.2826 0.2546 0.3907 0.0132  0.0777  -0.0651 146 LYS A CA  
1056 C C   . LYS A 131 ? 0.3062 0.1929 0.3710 0.0243  0.0674  -0.0703 146 LYS A C   
1057 O O   . LYS A 131 ? 0.2894 0.2313 0.3782 -0.0175 0.0806  -0.0717 146 LYS A O   
1058 C CB  . LYS A 131 ? 0.3344 0.2679 0.4710 0.0474  0.0380  -0.0625 146 LYS A CB  
1059 C CG  . LYS A 131 ? 0.3785 0.3059 0.6120 0.1106  -0.0596 -0.0779 146 LYS A CG  
1060 C CD  . LYS A 131 ? 0.5206 0.4689 0.7445 0.1485  -0.0365 -0.0981 146 LYS A CD  
1061 C CE  . LYS A 131 ? 0.5711 0.6652 0.8748 0.1670  0.0033  -0.0700 146 LYS A CE  
1062 N NZ  . LYS A 131 ? 0.6777 0.6856 0.9294 0.1915  0.0476  -0.0411 146 LYS A NZ  
1063 N N   . ALA A 132 ? 0.3029 0.2454 0.3545 0.0155  0.0674  -0.0891 147 ALA A N   
1064 C CA  . ALA A 132 ? 0.2930 0.2600 0.3020 0.0037  0.0365  -0.0798 147 ALA A CA  
1065 C C   . ALA A 132 ? 0.2575 0.2498 0.3171 0.0004  0.0194  -0.0925 147 ALA A C   
1066 O O   . ALA A 132 ? 0.2565 0.2675 0.3290 0.0224  0.0381  -0.0726 147 ALA A O   
1067 C CB  . ALA A 132 ? 0.3015 0.3174 0.2988 0.0208  0.0497  -0.0816 147 ALA A CB  
1068 N N   . ASP A 133 ? 0.2389 0.2076 0.3273 -0.0110 0.0598  -0.0787 148 ASP A N   
1069 C CA  . ASP A 133 ? 0.2174 0.2246 0.2922 0.0100  0.0268  -0.0728 148 ASP A CA  
1070 C C   . ASP A 133 ? 0.2377 0.2232 0.2813 0.0166  0.0119  -0.0549 148 ASP A C   
1071 O O   . ASP A 133 ? 0.2316 0.2057 0.3217 0.0145  0.0329  -0.0617 148 ASP A O   
1072 C CB  . ASP A 133 ? 0.2198 0.2095 0.3318 0.0180  0.0532  -0.0633 148 ASP A CB  
1073 C CG  . ASP A 133 ? 0.2508 0.2348 0.3762 0.0289  0.0515  -0.0235 148 ASP A CG  
1074 O OD1 . ASP A 133 ? 0.2670 0.2625 0.3621 0.0094  0.0217  -0.0234 148 ASP A OD1 
1075 O OD2 . ASP A 133 ? 0.2961 0.3173 0.4472 -0.0068 0.0530  0.0079  148 ASP A OD2 
1076 N N   . VAL A 134 ? 0.2133 0.2101 0.3022 0.0124  0.0214  -0.0369 149 VAL A N   
1077 C CA  . VAL A 134 ? 0.2481 0.2129 0.2907 0.0062  0.0158  -0.0511 149 VAL A CA  
1078 C C   . VAL A 134 ? 0.2432 0.2216 0.2961 0.0064  0.0187  -0.0458 149 VAL A C   
1079 O O   . VAL A 134 ? 0.2339 0.1963 0.3234 -0.0153 0.0260  -0.0495 149 VAL A O   
1080 C CB  . VAL A 134 ? 0.2429 0.2258 0.3215 -0.0027 -0.0021 -0.0283 149 VAL A CB  
1081 C CG1 . VAL A 134 ? 0.2744 0.2432 0.3531 0.0299  0.0029  -0.0189 149 VAL A CG1 
1082 C CG2 . VAL A 134 ? 0.2399 0.2373 0.3575 -0.0039 -0.0177 -0.0073 149 VAL A CG2 
1083 N N   . LYS A 135 ? 0.2217 0.2006 0.3164 -0.0087 0.0238  -0.0494 150 LYS A N   
1084 C CA  . LYS A 135 ? 0.2611 0.2201 0.3247 -0.0157 0.0229  -0.0824 150 LYS A CA  
1085 C C   . LYS A 135 ? 0.2417 0.2101 0.3174 -0.0228 0.0292  -0.0530 150 LYS A C   
1086 O O   . LYS A 135 ? 0.2535 0.1938 0.3111 -0.0091 0.0286  -0.0718 150 LYS A O   
1087 C CB  . LYS A 135 ? 0.2886 0.2499 0.3316 -0.0231 0.0395  -0.0975 150 LYS A CB  
1088 C CG  . LYS A 135 ? 0.3466 0.2618 0.4143 0.0489  0.0598  -0.1288 150 LYS A CG  
1089 C CD  . LYS A 135 ? 0.4684 0.4325 0.5444 0.0131  0.0428  -0.0530 150 LYS A CD  
1090 C CE  . LYS A 135 ? 0.5787 0.5516 0.6587 0.0861  0.0135  -0.0247 150 LYS A CE  
1091 N NZ  . LYS A 135 ? 0.5539 0.6162 0.7103 0.1165  -0.0395 -0.1074 150 LYS A NZ  
1092 N N   . MET A 136 ? 0.2208 0.1971 0.2901 -0.0125 0.0228  -0.0680 151 MET A N   
1093 C CA  . MET A 136 ? 0.2200 0.2038 0.2832 -0.0164 -0.0005 -0.0461 151 MET A CA  
1094 C C   . MET A 136 ? 0.2470 0.1935 0.2588 -0.0128 0.0103  -0.0471 151 MET A C   
1095 O O   . MET A 136 ? 0.2369 0.2115 0.2771 -0.0258 0.0129  -0.0458 151 MET A O   
1096 C CB  . MET A 136 ? 0.2518 0.2112 0.2976 -0.0248 0.0178  -0.0412 151 MET A CB  
1097 C CG  . MET A 136 ? 0.3170 0.1994 0.3240 -0.0101 0.0353  -0.0367 151 MET A CG  
1098 S SD  . MET A 136 ? 0.3331 0.2629 0.3619 -0.0189 0.0233  -0.0548 151 MET A SD  
1099 C CE  . MET A 136 ? 0.3478 0.2743 0.3435 -0.0525 -0.0121 -0.0261 151 MET A CE  
1100 N N   . LEU A 137 ? 0.2303 0.2041 0.2597 -0.0037 0.0159  -0.0485 152 LEU A N   
1101 C CA  . LEU A 137 ? 0.2548 0.2083 0.2549 0.0077  0.0060  -0.0378 152 LEU A CA  
1102 C C   . LEU A 137 ? 0.2350 0.2171 0.2715 -0.0166 0.0147  -0.0621 152 LEU A C   
1103 O O   . LEU A 137 ? 0.2383 0.2056 0.2939 -0.0156 0.0288  -0.0551 152 LEU A O   
1104 C CB  . LEU A 137 ? 0.2507 0.1996 0.2661 -0.0025 0.0065  -0.0386 152 LEU A CB  
1105 C CG  . LEU A 137 ? 0.2332 0.2082 0.3008 0.0027  0.0180  -0.0377 152 LEU A CG  
1106 C CD1 . LEU A 137 ? 0.2567 0.2038 0.3276 -0.0065 0.0264  -0.0628 152 LEU A CD1 
1107 C CD2 . LEU A 137 ? 0.2184 0.2018 0.2887 -0.0036 0.0055  -0.0530 152 LEU A CD2 
1108 N N   . GLU A 138 ? 0.2234 0.2104 0.3175 -0.0201 0.0319  -0.0420 153 GLU A N   
1109 C CA  . GLU A 138 ? 0.2605 0.2035 0.3158 -0.0202 0.0207  -0.0487 153 GLU A CA  
1110 C C   . GLU A 138 ? 0.2848 0.1861 0.2887 -0.0135 0.0113  -0.0358 153 GLU A C   
1111 O O   . GLU A 138 ? 0.2890 0.2325 0.3160 -0.0495 0.0128  -0.0515 153 GLU A O   
1112 C CB  . GLU A 138 ? 0.2828 0.2081 0.3072 -0.0083 0.0151  -0.0644 153 GLU A CB  
1113 C CG  . GLU A 138 ? 0.2900 0.2378 0.3110 0.0168  0.0225  -0.0545 153 GLU A CG  
1114 C CD  . GLU A 138 ? 0.3141 0.2720 0.3325 0.0466  -0.0112 -0.0448 153 GLU A CD  
1115 O OE1 . GLU A 138 ? 0.3430 0.3616 0.3512 0.0504  0.0042  -0.0674 153 GLU A OE1 
1116 O OE2 . GLU A 138 ? 0.3260 0.3044 0.4300 0.0402  -0.0315 -0.0414 153 GLU A OE2 
1117 N N   . TYR A 139 ? 0.2604 0.2063 0.2796 -0.0413 0.0301  -0.0578 154 TYR A N   
1118 C CA  . TYR A 139 ? 0.2649 0.1936 0.3247 -0.0257 -0.0007 -0.0619 154 TYR A CA  
1119 C C   . TYR A 139 ? 0.2448 0.2163 0.3032 -0.0364 0.0172  -0.0395 154 TYR A C   
1120 O O   . TYR A 139 ? 0.2383 0.2462 0.3122 -0.0420 0.0136  -0.0610 154 TYR A O   
1121 C CB  . TYR A 139 ? 0.2278 0.2670 0.3072 -0.0173 0.0161  -0.0599 154 TYR A CB  
1122 C CG  . TYR A 139 ? 0.2792 0.2520 0.2825 -0.0214 -0.0054 -0.0595 154 TYR A CG  
1123 C CD1 . TYR A 139 ? 0.3226 0.2427 0.2888 -0.0191 0.0003  -0.0690 154 TYR A CD1 
1124 C CD2 . TYR A 139 ? 0.2635 0.2469 0.2832 -0.0092 0.0112  -0.0658 154 TYR A CD2 
1125 C CE1 . TYR A 139 ? 0.3237 0.2637 0.3087 -0.0533 -0.0056 -0.0921 154 TYR A CE1 
1126 C CE2 . TYR A 139 ? 0.2883 0.3135 0.2860 0.0146  0.0107  -0.0746 154 TYR A CE2 
1127 C CZ  . TYR A 139 ? 0.2876 0.3438 0.3016 -0.0193 -0.0108 -0.0911 154 TYR A CZ  
1128 O OH  . TYR A 139 ? 0.3000 0.4626 0.3358 -0.0432 -0.0184 -0.1165 154 TYR A OH  
1129 N N   . GLY A 140 ? 0.2554 0.2048 0.2794 -0.0317 0.0374  -0.0589 155 GLY A N   
1130 C CA  . GLY A 140 ? 0.2348 0.2296 0.2785 -0.0160 0.0162  -0.0547 155 GLY A CA  
1131 C C   . GLY A 140 ? 0.2490 0.2195 0.2811 -0.0179 -0.0033 -0.0369 155 GLY A C   
1132 O O   . GLY A 140 ? 0.2358 0.2530 0.3051 -0.0305 0.0222  -0.0654 155 GLY A O   
1133 N N   . CYS A 141 ? 0.2359 0.2268 0.2745 0.0109  0.0011  -0.0551 156 CYS A N   
1134 C CA  . CYS A 141 ? 0.2627 0.2007 0.2631 -0.0141 -0.0018 -0.0721 156 CYS A CA  
1135 C C   . CYS A 141 ? 0.2724 0.2163 0.2842 -0.0322 0.0456  -0.0446 156 CYS A C   
1136 O O   . CYS A 141 ? 0.2432 0.2918 0.3605 -0.0545 0.0360  -0.0264 156 CYS A O   
1137 C CB  . CYS A 141 ? 0.2915 0.2272 0.3235 -0.0540 -0.0104 -0.0672 156 CYS A CB  
1138 S SG  . CYS A 141 ? 0.3022 0.2927 0.3649 -0.0244 0.0118  -0.0080 156 CYS A SG  
1139 N N   . ASN A 142 ? 0.2689 0.2334 0.3109 -0.0396 0.0260  -0.0376 157 ASN A N   
1140 C CA  . ASN A 142 ? 0.2859 0.2328 0.3278 -0.0501 0.0219  -0.0206 157 ASN A CA  
1141 C C   . ASN A 142 ? 0.3266 0.2286 0.3259 -0.0632 0.0233  -0.0213 157 ASN A C   
1142 O O   . ASN A 142 ? 0.3313 0.2757 0.4088 -0.0905 -0.0047 -0.0076 157 ASN A O   
1143 C CB  . ASN A 142 ? 0.3163 0.2032 0.3450 -0.0260 0.0099  -0.0061 157 ASN A CB  
1144 C CG  . ASN A 142 ? 0.3413 0.3136 0.3860 0.0115  -0.0035 -0.0075 157 ASN A CG  
1145 O OD1 . ASN A 142 ? 0.3321 0.4266 0.3858 0.0255  0.0072  -0.0126 157 ASN A OD1 
1146 N ND2 . ASN A 142 ? 0.3591 0.3205 0.4148 -0.0075 0.0307  -0.0086 157 ASN A ND2 
1147 N N   . GLU A 143 ? 0.2670 0.2360 0.3233 -0.0464 0.0113  -0.0495 158 GLU A N   
1148 C CA  . GLU A 143 ? 0.2859 0.2239 0.3559 -0.0730 0.0124  -0.0266 158 GLU A CA  
1149 C C   . GLU A 143 ? 0.2875 0.2438 0.3388 -0.0720 0.0261  -0.0649 158 GLU A C   
1150 O O   . GLU A 143 ? 0.2979 0.2744 0.4339 -0.0707 0.0424  -0.0790 158 GLU A O   
1151 C CB  . GLU A 143 ? 0.3086 0.2561 0.3524 -0.0562 0.0054  -0.0389 158 GLU A CB  
1152 C CG  . GLU A 143 ? 0.3658 0.3225 0.4446 -0.0277 -0.0343 -0.0747 158 GLU A CG  
1153 C CD  . GLU A 143 ? 0.4314 0.3658 0.5384 -0.1016 -0.0451 -0.0553 158 GLU A CD  
1154 O OE1 . GLU A 143 ? 0.4557 0.3053 0.6222 -0.0777 -0.0078 -0.0737 158 GLU A OE1 
1155 O OE2 . GLU A 143 ? 0.4813 0.4838 0.6718 -0.1389 -0.1299 -0.0483 158 GLU A OE2 
1156 N N   . LEU A 144 ? 0.2483 0.2364 0.3358 -0.0636 0.0223  -0.0610 159 LEU A N   
1157 C CA  . LEU A 144 ? 0.2468 0.2672 0.3147 -0.0395 0.0134  -0.0434 159 LEU A CA  
1158 C C   . LEU A 144 ? 0.2530 0.2448 0.3025 -0.0653 0.0022  -0.0370 159 LEU A C   
1159 O O   . LEU A 144 ? 0.2750 0.2858 0.3475 -0.0304 0.0331  -0.0712 159 LEU A O   
1160 C CB  . LEU A 144 ? 0.2534 0.2675 0.3029 -0.0428 -0.0022 -0.0653 159 LEU A CB  
1161 C CG  . LEU A 144 ? 0.2310 0.2800 0.3264 -0.0253 0.0143  -0.0728 159 LEU A CG  
1162 C CD1 . LEU A 144 ? 0.2278 0.2928 0.3012 -0.0145 0.0065  -0.0481 159 LEU A CD1 
1163 C CD2 . LEU A 144 ? 0.2574 0.3246 0.3309 -0.0533 0.0159  -0.0614 159 LEU A CD2 
1164 N N   . LYS A 145 ? 0.2642 0.2582 0.2983 -0.0537 0.0148  -0.0596 160 LYS A N   
1165 C CA  . LYS A 145 ? 0.2365 0.2683 0.3041 -0.0483 0.0337  -0.0257 160 LYS A CA  
