data_9JGD
# 
_entry.id   9JGD 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9JGD         pdb_00009jgd 10.2210/pdb9jgd/pdb 
WWPDB D_1300051277 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JGD 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              spkanaujia@gmail.com 
_pdbx_contact_author.name_first         Shankar 
_pdbx_contact_author.name_last          Kanaujia 
_pdbx_contact_author.name_mi            P. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9179-5723 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Saha, S.'       1 0000-0001-9937-2629 
'Kanaujia, S.P.' 2 0000-0001-9179-5723 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            292 
_citation.language                  ? 
_citation.page_first                2338 
_citation.page_last                 2358 
_citation.title                     
;Structural analysis of the ribosome assembly factor Nep1, an N1-specific pseudouridine methyltransferase, reveals mechanistic insights.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.70005 
_citation.pdbx_database_id_PubMed   39918246 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Saha, S.'       1 ? 
primary 'Kanaujia, S.P.' 2 ? 
# 
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 'Ribosomal RNA small subunit methyltransferase Nep1' 26926.430 1  2.1.1.- ? ? ? 
2 non-polymer syn 'CHLORIDE ION'                                       35.453    1  ?       ? ? ? 
3 non-polymer syn "5'-DEOXY-5'-METHYLTHIOADENOSINE"                    297.334   1  ?       ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                       62.068    1  ?       ? ? ? 
5 non-polymer syn GLYCEROL                                             92.094    2  ?       ? ? ? 
6 non-polymer syn 'ACETATE ION'                                        59.044    1  ?       ? ? ? 
7 water       nat water                                                18.015    90 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '16S rRNA (pseudouridine-N1-)-methyltransferase Nep1' 
# 
_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       
;MEEKKRLHLIIADAELETVPPEILDHPAIVNYAKRRKKRPEKIILDSTYHHAALRQLEDGERRGRPDIVHICLLNALDSI
LNKEDRLRVYVHTRNDYVIYIKPETRLPRNYNRFIGLMENLFEKGAVPEDLELLRMEKKTLNELIEEINPDVVFIMHEEG
ELMIPKNFGKLLDKFKKPTVIVGGFPHGDFKSKVDGVKISLYREPLMAWTIVNEVIVSYEWEVIKKFKS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MEEKKRLHLIIADAELETVPPEILDHPAIVNYAKRRKKRPEKIILDSTYHHAALRQLEDGERRGRPDIVHICLLNALDSI
LNKEDRLRVYVHTRNDYVIYIKPETRLPRNYNRFIGLMENLFEKGAVPEDLELLRMEKKTLNELIEEINPDVVFIMHEEG
ELMIPKNFGKLLDKFKKPTVIVGGFPHGDFKSKVDGVKISLYREPLMAWTIVNEVIVSYEWEVIKKFKS
;
_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 'CHLORIDE ION'                    CL  
3 "5'-DEOXY-5'-METHYLTHIOADENOSINE" MTA 
4 1,2-ETHANEDIOL                    EDO 
5 GLYCEROL                          GOL 
6 'ACETATE ION'                     ACT 
7 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   GLU n 
1 4   LYS n 
1 5   LYS n 
1 6   ARG n 
1 7   LEU n 
1 8   HIS n 
1 9   LEU n 
1 10  ILE n 
1 11  ILE n 
1 12  ALA n 
1 13  ASP n 
1 14  ALA n 
1 15  GLU n 
1 16  LEU n 
1 17  GLU n 
1 18  THR n 
1 19  VAL n 
1 20  PRO n 
1 21  PRO n 
1 22  GLU n 
1 23  ILE n 
1 24  LEU n 
1 25  ASP n 
1 26  HIS n 
1 27  PRO n 
1 28  ALA n 
1 29  ILE n 
1 30  VAL n 
1 31  ASN n 
1 32  TYR n 
1 33  ALA n 
1 34  LYS n 
1 35  ARG n 
1 36  ARG n 
1 37  LYS n 
1 38  LYS n 
1 39  ARG n 
1 40  PRO n 
1 41  GLU n 
1 42  LYS n 
1 43  ILE n 
1 44  ILE n 
1 45  LEU n 
1 46  ASP n 
1 47  SER n 
1 48  THR n 
1 49  TYR n 
1 50  HIS n 
1 51  HIS n 
1 52  ALA n 
1 53  ALA n 
1 54  LEU n 
1 55  ARG n 
1 56  GLN n 
1 57  LEU n 
1 58  GLU n 
1 59  ASP n 
1 60  GLY n 
1 61  GLU n 
1 62  ARG n 
1 63  ARG n 
1 64  GLY n 
1 65  ARG n 
1 66  PRO n 
1 67  ASP n 
1 68  ILE n 
1 69  VAL n 
1 70  HIS n 
1 71  ILE n 
1 72  CYS n 
1 73  LEU n 
1 74  LEU n 
1 75  ASN n 
1 76  ALA n 
1 77  LEU n 
1 78  ASP n 
1 79  SER n 
1 80  ILE n 
1 81  LEU n 
1 82  ASN n 
1 83  LYS n 
1 84  GLU n 
1 85  ASP n 
1 86  ARG n 
1 87  LEU n 
1 88  ARG n 
1 89  VAL n 
1 90  TYR n 
1 91  VAL n 
1 92  HIS n 
1 93  THR n 
1 94  ARG n 
1 95  ASN n 
1 96  ASP n 
1 97  TYR n 
1 98  VAL n 
1 99  ILE n 
1 100 TYR n 
1 101 ILE n 
1 102 LYS n 
1 103 PRO n 
1 104 GLU n 
1 105 THR n 
1 106 ARG n 
1 107 LEU n 
1 108 PRO n 
1 109 ARG n 
1 110 ASN n 
1 111 TYR n 
1 112 ASN n 
1 113 ARG n 
1 114 PHE n 
1 115 ILE n 
1 116 GLY n 
1 117 LEU n 
1 118 MET n 
1 119 GLU n 
1 120 ASN n 
1 121 LEU n 
1 122 PHE n 
1 123 GLU n 
1 124 LYS n 
1 125 GLY n 
1 126 ALA n 
1 127 VAL n 
1 128 PRO n 
1 129 GLU n 
1 130 ASP n 
1 131 LEU n 
1 132 GLU n 
1 133 LEU n 
1 134 LEU n 
1 135 ARG n 
1 136 MET n 
1 137 GLU n 
1 138 LYS n 
1 139 LYS n 
1 140 THR n 
1 141 LEU n 
1 142 ASN n 
1 143 GLU n 
1 144 LEU n 
1 145 ILE n 
1 146 GLU n 
1 147 GLU n 
1 148 ILE n 
1 149 ASN n 
1 150 PRO n 
1 151 ASP n 
1 152 VAL n 
1 153 VAL n 
1 154 PHE n 
1 155 ILE n 
1 156 MET n 
1 157 HIS n 
1 158 GLU n 
1 159 GLU n 
1 160 GLY n 
1 161 GLU n 
1 162 LEU n 
1 163 MET n 
1 164 ILE n 
1 165 PRO n 
1 166 LYS n 
1 167 ASN n 
1 168 PHE n 
1 169 GLY n 
1 170 LYS n 
1 171 LEU n 
1 172 LEU n 
1 173 ASP n 
1 174 LYS n 
1 175 PHE n 
1 176 LYS n 
1 177 LYS n 
1 178 PRO n 
1 179 THR n 
1 180 VAL n 
1 181 ILE n 
1 182 VAL n 
1 183 GLY n 
1 184 GLY n 
1 185 PHE n 
1 186 PRO n 
1 187 HIS n 
1 188 GLY n 
1 189 ASP n 
1 190 PHE n 
1 191 LYS n 
1 192 SER n 
1 193 LYS n 
1 194 VAL n 
1 195 ASP n 
1 196 GLY n 
1 197 VAL n 
1 198 LYS n 
1 199 ILE n 
1 200 SER n 
1 201 LEU n 
1 202 TYR n 
1 203 ARG n 
1 204 GLU n 
1 205 PRO n 
1 206 LEU n 
1 207 MET n 
1 208 ALA n 
1 209 TRP n 
1 210 THR n 
1 211 ILE n 
1 212 VAL n 
1 213 ASN n 
1 214 GLU n 
1 215 VAL n 
1 216 ILE n 
1 217 VAL n 
1 218 SER n 
1 219 TYR n 
1 220 GLU n 
1 221 TRP n 
1 222 GLU n 
1 223 VAL n 
1 224 ILE n 
1 225 LYS n 
1 226 LYS n 
1 227 PHE n 
1 228 LYS n 
1 229 SER 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                   229 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'nep1, PH1379' 
_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      'Pyrococcus horikoshii OT3' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     70601 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              Rosetta 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET28a 
_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 
ACT non-polymer         . 'ACETATE ION'                     ?                               'C2 H3 O2 -1'     59.044  
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 
CL  non-polymer         . 'CHLORIDE ION'                    ?                               'Cl -1'           35.453  
CYS 'L-peptide linking' y CYSTEINE                          ?                               'C3 H7 N O2 S'    121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                    'ETHYLENE GLYCOL'               'C2 H6 O2'        62.068  
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  
GOL non-polymer         . GLYCEROL                          'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'        92.094  
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 
MTA non-polymer         . "5'-DEOXY-5'-METHYLTHIOADENOSINE" ?                               'C11 H15 N5 O3 S' 297.334 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   2   GLU GLU A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   HIS 8   8   8   HIS HIS A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  HIS 26  26  26  HIS HIS A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  TYR 32  32  32  TYR TYR A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  HIS 50  50  50  HIS HIS A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  HIS 70  70  70  HIS HIS A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  CYS 72  72  72  CYS CYS A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ARG 94  94  94  ARG ARG A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PRO 103 103 103 PRO PRO A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ARG 106 106 106 ARG ARG A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 PRO 128 128 128 PRO PRO A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 MET 156 156 156 MET MET A . n 
A 1 157 HIS 157 157 157 HIS HIS A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 MET 163 163 163 MET MET A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 HIS 187 187 187 HIS HIS A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 PHE 190 190 190 PHE PHE A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 TYR 202 202 202 TYR TYR A . n 
A 1 203 ARG 203 203 203 ARG ARG A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 MET 207 207 207 MET MET A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 TRP 209 209 209 TRP TRP A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 TRP 221 221 221 TRP TRP A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 LYS 225 225 225 LYS LYS A . n 
A 1 226 LYS 226 226 226 LYS LYS A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 LYS 228 228 ?   ?   ?   A . n 
A 1 229 SER 229 229 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        MTA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   MTA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CL  1  301 1  CL  CL  A . 
C 3 MTA 1  302 2  MTA MTA A . 
D 4 EDO 1  303 3  EDO EDO A . 
E 5 GOL 1  304 4  GOL GOL A . 
F 5 GOL 1  305 5  GOL GOL A . 
G 6 ACT 1  306 6  ACT ACT A . 
H 7 HOH 1  401 14 HOH HOH A . 
H 7 HOH 2  402 53 HOH HOH A . 
H 7 HOH 3  403 26 HOH HOH A . 
H 7 HOH 4  404 36 HOH HOH A . 
H 7 HOH 5  405 88 HOH HOH A . 
H 7 HOH 6  406 32 HOH HOH A . 
H 7 HOH 7  407 68 HOH HOH A . 
H 7 HOH 8  408 84 HOH HOH A . 
H 7 HOH 9  409 37 HOH HOH A . 
H 7 HOH 10 410 35 HOH HOH A . 
H 7 HOH 11 411 65 HOH HOH A . 
H 7 HOH 12 412 66 HOH HOH A . 
H 7 HOH 13 413 56 HOH HOH A . 
H 7 HOH 14 414 25 HOH HOH A . 
H 7 HOH 15 415 15 HOH HOH A . 
H 7 HOH 16 416 71 HOH HOH A . 
H 7 HOH 17 417 17 HOH HOH A . 
H 7 HOH 18 418 64 HOH HOH A . 
H 7 HOH 19 419 38 HOH HOH A . 
H 7 HOH 20 420 10 HOH HOH A . 
H 7 HOH 21 421 9  HOH HOH A . 
H 7 HOH 22 422 41 HOH HOH A . 
H 7 HOH 23 423 76 HOH HOH A . 
H 7 HOH 24 424 11 HOH HOH A . 
H 7 HOH 25 425 79 HOH HOH A . 
H 7 HOH 26 426 31 HOH HOH A . 
H 7 HOH 27 427 47 HOH HOH A . 
H 7 HOH 28 428 50 HOH HOH A . 
H 7 HOH 29 429 54 HOH HOH A . 
H 7 HOH 30 430 57 HOH HOH A . 
H 7 HOH 31 431 42 HOH HOH A . 
H 7 HOH 32 432 8  HOH HOH A . 
H 7 HOH 33 433 27 HOH HOH A . 
H 7 HOH 34 434 86 HOH HOH A . 
H 7 HOH 35 435 23 HOH HOH A . 
H 7 HOH 36 436 7  HOH HOH A . 
H 7 HOH 37 437 13 HOH HOH A . 
H 7 HOH 38 438 29 HOH HOH A . 
H 7 HOH 39 439 82 HOH HOH A . 
H 7 HOH 40 440 4  HOH HOH A . 
H 7 HOH 41 441 5  HOH HOH A . 
H 7 HOH 42 442 46 HOH HOH A . 
H 7 HOH 43 443 67 HOH HOH A . 
H 7 HOH 44 444 18 HOH HOH A . 
H 7 HOH 45 445 2  HOH HOH A . 
H 7 HOH 46 446 16 HOH HOH A . 
H 7 HOH 47 447 77 HOH HOH A . 
H 7 HOH 48 448 52 HOH HOH A . 
H 7 HOH 49 449 22 HOH HOH A . 
H 7 HOH 50 450 12 HOH HOH A . 
H 7 HOH 51 451 59 HOH HOH A . 
H 7 HOH 52 452 78 HOH HOH A . 
H 7 HOH 53 453 21 HOH HOH A . 
H 7 HOH 54 454 1  HOH HOH A . 
H 7 HOH 55 455 45 HOH HOH A . 
H 7 HOH 56 456 6  HOH HOH A . 
H 7 HOH 57 457 24 HOH HOH A . 
H 7 HOH 58 458 34 HOH HOH A . 
H 7 HOH 59 459 69 HOH HOH A . 
H 7 HOH 60 460 19 HOH HOH A . 
H 7 HOH 61 461 33 HOH HOH A . 
H 7 HOH 62 462 48 HOH HOH A . 
H 7 HOH 63 463 39 HOH HOH A . 
H 7 HOH 64 464 61 HOH HOH A . 
H 7 HOH 65 465 51 HOH HOH A . 
H 7 HOH 66 466 90 HOH HOH A . 
H 7 HOH 67 467 28 HOH HOH A . 
H 7 HOH 68 468 87 HOH HOH A . 
H 7 HOH 69 469 20 HOH HOH A . 
H 7 HOH 70 470 40 HOH HOH A . 
H 7 HOH 71 471 75 HOH HOH A . 
H 7 HOH 72 472 58 HOH HOH A . 
H 7 HOH 73 473 83 HOH HOH A . 
H 7 HOH 74 474 72 HOH HOH A . 
H 7 HOH 75 475 62 HOH HOH A . 
H 7 HOH 76 476 3  HOH HOH A . 
H 7 HOH 77 477 89 HOH HOH A . 
H 7 HOH 78 478 43 HOH HOH A . 
H 7 HOH 79 479 49 HOH HOH A . 
H 7 HOH 80 480 74 HOH HOH A . 
H 7 HOH 81 481 60 HOH HOH A . 
H 7 HOH 82 482 44 HOH HOH A . 
H 7 HOH 83 483 73 HOH HOH A . 
H 7 HOH 84 484 81 HOH HOH A . 
H 7 HOH 85 485 80 HOH HOH A . 
H 7 HOH 86 486 70 HOH HOH A . 
H 7 HOH 87 487 85 HOH HOH A . 
H 7 HOH 88 488 55 HOH HOH A . 
H 7 HOH 89 489 30 HOH HOH A . 
H 7 HOH 90 490 63 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 collection' ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? 3000     1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? 7.4.0    2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.9    3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? 2.8.3    4 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0267 5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? 0.9.4.1  6 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 4.2      7 
# 
_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                     9JGD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.240 
_cell.length_a_esd                 ? 
_cell.length_b                     113.240 
_cell.length_b_esd                 ? 
_cell.length_c                     102.820 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         9JGD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JGD 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47 
_exptl_crystal.description                  Trigonal 
_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              5.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.2M potassium sodium tartrate tetrahydrate, 0.1M sodium citrate tribasic dihydrate pH 5.6, 2.0 ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'VariMax HF' 
_diffrn_detector.detector                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU RAXIS IV++' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-22 
_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   1.5418 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JGD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.20 
_reflns.d_resolution_low                               70.97 
_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                                     13053 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.06 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.141 
_reflns.pdbx_Rpim_I_all                                0.040 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       160893 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.136 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.20 
_reflns_shell.d_res_low                                     2.27 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           13625 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1127 
_reflns_shell.percent_possible_obs                          100.0 
_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                               12.1 
_reflns_shell.pdbx_chi_squared                              1.45 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     5.1 
_reflns_shell.pdbx_Rrim_I_all                               0.576 
_reflns_shell.pdbx_Rpim_I_all                               0.164 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.952 
_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                                  0.552 
_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]                            -1.32 
_refine.aniso_B[1][2]                            -0.66 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -1.32 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            4.29 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               41.882 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.926 
_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                                 9JGD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             70.97 
_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                     12283 
_refine.ls_number_reflns_R_free                  669 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.20 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18860 
_refine.ls_R_factor_R_free                       0.24986 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18537 
_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          'MOLECULAR REPLACEMENT' 
_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                       0.285 
_refine.pdbx_overall_ESU_R_Free                  0.226 
_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                             15.044 
_refine.overall_SU_ML                            0.183 
_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                       2.20 
_refine_hist.d_res_low                        70.97 
_refine_hist.number_atoms_solvent             90 
_refine_hist.number_atoms_total               2002 
_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        1871 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         41 
_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' ? 0.009  0.012  1949 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1932 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.532  1.668  2626 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.524  1.582  4459 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.910  5.000  225  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.936  5.000  16   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.253 10.000 371  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.072  0.200  292  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  2202 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  419  ? 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' ? 2.596  2.609  904  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.590  2.604  903  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.016  4.663  1127 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.016  4.667  1128 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.768  3.213  1045 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.767  3.217  1046 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.029  5.613  1500 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 9.016  26.60  2207 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 9.021  26.55  2193 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? 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                       2.200 
_refine_ls_shell.d_res_low                        2.257 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             65 
_refine_ls_shell.number_reflns_R_work             866 
_refine_ls_shell.percent_reflns_obs               95.10 
_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                  0.538 
_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   20 
_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                  0.570 
# 
_struct.entry_id                     9JGD 
_struct.title                        
;Crystal structure of Nep1 in complex with 5'-methylthioadenosine from Pyrococcus horikoshii OT3
;
_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        9JGD 
_struct_keywords.text            
;Conserved arginine residues, Globular loop extension, Inter-subunit interactions, Nep1, N1-pseudouridine methyltransferase, Trefoil knot, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NEP1_PYRHO 
_struct_ref.pdbx_db_accession          O50087 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEEKKRLHLIIADAELETVPPEILDHPAIVNYAKRRKKRPEKIILDSTYHHAALRQLEDGERRGRPDIVHICLLNALDSI
LNKEDRLRVYVHTRNDYVIYIKPETRLPRNYNRFIGLMENLFEKGAVPEDLELLRMEKKTLNELIEEINPDVVFIMHEEG
ELMIPKNFGKLLDKFKKPTVIVGGFPHGDFKSKVDGVKISLYREPLMAWTIVNEVIVSYEWEVIKKFKS
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9JGD 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 229 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O50087 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  229 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       229 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6560  ? 
1 MORE         -27   ? 
1 'SSA (A^2)'  19380 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z              1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000 0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 10_454 y-1/3,x+1/3,-z-2/3 -0.5000000000 0.8660254038 0.0000000000 -56.6200000000 0.8660254038 
0.5000000000 0.0000000000 32.6895722415 0.0000000000 0.0000000000 -1.0000000000 -68.5466666667 
# 
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 PRO A 20  ? LEU A 24  ? PRO A 20  LEU A 24  5 ? 5  
HELX_P HELX_P2  AA2 HIS A 26  ? ARG A 36  ? HIS A 26  ARG A 36  1 ? 11 
HELX_P HELX_P3  AA3 ARG A 39  ? ILE A 43  ? ARG A 39  ILE A 43  5 ? 5  
HELX_P HELX_P4  AA4 ASP A 46  ? HIS A 51  ? ASP A 46  HIS A 51  1 ? 6  
HELX_P HELX_P5  AA5 ALA A 52  ? LEU A 54  ? ALA A 52  LEU A 54  5 ? 3  
HELX_P HELX_P6  AA6 ASP A 59  ? ARG A 63  ? ASP A 59  ARG A 63  5 ? 5  
HELX_P HELX_P7  AA7 ARG A 65  ? ASP A 78  ? ARG A 65  ASP A 78  1 ? 14 
HELX_P HELX_P8  AA8 SER A 79  ? GLU A 84  ? SER A 79  GLU A 84  1 ? 6  
HELX_P HELX_P9  AA9 ASN A 110 ? GLY A 125 ? ASN A 110 GLY A 125 1 ? 16 
HELX_P HELX_P10 AB1 THR A 140 ? ASN A 149 ? THR A 140 ASN A 149 1 ? 10 
HELX_P HELX_P11 AB2 ILE A 164 ? ASP A 173 ? ILE A 164 ASP A 173 1 ? 10 
HELX_P HELX_P12 AB3 MET A 207 ? ILE A 224 ? MET A 207 ILE A 224 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          VAL 
_struct_mon_prot_cis.label_seq_id           127 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           VAL 
_struct_mon_prot_cis.auth_seq_id            127 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    128 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     128 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -25.05 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   9 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 126 ? VAL A 127 ? ALA A 126 VAL A 127 
AA1 2 LEU A 134 ? LYS A 138 ? LEU A 134 LYS A 138 
AA1 3 TYR A 97  ? ILE A 101 ? TYR A 97  ILE A 101 
AA1 4 LEU A 87  ? THR A 93  ? LEU A 87  THR A 93  
AA1 5 LEU A 7   ? ALA A 14  ? LEU A 7   ALA A 14  
AA1 6 PRO A 178 ? GLY A 183 ? PRO A 178 GLY A 183 
AA1 7 VAL A 152 ? MET A 156 ? VAL A 152 MET A 156 
AA1 8 VAL A 197 ? SER A 200 ? VAL A 197 SER A 200 
AA1 9 GLU A 161 ? LEU A 162 ? GLU A 161 LEU A 162 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 127 ? N VAL A 127 O LEU A 134 ? O LEU A 134 
AA1 2 3 O GLU A 137 ? O GLU A 137 N VAL A 98  ? N VAL A 98  
AA1 3 4 O ILE A 99  ? O ILE A 99  N VAL A 91  ? N VAL A 91  
AA1 4 5 O HIS A 92  ? O HIS A 92  N ALA A 14  ? N ALA A 14  
AA1 5 6 N HIS A 8   ? N HIS A 8   O VAL A 180 ? O VAL A 180 
AA1 6 7 O THR A 179 ? O THR A 179 N PHE A 154 ? N PHE A 154 
AA1 7 8 N ILE A 155 ? N ILE A 155 O VAL A 197 ? O VAL A 197 
AA1 8 9 O LYS A 198 ? O LYS A 198 N GLU A 161 ? N GLU A 161 
# 
_pdbx_entry_details.entry_id                   9JGD 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 451 ? ? O A HOH 453 ? ? 2.14 
2 1 O A HOH 470 ? ? O A HOH 475 ? ? 2.15 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     416 
_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    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     416 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              1.68 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 139 ? ? -175.63 140.89 
2 1 LYS A 177 ? ? -149.41 57.29  
3 1 TYR A 202 ? ? 178.06  149.56 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 65  ? ? 0.093 'SIDE CHAIN' 
2 1 ARG A 94  ? ? 0.119 'SIDE CHAIN' 
3 1 ARG A 109 ? ? 0.091 'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 468 ? H HOH . 
2 1 A HOH 474 ? H HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -16.4452 
_pdbx_refine_tls.origin_y         12.2807 
_pdbx_refine_tls.origin_z         -32.5755 
_pdbx_refine_tls.T[1][1]          0.0215 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0187 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0076 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0300 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0180 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0610 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.4904 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.5618 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1161 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.0369 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.2051 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.5863 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0642 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0157 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0728 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0734 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0822 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0807 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0255 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0359 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0180 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     2 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     227 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A LYS 228 ? A LYS 228 
3 1 Y 1 A SER 229 ? A SER 229 
# 
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 
ACT C      C  N N 1   
ACT O      O  N N 2   
ACT OXT    O  N N 3   
ACT CH3    C  N N 4   
ACT H1     H  N N 5   
ACT H2     H  N N 6   
ACT H3     H  N N 7   
ALA N      N  N N 8   
ALA CA     C  N S 9   
ALA C      C  N N 10  
ALA O      O  N N 11  
ALA CB     C  N N 12  
ALA OXT    O  N N 13  
ALA H      H  N N 14  
ALA H2     H  N N 15  
ALA HA     H  N N 16  
ALA HB1    H  N N 17  
ALA HB2    H  N N 18  
ALA HB3    H  N N 19  
ALA HXT    H  N N 20  
ARG N      N  N N 21  
ARG CA     C  N S 22  
ARG C      C  N N 23  
ARG O      O  N N 24  
ARG CB     C  N N 25  
ARG CG     C  N N 26  
ARG CD     C  N N 27  
ARG NE     N  N N 28  
ARG CZ     C  N N 29  
ARG NH1    N  N N 30  
ARG NH2    N  N N 31  
ARG OXT    O  N N 32  
ARG H      H  N N 33  
ARG H2     H  N N 34  
ARG HA     H  N N 35  
ARG HB2    H  N N 36  
ARG HB3    H  N N 37  
ARG HG2    H  N N 38  
ARG HG3    H  N N 39  
ARG HD2    H  N N 40  
ARG HD3    H  N N 41  
ARG HE     H  N N 42  
ARG HH11   H  N N 43  
ARG HH12   H  N N 44  
ARG HH21   H  N N 45  
ARG HH22   H  N N 46  
ARG HXT    H  N N 47  
ASN N      N  N N 48  
ASN CA     C  N S 49  
ASN C      C  N N 50  
ASN O      O  N N 51  
ASN CB     C  N N 52  
ASN CG     C  N N 53  
ASN OD1    O  N N 54  
ASN ND2    N  N N 55  
ASN OXT    O  N N 56  
ASN H      H  N N 57  
ASN H2     H  N N 58  
ASN HA     H  N N 59  
ASN HB2    H  N N 60  
ASN HB3    H  N N 61  
ASN HD21   H  N N 62  
ASN HD22   H  N N 63  
ASN HXT    H  N N 64  
ASP N      N  N N 65  
ASP CA     C  N S 66  
ASP C      C  N N 67  
ASP O      O  N N 68  
ASP CB     C  N N 69  
ASP CG     C  N N 70  
ASP OD1    O  N N 71  
ASP OD2    O  N N 72  
ASP OXT    O  N N 73  
ASP H      H  N N 74  
ASP H2     H  N N 75  
ASP HA     H  N N 76  
ASP HB2    H  N N 77  
ASP HB3    H  N N 78  
ASP HD2    H  N N 79  
ASP HXT    H  N N 80  
CL  CL     CL 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  
EDO C1     C  N N 96  
EDO O1     O  N N 97  
EDO C2     C  N N 98  
EDO O2     O  N N 99  
EDO H11    H  N N 100 
EDO H12    H  N N 101 
EDO HO1    H  N N 102 
EDO H21    H  N N 103 
EDO H22    H  N N 104 
EDO HO2    H  N N 105 
GLN N      N  N N 106 
GLN CA     C  N S 107 
GLN C      C  N N 108 
GLN O      O  N N 109 
GLN CB     C  N N 110 
GLN CG     C  N N 111 
GLN CD     C  N N 112 
GLN OE1    O  N N 113 
GLN NE2    N  N N 114 
GLN OXT    O  N N 115 
GLN H      H  N N 116 
GLN H2     H  N N 117 
GLN HA     H  N N 118 
GLN HB2    H  N N 119 
GLN HB3    H  N N 120 
GLN HG2    H  N N 121 
GLN HG3    H  N N 122 
GLN HE21   H  N N 123 
GLN HE22   H  N N 124 
GLN HXT    H  N N 125 
GLU N      N  N N 126 
GLU CA     C  N S 127 
GLU C      C  N N 128 
GLU O      O  N N 129 
GLU CB     C  N N 130 
GLU CG     C  N N 131 
GLU CD     C  N N 132 
GLU OE1    O  N N 133 
GLU OE2    O  N N 134 
GLU OXT    O  N N 135 
GLU H      H  N N 136 
GLU H2     H  N N 137 
GLU HA     H  N N 138 
GLU HB2    H  N N 139 
GLU HB3    H  N N 140 
GLU HG2    H  N N 141 
GLU HG3    H  N N 142 
GLU HE2    H  N N 143 
GLU HXT    H  N N 144 
GLY N      N  N N 145 
GLY CA     C  N N 146 
GLY C      C  N N 147 
GLY O      O  N N 148 
GLY OXT    O  N N 149 
GLY H      H  N N 150 
GLY H2     H  N N 151 
GLY HA2    H  N N 152 
GLY HA3    H  N N 153 
GLY HXT    H  N N 154 
GOL C1     C  N N 155 
GOL O1     O  N N 156 
GOL C2     C  N N 157 
GOL O2     O  N N 158 
GOL C3     C  N N 159 
GOL O3     O  N N 160 
GOL H11    H  N N 161 
GOL H12    H  N N 162 
GOL HO1    H  N N 163 
GOL H2     H  N N 164 
GOL HO2    H  N N 165 
GOL H31    H  N N 166 
GOL H32    H  N N 167 
GOL HO3    H  N N 168 
HIS N      N  N N 169 
HIS CA     C  N S 170 
HIS C      C  N N 171 
HIS O      O  N N 172 
HIS CB     C  N N 173 
HIS CG     C  Y N 174 
HIS ND1    N  Y N 175 
HIS CD2    C  Y N 176 
HIS CE1    C  Y N 177 
HIS NE2    N  Y N 178 
HIS OXT    O  N N 179 
HIS H      H  N N 180 
HIS H2     H  N N 181 
HIS HA     H  N N 182 
HIS HB2    H  N N 183 
HIS HB3    H  N N 184 
HIS HD1    H  N N 185 
HIS HD2    H  N N 186 
HIS HE1    H  N N 187 
HIS HE2    H  N N 188 
HIS HXT    H  N N 189 
HOH O      O  N N 190 
HOH H1     H  N N 191 
HOH H2     H  N N 192 
ILE N      N  N N 193 
ILE CA     C  N S 194 
ILE C      C  N N 195 
ILE O      O  N N 196 
ILE CB     C  N S 197 
ILE CG1    C  N N 198 
ILE CG2    C  N N 199 
ILE CD1    C  N N 200 
ILE OXT    O  N N 201 
ILE H      H  N N 202 
ILE H2     H  N N 203 
ILE HA     H  N N 204 
ILE HB     H  N N 205 
ILE HG12   H  N N 206 
ILE HG13   H  N N 207 
ILE HG21   H  N N 208 
ILE HG22   H  N N 209 
ILE HG23   H  N N 210 
ILE HD11   H  N N 211 
ILE HD12   H  N N 212 
ILE HD13   H  N N 213 
ILE HXT    H  N N 214 
LEU N      N  N N 215 
LEU CA     C  N S 216 
LEU C      C  N N 217 
LEU O      O  N N 218 
LEU CB     C  N N 219 
LEU CG     C  N N 220 
LEU CD1    C  N N 221 
LEU CD2    C  N N 222 
LEU OXT    O  N N 223 
LEU H      H  N N 224 
LEU H2     H  N N 225 
LEU HA     H  N N 226 
LEU HB2    H  N N 227 
LEU HB3    H  N N 228 
LEU HG     H  N N 229 
LEU HD11   H  N N 230 
LEU HD12   H  N N 231 
LEU HD13   H  N N 232 
LEU HD21   H  N N 233 
LEU HD22   H  N N 234 
LEU HD23   H  N N 235 
LEU HXT    H  N N 236 
LYS N      N  N N 237 
LYS CA     C  N S 238 
LYS C      C  N N 239 
LYS O      O  N N 240 
LYS CB     C  N N 241 
LYS CG     C  N N 242 
LYS CD     C  N N 243 
LYS CE     C  N N 244 
LYS NZ     N  N N 245 
LYS OXT    O  N N 246 
LYS H      H  N N 247 
LYS H2     H  N N 248 
LYS HA     H  N N 249 
LYS HB2    H  N N 250 
LYS HB3    H  N N 251 
LYS HG2    H  N N 252 
LYS HG3    H  N N 253 
LYS HD2    H  N N 254 
LYS HD3    H  N N 255 
LYS HE2    H  N N 256 
LYS HE3    H  N N 257 
LYS HZ1    H  N N 258 
LYS HZ2    H  N N 259 
LYS HZ3    H  N N 260 
LYS HXT    H  N N 261 
MET N      N  N N 262 
MET CA     C  N S 263 
MET C      C  N N 264 
MET O      O  N N 265 
MET CB     C  N N 266 
MET CG     C  N N 267 
MET SD     S  N N 268 
MET CE     C  N N 269 
MET OXT    O  N N 270 
MET H      H  N N 271 
MET H2     H  N N 272 
MET HA     H  N N 273 
MET HB2    H  N N 274 
MET HB3    H  N N 275 
MET HG2    H  N N 276 
MET HG3    H  N N 277 
MET HE1    H  N N 278 
MET HE2    H  N N 279 
MET HE3    H  N N 280 
MET HXT    H  N N 281 
MTA CS     C  N N 282 
MTA "S5'"  S  N N 283 
MTA "C5'"  C  N N 284 
MTA "C4'"  C  N S 285 
MTA "O4'"  O  N N 286 
MTA "C2'"  C  N R 287 
MTA "O2'"  O  N N 288 
MTA "C3'"  C  N S 289 
MTA "O3'"  O  N N 290 
MTA "C1'"  C  N R 291 
MTA N9     N  Y N 292 
MTA C8     C  Y N 293 
MTA N7     N  Y N 294 
MTA C5     C  Y N 295 
MTA C6     C  Y N 296 
MTA N6     N  N N 297 
MTA N1     N  Y N 298 
MTA C2     C  Y N 299 
MTA N3     N  Y N 300 
MTA C4     C  Y N 301 
MTA HCS1   H  N N 302 
MTA HCS2   H  N N 303 
MTA HCS3   H  N N 304 
MTA "H5'1" H  N N 305 
MTA "H5'2" H  N N 306 
MTA "H4'"  H  N N 307 
MTA "H2'"  H  N N 308 
MTA "HO2'" H  N N 309 
MTA "H3'"  H  N N 310 
MTA H3T    H  N N 311 
MTA "H1'"  H  N N 312 
MTA H8     H  N N 313 
MTA H61    H  N N 314 
MTA H62    H  N N 315 
MTA H2     H  N N 316 
PHE N      N  N N 317 
PHE CA     C  N S 318 
PHE C      C  N N 319 
PHE O      O  N N 320 
PHE CB     C  N N 321 
PHE CG     C  Y N 322 
PHE CD1    C  Y N 323 
PHE CD2    C  Y N 324 
PHE CE1    C  Y N 325 
PHE CE2    C  Y N 326 
PHE CZ     C  Y N 327 
PHE OXT    O  N N 328 
PHE H      H  N N 329 
PHE H2     H  N N 330 
PHE HA     H  N N 331 
PHE HB2    H  N N 332 
PHE HB3    H  N N 333 
PHE HD1    H  N N 334 
PHE HD2    H  N N 335 
PHE HE1    H  N N 336 
PHE HE2    H  N N 337 
PHE HZ     H  N N 338 
PHE HXT    H  N N 339 
PRO N      N  N N 340 
PRO CA     C  N S 341 
PRO C      C  N N 342 
PRO O      O  N N 343 
PRO CB     C  N N 344 
PRO CG     C  N N 345 
PRO CD     C  N N 346 
PRO OXT    O  N N 347 
PRO H      H  N N 348 
PRO HA     H  N N 349 
PRO HB2    H  N N 350 
PRO HB3    H  N N 351 
PRO HG2    H  N N 352 
PRO HG3    H  N N 353 
PRO HD2    H  N N 354 
PRO HD3    H  N N 355 
PRO HXT    H  N N 356 
SER N      N  N N 357 
SER CA     C  N S 358 
SER C      C  N N 359 
SER O      O  N N 360 
SER CB     C  N N 361 
SER OG     O  N N 362 
SER OXT    O  N N 363 
SER H      H  N N 364 
SER H2     H  N N 365 
SER HA     H  N N 366 
SER HB2    H  N N 367 
SER HB3    H  N N 368 
SER HG     H  N N 369 
SER HXT    H  N N 370 
THR N      N  N N 371 
THR CA     C  N S 372 
THR C      C  N N 373 
THR O      O  N N 374 
THR CB     C  N R 375 
THR OG1    O  N N 376 
THR CG2    C  N N 377 
THR OXT    O  N N 378 
THR H      H  N N 379 
THR H2     H  N N 380 
THR HA     H  N N 381 
THR HB     H  N N 382 
THR HG1    H  N N 383 
THR HG21   H  N N 384 
THR HG22   H  N N 385 
THR HG23   H  N N 386 
THR HXT    H  N N 387 
TRP N      N  N N 388 
TRP CA     C  N S 389 
TRP C      C  N N 390 
TRP O      O  N N 391 
TRP CB     C  N N 392 
TRP CG     C  Y N 393 
TRP CD1    C  Y N 394 
TRP CD2    C  Y N 395 
TRP NE1    N  Y N 396 
TRP CE2    C  Y N 397 
TRP CE3    C  Y N 398 
TRP CZ2    C  Y N 399 
TRP CZ3    C  Y N 400 
TRP CH2    C  Y N 401 
TRP OXT    O  N N 402 
TRP H      H  N N 403 
TRP H2     H  N N 404 
TRP HA     H  N N 405 
TRP HB2    H  N N 406 
TRP HB3    H  N N 407 
TRP HD1    H  N N 408 
TRP HE1    H  N N 409 
TRP HE3    H  N N 410 
TRP HZ2    H  N N 411 
TRP HZ3    H  N N 412 
TRP HH2    H  N N 413 
TRP HXT    H  N N 414 
TYR N      N  N N 415 
TYR CA     C  N S 416 
TYR C      C  N N 417 
TYR O      O  N N 418 
TYR CB     C  N N 419 
TYR CG     C  Y N 420 
TYR CD1    C  Y N 421 
TYR CD2    C  Y N 422 
TYR CE1    C  Y N 423 
TYR CE2    C  Y N 424 
TYR CZ     C  Y N 425 
TYR OH     O  N N 426 
TYR OXT    O  N N 427 
TYR H      H  N N 428 
TYR H2     H  N N 429 
TYR HA     H  N N 430 
TYR HB2    H  N N 431 
TYR HB3    H  N N 432 
TYR HD1    H  N N 433 
TYR HD2    H  N N 434 
TYR HE1    H  N N 435 
TYR HE2    H  N N 436 
TYR HH     H  N N 437 
TYR HXT    H  N N 438 
VAL N      N  N N 439 
VAL CA     C  N S 440 
VAL C      C  N N 441 
VAL O      O  N N 442 
VAL CB     C  N N 443 
VAL CG1    C  N N 444 
VAL CG2    C  N N 445 
VAL OXT    O  N N 446 
VAL H      H  N N 447 
VAL H2     H  N N 448 
VAL HA     H  N N 449 
VAL HB     H  N N 450 
VAL HG11   H  N N 451 
VAL HG12   H  N N 452 
VAL HG13   H  N N 453 
VAL HG21   H  N N 454 
VAL HG22   H  N N 455 
VAL HG23   H  N N 456 
VAL HXT    H  N N 457 
# 
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 
ACT C     O      doub N N 1   
ACT C     OXT    sing N N 2   
ACT C     CH3    sing N N 3   
ACT CH3   H1     sing N N 4   
ACT CH3   H2     sing N N 5   
ACT CH3   H3     sing N N 6   
ALA N     CA     sing N N 7   
ALA N     H      sing N N 8   
ALA N     H2     sing N N 9   
ALA CA    C      sing N N 10  
ALA CA    CB     sing N N 11  
ALA CA    HA     sing N N 12  
ALA C     O      doub N N 13  
ALA C     OXT    sing N N 14  
ALA CB    HB1    sing N N 15  
ALA CB    HB2    sing N N 16  
ALA CB    HB3    sing N N 17  
ALA OXT   HXT    sing N N 18  
ARG N     CA     sing N N 19  
ARG N     H      sing N N 20  
ARG N     H2     sing N N 21  
ARG CA    C      sing N N 22  
ARG CA    CB     sing N N 23  
ARG CA    HA     sing N N 24  
ARG C     O      doub N N 25  
ARG C     OXT    sing N N 26  
ARG CB    CG     sing N N 27  
ARG CB    HB2    sing N N 28  
ARG CB    HB3    sing N N 29  
ARG CG    CD     sing N N 30  
ARG CG    HG2    sing N N 31  
ARG CG    HG3    sing N N 32  
ARG CD    NE     sing N N 33  
ARG CD    HD2    sing N N 34  
ARG CD    HD3    sing N N 35  
ARG NE    CZ     sing N N 36  
ARG NE    HE     sing N N 37  
ARG CZ    NH1    sing N N 38  
ARG CZ    NH2    doub N N 39  
ARG NH1   HH11   sing N N 40  
ARG NH1   HH12   sing N N 41  
ARG NH2   HH21   sing N N 42  
ARG NH2   HH22   sing N N 43  
ARG OXT   HXT    sing N N 44  
ASN N     CA     sing N N 45  
ASN N     H      sing N N 46  
ASN N     H2     sing N N 47  
ASN CA    C      sing N N 48  
ASN CA    CB     sing N N 49  
ASN CA    HA     sing N N 50  
ASN C     O      doub N N 51  
ASN C     OXT    sing N N 52  
ASN CB    CG     sing N N 53  
ASN CB    HB2    sing N N 54  
ASN CB    HB3    sing N N 55  
ASN CG    OD1    doub N N 56  
ASN CG    ND2    sing N N 57  
ASN ND2   HD21   sing N N 58  
ASN ND2   HD22   sing N N 59  
ASN OXT   HXT    sing N N 60  
ASP N     CA     sing N N 61  
ASP N     H      sing N N 62  
ASP N     H2     sing N N 63  
ASP CA    C      sing N N 64  
ASP CA    CB     sing N N 65  
ASP CA    HA     sing N N 66  
ASP C     O      doub N N 67  
ASP C     OXT    sing N N 68  
ASP CB    CG     sing N N 69  
ASP CB    HB2    sing N N 70  
ASP CB    HB3    sing N N 71  
ASP CG    OD1    doub N N 72  
ASP CG    OD2    sing N N 73  
ASP OD2   HD2    sing N N 74  
ASP OXT   HXT    sing N N 75  
CYS N     CA     sing N N 76  
CYS N     H      sing N N 77  
CYS N     H2     sing N N 78  
CYS CA    C      sing N N 79  
CYS CA    CB     sing N N 80  
CYS CA    HA     sing N N 81  
CYS C     O      doub N N 82  
CYS C     OXT    sing N N 83  
CYS CB    SG     sing N N 84  
CYS CB    HB2    sing N N 85  
CYS CB    HB3    sing N N 86  
CYS SG    HG     sing N N 87  
CYS OXT   HXT    sing N N 88  
EDO C1    O1     sing N N 89  
EDO C1    C2     sing N N 90  
EDO C1    H11    sing N N 91  
EDO C1    H12    sing N N 92  
EDO O1    HO1    sing N N 93  
EDO C2    O2     sing N N 94  
EDO C2    H21    sing N N 95  
EDO C2    H22    sing N N 96  
EDO O2    HO2    sing N N 97  
GLN N     CA     sing N N 98  
GLN N     H      sing N N 99  
GLN N     H2     sing N N 100 
GLN CA    C      sing N N 101 
GLN CA    CB     sing N N 102 
GLN CA    HA     sing N N 103 
GLN C     O      doub N N 104 
GLN C     OXT    sing N N 105 
GLN CB    CG     sing N N 106 
GLN CB    HB2    sing N N 107 
GLN CB    HB3    sing N N 108 
GLN CG    CD     sing N N 109 
GLN CG    HG2    sing N N 110 
GLN CG    HG3    sing N N 111 
GLN CD    OE1    doub N N 112 
GLN CD    NE2    sing N N 113 
GLN NE2   HE21   sing N N 114 
GLN NE2   HE22   sing N N 115 
GLN OXT   HXT    sing N N 116 
GLU N     CA     sing N N 117 
GLU N     H      sing N N 118 
GLU N     H2     sing N N 119 
GLU CA    C      sing N N 120 
GLU CA    CB     sing N N 121 
GLU CA    HA     sing N N 122 
GLU C     O      doub N N 123 
GLU C     OXT    sing N N 124 
GLU CB    CG     sing N N 125 
GLU CB    HB2    sing N N 126 
GLU CB    HB3    sing N N 127 
GLU CG    CD     sing N N 128 
GLU CG    HG2    sing N N 129 
GLU CG    HG3    sing N N 130 
GLU CD    OE1    doub N N 131 
GLU CD    OE2    sing N N 132 
GLU OE2   HE2    sing N N 133 
GLU OXT   HXT    sing N N 134 
GLY N     CA     sing N N 135 
GLY N     H      sing N N 136 
GLY N     H2     sing N N 137 
GLY CA    C      sing N N 138 
GLY CA    HA2    sing N N 139 
GLY CA    HA3    sing N N 140 
GLY C     O      doub N N 141 
GLY C     OXT    sing N N 142 
GLY OXT   HXT    sing N N 143 
GOL C1    O1     sing N N 144 
GOL C1    C2     sing N N 145 
GOL C1    H11    sing N N 146 
GOL C1    H12    sing N N 147 
GOL O1    HO1    sing N N 148 
GOL C2    O2     sing N N 149 
GOL C2    C3     sing N N 150 
GOL C2    H2     sing N N 151 
GOL O2    HO2    sing N N 152 
GOL C3    O3     sing N N 153 
GOL C3    H31    sing N N 154 
GOL C3    H32    sing N N 155 
GOL O3    HO3    sing N N 156 
HIS N     CA     sing N N 157 
HIS N     H      sing N N 158 
HIS N     H2     sing N N 159 
HIS CA    C      sing N N 160 
HIS CA    CB     sing N N 161 
HIS CA    HA     sing N N 162 
HIS C     O      doub N N 163 
HIS C     OXT    sing N N 164 
HIS CB    CG     sing N N 165 
HIS CB    HB2    sing N N 166 
HIS CB    HB3    sing N N 167 
HIS CG    ND1    sing Y N 168 
HIS CG    CD2    doub Y N 169 
HIS ND1   CE1    doub Y N 170 
HIS ND1   HD1    sing N N 171 
HIS CD2   NE2    sing Y N 172 
HIS CD2   HD2    sing N N 173 
HIS CE1   NE2    sing Y N 174 
HIS CE1   HE1    sing N N 175 
HIS NE2   HE2    sing N N 176 
HIS OXT   HXT    sing N N 177 
HOH O     H1     sing N N 178 
HOH O     H2     sing N N 179 
ILE N     CA     sing N N 180 
ILE N     H      sing N N 181 
ILE N     H2     sing N N 182 
ILE CA    C      sing N N 183 
ILE CA    CB     sing N N 184 
ILE CA    HA     sing N N 185 
ILE C     O      doub N N 186 
ILE C     OXT    sing N N 187 
ILE CB    CG1    sing N N 188 
ILE CB    CG2    sing N N 189 
ILE CB    HB     sing N N 190 
ILE CG1   CD1    sing N N 191 
ILE CG1   HG12   sing N N 192 
ILE CG1   HG13   sing N N 193 
ILE CG2   HG21   sing N N 194 
ILE CG2   HG22   sing N N 195 
ILE CG2   HG23   sing N N 196 
ILE CD1   HD11   sing N N 197 
ILE CD1   HD12   sing N N 198 
ILE CD1   HD13   sing N N 199 
ILE OXT   HXT    sing N N 200 
LEU N     CA     sing N N 201 
LEU N     H      sing N N 202 
LEU N     H2     sing N N 203 
LEU CA    C      sing N N 204 
LEU CA    CB     sing N N 205 
LEU CA    HA     sing N N 206 
LEU C     O      doub N N 207 
LEU C     OXT    sing N N 208 
LEU CB    CG     sing N N 209 
LEU CB    HB2    sing N N 210 
LEU CB    HB3    sing N N 211 
LEU CG    CD1    sing N N 212 
LEU CG    CD2    sing N N 213 
LEU CG    HG     sing N N 214 
LEU CD1   HD11   sing N N 215 
LEU CD1   HD12   sing N N 216 
LEU CD1   HD13   sing N N 217 
LEU CD2   HD21   sing N N 218 
LEU CD2   HD22   sing N N 219 
LEU CD2   HD23   sing N N 220 
LEU OXT   HXT    sing N N 221 
LYS N     CA     sing N N 222 
LYS N     H      sing N N 223 
LYS N     H2     sing N N 224 
LYS CA    C      sing N N 225 
LYS CA    CB     sing N N 226 
LYS CA    HA     sing N N 227 
LYS C     O      doub N N 228 
LYS C     OXT    sing N N 229 
LYS CB    CG     sing N N 230 
LYS CB    HB2    sing N N 231 
LYS CB    HB3    sing N N 232 
LYS CG    CD     sing N N 233 
LYS CG    HG2    sing N N 234 
LYS CG    HG3    sing N N 235 
LYS CD    CE     sing N N 236 
LYS CD    HD2    sing N N 237 
LYS CD    HD3    sing N N 238 
LYS CE    NZ     sing N N 239 
LYS CE    HE2    sing N N 240 
LYS CE    HE3    sing N N 241 
LYS NZ    HZ1    sing N N 242 
LYS NZ    HZ2    sing N N 243 
LYS NZ    HZ3    sing N N 244 
LYS OXT   HXT    sing N N 245 
MET N     CA     sing N N 246 
MET N     H      sing N N 247 
MET N     H2     sing N N 248 
MET CA    C      sing N N 249 
MET CA    CB     sing N N 250 
MET CA    HA     sing N N 251 
MET C     O      doub N N 252 
MET C     OXT    sing N N 253 
MET CB    CG     sing N N 254 
MET CB    HB2    sing N N 255 
MET CB    HB3    sing N N 256 
MET CG    SD     sing N N 257 
MET CG    HG2    sing N N 258 
MET CG    HG3    sing N N 259 
MET SD    CE     sing N N 260 
MET CE    HE1    sing N N 261 
MET CE    HE2    sing N N 262 
MET CE    HE3    sing N N 263 
MET OXT   HXT    sing N N 264 
MTA CS    "S5'"  sing N N 265 
MTA CS    HCS1   sing N N 266 
MTA CS    HCS2   sing N N 267 
MTA CS    HCS3   sing N N 268 
MTA "S5'" "C5'"  sing N N 269 
MTA "C5'" "C4'"  sing N N 270 
MTA "C5'" "H5'1" sing N N 271 
MTA "C5'" "H5'2" sing N N 272 
MTA "C4'" "O4'"  sing N N 273 
MTA "C4'" "C3'"  sing N N 274 
MTA "C4'" "H4'"  sing N N 275 
MTA "O4'" "C1'"  sing N N 276 
MTA "C2'" "O2'"  sing N N 277 
MTA "C2'" "C3'"  sing N N 278 
MTA "C2'" "C1'"  sing N N 279 
MTA "C2'" "H2'"  sing N N 280 
MTA "O2'" "HO2'" sing N N 281 
MTA "C3'" "O3'"  sing N N 282 
MTA "C3'" "H3'"  sing N N 283 
MTA "O3'" H3T    sing N N 284 
MTA "C1'" N9     sing N N 285 
MTA "C1'" "H1'"  sing N N 286 
MTA N9    C8     sing Y N 287 
MTA N9    C4     sing Y N 288 
MTA C8    N7     doub Y N 289 
MTA C8    H8     sing N N 290 
MTA N7    C5     sing Y N 291 
MTA C5    C6     sing Y N 292 
MTA C5    C4     doub Y N 293 
MTA C6    N6     sing N N 294 
MTA C6    N1     doub Y N 295 
MTA N6    H61    sing N N 296 
MTA N6    H62    sing N N 297 
MTA N1    C2     sing Y N 298 
MTA C2    N3     doub Y N 299 
MTA C2    H2     sing N N 300 
MTA N3    C4     sing Y N 301 
PHE N     CA     sing N N 302 
PHE N     H      sing N N 303 
PHE N     H2     sing N N 304 
PHE CA    C      sing N N 305 
PHE CA    CB     sing N N 306 
PHE CA    HA     sing N N 307 
PHE C     O      doub N N 308 
PHE C     OXT    sing N N 309 
PHE CB    CG     sing N N 310 
PHE CB    HB2    sing N N 311 
PHE CB    HB3    sing N N 312 
PHE CG    CD1    doub Y N 313 
PHE CG    CD2    sing Y N 314 
PHE CD1   CE1    sing Y N 315 
PHE CD1   HD1    sing N N 316 
PHE CD2   CE2    doub Y N 317 
PHE CD2   HD2    sing N N 318 
PHE CE1   CZ     doub Y N 319 
PHE CE1   HE1    sing N N 320 
PHE CE2   CZ     sing Y N 321 
PHE CE2   HE2    sing N N 322 
PHE CZ    HZ     sing N N 323 
PHE OXT   HXT    sing N N 324 
PRO N     CA     sing N N 325 
PRO N     CD     sing N N 326 
PRO N     H      sing N N 327 
PRO CA    C      sing N N 328 
PRO CA    CB     sing N N 329 
PRO CA    HA     sing N N 330 
PRO C     O      doub N N 331 
PRO C     OXT    sing N N 332 
PRO CB    CG     sing N N 333 
PRO CB    HB2    sing N N 334 
PRO CB    HB3    sing N N 335 
PRO CG    CD     sing N N 336 
PRO CG    HG2    sing N N 337 
PRO CG    HG3    sing N N 338 
PRO CD    HD2    sing N N 339 
PRO CD    HD3    sing N N 340 
PRO OXT   HXT    sing N N 341 
SER N     CA     sing N N 342 
SER N     H      sing N N 343 
SER N     H2     sing N N 344 
SER CA    C      sing N N 345 
SER CA    CB     sing N N 346 
SER CA    HA     sing N N 347 
SER C     O      doub N N 348 
SER C     OXT    sing N N 349 
SER CB    OG     sing N N 350 
SER CB    HB2    sing N N 351 
SER CB    HB3    sing N N 352 
SER OG    HG     sing N N 353 
SER OXT   HXT    sing N N 354 
THR N     CA     sing N N 355 
THR N     H      sing N N 356 
THR N     H2     sing N N 357 
THR CA    C      sing N N 358 
THR CA    CB     sing N N 359 
THR CA    HA     sing N N 360 
THR C     O      doub N N 361 
THR C     OXT    sing N N 362 
THR CB    OG1    sing N N 363 
THR CB    CG2    sing N N 364 
THR CB    HB     sing N N 365 
THR OG1   HG1    sing N N 366 
THR CG2   HG21   sing N N 367 
THR CG2   HG22   sing N N 368 
THR CG2   HG23   sing N N 369 
THR OXT   HXT    sing N N 370 
TRP N     CA     sing N N 371 
TRP N     H      sing N N 372 
TRP N     H2     sing N N 373 
TRP CA    C      sing N N 374 
TRP CA    CB     sing N N 375 
TRP CA    HA     sing N N 376 
TRP C     O      doub N N 377 
TRP C     OXT    sing N N 378 
TRP CB    CG     sing N N 379 
TRP CB    HB2    sing N N 380 
TRP CB    HB3    sing N N 381 
TRP CG    CD1    doub Y N 382 
TRP CG    CD2    sing Y N 383 
TRP CD1   NE1    sing Y N 384 
TRP CD1   HD1    sing N N 385 
TRP CD2   CE2    doub Y N 386 
TRP CD2   CE3    sing Y N 387 
TRP NE1   CE2    sing Y N 388 
TRP NE1   HE1    sing N N 389 
TRP CE2   CZ2    sing Y N 390 
TRP CE3   CZ3    doub Y N 391 
TRP CE3   HE3    sing N N 392 
TRP CZ2   CH2    doub Y N 393 
TRP CZ2   HZ2    sing N N 394 
TRP CZ3   CH2    sing Y N 395 
TRP CZ3   HZ3    sing N N 396 
TRP CH2   HH2    sing N N 397 
TRP OXT   HXT    sing N N 398 
TYR N     CA     sing N N 399 
TYR N     H      sing N N 400 
TYR N     H2     sing N N 401 
TYR CA    C      sing N N 402 
TYR CA    CB     sing N N 403 
TYR CA    HA     sing N N 404 
TYR C     O      doub N N 405 
TYR C     OXT    sing N N 406 
TYR CB    CG     sing N N 407 
TYR CB    HB2    sing N N 408 
TYR CB    HB3    sing N N 409 
TYR CG    CD1    doub Y N 410 
TYR CG    CD2    sing Y N 411 
TYR CD1   CE1    sing Y N 412 
TYR CD1   HD1    sing N N 413 
TYR CD2   CE2    doub Y N 414 
TYR CD2   HD2    sing N N 415 
TYR CE1   CZ     doub Y N 416 
TYR CE1   HE1    sing N N 417 
TYR CE2   CZ     sing Y N 418 
TYR CE2   HE2    sing N N 419 
TYR CZ    OH     sing N N 420 
TYR OH    HH     sing N N 421 
TYR OXT   HXT    sing N N 422 
VAL N     CA     sing N N 423 
VAL N     H      sing N N 424 
VAL N     H2     sing N N 425 
VAL CA    C      sing N N 426 
VAL CA    CB     sing N N 427 
VAL CA    HA     sing N N 428 
VAL C     O      doub N N 429 
VAL C     OXT    sing N N 430 
VAL CB    CG1    sing N N 431 
VAL CB    CG2    sing N N 432 
VAL CB    HB     sing N N 433 
VAL CG1   HG11   sing N N 434 
VAL CG1   HG12   sing N N 435 
VAL CG1   HG13   sing N N 436 
VAL CG2   HG21   sing N N 437 
VAL CG2   HG22   sing N N 438 
VAL CG2   HG23   sing N N 439 
VAL OXT   HXT    sing N N 440 
# 
_pdbx_audit_support.funding_organization   'Department of Biotechnology (DBT, India)' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           BT/PR51982/NER/95/2011/2023 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9JGB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JGD 
_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]   0.008831 
_atom_sites.fract_transf_matrix[1][2]   0.005098 
_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]   0.010197 
_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]   0.009726 
_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  
CL 
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     . GLU A 1 2   ? -21.073 -1.576  -14.082 1.00 89.96  ? 2   GLU A N     1 
ATOM   2    C  CA    . GLU A 1 2   ? -20.279 -1.253  -15.304 1.00 90.58  ? 2   GLU A CA    1 
ATOM   3    C  C     . GLU A 1 2   ? -20.022 -2.490  -16.188 1.00 91.01  ? 2   GLU A C     1 
ATOM   4    O  O     . GLU A 1 2   ? -19.192 -2.422  -17.101 1.00 76.65  ? 2   GLU A O     1 
ATOM   5    C  CB    . GLU A 1 2   ? -18.982 -0.534  -14.910 1.00 90.14  ? 2   GLU A CB    1 
ATOM   6    C  CG    . GLU A 1 2   ? -19.186 0.936   -14.554 1.00 93.11  ? 2   GLU A CG    1 
ATOM   7    C  CD    . GLU A 1 2   ? -18.129 1.885   -15.105 1.00 96.13  ? 2   GLU A CD    1 
ATOM   8    O  OE1   . GLU A 1 2   ? -16.979 1.448   -15.303 1.00 92.13  ? 2   GLU A OE1   1 
ATOM   9    O  OE2   . GLU A 1 2   ? -18.471 3.051   -15.398 1.00 95.28  ? 2   GLU A OE2   1 
ATOM   10   N  N     . GLU A 1 3   ? -20.751 -3.605  -15.958 1.00 88.34  ? 3   GLU A N     1 
ATOM   11   C  CA    . GLU A 1 3   ? -20.756 -4.745  -16.872 1.00 76.84  ? 3   GLU A CA    1 
ATOM   12   C  C     . GLU A 1 3   ? -22.177 -4.991  -17.404 1.00 69.61  ? 3   GLU A C     1 
ATOM   13   O  O     . GLU A 1 3   ? -22.452 -6.074  -17.912 1.00 68.50  ? 3   GLU A O     1 
ATOM   14   C  CB    . GLU A 1 3   ? -20.170 -6.001  -16.206 1.00 82.19  ? 3   GLU A CB    1 