1166 C C   . LYS A 145 ? 0.1988 0.2849 0.3285 -0.0321 0.0233  -0.0380 160 LYS A C   
1167 O O   . LYS A 145 ? 0.2538 0.3049 0.3492 -0.0560 0.0583  -0.0446 160 LYS A O   
1168 C CB  . LYS A 145 ? 0.2598 0.3023 0.3445 -0.0637 0.0518  -0.0495 160 LYS A CB  
1169 C CG  . LYS A 145 ? 0.3173 0.3318 0.4116 -0.0817 0.0757  -0.0354 160 LYS A CG  
1170 C CD  . LYS A 145 ? 0.3413 0.3892 0.4624 -0.1068 0.0356  -0.0036 160 LYS A CD  
1171 C CE  . LYS A 145 ? 0.4531 0.3674 0.5908 -0.1005 0.0792  0.0541  160 LYS A CE  
1172 N NZ  . LYS A 145 ? 0.5764 0.3833 0.6846 -0.0379 0.0841  0.0938  160 LYS A NZ  
1173 N N   . SER A 146 ? 0.1970 0.2467 0.2927 -0.0308 0.0360  -0.0579 161 SER A N   
1174 C CA  . SER A 146 ? 0.2145 0.2272 0.2791 -0.0317 0.0383  -0.0584 161 SER A CA  
1175 C C   . SER A 146 ? 0.2229 0.2181 0.2953 -0.0295 0.0186  -0.0395 161 SER A C   
1176 O O   . SER A 146 ? 0.2306 0.2575 0.3130 -0.0123 0.0145  -0.0619 161 SER A O   
1177 C CB  . SER A 146 ? 0.2274 0.2568 0.3199 -0.0206 0.0460  -0.0365 161 SER A CB  
1178 O OG  . SER A 146 ? 0.2737 0.2251 0.3431 -0.0146 0.0479  -0.0562 161 SER A OG  
1179 N N   . ALA A 147 ? 0.2155 0.2867 0.2961 -0.0197 0.0203  -0.0622 162 ALA A N   
1180 C CA  . ALA A 147 ? 0.2474 0.2922 0.2788 -0.0327 0.0481  -0.0454 162 ALA A CA  
1181 C C   . ALA A 147 ? 0.2190 0.2466 0.2430 -0.0256 0.0322  -0.0383 162 ALA A C   
1182 O O   . ALA A 147 ? 0.2308 0.2539 0.2886 -0.0211 0.0201  -0.0305 162 ALA A O   
1183 C CB  . ALA A 147 ? 0.2850 0.3659 0.2893 -0.0712 0.0589  -0.0710 162 ALA A CB  
1184 N N   . TYR A 148 ? 0.2254 0.2492 0.2852 -0.0170 0.0275  -0.0456 163 TYR A N   
1185 C CA  . TYR A 148 ? 0.2399 0.2108 0.2879 -0.0023 0.0215  -0.0501 163 TYR A CA  
1186 C C   . TYR A 148 ? 0.1995 0.2166 0.2754 0.0046  0.0109  -0.0561 163 TYR A C   
1187 O O   . TYR A 148 ? 0.2231 0.2168 0.2947 -0.0022 0.0255  -0.0676 163 TYR A O   
1188 C CB  . TYR A 148 ? 0.2621 0.2390 0.2997 -0.0031 0.0328  -0.0441 163 TYR A CB  
1189 C CG  . TYR A 148 ? 0.2522 0.2295 0.3136 0.0046  0.0383  -0.0363 163 TYR A CG  
1190 C CD1 . TYR A 148 ? 0.2576 0.2512 0.3087 0.0365  0.0224  -0.0468 163 TYR A CD1 
1191 C CD2 . TYR A 148 ? 0.2383 0.2268 0.3327 -0.0203 0.0191  -0.0281 163 TYR A CD2 
1192 C CE1 . TYR A 148 ? 0.2717 0.2284 0.3616 0.0215  0.0473  -0.0627 163 TYR A CE1 
1193 C CE2 . TYR A 148 ? 0.2429 0.2363 0.3929 0.0244  0.0479  -0.0207 163 TYR A CE2 
1194 C CZ  . TYR A 148 ? 0.2729 0.2613 0.3373 0.0237  0.0794  -0.0373 163 TYR A CZ  
1195 O OH  . TYR A 148 ? 0.2776 0.2973 0.4552 0.0134  0.1199  -0.0646 163 TYR A OH  
1196 N N   . ILE A 149 ? 0.2234 0.2298 0.2768 -0.0170 0.0382  -0.0612 164 ILE A N   
1197 C CA  . ILE A 149 ? 0.2098 0.2305 0.2666 -0.0258 0.0483  -0.0490 164 ILE A CA  
1198 C C   . ILE A 149 ? 0.2028 0.2159 0.2355 -0.0070 0.0355  -0.0510 164 ILE A C   
1199 O O   . ILE A 149 ? 0.2054 0.2498 0.2944 -0.0013 0.0390  -0.0506 164 ILE A O   
1200 C CB  . ILE A 149 ? 0.2174 0.2182 0.3103 -0.0276 0.0329  -0.0559 164 ILE A CB  
1201 C CG1 . ILE A 149 ? 0.2330 0.2310 0.2957 -0.0295 0.0241  -0.0659 164 ILE A CG1 
1202 C CG2 . ILE A 149 ? 0.2413 0.2107 0.2932 -0.0240 0.0399  -0.0929 164 ILE A CG2 
1203 C CD1 . ILE A 149 ? 0.2676 0.2521 0.2852 -0.0361 0.0178  -0.0486 164 ILE A CD1 
1204 N N   . CYS A 150 ? 0.2202 0.2367 0.2941 -0.0286 0.0318  -0.0237 165 CYS A N   
1205 C CA  . CYS A 150 ? 0.2326 0.2460 0.3105 -0.0153 0.0354  -0.0353 165 CYS A CA  
1206 C C   . CYS A 150 ? 0.2280 0.2305 0.3129 -0.0182 0.0180  -0.0176 165 CYS A C   
1207 O O   . CYS A 150 ? 0.2549 0.2205 0.3160 -0.0120 0.0096  -0.0343 165 CYS A O   
1208 C CB  . CYS A 150 ? 0.2394 0.2799 0.3377 -0.0505 0.0241  -0.0305 165 CYS A CB  
1209 S SG  . CYS A 150 ? 0.2841 0.2939 0.4057 -0.0632 -0.0045 -0.0130 165 CYS A SG  
1210 N N   . ARG A 151 ? 0.2254 0.2361 0.2910 -0.0126 0.0246  -0.0432 166 ARG A N   
1211 C CA  . ARG A 151 ? 0.2250 0.2290 0.2799 -0.0183 0.0224  -0.0372 166 ARG A CA  
1212 C C   . ARG A 151 ? 0.2203 0.2202 0.2542 0.0148  0.0060  -0.0283 166 ARG A C   
1213 O O   . ARG A 151 ? 0.2142 0.2386 0.2938 0.0052  0.0017  -0.0386 166 ARG A O   
1214 C CB  . ARG A 151 ? 0.1997 0.2354 0.2792 -0.0086 0.0275  -0.0300 166 ARG A CB  
1215 C CG  . ARG A 151 ? 0.2210 0.2302 0.3080 -0.0056 0.0025  -0.0344 166 ARG A CG  
1216 C CD  . ARG A 151 ? 0.2442 0.2475 0.3283 0.0143  0.0199  -0.0465 166 ARG A CD  
1217 N NE  . ARG A 151 ? 0.2767 0.2128 0.3285 0.0204  0.0418  -0.0440 166 ARG A NE  
1218 C CZ  . ARG A 151 ? 0.2491 0.2378 0.3075 0.0091  0.0157  -0.0656 166 ARG A CZ  
1219 N NH1 . ARG A 151 ? 0.2903 0.2159 0.3192 0.0093  0.0493  -0.0718 166 ARG A NH1 
1220 N NH2 . ARG A 151 ? 0.2550 0.2355 0.3092 0.0173  0.0602  -0.0649 166 ARG A NH2 
1221 N N   . ASP A 152 ? 0.2138 0.2251 0.2781 0.0115  0.0127  -0.0318 167 ASP A N   
1222 C CA  . ASP A 152 ? 0.2195 0.2175 0.2801 -0.0248 0.0222  -0.0309 167 ASP A CA  
1223 C C   . ASP A 152 ? 0.2099 0.2194 0.2878 -0.0066 0.0014  -0.0355 167 ASP A C   
1224 O O   . ASP A 152 ? 0.2063 0.2188 0.3028 -0.0063 -0.0032 -0.0315 167 ASP A O   
1225 C CB  . ASP A 152 ? 0.2224 0.2039 0.2924 -0.0285 0.0175  -0.0224 167 ASP A CB  
1226 C CG  . ASP A 152 ? 0.2723 0.2592 0.2967 0.0056  0.0267  -0.0211 167 ASP A CG  
1227 O OD1 . ASP A 152 ? 0.2629 0.2441 0.3930 -0.0040 0.0170  -0.0496 167 ASP A OD1 
1228 O OD2 . ASP A 152 ? 0.2956 0.2141 0.3178 0.0069  0.0143  -0.0512 167 ASP A OD2 
1229 N N   . LEU A 153 ? 0.2021 0.2270 0.2933 0.0009  0.0105  -0.0221 168 LEU A N   
1230 C CA  . LEU A 153 ? 0.2197 0.2017 0.2891 0.0039  0.0061  -0.0316 168 LEU A CA  
1231 C C   . LEU A 153 ? 0.2036 0.2211 0.2649 -0.0246 0.0177  -0.0097 168 LEU A C   
1232 O O   . LEU A 153 ? 0.2371 0.2321 0.2992 -0.0023 0.0027  -0.0116 168 LEU A O   
1233 C CB  . LEU A 153 ? 0.2438 0.2518 0.3078 -0.0106 0.0083  -0.0387 168 LEU A CB  
1234 C CG  . LEU A 153 ? 0.2525 0.2379 0.3121 0.0057  0.0032  -0.0340 168 LEU A CG  
1235 C CD1 . LEU A 153 ? 0.2880 0.2784 0.3046 -0.0684 -0.0001 -0.0199 168 LEU A CD1 
1236 C CD2 . LEU A 153 ? 0.3165 0.2486 0.2987 0.0154  0.0211  -0.0471 168 LEU A CD2 
1237 N N   . ARG A 154 ? 0.2315 0.2280 0.2775 -0.0073 0.0288  -0.0038 169 ARG A N   
1238 C CA  . ARG A 154 ? 0.2283 0.2512 0.2851 -0.0168 0.0168  -0.0247 169 ARG A CA  
1239 C C   . ARG A 154 ? 0.2427 0.2761 0.2555 -0.0090 -0.0003 -0.0046 169 ARG A C   
1240 O O   . ARG A 154 ? 0.2596 0.2499 0.2910 0.0011  -0.0135 -0.0115 169 ARG A O   
1241 C CB  . ARG A 154 ? 0.2544 0.2561 0.3000 0.0050  0.0327  -0.0271 169 ARG A CB  
1242 C CG  . ARG A 154 ? 0.2398 0.2912 0.3047 -0.0264 0.0279  -0.0088 169 ARG A CG  
1243 C CD  . ARG A 154 ? 0.2887 0.3317 0.2998 -0.0229 0.0317  -0.0104 169 ARG A CD  
1244 N NE  . ARG A 154 ? 0.3191 0.3180 0.3216 -0.0353 0.0415  -0.0530 169 ARG A NE  
1245 C CZ  . ARG A 154 ? 0.3417 0.3286 0.3004 -0.0064 0.0604  -0.0270 169 ARG A CZ  
1246 N NH1 . ARG A 154 ? 0.3589 0.3349 0.3180 -0.0181 0.0509  -0.0154 169 ARG A NH1 
1247 N NH2 . ARG A 154 ? 0.3061 0.3123 0.3022 0.0060  0.0305  -0.0456 169 ARG A NH2 
1248 N N   . ASP A 155 ? 0.2255 0.2438 0.2763 -0.0005 -0.0071 -0.0174 170 ASP A N   
1249 C CA  . ASP A 155 ? 0.2499 0.2800 0.2754 -0.0156 -0.0081 -0.0320 170 ASP A CA  
1250 C C   . ASP A 155 ? 0.2100 0.2453 0.2566 -0.0268 -0.0112 -0.0113 170 ASP A C   
1251 O O   . ASP A 155 ? 0.2436 0.2626 0.3071 -0.0024 -0.0165 -0.0525 170 ASP A O   
1252 C CB  . ASP A 155 ? 0.2779 0.2524 0.2990 -0.0288 0.0121  -0.0637 170 ASP A CB  
1253 C CG  . ASP A 155 ? 0.2549 0.2764 0.3366 -0.0077 0.0267  -0.0286 170 ASP A CG  
1254 O OD1 . ASP A 155 ? 0.2788 0.2707 0.3438 -0.0060 0.0117  -0.0522 170 ASP A OD1 
1255 O OD2 . ASP A 155 ? 0.3116 0.2628 0.3761 0.0219  0.0190  -0.0582 170 ASP A OD2 
1256 N N   . MET A 156 ? 0.1986 0.2377 0.2799 -0.0046 0.0017  -0.0184 171 MET A N   
1257 C CA  . MET A 156 ? 0.2154 0.2049 0.2899 -0.0095 0.0104  -0.0104 171 MET A CA  
1258 C C   . MET A 156 ? 0.2205 0.2354 0.2949 -0.0026 0.0077  0.0070  171 MET A C   
1259 O O   . MET A 156 ? 0.2231 0.2880 0.3246 -0.0068 -0.0078 -0.0092 171 MET A O   
1260 C CB  . MET A 156 ? 0.2484 0.2252 0.2983 -0.0019 0.0070  0.0079  171 MET A CB  
1261 C CG  . MET A 156 ? 0.2301 0.2479 0.3371 -0.0116 0.0095  -0.0060 171 MET A CG  
1262 S SD  . MET A 156 ? 0.2633 0.2631 0.3342 0.0087  0.0225  -0.0183 171 MET A SD  
1263 C CE  . MET A 156 ? 0.3323 0.2430 0.3930 -0.0119 -0.0132 -0.0208 171 MET A CE  
1264 N N   . TYR A 157 ? 0.2331 0.2451 0.3163 -0.0125 0.0075  -0.0103 172 TYR A N   
1265 C CA  . TYR A 157 ? 0.2507 0.2573 0.3087 -0.0045 -0.0089 -0.0159 172 TYR A CA  
1266 C C   . TYR A 157 ? 0.2628 0.2692 0.3260 -0.0055 -0.0224 -0.0066 172 TYR A C   
1267 O O   . TYR A 157 ? 0.2755 0.2875 0.3795 -0.0220 -0.0373 0.0185  172 TYR A O   
1268 C CB  . TYR A 157 ? 0.2839 0.2524 0.3229 -0.0190 -0.0099 0.0011  172 TYR A CB  
1269 C CG  . TYR A 157 ? 0.2861 0.2316 0.3128 -0.0066 0.0034  0.0142  172 TYR A CG  
1270 C CD1 . TYR A 157 ? 0.3188 0.2354 0.3554 -0.0044 -0.0071 0.0073  172 TYR A CD1 
1271 C CD2 . TYR A 157 ? 0.2959 0.2491 0.3232 0.0075  -0.0173 0.0086  172 TYR A CD2 
1272 C CE1 . TYR A 157 ? 0.3338 0.2743 0.3710 0.0328  0.0172  -0.0364 172 TYR A CE1 
1273 C CE2 . TYR A 157 ? 0.2796 0.2421 0.3628 -0.0114 -0.0217 -0.0369 172 TYR A CE2 
1274 C CZ  . TYR A 157 ? 0.3514 0.2309 0.3492 0.0238  -0.0015 -0.0110 172 TYR A CZ  
1275 O OH  . TYR A 157 ? 0.4207 0.3266 0.3812 0.0190  -0.0186 -0.0704 172 TYR A OH  
1276 N N   . LYS A 158 ? 0.2729 0.2367 0.2979 -0.0167 -0.0029 0.0054  173 LYS A N   