ATOM   15   C  CG    . GLU A 1 3   ? -20.993 -6.548  -15.032 1.00 82.61  ? 3   GLU A CG    1 
ATOM   16   C  CD    . GLU A 1 3   ? -20.676 -7.980  -14.627 1.00 84.28  ? 3   GLU A CD    1 
ATOM   17   O  OE1   . GLU A 1 3   ? -21.581 -8.839  -14.705 1.00 81.49  ? 3   GLU A OE1   1 
ATOM   18   O  OE2   . GLU A 1 3   ? -19.528 -8.242  -14.227 1.00 85.89  ? 3   GLU A OE2   1 
ATOM   19   N  N     . LYS A 1 4   ? -23.083 -3.996  -17.306 1.00 62.94  ? 4   LYS A N     1 
ATOM   20   C  CA    . LYS A 1 4   ? -24.275 -3.960  -18.152 1.00 56.05  ? 4   LYS A CA    1 
ATOM   21   C  C     . LYS A 1 4   ? -23.901 -3.621  -19.598 1.00 46.25  ? 4   LYS A C     1 
ATOM   22   O  O     . LYS A 1 4   ? -22.821 -3.115  -19.861 1.00 44.41  ? 4   LYS A O     1 
ATOM   23   C  CB    . LYS A 1 4   ? -25.285 -2.909  -17.705 1.00 53.46  ? 4   LYS A CB    1 
ATOM   24   C  CG    . LYS A 1 4   ? -24.710 -1.517  -17.558 1.00 53.12  ? 4   LYS A CG    1 
ATOM   25   C  CD    . LYS A 1 4   ? -25.655 -0.478  -18.067 1.00 58.39  ? 4   LYS A CD    1 
ATOM   26   C  CE    . LYS A 1 4   ? -26.965 -0.413  -17.315 1.00 63.27  ? 4   LYS A CE    1 
ATOM   27   N  NZ    . LYS A 1 4   ? -26.809 0.303   -16.031 1.00 65.11  ? 4   LYS A NZ    1 
ATOM   28   N  N     . LYS A 1 5   ? -24.814 -3.894  -20.525 1.00 41.84  ? 5   LYS A N     1 
ATOM   29   C  CA    . LYS A 1 5   ? -24.582 -3.656  -21.934 1.00 40.51  ? 5   LYS A CA    1 
ATOM   30   C  C     . LYS A 1 5   ? -24.558 -2.156  -22.201 1.00 36.81  ? 5   LYS A C     1 
ATOM   31   O  O     . LYS A 1 5   ? -25.516 -1.446  -21.894 1.00 36.53  ? 5   LYS A O     1 
ATOM   32   C  CB    . LYS A 1 5   ? -25.662 -4.318  -22.792 1.00 43.21  ? 5   LYS A CB    1 
ATOM   33   C  CG    . LYS A 1 5   ? -25.672 -5.843  -22.721 1.00 46.94  ? 5   LYS A CG    1 
ATOM   34   C  CD    . LYS A 1 5   ? -26.704 -6.425  -23.634 1.00 49.39  ? 5   LYS A CD    1 
ATOM   35   C  CE    . LYS A 1 5   ? -26.470 -7.891  -23.899 1.00 56.13  ? 5   LYS A CE    1 
ATOM   36   N  NZ    . LYS A 1 5   ? -27.637 -8.474  -24.594 1.00 60.79  ? 5   LYS A NZ    1 
ATOM   37   N  N     . ARG A 1 6   ? -23.454 -1.713  -22.796 1.00 32.79  ? 6   ARG A N     1 
ATOM   38   C  CA    . ARG A 1 6   ? -23.301 -0.345  -23.230 1.00 33.34  ? 6   ARG A CA    1 
ATOM   39   C  C     . ARG A 1 6   ? -22.682 -0.286  -24.626 1.00 31.16  ? 6   ARG A C     1 
ATOM   40   O  O     . ARG A 1 6   ? -21.768 -1.050  -24.947 1.00 30.67  ? 6   ARG A O     1 
ATOM   41   C  CB    . ARG A 1 6   ? -22.376 0.426   -22.287 1.00 34.11  ? 6   ARG A CB    1 
ATOM   42   C  CG    . ARG A 1 6   ? -22.863 0.566   -20.864 1.00 35.02  ? 6   ARG A CG    1 
ATOM   43   C  CD    . ARG A 1 6   ? -22.368 1.900   -20.310 1.00 34.80  ? 6   ARG A CD    1 
ATOM   44   N  NE    . ARG A 1 6   ? -22.573 1.975   -18.853 1.00 38.27  ? 6   ARG A NE    1 
ATOM   45   C  CZ    . ARG A 1 6   ? -22.030 1.160   -17.945 1.00 38.32  ? 6   ARG A CZ    1 
ATOM   46   N  NH1   . ARG A 1 6   ? -21.028 0.365   -18.267 1.00 40.30  ? 6   ARG A NH1   1 
ATOM   47   N  NH2   . ARG A 1 6   ? -22.448 1.178   -16.696 1.00 39.77  ? 6   ARG A NH2   1 
ATOM   48   N  N     . LEU A 1 7   ? -23.143 0.702   -25.401 1.00 27.94  ? 7   LEU A N     1 
ATOM   49   C  CA    . LEU A 1 7   ? -22.568 1.019   -26.686 1.00 26.32  ? 7   LEU A CA    1 
ATOM   50   C  C     . LEU A 1 7   ? -21.384 1.939   -26.434 1.00 25.79  ? 7   LEU A C     1 
ATOM   51   O  O     . LEU A 1 7   ? -21.493 2.833   -25.617 1.00 25.61  ? 7   LEU A O     1 
ATOM   52   C  CB    . LEU A 1 7   ? -23.613 1.693   -27.587 1.00 25.93  ? 7   LEU A CB    1 
ATOM   53   C  CG    . LEU A 1 7   ? -23.105 2.273   -28.911 1.00 24.91  ? 7   LEU A CG    1 
ATOM   54   C  CD1   . LEU A 1 7   ? -22.565 1.200   -29.830 1.00 25.56  ? 7   LEU A CD1   1 
ATOM   55   C  CD2   . LEU A 1 7   ? -24.214 3.007   -29.632 1.00 26.65  ? 7   LEU A CD2   1 
ATOM   56   N  N     . HIS A 1 8   ? -20.257 1.648   -27.117 1.00 26.08  ? 8   HIS A N     1 
ATOM   57   C  CA    . HIS A 1 8   ? -19.042 2.438   -27.099 1.00 23.67  ? 8   HIS A CA    1 
ATOM   58   C  C     . HIS A 1 8   ? -18.908 3.018   -28.498 1.00 21.85  ? 8   HIS A C     1 
ATOM   59   O  O     . HIS A 1 8   ? -18.735 2.276   -29.455 1.00 23.55  ? 8   HIS A O     1 
ATOM   60   C  CB    . HIS A 1 8   ? -17.872 1.534   -26.713 1.00 24.96  ? 8   HIS A CB    1 
ATOM   61   C  CG    . HIS A 1 8   ? -17.962 1.082   -25.288 1.00 26.60  ? 8   HIS A CG    1 
ATOM   62   N  ND1   . HIS A 1 8   ? -17.148 1.585   -24.292 1.00 28.88  ? 8   HIS A ND1   1 
ATOM   63   C  CD2   . HIS A 1 8   ? -18.785 0.225   -24.689 1.00 27.08  ? 8   HIS A CD2   1 
ATOM   64   C  CE1   . HIS A 1 8   ? -17.460 1.010   -23.137 1.00 28.75  ? 8   HIS A CE1   1 
ATOM   65   N  NE2   . HIS A 1 8   ? -18.464 0.208   -23.360 1.00 28.15  ? 8   HIS A NE2   1 
ATOM   66   N  N     . LEU A 1 9   ? -19.129 4.322   -28.605 1.00 19.68  ? 9   LEU A N     1 
ATOM   67   C  CA    . LEU A 1 9   ? -19.196 5.008   -29.877 1.00 20.17  ? 9   LEU A CA    1 
ATOM   68   C  C     . LEU A 1 9   ? -17.973 5.904   -30.049 1.00 19.32  ? 9   LEU A C     1 
ATOM   69   O  O     . LEU A 1 9   ? -17.661 6.707   -29.191 1.00 20.78  ? 9   LEU A O     1 
ATOM   70   C  CB    . LEU A 1 9   ? -20.474 5.845   -29.883 1.00 21.32  ? 9   LEU A CB    1 
ATOM   71   C  CG    . LEU A 1 9   ? -20.606 6.840   -31.022 1.00 21.45  ? 9   LEU A CG    1 
ATOM   72   C  CD1   . LEU A 1 9   ? -20.841 6.118   -32.325 1.00 22.69  ? 9   LEU A CD1   1 
ATOM   73   C  CD2   . LEU A 1 9   ? -21.750 7.771   -30.735 1.00 22.30  ? 9   LEU A CD2   1 
ATOM   74   N  N     . ILE A 1 10  ? -17.291 5.779   -31.175 1.00 20.48  ? 10  ILE A N     1 
ATOM   75   C  CA    . ILE A 1 10  ? -16.059 6.505   -31.414 1.00 20.31  ? 10  ILE A CA    1 
ATOM   76   C  C     . ILE A 1 10  ? -16.232 7.309   -32.678 1.00 19.26  ? 10  ILE A C     1 
ATOM   77   O  O     . ILE A 1 10  ? -16.536 6.751   -33.709 1.00 16.65  ? 10  ILE A O     1 
ATOM   78   C  CB    . ILE A 1 10  ? -14.860 5.556   -31.548 1.00 22.33  ? 10  ILE A CB    1 
ATOM   79   C  CG1   . ILE A 1 10  ? -14.690 4.690   -30.301 1.00 24.29  ? 10  ILE A CG1   1 
ATOM   80   C  CG2   . ILE A 1 10  ? -13.619 6.373   -31.826 1.00 23.09  ? 10  ILE A CG2   1 
ATOM   81   C  CD1   . ILE A 1 10  ? -13.597 3.649   -30.450 1.00 27.52  ? 10  ILE A CD1   1 
ATOM   82   N  N     . ILE A 1 11  ? -16.102 8.634   -32.558 1.00 21.72  ? 11  ILE A N     1 
ATOM   83   C  CA    . ILE A 1 11  ? -16.087 9.473   -33.737 1.00 22.67  ? 11  ILE A CA    1 
ATOM   84   C  C     . ILE A 1 11  ? -14.625 9.516   -34.135 1.00 22.38  ? 11  ILE A C     1 
ATOM   85   O  O     . ILE A 1 11  ? -13.845 10.062  -33.364 1.00 20.48  ? 11  ILE A O     1 
ATOM   86   C  CB    . ILE A 1 11  ? -16.610 10.895  -33.421 1.00 21.93  ? 11  ILE A CB    1 
ATOM   87   C  CG1   . ILE A 1 11  ? -17.945 10.876  -32.674 1.00 23.64  ? 11  ILE A CG1   1 
ATOM   88   C  CG2   . ILE A 1 11  ? -16.649 11.754  -34.653 1.00 19.49  ? 11  ILE A CG2   1 
ATOM   89   C  CD1   . ILE A 1 11  ? -19.031 10.063  -33.348 1.00 24.80  ? 11  ILE A CD1   1 
ATOM   90   N  N     . ALA A 1 12  ? -14.261 8.993   -35.317 1.00 23.15  ? 12  ALA A N     1 
ATOM   91   C  CA    . ALA A 1 12  ? -12.846 8.721   -35.557 1.00 24.38  ? 12  ALA A CA    1 
ATOM   92   C  C     . ALA A 1 12  ? -12.315 9.563   -36.699 1.00 24.44  ? 12  ALA A C     1 
ATOM   93   O  O     . ALA A 1 12  ? -13.084 10.069  -37.508 1.00 21.59  ? 12  ALA A O     1 
ATOM   94   C  CB    . ALA A 1 12  ? -12.592 7.259   -35.814 1.00 24.17  ? 12  ALA A CB    1 
ATOM   95   N  N     . ASP A 1 13  ? -10.971 9.645   -36.729 1.00 23.84  ? 13  ASP A N     1 
ATOM   96   C  CA    . ASP A 1 13  ? -10.246 10.477  -37.664 1.00 23.30  ? 13  ASP A CA    1 
ATOM   97   C  C     . ASP A 1 13  ? -10.933 11.832  -37.776 1.00 23.43  ? 13  ASP A C     1 
ATOM   98   O  O     . ASP A 1 13  ? -11.059 12.359  -38.869 1.00 24.46  ? 13  ASP A O     1 
ATOM   99   C  CB    . ASP A 1 13  ? -10.147 9.818   -39.028 1.00 24.53  ? 13  ASP A CB    1 
ATOM   100  C  CG    . ASP A 1 13  ? -9.376  8.521   -39.006 1.00 26.86  ? 13  ASP A CG    1 
ATOM   101  O  OD1   . ASP A 1 13  ? -8.366  8.435   -38.226 1.00 29.48  ? 13  ASP A OD1   1 
ATOM   102  O  OD2   . ASP A 1 13  ? -9.785  7.613   -39.778 1.00 27.89  ? 13  ASP A OD2   1 
ATOM   103  N  N     . ALA A 1 14  ? -11.319 12.393  -36.628 1.00 23.53  ? 14  ALA A N     1 
ATOM   104  C  CA    . ALA A 1 14  ? -12.102 13.618  -36.580 1.00 25.34  ? 14  ALA A CA    1 
ATOM   105  C  C     . ALA A 1 14  ? -11.219 14.796  -36.971 1.00 25.97  ? 14  ALA A C     1 
ATOM   106  O  O     . ALA A 1 14  ? -10.061 14.855  -36.548 1.00 24.29  ? 14  ALA A O     1 
ATOM   107  C  CB    . ALA A 1 14  ? -12.692 13.839  -35.203 1.00 24.27  ? 14  ALA A CB    1 
ATOM   108  N  N     . GLU A 1 15  ? -11.811 15.701  -37.768 1.00 25.27  ? 15  GLU A N     1 
ATOM   109  C  CA    . GLU A 1 15  ? -11.170 16.919  -38.246 1.00 25.57  ? 15  GLU A CA    1 
ATOM   110  C  C     . GLU A 1 15  ? -11.269 17.998  -37.166 1.00 24.05  ? 15  GLU A C     1 
ATOM   111  O  O     . GLU A 1 15  ? -11.884 19.038  -37.372 1.00 23.81  ? 15  GLU A O     1 
ATOM   112  C  CB    . GLU A 1 15  ? -11.862 17.329  -39.550 1.00 27.17  ? 15  GLU A CB    1 
ATOM   113  C  CG    . GLU A 1 15  ? -11.828 16.258  -40.637 1.00 28.47  ? 15  GLU A CG    1 
ATOM   114  C  CD    . GLU A 1 15  ? -10.443 15.930  -41.168 1.00 32.34  ? 15  GLU A CD    1 
ATOM   115  O  OE1   . GLU A 1 15  ? -10.309 14.986  -41.981 1.00 42.10  ? 15  GLU A OE1   1 
ATOM   116  O  OE2   . GLU A 1 15  ? -9.501  16.621  -40.795 1.00 33.61  ? 15  GLU A OE2   1 
ATOM   117  N  N     . LEU A 1 16  ? -10.688 17.697  -36.002 1.00 25.87  ? 16  LEU A N     1 
ATOM   118  C  CA    . LEU A 1 16  ? -10.643 18.569  -34.837 1.00 25.93  ? 16  LEU A CA    1 
ATOM   119  C  C     . LEU A 1 16  ? -9.198  18.749  -34.398 1.00 26.65  ? 16  LEU A C     1 
ATOM   120  O  O     . LEU A 1 16  ? -8.601  17.807  -33.908 1.00 26.90  ? 16  LEU A O     1 
ATOM   121  C  CB    . LEU A 1 16  ? -11.436 17.894  -33.720 1.00 26.08  ? 16  LEU A CB    1 
ATOM   122  C  CG    . LEU A 1 16  ? -11.471 18.636  -32.386 1.00 26.49  ? 16  LEU A CG    1 
ATOM   123  C  CD1   . LEU A 1 16  ? -12.236 19.931  -32.525 1.00 29.55  ? 16  LEU A CD1   1 
ATOM   124  C  CD2   . LEU A 1 16  ? -12.075 17.768  -31.291 1.00 25.27  ? 16  LEU A CD2   1 
ATOM   125  N  N     . GLU A 1 17  ? -8.647  19.959  -34.573 1.00 28.94  ? 17  GLU A N     1 
ATOM   126  C  CA    . GLU A 1 17  ? -7.238  20.242  -34.335 1.00 27.23  ? 17  GLU A CA    1 
ATOM   127  C  C     . GLU A 1 17  ? -7.077  21.744  -34.235 1.00 27.19  ? 17  GLU A C     1 
ATOM   128  O  O     . GLU A 1 17  ? -7.942  22.477  -34.726 1.00 26.07  ? 17  GLU A O     1 
ATOM   129  C  CB    . GLU A 1 17  ? -6.377  19.714  -35.486 1.00 28.69  ? 17  GLU A CB    1 
ATOM   130  C  CG    . GLU A 1 17  ? -6.707  20.343  -36.837 1.00 29.03  ? 17  GLU A CG    1 
ATOM   131  C  CD    . GLU A 1 17  ? -5.984  19.759  -38.034 1.00 29.60  ? 17  GLU A CD    1 
ATOM   132  O  OE1   . GLU A 1 17  ? -6.590  19.692  -39.112 1.00 30.02  ? 17  GLU A OE1   1 
ATOM   133  O  OE2   . GLU A 1 17  ? -4.805  19.397  -37.888 1.00 31.41  ? 17  GLU A OE2   1 
ATOM   134  N  N     . THR A 1 18  ? -5.973  22.183  -33.610 1.00 27.52  ? 18  THR A N     1 
ATOM   135  C  CA    . THR A 1 18  ? -5.619  23.594  -33.639 1.00 28.72  ? 18  THR A CA    1 
ATOM   136  C  C     . THR A 1 18  ? -5.048  23.950  -35.012 1.00 28.16  ? 18  THR A C     1 
ATOM   137  O  O     . THR A 1 18  ? -4.684  23.102  -35.803 1.00 29.57  ? 18  THR A O     1 
ATOM   138  C  CB    . THR A 1 18  ? -4.654  23.972  -32.502 1.00 29.52  ? 18  THR A CB    1 
ATOM   139  O  OG1   . THR A 1 18  ? -3.587  23.045  -32.551 1.00 30.82  ? 18  THR A OG1   1 
ATOM   140  C  CG2   . THR A 1 18  ? -5.256  23.899  -31.117 1.00 29.57  ? 18  THR A CG2   1 
ATOM   141  N  N     . VAL A 1 19  ? -4.893  25.232  -35.282 1.00 30.52  ? 19  VAL A N     1 
ATOM   142  C  CA    . VAL A 1 19  ? -4.307  25.649  -36.534 1.00 32.94  ? 19  VAL A CA    1 
ATOM   143  C  C     . VAL A 1 19  ? -3.019  24.872  -36.786 1.00 34.38  ? 19  VAL A C     1 
ATOM   144  O  O     . VAL A 1 19  ? -2.134  24.831  -35.937 1.00 37.27  ? 19  VAL A O     1 
ATOM   145  C  CB    . VAL A 1 19  ? -4.051  27.155  -36.556 1.00 34.10  ? 19  VAL A CB    1 
ATOM   146  C  CG1   . VAL A 1 19  ? -3.434  27.565  -37.873 1.00 36.49  ? 19  VAL A CG1   1 
ATOM   147  C  CG2   . VAL A 1 19  ? -5.334  27.932  -36.331 1.00 34.74  ? 19  VAL A CG2   1 
ATOM   148  N  N     . PRO A 1 20  ? -2.908  24.184  -37.943 1.00 34.35  ? 20  PRO A N     1 
ATOM   149  C  CA    . PRO A 1 20  ? -1.701  23.452  -38.299 1.00 36.13  ? 20  PRO A CA    1 
ATOM   150  C  C     . PRO A 1 20  ? -0.468  24.348  -38.307 1.00 38.78  ? 20  PRO A C     1 
ATOM   151  O  O     . PRO A 1 20  ? -0.528  25.511  -38.715 1.00 39.59  ? 20  PRO A O     1 
ATOM   152  C  CB    . PRO A 1 20  ? -2.026  22.868  -39.681 1.00 35.34  ? 20  PRO A CB    1 
ATOM   153  C  CG    . PRO A 1 20  ? -3.510  22.684  -39.608 1.00 34.62  ? 20  PRO A CG    1 
ATOM   154  C  CD    . PRO A 1 20  ? -3.982  23.946  -38.916 1.00 34.45  ? 20  PRO A CD    1 
ATOM   155  N  N     . PRO A 1 21  ? 0.659   23.821  -37.774 1.00 40.94  ? 21  PRO A N     1 
ATOM   156  C  CA    . PRO A 1 21  ? 1.923   24.554  -37.742 1.00 43.71  ? 21  PRO A CA    1 
ATOM   157  C  C     . PRO A 1 21  ? 2.365   25.084  -39.106 1.00 47.01  ? 21  PRO A C     1 
ATOM   158  O  O     . PRO A 1 21  ? 2.944   26.155  -39.181 1.00 49.57  ? 21  PRO A O     1 
ATOM   159  C  CB    . PRO A 1 21  ? 2.920   23.543  -37.157 1.00 41.51  ? 21  PRO A CB    1 
ATOM   160  C  CG    . PRO A 1 21  ? 2.074   22.577  -36.374 1.00 39.99  ? 21  PRO A CG    1 
ATOM   161  C  CD    . PRO A 1 21  ? 0.738   22.520  -37.081 1.00 38.78  ? 21  PRO A CD    1 
ATOM   162  N  N     . GLU A 1 22  ? 2.039   24.372  -40.188 1.00 51.45  ? 22  GLU A N     1 
ATOM   163  C  CA    . GLU A 1 22  ? 2.460   24.781  -41.520 1.00 51.70  ? 22  GLU A CA    1 
ATOM   164  C  C     . GLU A 1 22  ? 1.858   26.116  -41.925 1.00 50.90  ? 22  GLU A C     1 
ATOM   165  O  O     . GLU A 1 22  ? 2.383   26.718  -42.840 1.00 51.65  ? 22  GLU A O     1 
ATOM   166  C  CB    . GLU A 1 22  ? 1.983   23.818  -42.606 1.00 54.10  ? 22  GLU A CB    1 
ATOM   167  C  CG    . GLU A 1 22  ? 2.453   22.395  -42.423 1.00 54.58  ? 22  GLU A CG    1 
ATOM   168  C  CD    . GLU A 1 22  ? 1.475   21.507  -41.675 1.00 52.99  ? 22  GLU A CD    1 
ATOM   169  O  OE1   . GLU A 1 22  ? 1.284   20.345  -42.121 1.00 61.25  ? 22  GLU A OE1   1 
ATOM   170  O  OE2   . GLU A 1 22  ? 0.926   21.965  -40.650 1.00 46.83  ? 22  GLU A OE2   1 
ATOM   171  N  N     . ILE A 1 23  ? 0.724   26.531  -41.325 1.00 52.20  ? 23  ILE A N     1 
ATOM   172  C  CA    . ILE A 1 23  ? 0.010   27.712  -41.802 1.00 50.11  ? 23  ILE A CA    1 
ATOM   173  C  C     . ILE A 1 23  ? -0.141  28.786  -40.722 1.00 51.35  ? 23  ILE A C     1 
ATOM   174  O  O     . ILE A 1 23  ? -0.904  29.728  -40.927 1.00 52.63  ? 23  ILE A O     1 
ATOM   175  C  CB    . ILE A 1 23  ? -1.356  27.288  -42.370 1.00 48.13  ? 23  ILE A CB    1 
ATOM   176  C  CG1   . ILE A 1 23  ? -2.274  26.729  -41.281 1.00 43.57  ? 23  ILE A CG1   1 
ATOM   177  C  CG2   . ILE A 1 23  ? -1.156  26.303  -43.507 1.00 49.28  ? 23  ILE A CG2   1 
ATOM   178  C  CD1   . ILE A 1 23  ? -3.652  26.452  -41.753 1.00 42.46  ? 23  ILE A CD1   1 
ATOM   179  N  N     . LEU A 1 24  ? 0.570   28.668  -39.590 1.00 53.16  ? 24  LEU A N     1 
ATOM   180  C  CA    . LEU A 1 24  ? 0.403   29.605  -38.486 1.00 55.00  ? 24  LEU A CA    1 
ATOM   181  C  C     . LEU A 1 24  ? 0.712   31.036  -38.917 1.00 62.49  ? 24  LEU A C     1 
ATOM   182  O  O     . LEU A 1 24  ? 0.169   31.958  -38.306 1.00 68.84  ? 24  LEU A O     1 
ATOM   183  C  CB    . LEU A 1 24  ? 1.290   29.219  -37.296 1.00 54.00  ? 24  LEU A CB    1 
ATOM   184  C  CG    . LEU A 1 24  ? 0.736   28.145  -36.361 1.00 53.19  ? 24  LEU A CG    1 
ATOM   185  C  CD1   . LEU A 1 24  ? 1.719   27.864  -35.247 1.00 52.51  ? 24  LEU A CD1   1 
ATOM   186  C  CD2   . LEU A 1 24  ? -0.605  28.554  -35.757 1.00 50.88  ? 24  LEU A CD2   1 
ATOM   187  N  N     . ASP A 1 25  ? 1.564   31.243  -39.939 1.00 64.87  ? 25  ASP A N     1 
ATOM   188  C  CA    . ASP A 1 25  ? 1.809   32.605  -40.409 1.00 71.64  ? 25  ASP A CA    1 
ATOM   189  C  C     . ASP A 1 25  ? 1.256   32.813  -41.825 1.00 71.70  ? 25  ASP A C     1 
ATOM   190  O  O     . ASP A 1 25  ? 1.705   33.706  -42.535 1.00 78.16  ? 25  ASP A O     1 
ATOM   191  C  CB    . ASP A 1 25  ? 3.272   33.036  -40.204 1.00 75.44  ? 25  ASP A CB    1 
ATOM   192  C  CG    . ASP A 1 25  ? 4.338   32.054  -40.673 1.00 82.04  ? 25  ASP A CG    1 
ATOM   193  O  OD1   . ASP A 1 25  ? 4.027   31.229  -41.549 1.00 83.32  ? 25  ASP A OD1   1 
ATOM   194  O  OD2   . ASP A 1 25  ? 5.483   32.120  -40.153 1.00 82.41  ? 25  ASP A OD2   1 
ATOM   195  N  N     . HIS A 1 26  ? 0.234   32.043  -42.213 1.00 69.20  ? 26  HIS A N     1 
ATOM   196  C  CA    . HIS A 1 26  ? -0.525  32.321  -43.425 1.00 73.31  ? 26  HIS A CA    1 
ATOM   197  C  C     . HIS A 1 26  ? -1.458  33.512  -43.162 1.00 74.40  ? 26  HIS A C     1 
ATOM   198  O  O     . HIS A 1 26  ? -2.137  33.542  -42.138 1.00 67.91  ? 26  HIS A O     1 
ATOM   199  C  CB    . HIS A 1 26  ? -1.259  31.059  -43.907 1.00 76.51  ? 26  HIS A CB    1 
ATOM   200  C  CG    . HIS A 1 26  ? -2.023  31.239  -45.183 1.00 81.74  ? 26  HIS A CG    1 
ATOM   201  N  ND1   . HIS A 1 26  ? -3.097  32.101  -45.314 1.00 82.51  ? 26  HIS A ND1   1 
ATOM   202  C  CD2   . HIS A 1 26  ? -1.852  30.677  -46.392 1.00 84.05  ? 26  HIS A CD2   1 
ATOM   203  C  CE1   . HIS A 1 26  ? -3.547  32.062  -46.565 1.00 81.38  ? 26  HIS A CE1   1 
ATOM   204  N  NE2   . HIS A 1 26  ? -2.807  31.201  -47.237 1.00 83.78  ? 26  HIS A NE2   1 
ATOM   205  N  N     . PRO A 1 27  ? -1.513  34.526  -44.068 1.00 80.12  ? 27  PRO A N     1 
ATOM   206  C  CA    . PRO A 1 27  ? -2.258  35.768  -43.836 1.00 78.42  ? 27  PRO A CA    1 
ATOM   207  C  C     . PRO A 1 27  ? -3.607  35.665  -43.135 1.00 75.96  ? 27  PRO A C     1 
ATOM   208  O  O     . PRO A 1 27  ? -3.806  36.308  -42.107 1.00 73.81  ? 27  PRO A O     1 
ATOM   209  C  CB    . PRO A 1 27  ? -2.464  36.273  -45.274 1.00 85.55  ? 27  PRO A CB    1 
ATOM   210  C  CG    . PRO A 1 27  ? -1.158  35.905  -45.966 1.00 88.76  ? 27  PRO A CG    1 
ATOM   211  C  CD    . PRO A 1 27  ? -0.796  34.561  -45.362 1.00 85.64  ? 27  PRO A CD    1 
ATOM   212  N  N     . ALA A 1 28  ? -4.511  34.844  -43.686 1.00 75.16  ? 28  ALA A N     1 
ATOM   213  C  CA    . ALA A 1 28  ? -5.868  34.713  -43.173 1.00 76.71  ? 28  ALA A CA    1 
ATOM   214  C  C     . ALA A 1 28  ? -5.868  34.223  -41.721 1.00 77.55  ? 28  ALA A C     1 
ATOM   215  O  O     . ALA A 1 28  ? -6.880  34.374  -41.032 1.00 80.86  ? 28  ALA A O     1 
ATOM   216  C  CB    . ALA A 1 28  ? -6.674  33.795  -44.070 1.00 74.75  ? 28  ALA A CB    1 
ATOM   217  N  N     . ILE A 1 29  ? -4.733  33.642  -41.280 1.00 74.41  ? 29  ILE A N     1 
ATOM   218  C  CA    . ILE A 1 29  ? -4.552  33.105  -39.936 1.00 69.11  ? 29  ILE A CA    1 
ATOM   219  C  C     . ILE A 1 29  ? -3.991  34.190  -39.011 1.00 64.03  ? 29  ILE A C     1 
ATOM   220  O  O     . ILE A 1 29  ? -4.399  34.307  -37.857 1.00 58.76  ? 29  ILE A O     1 
ATOM   221  C  CB    . ILE A 1 29  ? -3.637  31.858  -39.954 1.00 65.03  ? 29  ILE A CB    1 
ATOM   222  C  CG1   . ILE A 1 29  ? -4.159  30.755  -40.882 1.00 61.10  ? 29  ILE A CG1   1 
ATOM   223  C  CG2   . ILE A 1 29  ? -3.387  31.346  -38.541 1.00 62.68  ? 29  ILE A CG2   1 
ATOM   224  C  CD1   . ILE A 1 29  ? -5.412  30.069  -40.400 1.00 61.01  ? 29  ILE A CD1   1 
ATOM   225  N  N     . VAL A 1 30  ? -3.042  34.981  -39.508 1.00 65.40  ? 30  VAL A N     1 
ATOM   226  C  CA    . VAL A 1 30  ? -2.477  36.040  -38.686 1.00 70.07  ? 30  VAL A CA    1 
ATOM   227  C  C     . VAL A 1 30  ? -3.540  37.093  -38.368 1.00 69.81  ? 30  VAL A C     1 
ATOM   228  O  O     . VAL A 1 30  ? -3.470  37.687  -37.293 1.00 69.88  ? 30  VAL A O     1 
ATOM   229  C  CB    . VAL A 1 30  ? -1.228  36.683  -39.311 1.00 73.48  ? 30  VAL A CB    1 
ATOM   230  C  CG1   . VAL A 1 30  ? -0.569  37.633  -38.320 1.00 75.19  ? 30  VAL A CG1   1 
ATOM   231  C  CG2   . VAL A 1 30  ? -0.221  35.649  -39.792 1.00 72.39  ? 30  VAL A CG2   1 
ATOM   232  N  N     . ASN A 1 31  ? -4.521  37.290  -39.272 1.00 70.04  ? 31  ASN A N     1 
ATOM   233  C  CA    . ASN A 1 31  ? -5.511  38.359  -39.142 1.00 74.66  ? 31  ASN A CA    1 
ATOM   234  C  C     . ASN A 1 31  ? -6.729  37.892  -38.363 1.00 71.88  ? 31  ASN A C     1 
ATOM   235  O  O     . ASN A 1 31  ? -7.265  38.642  -37.550 1.00 77.06  ? 31  ASN A O     1 
ATOM   236  C  CB    . ASN A 1 31  ? -5.989  38.927  -40.483 1.00 78.96  ? 31  ASN A CB    1 
ATOM   237  C  CG    . ASN A 1 31  ? -4.854  39.533  -41.289 1.00 85.81  ? 31  ASN A CG    1 
ATOM   238  O  OD1   . ASN A 1 31  ? -3.863  40.003  -40.726 1.00 80.41  ? 31  ASN A OD1   1 
ATOM   239  N  ND2   . ASN A 1 31  ? -4.954  39.465  -42.609 1.00 88.12  ? 31  ASN A ND2   1 
ATOM   240  N  N     . TYR A 1 32  ? -7.188  36.670  -38.634 1.00 66.83  ? 32  TYR A N     1 
ATOM   241  C  CA    . TYR A 1 32  ? -8.138  36.053  -37.730 1.00 59.00  ? 32  TYR A CA    1 
ATOM   242  C  C     . TYR A 1 32  ? -7.579  36.164  -36.308 1.00 62.16  ? 32  TYR A C     1 
ATOM   243  O  O     . TYR A 1 32  ? -8.248  36.691  -35.415 1.00 60.08  ? 32  TYR A O     1 
ATOM   244  C  CB    . TYR A 1 32  ? -8.397  34.611  -38.163 1.00 53.97  ? 32  TYR A CB    1 
ATOM   245  C  CG    . TYR A 1 32  ? -9.480  33.937  -37.336 1.00 51.19  ? 32  TYR A CG    1 
ATOM   246  C  CD1   . TYR A 1 32  ? -10.827 34.031  -37.670 1.00 51.78  ? 32  TYR A CD1   1 
ATOM   247  C  CD2   . TYR A 1 32  ? -9.155  33.259  -36.173 1.00 50.89  ? 32  TYR A CD2   1 
ATOM   248  C  CE1   . TYR A 1 32  ? -11.806 33.426  -36.890 1.00 52.51  ? 32  TYR A CE1   1 
ATOM   249  C  CE2   . TYR A 1 32  ? -10.126 32.681  -35.372 1.00 50.27  ? 32  TYR A CE2   1 
ATOM   250  C  CZ    . TYR A 1 32  ? -11.455 32.752  -35.731 1.00 51.76  ? 32  TYR A CZ    1 
ATOM   251  O  OH    . TYR A 1 32  ? -12.357 32.116  -34.911 1.00 53.94  ? 32  TYR A OH    1 
ATOM   252  N  N     . ALA A 1 33  ? -6.318  35.731  -36.125 1.00 62.47  ? 33  ALA A N     1 
ATOM   253  C  CA    . ALA A 1 33  ? -5.747  35.554  -34.795 1.00 64.71  ? 33  ALA A CA    1 
ATOM   254  C  C     . ALA A 1 33  ? -5.708  36.878  -34.038 1.00 69.05  ? 33  ALA A C     1 
ATOM   255  O  O     . ALA A 1 33  ? -6.146  36.921  -32.887 1.00 68.56  ? 33  ALA A O     1 
ATOM   256  C  CB    . ALA A 1 33  ? -4.384  34.917  -34.874 1.00 61.79  ? 33  ALA A CB    1 
ATOM   257  N  N     . LYS A 1 34  ? -5.185  37.930  -34.690 1.00 74.17  ? 34  LYS A N     1 
ATOM   258  C  CA    . LYS A 1 34  ? -5.136  39.273  -34.124 1.00 78.03  ? 34  LYS A CA    1 
ATOM   259  C  C     . LYS A 1 34  ? -6.547  39.769  -33.806 1.00 77.78  ? 34  LYS A C     1 
ATOM   260  O  O     . LYS A 1 34  ? -6.811  40.255  -32.704 1.00 69.30  ? 34  LYS A O     1 
ATOM   261  C  CB    . LYS A 1 34  ? -4.479  40.248  -35.104 1.00 86.40  ? 34  LYS A CB    1 
ATOM   262  C  CG    . LYS A 1 34  ? -4.314  41.676  -34.582 1.00 95.33  ? 34  LYS A CG    1 
ATOM   263  C  CD    . LYS A 1 34  ? -4.524  42.763  -35.629 1.00 98.99  ? 34  LYS A CD    1 
ATOM   264  C  CE    . LYS A 1 34  ? -5.948  42.869  -36.149 1.00 102.75 ? 34  LYS A CE    1 
ATOM   265  N  NZ    . LYS A 1 34  ? -6.896  43.391  -35.135 1.00 101.51 ? 34  LYS A NZ    1 
ATOM   266  N  N     . ARG A 1 35  ? -7.452  39.629  -34.784 1.00 78.41  ? 35  ARG A N     1 
ATOM   267  C  CA    . ARG A 1 35  ? -8.820  40.080  -34.620 1.00 82.08  ? 35  ARG A CA    1 
ATOM   268  C  C     . ARG A 1 35  ? -9.406  39.452  -33.357 1.00 77.42  ? 35  ARG A C     1 
ATOM   269  O  O     . ARG A 1 35  ? -10.111 40.130  -32.618 1.00 78.36  ? 35  ARG A O     1 
ATOM   270  C  CB    . ARG A 1 35  ? -9.684  39.801  -35.861 1.00 86.51  ? 35  ARG A CB    1 
ATOM   271  C  CG    . ARG A 1 35  ? -9.427  40.731  -37.043 1.00 93.59  ? 35  ARG A CG    1 
ATOM   272  C  CD    . ARG A 1 35  ? -10.579 40.840  -38.041 1.00 100.05 ? 35  ARG A CD    1 
ATOM   273  N  NE    . ARG A 1 35  ? -11.293 39.591  -38.332 1.00 102.27 ? 35  ARG A NE    1 
ATOM   274  C  CZ    . ARG A 1 35  ? -11.008 38.742  -39.326 1.00 97.50  ? 35  ARG A CZ    1 
ATOM   275  N  NH1   . ARG A 1 35  ? -11.832 37.738  -39.592 1.00 89.94  ? 35  ARG A NH1   1 
ATOM   276  N  NH2   . ARG A 1 35  ? -9.913  38.899  -40.057 1.00 91.15  ? 35  ARG A NH2   1 
ATOM   277  N  N     . ARG A 1 36  ? -9.084  38.186  -33.068 1.00 72.21  ? 36  ARG A N     1 
ATOM   278  C  CA    . ARG A 1 36  ? -9.625  37.552  -31.875 1.00 67.77  ? 36  ARG A CA    1 
ATOM   279  C  C     . ARG A 1 36  ? -8.698  37.788  -30.674 1.00 67.14  ? 36  ARG A C     1 
ATOM   280  O  O     . ARG A 1 36  ? -8.975  37.306  -29.583 1.00 65.91  ? 36  ARG A O     1 
ATOM   281  C  CB    . ARG A 1 36  ? -9.887  36.068  -32.145 1.00 68.04  ? 36  ARG A CB    1 
ATOM   282  C  CG    . ARG A 1 36  ? -10.641 35.787  -33.438 1.00 74.79  ? 36  ARG A CG    1 
ATOM   283  C  CD    . ARG A 1 36  ? -12.151 35.948  -33.371 1.00 84.09  ? 36  ARG A CD    1 
ATOM   284  N  NE    . ARG A 1 36  ? -12.802 35.770  -34.674 1.00 95.42  ? 36  ARG A NE    1 
ATOM   285  C  CZ    . ARG A 1 36  ? -12.870 36.687  -35.645 1.00 107.96 ? 36  ARG A CZ    1 
ATOM   286  N  NH1   . ARG A 1 36  ? -12.467 37.927  -35.427 1.00 121.70 ? 36  ARG A NH1   1 
ATOM   287  N  NH2   . ARG A 1 36  ? -13.382 36.377  -36.826 1.00 104.85 ? 36  ARG A NH2   1 
ATOM   288  N  N     . LYS A 1 37  ? -7.609  38.544  -30.864 1.00 68.84  ? 37  LYS A N     1 
ATOM   289  C  CA    . LYS A 1 37  ? -6.592  38.750  -29.841 1.00 79.61  ? 37  LYS A CA    1 
ATOM   290  C  C     . LYS A 1 37  ? -6.197  37.438  -29.162 1.00 76.19  ? 37  LYS A C     1 
ATOM   291  O  O     . LYS A 1 37  ? -6.099  37.384  -27.932 1.00 74.18  ? 37  LYS A O     1 
ATOM   292  C  CB    . LYS A 1 37  ? -7.061  39.744  -28.772 1.00 89.66  ? 37  LYS A CB    1 
ATOM   293  C  CG    . LYS A 1 37  ? -7.381  41.146  -29.271 1.00 99.92  ? 37  LYS A CG    1 
ATOM   294  C  CD    . LYS A 1 37  ? -7.264  42.213  -28.195 1.00 108.23 ? 37  LYS A CD    1 
ATOM   295  C  CE    . LYS A 1 37  ? -8.229  42.022  -27.042 1.00 110.54 ? 37  LYS A CE    1 
ATOM   296  N  NZ    . LYS A 1 37  ? -9.618  42.388  -27.408 1.00 109.90 ? 37  LYS A NZ    1 
ATOM   297  N  N     . LYS A 1 38  ? -5.941  36.395  -29.968 1.00 72.44  ? 38  LYS A N     1 
ATOM   298  C  CA    . LYS A 1 38  ? -5.524  35.103  -29.441 1.00 68.78  ? 38  LYS A CA    1 
ATOM   299  C  C     . LYS A 1 38  ? -4.373  34.571  -30.287 1.00 61.98  ? 38  LYS A C     1 
ATOM   300  O  O     . LYS A 1 38  ? -4.274  34.875  -31.480 1.00 58.64  ? 38  LYS A O     1 
ATOM   301  C  CB    . LYS A 1 38  ? -6.696  34.117  -29.411 1.00 71.52  ? 38  LYS A CB    1 
ATOM   302  C  CG    . LYS A 1 38  ? -6.680  33.166  -28.224 1.00 77.91  ? 38  LYS A CG    1 
ATOM   303  C  CD    . LYS A 1 38  ? -7.433  31.870  -28.475 1.00 86.65  ? 38  LYS A CD    1 
ATOM   304  C  CE    . LYS A 1 38  ? -7.457  30.917  -27.292 1.00 88.85  ? 38  LYS A CE    1 
ATOM   305  N  NZ    . LYS A 1 38  ? -6.154  30.862  -26.585 1.00 89.61  ? 38  LYS A NZ    1 
ATOM   306  N  N     . ARG A 1 39  ? -3.488  33.795  -29.649 1.00 58.21  ? 39  ARG A N     1 
ATOM   307  C  CA    . ARG A 1 39  ? -2.330  33.253  -30.342 1.00 56.79  ? 39  ARG A CA    1 
ATOM   308  C  C     . ARG A 1 39  ? -2.810  32.209  -31.350 1.00 48.80  ? 39  ARG A C     1 
ATOM   309  O  O     . ARG A 1 39  ? -3.638  31.380  -31.018 1.00 43.62  ? 39  ARG A O     1 
ATOM   310  C  CB    . ARG A 1 39  ? -1.324  32.711  -29.325 1.00 62.43  ? 39  ARG A CB    1 
ATOM   311  C  CG    . ARG A 1 39  ? -0.682  33.808  -28.485 1.00 69.31  ? 39  ARG A CG    1 
ATOM   312  C  CD    . ARG A 1 39  ? 0.633   33.348  -27.894 1.00 79.07  ? 39  ARG A CD    1 
ATOM   313  N  NE    . ARG A 1 39  ? 0.501   32.477  -26.729 1.00 84.60  ? 39  ARG A NE    1 
ATOM   314  C  CZ    . ARG A 1 39  ? 1.318   32.498  -25.672 1.00 90.40  ? 39  ARG A CZ    1 
ATOM   315  N  NH1   . ARG A 1 39  ? 2.319   33.367  -25.608 1.00 87.10  ? 39  ARG A NH1   1 
ATOM   316  N  NH2   . ARG A 1 39  ? 1.132   31.644  -24.678 1.00 89.42  ? 39  ARG A NH2   1 
ATOM   317  N  N     . PRO A 1 40  ? -2.407  32.290  -32.637 1.00 46.34  ? 40  PRO A N     1 
ATOM   318  C  CA    . PRO A 1 40  ? -2.974  31.453  -33.688 1.00 42.70  ? 40  PRO A CA    1 
ATOM   319  C  C     . PRO A 1 40  ? -2.849  29.957  -33.449 1.00 42.14  ? 40  PRO A C     1 
ATOM   320  O  O     . PRO A 1 40  ? -3.707  29.189  -33.893 1.00 36.63  ? 40  PRO A O     1 
ATOM   321  C  CB    . PRO A 1 40  ? -2.214  31.795  -34.972 1.00 45.56  ? 40  PRO A CB    1 
ATOM   322  C  CG    . PRO A 1 40  ? -1.117  32.754  -34.553 1.00 49.77  ? 40  PRO A CG    1 
ATOM   323  C  CD    . PRO A 1 40  ? -1.461  33.280  -33.170 1.00 50.14  ? 40  PRO A CD    1 
ATOM   324  N  N     . GLU A 1 41  ? -1.816  29.545  -32.707 1.00 41.66  ? 41  GLU A N     1 
ATOM   325  C  CA    . GLU A 1 41  ? -1.650  28.126  -32.453 1.00 43.27  ? 41  GLU A CA    1 
ATOM   326  C  C     . GLU A 1 41  ? -2.692  27.600  -31.458 1.00 42.21  ? 41  GLU A C     1 
ATOM   327  O  O     . GLU A 1 41  ? -2.864  26.385  -31.352 1.00 41.61  ? 41  GLU A O     1 
ATOM   328  C  CB    . GLU A 1 41  ? -0.224  27.809  -31.998 1.00 45.22  ? 41  GLU A CB    1 
ATOM   329  C  CG    . GLU A 1 41  ? 0.169   28.447  -30.686 1.00 45.56  ? 41  GLU A CG    1 
ATOM   330  C  CD    . GLU A 1 41  ? 0.717   29.856  -30.813 1.00 47.60  ? 41  GLU A CD    1 
ATOM   331  O  OE1   . GLU A 1 41  ? 1.388   30.318  -29.860 1.00 50.56  ? 41  GLU A OE1   1 
ATOM   332  O  OE2   . GLU A 1 41  ? 0.440   30.495  -31.848 1.00 50.01  ? 41  GLU A OE2   1 
ATOM   333  N  N     . LYS A 1 42  ? -3.366  28.494  -30.728 1.00 41.51  ? 42  LYS A N     1 
ATOM   334  C  CA    . LYS A 1 42  ? -4.311  28.088  -29.698 1.00 42.69  ? 42  LYS A CA    1 
ATOM   335  C  C     . LYS A 1 42  ? -5.714  27.907  -30.256 1.00 38.60  ? 42  LYS A C     1 
ATOM   336  O  O     . LYS A 1 42  ? -6.552  27.293  -29.621 1.00 39.93  ? 42  LYS A O     1 
ATOM   337  C  CB    . LYS A 1 42  ? -4.351  29.148  -28.601 1.00 47.70  ? 42  LYS A CB    1 
ATOM   338  C  CG    . LYS A 1 42  ? -2.985  29.554  -28.055 1.00 51.00  ? 42  LYS A CG    1 
ATOM   339  C  CD    . LYS A 1 42  ? -2.181  28.371  -27.572 1.00 54.15  ? 42  LYS A CD    1 
ATOM   340  C  CE    . LYS A 1 42  ? -1.172  28.794  -26.532 1.00 61.39  ? 42  LYS A CE    1 
ATOM   341  N  NZ    . LYS A 1 42  ? -0.225  27.693  -26.237 1.00 65.43  ? 42  LYS A NZ    1 
ATOM   342  N  N     . ILE A 1 43  ? -5.926  28.413  -31.467 1.00 37.16  ? 43  ILE A N     1 
ATOM   343  C  CA    . ILE A 1 43  ? -7.214  28.480  -32.116 1.00 35.29  ? 43  ILE A CA    1 
ATOM   344  C  C     . ILE A 1 43  ? -7.518  27.162  -32.825 1.00 34.57  ? 43  ILE A C     1 
ATOM   345  O  O     . ILE A 1 43  ? -6.631  26.573  -33.454 1.00 31.04  ? 43  ILE A O     1 
ATOM   346  C  CB    . ILE A 1 43  ? -7.212  29.670  -33.092 1.00 36.78  ? 43  ILE A CB    1 
ATOM   347  C  CG1   . ILE A 1 43  ? -7.019  30.970  -32.310 1.00 38.99  ? 43  ILE A CG1   1 
ATOM   348  C  CG2   . ILE A 1 43  ? -8.475  29.681  -33.947 1.00 36.32  ? 43  ILE A CG2   1 
ATOM   349  C  CD1   . ILE A 1 43  ? -7.124  32.224  -33.126 1.00 42.31  ? 43  ILE A CD1   1 
ATOM   350  N  N     . ILE A 1 44  ? -8.794  26.736  -32.720 1.00 32.28  ? 44  ILE A N     1 
ATOM   351  C  CA    . ILE A 1 44  ? -9.274  25.552  -33.411 1.00 30.65  ? 44  ILE A CA    1 
ATOM   352  C  C     . ILE A 1 44  ? -9.462  25.849  -34.902 1.00 30.72  ? 44  ILE A C     1 
ATOM   353  O  O     . ILE A 1 44  ? -10.072 26.829  -35.306 1.00 31.70  ? 44  ILE A O     1 
ATOM   354  C  CB    . ILE A 1 44  ? -10.569 25.036  -32.766 1.00 29.58  ? 44  ILE A CB    1 
ATOM   355  C  CG1   . ILE A 1 44  ? -10.363 24.584  -31.321 1.00 29.67  ? 44  ILE A CG1   1 
ATOM   356  C  CG2   . ILE A 1 44  ? -11.158 23.930  -33.613 1.00 30.33  ? 44  ILE A CG2   1 
ATOM   357  C  CD1   . ILE A 1 44  ? -9.367  23.464  -31.140 1.00 31.73  ? 44  ILE A CD1   1 
ATOM   358  N  N     . LEU A 1 45  ? -8.925  24.977  -35.746 1.00 31.15  ? 45  LEU A N     1 
ATOM   359  C  CA    . LEU A 1 45  ? -9.069  25.162  -37.173 1.00 30.80  ? 45  LEU A CA    1 
ATOM   360  C  C     . LEU A 1 45  ? -10.558 25.015  -37.526 1.00 30.59  ? 45  LEU A C     1 
ATOM   361  O  O     . LEU A 1 45  ? -11.233 24.049  -37.129 1.00 26.39  ? 45  LEU A O     1 
ATOM   362  C  CB    . LEU A 1 45  ? -8.165  24.159  -37.892 1.00 29.82  ? 45  LEU A CB    1 
ATOM   363  C  CG    . LEU A 1 45  ? -8.113  24.313  -39.408 1.00 32.07  ? 45  LEU A CG    1 
ATOM   364  C  CD1   . LEU A 1 45  ? -7.281  25.523  -39.830 1.00 34.55  ? 45  LEU A CD1   1 
ATOM   365  C  CD2   . LEU A 1 45  ? -7.569  23.048  -40.045 1.00 31.47  ? 45  LEU A CD2   1 
ATOM   366  N  N     . ASP A 1 46  ? -11.037 26.014  -38.275 1.00 32.13  ? 46  ASP A N     1 
ATOM   367  C  CA    . ASP A 1 46  ? -12.422 26.162  -38.692 1.00 32.74  ? 46  ASP A CA    1 
ATOM   368  C  C     . ASP A 1 46  ? -12.397 26.560  -40.167 1.00 33.59  ? 46  ASP A C     1 
ATOM   369  O  O     . ASP A 1 46  ? -11.990 27.666  -40.496 1.00 33.06  ? 46  ASP A O     1 
ATOM   370  C  CB    . ASP A 1 46  ? -13.123 27.189  -37.809 1.00 33.35  ? 46  ASP A CB    1 
ATOM   371  C  CG    . ASP A 1 46  ? -14.629 27.249  -37.974 1.00 36.18  ? 46  ASP A CG    1 
ATOM   372  O  OD1   . ASP A 1 46  ? -15.110 26.698  -38.964 1.00 36.17  ? 46  ASP A OD1   1 
ATOM   373  O  OD2   . ASP A 1 46  ? -15.309 27.796  -37.054 1.00 38.15  ? 46  ASP A OD2   1 
ATOM   374  N  N     . SER A 1 47  ? -12.798 25.636  -41.043 1.00 35.02  ? 47  SER A N     1 
ATOM   375  C  CA    . SER A 1 47  ? -12.697 25.794  -42.487 1.00 38.18  ? 47  SER A CA    1 
ATOM   376  C  C     . SER A 1 47  ? -13.629 26.902  -42.967 1.00 39.93  ? 47  SER A C     1 
ATOM   377  O  O     . SER A 1 47  ? -13.425 27.472  -44.030 1.00 39.07  ? 47  SER A O     1 
ATOM   378  C  CB    . SER A 1 47  ? -13.037 24.497  -43.183 1.00 38.91  ? 47  SER A CB    1 
ATOM   379  O  OG    . SER A 1 47  ? -14.451 24.295  -43.188 1.00 38.89  ? 47  SER A OG    1 
ATOM   380  N  N     . THR A 1 48  ? -14.645 27.214  -42.160 1.00 40.97  ? 48  THR A N     1 
ATOM   381  C  CA    . THR A 1 48  ? -15.587 28.269  -42.500 1.00 44.51  ? 48  THR A CA    1 
ATOM   382  C  C     . THR A 1 48  ? -14.867 29.620  -42.537 1.00 49.47  ? 48  THR A C     1 
ATOM   383  O  O     . THR A 1 48  ? -15.094 30.405  -43.470 1.00 51.95  ? 48  THR A O     1 
ATOM   384  C  CB    . THR A 1 48  ? -16.810 28.192  -41.574 1.00 40.92  ? 48  THR A CB    1 
ATOM   385  O  OG1   . THR A 1 48  ? -17.564 27.030  -41.938 1.00 37.53  ? 48  THR A OG1   1 
ATOM   386  C  CG2   . THR A 1 48  ? -17.656 29.438  -41.655 1.00 42.08  ? 48  THR A CG2   1 
ATOM   387  N  N     . TYR A 1 49  ? -13.977 29.868  -41.562 1.00 50.43  ? 49  TYR A N     1 
ATOM   388  C  CA    . TYR A 1 49  ? -13.255 31.134  -41.492 1.00 60.17  ? 49  TYR A CA    1 
ATOM   389  C  C     . TYR A 1 49  ? -11.916 31.071  -42.243 1.00 61.94  ? 49  TYR A C     1 
ATOM   390  O  O     . TYR A 1 49  ? -11.447 32.049  -42.808 1.00 59.56  ? 49  TYR A O     1 
ATOM   391  C  CB    . TYR A 1 49  ? -12.972 31.521  -40.037 1.00 67.43  ? 49  TYR A CB    1 
ATOM   392  C  CG    . TYR A 1 49  ? -14.151 31.933  -39.158 1.00 80.88  ? 49  TYR A CG    1 
ATOM   393  C  CD1   . TYR A 1 49  ? -15.147 32.809  -39.604 1.00 86.93  ? 49  TYR A CD1   1 
ATOM   394  C  CD2   . TYR A 1 49  ? -14.235 31.488  -37.839 1.00 85.18  ? 49  TYR A CD2   1 
ATOM   395  C  CE1   . TYR A 1 49  ? -16.203 33.187  -38.782 1.00 85.09  ? 49  TYR A CE1   1 
ATOM   396  C  CE2   . TYR A 1 49  ? -15.273 31.878  -37.004 1.00 84.38  ? 49  TYR A CE2   1 
ATOM   397  C  CZ    . TYR A 1 49  ? -16.260 32.730  -37.471 1.00 82.35  ? 49  TYR A CZ    1 
ATOM   398  O  OH    . TYR A 1 49  ? -17.250 33.097  -36.600 1.00 73.86  ? 49  TYR A OH    1 
ATOM   399  N  N     . HIS A 1 50  ? -11.284 29.902  -42.259 1.00 62.95  ? 50  HIS A N     1 
ATOM   400  C  CA    . HIS A 1 50  ? -9.883  29.802  -42.612 1.00 61.28  ? 50  HIS A CA    1 
ATOM   401  C  C     . HIS A 1 50  ? -9.689  29.173  -43.995 1.00 65.44  ? 50  HIS A C     1 
ATOM   402  O  O     . HIS A 1 50  ? -8.601  28.661  -44.262 1.00 65.01  ? 50  HIS A O     1 
ATOM   403  C  CB    . HIS A 1 50  ? -9.155  28.938  -41.575 1.00 56.57  ? 50  HIS A CB    1 
ATOM   404  C  CG    . HIS A 1 50  ? -9.320  29.339  -40.148 1.00 53.26  ? 50  HIS A CG    1 
ATOM   405  N  ND1   . HIS A 1 50  ? -9.470  28.405  -39.142 1.00 45.66  ? 50  HIS A ND1   1 
ATOM   406  C  CD2   . HIS A 1 50  ? -9.290  30.535  -39.547 1.00 51.59  ? 50  HIS A CD2   1 
ATOM   407  C  CE1   . HIS A 1 50  ? -9.522  29.019  -37.974 1.00 45.75  ? 50  HIS A CE1   1 
ATOM   408  N  NE2   . HIS A 1 50  ? -9.419  30.315  -38.198 1.00 51.16  ? 50  HIS A NE2   1 
ATOM   409  N  N     . HIS A 1 51  ? -10.710 29.236  -44.867 1.00 66.67  ? 51  HIS A N     1 
ATOM   410  C  CA    . HIS A 1 51  ? -10.741 28.440  -46.090 1.00 69.38  ? 51  HIS A CA    1 
ATOM   411  C  C     . HIS A 1 51  ? -9.594  28.783  -47.046 1.00 71.30  ? 51  HIS A C     1 
ATOM   412  O  O     . HIS A 1 51  ? -9.019  27.884  -47.673 1.00 63.88  ? 51  HIS A O     1 
ATOM   413  C  CB    . HIS A 1 51  ? -12.076 28.574  -46.832 1.00 74.83  ? 51  HIS A CB    1 
ATOM   414  C  CG    . HIS A 1 51  ? -12.636 29.954  -46.930 1.00 80.41  ? 51  HIS A CG    1 
ATOM   415  N  ND1   . HIS A 1 51  ? -12.579 30.689  -48.096 1.00 89.71  ? 51  HIS A ND1   1 
ATOM   416  C  CD2   . HIS A 1 51  ? -13.283 30.717  -46.040 1.00 80.18  ? 51  HIS A CD2   1 
ATOM   417  C  CE1   . HIS A 1 51  ? -13.182 31.857  -47.910 1.00 88.89  ? 51  HIS A CE1   1 
ATOM   418  N  NE2   . HIS A 1 51  ? -13.621 31.893  -46.669 1.00 88.05  ? 51  HIS A NE2   1 
ATOM   419  N  N     . ALA A 1 52  ? -9.269  30.082  -47.150 1.00 72.04  ? 52  ALA A N     1 
ATOM   420  C  CA    . ALA A 1 52  ? -8.187  30.540  -48.012 1.00 70.20  ? 52  ALA A CA    1 
ATOM   421  C  C     . ALA A 1 52  ? -6.818  30.033  -47.525 1.00 67.84  ? 52  ALA A C     1 
ATOM   422  O  O     . ALA A 1 52  ? -5.885  29.997  -48.322 1.00 73.64  ? 52  ALA A O     1 
ATOM   423  C  CB    . ALA A 1 52  ? -8.229  32.048  -48.152 1.00 69.84  ? 52  ALA A CB    1 
ATOM   424  N  N     . ALA A 1 53  ? -6.684  29.580  -46.264 1.00 62.78  ? 53  ALA A N     1 
ATOM   425  C  CA    . ALA A 1 53  ? -5.407  29.044  -45.783 1.00 63.51  ? 53  ALA A CA    1 
ATOM   426  C  C     . ALA A 1 53  ? -5.306  27.515  -45.891 1.00 62.24  ? 53  ALA A C     1 
ATOM   427  O  O     . ALA A 1 53  ? -4.250  26.954  -45.581 1.00 63.08  ? 53  ALA A O     1 
ATOM   428  C  CB    . ALA A 1 53  ? -5.147  29.493  -44.362 1.00 58.98  ? 53  ALA A CB    1 
ATOM   429  N  N     . LEU A 1 54  ? -6.365  26.825  -46.339 1.00 59.77  ? 54  LEU A N     1 
ATOM   430  C  CA    . LEU A 1 54  ? -6.324  25.367  -46.382 1.00 61.14  ? 54  LEU A CA    1 
ATOM   431  C  C     . LEU A 1 54  ? -5.876  24.861  -47.756 1.00 66.24  ? 54  LEU A C     1 
ATOM   432  O  O     . LEU A 1 54  ? -5.521  23.679  -47.879 1.00 61.71  ? 54  LEU A O     1 
ATOM   433  C  CB    . LEU A 1 54  ? -7.702  24.802  -46.009 1.00 57.32  ? 54  LEU A CB    1 
ATOM   434  C  CG    . LEU A 1 54  ? -8.135  24.968  -44.548 1.00 58.36  ? 54  LEU A CG    1 
ATOM   435  C  CD1   . LEU A 1 54  ? -9.448  24.247  -44.275 1.00 57.25  ? 54  LEU A CD1   1 
ATOM   436  C  CD2   . LEU A 1 54  ? -7.078  24.461  -43.579 1.00 58.44  ? 54  LEU A CD2   1 
ATOM   437  N  N     . ARG A 1 55  ? -5.890  25.766  -48.758 1.00 72.69  ? 55  ARG A N     1 
ATOM   438  C  CA    . ARG A 1 55  ? -5.693  25.452  -50.172 1.00 77.32  ? 55  ARG A CA    1 
ATOM   439  C  C     . ARG A 1 55  ? -4.468  24.556  -50.390 1.00 79.18  ? 55  ARG A C     1 
ATOM   440  O  O     . ARG A 1 55  ? -4.527  23.573  -51.138 1.00 76.50  ? 55  ARG A O     1 
ATOM   441  C  CB    . ARG A 1 55  ? -5.500  26.734  -50.991 1.00 82.77  ? 55  ARG A CB    1 
ATOM   442  C  CG    . ARG A 1 55  ? -6.716  27.646  -51.085 1.00 90.15  ? 55  ARG A CG    1 
ATOM   443  C  CD    . ARG A 1 55  ? -6.417  28.856  -51.969 1.00 96.64  ? 55  ARG A CD    1 
ATOM   444  N  NE    . ARG A 1 55  ? -7.384  29.951  -51.860 1.00 99.20  ? 55  ARG A NE    1 
ATOM   445  C  CZ    . ARG A 1 55  ? -8.626  29.954  -52.353 1.00 99.06  ? 55  ARG A CZ    1 
ATOM   446  N  NH1   . ARG A 1 55  ? -9.064  28.957  -53.106 1.00 98.71  ? 55  ARG A NH1   1 
ATOM   447  N  NH2   . ARG A 1 55  ? -9.428  30.977  -52.104 1.00 98.07  ? 55  ARG A NH2   1 
ATOM   448  N  N     . GLN A 1 56  ? -3.347  24.905  -49.746 1.00 77.62  ? 56  GLN A N     1 
ATOM   449  C  CA    . GLN A 1 56  ? -2.100  24.195  -49.995 1.00 85.17  ? 56  GLN A CA    1 
ATOM   450  C  C     . GLN A 1 56  ? -1.848  23.136  -48.914 1.00 79.57  ? 56  GLN A C     1 
ATOM   451  O  O     . GLN A 1 56  ? -1.023  22.254  -49.141 1.00 74.59  ? 56  GLN A O     1 
ATOM   452  C  CB    . GLN A 1 56  ? -0.925  25.162  -50.227 1.00 96.21  ? 56  GLN A CB    1 
ATOM   453  C  CG    . GLN A 1 56  ? -1.001  26.499  -49.490 1.00 101.44 ? 56  GLN A CG    1 
ATOM   454  C  CD    . GLN A 1 56  ? -1.143  26.333  -47.993 1.00 103.67 ? 56  GLN A CD    1 
ATOM   455  O  OE1   . GLN A 1 56  ? -0.336  25.670  -47.342 1.00 99.00  ? 56  GLN A OE1   1 
ATOM   456  N  NE2   . GLN A 1 56  ? -2.191  26.917  -47.434 1.00 104.35 ? 56  GLN A NE2   1 
ATOM   457  N  N     . LEU A 1 57  ? -2.580  23.180  -47.781 1.00 73.60  ? 57  LEU A N     1 
ATOM   458  C  CA    . LEU A 1 57  ? -2.486  22.152  -46.747 1.00 66.80  ? 57  LEU A CA    1 
ATOM   459  C  C     . LEU A 1 57  ? -2.789  20.783  -47.332 1.00 67.12  ? 57  LEU A C     1 
ATOM   460  O  O     . LEU A 1 57  ? -3.651  20.662  -48.204 1.00 67.33  ? 57  LEU A O     1 
ATOM   461  C  CB    . LEU A 1 57  ? -3.488  22.400  -45.616 1.00 63.55  ? 57  LEU A CB    1 
ATOM   462  C  CG    . LEU A 1 57  ? -2.928  22.926  -44.301 1.00 63.83  ? 57  LEU A CG    1 
ATOM   463  C  CD1   . LEU A 1 57  ? -3.996  22.833  -43.238 1.00 61.83  ? 57  LEU A CD1   1 
ATOM   464  C  CD2   . LEU A 1 57  ? -1.684  22.170  -43.867 1.00 67.45  ? 57  LEU A CD2   1 
ATOM   465  N  N     . GLU A 1 58  ? -2.103  19.764  -46.794 1.00 70.08  ? 58  GLU A N     1 
ATOM   466  C  CA    . GLU A 1 58  ? -2.398  18.376  -47.113 1.00 70.27  ? 58  GLU A CA    1 
ATOM   467  C  C     . GLU A 1 58  ? -3.796  18.072  -46.593 1.00 62.34  ? 58  GLU A C     1 
ATOM   468  O  O     . GLU A 1 58  ? -4.100  18.411  -45.450 1.00 58.04  ? 58  GLU A O     1 
ATOM   469  C  CB    . GLU A 1 58  ? -1.363  17.429  -46.495 1.00 74.38  ? 58  GLU A CB    1 
ATOM   470  C  CG    . GLU A 1 58  ? -1.661  15.962  -46.759 1.00 81.31  ? 58  GLU A CG    1 
ATOM   471  C  CD    . GLU A 1 58  ? -0.706  14.994  -46.088 1.00 89.42  ? 58  GLU A CD    1 
ATOM   472  O  OE1   . GLU A 1 58  ? -1.137  14.316  -45.134 1.00 91.63  ? 58  GLU A OE1   1 
ATOM   473  O  OE2   . GLU A 1 58  ? 0.459   14.909  -46.529 1.00 92.43  ? 58  GLU A OE2   1 
ATOM   474  N  N     . ASP A 1 59  ? -4.634  17.472  -47.450 1.00 61.47  ? 59  ASP A N     1 
ATOM   475  C  CA    . ASP A 1 59  ? -5.985  17.092  -47.075 1.00 61.88  ? 59  ASP A CA    1 
ATOM   476  C  C     . ASP A 1 59  ? -6.814  18.326  -46.748 1.00 57.81  ? 59  ASP A C     1 
ATOM   477  O  O     . ASP A 1 59  ? -7.831  18.217  -46.077 1.00 59.62  ? 59  ASP A O     1 
ATOM   478  C  CB    . ASP A 1 59  ? -6.003  16.210  -45.824 1.00 69.06  ? 59  ASP A CB    1 
ATOM   479  C  CG    . ASP A 1 59  ? -6.457  14.784  -46.040 1.00 71.80  ? 59  ASP A CG    1 
ATOM   480  O  OD1   . ASP A 1 59  ? -5.708  14.028  -46.721 1.00 71.95  ? 59  ASP A OD1   1 
ATOM   481  O  OD2   . ASP A 1 59  ? -7.533  14.441  -45.475 1.00 65.57  ? 59  ASP A OD2   1 
ATOM   482  N  N     . GLY A 1 60  ? -6.391  19.490  -47.238 1.00 59.24  ? 60  GLY A N     1 
ATOM   483  C  CA    . GLY A 1 60  ? -6.926  20.759  -46.772 1.00 58.09  ? 60  GLY A CA    1 
ATOM   484  C  C     . GLY A 1 60  ? -8.436  20.855  -46.940 1.00 59.49  ? 60  GLY A C     1 
ATOM   485  O  O     . GLY A 1 60  ? -9.109  21.470  -46.112 1.00 65.37  ? 60  GLY A O     1 
ATOM   486  N  N     . GLU A 1 61  ? -8.944  20.228  -48.009 1.00 61.37  ? 61  GLU A N     1 
ATOM   487  C  CA    . GLU A 1 61  ? -10.342 20.333  -48.393 1.00 66.05  ? 61  GLU A CA    1 
ATOM   488  C  C     . GLU A 1 61  ? -11.249 19.773  -47.293 1.00 62.08  ? 61  GLU A C     1 
ATOM   489  O  O     . GLU A 1 61  ? -12.362 20.268  -47.136 1.00 70.16  ? 61  GLU A O     1 
ATOM   490  C  CB    . GLU A 1 61  ? -10.601 19.644  -49.738 1.00 71.30  ? 61  GLU A CB    1 
ATOM   491  C  CG    . GLU A 1 61  ? -11.054 18.181  -49.641 1.00 75.36  ? 61  GLU A CG    1 
ATOM   492  C  CD    . GLU A 1 61  ? -9.988  17.088  -49.568 1.00 84.97  ? 61  GLU A CD    1 
ATOM   493  O  OE1   . GLU A 1 61  ? -10.373 15.893  -49.395 1.00 86.89  ? 61  GLU A OE1   1 
ATOM   494  O  OE2   . GLU A 1 61  ? -8.775  17.409  -49.720 1.00 87.51  ? 61  GLU A OE2   1 
ATOM   495  N  N     . ARG A 1 62  ? -10.791 18.766  -46.530 1.00 55.19  ? 62  ARG A N     1 
ATOM   496  C  CA    . ARG A 1 62  ? -11.662 18.107  -45.563 1.00 54.95  ? 62  ARG A CA    1 
ATOM   497  C  C     . ARG A 1 62  ? -11.261 18.431  -44.119 1.00 48.87  ? 62  ARG A C     1 
ATOM   498  O  O     . ARG A 1 62  ? -11.831 17.864  -43.181 1.00 53.12  ? 62  ARG A O     1 
ATOM   499  C  CB    . ARG A 1 62  ? -11.726 16.597  -45.834 1.00 56.62  ? 62  ARG A CB    1 
ATOM   500  C  CG    . ARG A 1 62  ? -10.428 15.826  -45.646 1.00 57.72  ? 62  ARG A CG    1 
ATOM   501  C  CD    . ARG A 1 62  ? -10.575 14.380  -46.109 1.00 62.44  ? 62  ARG A CD    1 
ATOM   502  N  NE    . ARG A 1 62  ? -10.665 13.403  -45.024 1.00 62.72  ? 62  ARG A NE    1 
ATOM   503  C  CZ    . ARG A 1 62  ? -10.882 12.092  -45.172 1.00 58.98  ? 62  ARG A CZ    1 
ATOM   504  N  NH1   . ARG A 1 62  ? -11.340 11.591  -46.299 1.00 58.39  ? 62  ARG A NH1   1 
ATOM   505  N  NH2   . ARG A 1 62  ? -10.728 11.278  -44.146 1.00 64.70  ? 62  ARG A NH2   1 
ATOM   506  N  N     . ARG A 1 63  ? -10.340 19.388  -43.933 1.00 41.61  ? 63  ARG A N     1 
ATOM   507  C  CA    . ARG A 1 63  ? -9.851  19.740  -42.606 1.00 36.31  ? 63  ARG A CA    1 
ATOM   508  C  C     . ARG A 1 63  ? -10.578 20.951  -42.006 1.00 30.74  ? 63  ARG A C     1 
ATOM   509  O  O     . ARG A 1 63  ? -11.222 21.739  -42.682 1.00 29.56  ? 63  ARG A O     1 
ATOM   510  C  CB    . ARG A 1 63  ? -8.333  19.923  -42.683 1.00 36.86  ? 63  ARG A CB    1 
ATOM   511  C  CG    . ARG A 1 63  ? -7.624  18.580  -42.720 1.00 38.11  ? 63  ARG A CG    1 
ATOM   512  C  CD    . ARG A 1 63  ? -6.152  18.682  -43.000 1.00 38.35  ? 63  ARG A CD    1 
ATOM   513  N  NE    . ARG A 1 63  ? -5.378  18.910  -41.796 1.00 37.96  ? 63  ARG A NE    1 
ATOM   514  C  CZ    . ARG A 1 63  ? -4.043  18.990  -41.780 1.00 37.25  ? 63  ARG A CZ    1 
ATOM   515  N  NH1   . ARG A 1 63  ? -3.358  18.926  -42.912 1.00 37.72  ? 63  ARG A NH1   1 
ATOM   516  N  NH2   . ARG A 1 63  ? -3.397  19.138  -40.634 1.00 35.96  ? 63  ARG A NH2   1 
ATOM   517  N  N     . GLY A 1 64  ? -10.469 21.067  -40.686 1.00 30.44  ? 64  GLY A N     1 
ATOM   518  C  CA    . GLY A 1 64  ? -11.125 22.102  -39.911 1.00 31.89  ? 64  GLY A CA    1 
ATOM   519  C  C     . GLY A 1 64  ? -12.651 21.991  -39.962 1.00 29.30  ? 64  GLY A C     1 
ATOM   520  O  O     . GLY A 1 64  ? -13.337 22.936  -40.344 1.00 26.82  ? 64  GLY A O     1 
ATOM   521  N  N     . ARG A 1 65  ? -13.164 20.822  -39.568 1.00 28.98  ? 65  ARG A N     1 
ATOM   522  C  CA    . ARG A 1 65  ? -14.607 20.604  -39.485 1.00 27.67  ? 65  ARG A CA    1 
ATOM   523  C  C     . ARG A 1 65  ? -14.968 20.149  -38.077 1.00 24.52  ? 65  ARG A C     1 
ATOM   524  O  O     . ARG A 1 65  ? -15.610 19.134  -37.899 1.00 24.28  ? 65  ARG A O     1 
ATOM   525  C  CB    . ARG A 1 65  ? -15.104 19.620  -40.543 1.00 28.64  ? 65  ARG A CB    1 
ATOM   526  C  CG    . ARG A 1 65  ? -14.959 20.132  -41.979 1.00 35.74  ? 65  ARG A CG    1 
ATOM   527  C  CD    . ARG A 1 65  ? -15.821 21.325  -42.364 1.00 40.75  ? 65  ARG A CD    1 
ATOM   528  N  NE    . ARG A 1 65  ? -17.251 21.167  -42.047 1.00 50.78  ? 65  ARG A NE    1 
ATOM   529  C  CZ    . ARG A 1 65  ? -18.131 20.399  -42.714 1.00 49.63  ? 65  ARG A CZ    1 
ATOM   530  N  NH1   . ARG A 1 65  ? -17.920 20.049  -43.981 1.00 48.59  ? 65  ARG A NH1   1 
ATOM   531  N  NH2   . ARG A 1 65  ? -19.269 20.060  -42.121 1.00 46.54  ? 65  ARG A NH2   1 
ATOM   532  N  N     . PRO A 1 66  ? -14.720 20.977  -37.047 1.00 22.89  ? 66  PRO A N     1 
ATOM   533  C  CA    . PRO A 1 66  ? -15.140 20.622  -35.693 1.00 22.56  ? 66  PRO A CA    1 
ATOM   534  C  C     . PRO A 1 66  ? -16.653 20.723  -35.417 1.00 23.29  ? 66  PRO A C     1 
ATOM   535  O  O     . PRO A 1 66  ? -17.127 20.283  -34.367 1.00 20.82  ? 66  PRO A O     1 
ATOM   536  C  CB    . PRO A 1 66  ? -14.345 21.643  -34.877 1.00 23.00  ? 66  PRO A CB    1 
ATOM   537  C  CG    . PRO A 1 66  ? -14.376 22.889  -35.775 1.00 23.90  ? 66  PRO A CG    1 
ATOM   538  C  CD    . PRO A 1 66  ? -14.176 22.343  -37.168 1.00 23.05  ? 66  PRO A CD    1 
ATOM   539  N  N     . ASP A 1 67  ? -17.404 21.303  -36.370 1.00 24.01  ? 67  ASP A N     1 
ATOM   540  C  CA    . ASP A 1 67  ? -18.859 21.318  -36.340 1.00 26.46  ? 67  ASP A CA    1 
ATOM   541  C  C     . ASP A 1 67  ? -19.388 19.877  -36.390 1.00 25.64  ? 67  ASP A C     1 
ATOM   542  O  O     . ASP A 1 67  ? -20.338 19.516  -35.687 1.00 24.99  ? 67  ASP A O     1 
ATOM   543  C  CB    . ASP A 1 67  ? -19.391 22.218  -37.466 1.00 29.61  ? 67  ASP A CB    1 
ATOM   544  C  CG    . ASP A 1 67  ? -18.937 21.790  -38.857 1.00 32.27  ? 67  ASP A CG    1 
ATOM   545  O  OD1   . ASP A 1 67  ? -17.804 21.443  -39.005 1.00 31.00  ? 67  ASP A OD1   1 
ATOM   546  O  OD2   . ASP A 1 67  ? -19.717 21.844  -39.780 1.00 39.77  ? 67  ASP A OD2   1 
ATOM   547  N  N     . ILE A 1 68  ? -18.731 19.006  -37.165 1.00 25.13  ? 68  ILE A N     1 
ATOM   548  C  CA    . ILE A 1 68  ? -19.209 17.641  -37.272 1.00 22.80  ? 68  ILE A CA    1 
ATOM   549  C  C     . ILE A 1 68  ? -19.185 16.992  -35.894 1.00 22.44  ? 68  ILE A C     1 
ATOM   550  O  O     . ILE A 1 68  ? -20.137 16.335  -35.498 1.00 23.74  ? 68  ILE A O     1 
ATOM   551  C  CB    . ILE A 1 68  ? -18.402 16.864  -38.323 1.00 24.63  ? 68  ILE A CB    1 
ATOM   552  C  CG1   . ILE A 1 68  ? -18.669 17.351  -39.757 1.00 25.38  ? 68  ILE A CG1   1 
ATOM   553  C  CG2   . ILE A 1 68  ? -18.655 15.380  -38.192 1.00 23.57  ? 68  ILE A CG2   1 
ATOM   554  C  CD1   . ILE A 1 68  ? -17.748 16.691  -40.770 1.00 25.71  ? 68  ILE A CD1   1 
ATOM   555  N  N     . VAL A 1 69  ? -18.109 17.210  -35.144 1.00 24.93  ? 69  VAL A N     1 
ATOM   556  C  CA    . VAL A 1 69  ? -17.940 16.673  -33.800 1.00 23.35  ? 69  VAL A CA    1 
ATOM   557  C  C     . VAL A 1 69  ? -18.972 17.286  -32.862 1.00 23.28  ? 69  VAL A C     1 
ATOM   558  O  O     . VAL A 1 69  ? -19.603 16.569  -32.083 1.00 22.46  ? 69  VAL A O     1 
ATOM   559  C  CB    . VAL A 1 69  ? -16.515 16.874  -33.249 1.00 23.48  ? 69  VAL A CB    1 