1277 C CA  . LYS A 158 ? 0.2982 0.2850 0.2868 -0.0249 0.0060  0.0117  173 LYS A CA  
1278 C C   . LYS A 158 ? 0.2898 0.3012 0.3167 -0.0046 -0.0288 0.0079  173 LYS A C   
1279 O O   . LYS A 158 ? 0.3182 0.3601 0.3452 -0.0299 -0.0345 0.0364  173 LYS A O   
1280 C CB  . LYS A 158 ? 0.2986 0.3168 0.3379 -0.0176 -0.0135 -0.0311 173 LYS A CB  
1281 C CG  . LYS A 158 ? 0.3390 0.4232 0.3466 -0.0222 -0.0122 -0.0519 173 LYS A CG  
1282 C CD  . LYS A 158 ? 0.4083 0.4491 0.4399 -0.0146 0.0351  -0.0902 173 LYS A CD  
1283 C CE  . LYS A 158 ? 0.5601 0.5367 0.5667 0.0032  0.0623  -0.1304 173 LYS A CE  
1284 N NZ  . LYS A 158 ? 0.6218 0.5993 0.6507 0.0211  0.1535  -0.1115 173 LYS A NZ  
1285 N N   . TYR A 159 ? 0.2597 0.3197 0.3174 -0.0028 -0.0489 0.0086  174 TYR A N   
1286 C CA  . TYR A 159 ? 0.2580 0.3130 0.3530 -0.0246 -0.0344 -0.0228 174 TYR A CA  
1287 C C   . TYR A 159 ? 0.2484 0.3259 0.3737 -0.0167 -0.0540 -0.0312 174 TYR A C   
1288 O O   . TYR A 159 ? 0.2744 0.4143 0.5098 -0.0488 -0.0539 -0.0455 174 TYR A O   
1289 C CB  . TYR A 159 ? 0.2937 0.2979 0.3478 -0.0331 -0.0194 -0.0109 174 TYR A CB  
1290 C CG  . TYR A 159 ? 0.3246 0.2930 0.3634 -0.0440 -0.0269 -0.0562 174 TYR A CG  
1291 C CD1 . TYR A 159 ? 0.3904 0.3258 0.3875 -0.0319 -0.0027 -0.0916 174 TYR A CD1 
1292 C CD2 . TYR A 159 ? 0.3050 0.3508 0.4311 -0.0851 0.0088  -0.1024 174 TYR A CD2 
1293 C CE1 . TYR A 159 ? 0.4848 0.3126 0.3623 -0.0061 0.0217  -0.0831 174 TYR A CE1 
1294 C CE2 . TYR A 159 ? 0.3723 0.3514 0.4781 -0.0704 0.0380  -0.1089 174 TYR A CE2 
1295 C CZ  . TYR A 159 ? 0.4561 0.4373 0.4168 -0.0416 0.0991  -0.0756 174 TYR A CZ  
1296 O OH  . TYR A 159 ? 0.6379 0.4129 0.5503 -0.0336 0.1671  -0.1114 174 TYR A OH  
1297 N N   . LEU A 160 ? 0.2635 0.3008 0.3732 -0.0121 -0.0190 -0.0134 175 LEU A N   
1298 C CA  . LEU A 160 ? 0.2644 0.3136 0.4609 0.0131  -0.0095 -0.0029 175 LEU A CA  
1299 C C   . LEU A 160 ? 0.2440 0.3664 0.4740 0.0007  -0.0111 0.0146  175 LEU A C   
1300 O O   . LEU A 160 ? 0.2804 0.4982 0.5624 0.0477  -0.0458 0.0440  175 LEU A O   
1301 C CB  . LEU A 160 ? 0.2797 0.3657 0.4162 0.0127  0.0181  0.0120  175 LEU A CB  
1302 C CG  . LEU A 160 ? 0.3111 0.3271 0.4425 0.0351  0.0398  0.0192  175 LEU A CG  
1303 C CD1 . LEU A 160 ? 0.3525 0.3130 0.4133 0.0574  0.0443  0.0332  175 LEU A CD1 
1304 C CD2 . LEU A 160 ? 0.3499 0.3524 0.4571 0.0483  0.0668  0.0503  175 LEU A CD2 
1305 N N   . GLY A 161 ? 0.2935 0.3639 0.4579 0.0086  -0.0595 0.0587  176 GLY A N   
1306 C CA  . GLY A 161 ? 0.2954 0.4158 0.4465 -0.0104 -0.0737 0.0736  176 GLY A CA  
1307 C C   . GLY A 161 ? 0.3124 0.4375 0.4492 0.0042  -0.0728 0.0829  176 GLY A C   
1308 O O   . GLY A 161 ? 0.4157 0.4385 0.5105 -0.0032 -0.0689 0.1461  176 GLY A O   
1309 N N   . ASP A 162 ? 0.2730 0.3929 0.4426 -0.0061 -0.0382 0.0627  177 ASP A N   
1310 C CA  . ASP A 162 ? 0.2739 0.3777 0.4198 0.0017  0.0004  0.0479  177 ASP A CA  
1311 C C   . ASP A 162 ? 0.2994 0.4144 0.3625 -0.0435 -0.0224 0.0480  177 ASP A C   
1312 O O   . ASP A 162 ? 0.2968 0.4068 0.3588 -0.0081 -0.0034 0.0467  177 ASP A O   
1313 C CB  . ASP A 162 ? 0.2607 0.3823 0.4279 -0.0195 0.0129  0.0519  177 ASP A CB  
1314 C CG  . ASP A 162 ? 0.3225 0.4161 0.4612 -0.0421 0.0223  0.0340  177 ASP A CG  
1315 O OD1 . ASP A 162 ? 0.3636 0.4035 0.4277 -0.0284 0.0130  0.0830  177 ASP A OD1 
1316 O OD2 . ASP A 162 ? 0.3914 0.4200 0.5099 0.0144  0.0265  -0.0174 177 ASP A OD2 
1317 N N   . LYS A 163 ? 0.2814 0.4401 0.3946 0.0134  -0.0470 0.0764  178 LYS A N   
1318 C CA  . LYS A 163 ? 0.3298 0.4756 0.3815 0.0056  -0.0132 0.0603  178 LYS A CA  
1319 C C   . LYS A 163 ? 0.3450 0.3936 0.3673 -0.0075 -0.0068 0.0625  178 LYS A C   
1320 O O   . LYS A 163 ? 0.3368 0.4203 0.3967 0.0004  -0.0012 0.0909  178 LYS A O   
1321 C CB  . LYS A 163 ? 0.3637 0.5767 0.4090 -0.0155 -0.0120 0.0804  178 LYS A CB  
1322 C CG  . LYS A 163 ? 0.3951 0.6440 0.4992 -0.0358 -0.0553 0.0386  178 LYS A CG  
1323 C CD  . LYS A 163 ? 0.5113 0.6988 0.5825 -0.0775 -0.0431 0.0581  178 LYS A CD  
1324 C CE  . LYS A 163 ? 0.7231 0.7297 0.7610 -0.1014 -0.0770 -0.0180 178 LYS A CE  
1325 N NZ  . LYS A 163 ? 0.8475 0.7373 0.8624 -0.0652 -0.0911 -0.0382 178 LYS A NZ  
1326 N N   . GLU A 164 ? 0.3455 0.4036 0.3914 0.0124  -0.0134 0.0676  179 GLU A N   
1327 C CA  . GLU A 164 ? 0.3761 0.3580 0.3863 -0.0070 -0.0139 0.0611  179 GLU A CA  
1328 C C   . GLU A 164 ? 0.3709 0.3181 0.3852 0.0010  0.0003  0.0392  179 GLU A C   
1329 O O   . GLU A 164 ? 0.3483 0.2838 0.3778 -0.0097 0.0038  0.0103  179 GLU A O   
1330 C CB  . GLU A 164 ? 0.4737 0.3771 0.4815 0.0216  -0.0445 0.0808  179 GLU A CB  
1331 C CG  . GLU A 164 ? 0.5910 0.4212 0.6054 -0.0325 0.0024  0.0356  179 GLU A CG  
1332 C CD  . GLU A 164 ? 0.6968 0.4412 0.6709 -0.0431 0.1097  0.0162  179 GLU A CD  
1333 O OE1 . GLU A 164 ? 0.6958 0.6113 0.8385 0.0359  0.0903  0.0310  179 GLU A OE1 
1334 O OE2 . GLU A 164 ? 0.8561 0.4857 0.7489 -0.1342 0.1164  0.0470  179 GLU A OE2 
1335 N N   . LYS A 165 ? 0.3226 0.3006 0.3736 0.0179  0.0026  0.0317  180 LYS A N   
1336 C CA  . LYS A 165 ? 0.3030 0.2902 0.3908 -0.0007 0.0066  0.0263  180 LYS A CA  
1337 C C   . LYS A 165 ? 0.3337 0.2859 0.2853 -0.0173 0.0208  0.0208  180 LYS A C   
1338 O O   . LYS A 165 ? 0.3173 0.2933 0.3387 -0.0132 0.0178  0.0405  180 LYS A O   
1339 C CB  . LYS A 165 ? 0.3117 0.2671 0.3773 0.0143  0.0136  0.0402  180 LYS A CB  
1340 C CG  . LYS A 165 ? 0.3893 0.2777 0.5026 0.0206  0.0067  0.0182  180 LYS A CG  
1341 C CD  . LYS A 165 ? 0.4602 0.4962 0.5538 0.0238  -0.0032 -0.0177 180 LYS A CD  
1342 C CE  . LYS A 165 ? 0.4446 0.3977 0.6003 0.0570  -0.0571 -0.0159 180 LYS A CE  
1343 N NZ  . LYS A 165 ? 0.5597 0.4404 0.6270 -0.0173 -0.0253 -0.1415 180 LYS A NZ  
1344 N N   . THR A 166 ? 0.2990 0.3101 0.3172 -0.0244 -0.0213 0.0319  181 THR A N   
1345 C CA  . THR A 166 ? 0.3046 0.2962 0.3280 -0.0326 -0.0045 0.0410  181 THR A CA  
1346 C C   . THR A 166 ? 0.3093 0.2857 0.3824 -0.0431 0.0221  0.0577  181 THR A C   
1347 O O   . THR A 166 ? 0.3046 0.3001 0.3419 -0.0381 -0.0200 0.0240  181 THR A O   
1348 C CB  . THR A 166 ? 0.2906 0.3350 0.3206 -0.0385 -0.0027 0.0366  181 THR A CB  
1349 O OG1 . THR A 166 ? 0.2936 0.3123 0.3658 -0.0473 0.0097  -0.0054 181 THR A OG1 
1350 C CG2 . THR A 166 ? 0.3009 0.3541 0.3199 -0.0380 0.0005  -0.0058 181 THR A CG2 
1351 N N   . LYS A 167 ? 0.3037 0.2971 0.3369 -0.0477 0.0091  0.0255  182 LYS A N   
1352 C CA  . LYS A 167 ? 0.2977 0.2974 0.3793 -0.0663 0.0344  0.0121  182 LYS A CA  
1353 C C   . LYS A 167 ? 0.3641 0.2797 0.3638 -0.0354 0.0180  0.0142  182 LYS A C   
1354 O O   . LYS A 167 ? 0.3379 0.2963 0.3404 -0.0434 0.0214  0.0266  182 LYS A O   
1355 C CB  . LYS A 167 ? 0.3939 0.2924 0.3900 -0.0779 0.0348  0.0157  182 LYS A CB  
1356 C CG  . LYS A 167 ? 0.4240 0.3756 0.4854 -0.0981 0.0149  0.0392  182 LYS A CG  
1357 C CD  . LYS A 167 ? 0.5794 0.5431 0.6007 -0.0731 0.0172  0.0384  182 LYS A CD  
1358 C CE  . LYS A 167 ? 0.6316 0.5658 0.6460 -0.1172 0.0828  0.0921  182 LYS A CE  
1359 N NZ  . LYS A 167 ? 0.6310 0.6817 0.6331 -0.0972 0.1074  0.1313  182 LYS A NZ  
1360 N N   . GLU A 168 ? 0.3124 0.2682 0.3597 -0.0508 0.0202  0.0164  183 GLU A N   
1361 C CA  . GLU A 168 ? 0.2986 0.2672 0.3594 -0.0528 0.0344  0.0238  183 GLU A CA  
1362 C C   . GLU A 168 ? 0.3118 0.2929 0.3373 -0.0473 0.0202  0.0092  183 GLU A C   
1363 O O   . GLU A 168 ? 0.2873 0.2910 0.3645 -0.0456 0.0216  0.0101  183 GLU A O   
1364 C CB  . GLU A 168 ? 0.3223 0.2541 0.3731 -0.0328 0.0208  0.0259  183 GLU A CB  
1365 C CG  . GLU A 168 ? 0.3681 0.2823 0.4019 -0.0428 0.0001  0.0138  183 GLU A CG  
1366 C CD  . GLU A 168 ? 0.3885 0.3340 0.4237 -0.0407 0.0169  -0.0290 183 GLU A CD  
1367 O OE1 . GLU A 168 ? 0.4678 0.3869 0.4758 0.0526  -0.0139 -0.0915 183 GLU A OE1 
1368 O OE2 . GLU A 168 ? 0.4249 0.3404 0.4197 -0.0208 0.0000  -0.0225 183 GLU A OE2 
1369 N N   . TYR A 169 ? 0.2651 0.2632 0.3329 -0.0316 0.0154  0.0043  184 TYR A N   
1370 C CA  . TYR A 169 ? 0.2521 0.2734 0.3511 -0.0258 0.0174  -0.0008 184 TYR A CA  
1371 C C   . TYR A 169 ? 0.3196 0.2495 0.3544 -0.0492 0.0171  -0.0185 184 TYR A C   
1372 O O   . TYR A 169 ? 0.3022 0.2840 0.3574 -0.0278 0.0172  -0.0181 184 TYR A O   
1373 C CB  . TYR A 169 ? 0.2507 0.2738 0.3452 -0.0361 0.0130  0.0152  184 TYR A CB  
1374 C CG  . TYR A 169 ? 0.2922 0.2195 0.3312 -0.0020 0.0072  0.0335  184 TYR A CG  
1375 C CD1 . TYR A 169 ? 0.3051 0.2499 0.3136 -0.0166 -0.0006 -0.0020 184 TYR A CD1 
1376 C CD2 . TYR A 169 ? 0.3072 0.2723 0.3291 0.0160  -0.0026 0.0156  184 TYR A CD2 
1377 C CE1 . TYR A 169 ? 0.3148 0.2664 0.3691 -0.0156 -0.0054 -0.0019 184 TYR A CE1 
1378 C CE2 . TYR A 169 ? 0.2980 0.2939 0.3550 0.0274  0.0310  -0.0206 184 TYR A CE2 
1379 C CZ  . TYR A 169 ? 0.3537 0.2428 0.3681 -0.0054 0.0119  -0.0224 184 TYR A CZ  
1380 O OH  . TYR A 169 ? 0.4101 0.2955 0.3623 0.0325  0.0239  -0.0354 184 TYR A OH  
1381 N N   . ASN A 170 ? 0.2937 0.2758 0.3411 -0.0288 0.0401  -0.0283 185 ASN A N   
1382 C CA  . ASN A 170 ? 0.3350 0.3231 0.3479 -0.0533 0.0592  -0.0210 185 ASN A CA  
1383 C C   . ASN A 170 ? 0.3185 0.3659 0.3497 -0.0348 0.0680  -0.0512 185 ASN A C   
1384 O O   . ASN A 170 ? 0.3247 0.4074 0.4000 0.0091  0.0919  -0.0250 185 ASN A O   
1385 C CB  . ASN A 170 ? 0.3861 0.4169 0.3483 -0.0290 0.0888  -0.0038 185 ASN A CB  
1386 C CG  . ASN A 170 ? 0.5371 0.5181 0.4031 -0.0691 0.0464  -0.0167 185 ASN A CG  
1387 O OD1 . ASN A 170 ? 0.6819 0.7734 0.5736 -0.1309 0.1895  0.0478  185 ASN A OD1 
1388 N ND2 . ASN A 170 ? 0.3419 0.4172 0.3246 -0.1014 0.0701  -0.0538 185 ASN A ND2 