ATOM   560  C  CG1   . VAL A 1 69  ? -16.398 16.426  -31.801 1.00 25.82  ? 69  VAL A CG1   1 
ATOM   561  C  CG2   . VAL A 1 69  ? -15.476 16.128  -34.057 1.00 24.34  ? 69  VAL A CG2   1 
ATOM   562  N  N     . HIS A 1 70  ? -19.142 18.610  -32.935 1.00 24.10  ? 70  HIS A N     1 
ATOM   563  C  CA    . HIS A 1 70  ? -20.150 19.265  -32.117 1.00 22.84  ? 70  HIS A CA    1 
ATOM   564  C  C     . HIS A 1 70  ? -21.518 18.598  -32.290 1.00 20.72  ? 70  HIS A C     1 
ATOM   565  O  O     . HIS A 1 70  ? -22.123 18.181  -31.309 1.00 19.29  ? 70  HIS A O     1 
ATOM   566  C  CB    . HIS A 1 70  ? -20.188 20.753  -32.421 1.00 22.88  ? 70  HIS A CB    1 
ATOM   567  C  CG    . HIS A 1 70  ? -21.081 21.533  -31.519 1.00 23.76  ? 70  HIS A CG    1 
ATOM   568  N  ND1   . HIS A 1 70  ? -21.981 22.456  -32.009 1.00 23.55  ? 70  HIS A ND1   1 
ATOM   569  C  CD2   . HIS A 1 70  ? -21.195 21.560  -30.188 1.00 24.49  ? 70  HIS A CD2   1 
ATOM   570  C  CE1   . HIS A 1 70  ? -22.605 23.027  -30.991 1.00 24.28  ? 70  HIS A CE1   1 
ATOM   571  N  NE2   . HIS A 1 70  ? -22.158 22.479  -29.869 1.00 25.37  ? 70  HIS A NE2   1 
ATOM   572  N  N     . ILE A 1 71  ? -21.979 18.448  -33.534 1.00 21.21  ? 71  ILE A N     1 
ATOM   573  C  CA    . ILE A 1 71  ? -23.332 17.950  -33.770 1.00 23.80  ? 71  ILE A CA    1 
ATOM   574  C  C     . ILE A 1 71  ? -23.417 16.458  -33.435 1.00 21.69  ? 71  ILE A C     1 
ATOM   575  O  O     . ILE A 1 71  ? -24.389 16.004  -32.841 1.00 20.42  ? 71  ILE A O     1 
ATOM   576  C  CB    . ILE A 1 71  ? -23.796 18.300  -35.195 1.00 25.06  ? 71  ILE A CB    1 
ATOM   577  C  CG1   . ILE A 1 71  ? -23.765 19.830  -35.371 1.00 34.55  ? 71  ILE A CG1   1 
ATOM   578  C  CG2   . ILE A 1 71  ? -25.186 17.739  -35.380 1.00 24.51  ? 71  ILE A CG2   1 
ATOM   579  C  CD1   . ILE A 1 71  ? -23.330 20.408  -36.768 1.00 38.71  ? 71  ILE A CD1   1 
ATOM   580  N  N     . CYS A 1 72  ? -22.351 15.699  -33.695 1.00 19.90  ? 72  CYS A N     1 
ATOM   581  C  CA    . CYS A 1 72  ? -22.364 14.303  -33.282 1.00 21.12  ? 72  CYS A CA    1 
ATOM   582  C  C     . CYS A 1 72  ? -22.454 14.143  -31.762 1.00 19.98  ? 72  CYS A C     1 
ATOM   583  O  O     . CYS A 1 72  ? -23.127 13.221  -31.270 1.00 19.99  ? 72  CYS A O     1 
ATOM   584  C  CB    . CYS A 1 72  ? -21.136 13.562  -33.782 1.00 20.26  ? 72  CYS A CB    1 
ATOM   585  S  SG    . CYS A 1 72  ? -21.237 13.195  -35.540 1.00 22.81  ? 72  CYS A SG    1 
ATOM   586  N  N     . LEU A 1 73  ? -21.737 14.997  -31.031 1.00 19.63  ? 73  LEU A N     1 
ATOM   587  C  CA    . LEU A 1 73  ? -21.699 14.899  -29.582 1.00 21.75  ? 73  LEU A CA    1 
ATOM   588  C  C     . LEU A 1 73  ? -23.014 15.389  -28.974 1.00 25.93  ? 73  LEU A C     1 
ATOM   589  O  O     . LEU A 1 73  ? -23.442 14.867  -27.944 1.00 27.50  ? 73  LEU A O     1 
ATOM   590  C  CB    . LEU A 1 73  ? -20.528 15.704  -29.017 1.00 22.24  ? 73  LEU A CB    1 
ATOM   591  C  CG    . LEU A 1 73  ? -19.121 15.131  -29.218 1.00 23.84  ? 73  LEU A CG    1 
ATOM   592  C  CD1   . LEU A 1 73  ? -18.088 15.964  -28.476 1.00 24.67  ? 73  LEU A CD1   1 
ATOM   593  C  CD2   . LEU A 1 73  ? -19.002 13.677  -28.791 1.00 24.86  ? 73  LEU A CD2   1 
ATOM   594  N  N     . LEU A 1 74  ? -23.635 16.436  -29.540 1.00 25.75  ? 74  LEU A N     1 
ATOM   595  C  CA    . LEU A 1 74  ? -24.918 16.868  -28.994 1.00 26.20  ? 74  LEU A CA    1 
ATOM   596  C  C     . LEU A 1 74  ? -25.925 15.747  -29.183 1.00 24.86  ? 74  LEU A C     1 
ATOM   597  O  O     . LEU A 1 74  ? -26.723 15.464  -28.311 1.00 25.07  ? 74  LEU A O     1 
ATOM   598  C  CB    . LEU A 1 74  ? -25.420 18.155  -29.654 1.00 25.70  ? 74  LEU A CB    1 
ATOM   599  C  CG    . LEU A 1 74  ? -24.628 19.416  -29.310 1.00 26.64  ? 74  LEU A CG    1 
ATOM   600  C  CD1   . LEU A 1 74  ? -25.233 20.634  -29.983 1.00 27.63  ? 74  LEU A CD1   1 
ATOM   601  C  CD2   . LEU A 1 74  ? -24.567 19.640  -27.808 1.00 27.52  ? 74  LEU A CD2   1 
ATOM   602  N  N     . ASN A 1 75  ? -25.905 15.115  -30.344 1.00 24.60  ? 75  ASN A N     1 
ATOM   603  C  CA    . ASN A 1 75  ? -26.841 14.035  -30.583 1.00 24.12  ? 75  ASN A CA    1 
ATOM   604  C  C     . ASN A 1 75  ? -26.588 12.924  -29.582 1.00 24.43  ? 75  ASN A C     1 
ATOM   605  O  O     . ASN A 1 75  ? -27.522 12.457  -28.940 1.00 29.23  ? 75  ASN A O     1 
ATOM   606  C  CB    . ASN A 1 75  ? -26.808 13.589  -32.041 1.00 24.47  ? 75  ASN A CB    1 
ATOM   607  C  CG    . ASN A 1 75  ? -27.531 14.566  -32.938 1.00 25.09  ? 75  ASN A CG    1 
ATOM   608  O  OD1   . ASN A 1 75  ? -28.467 15.229  -32.520 1.00 22.65  ? 75  ASN A OD1   1 
ATOM   609  N  ND2   . ASN A 1 75  ? -27.172 14.578  -34.210 1.00 32.10  ? 75  ASN A ND2   1 
ATOM   610  N  N     . ALA A 1 76  ? -25.325 12.572  -29.350 1.00 23.41  ? 76  ALA A N     1 
ATOM   611  C  CA    . ALA A 1 76  ? -25.051 11.384  -28.554 1.00 22.66  ? 76  ALA A CA    1 
ATOM   612  C  C     . ALA A 1 76  ? -25.293 11.614  -27.056 1.00 22.80  ? 76  ALA A C     1 
ATOM   613  O  O     . ALA A 1 76  ? -25.958 10.801  -26.399 1.00 21.04  ? 76  ALA A O     1 
ATOM   614  C  CB    . ALA A 1 76  ? -23.629 10.946  -28.830 1.00 24.64  ? 76  ALA A CB    1 
ATOM   615  N  N     . LEU A 1 77  ? -24.727 12.709  -26.522 1.00 21.46  ? 77  LEU A N     1 
ATOM   616  C  CA    . LEU A 1 77  ? -24.787 13.020  -25.108 1.00 24.13  ? 77  LEU A CA    1 
ATOM   617  C  C     . LEU A 1 77  ? -26.208 13.369  -24.630 1.00 25.65  ? 77  LEU A C     1 
ATOM   618  O  O     . LEU A 1 77  ? -26.571 13.136  -23.478 1.00 26.10  ? 77  LEU A O     1 
ATOM   619  C  CB    . LEU A 1 77  ? -23.796 14.156  -24.815 1.00 27.58  ? 77  LEU A CB    1 
ATOM   620  C  CG    . LEU A 1 77  ? -22.299 13.825  -24.888 1.00 31.06  ? 77  LEU A CG    1 
ATOM   621  C  CD1   . LEU A 1 77  ? -21.483 15.038  -24.541 1.00 31.51  ? 77  LEU A CD1   1 
ATOM   622  C  CD2   . LEU A 1 77  ? -21.885 12.683  -23.953 1.00 35.23  ? 77  LEU A CD2   1 
ATOM   623  N  N     . ASP A 1 78  ? -27.062 13.881  -25.499 1.00 24.01  ? 78  ASP A N     1 
ATOM   624  C  CA    . ASP A 1 78  ? -28.413 14.180  -25.074 1.00 25.61  ? 78  ASP A CA    1 
ATOM   625  C  C     . ASP A 1 78  ? -29.346 12.984  -25.332 1.00 24.98  ? 78  ASP A C     1 
ATOM   626  O  O     . ASP A 1 78  ? -30.529 13.031  -25.015 1.00 25.27  ? 78  ASP A O     1 
ATOM   627  C  CB    . ASP A 1 78  ? -28.836 15.513  -25.692 1.00 28.46  ? 78  ASP A CB    1 
ATOM   628  C  CG    . ASP A 1 78  ? -27.848 16.659  -25.415 1.00 38.37  ? 78  ASP A CG    1 
ATOM   629  O  OD1   . ASP A 1 78  ? -27.308 16.780  -24.294 1.00 46.68  ? 78  ASP A OD1   1 
ATOM   630  O  OD2   . ASP A 1 78  ? -27.632 17.464  -26.309 1.00 53.26  ? 78  ASP A OD2   1 
ATOM   631  N  N     . SER A 1 79  ? -28.839 11.878  -25.881 1.00 23.33  ? 79  SER A N     1 
ATOM   632  C  CA    . SER A 1 79  ? -29.682 10.740  -26.209 1.00 21.42  ? 79  SER A CA    1 
ATOM   633  C  C     . SER A 1 79  ? -30.341 10.199  -24.943 1.00 24.07  ? 79  SER A C     1 
ATOM   634  O  O     . SER A 1 79  ? -29.781 10.290  -23.841 1.00 23.82  ? 79  SER A O     1 
ATOM   635  C  CB    . SER A 1 79  ? -28.904 9.640   -26.914 1.00 19.84  ? 79  SER A CB    1 
ATOM   636  O  OG    . SER A 1 79  ? -27.835 9.149   -26.085 1.00 19.52  ? 79  SER A OG    1 
ATOM   637  N  N     . ILE A 1 80  ? -31.528 9.609   -25.140 1.00 24.24  ? 80  ILE A N     1 
ATOM   638  C  CA    . ILE A 1 80  ? -32.122 8.741   -24.152 1.00 26.09  ? 80  ILE A CA    1 
ATOM   639  C  C     . ILE A 1 80  ? -31.128 7.636   -23.803 1.00 26.74  ? 80  ILE A C     1 
ATOM   640  O  O     . ILE A 1 80  ? -30.965 7.316   -22.640 1.00 27.71  ? 80  ILE A O     1 
ATOM   641  C  CB    . ILE A 1 80  ? -33.451 8.171   -24.677 1.00 28.49  ? 80  ILE A CB    1 
ATOM   642  C  CG1   . ILE A 1 80  ? -34.458 9.291   -24.954 1.00 28.73  ? 80  ILE A CG1   1 
ATOM   643  C  CG2   . ILE A 1 80  ? -33.983 7.121   -23.710 1.00 30.82  ? 80  ILE A CG2   1 
ATOM   644  C  CD1   . ILE A 1 80  ? -35.881 8.862   -25.194 1.00 30.29  ? 80  ILE A CD1   1 
ATOM   645  N  N     . LEU A 1 81  ? -30.453 7.051   -24.803 1.00 27.16  ? 81  LEU A N     1 
ATOM   646  C  CA    . LEU A 1 81  ? -29.477 5.995   -24.542 1.00 26.50  ? 81  LEU A CA    1 
ATOM   647  C  C     . LEU A 1 81  ? -28.448 6.496   -23.528 1.00 27.20  ? 81  LEU A C     1 
ATOM   648  O  O     . LEU A 1 81  ? -28.144 5.789   -22.552 1.00 27.34  ? 81  LEU A O     1 
ATOM   649  C  CB    . LEU A 1 81  ? -28.792 5.588   -25.842 1.00 25.25  ? 81  LEU A CB    1 
ATOM   650  C  CG    . LEU A 1 81  ? -27.935 4.307   -25.817 1.00 25.37  ? 81  LEU A CG    1 
ATOM   651  C  CD1   . LEU A 1 81  ? -28.787 3.056   -25.690 1.00 25.63  ? 81  LEU A CD1   1 
ATOM   652  C  CD2   . LEU A 1 81  ? -27.092 4.225   -27.085 1.00 24.02  ? 81  LEU A CD2   1 
ATOM   653  N  N     . ASN A 1 82  ? -27.981 7.747   -23.723 1.00 25.48  ? 82  ASN A N     1 
ATOM   654  C  CA    . ASN A 1 82  ? -27.018 8.315   -22.794 1.00 25.66  ? 82  ASN A CA    1 
ATOM   655  C  C     . ASN A 1 82  ? -27.552 8.472   -21.378 1.00 26.28  ? 82  ASN A C     1 
ATOM   656  O  O     . ASN A 1 82  ? -26.881 8.040   -20.457 1.00 26.24  ? 82  ASN A O     1 
ATOM   657  C  CB    . ASN A 1 82  ? -26.418 9.630   -23.235 1.00 25.25  ? 82  ASN A CB    1 
ATOM   658  C  CG    . ASN A 1 82  ? -25.185 9.944   -22.419 1.00 26.52  ? 82  ASN A CG    1 
ATOM   659  O  OD1   . ASN A 1 82  ? -24.350 9.065   -22.152 1.00 27.14  ? 82  ASN A OD1   1 
ATOM   660  N  ND2   . ASN A 1 82  ? -25.061 11.203  -22.036 1.00 25.66  ? 82  ASN A ND2   1 
ATOM   661  N  N     . LYS A 1 83  ? -28.780 8.962   -21.227 1.00 27.46  ? 83  LYS A N     1 
ATOM   662  C  CA    . LYS A 1 83  ? -29.384 9.169   -19.924 1.00 31.33  ? 83  LYS A CA    1 
ATOM   663  C  C     . LYS A 1 83  ? -29.644 7.857   -19.169 1.00 34.51  ? 83  LYS A C     1 
ATOM   664  O  O     . LYS A 1 83  ? -29.828 7.878   -17.948 1.00 33.40  ? 83  LYS A O     1 
ATOM   665  C  CB    . LYS A 1 83  ? -30.669 9.984   -20.114 1.00 33.10  ? 83  LYS A CB    1 
ATOM   666  C  CG    . LYS A 1 83  ? -30.424 11.371  -20.708 1.00 35.89  ? 83  LYS A CG    1 
ATOM   667  C  CD    . LYS A 1 83  ? -31.651 12.255  -20.759 1.00 41.06  ? 83  LYS A CD    1 
ATOM   668  C  CE    . LYS A 1 83  ? -31.403 13.645  -21.314 1.00 42.75  ? 83  LYS A CE    1 
ATOM   669  N  NZ    . LYS A 1 83  ? -30.292 14.316  -20.617 1.00 43.89  ? 83  LYS A NZ    1 
ATOM   670  N  N     . GLU A 1 84  ? -29.745 6.736   -19.902 1.00 36.02  ? 84  GLU A N     1 
ATOM   671  C  CA    . GLU A 1 84  ? -30.012 5.419   -19.342 1.00 38.07  ? 84  GLU A CA    1 
ATOM   672  C  C     . GLU A 1 84  ? -28.708 4.683   -19.027 1.00 36.89  ? 84  GLU A C     1 
ATOM   673  O  O     . GLU A 1 84  ? -28.728 3.484   -18.769 1.00 39.85  ? 84  GLU A O     1 
ATOM   674  C  CB    . GLU A 1 84  ? -30.784 4.563   -20.352 1.00 40.15  ? 84  GLU A CB    1 
ATOM   675  C  CG    . GLU A 1 84  ? -32.177 5.049   -20.617 1.00 42.42  ? 84  GLU A CG    1 
ATOM   676  C  CD    . GLU A 1 84  ? -33.156 4.717   -19.507 1.00 49.85  ? 84  GLU A CD    1 
ATOM   677  O  OE1   . GLU A 1 84  ? -33.951 5.609   -19.151 1.00 47.55  ? 84  GLU A OE1   1 
ATOM   678  O  OE2   . GLU A 1 84  ? -33.104 3.565   -18.974 1.00 58.98  ? 84  GLU A OE2   1 
ATOM   679  N  N     . ASP A 1 85  ? -27.572 5.374   -19.132 1.00 33.93  ? 85  ASP A N     1 
ATOM   680  C  CA    . ASP A 1 85  ? -26.272 4.832   -18.772 1.00 31.96  ? 85  ASP A CA    1 
ATOM   681  C  C     . ASP A 1 85  ? -25.867 3.701   -19.705 1.00 31.27  ? 85  ASP A C     1 
ATOM   682  O  O     . ASP A 1 85  ? -25.144 2.798   -19.308 1.00 30.80  ? 85  ASP A O     1 
ATOM   683  C  CB    . ASP A 1 85  ? -26.205 4.380   -17.313 1.00 33.91  ? 85  ASP A CB    1 
ATOM   684  C  CG    . ASP A 1 85  ? -24.771 4.040   -16.923 1.00 36.01  ? 85  ASP A CG    1 
ATOM   685  O  OD1   . ASP A 1 85  ? -23.870 4.676   -17.491 1.00 33.29  ? 85  ASP A OD1   1 
ATOM   686  O  OD2   . ASP A 1 85  ? -24.553 3.145   -16.044 1.00 38.83  ? 85  ASP A OD2   1 
ATOM   687  N  N     . ARG A 1 86  ? -26.271 3.783   -20.974 1.00 31.46  ? 86  ARG A N     1 
ATOM   688  C  CA    . ARG A 1 86  ? -25.963 2.740   -21.935 1.00 30.27  ? 86  ARG A CA    1 
ATOM   689  C  C     . ARG A 1 86  ? -25.086 3.265   -23.063 1.00 28.67  ? 86  ARG A C     1 
ATOM   690  O  O     . ARG A 1 86  ? -25.042 2.650   -24.137 1.00 26.79  ? 86  ARG A O     1 
ATOM   691  C  CB    . ARG A 1 86  ? -27.222 2.240   -22.633 1.00 32.72  ? 86  ARG A CB    1 
ATOM   692  C  CG    . ARG A 1 86  ? -28.326 1.784   -21.698 1.00 35.47  ? 86  ARG A CG    1 
ATOM   693  C  CD    . ARG A 1 86  ? -28.098 0.359   -21.406 1.00 38.70  ? 86  ARG A CD    1 
ATOM   694  N  NE    . ARG A 1 86  ? -29.207 -0.212  -20.680 1.00 44.57  ? 86  ARG A NE    1 
ATOM   695  C  CZ    . ARG A 1 86  ? -29.223 -1.486  -20.304 1.00 47.11  ? 86  ARG A CZ    1 
ATOM   696  N  NH1   . ARG A 1 86  ? -28.222 -2.281  -20.675 1.00 44.54  ? 86  ARG A NH1   1 
ATOM   697  N  NH2   . ARG A 1 86  ? -30.233 -1.949  -19.577 1.00 47.15  ? 86  ARG A NH2   1 
ATOM   698  N  N     . LEU A 1 87  ? -24.374 4.377   -22.830 1.00 27.67  ? 87  LEU A N     1 
ATOM   699  C  CA    . LEU A 1 87  ? -23.476 4.879   -23.860 1.00 26.47  ? 87  LEU A CA    1 
ATOM   700  C  C     . LEU A 1 87  ? -22.188 5.437   -23.249 1.00 27.17  ? 87  LEU A C     1 
ATOM   701  O  O     . LEU A 1 87  ? -22.204 6.041   -22.167 1.00 26.55  ? 87  LEU A O     1 
ATOM   702  C  CB    . LEU A 1 87  ? -24.243 5.930   -24.652 1.00 25.65  ? 87  LEU A CB    1 
ATOM   703  C  CG    . LEU A 1 87  ? -23.432 6.730   -25.654 1.00 25.15  ? 87  LEU A CG    1 
ATOM   704  C  CD1   . LEU A 1 87  ? -23.137 5.927   -26.910 1.00 24.80  ? 87  LEU A CD1   1 
ATOM   705  C  CD2   . LEU A 1 87  ? -24.214 7.983   -26.006 1.00 26.63  ? 87  LEU A CD2   1 
ATOM   706  N  N     . ARG A 1 88  ? -21.082 5.179   -23.964 1.00 25.68  ? 88  ARG A N     1 
ATOM   707  C  CA    . ARG A 1 88  ? -19.781 5.786   -23.721 1.00 25.16  ? 88  ARG A CA    1 
ATOM   708  C  C     . ARG A 1 88  ? -19.284 6.315   -25.059 1.00 24.29  ? 88  ARG A C     1 
ATOM   709  O  O     . ARG A 1 88  ? -19.349 5.625   -26.080 1.00 25.92  ? 88  ARG A O     1 
ATOM   710  C  CB    . ARG A 1 88  ? -18.815 4.741   -23.146 1.00 26.92  ? 88  ARG A CB    1 
ATOM   711  C  CG    . ARG A 1 88  ? -19.186 4.216   -21.768 1.00 27.75  ? 88  ARG A CG    1 
ATOM   712  C  CD    . ARG A 1 88  ? -19.234 5.313   -20.719 1.00 29.44  ? 88  ARG A CD    1 
ATOM   713  N  NE    . ARG A 1 88  ? -19.646 4.869   -19.392 1.00 30.47  ? 88  ARG A NE    1 
ATOM   714  C  CZ    . ARG A 1 88  ? -20.894 4.908   -18.917 1.00 29.71  ? 88  ARG A CZ    1 
ATOM   715  N  NH1   . ARG A 1 88  ? -21.925 5.174   -19.685 1.00 28.62  ? 88  ARG A NH1   1 
ATOM   716  N  NH2   . ARG A 1 88  ? -21.125 4.616   -17.661 1.00 31.83  ? 88  ARG A NH2   1 
ATOM   717  N  N     . VAL A 1 89  ? -18.859 7.568   -25.109 1.00 24.30  ? 89  VAL A N     1 
ATOM   718  C  CA    . VAL A 1 89  ? -18.517 8.115   -26.415 1.00 25.71  ? 89  VAL A CA    1 
ATOM   719  C  C     . VAL A 1 89  ? -17.092 8.657   -26.364 1.00 23.94  ? 89  VAL A C     1 
ATOM   720  O  O     . VAL A 1 89  ? -16.649 9.143   -25.332 1.00 27.27  ? 89  VAL A O     1 
ATOM   721  C  CB    . VAL A 1 89  ? -19.563 9.157   -26.900 1.00 26.29  ? 89  VAL A CB    1 
ATOM   722  C  CG1   . VAL A 1 89  ? -19.744 10.261  -25.926 1.00 28.06  ? 89  VAL A CG1   1 
ATOM   723  C  CG2   . VAL A 1 89  ? -19.187 9.773   -28.231 1.00 27.29  ? 89  VAL A CG2   1 
ATOM   724  N  N     . TYR A 1 90  ? -16.385 8.573   -27.491 1.00 24.09  ? 90  TYR A N     1 
ATOM   725  C  CA    . TYR A 1 90  ? -14.999 8.999   -27.580 1.00 24.21  ? 90  TYR A CA    1 
ATOM   726  C  C     . TYR A 1 90  ? -14.792 9.758   -28.891 1.00 23.59  ? 90  TYR A C     1 
ATOM   727  O  O     . TYR A 1 90  ? -15.438 9.429   -29.882 1.00 23.77  ? 90  TYR A O     1 
ATOM   728  C  CB    . TYR A 1 90  ? -14.015 7.817   -27.573 1.00 23.26  ? 90  TYR A CB    1 
ATOM   729  C  CG    . TYR A 1 90  ? -14.301 6.751   -26.524 1.00 25.29  ? 90  TYR A CG    1 
ATOM   730  C  CD1   . TYR A 1 90  ? -15.378 5.893   -26.682 1.00 25.69  ? 90  TYR A CD1   1 
ATOM   731  C  CD2   . TYR A 1 90  ? -13.501 6.589   -25.387 1.00 26.26  ? 90  TYR A CD2   1 
ATOM   732  C  CE1   . TYR A 1 90  ? -15.671 4.931   -25.740 1.00 26.78  ? 90  TYR A CE1   1 
ATOM   733  C  CE2   . TYR A 1 90  ? -13.768 5.608   -24.445 1.00 26.67  ? 90  TYR A CE2   1 
ATOM   734  C  CZ    . TYR A 1 90  ? -14.878 4.797   -24.617 1.00 27.32  ? 90  TYR A CZ    1 
ATOM   735  O  OH    . TYR A 1 90  ? -15.217 3.772   -23.786 1.00 27.66  ? 90  TYR A OH    1 
ATOM   736  N  N     . VAL A 1 91  ? -13.833 10.708  -28.904 1.00 23.13  ? 91  VAL A N     1 
ATOM   737  C  CA    . VAL A 1 91  ? -13.379 11.312  -30.145 1.00 22.89  ? 91  VAL A CA    1 
ATOM   738  C  C     . VAL A 1 91  ? -11.938 10.900  -30.400 1.00 24.96  ? 91  VAL A C     1 
ATOM   739  O  O     . VAL A 1 91  ? -11.085 11.004  -29.527 1.00 29.69  ? 91  VAL A O     1 
ATOM   740  C  CB    . VAL A 1 91  ? -13.518 12.846  -30.145 1.00 24.42  ? 91  VAL A CB    1 
ATOM   741  C  CG1   . VAL A 1 91  ? -13.012 13.459  -31.455 1.00 23.27  ? 91  VAL A CG1   1 
ATOM   742  C  CG2   . VAL A 1 91  ? -14.973 13.254  -29.882 1.00 24.14  ? 91  VAL A CG2   1 
ATOM   743  N  N     . HIS A 1 92  ? -11.688 10.404  -31.610 1.00 23.42  ? 92  HIS A N     1 
ATOM   744  C  CA    . HIS A 1 92  ? -10.341 10.213  -32.104 1.00 23.75  ? 92  HIS A CA    1 
ATOM   745  C  C     . HIS A 1 92  ? -10.117 11.193  -33.256 1.00 22.26  ? 92  HIS A C     1 
ATOM   746  O  O     . HIS A 1 92  ? -10.906 11.247  -34.205 1.00 21.54  ? 92  HIS A O     1 
ATOM   747  C  CB    . HIS A 1 92  ? -10.100 8.738   -32.465 1.00 21.81  ? 92  HIS A CB    1 
ATOM   748  C  CG    . HIS A 1 92  ? -8.878  8.535   -33.281 1.00 21.07  ? 92  HIS A CG    1 
ATOM   749  N  ND1   . HIS A 1 92  ? -8.938  8.496   -34.656 1.00 19.40  ? 92  HIS A ND1   1 
ATOM   750  C  CD2   . HIS A 1 92  ? -7.587  8.388   -32.954 1.00 21.63  ? 92  HIS A CD2   1 
ATOM   751  C  CE1   . HIS A 1 92  ? -7.736  8.297   -35.155 1.00 19.33  ? 92  HIS A CE1   1 
ATOM   752  N  NE2   . HIS A 1 92  ? -6.888  8.267   -34.139 1.00 20.76  ? 92  HIS A NE2   1 
ATOM   753  N  N     . THR A 1 93  ? -9.019  11.931  -33.162 1.00 21.06  ? 93  THR A N     1 
ATOM   754  C  CA    . THR A 1 93  ? -8.751  12.974  -34.127 1.00 22.66  ? 93  THR A CA    1 
ATOM   755  C  C     . THR A 1 93  ? -7.777  12.449  -35.166 1.00 23.47  ? 93  THR A C     1 
ATOM   756  O  O     . THR A 1 93  ? -7.122  11.444  -34.923 1.00 24.44  ? 93  THR A O     1 
ATOM   757  C  CB    . THR A 1 93  ? -8.135  14.231  -33.491 1.00 22.47  ? 93  THR A CB    1 
ATOM   758  O  OG1   . THR A 1 93  ? -6.756  13.961  -33.234 1.00 22.29  ? 93  THR A OG1   1 
ATOM   759  C  CG2   . THR A 1 93  ? -8.849  14.667  -32.233 1.00 22.16  ? 93  THR A CG2   1 
ATOM   760  N  N     . ARG A 1 94  ? -7.679  13.199  -36.272 1.00 24.70  ? 94  ARG A N     1 
ATOM   761  C  CA    . ARG A 1 94  ? -6.869  12.881  -37.435 1.00 25.27  ? 94  ARG A CA    1 
ATOM   762  C  C     . ARG A 1 94  ? -5.384  12.964  -37.091 1.00 25.51  ? 94  ARG A C     1 
ATOM   763  O  O     . ARG A 1 94  ? -4.576  12.623  -37.935 1.00 27.99  ? 94  ARG A O     1 
ATOM   764  C  CB    . ARG A 1 94  ? -7.158  13.861  -38.582 1.00 27.15  ? 94  ARG A CB    1 
ATOM   765  C  CG    . ARG A 1 94  ? -6.832  15.318  -38.264 1.00 30.28  ? 94  ARG A CG    1 
ATOM   766  C  CD    . ARG A 1 94  ? -5.833  15.964  -39.209 1.00 34.90  ? 94  ARG A CD    1 
ATOM   767  N  NE    . ARG A 1 94  ? -6.431  15.960  -40.535 1.00 44.00  ? 94  ARG A NE    1 
ATOM   768  C  CZ    . ARG A 1 94  ? -5.881  15.486  -41.657 1.00 47.04  ? 94  ARG A CZ    1 
ATOM   769  N  NH1   . ARG A 1 94  ? -6.674  15.065  -42.641 1.00 50.18  ? 94  ARG A NH1   1 
ATOM   770  N  NH2   . ARG A 1 94  ? -4.569  15.339  -41.743 1.00 41.84  ? 94  ARG A NH2   1 
ATOM   771  N  N     . ASN A 1 95  ? -5.025  13.459  -35.895 1.00 27.13  ? 95  ASN A N     1 
ATOM   772  C  CA    . ASN A 1 95  ? -3.629  13.586  -35.476 1.00 27.07  ? 95  ASN A CA    1 
ATOM   773  C  C     . ASN A 1 95  ? -3.292  12.539  -34.412 1.00 26.13  ? 95  ASN A C     1 
ATOM   774  O  O     . ASN A 1 95  ? -2.238  12.621  -33.770 1.00 27.83  ? 95  ASN A O     1 
ATOM   775  C  CB    . ASN A 1 95  ? -3.326  14.997  -34.965 1.00 29.47  ? 95  ASN A CB    1 
ATOM   776  C  CG    . ASN A 1 95  ? -3.497  16.054  -36.039 1.00 33.65  ? 95  ASN A CG    1 
ATOM   777  O  OD1   . ASN A 1 95  ? -2.945  15.935  -37.123 1.00 33.26  ? 95  ASN A OD1   1 
ATOM   778  N  ND2   . ASN A 1 95  ? -4.299  17.075  -35.779 1.00 36.52  ? 95  ASN A ND2   1 
ATOM   779  N  N     . ASP A 1 96  ? -4.196  11.576  -34.194 1.00 23.08  ? 96  ASP A N     1 
ATOM   780  C  CA    . ASP A 1 96  ? -3.971  10.513  -33.236 1.00 22.90  ? 96  ASP A CA    1 
ATOM   781  C  C     . ASP A 1 96  ? -3.905  11.060  -31.805 1.00 23.65  ? 96  ASP A C     1 
ATOM   782  O  O     . ASP A 1 96  ? -3.013  10.733  -31.029 1.00 23.55  ? 96  ASP A O     1 
ATOM   783  C  CB    . ASP A 1 96  ? -2.742  9.715   -33.631 1.00 25.04  ? 96  ASP A CB    1 
ATOM   784  C  CG    . ASP A 1 96  ? -2.970  8.575   -34.614 1.00 28.68  ? 96  ASP A CG    1 
ATOM   785  O  OD1   . ASP A 1 96  ? -4.174  8.157   -34.886 1.00 28.95  ? 96  ASP A OD1   1 
ATOM   786  O  OD2   . ASP A 1 96  ? -1.935  8.049   -35.057 1.00 30.45  ? 96  ASP A OD2   1 
ATOM   787  N  N     . TYR A 1 97  ? -4.913  11.855  -31.452 1.00 22.58  ? 97  TYR A N     1 
ATOM   788  C  CA    . TYR A 1 97  ? -5.268  12.156  -30.085 1.00 23.16  ? 97  TYR A CA    1 
ATOM   789  C  C     . TYR A 1 97  ? -6.662  11.611  -29.815 1.00 23.91  ? 97  TYR A C     1 
ATOM   790  O  O     . TYR A 1 97  ? -7.502  11.493  -30.708 1.00 25.82  ? 97  TYR A O     1 
ATOM   791  C  CB    . TYR A 1 97  ? -5.282  13.655  -29.775 1.00 23.59  ? 97  TYR A CB    1 
ATOM   792  C  CG    . TYR A 1 97  ? -3.906  14.267  -29.919 1.00 24.00  ? 97  TYR A CG    1 
ATOM   793  C  CD1   . TYR A 1 97  ? -3.387  14.522  -31.181 1.00 24.71  ? 97  TYR A CD1   1 
ATOM   794  C  CD2   . TYR A 1 97  ? -3.070  14.458  -28.811 1.00 24.21  ? 97  TYR A CD2   1 
ATOM   795  C  CE1   . TYR A 1 97  ? -2.097  15.011  -31.339 1.00 25.15  ? 97  TYR A CE1   1 
ATOM   796  C  CE2   . TYR A 1 97  ? -1.790  14.982  -28.968 1.00 24.74  ? 97  TYR A CE2   1 
ATOM   797  C  CZ    . TYR A 1 97  ? -1.305  15.262  -30.234 1.00 25.47  ? 97  TYR A CZ    1 
ATOM   798  O  OH    . TYR A 1 97  ? -0.042  15.733  -30.491 1.00 29.75  ? 97  TYR A OH    1 
ATOM   799  N  N     . VAL A 1 98  ? -6.918  11.330  -28.548 1.00 23.32  ? 98  VAL A N     1 
ATOM   800  C  CA    . VAL A 1 98  ? -8.221  10.851  -28.169 1.00 22.96  ? 98  VAL A CA    1 
ATOM   801  C  C     . VAL A 1 98  ? -8.759  11.762  -27.074 1.00 23.48  ? 98  VAL A C     1 
ATOM   802  O  O     . VAL A 1 98  ? -8.035  12.192  -26.186 1.00 24.56  ? 98  VAL A O     1 
ATOM   803  C  CB    . VAL A 1 98  ? -8.138  9.376   -27.755 1.00 24.23  ? 98  VAL A CB    1 
ATOM   804  C  CG1   . VAL A 1 98  ? -9.367  8.907   -27.010 1.00 24.52  ? 98  VAL A CG1   1 
ATOM   805  C  CG2   . VAL A 1 98  ? -7.906  8.501   -28.972 1.00 24.62  ? 98  VAL A CG2   1 
ATOM   806  N  N     . ILE A 1 99  ? -10.050 12.053  -27.171 1.00 23.65  ? 99  ILE A N     1 
ATOM   807  C  CA    . ILE A 1 99  ? -10.782 12.725  -26.123 1.00 24.78  ? 99  ILE A CA    1 
ATOM   808  C  C     . ILE A 1 99  ? -11.799 11.756  -25.541 1.00 26.96  ? 99  ILE A C     1 
ATOM   809  O  O     . ILE A 1 99  ? -12.648 11.228  -26.262 1.00 27.01  ? 99  ILE A O     1 
ATOM   810  C  CB    . ILE A 1 99  ? -11.485 13.974  -26.663 1.00 24.30  ? 99  ILE A CB    1 
ATOM   811  C  CG1   . ILE A 1 99  ? -10.482 14.889  -27.364 1.00 24.29  ? 99  ILE A CG1   1 
ATOM   812  C  CG2   . ILE A 1 99  ? -12.232 14.651  -25.528 1.00 25.43  ? 99  ILE A CG2   1 
ATOM   813  C  CD1   . ILE A 1 99  ? -11.104 15.960  -28.209 1.00 25.25  ? 99  ILE A CD1   1 
ATOM   814  N  N     . TYR A 1 100 ? -11.632 11.554  -24.233 1.00 28.87  ? 100 TYR A N     1 
ATOM   815  C  CA    . TYR A 1 100 ? -12.498 10.802  -23.359 1.00 28.15  ? 100 TYR A CA    1 
ATOM   816  C  C     . TYR A 1 100 ? -13.520 11.754  -22.773 1.00 28.10  ? 100 TYR A C     1 
ATOM   817  O  O     . TYR A 1 100 ? -13.164 12.866  -22.422 1.00 28.94  ? 100 TYR A O     1 
ATOM   818  C  CB    . TYR A 1 100 ? -11.618 10.197  -22.261 1.00 27.81  ? 100 TYR A CB    1 
ATOM   819  C  CG    . TYR A 1 100 ? -10.544 9.233   -22.757 1.00 27.72  ? 100 TYR A CG    1 
ATOM   820  C  CD1   . TYR A 1 100 ? -10.825 7.883   -22.947 1.00 27.68  ? 100 TYR A CD1   1 
ATOM   821  C  CD2   . TYR A 1 100 ? -9.243  9.669   -23.048 1.00 27.02  ? 100 TYR A CD2   1 
ATOM   822  C  CE1   . TYR A 1 100 ? -9.838  6.988   -23.347 1.00 27.92  ? 100 TYR A CE1   1 
ATOM   823  C  CE2   . TYR A 1 100 ? -8.254  8.786   -23.459 1.00 26.27  ? 100 TYR A CE2   1 
ATOM   824  C  CZ    . TYR A 1 100 ? -8.553  7.442   -23.586 1.00 27.97  ? 100 TYR A CZ    1 
ATOM   825  O  OH    . TYR A 1 100 ? -7.636  6.536   -24.017 1.00 30.83  ? 100 TYR A OH    1 
ATOM   826  N  N     . ILE A 1 101 ? -14.759 11.278  -22.636 1.00 27.94  ? 101 ILE A N     1 
ATOM   827  C  CA    . ILE A 1 101 ? -15.897 12.119  -22.297 1.00 28.35  ? 101 ILE A CA    1 
ATOM   828  C  C     . ILE A 1 101 ? -16.683 11.425  -21.191 1.00 28.00  ? 101 ILE A C     1 
ATOM   829  O  O     . ILE A 1 101 ? -17.182 10.315  -21.381 1.00 28.56  ? 101 ILE A O     1 
ATOM   830  C  CB    . ILE A 1 101 ? -16.778 12.384  -23.542 1.00 28.76  ? 101 ILE A CB    1 
ATOM   831  C  CG1   . ILE A 1 101 ? -16.001 13.009  -24.700 1.00 28.75  ? 101 ILE A CG1   1 
ATOM   832  C  CG2   . ILE A 1 101 ? -18.013 13.226  -23.217 1.00 28.86  ? 101 ILE A CG2   1 
ATOM   833  C  CD1   . ILE A 1 101 ? -16.742 12.860  -26.024 1.00 29.21  ? 101 ILE A CD1   1 
ATOM   834  N  N     . LYS A 1 102 ? -16.796 12.061  -20.029 1.00 28.93  ? 102 LYS A N     1 
ATOM   835  C  CA    . LYS A 1 102 ? -17.587 11.452  -18.972 1.00 32.46  ? 102 LYS A CA    1 
ATOM   836  C  C     . LYS A 1 102 ? -19.056 11.528  -19.361 1.00 31.60  ? 102 LYS A C     1 
ATOM   837  O  O     . LYS A 1 102 ? -19.492 12.498  -19.957 1.00 34.62  ? 102 LYS A O     1 
ATOM   838  C  CB    . LYS A 1 102 ? -17.212 12.032  -17.604 1.00 38.84  ? 102 LYS A CB    1 
ATOM   839  C  CG    . LYS A 1 102 ? -15.886 11.473  -17.110 1.00 44.60  ? 102 LYS A CG    1 
ATOM   840  C  CD    . LYS A 1 102 ? -15.778 11.209  -15.634 1.00 56.50  ? 102 LYS A CD    1 
ATOM   841  C  CE    . LYS A 1 102 ? -14.552 10.390  -15.274 1.00 62.46  ? 102 LYS A CE    1 
ATOM   842  N  NZ    . LYS A 1 102 ? -14.139 10.650  -13.871 1.00 72.85  ? 102 LYS A NZ    1 
ATOM   843  N  N     . PRO A 1 103 ? -19.865 10.479  -19.130 1.00 32.30  ? 103 PRO A N     1 
ATOM   844  C  CA    . PRO A 1 103 ? -21.251 10.473  -19.597 1.00 34.52  ? 103 PRO A CA    1 
ATOM   845  C  C     . PRO A 1 103 ? -22.065 11.724  -19.254 1.00 35.69  ? 103 PRO A C     1 
ATOM   846  O  O     . PRO A 1 103 ? -22.909 12.146  -20.049 1.00 31.27  ? 103 PRO A O     1 
ATOM   847  C  CB    . PRO A 1 103 ? -21.848 9.272   -18.850 1.00 36.40  ? 103 PRO A CB    1 
ATOM   848  C  CG    . PRO A 1 103 ? -20.684 8.333   -18.700 1.00 38.42  ? 103 PRO A CG    1 
ATOM   849  C  CD    . PRO A 1 103 ? -19.485 9.229   -18.467 1.00 35.98  ? 103 PRO A CD    1 
ATOM   850  N  N     . GLU A 1 104 ? -21.798 12.292  -18.068 1.00 35.66  ? 104 GLU A N     1 
ATOM   851  C  CA    . GLU A 1 104 ? -22.625 13.346  -17.507 1.00 39.77  ? 104 GLU A CA    1 
ATOM   852  C  C     . GLU A 1 104 ? -22.255 14.696  -18.121 1.00 36.66  ? 104 GLU A C     1 
ATOM   853  O  O     . GLU A 1 104 ? -22.840 15.701  -17.747 1.00 42.26  ? 104 GLU A O     1 
ATOM   854  C  CB    . GLU A 1 104 ? -22.551 13.365  -15.962 1.00 42.68  ? 104 GLU A CB    1 
ATOM   855  C  CG    . GLU A 1 104 ? -21.150 13.494  -15.383 1.00 48.67  ? 104 GLU A CG    1 
ATOM   856  C  CD    . GLU A 1 104 ? -20.362 12.188  -15.251 1.00 56.15  ? 104 GLU A CD    1 
ATOM   857  O  OE1   . GLU A 1 104 ? -19.697 12.015  -14.219 1.00 67.49  ? 104 GLU A OE1   1 
ATOM   858  O  OE2   . GLU A 1 104 ? -20.418 11.328  -16.156 1.00 53.34  ? 104 GLU A OE2   1 
ATOM   859  N  N     . THR A 1 105 ? -21.285 14.728  -19.030 1.00 33.34  ? 105 THR A N     1 
ATOM   860  C  CA    . THR A 1 105 ? -20.812 15.975  -19.625 1.00 34.58  ? 105 THR A CA    1 
ATOM   861  C  C     . THR A 1 105 ? -21.939 16.757  -20.334 1.00 36.49  ? 105 THR A C     1 
ATOM   862  O  O     . THR A 1 105 ? -22.647 16.235  -21.187 1.00 32.59  ? 105 THR A O     1 
ATOM   863  C  CB    . THR A 1 105 ? -19.681 15.695  -20.631 1.00 31.19  ? 105 THR A CB    1 
ATOM   864  O  OG1   . THR A 1 105 ? -18.651 14.904  -20.034 1.00 32.46  ? 105 THR A OG1   1 
ATOM   865  C  CG2   . THR A 1 105 ? -19.065 16.962  -21.183 1.00 32.12  ? 105 THR A CG2   1 
ATOM   866  N  N     . ARG A 1 106 ? -22.052 18.059  -20.066 1.00 39.84  ? 106 ARG A N     1 
ATOM   867  C  CA    . ARG A 1 106 ? -23.011 18.875  -20.797 1.00 43.35  ? 106 ARG A CA    1 
ATOM   868  C  C     . ARG A 1 106 ? -22.252 19.788  -21.746 1.00 37.21  ? 106 ARG A C     1 
ATOM   869  O  O     . ARG A 1 106 ? -21.848 20.867  -21.347 1.00 36.36  ? 106 ARG A O     1 
ATOM   870  C  CB    . ARG A 1 106 ? -23.898 19.707  -19.850 1.00 51.87  ? 106 ARG A CB    1 
ATOM   871  C  CG    . ARG A 1 106 ? -25.065 20.426  -20.525 1.00 59.26  ? 106 ARG A CG    1 
ATOM   872  C  CD    . ARG A 1 106 ? -25.902 21.237  -19.535 1.00 71.85  ? 106 ARG A CD    1 
ATOM   873  N  NE    . ARG A 1 106 ? -26.952 22.068  -20.133 1.00 81.82  ? 106 ARG A NE    1 
ATOM   874  C  CZ    . ARG A 1 106 ? -26.745 23.185  -20.841 1.00 90.49  ? 106 ARG A CZ    1 
ATOM   875  N  NH1   . ARG A 1 106 ? -25.516 23.578  -21.134 1.00 96.86  ? 106 ARG A NH1   1 
ATOM   876  N  NH2   . ARG A 1 106 ? -27.772 23.907  -21.266 1.00 87.70  ? 106 ARG A NH2   1 
ATOM   877  N  N     . LEU A 1 107 ? -22.134 19.376  -23.011 1.00 38.87  ? 107 LEU A N     1 
ATOM   878  C  CA    . LEU A 1 107 ? -21.491 20.182  -24.036 1.00 37.81  ? 107 LEU A CA    1 
ATOM   879  C  C     . LEU A 1 107 ? -22.270 21.477  -24.235 1.00 34.88  ? 107 LEU A C     1 
ATOM   880  O  O     . LEU A 1 107 ? -23.507 21.456  -24.297 1.00 33.68  ? 107 LEU A O     1 
ATOM   881  C  CB    . LEU A 1 107 ? -21.502 19.425  -25.366 1.00 40.31  ? 107 LEU A CB    1 
ATOM   882  C  CG    . LEU A 1 107 ? -20.276 18.609  -25.768 1.00 42.68  ? 107 LEU A CG    1 
ATOM   883  C  CD1   . LEU A 1 107 ? -20.229 18.565  -27.274 1.00 45.77  ? 107 LEU A CD1   1 
ATOM   884  C  CD2   . LEU A 1 107 ? -18.965 19.144  -25.237 1.00 44.94  ? 107 LEU A CD2   1 
ATOM   885  N  N     . PRO A 1 108 ? -21.582 22.625  -24.426 1.00 30.09  ? 108 PRO A N     1 
ATOM   886  C  CA    . PRO A 1 108 ? -22.254 23.835  -24.893 1.00 28.38  ? 108 PRO A CA    1 
ATOM   887  C  C     . PRO A 1 108 ? -23.101 23.502  -26.113 1.00 29.15  ? 108 PRO A C     1 
ATOM   888  O  O     . PRO A 1 108 ? -22.632 22.864  -27.054 1.00 26.68  ? 108 PRO A O     1 
ATOM   889  C  CB    . PRO A 1 108 ? -21.101 24.752  -25.259 1.00 29.15  ? 108 PRO A CB    1 
ATOM   890  C  CG    . PRO A 1 108 ? -19.966 24.317  -24.389 1.00 30.05  ? 108 PRO A CG    1 
ATOM   891  C  CD    . PRO A 1 108 ? -20.160 22.831  -24.145 1.00 30.20  ? 108 PRO A CD    1 
ATOM   892  N  N     . ARG A 1 109 ? -24.373 23.895  -26.071 1.00 32.81  ? 109 ARG A N     1 
ATOM   893  C  CA    . ARG A 1 109 ? -25.257 23.778  -27.217 1.00 32.24  ? 109 ARG A CA    1 
ATOM   894  C  C     . ARG A 1 109 ? -24.772 24.723  -28.313 1.00 31.30  ? 109 ARG A C     1 
ATOM   895  O  O     . ARG A 1 109 ? -24.953 24.470  -29.505 1.00 31.39  ? 109 ARG A O     1 
ATOM   896  C  CB    . ARG A 1 109 ? -26.691 24.128  -26.827 1.00 35.83  ? 109 ARG A CB    1 
ATOM   897  C  CG    . ARG A 1 109 ? -27.431 23.070  -26.032 1.00 41.68  ? 109 ARG A CG    1 
ATOM   898  C  CD    . ARG A 1 109 ? -27.163 22.995  -24.542 1.00 48.34  ? 109 ARG A CD    1 
ATOM   899  N  NE    . ARG A 1 109 ? -26.270 21.903  -24.186 1.00 55.93  ? 109 ARG A NE    1 
ATOM   900  C  CZ    . ARG A 1 109 ? -26.625 20.630  -24.045 1.00 55.86  ? 109 ARG A CZ    1 
ATOM   901  N  NH1   . ARG A 1 109 ? -25.700 19.697  -24.106 1.00 52.88  ? 109 ARG A NH1   1 
ATOM   902  N  NH2   . ARG A 1 109 ? -27.893 20.280  -23.927 1.00 58.26  ? 109 ARG A NH2   1 
ATOM   903  N  N     . ASN A 1 110 ? -24.149 25.826  -27.894 1.00 30.02  ? 110 ASN A N     1 
ATOM   904  C  CA    . ASN A 1 110 ? -23.764 26.864  -28.824 1.00 29.80  ? 110 ASN A CA    1 
ATOM   905  C  C     . ASN A 1 110 ? -22.378 26.596  -29.393 1.00 31.36  ? 110 ASN A C     1 
ATOM   906  O  O     . ASN A 1 110 ? -21.432 26.452  -28.633 1.00 30.40  ? 110 ASN A O     1 
ATOM   907  C  CB    . ASN A 1 110 ? -23.706 28.218  -28.145 1.00 29.82  ? 110 ASN A CB    1 
ATOM   908  C  CG    . ASN A 1 110 ? -23.331 29.297  -29.130 1.00 32.94  ? 110 ASN A CG    1 
ATOM   909  O  OD1   . ASN A 1 110 ? -22.150 29.562  -29.379 1.00 32.44  ? 110 ASN A OD1   1 
ATOM   910  N  ND2   . ASN A 1 110 ? -24.343 29.983  -29.631 1.00 35.26  ? 110 ASN A ND2   1 
ATOM   911  N  N     . TYR A 1 111 ? -22.258 26.643  -30.728 1.00 29.55  ? 111 TYR A N     1 
ATOM   912  C  CA    . TYR A 1 111 ? -21.050 26.219  -31.406 1.00 28.38  ? 111 TYR A CA    1 
ATOM   913  C  C     . TYR A 1 111 ? -19.812 26.994  -30.943 1.00 28.23  ? 111 TYR A C     1 
ATOM   914  O  O     . TYR A 1 111 ? -18.732 26.423  -30.809 1.00 25.76  ? 111 TYR A O     1 
ATOM   915  C  CB    . TYR A 1 111 ? -21.222 26.435  -32.902 1.00 27.96  ? 111 TYR A CB    1 
ATOM   916  C  CG    . TYR A 1 111 ? -19.963 26.185  -33.725 1.00 28.02  ? 111 TYR A CG    1 
ATOM   917  C  CD1   . TYR A 1 111 ? -19.449 24.899  -33.896 1.00 29.61  ? 111 TYR A CD1   1 
ATOM   918  C  CD2   . TYR A 1 111 ? -19.304 27.231  -34.354 1.00 29.36  ? 111 TYR A CD2   1 
ATOM   919  C  CE1   . TYR A 1 111 ? -18.336 24.660  -34.692 1.00 29.44  ? 111 TYR A CE1   1 
ATOM   920  C  CE2   . TYR A 1 111 ? -18.187 27.012  -35.151 1.00 30.24  ? 111 TYR A CE2   1 
ATOM   921  C  CZ    . TYR A 1 111 ? -17.701 25.724  -35.312 1.00 31.07  ? 111 TYR A CZ    1 
ATOM   922  O  OH    . TYR A 1 111 ? -16.621 25.512  -36.119 1.00 37.52  ? 111 TYR A OH    1 
ATOM   923  N  N     . ASN A 1 112 ? -19.956 28.299  -30.753 1.00 28.16  ? 112 ASN A N     1 
ATOM   924  C  CA    . ASN A 1 112 ? -18.806 29.131  -30.459 1.00 29.60  ? 112 ASN A CA    1 
ATOM   925  C  C     . ASN A 1 112 ? -18.364 28.874  -29.024 1.00 30.31  ? 112 ASN A C     1 
ATOM   926  O  O     . ASN A 1 112 ? -17.178 29.025  -28.758 1.00 32.28  ? 112 ASN A O     1 
ATOM   927  C  CB    . ASN A 1 112 ? -19.053 30.611  -30.773 1.00 30.16  ? 112 ASN A CB    1 
ATOM   928  C  CG    . ASN A 1 112 ? -19.323 30.865  -32.249 1.00 32.15  ? 112 ASN A CG    1 
ATOM   929  O  OD1   . ASN A 1 112 ? -18.558 30.479  -33.137 1.00 31.67  ? 112 ASN A OD1   1 
ATOM   930  N  ND2   . ASN A 1 112 ? -20.431 31.519  -32.543 1.00 32.99  ? 112 ASN A ND2   1 
ATOM   931  N  N     . ARG A 1 113 ? -19.278 28.462  -28.123 1.00 31.74  ? 113 ARG A N     1 
ATOM   932  C  CA    . ARG A 1 113 ? -18.883 28.092  -26.767 1.00 36.17  ? 113 ARG A CA    1 
ATOM   933  C  C     . ARG A 1 113 ? -18.176 26.733  -26.791 1.00 33.11  ? 113 ARG A C     1 
ATOM   934  O  O     . ARG A 1 113 ? -17.204 26.518  -26.061 1.00 32.05  ? 113 ARG A O     1 
ATOM   935  C  CB    . ARG A 1 113 ? -20.028 28.064  -25.755 1.00 42.30  ? 113 ARG A CB    1 
ATOM   936  C  CG    . ARG A 1 113 ? -20.120 29.304  -24.875 1.00 53.64  ? 113 ARG A CG    1 
ATOM   937  C  CD    . ARG A 1 113 ? -21.142 29.081  -23.754 1.00 66.93  ? 113 ARG A CD    1 
ATOM   938  N  NE    . ARG A 1 113 ? -21.603 30.313  -23.097 1.00 76.56  ? 113 ARG A NE    1 
ATOM   939  C  CZ    . ARG A 1 113 ? -22.868 30.763  -23.047 1.00 79.08  ? 113 ARG A CZ    1 
ATOM   940  N  NH1   . ARG A 1 113 ? -23.865 30.078  -23.586 1.00 77.70  ? 113 ARG A NH1   1 
ATOM   941  N  NH2   . ARG A 1 113 ? -23.128 31.922  -22.458 1.00 79.73  ? 113 ARG A NH2   1 
ATOM   942  N  N     . PHE A 1 114 ? -18.650 25.837  -27.654 1.00 28.51  ? 114 PHE A N     1 
ATOM   943  C  CA    . PHE A 1 114 ? -18.014 24.552  -27.839 1.00 28.02  ? 114 PHE A CA    1 
ATOM   944  C  C     . PHE A 1 114 ? -16.580 24.757  -28.311 1.00 27.68  ? 114 PHE A C     1 
ATOM   945  O  O     . PHE A 1 114 ? -15.699 24.075  -27.821 1.00 25.53  ? 114 PHE A O     1 
ATOM   946  C  CB    . PHE A 1 114 ? -18.805 23.730  -28.849 1.00 28.82  ? 114 PHE A CB    1 
ATOM   947  C  CG    . PHE A 1 114 ? -18.079 22.522  -29.377 1.00 28.56  ? 114 PHE A CG    1 
ATOM   948  C  CD1   . PHE A 1 114 ? -17.911 21.398  -28.579 1.00 30.44  ? 114 PHE A CD1   1 
ATOM   949  C  CD2   . PHE A 1 114 ? -17.523 22.537  -30.649 1.00 26.45  ? 114 PHE A CD2   1 
ATOM   950  C  CE1   . PHE A 1 114 ? -17.225 20.293  -29.067 1.00 29.89  ? 114 PHE A CE1   1 
ATOM   951  C  CE2   . PHE A 1 114 ? -16.850 21.431  -31.134 1.00 25.61  ? 114 PHE A CE2   1 
ATOM   952  C  CZ    . PHE A 1 114 ? -16.715 20.313  -30.352 1.00 27.63  ? 114 PHE A CZ    1 
ATOM   953  N  N     . ILE A 1 115 ? -16.378 25.695  -29.256 1.00 27.27  ? 115 ILE A N     1 
ATOM   954  C  CA    . ILE A 1 115 ? -15.070 26.009  -29.793 1.00 27.23  ? 115 ILE A CA    1 
ATOM   955  C  C     . ILE A 1 115 ? -14.163 26.491  -28.674 1.00 28.07  ? 115 ILE A C     1 
ATOM   956  O  O     . ILE A 1 115 ? -13.044 25.971  -28.538 1.00 27.25  ? 115 ILE A O     1 
ATOM   957  C  CB    . ILE A 1 115 ? -15.149 27.033  -30.931 1.00 28.28  ? 115 ILE A CB    1 
ATOM   958  C  CG1   . ILE A 1 115 ? -15.791 26.434  -32.187 1.00 30.18  ? 115 ILE A CG1   1 
ATOM   959  C  CG2   . ILE A 1 115 ? -13.783 27.627  -31.226 1.00 29.38  ? 115 ILE A CG2   1 
ATOM   960  C  CD1   . ILE A 1 115 ? -15.045 25.271  -32.811 1.00 33.22  ? 115 ILE A CD1   1 
ATOM   961  N  N     . GLY A 1 116 ? -14.678 27.453  -27.893 1.00 28.72  ? 116 GLY A N     1 
ATOM   962  C  CA    . GLY A 1 116 ? -14.028 27.986  -26.702 1.00 29.13  ? 116 GLY A CA    1 
ATOM   963  C  C     . GLY A 1 116 ? -13.557 26.870  -25.776 1.00 30.83  ? 116 GLY A C     1 
ATOM   964  O  O     . GLY A 1 116 ? -12.417 26.861  -25.306 1.00 32.76  ? 116 GLY A O     1 
ATOM   965  N  N     . LEU A 1 117 ? -14.435 25.881  -25.592 1.00 29.72  ? 117 LEU A N     1 
ATOM   966  C  CA    . LEU A 1 117 ? -14.184 24.778  -24.688 1.00 29.88  ? 117 LEU A CA    1 
ATOM   967  C  C     . LEU A 1 117 ? -13.103 23.864  -25.247 1.00 30.00  ? 117 LEU A C     1 
ATOM   968  O  O     . LEU A 1 117 ? -12.269 23.374  -24.470 1.00 32.89  ? 117 LEU A O     1 
ATOM   969  C  CB    . LEU A 1 117 ? -15.480 24.004  -24.468 1.00 30.14  ? 117 LEU A CB    1 
ATOM   970  C  CG    . LEU A 1 117 ? -15.355 22.798  -23.545 1.00 32.61  ? 117 LEU A CG    1 
ATOM   971  C  CD1   . LEU A 1 117 ? -14.944 23.267  -22.162 1.00 35.15  ? 117 LEU A CD1   1 
ATOM   972  C  CD2   . LEU A 1 117 ? -16.666 22.023  -23.487 1.00 32.37  ? 117 LEU A CD2   1 
ATOM   973  N  N     . MET A 1 118 ? -13.129 23.635  -26.572 1.00 28.45  ? 118 MET A N     1 
ATOM   974  C  CA    . MET A 1 118 ? -12.105 22.823  -27.223 1.00 29.51  ? 118 MET A CA    1 
ATOM   975  C  C     . MET A 1 118 ? -10.735 23.500  -27.155 1.00 29.84  ? 118 MET A C     1 
ATOM   976  O  O     . MET A 1 118 ? -9.722  22.815  -27.058 1.00 27.97  ? 118 MET A O     1 
ATOM   977  C  CB    . MET A 1 118 ? -12.456 22.544  -28.690 1.00 29.36  ? 118 MET A CB    1 
ATOM   978  C  CG    . MET A 1 118 ? -13.658 21.598  -28.835 1.00 32.38  ? 118 MET A CG    1 
ATOM   979  S  SD    . MET A 1 118 ? -13.423 19.932  -28.082 1.00 30.68  ? 118 MET A SD    1 
ATOM   980  C  CE    . MET A 1 118 ? -14.216 20.135  -26.491 1.00 34.01  ? 118 MET A CE    1 
ATOM   981  N  N     . GLU A 1 119 ? -10.697 24.832  -27.259 1.00 29.54  ? 119 GLU A N     1 
ATOM   982  C  CA    . GLU A 1 119 ? -9.426  25.533  -27.180 1.00 34.12  ? 119 GLU A CA    1 
ATOM   983  C  C     . GLU A 1 119 ? -8.817  25.298  -25.796 1.00 35.79  ? 119 GLU A C     1 
ATOM   984  O  O     . GLU A 1 119 ? -7.606  25.098  -25.673 1.00 35.66  ? 119 GLU A O     1 
ATOM   985  C  CB    . GLU A 1 119 ? -9.594  27.015  -27.534 1.00 35.51  ? 119 GLU A CB    1 
ATOM   986  C  CG    . GLU A 1 119 ? -9.995  27.156  -28.982 1.00 37.04  ? 119 GLU A CG    1 
ATOM   987  C  CD    . GLU A 1 119 ? -10.388 28.510  -29.530 1.00 39.06  ? 119 GLU A CD    1 
ATOM   988  O  OE1   . GLU A 1 119 ? -10.429 28.616  -30.812 1.00 38.06  ? 119 GLU A OE1   1 
ATOM   989  O  OE2   . GLU A 1 119 ? -10.631 29.441  -28.709 1.00 39.94  ? 119 GLU A OE2   1 
ATOM   990  N  N     . ASN A 1 120 ? -9.671  25.329  -24.768 1.00 37.67  ? 120 ASN A N     1 
ATOM   991  C  CA    . ASN A 1 120 ? -9.243  25.084  -23.405 1.00 40.41  ? 120 ASN A CA    1 
ATOM   992  C  C     . ASN A 1 120 ? -8.790  23.632  -23.266 1.00 36.47  ? 120 ASN A C     1 
ATOM   993  O  O     . ASN A 1 120 ? -7.773  23.398  -22.621 1.00 34.35  ? 120 ASN A O     1 
ATOM   994  C  CB    . ASN A 1 120 ? -10.337 25.389  -22.381 1.00 44.95  ? 120 ASN A CB    1 
ATOM   995  C  CG    . ASN A 1 120 ? -10.610 26.870  -22.223 1.00 53.53  ? 120 ASN A CG    1 
ATOM   996  O  OD1   . ASN A 1 120 ? -9.784  27.714  -22.572 1.00 60.24  ? 120 ASN A OD1   1 
ATOM   997  N  ND2   . ASN A 1 120 ? -11.770 27.197  -21.677 1.00 57.58  ? 120 ASN A ND2   1 
ATOM   998  N  N     . LEU A 1 121 ? -9.563  22.675  -23.804 1.00 31.11  ? 121 LEU A N     1 
ATOM   999  C  CA    . LEU A 1 121 ? -9.195  21.275  -23.655 1.00 31.76  ? 121 LEU A CA    1 
ATOM   1000 C  C     . LEU A 1 121 ? -7.816  21.002  -24.280 1.00 32.52  ? 121 LEU A C     1 
ATOM   1001 O  O     . LEU A 1 121 ? -6.943  20.378  -23.654 1.00 34.14  ? 121 LEU A O     1 
ATOM   1002 C  CB    . LEU A 1 121 ? -10.292 20.402  -24.257 1.00 30.84  ? 121 LEU A CB    1 
ATOM   1003 C  CG    . LEU A 1 121 ? -9.960  18.911  -24.329 1.00 30.59  ? 121 LEU A CG    1 
ATOM   1004 C  CD1   . LEU A 1 121 ? -9.674  18.352  -22.956 1.00 33.15  ? 121 LEU A CD1   1 
ATOM   1005 C  CD2   . LEU A 1 121 ? -11.100 18.138  -24.947 1.00 29.33  ? 121 LEU A CD2   1 
ATOM   1006 N  N     . PHE A 1 122 ? -7.559  21.568  -25.469 1.00 31.96  ? 122 PHE A N     1 
ATOM   1007 C  CA    . PHE A 1 122 ? -6.298  21.349  -26.161 1.00 32.19  ? 122 PHE A CA    1 
ATOM   1008 C  C     . PHE A 1 122 ? -5.129  21.954  -25.381 1.00 36.39  ? 122 PHE A C     1 
ATOM   1009 O  O     . PHE A 1 122 ? -4.048  21.378  -25.350 1.00 38.62  ? 122 PHE A O     1 
ATOM   1010 C  CB    . PHE A 1 122 ? -6.348  21.860  -27.598 1.00 30.78  ? 122 PHE A CB    1 
ATOM   1011 C  CG    . PHE A 1 122 ? -6.882  20.860  -28.593 1.00 30.49  ? 122 PHE A CG    1 
ATOM   1012 C  CD1   . PHE A 1 122 ? -8.217  20.511  -28.625 1.00 31.59  ? 122 PHE A CD1   1 
ATOM   1013 C  CD2   . PHE A 1 122 ? -6.050  20.254  -29.518 1.00 30.15  ? 122 PHE A CD2   1 
ATOM   1014 C  CE1   . PHE A 1 122 ? -8.706  19.598  -29.563 1.00 31.22  ? 122 PHE A CE1   1 
ATOM   1015 C  CE2   . PHE A 1 122 ? -6.539  19.350  -30.445 1.00 27.86  ? 122 PHE A CE2   1 
ATOM   1016 C  CZ    . PHE A 1 122 ? -7.868  19.030  -30.481 1.00 27.36  ? 122 PHE A CZ    1 
ATOM   1017 N  N     . GLU A 1 123 ? -5.371  23.090  -24.730 1.00 38.55  ? 123 GLU A N     1 
ATOM   1018 C  CA    . GLU A 1 123 ? -4.371  23.808  -23.971 1.00 42.51  ? 123 GLU A CA    1 
ATOM   1019 C  C     . GLU A 1 123 ? -4.046  23.093  -22.656 1.00 42.98  ? 123 GLU A C     1 
ATOM   1020 O  O     . GLU A 1 123 ? -2.882  22.959  -22.293 1.00 43.43  ? 123 GLU A O     1 
ATOM   1021 C  CB    . GLU A 1 123 ? -4.861  25.241  -23.755 1.00 46.70  ? 123 GLU A CB    1 
ATOM   1022 C  CG    . GLU A 1 123 ? -3.956  26.078  -22.861 1.00 55.64  ? 123 GLU A CG    1 
ATOM   1023 C  CD    . GLU A 1 123 ? -2.576  26.429  -23.419 1.00 63.52  ? 123 GLU A CD    1 
ATOM   1024 O  OE1   . GLU A 1 123 ? -2.264  26.024  -24.573 1.00 65.19  ? 123 GLU A OE1   1 
ATOM   1025 O  OE2   . GLU A 1 123 ? -1.799  27.121  -22.693 1.00 69.36  ? 123 GLU A OE2   1 
ATOM   1026 N  N     . LYS A 1 124 ? -5.053  22.656  -21.906 1.00 40.99  ? 124 LYS A N     1 
ATOM   1027 C  CA    . LYS A 1 124 ? -4.793  22.179  -20.559 1.00 42.39  ? 124 LYS A CA    1 
ATOM   1028 C  C     . LYS A 1 124 ? -4.795  20.660  -20.514 1.00 39.58  ? 124 LYS A C     1 
ATOM   1029 O  O     . LYS A 1 124 ? -4.351  20.100  -19.534 1.00 41.69  ? 124 LYS A O     1 
ATOM   1030 C  CB    . LYS A 1 124 ? -5.844  22.737  -19.604 1.00 48.95  ? 124 LYS A CB    1 
ATOM   1031 C  CG    . LYS A 1 124 ? -5.942  24.258  -19.579 1.00 53.95  ? 124 LYS A CG    1 
ATOM   1032 C  CD    . LYS A 1 124 ? -7.334  24.716  -19.262 1.00 62.02  ? 124 LYS A CD    1 
ATOM   1033 C  CE    . LYS A 1 124 ? -7.558  26.200  -19.477 1.00 74.90  ? 124 LYS A CE    1 
ATOM   1034 N  NZ    . LYS A 1 124 ? -8.999  26.554  -19.398 1.00 77.49  ? 124 LYS A NZ    1 
ATOM   1035 N  N     . GLY A 1 125 ? -5.352  20.002  -21.533 1.00 36.26  ? 125 GLY A N     1 
ATOM   1036 C  CA    . GLY A 1 125 ? -5.354  18.557  -21.589 1.00 36.21  ? 125 GLY A CA    1 
ATOM   1037 C  C     . GLY A 1 125 ? -6.571  17.928  -20.911 1.00 37.14  ? 125 GLY A C     1 
ATOM   1038 O  O     . GLY A 1 125 ? -6.831  16.740  -21.122 1.00 33.40  ? 125 GLY A O     1 
ATOM   1039 N  N     . ALA A 1 126 ? -7.336  18.725  -20.145 1.00 37.17  ? 126 ALA A N     1 
ATOM   1040 C  CA    . ALA A 1 126 ? -8.448  18.198  -19.366 1.00 39.21  ? 126 ALA A CA    1 
ATOM   1041 C  C     . ALA A 1 126 ? -9.285  19.356  -18.836 1.00 41.00  ? 126 ALA A C     1 
ATOM   1042 O  O     . ALA A 1 126 ? -8.716  20.294  -18.286 1.00 42.25  ? 126 ALA A O     1 
ATOM   1043 C  CB    . ALA A 1 126 ? -7.910  17.342  -18.227 1.00 38.98  ? 126 ALA A CB    1 
ATOM   1044 N  N     . VAL A 1 127 ? -10.619 19.279  -18.984 1.00 41.77  ? 127 VAL A N     1 
ATOM   1045 C  CA    . VAL A 1 127 ? -11.482 20.348  -18.496 1.00 45.33  ? 127 VAL A CA    1 
ATOM   1046 C  C     . VAL A 1 127 ? -12.685 19.762  -17.750 1.00 48.61  ? 127 VAL A C     1 
ATOM   1047 O  O     . VAL A 1 127 ? -13.111 18.657  -18.022 1.00 43.18  ? 127 VAL A O     1 
ATOM   1048 C  CB    . VAL A 1 127 ? -11.956 21.276  -19.628 1.00 42.52  ? 127 VAL A CB    1 
ATOM   1049 C  CG1   . VAL A 1 127 ? -10.819 22.045  -20.269 1.00 43.43  ? 127 VAL A CG1   1 
ATOM   1050 C  CG2   . VAL A 1 127 ? -12.688 20.492  -20.684 1.00 43.71  ? 127 VAL A CG2   1 
ATOM   1051 N  N     . PRO A 1 128 ? -13.237 20.446  -16.723 1.00 56.11  ? 128 PRO A N     1 
ATOM   1052 C  CA    . PRO A 1 128 ? -12.487 21.422  -15.931 1.00 60.27  ? 128 PRO A CA    1 
ATOM   1053 C  C     . PRO A 1 128 ? -11.378 20.837  -15.055 1.00 63.26  ? 128 PRO A C     1 
ATOM   1054 O  O     . PRO A 1 128 ? -11.235 19.628  -14.893 1.00 59.74  ? 128 PRO A O     1 
ATOM   1055 C  CB    . PRO A 1 128 ? -13.520 21.974  -14.925 1.00 63.52  ? 128 PRO A CB    1 
ATOM   1056 C  CG    . PRO A 1 128 ? -14.876 21.683  -15.558 1.00 62.27  ? 128 PRO A CG    1 
ATOM   1057 C  CD    . PRO A 1 128 ? -14.669 20.428  -16.387 1.00 60.04  ? 128 PRO A CD    1 
ATOM   1058 N  N     . GLU A 1 129 ? -10.595 21.741  -14.475 1.00 73.15  ? 129 GLU A N     1 
ATOM   1059 C  CA    . GLU A 1 129 ? -9.383  21.386  -13.760 1.00 84.70  ? 129 GLU A CA    1 
ATOM   1060 C  C     . GLU A 1 129 ? -9.520  20.099  -12.933 1.00 83.63  ? 129 GLU A C     1 
ATOM   1061 O  O     . GLU A 1 129 ? -8.669  19.215  -13.029 1.00 75.05  ? 129 GLU A O     1 
ATOM   1062 C  CB    . GLU A 1 129 ? -8.907  22.581  -12.917 1.00 94.16  ? 129 GLU A CB    1 
ATOM   1063 C  CG    . GLU A 1 129 ? -9.453  23.965  -13.332 1.00 99.45  ? 129 GLU A CG    1 
ATOM   1064 C  CD    . GLU A 1 129 ? -9.572  24.339  -14.812 1.00 97.38  ? 129 GLU A CD    1 
ATOM   1065 O  OE1   . GLU A 1 129 ? -10.701 24.678  -15.240 1.00 84.38  ? 129 GLU A OE1   1 
ATOM   1066 O  OE2   . GLU A 1 129 ? -8.542  24.331  -15.534 1.00 97.98  ? 129 GLU A OE2   1 
ATOM   1067 N  N     . ASP A 1 130 ? -10.601 19.981  -12.142 1.00 85.36  ? 130 ASP A N     1 
ATOM   1068 C  CA    . ASP A 1 130 ? -10.774 18.856  -11.229 1.00 86.56  ? 130 ASP A CA    1 
ATOM   1069 C  C     . ASP A 1 130 ? -11.498 17.679  -11.881 1.00 82.10  ? 130 ASP A C     1 
ATOM   1070 O  O     . ASP A 1 130 ? -10.993 16.557  -11.846 1.00 77.89  ? 130 ASP A O     1 
ATOM   1071 C  CB    . ASP A 1 130 ? -11.534 19.266  -9.968  1.00 90.09  ? 130 ASP A CB    1 
ATOM   1072 C  CG    . ASP A 1 130 ? -10.616 19.683  -8.839  1.00 98.78  ? 130 ASP A CG    1 
ATOM   1073 O  OD1   . ASP A 1 130 ? -9.392  19.736  -9.081  1.00 105.63 ? 130 ASP A OD1   1 
ATOM   1074 O  OD2   . ASP A 1 130 ? -11.128 19.927  -7.724  1.00 103.76 ? 130 ASP A OD2   1 
ATOM   1075 N  N     . LEU A 1 131 ? -12.694 17.940  -12.431 1.00 79.66  ? 131 LEU A N     1 
ATOM   1076 C  CA    . LEU A 1 131 ? -13.614 16.907  -12.902 1.00 73.76  ? 131 LEU A CA    1 
ATOM   1077 C  C     . LEU A 1 131 ? -12.991 16.058  -14.010 1.00 70.74  ? 131 LEU A C     1 
ATOM   1078 O  O     . LEU A 1 131 ? -13.282 14.859  -14.134 1.00 63.89  ? 131 LEU A O     1 
ATOM   1079 C  CB    . LEU A 1 131 ? -14.892 17.574  -13.436 1.00 72.76  ? 131 LEU A CB    1 
ATOM   1080 C  CG    . LEU A 1 131 ? -15.945 17.995  -12.407 1.00 79.61  ? 131 LEU A CG    1 
ATOM   1081 C  CD1   . LEU A 1 131 ? -17.078 18.784  -13.061 1.00 75.62  ? 131 LEU A CD1   1 
ATOM   1082 C  CD2   . LEU A 1 131 ? -16.517 16.785  -11.678 1.00 81.73  ? 131 LEU A CD2   1 
ATOM   1083 N  N     . GLU A 1 132 ? -12.193 16.717  -14.859 1.00 66.38  ? 132 GLU A N     1 
ATOM   1084 C  CA    . GLU A 1 132 ? -11.743 16.132  -16.105 1.00 60.01  ? 132 GLU A CA    1 
ATOM   1085 C  C     . GLU A 1 132 ? -12.927 15.410  -16.745 1.00 57.76  ? 132 GLU A C     1 
ATOM   1086 O  O     . GLU A 1 132 ? -12.812 14.212  -17.043 1.00 61.92  ? 132 GLU A O     1 
ATOM   1087 C  CB    . GLU A 1 132 ? -10.568 15.189  -15.851 1.00 64.86  ? 132 GLU A CB    1 
ATOM   1088 C  CG    . GLU A 1 132 ? -9.486  15.804  -14.969 1.00 76.22  ? 132 GLU A CG    1 
ATOM   1089 C  CD    . GLU A 1 132 ? -8.179  15.025  -14.846 1.00 83.20  ? 132 GLU A CD    1 
ATOM   1090 O  OE1   . GLU A 1 132 ? -7.381  15.357  -13.921 1.00 79.49  ? 132 GLU A OE1   1 
ATOM   1091 O  OE2   . GLU A 1 132 ? -7.940  14.103  -15.686 1.00 77.58  ? 132 GLU A OE2   1 
ATOM   1092 N  N     . LEU A 1 133 ? -14.047 16.145  -16.935 1.00 43.99  ? 133 LEU A N     1 
ATOM   1093 C  CA    . LEU A 1 133 ? -15.158 15.636  -17.727 1.00 41.38  ? 133 LEU A CA    1 
ATOM   1094 C  C     . LEU A 1 133 ? -14.709 15.348  -19.163 1.00 37.46  ? 133 LEU A C     1 
ATOM   1095 O  O     . LEU A 1 133 ? -15.198 14.394  -19.782 1.00 33.27  ? 133 LEU A O     1 
ATOM   1096 C  CB    . LEU A 1 133 ? -16.319 16.636  -17.736 1.00 39.84  ? 133 LEU A CB    1 
ATOM   1097 C  CG    . LEU A 1 133 ? -16.985 16.896  -16.384 1.00 42.30  ? 133 LEU A CG    1 
ATOM   1098 C  CD1   . LEU A 1 133 ? -18.038 17.996  -16.499 1.00 40.40  ? 133 LEU A CD1   1 
ATOM   1099 C  CD2   . LEU A 1 133 ? -17.603 15.624  -15.805 1.00 42.09  ? 133 LEU A CD2   1 
ATOM   1100 N  N     . LEU A 1 134 ? -13.848 16.232  -19.697 1.00 33.18  ? 134 LEU A N     1 
ATOM   1101 C  CA    . LEU A 1 134 ? -13.122 15.998  -20.927 1.00 32.27  ? 134 LEU A CA    1 
ATOM   1102 C  C     . LEU A 1 134 ? -11.636 15.855  -20.608 1.00 32.72  ? 134 LEU A C     1 
ATOM   1103 O  O     . LEU A 1 134 ? -11.089 16.592  -19.793 1.00 34.98  ? 134 LEU A O     1 