1389 N N   . ASP A 171 ? 0.3058 0.3487 0.3517 -0.0376 0.0533  -0.0080 186 ASP A N   
1390 C CA  . ASP A 171 ? 0.3303 0.3808 0.3592 -0.0538 0.0779  0.0067  186 ASP A CA  
1391 C C   . ASP A 171 ? 0.3542 0.3637 0.3742 -0.0614 0.0532  0.0330  186 ASP A C   
1392 O O   . ASP A 171 ? 0.3276 0.4590 0.4078 -0.0673 0.0372  0.0005  186 ASP A O   
1393 C CB  . ASP A 171 ? 0.3485 0.3401 0.3948 -0.0803 0.0523  0.0283  186 ASP A CB  
1394 C CG  . ASP A 171 ? 0.4176 0.4359 0.4271 -0.0499 0.0704  0.0170  186 ASP A CG  
1395 O OD1 . ASP A 171 ? 0.4837 0.5444 0.3874 -0.0763 0.0708  0.0291  186 ASP A OD1 
1396 O OD2 . ASP A 171 ? 0.5874 0.4691 0.5861 -0.0472 0.0723  0.0759  186 ASP A OD2 
1397 N N   . LYS A 172 ? 0.3267 0.3512 0.3360 -0.0939 0.0300  0.0094  187 LYS A N   
1398 C CA  . LYS A 172 ? 0.3085 0.3732 0.3466 -0.0707 0.0080  -0.0146 187 LYS A CA  
1399 C C   . LYS A 172 ? 0.3184 0.3995 0.3049 -0.0493 0.0129  -0.0220 187 LYS A C   
1400 O O   . LYS A 172 ? 0.2979 0.4025 0.3919 -0.0520 0.0168  0.0001  187 LYS A O   
1401 C CB  . LYS A 172 ? 0.3284 0.3225 0.3290 -0.0455 0.0036  -0.0102 187 LYS A CB  
1402 C CG  . LYS A 172 ? 0.3438 0.3050 0.4037 -0.0601 0.0201  0.0000  187 LYS A CG  
1403 C CD  . LYS A 172 ? 0.3689 0.3109 0.3387 -0.0397 -0.0022 -0.0311 187 LYS A CD  
1404 C CE  . LYS A 172 ? 0.3993 0.3094 0.4019 -0.0084 0.0101  -0.0107 187 LYS A CE  
1405 N NZ  . LYS A 172 ? 0.4404 0.3109 0.3913 -0.0018 -0.0053 -0.0266 187 LYS A NZ  
1406 N N   . MET A 173 ? 0.2987 0.3730 0.3575 -0.0220 0.0085  -0.0355 188 MET A N   
1407 C CA  . MET A 173 ? 0.3197 0.3846 0.3861 -0.0256 0.0183  0.0014  188 MET A CA  
1408 C C   . MET A 173 ? 0.3388 0.4545 0.4437 0.0066  0.0483  0.0120  188 MET A C   
1409 O O   . MET A 173 ? 0.3717 0.3905 0.5113 0.0290  0.0318  0.0289  188 MET A O   
1410 C CB  . MET A 173 ? 0.3370 0.4145 0.4093 -0.0237 0.0259  -0.0089 188 MET A CB  
1411 C CG  . MET A 173 ? 0.3719 0.3967 0.3496 -0.0446 0.0618  0.0097  188 MET A CG  
1412 S SD  . MET A 173 ? 0.3895 0.4143 0.4180 -0.0673 0.0420  -0.0349 188 MET A SD  
1413 C CE  . MET A 173 ? 0.3006 0.3624 0.3136 -0.0678 0.1025  -0.0166 188 MET A CE  
1414 N N   . LYS A 174 ? 0.3328 0.6135 0.4058 0.0526  0.0625  0.0538  189 LYS A N   
1415 C CA  . LYS A 174 ? 0.3687 0.7317 0.4279 0.1026  0.0949  0.0741  189 LYS A CA  
1416 C C   . LYS A 174 ? 0.3930 0.7308 0.4479 0.0358  0.1092  0.0996  189 LYS A C   
1417 O O   . LYS A 174 ? 0.4283 0.7847 0.5376 0.0569  0.1900  0.0203  189 LYS A O   
1418 C CB  . LYS A 174 ? 0.5014 0.8420 0.3939 0.1296  0.1285  0.0952  189 LYS A CB  
1419 C CG  . LYS A 174 ? 0.5810 0.9010 0.4727 0.1389  0.0434  0.1309  189 LYS A CG  
1420 C CD  . LYS A 174 ? 0.6562 0.9819 0.5123 0.2042  0.0519  0.1241  189 LYS A CD  
1421 C CE  . LYS A 174 ? 0.7202 1.0218 0.6910 0.1941  0.0226  0.1099  189 LYS A CE  
1422 N NZ  . LYS A 174 ? 0.8395 1.1088 0.8264 0.2216  0.0303  0.1216  189 LYS A NZ  
1423 N N   . ASN A 175 ? 0.3693 0.6114 0.4525 -0.0398 0.1095  0.0970  190 ASN A N   
1424 C CA  . ASN A 175 ? 0.3781 0.6108 0.5963 -0.0564 0.0746  0.0657  190 ASN A CA  
1425 C C   . ASN A 175 ? 0.3416 0.4946 0.5241 -0.0958 0.0680  -0.0135 190 ASN A C   
1426 O O   . ASN A 175 ? 0.4548 0.4494 0.6280 -0.1192 0.0194  -0.0105 190 ASN A O   
1427 C CB  . ASN A 175 ? 0.4101 0.6190 0.7160 -0.0840 0.0427  0.1067  190 ASN A CB  
1428 C CG  . ASN A 175 ? 0.4370 0.8066 0.8139 -0.0185 0.1253  0.1490  190 ASN A CG  
1429 O OD1 . ASN A 175 ? 0.5867 0.9610 1.0404 0.1576  0.1009  0.1671  190 ASN A OD1 
1430 N ND2 . ASN A 175 ? 0.5766 0.8817 0.8437 0.0053  0.1470  0.1034  190 ASN A ND2 
1431 N N   . GLY A 176 ? 0.3759 0.4758 0.4130 -0.0217 0.1110  -0.0334 191 GLY A N   
1432 C CA  . GLY A 176 ? 0.3244 0.4181 0.3825 -0.0204 0.0713  -0.0392 191 GLY A CA  
1433 C C   . GLY A 176 ? 0.3114 0.4037 0.3720 -0.0361 0.0938  -0.0221 191 GLY A C   
1434 O O   . GLY A 176 ? 0.3621 0.5295 0.4386 -0.0174 0.1455  -0.0281 191 GLY A O   
1435 N N   . ASP A 177 ? 0.2496 0.3510 0.3835 -0.0574 0.0718  -0.0371 192 ASP A N   
1436 C CA  . ASP A 177 ? 0.2201 0.3666 0.4570 -0.0607 0.0476  -0.0431 192 ASP A CA  
1437 C C   . ASP A 177 ? 0.2291 0.3519 0.4224 -0.0461 0.0614  -0.0709 192 ASP A C   
1438 O O   . ASP A 177 ? 0.2282 0.3664 0.4032 -0.0352 0.0428  -0.0446 192 ASP A O   
1439 C CB  . ASP A 177 ? 0.3127 0.4217 0.4790 -0.0185 -0.0023 -0.0954 192 ASP A CB  
1440 C CG  . ASP A 177 ? 0.3412 0.4728 0.5961 -0.0318 -0.0492 -0.1444 192 ASP A CG  
1441 O OD1 . ASP A 177 ? 0.3362 0.4280 0.6750 -0.0304 -0.0023 -0.1427 192 ASP A OD1 
1442 O OD2 . ASP A 177 ? 0.4896 0.5699 0.6929 -0.0128 -0.1333 -0.1997 192 ASP A OD2 
1443 N N   . GLU A 178 ? 0.2417 0.3839 0.4836 -0.0581 0.0761  -0.0730 193 GLU A N   
1444 C CA  . GLU A 178 ? 0.2448 0.3995 0.4933 -0.0258 0.0922  -0.0637 193 GLU A CA  
1445 C C   . GLU A 178 ? 0.2218 0.4167 0.4676 -0.0278 0.0595  -0.0828 193 GLU A C   
1446 O O   . GLU A 178 ? 0.2454 0.4266 0.4679 -0.0271 0.0488  -0.0875 193 GLU A O   
1447 C CB  . GLU A 178 ? 0.3202 0.4232 0.5882 -0.0564 0.1730  -0.0323 193 GLU A CB  
1448 C CG  . GLU A 178 ? 0.3996 0.5056 0.6949 -0.0278 0.1582  -0.0470 193 GLU A CG  
1449 C CD  . GLU A 178 ? 0.4416 0.5465 0.7418 -0.1035 0.1532  -0.0297 193 GLU A CD  
1450 O OE1 . GLU A 178 ? 0.4906 0.7335 0.7175 0.0687  0.1579  -0.0254 193 GLU A OE1 
1451 O OE2 . GLU A 178 ? 0.6300 0.6036 0.9433 -0.1104 0.1166  -0.0724 193 GLU A OE2 
1452 N N   . LYS A 179 ? 0.2291 0.4303 0.4523 -0.0341 0.0077  -0.0760 194 LYS A N   
1453 C CA  . LYS A 179 ? 0.2386 0.4010 0.4519 -0.0069 0.0175  -0.0666 194 LYS A CA  
1454 C C   . LYS A 179 ? 0.2585 0.4042 0.4223 -0.0192 0.0144  -0.0170 194 LYS A C   
1455 O O   . LYS A 179 ? 0.2277 0.4188 0.5053 -0.0175 -0.0182 0.0057  194 LYS A O   
1456 C CB  . LYS A 179 ? 0.3181 0.4737 0.5353 -0.1143 -0.0324 -0.0701 194 LYS A CB  
1457 C CG  . LYS A 179 ? 0.3855 0.5796 0.5623 -0.1157 -0.0007 -0.1328 194 LYS A CG  
1458 C CD  . LYS A 179 ? 0.4690 0.7117 0.5515 -0.1166 -0.0524 -0.1923 194 LYS A CD  
1459 C CE  . LYS A 179 ? 0.4727 0.7982 0.6639 -0.1310 -0.0588 -0.2019 194 LYS A CE  
1460 N NZ  . LYS A 179 ? 0.5589 0.8911 0.6805 -0.0955 -0.0725 -0.2252 194 LYS A NZ  
1461 N N   . TRP A 180 ? 0.2282 0.3767 0.3633 -0.0040 0.0263  -0.0140 195 TRP A N   
1462 C CA  . TRP A 180 ? 0.2355 0.3428 0.3315 -0.0053 0.0418  -0.0187 195 TRP A CA  
1463 C C   . TRP A 180 ? 0.2243 0.3148 0.3123 0.0015  0.0311  -0.0189 195 TRP A C   
1464 O O   . TRP A 180 ? 0.2348 0.3156 0.3463 -0.0201 0.0428  -0.0347 195 TRP A O   
1465 C CB  . TRP A 180 ? 0.2222 0.3375 0.3302 0.0007  0.0187  -0.0511 195 TRP A CB  
1466 C CG  . TRP A 180 ? 0.2427 0.3527 0.3453 -0.0016 0.0221  -0.0398 195 TRP A CG  
1467 C CD1 . TRP A 180 ? 0.2408 0.3949 0.3784 -0.0441 -0.0147 -0.0558 195 TRP A CD1 
1468 C CD2 . TRP A 180 ? 0.1892 0.4417 0.3667 -0.0422 0.0240  -0.0621 195 TRP A CD2 
1469 N NE1 . TRP A 180 ? 0.2676 0.3944 0.4024 -0.0404 -0.0066 -0.0850 195 TRP A NE1 
1470 C CE2 . TRP A 180 ? 0.2187 0.4200 0.3587 -0.0332 0.0200  -0.0403 195 TRP A CE2 
1471 C CE3 . TRP A 180 ? 0.2500 0.4720 0.3209 -0.0416 0.0634  0.0240  195 TRP A CE3 
1472 C CZ2 . TRP A 180 ? 0.2430 0.4924 0.3670 -0.0844 -0.0010 -0.0639 195 TRP A CZ2 
1473 C CZ3 . TRP A 180 ? 0.2470 0.4835 0.3409 -0.0724 0.0640  -0.0022 195 TRP A CZ3 
1474 C CH2 . TRP A 180 ? 0.2818 0.5178 0.2875 -0.0505 0.0346  -0.0131 195 TRP A CH2 
1475 N N   . ASN A 181 ? 0.2588 0.3017 0.3394 -0.0412 0.0585  -0.0313 196 ASN A N   
1476 C CA  . ASN A 181 ? 0.2883 0.2747 0.3195 -0.0082 0.0819  -0.0310 196 ASN A CA  
1477 C C   . ASN A 181 ? 0.3156 0.2799 0.3481 -0.0077 0.0918  -0.0178 196 ASN A C   
1478 O O   . ASN A 181 ? 0.3109 0.3379 0.3849 -0.0057 0.1116  -0.0224 196 ASN A O   
1479 C CB  . ASN A 181 ? 0.3624 0.3020 0.3383 -0.0215 0.1186  -0.0359 196 ASN A CB  
1480 C CG  . ASN A 181 ? 0.5122 0.3731 0.3645 -0.0302 0.1034  -0.0307 196 ASN A CG  
1481 O OD1 . ASN A 181 ? 0.5434 0.4280 0.4428 -0.0827 0.0604  -0.0520 196 ASN A OD1 
1482 N ND2 . ASN A 181 ? 0.5988 0.5138 0.4650 -0.0502 0.1843  -0.0380 196 ASN A ND2 
1483 N N   . SER A 182 ? 0.2471 0.2696 0.3480 -0.0014 0.0864  -0.0187 197 SER A N   
1484 C CA  . SER A 182 ? 0.2326 0.2733 0.3840 0.0001  0.0567  -0.0089 197 SER A CA  
1485 C C   . SER A 182 ? 0.2028 0.2654 0.3253 0.0172  0.0667  -0.0266 197 SER A C   
1486 O O   . SER A 182 ? 0.2119 0.2658 0.2930 0.0112  0.0617  -0.0364 197 SER A O   
1487 C CB  . SER A 182 ? 0.2363 0.3861 0.4119 -0.0153 -0.0040 0.0065  197 SER A CB  
1488 O OG  . SER A 182 ? 0.2995 0.3954 0.5080 -0.0218 -0.0067 0.0915  197 SER A OG  
1489 N N   . VAL A 183 ? 0.2362 0.2650 0.2954 0.0292  0.0910  -0.0334 198 VAL A N   
1490 C CA  . VAL A 183 ? 0.2370 0.2281 0.2764 0.0388  0.0820  -0.0273 198 VAL A CA  
1491 C C   . VAL A 183 ? 0.2518 0.2565 0.2545 0.0407  0.0586  -0.0470 198 VAL A C   
1492 O O   . VAL A 183 ? 0.2373 0.2289 0.2936 0.0149  0.0536  -0.0543 198 VAL A O   
1493 C CB  . VAL A 183 ? 0.3767 0.2766 0.2936 0.0670  0.0872  -0.0616 198 VAL A CB  
1494 C CG1 . VAL A 183 ? 0.4078 0.3051 0.3156 0.0392  0.0845  -0.0552 198 VAL A CG1 
1495 C CG2 . VAL A 183 ? 0.3814 0.2719 0.3299 0.0614  0.1161  -0.0097 198 VAL A CG2 
1496 N N   . LEU A 184 ? 0.2085 0.2669 0.2661 0.0357  0.0489  -0.0333 199 LEU A N   
1497 C CA  . LEU A 184 ? 0.2319 0.2584 0.2758 0.0130  0.0265  -0.0380 199 LEU A CA  
1498 C C   . LEU A 184 ? 0.2282 0.2396 0.2546 0.0138  0.0304  -0.0308 199 LEU A C   
1499 O O   . LEU A 184 ? 0.2186 0.2353 0.2800 -0.0011 0.0470  -0.0310 199 LEU A O   
1500 C CB  . LEU A 184 ? 0.2097 0.2701 0.3047 0.0291  0.0514  -0.0205 199 LEU A CB  
1501 C CG  . LEU A 184 ? 0.2221 0.2876 0.2859 0.0516  0.0342  -0.0127 199 LEU A CG  
1502 C CD1 . LEU A 184 ? 0.2319 0.3300 0.3222 0.0331  0.0304  0.0044  199 LEU A CD1 
1503 C CD2 . LEU A 184 ? 0.2381 0.3075 0.3106 0.0511  0.0372  -0.0158 199 LEU A CD2 
1504 N N   . TYR A 185 ? 0.1966 0.2356 0.2717 -0.0016 0.0662  -0.0337 200 TYR A N   
1505 C CA  . TYR A 185 ? 0.2226 0.2163 0.2333 0.0042  0.0340  -0.0513 200 TYR A CA  
1506 C C   . TYR A 185 ? 0.2336 0.2290 0.2322 0.0040  0.0393  -0.0273 200 TYR A C   
1507 O O   . TYR A 185 ? 0.2278 0.2422 0.2835 0.0088  0.0326  -0.0759 200 TYR A O   
1508 C CB  . TYR A 185 ? 0.2255 0.2314 0.2636 -0.0060 0.0294  -0.0503 200 TYR A CB  
1509 C CG  . TYR A 185 ? 0.1861 0.2515 0.2751 -0.0104 0.0376  -0.0403 200 TYR A CG  
1510 C CD1 . TYR A 185 ? 0.2131 0.2688 0.2954 -0.0158 0.0100  -0.0331 200 TYR A CD1 
1511 C CD2 . TYR A 185 ? 0.2078 0.3664 0.3361 -0.0302 0.0289  0.0444  200 TYR A CD2 
1512 C CE1 . TYR A 185 ? 0.2220 0.3138 0.3080 0.0081  0.0166  -0.0029 200 TYR A CE1 
1513 C CE2 . TYR A 185 ? 0.2112 0.4581 0.4184 -0.0500 -0.0165 0.0799  200 TYR A CE2 
1514 C CZ  . TYR A 185 ? 0.2138 0.4225 0.4145 -0.0288 -0.0221 0.0867  200 TYR A CZ  
1515 O OH  . TYR A 185 ? 0.2908 0.5928 0.4808 -0.0819 -0.0773 0.1666  200 TYR A OH  
1516 N N   . ASP A 186 ? 0.2223 0.2091 0.2486 0.0154  0.0322  -0.0460 201 ASP A N   
1517 C CA  . ASP A 186 ? 0.2607 0.1895 0.2413 0.0126  0.0294  -0.0418 201 ASP A CA  
1518 C C   . ASP A 186 ? 0.2216 0.2380 0.2396 0.0149  0.0564  -0.0482 201 ASP A C   
1519 O O   . ASP A 186 ? 0.2352 0.2107 0.2933 0.0128  0.0370  -0.0400 201 ASP A O   
1520 C CB  . ASP A 186 ? 0.2826 0.2051 0.2473 -0.0093 0.0334  -0.0468 201 ASP A CB  
1521 C CG  . ASP A 186 ? 0.2824 0.2456 0.2880 -0.0182 0.0214  -0.0324 201 ASP A CG  
1522 O OD1 . ASP A 186 ? 0.2661 0.2310 0.2728 0.0131  0.0236  -0.0369 201 ASP A OD1 
1523 O OD2 . ASP A 186 ? 0.3463 0.3153 0.2933 0.0011  0.0514  -0.0315 201 ASP A OD2 
1524 N N   . TYR A 187 ? 0.2245 0.2060 0.2635 0.0140  0.0456  -0.0535 202 TYR A N   
1525 C CA  . TYR A 187 ? 0.2081 0.1967 0.2993 0.0074  0.0529  -0.0406 202 TYR A CA  
1526 C C   . TYR A 187 ? 0.2433 0.2367 0.2948 0.0263  0.0476  -0.0499 202 TYR A C   
1527 O O   . TYR A 187 ? 0.2648 0.2318 0.3437 0.0027  0.0473  -0.0285 202 TYR A O   
1528 C CB  . TYR A 187 ? 0.2319 0.2347 0.2752 0.0079  0.0478  -0.0507 202 TYR A CB  
1529 C CG  . TYR A 187 ? 0.2243 0.2069 0.2805 0.0186  0.0431  -0.0384 202 TYR A CG  
1530 C CD1 . TYR A 187 ? 0.2550 0.1811 0.3473 -0.0027 0.0493  -0.0454 202 TYR A CD1 
1531 C CD2 . TYR A 187 ? 0.2564 0.2314 0.3187 -0.0030 0.0552  -0.0286 202 TYR A CD2 
1532 C CE1 . TYR A 187 ? 0.2445 0.2122 0.3508 -0.0049 0.0349  -0.0377 202 TYR A CE1 
1533 C CE2 . TYR A 187 ? 0.2643 0.2045 0.3228 -0.0087 0.0336  -0.0235 202 TYR A CE2 
1534 C CZ  . TYR A 187 ? 0.2548 0.2366 0.3076 0.0062  0.0102  -0.0237 202 TYR A CZ  
1535 O OH  . TYR A 187 ? 0.2349 0.2369 0.3639 0.0049  0.0054  -0.0223 202 TYR A OH  
1536 N N   . LYS A 188 ? 0.2503 0.2087 0.2816 0.0148  0.0092  -0.0579 203 LYS A N   
1537 C CA  . LYS A 188 ? 0.2385 0.2653 0.3079 0.0159  0.0022  -0.0723 203 LYS A CA  
1538 C C   . LYS A 188 ? 0.3293 0.2432 0.3230 0.0435  -0.0313 -0.0795 203 LYS A C   
1539 O O   . LYS A 188 ? 0.3601 0.2852 0.4064 0.0389  -0.0378 -0.1398 203 LYS A O   
1540 C CB  . LYS A 188 ? 0.2611 0.2578 0.2903 0.0133  -0.0108 -0.0806 203 LYS A CB  
1541 C CG  . LYS A 188 ? 0.2584 0.2772 0.3057 0.0138  0.0041  -0.0775 203 LYS A CG  
1542 C CD  . LYS A 188 ? 0.2920 0.2558 0.2931 0.0246  0.0040  -0.0815 203 LYS A CD  
1543 C CE  . LYS A 188 ? 0.3207 0.2423 0.3261 0.0313  0.0219  -0.0572 203 LYS A CE  
1544 N NZ  . LYS A 188 ? 0.3642 0.2701 0.3524 0.0389  0.0072  -0.0773 203 LYS A NZ  
1545 N N   . HIS A 189 ? 0.2765 0.2179 0.2749 0.0300  0.0169  -0.0794 204 HIS A N   
1546 C CA  . HIS A 189 ? 0.3245 0.2030 0.3098 0.0314  0.0190  -0.0825 204 HIS A CA  
1547 C C   . HIS A 189 ? 0.2968 0.2193 0.2717 0.0110  0.0040  -0.0707 204 HIS A C   
1548 O O   . HIS A 189 ? 0.2870 0.2429 0.2649 0.0414  0.0291  -0.0476 204 HIS A O   
1549 C CB  . HIS A 189 ? 0.3312 0.2700 0.2993 0.0311  0.0375  -0.0723 204 HIS A CB  
1550 C CG  . HIS A 189 ? 0.3731 0.3280 0.2835 0.0442  0.0726  -0.0773 204 HIS A CG  
1551 N ND1 . HIS A 189 ? 0.4785 0.3385 0.3571 0.0856  0.1120  -0.0513 204 HIS A ND1 
1552 C CD2 . HIS A 189 ? 0.3216 0.2959 0.2337 0.0321  0.0799  -0.0336 204 HIS A CD2 
1553 C CE1 . HIS A 189 ? 0.4230 0.3349 0.3024 0.0815  0.1741  -0.0441 204 HIS A CE1 
1554 N NE2 . HIS A 189 ? 0.4148 0.4414 0.3704 0.0275  0.1511  -0.0559 204 HIS A NE2 
1555 N N   . MET A 190 ? 0.3558 0.2385 0.3013 0.0215  0.0293  -0.0934 205 MET A N   
1556 C CA  . MET A 190 ? 0.3527 0.2520 0.3348 0.0246  0.0022  -0.0784 205 MET A CA  
1557 C C   . MET A 190 ? 0.2865 0.2331 0.3083 0.0366  0.0659  -0.0700 205 MET A C   
1558 O O   . MET A 190 ? 0.3570 0.2613 0.3295 -0.0061 0.0512  -0.0418 205 MET A O   
1559 C CB  . MET A 190 ? 0.3661 0.2775 0.3506 0.0319  0.0150  -0.0835 205 MET A CB  
1560 C CG  . MET A 190 ? 0.4430 0.3355 0.4354 0.0532  0.0482  -0.1450 205 MET A CG  
1561 S SD  . MET A 190 ? 0.4020 0.3635 0.5390 0.0534  0.1043  -0.0755 205 MET A SD  
1562 C CE  . MET A 190 ? 0.5444 0.2748 0.7129 -0.0205 -0.0470 -0.1228 205 MET A CE  
1563 N N   . ARG A 191 ? 0.2917 0.2359 0.3062 0.0483  0.0520  -0.0451 206 ARG A N   
1564 C CA  . ARG A 191 ? 0.2654 0.2631 0.3017 0.0221  0.0590  -0.0408 206 ARG A CA  
1565 C C   . ARG A 191 ? 0.2338 0.2721 0.2731 0.0078  0.0507  -0.0475 206 ARG A C   
1566 O O   . ARG A 191 ? 0.2389 0.2643 0.3042 0.0242  0.0740  -0.0415 206 ARG A O   
1567 C CB  . ARG A 191 ? 0.2859 0.3108 0.3246 0.0266  0.0912  -0.0581 206 ARG A CB  
1568 C CG  . ARG A 191 ? 0.3042 0.3476 0.3546 0.0514  0.0886  -0.0379 206 ARG A CG  
1569 C CD  . ARG A 191 ? 0.2777 0.3474 0.3508 0.0717  0.0889  -0.0381 206 ARG A CD  
1570 N NE  . ARG A 191 ? 0.3084 0.3293 0.3293 0.0694  0.0804  -0.0182 206 ARG A NE  
1571 C CZ  . ARG A 191 ? 0.3012 0.3070 0.3250 0.0490  0.0863  -0.0188 206 ARG A CZ  
1572 N NH1 . ARG A 191 ? 0.3077 0.3120 0.3532 0.0515  0.1074  -0.0129 206 ARG A NH1 
1573 N NH2 . ARG A 191 ? 0.3337 0.2745 0.3236 0.0513  0.0757  -0.0366 206 ARG A NH2 
1574 N N   . TYR A 192 ? 0.2263 0.2441 0.2554 0.0101  0.0561  -0.0519 207 TYR A N   
1575 C CA  . TYR A 192 ? 0.2165 0.2472 0.2389 0.0145  0.0294  -0.0562 207 TYR A CA  
1576 C C   . TYR A 192 ? 0.2324 0.2450 0.2500 0.0276  0.0639  -0.0495 207 TYR A C   
1577 O O   . TYR A 192 ? 0.2287 0.2305 0.2814 0.0252  0.0458  -0.0313 207 TYR A O   
1578 C CB  . TYR A 192 ? 0.2431 0.1960 0.2753 0.0069  0.0360  -0.0487 207 TYR A CB  
1579 C CG  . TYR A 192 ? 0.2162 0.1928 0.2774 0.0109  0.0421  -0.0527 207 TYR A CG  
1580 C CD1 . TYR A 192 ? 0.2173 0.2153 0.2617 -0.0022 0.0476  -0.0411 207 TYR A CD1 
1581 C CD2 . TYR A 192 ? 0.2050 0.2200 0.2918 -0.0084 0.0424  -0.0680 207 TYR A CD2 
1582 C CE1 . TYR A 192 ? 0.2214 0.2263 0.2643 0.0035  0.0445  -0.0627 207 TYR A CE1 
1583 C CE2 . TYR A 192 ? 0.2221 0.2372 0.2642 0.0116  0.0580  -0.0608 207 TYR A CE2 
1584 C CZ  . TYR A 192 ? 0.2532 0.2214 0.2442 0.0072  0.0452  -0.0554 207 TYR A CZ  
1585 O OH  . TYR A 192 ? 0.2424 0.2282 0.2955 0.0157  0.0589  -0.0759 207 TYR A OH  
1586 N N   . ILE A 193 ? 0.2183 0.2367 0.2651 0.0047  0.0314  -0.0292 208 ILE A N   
1587 C CA  . ILE A 193 ? 0.2267 0.2286 0.2534 0.0390  0.0565  -0.0429 208 ILE A CA  
1588 C C   . ILE A 193 ? 0.2271 0.2110 0.2630 0.0158  0.0274  -0.0224 208 ILE A C   
1589 O O   . ILE A 193 ? 0.2483 0.2342 0.3158 0.0334  0.0637  -0.0036 208 ILE A O   
1590 C CB  . ILE A 193 ? 0.2164 0.2852 0.2812 0.0332  0.0373  -0.0484 208 ILE A CB  
1591 C CG1 . ILE A 193 ? 0.1984 0.2732 0.2944 0.0343  0.0268  -0.0489 208 ILE A CG1 
1592 C CG2 . ILE A 193 ? 0.2583 0.2862 0.2566 0.0323  0.0049  -0.0659 208 ILE A CG2 
1593 C CD1 . ILE A 193 ? 0.2270 0.2846 0.2972 0.0240  0.0268  -0.0583 208 ILE A CD1 
1594 N N   . HIS A 194 ? 0.2386 0.1960 0.2800 0.0267  0.0610  -0.0064 209 HIS A N   
1595 C CA  . HIS A 194 ? 0.2535 0.2018 0.2502 -0.0003 0.0531  -0.0035 209 HIS A CA  
1596 C C   . HIS A 194 ? 0.2368 0.2058 0.2680 0.0099  0.0610  -0.0201 209 HIS A C   
1597 O O   . HIS A 194 ? 0.2179 0.2353 0.3009 0.0051  0.0725  -0.0464 209 HIS A O   
1598 C CB  . HIS A 194 ? 0.2400 0.2163 0.2626 -0.0122 0.0764  -0.0383 209 HIS A CB  
1599 C CG  . HIS A 194 ? 0.2158 0.2054 0.2552 0.0137  0.0503  -0.0200 209 HIS A CG  
1600 N ND1 . HIS A 194 ? 0.2631 0.2273 0.2677 0.0205  0.0698  -0.0188 209 HIS A ND1 
1601 C CD2 . HIS A 194 ? 0.2585 0.2053 0.2662 0.0410  0.0426  -0.0303 209 HIS A CD2 
1602 C CE1 . HIS A 194 ? 0.3022 0.2261 0.2621 -0.0029 0.0820  0.0092  209 HIS A CE1 
1603 N NE2 . HIS A 194 ? 0.2969 0.2150 0.2534 0.0040  0.0523  -0.0206 209 HIS A NE2 
1604 N N   . GLY A 195 ? 0.2261 0.2285 0.2682 0.0085  0.0444  -0.0399 210 GLY A N   
1605 C CA  . GLY A 195 ? 0.2426 0.2361 0.2813 0.0261  0.0585  -0.0481 210 GLY A CA  
1606 C C   . GLY A 195 ? 0.2201 0.2191 0.3209 0.0212  0.0735  -0.0491 210 GLY A C   
1607 O O   . GLY A 195 ? 0.2660 0.2294 0.3786 0.0037  0.0527  -0.0302 210 GLY A O   
1608 N N   . GLY A 196 ? 0.2105 0.2066 0.3703 0.0172  0.0768  -0.0547 211 GLY A N   
1609 C CA  . GLY A 196 ? 0.2634 0.1931 0.3966 0.0087  0.0764  -0.0411 211 GLY A CA  
1610 C C   . GLY A 196 ? 0.2365 0.2027 0.3750 0.0196  0.0756  -0.0212 211 GLY A C   