ATOM   1104 C  CB    . LEU A 1 134 ? -13.349 17.190  -21.855 1.00 34.05  ? 134 LEU A CB    1 
ATOM   1105 C  CG    . LEU A 1 134 ? -14.796 17.465  -22.275 1.00 33.92  ? 134 LEU A CG    1 
ATOM   1106 C  CD1   . LEU A 1 134 ? -14.924 18.834  -22.877 1.00 36.40  ? 134 LEU A CD1   1 
ATOM   1107 C  CD2   . LEU A 1 134 ? -15.307 16.442  -23.272 1.00 32.08  ? 134 LEU A CD2   1 
ATOM   1108 N  N     . ARG A 1 135 ? -10.994 14.921  -21.303 1.00 32.54  ? 135 ARG A N     1 
ATOM   1109 C  CA    . ARG A 1 135 ? -9.613  14.519  -21.072 1.00 35.09  ? 135 ARG A CA    1 
ATOM   1110 C  C     . ARG A 1 135 ? -9.056  14.073  -22.414 1.00 31.09  ? 135 ARG A C     1 
ATOM   1111 O  O     . ARG A 1 135 ? -9.689  13.270  -23.061 1.00 29.67  ? 135 ARG A O     1 
ATOM   1112 C  CB    . ARG A 1 135 ? -9.555  13.365  -20.067 1.00 37.47  ? 135 ARG A CB    1 
ATOM   1113 C  CG    . ARG A 1 135 ? -8.167  12.853  -19.752 1.00 42.12  ? 135 ARG A CG    1 
ATOM   1114 C  CD    . ARG A 1 135 ? -8.226  11.842  -18.614 1.00 46.47  ? 135 ARG A CD    1 
ATOM   1115 N  NE    . ARG A 1 135 ? -8.934  10.595  -18.939 1.00 46.10  ? 135 ARG A NE    1 
ATOM   1116 C  CZ    . ARG A 1 135 ? -8.395  9.551   -19.571 1.00 40.17  ? 135 ARG A CZ    1 
ATOM   1117 N  NH1   . ARG A 1 135 ? -7.151  9.613   -20.000 1.00 39.76  ? 135 ARG A NH1   1 
ATOM   1118 N  NH2   . ARG A 1 135 ? -9.102  8.460   -19.805 1.00 37.91  ? 135 ARG A NH2   1 
ATOM   1119 N  N     . MET A 1 136 ? -7.885  14.583  -22.795 1.00 30.50  ? 136 MET A N     1 
ATOM   1120 C  CA    . MET A 1 136 ? -7.281  14.351  -24.100 1.00 31.35  ? 136 MET A CA    1 
ATOM   1121 C  C     . MET A 1 136 ? -5.893  13.716  -23.958 1.00 29.97  ? 136 MET A C     1 
ATOM   1122 O  O     . MET A 1 136 ? -5.147  14.050  -23.074 1.00 28.89  ? 136 MET A O     1 
ATOM   1123 C  CB    . MET A 1 136 ? -7.109  15.698  -24.803 1.00 35.30  ? 136 MET A CB    1 
ATOM   1124 C  CG    . MET A 1 136 ? -6.456  15.607  -26.165 1.00 40.52  ? 136 MET A CG    1 
ATOM   1125 S  SD    . MET A 1 136 ? -6.590  17.191  -26.995 1.00 37.75  ? 136 MET A SD    1 
ATOM   1126 C  CE    . MET A 1 136 ? -5.329  18.026  -26.044 1.00 44.85  ? 136 MET A CE    1 
ATOM   1127 N  N     . GLU A 1 137 ? -5.504  12.818  -24.850 1.00 29.11  ? 137 GLU A N     1 
ATOM   1128 C  CA    . GLU A 1 137 ? -4.131  12.394  -24.835 1.00 30.60  ? 137 GLU A CA    1 
ATOM   1129 C  C     . GLU A 1 137 ? -3.787  11.768  -26.171 1.00 28.44  ? 137 GLU A C     1 
ATOM   1130 O  O     . GLU A 1 137 ? -4.670  11.476  -26.963 1.00 26.62  ? 137 GLU A O     1 
ATOM   1131 C  CB    . GLU A 1 137 ? -3.875  11.444  -23.669 1.00 36.41  ? 137 GLU A CB    1 
ATOM   1132 C  CG    . GLU A 1 137 ? -4.671  10.165  -23.757 1.00 37.27  ? 137 GLU A CG    1 
ATOM   1133 C  CD    . GLU A 1 137 ? -4.682  9.387   -22.460 1.00 42.11  ? 137 GLU A CD    1 
ATOM   1134 O  OE1   . GLU A 1 137 ? -4.888  10.021  -21.418 1.00 45.78  ? 137 GLU A OE1   1 
ATOM   1135 O  OE2   . GLU A 1 137 ? -4.510  8.152   -22.502 1.00 51.68  ? 137 GLU A OE2   1 
ATOM   1136 N  N     . LYS A 1 138 ? -2.479  11.607  -26.387 1.00 27.47  ? 138 LYS A N     1 
ATOM   1137 C  CA    . LYS A 1 138 ? -1.948  11.050  -27.607 1.00 27.15  ? 138 LYS A CA    1 
ATOM   1138 C  C     . LYS A 1 138 ? -2.356  9.591   -27.663 1.00 26.88  ? 138 LYS A C     1 
ATOM   1139 O  O     . LYS A 1 138 ? -2.111  8.858   -26.710 1.00 27.16  ? 138 LYS A O     1 
ATOM   1140 C  CB    . LYS A 1 138 ? -0.420  11.146  -27.590 1.00 29.28  ? 138 LYS A CB    1 
ATOM   1141 C  CG    . LYS A 1 138 ? 0.266   10.834  -28.907 1.00 29.63  ? 138 LYS A CG    1 
ATOM   1142 C  CD    . LYS A 1 138 ? 0.085   11.932  -29.977 1.00 30.23  ? 138 LYS A CD    1 
ATOM   1143 C  CE    . LYS A 1 138 ? 0.200   11.322  -31.355 1.00 31.58  ? 138 LYS A CE    1 
ATOM   1144 N  NZ    . LYS A 1 138 ? 0.426   12.347  -32.364 1.00 33.24  ? 138 LYS A NZ    1 
ATOM   1145 N  N     . LYS A 1 139 ? -2.877  9.143   -28.801 1.00 27.35  ? 139 LYS A N     1 
ATOM   1146 C  CA    . LYS A 1 139 ? -3.341  7.771   -28.871 1.00 28.33  ? 139 LYS A CA    1 
ATOM   1147 C  C     . LYS A 1 139 ? -3.799  7.428   -30.281 1.00 26.57  ? 139 LYS A C     1 
ATOM   1148 O  O     . LYS A 1 139 ? -4.484  8.214   -30.924 1.00 25.85  ? 139 LYS A O     1 
ATOM   1149 C  CB    . LYS A 1 139 ? -4.482  7.658   -27.864 1.00 31.48  ? 139 LYS A CB    1 
ATOM   1150 C  CG    . LYS A 1 139 ? -5.043  6.270   -27.677 1.00 33.82  ? 139 LYS A CG    1 
ATOM   1151 C  CD    . LYS A 1 139 ? -5.365  6.005   -26.261 1.00 35.68  ? 139 LYS A CD    1 
ATOM   1152 C  CE    . LYS A 1 139 ? -4.146  5.583   -25.498 1.00 38.01  ? 139 LYS A CE    1 
ATOM   1153 N  NZ    . LYS A 1 139 ? -4.446  5.459   -24.063 1.00 39.03  ? 139 LYS A NZ    1 
ATOM   1154 N  N     . THR A 1 140 ? -3.496  6.215   -30.729 1.00 26.48  ? 140 THR A N     1 
ATOM   1155 C  CA    . THR A 1 140 ? -3.979  5.783   -32.027 1.00 25.52  ? 140 THR A CA    1 
ATOM   1156 C  C     . THR A 1 140 ? -5.353  5.159   -31.808 1.00 24.71  ? 140 THR A C     1 
ATOM   1157 O  O     . THR A 1 140 ? -5.788  4.970   -30.664 1.00 27.04  ? 140 THR A O     1 
ATOM   1158 C  CB    . THR A 1 140 ? -3.017  4.801   -32.717 1.00 26.54  ? 140 THR A CB    1 
ATOM   1159 O  OG1   . THR A 1 140 ? -2.997  3.616   -31.915 1.00 26.66  ? 140 THR A OG1   1 
ATOM   1160 C  CG2   . THR A 1 140 ? -1.621  5.365   -32.940 1.00 27.01  ? 140 THR A CG2   1 
ATOM   1161 N  N     . LEU A 1 141 ? -6.026  4.822   -32.922 1.00 23.09  ? 141 LEU A N     1 
ATOM   1162 C  CA    . LEU A 1 141 ? -7.347  4.220   -32.841 1.00 21.82  ? 141 LEU A CA    1 
ATOM   1163 C  C     . LEU A 1 141 ? -7.240  2.827   -32.216 1.00 22.98  ? 141 LEU A C     1 
ATOM   1164 O  O     . LEU A 1 141 ? -8.052  2.467   -31.365 1.00 22.71  ? 141 LEU A O     1 
ATOM   1165 C  CB    . LEU A 1 141 ? -7.966  4.220   -34.240 1.00 20.86  ? 141 LEU A CB    1 
ATOM   1166 C  CG    . LEU A 1 141 ? -9.408  3.742   -34.337 1.00 21.18  ? 141 LEU A CG    1 
ATOM   1167 C  CD1   . LEU A 1 141 ? -10.301 4.404   -33.303 1.00 22.20  ? 141 LEU A CD1   1 
ATOM   1168 C  CD2   . LEU A 1 141 ? -9.952  4.057   -35.715 1.00 22.27  ? 141 LEU A CD2   1 
ATOM   1169 N  N     . ASN A 1 142 ? -6.218  2.055   -32.631 1.00 24.07  ? 142 ASN A N     1 
ATOM   1170 C  CA    . ASN A 1 142 ? -5.996  0.710   -32.133 1.00 23.32  ? 142 ASN A CA    1 
ATOM   1171 C  C     . ASN A 1 142 ? -5.664  0.737   -30.653 1.00 23.50  ? 142 ASN A C     1 
ATOM   1172 O  O     . ASN A 1 142 ? -6.135  -0.104  -29.911 1.00 24.00  ? 142 ASN A O     1 
ATOM   1173 C  CB    . ASN A 1 142 ? -4.874  0.002   -32.884 1.00 25.40  ? 142 ASN A CB    1 
ATOM   1174 C  CG    . ASN A 1 142 ? -5.312  -0.654  -34.187 1.00 26.00  ? 142 ASN A CG    1 
ATOM   1175 O  OD1   . ASN A 1 142 ? -6.436  -1.140  -34.357 1.00 26.56  ? 142 ASN A OD1   1 
ATOM   1176 N  ND2   . ASN A 1 142 ? -4.378  -0.751  -35.102 1.00 26.92  ? 142 ASN A ND2   1 
ATOM   1177 N  N     . GLU A 1 143 ? -4.904  1.733   -30.205 1.00 24.10  ? 143 GLU A N     1 
ATOM   1178 C  CA    . GLU A 1 143 ? -4.551  1.853   -28.788 1.00 24.79  ? 143 GLU A CA    1 
ATOM   1179 C  C     . GLU A 1 143 ? -5.839  2.084   -27.994 1.00 24.78  ? 143 GLU A C     1 
ATOM   1180 O  O     . GLU A 1 143 ? -6.000  1.538   -26.903 1.00 23.96  ? 143 GLU A O     1 
ATOM   1181 C  CB    . GLU A 1 143 ? -3.487  2.942   -28.577 1.00 25.91  ? 143 GLU A CB    1 
ATOM   1182 C  CG    . GLU A 1 143 ? -2.151  2.611   -29.259 1.00 27.53  ? 143 GLU A CG    1 
ATOM   1183 C  CD    . GLU A 1 143 ? -1.074  3.679   -29.475 1.00 29.30  ? 143 GLU A CD    1 
ATOM   1184 O  OE1   . GLU A 1 143 ? 0.058   3.281   -29.877 1.00 31.68  ? 143 GLU A OE1   1 
ATOM   1185 O  OE2   . GLU A 1 143 ? -1.315  4.883   -29.217 1.00 26.76  ? 143 GLU A OE2   1 
ATOM   1186 N  N     . LEU A 1 144 ? -6.755  2.886   -28.565 1.00 23.50  ? 144 LEU A N     1 
ATOM   1187 C  CA    . LEU A 1 144 ? -8.016  3.189   -27.910 1.00 23.28  ? 144 LEU A CA    1 
ATOM   1188 C  C     . LEU A 1 144 ? -8.889  1.930   -27.824 1.00 23.54  ? 144 LEU A C     1 
ATOM   1189 O  O     . LEU A 1 144 ? -9.379  1.562   -26.754 1.00 26.14  ? 144 LEU A O     1 
ATOM   1190 C  CB    . LEU A 1 144 ? -8.736  4.310   -28.668 1.00 21.39  ? 144 LEU A CB    1 
ATOM   1191 C  CG    . LEU A 1 144 ? -10.145 4.641   -28.169 1.00 21.94  ? 144 LEU A CG    1 
ATOM   1192 C  CD1   . LEU A 1 144 ? -10.169 4.981   -26.679 1.00 21.95  ? 144 LEU A CD1   1 
ATOM   1193 C  CD2   . LEU A 1 144 ? -10.770 5.785   -28.963 1.00 20.88  ? 144 LEU A CD2   1 
ATOM   1194 N  N     . ILE A 1 145 ? -9.023  1.237   -28.942 1.00 22.96  ? 145 ILE A N     1 
ATOM   1195 C  CA    . ILE A 1 145 ? -9.766  -0.005  -28.997 1.00 23.21  ? 145 ILE A CA    1 
ATOM   1196 C  C     . ILE A 1 145 ? -9.210  -1.023  -28.000 1.00 23.69  ? 145 ILE A C     1 
ATOM   1197 O  O     . ILE A 1 145 ? -9.978  -1.769  -27.443 1.00 23.78  ? 145 ILE A O     1 
ATOM   1198 C  CB    . ILE A 1 145 ? -9.778  -0.495  -30.457 1.00 24.02  ? 145 ILE A CB    1 
ATOM   1199 C  CG1   . ILE A 1 145 ? -10.713 0.378   -31.300 1.00 23.40  ? 145 ILE A CG1   1 
ATOM   1200 C  CG2   . ILE A 1 145 ? -10.131 -1.966  -30.557 1.00 24.20  ? 145 ILE A CG2   1 
ATOM   1201 C  CD1   . ILE A 1 145 ? -10.510 0.222   -32.796 1.00 23.12  ? 145 ILE A CD1   1 
ATOM   1202 N  N     . GLU A 1 146 ? -7.905  -1.035  -27.747 1.00 25.38  ? 146 GLU A N     1 
ATOM   1203 C  CA    . GLU A 1 146 ? -7.269  -1.981  -26.833 1.00 28.51  ? 146 GLU A CA    1 
ATOM   1204 C  C     . GLU A 1 146 ? -7.757  -1.764  -25.400 1.00 28.91  ? 146 GLU A C     1 
ATOM   1205 O  O     . GLU A 1 146 ? -7.964  -2.706  -24.641 1.00 26.73  ? 146 GLU A O     1 
ATOM   1206 C  CB    . GLU A 1 146 ? -5.739  -1.796  -26.868 1.00 29.88  ? 146 GLU A CB    1 
ATOM   1207 C  CG    . GLU A 1 146 ? -4.955  -2.732  -25.956 1.00 31.99  ? 146 GLU A CG    1 
ATOM   1208 C  CD    . GLU A 1 146 ? -3.427  -2.622  -25.935 1.00 34.80  ? 146 GLU A CD    1 
ATOM   1209 O  OE1   . GLU A 1 146 ? -2.841  -1.614  -26.444 1.00 35.20  ? 146 GLU A OE1   1 
ATOM   1210 O  OE2   . GLU A 1 146 ? -2.793  -3.561  -25.395 1.00 36.66  ? 146 GLU A OE2   1 
ATOM   1211 N  N     . GLU A 1 147 ? -7.835  -0.488  -25.031 1.00 29.64  ? 147 GLU A N     1 
ATOM   1212 C  CA    . GLU A 1 147 ? -8.360  -0.064  -23.757 1.00 31.91  ? 147 GLU A CA    1 
ATOM   1213 C  C     . GLU A 1 147 ? -9.819  -0.429  -23.598 1.00 27.69  ? 147 GLU A C     1 
ATOM   1214 O  O     . GLU A 1 147 ? -10.241 -0.820  -22.528 1.00 29.13  ? 147 GLU A O     1 
ATOM   1215 C  CB    . GLU A 1 147 ? -8.398  1.458   -23.670 1.00 38.00  ? 147 GLU A CB    1 
ATOM   1216 C  CG    . GLU A 1 147 ? -7.121  2.098   -23.246 1.00 44.40  ? 147 GLU A CG    1 
ATOM   1217 C  CD    . GLU A 1 147 ? -7.342  3.596   -23.268 1.00 51.91  ? 147 GLU A CD    1 
ATOM   1218 O  OE1   . GLU A 1 147 ? -8.231  4.087   -22.516 1.00 53.34  ? 147 GLU A OE1   1 
ATOM   1219 O  OE2   . GLU A 1 147 ? -6.641  4.255   -24.053 1.00 60.89  ? 147 GLU A OE2   1 
ATOM   1220 N  N     . ILE A 1 148 ? -10.628 -0.100  -24.595 1.00 25.67  ? 148 ILE A N     1 
ATOM   1221 C  CA    . ILE A 1 148 ? -12.053 -0.374  -24.491 1.00 26.11  ? 148 ILE A CA    1 
ATOM   1222 C  C     . ILE A 1 148 ? -12.252 -1.877  -24.308 1.00 27.18  ? 148 ILE A C     1 
ATOM   1223 O  O     . ILE A 1 148 ? -13.067 -2.313  -23.506 1.00 26.85  ? 148 ILE A O     1 
ATOM   1224 C  CB    . ILE A 1 148 ? -12.813 0.183   -25.708 1.00 24.89  ? 148 ILE A CB    1 
ATOM   1225 C  CG1   . ILE A 1 148 ? -12.807 1.711   -25.694 1.00 24.34  ? 148 ILE A CG1   1 
ATOM   1226 C  CG2   . ILE A 1 148 ? -14.223 -0.377  -25.779 1.00 24.33  ? 148 ILE A CG2   1 
ATOM   1227 C  CD1   . ILE A 1 148 ? -13.216 2.327   -27.000 1.00 23.77  ? 148 ILE A CD1   1 
ATOM   1228 N  N     . ASN A 1 149 ? -11.462 -2.662  -25.047 1.00 27.22  ? 149 ASN A N     1 
ATOM   1229 C  CA    . ASN A 1 149 ? -11.517 -4.103  -24.951 1.00 27.65  ? 149 ASN A CA    1 
ATOM   1230 C  C     . ASN A 1 149 ? -12.939 -4.545  -25.237 1.00 26.53  ? 149 ASN A C     1 
ATOM   1231 O  O     . ASN A 1 149 ? -13.519 -5.235  -24.423 1.00 26.14  ? 149 ASN A O     1 
ATOM   1232 C  CB    . ASN A 1 149 ? -11.063 -4.575  -23.582 1.00 29.91  ? 149 ASN A CB    1 
ATOM   1233 C  CG    . ASN A 1 149 ? -10.967 -6.080  -23.508 1.00 32.67  ? 149 ASN A CG    1 
ATOM   1234 O  OD1   . ASN A 1 149 ? -10.806 -6.753  -24.520 1.00 33.63  ? 149 ASN A OD1   1 
ATOM   1235 N  ND2   . ASN A 1 149 ? -11.052 -6.611  -22.304 1.00 33.37  ? 149 ASN A ND2   1 
ATOM   1236 N  N     . PRO A 1 150 ? -13.481 -4.222  -26.440 1.00 26.93  ? 150 PRO A N     1 
ATOM   1237 C  CA    . PRO A 1 150 ? -14.835 -4.610  -26.838 1.00 26.60  ? 150 PRO A CA    1 
ATOM   1238 C  C     . PRO A 1 150 ? -14.891 -6.089  -27.242 1.00 29.34  ? 150 PRO A C     1 
ATOM   1239 O  O     . PRO A 1 150 ? -13.847 -6.694  -27.486 1.00 28.23  ? 150 PRO A O     1 
ATOM   1240 C  CB    . PRO A 1 150 ? -15.092 -3.714  -28.057 1.00 24.97  ? 150 PRO A CB    1 
ATOM   1241 C  CG    . PRO A 1 150 ? -13.739 -3.585  -28.721 1.00 24.81  ? 150 PRO A CG    1 
ATOM   1242 C  CD    . PRO A 1 150 ? -12.742 -3.614  -27.574 1.00 25.94  ? 150 PRO A CD    1 
ATOM   1243 N  N     . ASP A 1 151 ? -16.111 -6.660  -27.318 1.00 29.50  ? 151 ASP A N     1 
ATOM   1244 C  CA    . ASP A 1 151 ? -16.282 -8.005  -27.831 1.00 30.35  ? 151 ASP A CA    1 
ATOM   1245 C  C     . ASP A 1 151 ? -16.643 -7.939  -29.311 1.00 29.03  ? 151 ASP A C     1 
ATOM   1246 O  O     . ASP A 1 151 ? -16.712 -8.967  -29.973 1.00 30.59  ? 151 ASP A O     1 
ATOM   1247 C  CB    . ASP A 1 151 ? -17.294 -8.819  -27.028 1.00 32.31  ? 151 ASP A CB    1 
ATOM   1248 C  CG    . ASP A 1 151 ? -18.674 -8.200  -26.836 1.00 32.51  ? 151 ASP A CG    1 
ATOM   1249 O  OD1   . ASP A 1 151 ? -18.816 -6.978  -27.015 1.00 33.52  ? 151 ASP A OD1   1 
ATOM   1250 O  OD2   . ASP A 1 151 ? -19.605 -8.953  -26.486 1.00 34.43  ? 151 ASP A OD2   1 
ATOM   1251 N  N     . VAL A 1 152 ? -16.847 -6.741  -29.855 1.00 26.72  ? 152 VAL A N     1 
ATOM   1252 C  CA    . VAL A 1 152 ? -16.994 -6.650  -31.299 1.00 27.16  ? 152 VAL A CA    1 
ATOM   1253 C  C     . VAL A 1 152 ? -16.795 -5.198  -31.721 1.00 24.64  ? 152 VAL A C     1 
ATOM   1254 O  O     . VAL A 1 152 ? -17.096 -4.297  -30.971 1.00 24.38  ? 152 VAL A O     1 
ATOM   1255 C  CB    . VAL A 1 152 ? -18.369 -7.167  -31.758 1.00 28.83  ? 152 VAL A CB    1 
ATOM   1256 C  CG1   . VAL A 1 152 ? -19.466 -6.191  -31.405 1.00 29.09  ? 152 VAL A CG1   1 
ATOM   1257 C  CG2   . VAL A 1 152 ? -18.410 -7.463  -33.244 1.00 29.49  ? 152 VAL A CG2   1 
ATOM   1258 N  N     . VAL A 1 153 ? -16.303 -4.999  -32.936 1.00 23.93  ? 153 VAL A N     1 
ATOM   1259 C  CA    . VAL A 1 153 ? -16.071 -3.689  -33.477 1.00 23.92  ? 153 VAL A CA    1 
ATOM   1260 C  C     . VAL A 1 153 ? -16.792 -3.588  -34.812 1.00 24.04  ? 153 VAL A C     1 
ATOM   1261 O  O     . VAL A 1 153 ? -16.611 -4.409  -35.705 1.00 23.76  ? 153 VAL A O     1 
ATOM   1262 C  CB    . VAL A 1 153 ? -14.568 -3.402  -33.634 1.00 25.39  ? 153 VAL A CB    1 
ATOM   1263 C  CG1   . VAL A 1 153 ? -14.342 -1.993  -34.190 1.00 24.73  ? 153 VAL A CG1   1 
ATOM   1264 C  CG2   . VAL A 1 153 ? -13.819 -3.580  -32.322 1.00 26.43  ? 153 VAL A CG2   1 
ATOM   1265 N  N     . PHE A 1 154 ? -17.629 -2.561  -34.932 1.00 23.70  ? 154 PHE A N     1 
ATOM   1266 C  CA    . PHE A 1 154 ? -18.297 -2.292  -36.183 1.00 23.03  ? 154 PHE A CA    1 
ATOM   1267 C  C     . PHE A 1 154 ? -17.752 -0.988  -36.702 1.00 22.81  ? 154 PHE A C     1 
ATOM   1268 O  O     . PHE A 1 154 ? -17.527 -0.073  -35.936 1.00 23.40  ? 154 PHE A O     1 
ATOM   1269 C  CB    . PHE A 1 154 ? -19.794 -2.168  -35.953 1.00 22.69  ? 154 PHE A CB    1 
ATOM   1270 C  CG    . PHE A 1 154 ? -20.493 -3.444  -35.583 1.00 23.05  ? 154 PHE A CG    1 
ATOM   1271 C  CD1   . PHE A 1 154 ? -20.729 -4.415  -36.545 1.00 24.93  ? 154 PHE A CD1   1 
ATOM   1272 C  CD2   . PHE A 1 154 ? -20.876 -3.689  -34.277 1.00 22.41  ? 154 PHE A CD2   1 
ATOM   1273 C  CE1   . PHE A 1 154 ? -21.368 -5.601  -36.226 1.00 25.04  ? 154 PHE A CE1   1 
ATOM   1274 C  CE2   . PHE A 1 154 ? -21.531 -4.857  -33.951 1.00 24.35  ? 154 PHE A CE2   1 
ATOM   1275 C  CZ    . PHE A 1 154 ? -21.785 -5.818  -34.925 1.00 26.11  ? 154 PHE A CZ    1 
ATOM   1276 N  N     . ILE A 1 155 ? -17.597 -0.903  -38.009 1.00 24.62  ? 155 ILE A N     1 
ATOM   1277 C  CA    . ILE A 1 155 ? -17.183 0.329   -38.631 1.00 24.59  ? 155 ILE A CA    1 
ATOM   1278 C  C     . ILE A 1 155 ? -18.253 0.740   -39.635 1.00 24.34  ? 155 ILE A C     1 
ATOM   1279 O  O     . ILE A 1 155 ? -18.539 0.008   -40.590 1.00 23.03  ? 155 ILE A O     1 
ATOM   1280 C  CB    . ILE A 1 155 ? -15.832 0.164   -39.332 1.00 27.45  ? 155 ILE A CB    1 
ATOM   1281 C  CG1   . ILE A 1 155 ? -14.723 -0.292  -38.385 1.00 28.29  ? 155 ILE A CG1   1 
ATOM   1282 C  CG2   . ILE A 1 155 ? -15.480 1.486   -39.983 1.00 28.27  ? 155 ILE A CG2   1 
ATOM   1283 C  CD1   . ILE A 1 155 ? -13.649 -1.046  -39.080 1.00 31.33  ? 155 ILE A CD1   1 
ATOM   1284 N  N     . MET A 1 156 ? -18.815 1.930   -39.407 1.00 22.77  ? 156 MET A N     1 
ATOM   1285 C  CA    . MET A 1 156 ? -19.879 2.413   -40.245 1.00 23.68  ? 156 MET A CA    1 
ATOM   1286 C  C     . MET A 1 156 ? -19.266 2.922   -41.557 1.00 24.77  ? 156 MET A C     1 
ATOM   1287 O  O     . MET A 1 156 ? -18.398 3.793   -41.567 1.00 24.76  ? 156 MET A O     1 
ATOM   1288 C  CB    . MET A 1 156 ? -20.692 3.485   -39.523 1.00 23.54  ? 156 MET A CB    1 
ATOM   1289 C  CG    . MET A 1 156 ? -21.152 3.070   -38.131 1.00 23.26  ? 156 MET A CG    1 
ATOM   1290 S  SD    . MET A 1 156 ? -22.051 1.505   -38.034 1.00 26.52  ? 156 MET A SD    1 
ATOM   1291 C  CE    . MET A 1 156 ? -23.363 1.695   -39.230 1.00 26.26  ? 156 MET A CE    1 
ATOM   1292 N  N     . HIS A 1 157 ? -19.703 2.304   -42.662 1.00 25.29  ? 157 HIS A N     1 
ATOM   1293 C  CA    . HIS A 1 157 ? -19.157 2.591   -43.970 1.00 29.18  ? 157 HIS A CA    1 
ATOM   1294 C  C     . HIS A 1 157 ? -20.294 2.427   -44.961 1.00 27.61  ? 157 HIS A C     1 
ATOM   1295 O  O     . HIS A 1 157 ? -21.008 1.419   -44.942 1.00 26.90  ? 157 HIS A O     1 
ATOM   1296 C  CB    . HIS A 1 157 ? -17.948 1.687   -44.267 1.00 33.16  ? 157 HIS A CB    1 
ATOM   1297 C  CG    . HIS A 1 157 ? -17.036 2.307   -45.258 1.00 43.66  ? 157 HIS A CG    1 
ATOM   1298 N  ND1   . HIS A 1 157 ? -17.444 2.622   -46.547 1.00 57.78  ? 157 HIS A ND1   1 
ATOM   1299 C  CD2   . HIS A 1 157 ? -15.785 2.736   -45.144 1.00 47.60  ? 157 HIS A CD2   1 
ATOM   1300 C  CE1   . HIS A 1 157 ? -16.448 3.196   -47.204 1.00 55.21  ? 157 HIS A CE1   1 
ATOM   1301 N  NE2   . HIS A 1 157 ? -15.438 3.297   -46.358 1.00 59.29  ? 157 HIS A NE2   1 
ATOM   1302 N  N     . GLU A 1 158 ? -20.437 3.411   -45.844 1.00 28.51  ? 158 GLU A N     1 
ATOM   1303 C  CA    . GLU A 1 158 ? -21.482 3.357   -46.852 1.00 30.33  ? 158 GLU A CA    1 
ATOM   1304 C  C     . GLU A 1 158 ? -21.356 2.109   -47.736 1.00 30.29  ? 158 GLU A C     1 
ATOM   1305 O  O     . GLU A 1 158 ? -22.354 1.559   -48.191 1.00 30.39  ? 158 GLU A O     1 
ATOM   1306 C  CB    . GLU A 1 158 ? -21.412 4.578   -47.740 1.00 32.84  ? 158 GLU A CB    1 
ATOM   1307 C  CG    . GLU A 1 158 ? -22.586 4.634   -48.688 1.00 38.97  ? 158 GLU A CG    1 
ATOM   1308 C  CD    . GLU A 1 158 ? -22.256 5.411   -49.938 1.00 42.45  ? 158 GLU A CD    1 
ATOM   1309 O  OE1   . GLU A 1 158 ? -22.944 5.218   -50.970 1.00 45.47  ? 158 GLU A OE1   1 
ATOM   1310 O  OE2   . GLU A 1 158 ? -21.341 6.248   -49.839 1.00 49.71  ? 158 GLU A OE2   1 
ATOM   1311 N  N     . GLU A 1 159 ? -20.126 1.633   -47.925 1.00 30.50  ? 159 GLU A N     1 
ATOM   1312 C  CA    . GLU A 1 159 ? -19.846 0.495   -48.777 1.00 33.48  ? 159 GLU A CA    1 
ATOM   1313 C  C     . GLU A 1 159 ? -19.743 -0.813  -47.982 1.00 30.33  ? 159 GLU A C     1 
ATOM   1314 O  O     . GLU A 1 159 ? -19.381 -1.832  -48.522 1.00 32.37  ? 159 GLU A O     1 
ATOM   1315 C  CB    . GLU A 1 159 ? -18.600 0.802   -49.621 1.00 38.03  ? 159 GLU A CB    1 
ATOM   1316 C  CG    . GLU A 1 159 ? -18.729 2.088   -50.470 1.00 44.40  ? 159 GLU A CG    1 
ATOM   1317 C  CD    . GLU A 1 159 ? -20.121 2.465   -51.009 1.00 55.71  ? 159 GLU A CD    1 
ATOM   1318 O  OE1   . GLU A 1 159 ? -20.786 1.615   -51.680 1.00 54.84  ? 159 GLU A OE1   1 
ATOM   1319 O  OE2   . GLU A 1 159 ? -20.580 3.618   -50.746 1.00 61.43  ? 159 GLU A OE2   1 
ATOM   1320 N  N     . GLY A 1 160 ? -20.119 -0.857  -46.714 1.00 30.45  ? 160 GLY A N     1 
ATOM   1321 C  CA    . GLY A 1 160 ? -20.088 -2.131  -46.002 1.00 31.64  ? 160 GLY A CA    1 
ATOM   1322 C  C     . GLY A 1 160 ? -21.346 -2.963  -46.212 1.00 32.21  ? 160 GLY A C     1 
ATOM   1323 O  O     . GLY A 1 160 ? -22.197 -2.600  -47.008 1.00 32.10  ? 160 GLY A O     1 
ATOM   1324 N  N     . GLU A 1 161 ? -21.495 -4.037  -45.429 1.00 34.82  ? 161 GLU A N     1 
ATOM   1325 C  CA    . GLU A 1 161 ? -22.674 -4.903  -45.464 1.00 36.98  ? 161 GLU A CA    1 
ATOM   1326 C  C     . GLU A 1 161 ? -23.923 -4.093  -45.132 1.00 34.68  ? 161 GLU A C     1 
ATOM   1327 O  O     . GLU A 1 161 ? -23.952 -3.488  -44.074 1.00 33.66  ? 161 GLU A O     1 
ATOM   1328 C  CB    . GLU A 1 161 ? -22.487 -6.017  -44.430 1.00 42.47  ? 161 GLU A CB    1 
ATOM   1329 C  CG    . GLU A 1 161 ? -23.733 -6.859  -44.185 1.00 48.64  ? 161 GLU A CG    1 
ATOM   1330 C  CD    . GLU A 1 161 ? -23.909 -7.907  -45.261 1.00 55.52  ? 161 GLU A CD    1 
ATOM   1331 O  OE1   . GLU A 1 161 ? -22.933 -8.637  -45.489 1.00 64.42  ? 161 GLU A OE1   1 
ATOM   1332 O  OE2   . GLU A 1 161 ? -24.996 -7.974  -45.882 1.00 64.09  ? 161 GLU A OE2   1 
ATOM   1333 N  N     . LEU A 1 162 ? -24.930 -4.060  -46.025 1.00 35.74  ? 162 LEU A N     1 
ATOM   1334 C  CA    . LEU A 1 162 ? -26.095 -3.212  -45.820 1.00 35.26  ? 162 LEU A CA    1 
ATOM   1335 C  C     . LEU A 1 162 ? -27.016 -3.813  -44.760 1.00 36.90  ? 162 LEU A C     1 
ATOM   1336 O  O     . LEU A 1 162 ? -27.471 -4.945  -44.887 1.00 38.25  ? 162 LEU A O     1 
ATOM   1337 C  CB    . LEU A 1 162 ? -26.862 -2.990  -47.131 1.00 36.45  ? 162 LEU A CB    1 
ATOM   1338 C  CG    . LEU A 1 162 ? -28.159 -2.170  -46.976 1.00 36.62  ? 162 LEU A CG    1 
ATOM   1339 C  CD1   . LEU A 1 162 ? -27.897 -0.674  -46.788 1.00 35.00  ? 162 LEU A CD1   1 
ATOM   1340 C  CD2   . LEU A 1 162 ? -29.104 -2.377  -48.136 1.00 37.92  ? 162 LEU A CD2   1 
ATOM   1341 N  N     . MET A 1 163 ? -27.406 -2.985  -43.793 1.00 38.20  ? 163 MET A N     1 
ATOM   1342 C  CA    . MET A 1 163 ? -28.381 -3.389  -42.794 1.00 41.44  ? 163 MET A CA    1 
ATOM   1343 C  C     . MET A 1 163 ? -29.484 -2.342  -42.616 1.00 43.65  ? 163 MET A C     1 
ATOM   1344 O  O     . MET A 1 163 ? -29.290 -1.126  -42.762 1.00 38.92  ? 163 MET A O     1 
ATOM   1345 C  CB    . MET A 1 163 ? -27.689 -3.692  -41.464 1.00 42.12  ? 163 MET A CB    1 
ATOM   1346 C  CG    . MET A 1 163 ? -26.961 -5.006  -41.563 1.00 45.76  ? 163 MET A CG    1 
ATOM   1347 S  SD    . MET A 1 163 ? -26.358 -5.549  -40.001 1.00 50.97  ? 163 MET A SD    1 
ATOM   1348 C  CE    . MET A 1 163 ? -27.841 -6.226  -39.260 1.00 55.09  ? 163 MET A CE    1 
ATOM   1349 N  N     . ILE A 1 164 ? -30.685 -2.872  -42.346 1.00 45.89  ? 164 ILE A N     1 
ATOM   1350 C  CA    . ILE A 1 164 ? -31.795 -2.068  -41.881 1.00 45.13  ? 164 ILE A CA    1 
ATOM   1351 C  C     . ILE A 1 164 ? -31.400 -1.598  -40.489 1.00 40.64  ? 164 ILE A C     1 
ATOM   1352 O  O     . ILE A 1 164 ? -30.976 -2.401  -39.669 1.00 39.23  ? 164 ILE A O     1 
ATOM   1353 C  CB    . ILE A 1 164 ? -33.101 -2.880  -41.869 1.00 49.50  ? 164 ILE A CB    1 
ATOM   1354 C  CG1   . ILE A 1 164 ? -33.348 -3.584  -43.207 1.00 57.09  ? 164 ILE A CG1   1 
ATOM   1355 C  CG2   . ILE A 1 164 ? -34.282 -2.009  -41.470 1.00 50.27  ? 164 ILE A CG2   1 
ATOM   1356 C  CD1   . ILE A 1 164 ? -33.373 -2.669  -44.404 1.00 59.39  ? 164 ILE A CD1   1 
ATOM   1357 N  N     . PRO A 1 165 ? -31.482 -0.291  -40.188 1.00 35.50  ? 165 PRO A N     1 
ATOM   1358 C  CA    . PRO A 1 165 ? -31.086 0.201   -38.875 1.00 33.19  ? 165 PRO A CA    1 
ATOM   1359 C  C     . PRO A 1 165 ? -31.737 -0.536  -37.708 1.00 36.35  ? 165 PRO A C     1 
ATOM   1360 O  O     . PRO A 1 165 ? -31.051 -0.868  -36.747 1.00 36.97  ? 165 PRO A O     1 
ATOM   1361 C  CB    . PRO A 1 165 ? -31.546 1.664   -38.912 1.00 31.75  ? 165 PRO A CB    1 
ATOM   1362 C  CG    . PRO A 1 165 ? -31.494 2.016   -40.383 1.00 31.94  ? 165 PRO A CG    1 
ATOM   1363 C  CD    . PRO A 1 165 ? -31.981 0.768   -41.078 1.00 33.99  ? 165 PRO A CD    1 
ATOM   1364 N  N     . LYS A 1 166 ? -33.054 -0.782  -37.790 1.00 38.54  ? 166 LYS A N     1 
ATOM   1365 C  CA    . LYS A 1 166 ? -33.739 -1.615  -36.813 1.00 41.96  ? 166 LYS A CA    1 
ATOM   1366 C  C     . LYS A 1 166 ? -32.893 -2.862  -36.538 1.00 37.37  ? 166 LYS A C     1 
ATOM   1367 O  O     . LYS A 1 166 ? -32.608 -3.220  -35.404 1.00 36.46  ? 166 LYS A O     1 
ATOM   1368 C  CB    . LYS A 1 166 ? -35.130 -1.958  -37.359 1.00 49.11  ? 166 LYS A CB    1 
ATOM   1369 C  CG    . LYS A 1 166 ? -35.974 -2.946  -36.560 1.00 60.19  ? 166 LYS A CG    1 
ATOM   1370 C  CD    . LYS A 1 166 ? -37.383 -3.187  -37.165 1.00 69.60  ? 166 LYS A CD    1 
ATOM   1371 C  CE    . LYS A 1 166 ? -38.348 -3.918  -36.239 1.00 79.25  ? 166 LYS A CE    1 
ATOM   1372 N  NZ    . LYS A 1 166 ? -39.781 -3.720  -36.604 1.00 82.28  ? 166 LYS A NZ    1 
ATOM   1373 N  N     . ASN A 1 167 ? -32.490 -3.535  -37.608 1.00 36.27  ? 167 ASN A N     1 
ATOM   1374 C  CA    . ASN A 1 167 ? -31.828 -4.814  -37.507 1.00 35.71  ? 167 ASN A CA    1 
ATOM   1375 C  C     . ASN A 1 167 ? -30.420 -4.628  -36.968 1.00 33.84  ? 167 ASN A C     1 