1611 O O   . GLY A 196 ? 0.2958 0.2072 0.4433 -0.0019 0.0932  -0.0119 211 GLY A O   
1612 N N   . TYR A 197 ? 0.2365 0.2100 0.3566 0.0017  0.0810  -0.0417 212 TYR A N   
1613 C CA  . TYR A 197 ? 0.2610 0.2097 0.3451 0.0222  0.0566  -0.0055 212 TYR A CA  
1614 C C   . TYR A 197 ? 0.2913 0.2186 0.3705 0.0194  0.0584  0.0209  212 TYR A C   
1615 O O   . TYR A 197 ? 0.2604 0.2707 0.3926 0.0166  0.0588  -0.0041 212 TYR A O   
1616 C CB  . TYR A 197 ? 0.2882 0.2013 0.3871 0.0247  0.0572  -0.0152 212 TYR A CB  
1617 C CG  . TYR A 197 ? 0.2556 0.1970 0.3547 0.0028  0.0599  -0.0118 212 TYR A CG  
1618 C CD1 . TYR A 197 ? 0.2660 0.2150 0.4184 0.0167  0.0815  -0.0018 212 TYR A CD1 
1619 C CD2 . TYR A 197 ? 0.2796 0.2144 0.3230 0.0025  0.0590  -0.0237 212 TYR A CD2 
1620 C CE1 . TYR A 197 ? 0.2951 0.1950 0.4261 0.0292  0.0854  0.0045  212 TYR A CE1 
1621 C CE2 . TYR A 197 ? 0.2510 0.2662 0.3249 0.0130  0.0704  -0.0166 212 TYR A CE2 
1622 C CZ  . TYR A 197 ? 0.2743 0.2626 0.3885 0.0235  0.0870  -0.0011 212 TYR A CZ  
1623 O OH  . TYR A 197 ? 0.2699 0.2713 0.3804 0.0488  0.0811  0.0184  212 TYR A OH  
1624 N N   . SER A 198 ? 0.2252 0.1995 0.3559 -0.0015 0.0908  -0.0250 213 SER A N   
1625 C CA  . SER A 198 ? 0.2287 0.2135 0.3708 0.0163  0.0825  -0.0405 213 SER A CA  
1626 C C   . SER A 198 ? 0.2445 0.2188 0.3501 0.0218  0.0980  -0.0205 213 SER A C   
1627 O O   . SER A 198 ? 0.2685 0.2052 0.3720 -0.0027 0.1132  -0.0289 213 SER A O   
1628 C CB  . SER A 198 ? 0.2268 0.2121 0.3618 0.0406  0.0872  -0.0306 213 SER A CB  
1629 O OG  . SER A 198 ? 0.2501 0.1883 0.4079 0.0022  0.0990  -0.0088 213 SER A OG  
1630 N N   . SER A 199 ? 0.2514 0.1853 0.3370 0.0163  0.0880  -0.0371 214 SER A N   
1631 C CA  . SER A 199 ? 0.2771 0.2337 0.4002 -0.0003 0.1165  -0.0239 214 SER A CA  
1632 C C   . SER A 199 ? 0.2627 0.2232 0.3368 -0.0034 0.1012  -0.0258 214 SER A C   
1633 O O   . SER A 199 ? 0.2750 0.2280 0.4369 -0.0248 0.1048  -0.0062 214 SER A O   
1634 C CB  . SER A 199 ? 0.3075 0.2708 0.3635 -0.0367 0.0939  -0.0138 214 SER A CB  
1635 O OG  . SER A 199 ? 0.3234 0.3129 0.4030 0.0262  0.1078  0.0127  214 SER A OG  
1636 N N   . TRP A 200 ? 0.2403 0.2349 0.3587 0.0077  0.0902  -0.0343 215 TRP A N   
1637 C CA  . TRP A 200 ? 0.2508 0.2250 0.3415 -0.0053 0.0926  -0.0281 215 TRP A CA  
1638 C C   . TRP A 200 ? 0.2574 0.2135 0.3647 -0.0264 0.0659  -0.0496 215 TRP A C   
1639 O O   . TRP A 200 ? 0.2595 0.2592 0.4576 -0.0127 0.0429  -0.1180 215 TRP A O   
1640 C CB  . TRP A 200 ? 0.2442 0.2231 0.3466 -0.0008 0.0575  -0.0465 215 TRP A CB  
1641 C CG  . TRP A 200 ? 0.2419 0.2489 0.3470 -0.0093 0.0765  -0.0410 215 TRP A CG  
1642 C CD1 . TRP A 200 ? 0.2525 0.2269 0.3369 -0.0075 0.0690  -0.0206 215 TRP A CD1 
1643 C CD2 . TRP A 200 ? 0.2319 0.2270 0.3358 0.0014  0.0724  -0.0296 215 TRP A CD2 
1644 N NE1 . TRP A 200 ? 0.2556 0.1895 0.3645 -0.0210 0.0718  -0.0357 215 TRP A NE1 
1645 C CE2 . TRP A 200 ? 0.2366 0.2355 0.3652 -0.0065 0.0669  -0.0472 215 TRP A CE2 
1646 C CE3 . TRP A 200 ? 0.2466 0.2647 0.3814 -0.0184 0.0601  -0.0234 215 TRP A CE3 
1647 C CZ2 . TRP A 200 ? 0.2552 0.2304 0.3705 0.0110  0.0825  -0.0435 215 TRP A CZ2 
1648 C CZ3 . TRP A 200 ? 0.2699 0.2217 0.4169 -0.0340 0.0892  -0.0169 215 TRP A CZ3 
1649 C CH2 . TRP A 200 ? 0.2432 0.2566 0.3979 -0.0021 0.0961  -0.0219 215 TRP A CH2 
1650 N N   . TRP A 201 ? 0.2519 0.2121 0.3863 -0.0022 0.0952  -0.0439 216 TRP A N   
1651 C CA  . TRP A 201 ? 0.2678 0.2187 0.3936 -0.0059 0.0961  -0.0286 216 TRP A CA  
1652 C C   . TRP A 201 ? 0.2484 0.2143 0.3992 -0.0073 0.0963  -0.0367 216 TRP A C   
1653 O O   . TRP A 201 ? 0.3018 0.2172 0.5091 -0.0313 0.1292  -0.0692 216 TRP A O   
1654 C CB  . TRP A 201 ? 0.2819 0.2006 0.3991 -0.0179 0.1016  -0.0449 216 TRP A CB  
1655 C CG  . TRP A 201 ? 0.2848 0.2289 0.3950 -0.0196 0.1159  -0.0482 216 TRP A CG  
1656 C CD1 . TRP A 201 ? 0.2968 0.2213 0.4108 -0.0237 0.0916  -0.0718 216 TRP A CD1 
1657 C CD2 . TRP A 201 ? 0.3169 0.2516 0.4310 -0.0034 0.1235  -0.0698 216 TRP A CD2 
1658 N NE1 . TRP A 201 ? 0.3234 0.2472 0.4789 -0.0194 0.1130  -0.0935 216 TRP A NE1 
1659 C CE2 . TRP A 201 ? 0.3339 0.2277 0.4568 -0.0138 0.1034  -0.1019 216 TRP A CE2 
1660 C CE3 . TRP A 201 ? 0.3894 0.2747 0.4076 -0.0186 0.0984  -0.0879 216 TRP A CE3 
1661 C CZ2 . TRP A 201 ? 0.3700 0.2588 0.4447 -0.0136 0.1015  -0.0999 216 TRP A CZ2 
1662 C CZ3 . TRP A 201 ? 0.3360 0.3279 0.4293 -0.0468 0.0923  -0.0863 216 TRP A CZ3 
1663 C CH2 . TRP A 201 ? 0.4098 0.3019 0.4757 -0.0211 0.0969  -0.1389 216 TRP A CH2 
1664 N N   . LEU A 202 ? 0.2565 0.1884 0.4188 0.0281  0.0775  -0.0213 217 LEU A N   
1665 C CA  . LEU A 202 ? 0.2468 0.2104 0.4477 0.0177  0.0880  0.0015  217 LEU A CA  
1666 C C   . LEU A 202 ? 0.2836 0.1950 0.4595 -0.0010 0.1011  -0.0150 217 LEU A C   
1667 O O   . LEU A 202 ? 0.3130 0.1860 0.5391 0.0101  0.1073  -0.0038 217 LEU A O   
1668 C CB  . LEU A 202 ? 0.2844 0.2175 0.4373 0.0165  0.1012  0.0432  217 LEU A CB  
1669 C CG  . LEU A 202 ? 0.2634 0.2339 0.4577 0.0339  0.0775  0.0388  217 LEU A CG  
1670 C CD1 . LEU A 202 ? 0.3207 0.2958 0.4830 0.0171  0.0735  0.0131  217 LEU A CD1 
1671 C CD2 . LEU A 202 ? 0.2730 0.2661 0.4936 0.0435  0.0985  0.0438  217 LEU A CD2 
1672 N N   . LEU A 203 ? 0.2943 0.2014 0.4883 -0.0149 0.0923  -0.0088 218 LEU A N   
1673 C CA  . LEU A 203 ? 0.3089 0.1796 0.5268 -0.0238 0.1115  0.0044  218 LEU A CA  
1674 C C   . LEU A 203 ? 0.2644 0.2389 0.5265 -0.0270 0.0942  -0.0174 218 LEU A C   
1675 O O   . LEU A 203 ? 0.3417 0.2479 0.6529 -0.0807 0.1011  -0.0126 218 LEU A O   
1676 C CB  . LEU A 203 ? 0.3063 0.2025 0.5165 -0.0268 0.1280  0.0369  218 LEU A CB  
1677 C CG  . LEU A 203 ? 0.3437 0.2344 0.5405 -0.0187 0.1369  0.0188  218 LEU A CG  
1678 C CD1 . LEU A 203 ? 0.2679 0.2397 0.5854 -0.0334 0.1230  -0.0179 218 LEU A CD1 
1679 C CD2 . LEU A 203 ? 0.3726 0.2956 0.5291 0.0201  0.1630  0.0414  218 LEU A CD2 
1680 N N   . GLU A 204 ? 0.3572 0.2139 0.5429 -0.0185 0.1196  -0.0176 219 GLU A N   
1681 C CA  . GLU A 204 ? 0.3254 0.2454 0.5480 -0.0363 0.0746  -0.0468 219 GLU A CA  
1682 C C   . GLU A 204 ? 0.3682 0.2891 0.5685 0.0065  0.0766  -0.0489 219 GLU A C   
1683 O O   . GLU A 204 ? 0.4967 0.2873 0.6611 -0.0016 0.0789  -0.0681 219 GLU A O   
1684 C CB  . GLU A 204 ? 0.3793 0.2699 0.5348 -0.0346 0.0479  -0.0202 219 GLU A CB  
1685 C CG  . GLU A 204 ? 0.3947 0.2567 0.5380 -0.0355 0.0766  -0.0369 219 GLU A CG  
1686 C CD  . GLU A 204 ? 0.4087 0.2625 0.5947 -0.0928 0.0190  -0.0039 219 GLU A CD  
1687 O OE1 . GLU A 204 ? 0.4950 0.3553 0.7897 -0.1337 0.0092  -0.0914 219 GLU A OE1 
1688 O OE2 . GLU A 204 ? 0.3735 0.2601 0.5263 -0.0512 0.0813  -0.0371 219 GLU A OE2 
1689 N N   . LYS A 205 ? 0.4140 0.2601 0.5803 0.0300  0.1015  -0.0710 220 LYS A N   
1690 C CA  . LYS A 205 ? 0.4663 0.3593 0.6906 0.1302  0.1302  -0.0427 220 LYS A CA  
1691 C C   . LYS A 205 ? 0.5136 0.3950 0.7815 0.1054  0.1355  -0.0138 220 LYS A C   
1692 O O   . LYS A 205 ? 0.6403 0.4473 0.9672 0.1721  0.1394  0.0103  220 LYS A O   
1693 C CB  . LYS A 205 ? 0.4927 0.3906 0.6860 0.1329  0.1190  -0.0667 220 LYS A CB  
1694 C CG  . LYS A 205 ? 0.6252 0.4787 0.7472 0.1246  0.1413  -0.0292 220 LYS A CG  
1695 C CD  . LYS A 205 ? 0.7117 0.4780 0.7784 0.1244  0.1550  -0.0835 220 LYS A CD  
1696 C CE  . LYS A 205 ? 0.8246 0.5798 0.8978 0.1393  0.1520  -0.1086 220 LYS A CE  
1697 N NZ  . LYS A 205 ? 0.9154 0.5629 0.9416 0.1099  0.1718  -0.1722 220 LYS A NZ  
1698 N N   . ILE A 206 ? 0.5723 0.3554 0.8015 0.0979  0.1337  0.0084  221 ILE A N   
1699 C CA  . ILE A 206 ? 0.7144 0.4476 0.8503 0.0699  0.1572  0.0322  221 ILE A CA  
1700 C C   . ILE A 206 ? 0.8994 0.4660 1.0315 -0.0122 0.1854  0.0244  221 ILE A C   
1701 O O   . ILE A 206 ? 0.9396 0.7609 1.0120 0.0179  0.2202  0.1582  221 ILE A O   
1702 C CB  . ILE A 206 ? 0.7610 0.3366 0.7414 0.0323  0.1730  0.0671  221 ILE A CB  
1703 C CG1 . ILE A 206 ? 0.7098 0.3656 0.6401 0.0028  0.1560  0.0852  221 ILE A CG1 
1704 C CG2 . ILE A 206 ? 0.8220 0.4993 0.7953 0.0095  0.1354  0.0699  221 ILE A CG2 
1705 C CD1 . ILE A 206 ? 0.7731 0.4436 0.7082 0.0424  0.1055  0.0701  221 ILE A CD1 
1706 N N   . LYS A 207 ? 0.9498 0.4323 1.1708 -0.0383 0.1522  -0.0569 222 LYS A N   
1707 C CA  . LYS A 207 ? 0.9681 0.5811 1.2854 -0.0416 0.1444  -0.1306 222 LYS A CA  
1708 C C   . LYS A 207 ? 1.0539 0.6551 1.2630 -0.0975 0.1829  -0.1913 222 LYS A C   
1709 O O   . LYS A 207 ? 1.1234 0.7381 1.2170 -0.1704 0.1865  -0.3474 222 LYS A O   
1710 C CB  . LYS A 207 ? 0.9903 0.4914 1.4280 0.0420  0.0797  -0.0828 222 LYS A CB  
1711 C CG  . LYS A 207 ? 0.9640 0.7023 1.5254 0.0813  0.0419  -0.0171 222 LYS A CG  
1712 C CD  . LYS A 207 ? 0.9063 0.7651 1.6559 0.1195  0.0922  -0.0167 222 LYS A CD  
1713 C CE  . LYS A 207 ? 0.8332 0.8768 1.7097 0.1580  0.1251  -0.0613 222 LYS A CE  
1714 N NZ  . LYS A 207 ? 0.7406 1.0091 1.7188 0.1041  0.1980  -0.0609 222 LYS A NZ  
1715 C C   . ACY B .   ? 0.3781 0.6095 0.9810 -0.0395 -0.1262 0.0160  301 ACY A C   
1716 O O   . ACY B .   ? 0.6055 0.6407 1.0384 0.0515  -0.0858 0.0421  301 ACY A O   
1717 O OXT . ACY B .   ? 0.4356 0.8017 1.0850 -0.0228 -0.2334 -0.0325 301 ACY A OXT 
1718 C CH3 . ACY B .   ? 0.5131 0.4730 0.9784 -0.0339 -0.0280 -0.0025 301 ACY A CH3 
1719 O O   . HOH C .   ? 0.6429 0.4226 0.5250 -0.0513 0.2346  -0.0784 401 HOH A O   
1720 O O   . HOH C .   ? 0.5376 0.9099 1.1562 0.0631  0.1154  0.2972  402 HOH A O   
1721 O O   . HOH C .   ? 0.4535 0.7954 0.9476 -0.0037 0.0449  0.0266  403 HOH A O   
1722 O O   . HOH C .   ? 0.7497 1.0065 0.7656 0.3671  0.0854  -0.0447 404 HOH A O   
1723 O O   . HOH C .   ? 0.7233 0.7977 0.4998 0.1294  -0.1842 -0.3456 405 HOH A O   
1724 O O   . HOH C .   ? 0.7363 0.6874 0.7615 -0.1555 -0.1947 0.0069  406 HOH A O   
1725 O O   . HOH C .   ? 0.6238 0.5218 0.4807 -0.0753 0.0272  0.0906  407 HOH A O   
1726 O O   . HOH C .   ? 0.5773 0.3473 0.7593 -0.0406 0.0711  -0.0576 408 HOH A O   
1727 O O   . HOH C .   ? 0.4694 0.6351 1.3604 -0.0867 0.0519  -0.0949 409 HOH A O   
1728 O O   . HOH C .   ? 0.4007 0.4165 0.4226 0.0646  0.0018  -0.1221 410 HOH A O   
1729 O O   . HOH C .   ? 0.4790 0.4672 0.6948 -0.0650 0.0986  -0.1371 411 HOH A O   
1730 O O   . HOH C .   ? 0.5772 1.2390 0.7526 -0.0837 0.0277  -0.2318 412 HOH A O   
1731 O O   . HOH C .   ? 0.4132 0.3176 0.3955 0.0291  0.0961  -0.0513 413 HOH A O   
1732 O O   . HOH C .   ? 0.6460 0.4840 0.5553 0.0861  -0.1199 -0.1711 414 HOH A O   
1733 O O   . HOH C .   ? 0.5685 0.7959 0.6587 0.2133  0.0033  0.0448  415 HOH A O   
1734 O O   . HOH C .   ? 0.2553 0.6120 0.6995 -0.0743 0.0886  0.0666  416 HOH A O   
1735 O O   . HOH C .   ? 0.4911 0.5402 0.5562 -0.1806 -0.0479 0.0343  417 HOH A O   
1736 O O   . HOH C .   ? 0.4205 0.8236 0.8753 0.4439  -0.0878 -0.1420 418 HOH A O   
1737 O O   . HOH C .   ? 0.4048 0.4670 0.5510 0.1193  -0.0029 -0.0295 419 HOH A O   
1738 O O   . HOH C .   ? 0.6048 0.6032 0.4404 0.0061  0.0975  0.0038  420 HOH A O   
1739 O O   . HOH C .   ? 0.3927 0.3315 0.5268 0.0704  -0.0032 -0.1182 421 HOH A O   
1740 O O   . HOH C .   ? 0.3236 0.4988 0.6093 -0.0259 0.0954  0.0216  422 HOH A O   
1741 O O   . HOH C .   ? 0.3224 0.4084 0.6457 0.0014  0.0385  -0.1024 423 HOH A O   
1742 O O   . HOH C .   ? 0.6325 0.4368 0.7536 -0.0131 -0.0688 0.0593  424 HOH A O   
1743 O O   . HOH C .   ? 0.4000 0.7461 0.8533 0.0994  -0.1249 -0.3783 425 HOH A O   
1744 O O   . HOH C .   ? 0.3030 0.5728 0.7112 -0.0063 -0.0097 0.0039  426 HOH A O   
1745 O O   . HOH C .   ? 0.2437 0.2351 0.2957 0.0189  0.0246  -0.0831 427 HOH A O   
1746 O O   . HOH C .   ? 0.5117 0.5558 0.5968 0.0373  -0.1990 -0.1036 428 HOH A O   
1747 O O   . HOH C .   ? 0.2572 0.2173 0.2933 0.0001  0.0320  -0.0428 429 HOH A O   
1748 O O   . HOH C .   ? 0.5754 0.8912 0.8573 0.0745  -0.0158 0.2690  430 HOH A O   
1749 O O   . HOH C .   ? 0.5829 0.5572 0.4282 0.0178  0.0098  -0.0413 431 HOH A O   
1750 O O   . HOH C .   ? 1.1002 0.5444 0.7824 0.0934  0.2928  -0.1163 432 HOH A O   
1751 O O   . HOH C .   ? 0.6315 0.5663 0.9037 -0.0150 -0.2903 -0.0425 433 HOH A O   
1752 O O   . HOH C .   ? 0.3654 0.5713 0.3250 0.0255  0.0148  -0.0878 434 HOH A O   
1753 O O   . HOH C .   ? 0.5594 0.5384 0.5288 0.0672  -0.1378 -0.0438 435 HOH A O   
1754 O O   . HOH C .   ? 0.5455 0.4978 0.9411 0.0475  -0.2773 -0.1917 436 HOH A O   
1755 O O   . HOH C .   ? 0.4508 0.9055 0.6370 -0.0910 -0.0330 0.3357  437 HOH A O   
1756 O O   . HOH C .   ? 0.2507 0.3066 0.3884 0.0248  0.0477  0.0358  438 HOH A O   
1757 O O   . HOH C .   ? 0.4597 0.4016 0.5104 0.0677  0.0374  -0.0338 439 HOH A O   
1758 O O   . HOH C .   ? 1.1976 1.1628 1.0092 0.0154  -0.0898 0.3496  440 HOH A O   
1759 O O   . HOH C .   ? 0.3102 0.2522 0.3804 0.0145  0.0328  -0.0309 441 HOH A O   
1760 O O   . HOH C .   ? 0.2634 0.2824 0.4884 -0.0164 -0.0142 0.0594  442 HOH A O   
1761 O O   . HOH C .   ? 0.2796 0.3034 0.4741 0.0269  0.0274  -0.0972 443 HOH A O   
1762 O O   . HOH C .   ? 0.2870 0.2826 0.3769 -0.0142 0.0224  -0.1154 444 HOH A O   
1763 O O   . HOH C .   ? 0.8574 0.4897 0.6374 0.0518  -0.0593 0.0799  445 HOH A O   
1764 O O   . HOH C .   ? 0.4210 0.6823 0.6919 0.0001  0.1536  -0.0287 446 HOH A O   
1765 O O   . HOH C .   ? 0.2911 0.2806 0.3088 -0.0119 0.0353  -0.0857 447 HOH A O   
1766 O O   . HOH C .   ? 0.3693 0.5903 0.4841 0.0056  0.1289  0.0844  448 HOH A O   
1767 O O   . HOH C .   ? 0.4656 0.5407 0.4837 -0.0386 0.1755  -0.1296 449 HOH A O   
1768 O O   . HOH C .   ? 0.5313 0.5644 0.3702 0.0820  0.0014  0.0430  450 HOH A O   
1769 O O   . HOH C .   ? 0.4481 0.7243 0.5760 -0.2472 0.1886  -0.2104 451 HOH A O   
1770 O O   . HOH C .   ? 0.4178 0.3516 0.4260 0.0071  0.0316  -0.0854 452 HOH A O   
1771 O O   . HOH C .   ? 0.2875 0.2348 0.4188 0.0391  0.0674  -0.0419 453 HOH A O   
1772 O O   . HOH C .   ? 0.4776 0.3276 0.5293 -0.0294 0.0739  0.0548  454 HOH A O   
1773 O O   . HOH C .   ? 0.7218 1.1297 0.7458 -0.0581 0.0179  -0.0508 455 HOH A O   
1774 O O   . HOH C .   ? 0.4506 0.3382 0.4769 -0.0055 -0.0402 -0.0995 456 HOH A O   
1775 O O   . HOH C .   ? 0.6857 0.6571 1.0085 -0.2969 -0.0994 0.0030  457 HOH A O   
1776 O O   . HOH C .   ? 0.4402 0.2899 0.4163 0.0266  0.0716  0.0193  458 HOH A O   
1777 O O   . HOH C .   ? 0.4006 0.5173 0.5946 -0.0542 0.0391  -0.0492 459 HOH A O   
1778 O O   . HOH C .   ? 0.2789 0.1950 0.3920 0.0000  0.0575  -0.0534 460 HOH A O   
1779 O O   . HOH C .   ? 0.5505 0.6551 0.6030 -0.2286 -0.1128 -0.0055 461 HOH A O   
1780 O O   . HOH C .   ? 0.2578 0.2285 0.3158 0.0035  0.0286  -0.0295 462 HOH A O   
1781 O O   . HOH C .   ? 0.3650 0.3498 0.4333 0.0391  0.0493  -0.1266 463 HOH A O   
1782 O O   . HOH C .   ? 0.5789 0.6781 0.4639 0.0619  0.0975  0.0756  464 HOH A O   
1783 O O   . HOH C .   ? 0.3061 0.2444 0.3971 0.0064  0.0685  -0.0332 465 HOH A O   
1784 O O   . HOH C .   ? 0.3049 0.3856 0.3660 -0.0462 0.0106  -0.0201 466 HOH A O   
1785 O O   . HOH C .   ? 0.2438 0.2258 0.3792 -0.0115 0.0772  -0.0447 467 HOH A O   
1786 O O   . HOH C .   ? 0.4551 0.4250 0.5774 -0.1101 0.1059  -0.1887 468 HOH A O   
1787 O O   . HOH C .   ? 0.6434 0.4621 0.3509 0.1689  0.0308  0.0266  469 HOH A O   
1788 O O   . HOH C .   ? 0.3593 0.3705 0.3407 -0.0261 0.0358  -0.0392 470 HOH A O   
1789 O O   . HOH C .   ? 0.2799 0.4855 0.5987 -0.0538 -0.0615 -0.0756 471 HOH A O   
1790 O O   . HOH C .   ? 0.3443 0.4165 0.3927 0.0560  0.0686  0.0288  472 HOH A O   
1791 O O   . HOH C .   ? 0.3759 0.3195 0.4098 -0.0473 -0.0792 0.0443  473 HOH A O   
1792 O O   . HOH C .   ? 0.4275 0.5010 0.4125 -0.1372 -0.0418 -0.0180 474 HOH A O   
1793 O O   . HOH C .   ? 0.3437 0.3644 0.4990 0.0451  0.0321  -0.0031 475 HOH A O   
1794 O O   . HOH C .   ? 0.3323 0.2970 0.4449 -0.0709 0.1176  -0.1641 476 HOH A O   
1795 O O   . HOH C .   ? 0.6192 0.3771 0.5428 -0.0591 -0.0433 -0.0414 477 HOH A O   
1796 O O   . HOH C .   ? 0.5842 0.4276 0.3655 0.0395  0.1341  -0.0365 478 HOH A O   
1797 O O   . HOH C .   ? 0.4876 0.5044 0.6243 0.1559  -0.1035 0.0320  479 HOH A O   
1798 O O   . HOH C .   ? 0.3883 0.2420 0.6016 0.0223  0.1495  -0.0483 480 HOH A O   
1799 O O   . HOH C .   ? 0.2839 0.2062 0.3925 -0.0255 0.0480  -0.0508 481 HOH A O   
1800 O O   . HOH C .   ? 0.2230 0.3146 0.3683 -0.0266 0.0423  -0.0579 482 HOH A O   
1801 O O   . HOH C .   ? 0.4297 0.2938 0.4419 -0.0031 0.0004  -0.0368 483 HOH A O   
1802 O O   . HOH C .   ? 0.3724 0.6558 0.7166 -0.0590 -0.0228 -0.1918 484 HOH A O   
1803 O O   . HOH C .   ? 0.4536 0.3244 0.8771 -0.0305 -0.0557 -0.0420 485 HOH A O   
1804 O O   . HOH C .   ? 0.3960 0.3652 0.5953 -0.0950 -0.0674 0.0024  486 HOH A O   
1805 O O   . HOH C .   ? 0.2339 0.4693 0.5699 -0.0412 0.0216  0.0732  487 HOH A O   
1806 O O   . HOH C .   ? 0.4463 0.2283 0.4586 -0.0257 -0.0284 -0.1069 488 HOH A O   
1807 O O   . HOH C .   ? 0.2490 0.2019 0.3188 -0.0051 0.0331  -0.0481 489 HOH A O   
1808 O O   . HOH C .   ? 0.3519 0.4724 0.7612 -0.0184 0.1229  0.1059  490 HOH A O   
1809 O O   . HOH C .   ? 0.4581 0.5089 0.5783 0.1397  0.0691  0.1080  491 HOH A O   
1810 O O   . HOH C .   ? 0.3460 0.5493 0.5237 0.0256  0.1718  0.0607  492 HOH A O   
1811 O O   . HOH C .   ? 0.7380 0.6094 1.1896 0.1482  -0.3127 -0.0800 493 HOH A O   
1812 O O   . HOH C .   ? 0.6050 0.5162 0.3581 -0.0754 0.0459  -0.0887 494 HOH A O   
1813 O O   . HOH C .   ? 0.6245 0.8456 0.7316 -0.0492 0.1675  0.0316  495 HOH A O   
1814 O O   . HOH C .   ? 0.5810 0.4882 0.7585 -0.0033 0.2157  -0.1273 496 HOH A O   
1815 O O   . HOH C .   ? 0.5130 0.5218 0.4682 -0.2468 0.0366  -0.1137 497 HOH A O   
1816 O O   . HOH C .   ? 0.7008 0.4148 0.8118 0.0878  -0.1218 -0.0670 498 HOH A O   
1817 O O   . HOH C .   ? 0.3261 0.2857 0.5702 0.0516  0.0457  -0.0395 499 HOH A O   
1818 O O   . HOH C .   ? 0.8947 0.5737 0.5029 -0.0281 0.0569  -0.0260 500 HOH A O   
1819 O O   . HOH C .   ? 0.5352 0.5503 0.4573 -0.0518 -0.0315 -0.0862 501 HOH A O   
1820 O O   . HOH C .   ? 0.4153 0.4007 0.6368 -0.0204 -0.0125 -0.1368 502 HOH A O   
1821 O O   . HOH C .   ? 0.4119 0.5694 0.5081 -0.0702 0.0797  0.0310  503 HOH A O   
1822 O O   . HOH C .   ? 0.6210 0.4030 0.7111 -0.0780 0.0297  0.0684  504 HOH A O   
1823 O O   . HOH C .   ? 0.3111 0.3111 0.3736 0.0285  0.0958  0.0250  505 HOH A O   
1824 O O   . HOH C .   ? 0.4423 0.3925 0.4906 -0.1133 -0.0374 0.0970  506 HOH A O   
1825 O O   . HOH C .   ? 0.3910 0.6659 0.6358 0.1043  0.0080  -0.3220 507 HOH A O   
1826 O O   . HOH C .   ? 1.1780 0.7293 0.4342 -0.0458 -0.0054 -0.0254 508 HOH A O   
1827 O O   . HOH C .   ? 0.4344 0.4476 0.4966 0.0901  0.2425  -0.0273 509 HOH A O   
1828 O O   . HOH C .   ? 0.7081 0.4796 0.3597 -0.1868 0.1820  -0.0846 510 HOH A O   
1829 O O   . HOH C .   ? 0.2507 0.2430 0.3300 -0.0003 0.0133  -0.0555 511 HOH A O   
1830 O O   . HOH C .   ? 0.3545 0.3503 0.9680 0.0338  0.0604  -0.0390 512 HOH A O   
1831 O O   . HOH C .   ? 0.3024 0.2516 0.4187 0.0409  0.1121  -0.0221 513 HOH A O   
1832 O O   . HOH C .   ? 0.7536 0.7310 0.9418 -0.1298 0.0620  -0.0431 514 HOH A O   
1833 O O   . HOH C .   ? 0.3526 0.4317 0.3934 -0.0470 0.0289  -0.0958 515 HOH A O   
1834 O O   . HOH C .   ? 0.5480 0.6168 0.8132 -0.0384 -0.2181 -0.0690 516 HOH A O   
1835 O O   . HOH C .   ? 0.3804 1.1093 0.5900 0.1398  0.0585  0.2091  517 HOH A O   
1836 O O   . HOH C .   ? 0.9273 0.4980 0.6707 0.0494  0.0046  0.0554  518 HOH A O   
1837 O O   . HOH C .   ? 0.2836 0.3513 0.3439 -0.0262 0.0056  -0.0287 519 HOH A O   
1838 O O   . HOH C .   ? 0.3167 0.2529 0.4223 -0.0002 0.1214  -0.0297 520 HOH A O   
1839 O O   . HOH C .   ? 0.4473 0.8024 0.5687 -0.0625 -0.0419 0.0613  521 HOH A O   
1840 O O   . HOH C .   ? 0.7800 0.5608 1.0804 0.0885  0.2306  -0.0402 522 HOH A O   
1841 O O   . HOH C .   ? 0.3979 0.5587 0.4254 -0.1436 0.0348  -0.1131 523 HOH A O   
1842 O O   . HOH C .   ? 0.6093 0.3958 0.4369 0.1105  0.2048  0.0009  524 HOH A O   
1843 O O   . HOH C .   ? 0.6960 0.4027 0.4986 0.1172  0.0513  -0.0641 525 HOH A O   
1844 O O   . HOH C .   ? 0.3900 0.3451 0.6239 0.0750  0.0585  -0.1258 526 HOH A O   
1845 O O   . HOH C .   ? 0.3949 0.3464 0.4881 0.0612  0.1518  0.0292  527 HOH A O   
1846 O O   . HOH C .   ? 0.3646 0.4881 0.4043 -0.0651 0.0200  -0.0253 528 HOH A O   
1847 O O   . HOH C .   ? 0.4478 0.7390 0.5963 0.1299  0.1158  -0.1648 529 HOH A O   
1848 O O   . HOH C .   ? 0.4968 0.7979 0.6283 -0.0611 0.1546  -0.0765 530 HOH A O   
1849 O O   . HOH C .   ? 0.8711 0.6353 0.8854 0.0630  -0.0786 0.0723  531 HOH A O   
1850 O O   . HOH C .   ? 0.3774 0.5475 0.5159 0.0299  -0.0174 0.1145  532 HOH A O   
1851 O O   . HOH C .   ? 0.8013 0.6199 0.7449 0.1904  0.1924  0.1713  533 HOH A O   
1852 O O   . HOH C .   ? 0.4524 0.5108 0.6775 -0.1615 0.1414  -0.2961 534 HOH A O   
1853 O O   . HOH C .   ? 0.5530 0.7536 0.6011 -0.0793 0.2056  0.2730  535 HOH A O   
1854 O O   . HOH C .   ? 0.5590 0.7466 0.5144 0.0540  0.0271  0.2836  536 HOH A O   
1855 O O   . HOH C .   ? 0.6140 0.3787 0.3584 0.0392  -0.0050 -0.1210 537 HOH A O   
1856 O O   . HOH C .   ? 0.5761 0.4736 0.4910 0.1303  -0.0477 0.0975  538 HOH A O   
1857 O O   . HOH C .   ? 0.5715 0.4999 0.4737 0.1426  0.0970  -0.0878 539 HOH A O   
1858 O O   . HOH C .   ? 0.4024 0.4745 0.6827 -0.1096 0.1669  -0.0661 540 HOH A O   
1859 O O   . HOH C .   ? 0.2871 0.6557 0.7712 0.0993  0.1142  -0.1517 541 HOH A O   
1860 O O   . HOH C .   ? 0.7637 1.1236 0.6068 -0.0479 -0.1973 -0.1668 542 HOH A O   
1861 O O   . HOH C .   ? 0.6681 0.7068 0.8466 -0.0576 -0.0165 0.0224  543 HOH A O   
1862 O O   . HOH C .   ? 0.6295 0.7848 0.9881 -0.0614 0.1996  -0.2682 544 HOH A O   
1863 O O   . HOH C .   ? 0.4525 0.4277 0.5464 -0.0862 0.0026  -0.1999 545 HOH A O   
1864 O O   . HOH C .   ? 0.6082 0.5584 1.0500 -0.1423 -0.0885 0.1130  546 HOH A O   
1865 O O   . HOH C .   ? 0.7253 0.6529 0.8806 0.0166  0.1349  -0.0979 547 HOH A O   
1866 O O   . HOH C .   ? 0.6042 0.8116 0.5711 0.0804  0.0073  0.1422  548 HOH A O   
1867 O O   . HOH C .   ? 0.3746 0.6466 0.4912 0.0728  0.0931  -0.1102 549 HOH A O   
1868 O O   . HOH C .   ? 0.7964 0.7317 0.6791 0.1295  0.0381  0.2427  550 HOH A O   
1869 O O   . HOH C .   ? 0.3996 0.3660 0.6880 -0.0477 0.1259  -0.1797 551 HOH A O   
1870 O O   . HOH C .   ? 0.5542 0.4986 0.8438 0.0384  -0.1652 -0.1016 552 HOH A O   
1871 O O   . HOH C .   ? 0.4409 0.3205 0.4537 -0.0390 0.0680  -0.0813 553 HOH A O   
1872 O O   . HOH C .   ? 0.7064 1.0927 0.8625 0.0618  0.1037  0.0191  554 HOH A O   
1873 O O   . HOH C .   ? 0.5806 0.6176 0.4709 -0.0946 0.0565  -0.0796 555 HOH A O   
1874 O O   . HOH C .   ? 0.7267 0.5216 1.0005 -0.0804 0.0724  -0.1096 556 HOH A O   
1875 O O   . HOH C .   ? 0.7931 0.6917 0.5404 0.2690  0.1984  0.1128  557 HOH A O   
1876 O O   . HOH C .   ? 0.7896 0.5436 0.6337 0.0787  -0.1064 -0.1069 558 HOH A O   
1877 O O   . HOH C .   ? 0.4178 0.5887 0.6825 0.0688  0.0051  -0.1888 559 HOH A O   
1878 O O   . HOH C .   ? 0.4160 0.7527 0.6277 -0.1498 0.0908  -0.1034 560 HOH A O   
1879 O O   . HOH C .   ? 0.4246 0.6712 0.5287 -0.0778 -0.0921 0.1165  561 HOH A O   
1880 O O   . HOH C .   ? 0.5295 0.7966 0.7138 -0.0733 -0.1799 0.3900  562 HOH A O   
1881 O O   . HOH C .   ? 0.5481 0.8766 0.7114 0.1584  0.1438  -0.2608 563 HOH A O   
1882 O O   . HOH C .   ? 0.7526 0.4242 0.8378 -0.0868 -0.4395 0.0826  564 HOH A O   
1883 O O   . HOH C .   ? 0.5261 0.5825 0.8158 0.0452  0.0657  -0.0355 565 HOH A O   
1884 O O   . HOH C .   ? 0.2888 0.4069 0.7015 0.0001  0.1317  -0.2038 566 HOH A O   
1885 O O   . HOH C .   ? 0.6434 0.6717 0.7775 0.0619  -0.3426 -0.2188 567 HOH A O   
1886 O O   . HOH C .   ? 0.5238 0.5097 0.5689 -0.1857 0.1377  -0.2271 568 HOH A O   
1887 O O   . HOH C .   ? 0.9424 0.4362 1.0237 0.2988  0.1905  -0.2574 569 HOH A O   
1888 O O   . HOH C .   ? 0.7697 0.5904 0.8647 0.1765  -0.2235 -0.0549 570 HOH A O   
1889 O O   . HOH C .   ? 0.5295 0.5985 0.7134 0.0154  0.0544  -0.2062 571 HOH A O   
1890 O O   . HOH C .   ? 0.4147 0.5271 0.5510 -0.0438 0.0085  -0.2085 572 HOH A O   
1891 O O   . HOH C .   ? 0.2361 0.2509 0.3535 0.0088  0.0119  -0.0445 573 HOH A O   
1892 O O   . HOH C .   ? 0.9451 0.5041 1.1951 -0.0041 0.2888  0.1677  574 HOH A O   
1893 O O   . HOH C .   ? 0.7463 0.5457 0.7706 -0.0618 0.1964  -0.2314 575 HOH A O   
1894 O O   . HOH C .   ? 0.4637 0.4538 0.4269 -0.0035 -0.0121 0.0117  576 HOH A O   
1895 O O   . HOH C .   ? 0.5271 1.0735 0.4782 0.0613  -0.0550 -0.1248 577 HOH A O   
1896 O O   . HOH C .   ? 0.4004 0.9656 0.7539 -0.1709 -0.0009 0.0521  578 HOH A O   
1897 O O   . HOH C .   ? 0.6681 0.6802 0.5404 -0.0124 0.1549  -0.0250 579 HOH A O   
1898 O O   . HOH C .   ? 0.7639 0.4608 0.9144 -0.0180 -0.0593 0.0087  580 HOH A O   
1899 O O   . HOH C .   ? 0.8802 0.4278 0.5618 -0.0006 0.1882  -0.1144 581 HOH A O   
1900 O O   . HOH C .   ? 0.5021 0.4590 0.6698 -0.0312 0.1727  -0.0957 582 HOH A O   
1901 O O   . HOH C .   ? 0.5780 0.7410 0.7203 -0.1165 0.1975  -0.2702 583 HOH A O   
1902 O O   . HOH C .   ? 0.4784 1.0347 1.0091 0.1667  0.1452  0.1597  584 HOH A O   
1903 O O   . HOH C .   ? 0.4621 0.7389 0.6911 -0.0215 0.1707  0.1017  585 HOH A O   
1904 O O   . HOH C .   ? 0.5179 0.7076 1.1669 -0.0584 0.3562  -0.0045 586 HOH A O   
1905 O O   . HOH C .   ? 1.1945 0.7368 0.6823 -0.3202 0.2930  -0.1156 587 HOH A O   
1906 O O   . HOH C .   ? 0.8861 0.3784 0.5102 0.1546  -0.1616 -0.1548 588 HOH A O   
1907 O O   . HOH C .   ? 0.4814 0.5172 0.5311 0.0588  0.1857  -0.0613 589 HOH A O   
1908 O O   . HOH C .   ? 0.9645 0.5908 0.6442 0.0764  0.0845  -0.0416 590 HOH A O   
1909 O O   . HOH C .   ? 0.7520 0.8274 0.6284 0.3488  0.1850  0.0114  591 HOH A O   
1910 O O   . HOH C .   ? 0.9575 0.5703 0.5462 0.2206  0.0489  -0.1656 592 HOH A O   
1911 O O   . HOH C .   ? 1.0630 0.8405 0.9825 -0.0318 -0.0268 0.0642  593 HOH A O   
1912 O O   . HOH C .   ? 0.4842 0.6346 0.4581 -0.0662 -0.0439 -0.0681 594 HOH A O   
1913 O O   . HOH C .   ? 0.7271 0.7059 0.4329 0.0528  0.0128  -0.0943 595 HOH A O   
1914 O O   . HOH C .   ? 1.0462 0.8043 0.6790 -0.3302 0.0463  0.1174  596 HOH A O   
1915 O O   . HOH C .   ? 0.3992 0.6232 0.4184 0.1038  0.1105  -0.0299 597 HOH A O   
1916 O O   . HOH C .   ? 0.3163 0.3879 0.4470 0.0298  -0.0148 -0.1032 598 HOH A O   
1917 O O   . HOH C .   ? 0.6125 0.6713 0.8938 -0.0354 0.0725  -0.0886 599 HOH A O   
1918 O O   . HOH C .   ? 0.5208 0.6758 0.6302 -0.0139 -0.0184 0.0180  600 HOH A O   
1919 O O   . HOH C .   ? 0.8624 0.5753 0.8814 0.1193  -0.2425 -0.0102 601 HOH A O   
1920 O O   . HOH C .   ? 0.8916 0.6531 0.5648 0.0947  0.2523  0.1464  602 HOH A O   
1921 O O   . HOH C .   ? 0.7603 0.6206 0.6530 -0.0991 -0.0993 -0.2204 603 HOH A O   
1922 O O   . HOH C .   ? 0.7924 0.7139 1.0178 -0.1341 0.3474  -0.0926 604 HOH A O   
1923 O O   . HOH C .   ? 0.6990 0.7711 0.8172 -0.2138 -0.0800 0.0495  605 HOH A O   
1924 O O   . HOH C .   ? 0.7802 0.7354 0.6180 -0.1336 0.1472  -0.0507 606 HOH A O   
1925 O O   . HOH C .   ? 1.0773 0.4998 0.8321 0.1179  0.0369  -0.1440 607 HOH A O   
1926 O O   . HOH C .   ? 0.4416 0.6480 0.6609 -0.0164 0.0927  -0.0097 608 HOH A O   
1927 O O   . HOH C .   ? 0.3342 0.8537 0.8154 -0.0377 0.0080  -0.2281 609 HOH A O   
1928 O O   . HOH C .   ? 0.5904 0.4977 0.5712 0.1025  -0.0601 -0.1502 610 HOH A O   
1929 O O   . HOH C .   ? 0.4965 0.5617 0.8033 -0.0784 0.0333  -0.0521 611 HOH A O   
1930 O O   . HOH C .   ? 0.5338 0.9401 0.9065 -0.2910 0.2928  0.0009  612 HOH A O   
1931 O O   . HOH C .   ? 0.8348 0.6575 0.5952 -0.2460 0.0123  0.0477  613 HOH A O   
1932 O O   . HOH C .   ? 0.4992 0.6867 0.5481 -0.1309 -0.1763 0.1151  614 HOH A O   
1933 O O   . HOH C .   ? 0.5723 0.6186 0.9210 0.0956  -0.2032 -0.2016 615 HOH A O   
1934 O O   . HOH C .   ? 0.7185 0.3642 0.6499 0.0018  0.2459  -0.0828 616 HOH A O   
1935 O O   . HOH C .   ? 0.5470 0.7045 0.5739 0.0184  -0.0613 0.1691  617 HOH A O   
1936 O O   . HOH C .   ? 0.5457 0.7097 0.8306 -0.1417 0.1539  0.0650  618 HOH A O   
1937 O O   . HOH C .   ? 0.8013 0.9395 0.8310 -0.1147 0.0139  0.0698  619 HOH A O   
1938 O O   . HOH C .   ? 0.6378 0.4838 1.1556 -0.0887 0.0029  -0.0326 620 HOH A O   
1939 O O   . HOH C .   ? 0.4416 0.7608 0.7095 -0.0590 0.1703  -0.1999 621 HOH A O   
1940 O O   . HOH C .   ? 0.5558 0.7030 0.7607 0.1669  0.2373  -0.1071 622 HOH A O   
1941 O O   . HOH C .   ? 0.6874 0.4463 0.7896 0.1358  0.0459  -0.0079 623 HOH A O   
1942 O O   . HOH C .   ? 0.6726 1.0011 0.5597 0.0102  0.0303  0.1353  624 HOH A O   
1943 O O   . HOH C .   ? 0.5853 0.7668 0.7946 0.0031  -0.0411 -0.2497 625 HOH A O   
# 