ATOM   1376 O  O     . ASN A 1 167 ? -29.901 -5.511  -36.311 1.00 32.96  ? 167 ASN A O     1 
ATOM   1377 C  CB    . ASN A 1 167 ? -31.777 -5.495  -38.866 1.00 38.68  ? 167 ASN A CB    1 
ATOM   1378 C  CG    . ASN A 1 167 ? -33.108 -6.057  -39.305 1.00 41.64  ? 167 ASN A CG    1 
ATOM   1379 O  OD1   . ASN A 1 167 ? -34.070 -6.112  -38.547 1.00 43.66  ? 167 ASN A OD1   1 
ATOM   1380 N  ND2   . ASN A 1 167 ? -33.149 -6.527  -40.534 1.00 44.15  ? 167 ASN A ND2   1 
ATOM   1381 N  N     . PHE A 1 168 ? -29.797 -3.475  -37.234 1.00 32.14  ? 168 PHE A N     1 
ATOM   1382 C  CA    . PHE A 1 168 ? -28.462 -3.269  -36.721 1.00 30.58  ? 168 PHE A CA    1 
ATOM   1383 C  C     . PHE A 1 168 ? -28.509 -3.095  -35.214 1.00 31.53  ? 168 PHE A C     1 
ATOM   1384 O  O     . PHE A 1 168 ? -27.628 -3.618  -34.519 1.00 31.34  ? 168 PHE A O     1 
ATOM   1385 C  CB    . PHE A 1 168 ? -27.781 -2.104  -37.404 1.00 28.16  ? 168 PHE A CB    1 
ATOM   1386 C  CG    . PHE A 1 168 ? -26.342 -1.939  -37.024 1.00 26.67  ? 168 PHE A CG    1 
ATOM   1387 C  CD1   . PHE A 1 168 ? -25.486 -3.018  -37.043 1.00 27.68  ? 168 PHE A CD1   1 
ATOM   1388 C  CD2   . PHE A 1 168 ? -25.840 -0.696  -36.664 1.00 24.96  ? 168 PHE A CD2   1 
ATOM   1389 C  CE1   . PHE A 1 168 ? -24.145 -2.856  -36.718 1.00 28.00  ? 168 PHE A CE1   1 
ATOM   1390 C  CE2   . PHE A 1 168 ? -24.502 -0.537  -36.346 1.00 24.49  ? 168 PHE A CE2   1 
ATOM   1391 C  CZ    . PHE A 1 168 ? -23.647 -1.610  -36.393 1.00 25.10  ? 168 PHE A CZ    1 
ATOM   1392 N  N     . GLY A 1 169 ? -29.580 -2.445  -34.728 1.00 31.08  ? 169 GLY A N     1 
ATOM   1393 C  CA    . GLY A 1 169 ? -29.815 -2.300  -33.296 1.00 30.78  ? 169 GLY A CA    1 
ATOM   1394 C  C     . GLY A 1 169 ? -29.961 -3.656  -32.602 1.00 32.80  ? 169 GLY A C     1 
ATOM   1395 O  O     . GLY A 1 169 ? -29.441 -3.872  -31.497 1.00 31.26  ? 169 GLY A O     1 
ATOM   1396 N  N     . LYS A 1 170 ? -30.679 -4.558  -33.278 1.00 34.11  ? 170 LYS A N     1 
ATOM   1397 C  CA    . LYS A 1 170 ? -30.888 -5.888  -32.749 1.00 38.88  ? 170 LYS A CA    1 
ATOM   1398 C  C     . LYS A 1 170 ? -29.539 -6.575  -32.669 1.00 37.33  ? 170 LYS A C     1 
ATOM   1399 O  O     . LYS A 1 170 ? -29.258 -7.295  -31.720 1.00 41.31  ? 170 LYS A O     1 
ATOM   1400 C  CB    . LYS A 1 170 ? -31.876 -6.699  -33.601 1.00 43.52  ? 170 LYS A CB    1 
ATOM   1401 C  CG    . LYS A 1 170 ? -33.308 -6.180  -33.572 1.00 46.68  ? 170 LYS A CG    1 
ATOM   1402 C  CD    . LYS A 1 170 ? -34.348 -7.130  -34.165 1.00 49.51  ? 170 LYS A CD    1 
ATOM   1403 C  CE    . LYS A 1 170 ? -35.738 -6.554  -34.013 1.00 54.89  ? 170 LYS A CE    1 
ATOM   1404 N  NZ    . LYS A 1 170 ? -36.603 -6.805  -35.188 1.00 59.99  ? 170 LYS A NZ    1 
ATOM   1405 N  N     . LEU A 1 171 ? -28.717 -6.352  -33.680 1.00 36.47  ? 171 LEU A N     1 
ATOM   1406 C  CA    . LEU A 1 171 ? -27.435 -7.025  -33.773 1.00 36.29  ? 171 LEU A CA    1 
ATOM   1407 C  C     . LEU A 1 171 ? -26.523 -6.561  -32.644 1.00 32.49  ? 171 LEU A C     1 
ATOM   1408 O  O     . LEU A 1 171 ? -25.915 -7.396  -31.976 1.00 33.45  ? 171 LEU A O     1 
ATOM   1409 C  CB    . LEU A 1 171 ? -26.835 -6.747  -35.154 1.00 38.60  ? 171 LEU A CB    1 
ATOM   1410 C  CG    . LEU A 1 171 ? -25.479 -7.402  -35.443 1.00 41.31  ? 171 LEU A CG    1 
ATOM   1411 C  CD1   . LEU A 1 171 ? -25.507 -8.914  -35.191 1.00 41.21  ? 171 LEU A CD1   1 
ATOM   1412 C  CD2   . LEU A 1 171 ? -25.070 -7.125  -36.883 1.00 41.25  ? 171 LEU A CD2   1 
ATOM   1413 N  N     . LEU A 1 172 ? -26.462 -5.243  -32.423 1.00 29.69  ? 172 LEU A N     1 
ATOM   1414 C  CA    . LEU A 1 172 ? -25.595 -4.679  -31.397 1.00 28.91  ? 172 LEU A CA    1 
ATOM   1415 C  C     . LEU A 1 172 ? -25.998 -5.209  -30.029 1.00 31.19  ? 172 LEU A C     1 
ATOM   1416 O  O     . LEU A 1 172 ? -25.148 -5.321  -29.140 1.00 29.24  ? 172 LEU A O     1 
ATOM   1417 C  CB    . LEU A 1 172 ? -25.706 -3.160  -31.360 1.00 26.54  ? 172 LEU A CB    1 
ATOM   1418 C  CG    . LEU A 1 172 ? -25.144 -2.385  -32.543 1.00 25.98  ? 172 LEU A CG    1 
ATOM   1419 C  CD1   . LEU A 1 172 ? -25.691 -0.967  -32.529 1.00 25.47  ? 172 LEU A CD1   1 
ATOM   1420 C  CD2   . LEU A 1 172 ? -23.624 -2.358  -32.512 1.00 25.73  ? 172 LEU A CD2   1 
ATOM   1421 N  N     . ASP A 1 173 ? -27.308 -5.494  -29.869 1.00 32.97  ? 173 ASP A N     1 
ATOM   1422 C  CA    . ASP A 1 173 ? -27.829 -5.909  -28.578 1.00 35.80  ? 173 ASP A CA    1 
ATOM   1423 C  C     . ASP A 1 173 ? -27.480 -7.360  -28.275 1.00 37.03  ? 173 ASP A C     1 
ATOM   1424 O  O     . ASP A 1 173 ? -27.789 -7.855  -27.202 1.00 38.83  ? 173 ASP A O     1 
ATOM   1425 C  CB    . ASP A 1 173 ? -29.342 -5.735  -28.481 1.00 39.84  ? 173 ASP A CB    1 
ATOM   1426 C  CG    . ASP A 1 173 ? -29.834 -5.990  -27.074 1.00 42.82  ? 173 ASP A CG    1 
ATOM   1427 O  OD1   . ASP A 1 173 ? -29.258 -5.393  -26.146 1.00 47.95  ? 173 ASP A OD1   1 
ATOM   1428 O  OD2   . ASP A 1 173 ? -30.729 -6.821  -26.912 1.00 45.50  ? 173 ASP A OD2   1 
ATOM   1429 N  N     . LYS A 1 174 ? -26.802 -8.033  -29.200 1.00 38.08  ? 174 LYS A N     1 
ATOM   1430 C  CA    . LYS A 1 174 ? -26.351 -9.383  -28.952 1.00 39.22  ? 174 LYS A CA    1 
ATOM   1431 C  C     . LYS A 1 174 ? -24.976 -9.378  -28.309 1.00 36.92  ? 174 LYS A C     1 
ATOM   1432 O  O     . LYS A 1 174 ? -24.560 -10.419 -27.864 1.00 39.49  ? 174 LYS A O     1 
ATOM   1433 C  CB    . LYS A 1 174 ? -26.296 -10.192 -30.250 1.00 42.70  ? 174 LYS A CB    1 
ATOM   1434 C  CG    . LYS A 1 174 ? -27.651 -10.510 -30.867 1.00 44.44  ? 174 LYS A CG    1 
ATOM   1435 C  CD    . LYS A 1 174 ? -27.543 -10.971 -32.305 1.00 48.70  ? 174 LYS A CD    1 
ATOM   1436 C  CE    . LYS A 1 174 ? -28.783 -10.711 -33.142 1.00 52.30  ? 174 LYS A CE    1 
ATOM   1437 N  NZ    . LYS A 1 174 ? -29.886 -11.643 -32.813 1.00 53.52  ? 174 LYS A NZ    1 
ATOM   1438 N  N     . PHE A 1 175 ? -24.281 -8.243  -28.219 1.00 34.75  ? 175 PHE A N     1 
ATOM   1439 C  CA    . PHE A 1 175 ? -22.931 -8.254  -27.662 1.00 35.53  ? 175 PHE A CA    1 
ATOM   1440 C  C     . PHE A 1 175 ? -22.931 -7.554  -26.299 1.00 36.36  ? 175 PHE A C     1 
ATOM   1441 O  O     . PHE A 1 175 ? -23.917 -6.918  -25.932 1.00 38.68  ? 175 PHE A O     1 
ATOM   1442 C  CB    . PHE A 1 175 ? -21.973 -7.650  -28.694 1.00 34.65  ? 175 PHE A CB    1 
ATOM   1443 C  CG    . PHE A 1 175 ? -21.908 -8.410  -30.001 1.00 34.74  ? 175 PHE A CG    1 
ATOM   1444 C  CD1   . PHE A 1 175 ? -21.144 -9.567  -30.119 1.00 35.77  ? 175 PHE A CD1   1 
ATOM   1445 C  CD2   . PHE A 1 175 ? -22.676 -8.018  -31.091 1.00 32.95  ? 175 PHE A CD2   1 
ATOM   1446 C  CE1   . PHE A 1 175 ? -21.118 -10.281 -31.313 1.00 36.40  ? 175 PHE A CE1   1 
ATOM   1447 C  CE2   . PHE A 1 175 ? -22.649 -8.729  -32.281 1.00 34.36  ? 175 PHE A CE2   1 
ATOM   1448 C  CZ    . PHE A 1 175 ? -21.859 -9.852  -32.401 1.00 35.94  ? 175 PHE A CZ    1 
ATOM   1449 N  N     . LYS A 1 176 ? -21.855 -7.697  -25.523 1.00 37.49  ? 176 LYS A N     1 
ATOM   1450 C  CA    . LYS A 1 176 ? -21.799 -7.090  -24.196 1.00 43.22  ? 176 LYS A CA    1 
ATOM   1451 C  C     . LYS A 1 176 ? -21.251 -5.670  -24.246 1.00 40.65  ? 176 LYS A C     1 
ATOM   1452 O  O     . LYS A 1 176 ? -21.659 -4.801  -23.472 1.00 41.66  ? 176 LYS A O     1 
ATOM   1453 C  CB    . LYS A 1 176 ? -20.933 -7.908  -23.240 1.00 50.10  ? 176 LYS A CB    1 
ATOM   1454 C  CG    . LYS A 1 176 ? -21.526 -9.270  -22.878 1.00 58.97  ? 176 LYS A CG    1 
ATOM   1455 C  CD    . LYS A 1 176 ? -20.464 -10.325 -22.599 1.00 66.63  ? 176 LYS A CD    1 
ATOM   1456 C  CE    . LYS A 1 176 ? -20.841 -11.706 -23.101 1.00 75.61  ? 176 LYS A CE    1 
ATOM   1457 N  NZ    . LYS A 1 176 ? -21.952 -12.301 -22.316 1.00 80.98  ? 176 LYS A NZ    1 
ATOM   1458 N  N     . LYS A 1 177 ? -20.338 -5.435  -25.181 1.00 39.70  ? 177 LYS A N     1 
ATOM   1459 C  CA    . LYS A 1 177 ? -19.508 -4.246  -25.149 1.00 37.49  ? 177 LYS A CA    1 
ATOM   1460 C  C     . LYS A 1 177 ? -19.193 -3.896  -26.600 1.00 32.19  ? 177 LYS A C     1 
ATOM   1461 O  O     . LYS A 1 177 ? -18.032 -3.871  -26.993 1.00 29.98  ? 177 LYS A O     1 
ATOM   1462 C  CB    . LYS A 1 177 ? -18.278 -4.546  -24.273 1.00 40.20  ? 177 LYS A CB    1 
ATOM   1463 C  CG    . LYS A 1 177 ? -17.563 -3.313  -23.740 1.00 44.31  ? 177 LYS A CG    1 
ATOM   1464 C  CD    . LYS A 1 177 ? -16.365 -3.522  -22.765 1.00 46.07  ? 177 LYS A CD    1 
ATOM   1465 C  CE    . LYS A 1 177 ? -15.896 -2.144  -22.309 1.00 48.79  ? 177 LYS A CE    1 
ATOM   1466 N  NZ    . LYS A 1 177 ? -14.926 -2.107  -21.185 1.00 46.97  ? 177 LYS A NZ    1 
ATOM   1467 N  N     . PRO A 1 178 ? -20.224 -3.681  -27.449 1.00 28.80  ? 178 PRO A N     1 
ATOM   1468 C  CA    . PRO A 1 178 ? -20.016 -3.395  -28.867 1.00 27.37  ? 178 PRO A CA    1 
ATOM   1469 C  C     . PRO A 1 178 ? -19.450 -1.994  -29.043 1.00 27.42  ? 178 PRO A C     1 
ATOM   1470 O  O     . PRO A 1 178 ? -19.810 -1.065  -28.311 1.00 29.02  ? 178 PRO A O     1 
ATOM   1471 C  CB    . PRO A 1 178 ? -21.406 -3.452  -29.480 1.00 28.00  ? 178 PRO A CB    1 
ATOM   1472 C  CG    . PRO A 1 178 ? -22.327 -3.072  -28.311 1.00 28.26  ? 178 PRO A CG    1 
ATOM   1473 C  CD    . PRO A 1 178 ? -21.645 -3.665  -27.090 1.00 29.37  ? 178 PRO A CD    1 
ATOM   1474 N  N     . THR A 1 179 ? -18.549 -1.869  -30.017 1.00 25.13  ? 179 THR A N     1 
ATOM   1475 C  CA    . THR A 1 179 ? -17.922 -0.602  -30.326 1.00 24.10  ? 179 THR A CA    1 
ATOM   1476 C  C     . THR A 1 179 ? -18.361 -0.247  -31.726 1.00 23.31  ? 179 THR A C     1 
ATOM   1477 O  O     . THR A 1 179 ? -18.374 -1.117  -32.575 1.00 24.48  ? 179 THR A O     1 
ATOM   1478 C  CB    . THR A 1 179 ? -16.396 -0.699  -30.171 1.00 23.67  ? 179 THR A CB    1 
ATOM   1479 O  OG1   . THR A 1 179 ? -16.158 -0.735  -28.758 1.00 24.06  ? 179 THR A OG1   1 
ATOM   1480 C  CG2   . THR A 1 179 ? -15.670 0.447   -30.828 1.00 21.14  ? 179 THR A CG2   1 
ATOM   1481 N  N     . VAL A 1 180 ? -18.780 1.001   -31.927 1.00 22.51  ? 180 VAL A N     1 
ATOM   1482 C  CA    . VAL A 1 180 ? -19.181 1.420   -33.248 1.00 22.26  ? 180 VAL A CA    1 
ATOM   1483 C  C     . VAL A 1 180 ? -18.363 2.650   -33.568 1.00 22.34  ? 180 VAL A C     1 
ATOM   1484 O  O     . VAL A 1 180 ? -18.278 3.529   -32.716 1.00 21.81  ? 180 VAL A O     1 
ATOM   1485 C  CB    . VAL A 1 180 ? -20.690 1.718   -33.319 1.00 22.83  ? 180 VAL A CB    1 
ATOM   1486 C  CG1   . VAL A 1 180 ? -21.069 2.329   -34.641 1.00 21.94  ? 180 VAL A CG1   1 
ATOM   1487 C  CG2   . VAL A 1 180 ? -21.553 0.480   -33.044 1.00 25.17  ? 180 VAL A CG2   1 
ATOM   1488 N  N     . ILE A 1 181 ? -17.820 2.699   -34.793 1.00 22.18  ? 181 ILE A N     1 
ATOM   1489 C  CA    . ILE A 1 181 ? -16.912 3.761   -35.212 1.00 22.13  ? 181 ILE A CA    1 
ATOM   1490 C  C     . ILE A 1 181 ? -17.542 4.495   -36.404 1.00 20.81  ? 181 ILE A C     1 
ATOM   1491 O  O     . ILE A 1 181 ? -17.891 3.872   -37.400 1.00 18.48  ? 181 ILE A O     1 
ATOM   1492 C  CB    . ILE A 1 181 ? -15.517 3.188   -35.562 1.00 23.06  ? 181 ILE A CB    1 
ATOM   1493 C  CG1   . ILE A 1 181 ? -14.823 2.554   -34.364 1.00 25.21  ? 181 ILE A CG1   1 
ATOM   1494 C  CG2   . ILE A 1 181 ? -14.584 4.223   -36.163 1.00 24.48  ? 181 ILE A CG2   1 
ATOM   1495 C  CD1   . ILE A 1 181 ? -13.775 1.539   -34.766 1.00 26.52  ? 181 ILE A CD1   1 
ATOM   1496 N  N     . VAL A 1 182 ? -17.655 5.826   -36.276 1.00 19.31  ? 182 VAL A N     1 
ATOM   1497 C  CA    . VAL A 1 182 ? -18.162 6.703   -37.308 1.00 19.40  ? 182 VAL A CA    1 
ATOM   1498 C  C     . VAL A 1 182 ? -17.105 7.738   -37.651 1.00 19.95  ? 182 VAL A C     1 
ATOM   1499 O  O     . VAL A 1 182 ? -16.527 8.320   -36.740 1.00 22.04  ? 182 VAL A O     1 
ATOM   1500 C  CB    . VAL A 1 182 ? -19.415 7.409   -36.807 1.00 20.06  ? 182 VAL A CB    1 
ATOM   1501 C  CG1   . VAL A 1 182 ? -19.976 8.282   -37.908 1.00 21.41  ? 182 VAL A CG1   1 
ATOM   1502 C  CG2   . VAL A 1 182 ? -20.425 6.399   -36.304 1.00 20.01  ? 182 VAL A CG2   1 
ATOM   1503 N  N     . GLY A 1 183 ? -16.872 7.978   -38.949 1.00 20.15  ? 183 GLY A N     1 
ATOM   1504 C  CA    . GLY A 1 183 ? -15.879 8.953   -39.354 1.00 21.23  ? 183 GLY A CA    1 
ATOM   1505 C  C     . GLY A 1 183 ? -16.337 10.387  -39.047 1.00 23.01  ? 183 GLY A C     1 
ATOM   1506 O  O     . GLY A 1 183 ? -17.481 10.772  -39.350 1.00 21.25  ? 183 GLY A O     1 
ATOM   1507 N  N     . GLY A 1 184 ? -15.429 11.189  -38.464 1.00 24.38  ? 184 GLY A N     1 
ATOM   1508 C  CA    . GLY A 1 184 ? -15.730 12.583  -38.129 1.00 25.23  ? 184 GLY A CA    1 
ATOM   1509 C  C     . GLY A 1 184 ? -15.237 13.550  -39.198 1.00 26.16  ? 184 GLY A C     1 
ATOM   1510 O  O     . GLY A 1 184 ? -14.663 14.578  -38.906 1.00 29.92  ? 184 GLY A O     1 
ATOM   1511 N  N     . PHE A 1 185 ? -15.385 13.159  -40.455 1.00 35.00  ? 185 PHE A N     1 
ATOM   1512 C  CA    . PHE A 1 185 ? -14.869 13.906  -41.592 1.00 34.61  ? 185 PHE A CA    1 
ATOM   1513 C  C     . PHE A 1 185 ? -15.999 14.036  -42.615 1.00 35.35  ? 185 PHE A C     1 
ATOM   1514 O  O     . PHE A 1 185 ? -16.922 13.226  -42.643 1.00 37.37  ? 185 PHE A O     1 
ATOM   1515 C  CB    . PHE A 1 185 ? -13.602 13.234  -42.137 1.00 34.21  ? 185 PHE A CB    1 
ATOM   1516 C  CG    . PHE A 1 185 ? -13.683 11.739  -42.318 1.00 31.92  ? 185 PHE A CG    1 
ATOM   1517 C  CD1   . PHE A 1 185 ? -13.259 10.890  -41.314 1.00 31.74  ? 185 PHE A CD1   1 
ATOM   1518 C  CD2   . PHE A 1 185 ? -14.114 11.187  -43.514 1.00 30.35  ? 185 PHE A CD2   1 
ATOM   1519 C  CE1   . PHE A 1 185 ? -13.311 9.517   -41.481 1.00 30.17  ? 185 PHE A CE1   1 
ATOM   1520 C  CE2   . PHE A 1 185 ? -14.197 9.816   -43.663 1.00 30.26  ? 185 PHE A CE2   1 
ATOM   1521 C  CZ    . PHE A 1 185 ? -13.794 8.985   -42.650 1.00 28.59  ? 185 PHE A CZ    1 
ATOM   1522 N  N     . PRO A 1 186 ? -16.005 15.096  -43.440 1.00 34.34  ? 186 PRO A N     1 
ATOM   1523 C  CA    . PRO A 1 186 ? -17.165 15.385  -44.274 1.00 35.97  ? 186 PRO A CA    1 
ATOM   1524 C  C     . PRO A 1 186 ? -17.308 14.440  -45.473 1.00 37.71  ? 186 PRO A C     1 
ATOM   1525 O  O     . PRO A 1 186 ? -18.415 14.203  -45.929 1.00 41.51  ? 186 PRO A O     1 
ATOM   1526 C  CB    . PRO A 1 186 ? -16.887 16.831  -44.699 1.00 35.46  ? 186 PRO A CB    1 
ATOM   1527 C  CG    . PRO A 1 186 ? -15.382 16.893  -44.789 1.00 36.38  ? 186 PRO A CG    1 
ATOM   1528 C  CD    . PRO A 1 186 ? -14.908 16.058  -43.618 1.00 34.62  ? 186 PRO A CD    1 
ATOM   1529 N  N     . HIS A 1 187 ? -16.198 13.919  -46.001 1.00 39.87  ? 187 HIS A N     1 
ATOM   1530 C  CA    . HIS A 1 187 ? -16.237 13.000  -47.132 1.00 42.52  ? 187 HIS A CA    1 
ATOM   1531 C  C     . HIS A 1 187 ? -14.922 12.240  -47.221 1.00 45.05  ? 187 HIS A C     1 
ATOM   1532 O  O     . HIS A 1 187 ? -13.914 12.633  -46.611 1.00 47.37  ? 187 HIS A O     1 
ATOM   1533 C  CB    . HIS A 1 187 ? -16.486 13.734  -48.450 1.00 44.00  ? 187 HIS A CB    1 
ATOM   1534 C  CG    . HIS A 1 187 ? -15.604 14.922  -48.590 1.00 50.93  ? 187 HIS A CG    1 
ATOM   1535 N  ND1   . HIS A 1 187 ? -14.226 14.841  -48.649 1.00 56.44  ? 187 HIS A ND1   1 
ATOM   1536 C  CD2   . HIS A 1 187 ? -15.912 16.234  -48.659 1.00 55.72  ? 187 HIS A CD2   1 
ATOM   1537 C  CE1   . HIS A 1 187 ? -13.722 16.062  -48.768 1.00 58.59  ? 187 HIS A CE1   1 
ATOM   1538 N  NE2   . HIS A 1 187 ? -14.727 16.930  -48.775 1.00 59.16  ? 187 HIS A NE2   1 
ATOM   1539 N  N     . GLY A 1 188 ? -14.973 11.166  -48.014 1.00 46.12  ? 188 GLY A N     1 
ATOM   1540 C  CA    . GLY A 1 188 ? -13.843 10.282  -48.233 1.00 47.64  ? 188 GLY A CA    1 
ATOM   1541 C  C     . GLY A 1 188 ? -13.852 9.101   -47.268 1.00 48.07  ? 188 GLY A C     1 
ATOM   1542 O  O     . GLY A 1 188 ? -14.890 8.768   -46.684 1.00 50.49  ? 188 GLY A O     1 
ATOM   1543 N  N     . ASP A 1 189 ? -12.673 8.486   -47.094 1.00 49.84  ? 189 ASP A N     1 
ATOM   1544 C  CA    . ASP A 1 189 ? -12.571 7.234   -46.363 1.00 49.07  ? 189 ASP A CA    1 
ATOM   1545 C  C     . ASP A 1 189 ? -11.829 7.465   -45.061 1.00 40.41  ? 189 ASP A C     1 
ATOM   1546 O  O     . ASP A 1 189 ? -11.213 8.501   -44.859 1.00 36.56  ? 189 ASP A O     1 
ATOM   1547 C  CB    . ASP A 1 189 ? -11.864 6.159   -47.184 1.00 57.68  ? 189 ASP A CB    1 
ATOM   1548 C  CG    . ASP A 1 189 ? -12.696 5.692   -48.364 1.00 70.95  ? 189 ASP A CG    1 
ATOM   1549 O  OD1   . ASP A 1 189 ? -13.821 5.182   -48.105 1.00 83.38  ? 189 ASP A OD1   1 
ATOM   1550 O  OD2   . ASP A 1 189 ? -12.218 5.841   -49.526 1.00 67.95  ? 189 ASP A OD2   1 
ATOM   1551 N  N     . PHE A 1 190 ? -11.885 6.457   -44.200 1.00 37.34  ? 190 PHE A N     1 
ATOM   1552 C  CA    . PHE A 1 190 ? -11.076 6.429   -43.002 1.00 35.75  ? 190 PHE A CA    1 
ATOM   1553 C  C     . PHE A 1 190 ? -9.599  6.511   -43.386 1.00 36.75  ? 190 PHE A C     1 
ATOM   1554 O  O     . PHE A 1 190 ? -9.183  6.015   -44.431 1.00 42.50  ? 190 PHE A O     1 
ATOM   1555 C  CB    . PHE A 1 190 ? -11.393 5.157   -42.218 1.00 31.83  ? 190 PHE A CB    1 
ATOM   1556 C  CG    . PHE A 1 190 ? -12.713 5.187   -41.502 1.00 29.18  ? 190 PHE A CG    1 
ATOM   1557 C  CD1   . PHE A 1 190 ? -12.837 5.821   -40.283 1.00 26.85  ? 190 PHE A CD1   1 
ATOM   1558 C  CD2   . PHE A 1 190 ? -13.833 4.593   -42.051 1.00 30.92  ? 190 PHE A CD2   1 
ATOM   1559 C  CE1   . PHE A 1 190 ? -14.044 5.819   -39.602 1.00 27.16  ? 190 PHE A CE1   1 
ATOM   1560 C  CE2   . PHE A 1 190 ? -15.059 4.658   -41.407 1.00 31.12  ? 190 PHE A CE2   1 
ATOM   1561 C  CZ    . PHE A 1 190 ? -15.155 5.240   -40.160 1.00 28.70  ? 190 PHE A CZ    1 
ATOM   1562 N  N     . LYS A 1 191 ? -8.825  7.163   -42.531 1.00 37.28  ? 191 LYS A N     1 
ATOM   1563 C  CA    . LYS A 1 191 ? -7.375  7.110   -42.599 1.00 41.95  ? 191 LYS A CA    1 
ATOM   1564 C  C     . LYS A 1 191 ? -6.901  5.911   -41.770 1.00 42.32  ? 191 LYS A C     1 
ATOM   1565 O  O     . LYS A 1 191 ? -6.053  5.152   -42.230 1.00 46.26  ? 191 LYS A O     1 
ATOM   1566 C  CB    . LYS A 1 191 ? -6.841  8.486   -42.184 1.00 46.29  ? 191 LYS A CB    1 
ATOM   1567 C  CG    . LYS A 1 191 ? -5.579  8.503   -41.338 1.00 55.92  ? 191 LYS A CG    1 
ATOM   1568 C  CD    . LYS A 1 191 ? -4.290  8.577   -42.115 1.00 62.92  ? 191 LYS A CD    1 
ATOM   1569 C  CE    . LYS A 1 191 ? -3.105  8.397   -41.193 1.00 66.20  ? 191 LYS A CE    1 
ATOM   1570 N  NZ    . LYS A 1 191 ? -1.858  8.865   -41.826 1.00 71.71  ? 191 LYS A NZ    1 
ATOM   1571 N  N     . SER A 1 192 ? -7.496  5.713   -40.576 1.00 40.39  ? 192 SER A N     1 
ATOM   1572 C  CA    . SER A 1 192 ? -7.097  4.679   -39.630 1.00 39.62  ? 192 SER A CA    1 
ATOM   1573 C  C     . SER A 1 192 ? -7.800  3.363   -39.947 1.00 42.93  ? 192 SER A C     1 
ATOM   1574 O  O     . SER A 1 192 ? -8.934  3.176   -39.516 1.00 52.83  ? 192 SER A O     1 
ATOM   1575 C  CB    . SER A 1 192 ? -7.397  5.092   -38.205 1.00 35.28  ? 192 SER A CB    1 
ATOM   1576 O  OG    . SER A 1 192 ? -6.825  6.348   -37.918 1.00 34.21  ? 192 SER A OG    1 
ATOM   1577 N  N     . LYS A 1 193 ? -7.127  2.458   -40.671 1.00 44.52  ? 193 LYS A N     1 
ATOM   1578 C  CA    . LYS A 1 193 ? -7.658  1.125   -40.945 1.00 49.55  ? 193 LYS A CA    1 
ATOM   1579 C  C     . LYS A 1 193 ? -7.467  0.235   -39.720 1.00 44.27  ? 193 LYS A C     1 
ATOM   1580 O  O     . LYS A 1 193 ? -6.332  -0.007  -39.313 1.00 47.97  ? 193 LYS A O     1 
ATOM   1581 C  CB    . LYS A 1 193 ? -6.945  0.481   -42.141 1.00 56.68  ? 193 LYS A CB    1 
ATOM   1582 C  CG    . LYS A 1 193 ? -7.136  1.202   -43.467 1.00 65.87  ? 193 LYS A CG    1 
ATOM   1583 C  CD    . LYS A 1 193 ? -8.600  1.482   -43.816 1.00 71.93  ? 193 LYS A CD    1 
ATOM   1584 C  CE    . LYS A 1 193 ? -8.833  1.867   -45.268 1.00 77.58  ? 193 LYS A CE    1 
ATOM   1585 N  NZ    . LYS A 1 193 ? -8.479  3.281   -45.549 1.00 74.90  ? 193 LYS A NZ    1 
ATOM   1586 N  N     . VAL A 1 194 ? -8.572  -0.214  -39.118 1.00 37.94  ? 194 VAL A N     1 
ATOM   1587 C  CA    . VAL A 1 194 ? -8.529  -1.166  -38.012 1.00 35.41  ? 194 VAL A CA    1 
ATOM   1588 C  C     . VAL A 1 194 ? -9.478  -2.315  -38.323 1.00 34.44  ? 194 VAL A C     1 
ATOM   1589 O  O     . VAL A 1 194 ? -10.294 -2.240  -39.254 1.00 32.66  ? 194 VAL A O     1 
ATOM   1590 C  CB    . VAL A 1 194 ? -8.883  -0.538  -36.647 1.00 35.36  ? 194 VAL A CB    1 
ATOM   1591 C  CG1   . VAL A 1 194 ? -7.868  0.529   -36.230 1.00 32.81  ? 194 VAL A CG1   1 
ATOM   1592 C  CG2   . VAL A 1 194 ? -10.317 -0.001  -36.602 1.00 34.76  ? 194 VAL A CG2   1 
ATOM   1593 N  N     . ASP A 1 195 ? -9.336  -3.392  -37.538 1.00 37.33  ? 195 ASP A N     1 
ATOM   1594 C  CA    . ASP A 1 195 ? -10.125 -4.606  -37.733 1.00 35.23  ? 195 ASP A CA    1 
ATOM   1595 C  C     . ASP A 1 195 ? -11.549 -4.353  -37.265 1.00 34.69  ? 195 ASP A C     1 
ATOM   1596 O  O     . ASP A 1 195 ? -11.740 -3.807  -36.179 1.00 40.97  ? 195 ASP A O     1 
ATOM   1597 C  CB    . ASP A 1 195 ? -9.594  -5.804  -36.938 1.00 35.43  ? 195 ASP A CB    1 
ATOM   1598 C  CG    . ASP A 1 195 ? -8.430  -6.545  -37.571 1.00 36.12  ? 195 ASP A CG    1 
ATOM   1599 O  OD1   . ASP A 1 195 ? -7.803  -5.993  -38.479 1.00 35.93  ? 195 ASP A OD1   1 
ATOM   1600 O  OD2   . ASP A 1 195 ? -8.165  -7.675  -37.139 1.00 39.35  ? 195 ASP A OD2   1 
ATOM   1601 N  N     . GLY A 1 196 ? -12.522 -4.762  -38.088 1.00 33.02  ? 196 GLY A N     1 
ATOM   1602 C  CA    . GLY A 1 196 ? -13.920 -4.663  -37.722 1.00 31.86  ? 196 GLY A CA    1 
ATOM   1603 C  C     . GLY A 1 196 ? -14.864 -4.917  -38.899 1.00 31.06  ? 196 GLY A C     1 
ATOM   1604 O  O     . GLY A 1 196 ? -14.460 -4.955  -40.054 1.00 29.81  ? 196 GLY A O     1 
ATOM   1605 N  N     . VAL A 1 197 ? -16.148 -5.022  -38.580 1.00 29.82  ? 197 VAL A N     1 
ATOM   1606 C  CA    . VAL A 1 197 ? -17.164 -5.263  -39.575 1.00 31.58  ? 197 VAL A CA    1 
ATOM   1607 C  C     . VAL A 1 197 ? -17.713 -3.935  -40.080 1.00 29.33  ? 197 VAL A C     1 
ATOM   1608 O  O     . VAL A 1 197 ? -18.250 -3.130  -39.322 1.00 27.90  ? 197 VAL A O     1 
ATOM   1609 C  CB    . VAL A 1 197 ? -18.265 -6.142  -38.969 1.00 35.19  ? 197 VAL A CB    1 
ATOM   1610 C  CG1   . VAL A 1 197 ? -19.266 -6.576  -40.029 1.00 35.87  ? 197 VAL A CG1   1 
ATOM   1611 C  CG2   . VAL A 1 197 ? -17.649 -7.338  -38.244 1.00 37.62  ? 197 VAL A CG2   1 
ATOM   1612 N  N     . LYS A 1 198 ? -17.628 -3.776  -41.394 1.00 30.29  ? 198 LYS A N     1 
ATOM   1613 C  CA    . LYS A 1 198 ? -18.125 -2.609  -42.097 1.00 31.57  ? 198 LYS A CA    1 
ATOM   1614 C  C     . LYS A 1 198 ? -19.622 -2.718  -42.306 1.00 29.91  ? 198 LYS A C     1 
ATOM   1615 O  O     . LYS A 1 198 ? -20.057 -3.648  -42.952 1.00 31.83  ? 198 LYS A O     1 
ATOM   1616 C  CB    . LYS A 1 198 ? -17.415 -2.464  -43.447 1.00 35.28  ? 198 LYS A CB    1 
ATOM   1617 C  CG    . LYS A 1 198 ? -15.933 -2.163  -43.281 1.00 39.08  ? 198 LYS A CG    1 
ATOM   1618 C  CD    . LYS A 1 198 ? -15.245 -1.821  -44.545 1.00 45.91  ? 198 LYS A CD    1 
ATOM   1619 C  CE    . LYS A 1 198 ? -13.765 -1.573  -44.335 1.00 52.45  ? 198 LYS A CE    1 
ATOM   1620 N  NZ    . LYS A 1 198 ? -13.040 -1.571  -45.631 1.00 58.22  ? 198 LYS A NZ    1 
ATOM   1621 N  N     . ILE A 1 199 ? -20.374 -1.719  -41.824 1.00 28.75  ? 199 ILE A N     1 
ATOM   1622 C  CA    . ILE A 1 199 ? -21.827 -1.717  -41.920 1.00 29.21  ? 199 ILE A CA    1 
ATOM   1623 C  C     . ILE A 1 199 ? -22.307 -0.448  -42.620 1.00 27.55  ? 199 ILE A C     1 
ATOM   1624 O  O     . ILE A 1 199 ? -21.981 0.652   -42.209 1.00 24.49  ? 199 ILE A O     1 
ATOM   1625 C  CB    . ILE A 1 199 ? -22.465 -1.816  -40.525 1.00 28.01  ? 199 ILE A CB    1 
ATOM   1626 C  CG1   . ILE A 1 199 ? -21.919 -3.018  -39.739 1.00 29.32  ? 199 ILE A CG1   1 
ATOM   1627 C  CG2   . ILE A 1 199 ? -23.983 -1.808  -40.638 1.00 26.68  ? 199 ILE A CG2   1 
ATOM   1628 C  CD1   . ILE A 1 199 ? -22.425 -4.350  -40.222 1.00 31.61  ? 199 ILE A CD1   1 
ATOM   1629 N  N     . SER A 1 200 ? -23.119 -0.636  -43.661 1.00 29.06  ? 200 SER A N     1 
ATOM   1630 C  CA    . SER A 1 200 ? -23.846 0.440   -44.304 1.00 28.30  ? 200 SER A CA    1 
ATOM   1631 C  C     . SER A 1 200 ? -25.266 0.449   -43.780 1.00 28.74  ? 200 SER A C     1 
ATOM   1632 O  O     . SER A 1 200 ? -25.854 -0.621  -43.625 1.00 28.80  ? 200 SER A O     1 
ATOM   1633 C  CB    . SER A 1 200 ? -23.867 0.224   -45.780 1.00 30.40  ? 200 SER A CB    1 
ATOM   1634 O  OG    . SER A 1 200 ? -24.674 1.207   -46.398 1.00 29.94  ? 200 SER A OG    1 
ATOM   1635 N  N     . LEU A 1 201 ? -25.815 1.643   -43.543 1.00 29.17  ? 201 LEU A N     1 
ATOM   1636 C  CA    . LEU A 1 201 ? -27.206 1.754   -43.136 1.00 28.69  ? 201 LEU A CA    1 
ATOM   1637 C  C     . LEU A 1 201 ? -28.034 2.340   -44.256 1.00 28.55  ? 201 LEU A C     1 
ATOM   1638 O  O     . LEU A 1 201 ? -29.211 2.612   -44.054 1.00 28.58  ? 201 LEU A O     1 
ATOM   1639 C  CB    . LEU A 1 201 ? -27.339 2.649   -41.897 1.00 29.23  ? 201 LEU A CB    1 
ATOM   1640 C  CG    . LEU A 1 201 ? -26.720 2.098   -40.620 1.00 30.09  ? 201 LEU A CG    1 
ATOM   1641 C  CD1   . LEU A 1 201 ? -27.013 3.020   -39.444 1.00 31.52  ? 201 LEU A CD1   1 
ATOM   1642 C  CD2   . LEU A 1 201 ? -27.216 0.701   -40.322 1.00 30.94  ? 201 LEU A CD2   1 
ATOM   1643 N  N     . TYR A 1 202 ? -27.445 2.522   -45.436 1.00 30.36  ? 202 TYR A N     1 
ATOM   1644 C  CA    . TYR A 1 202 ? -28.163 3.174   -46.520 1.00 32.28  ? 202 TYR A CA    1 
ATOM   1645 C  C     . TYR A 1 202 ? -27.218 3.271   -47.692 1.00 35.35  ? 202 TYR A C     1 
ATOM   1646 O  O     . TYR A 1 202 ? -26.009 3.408   -47.530 1.00 34.05  ? 202 TYR A O     1 
ATOM   1647 C  CB    . TYR A 1 202 ? -28.575 4.596   -46.117 1.00 31.57  ? 202 TYR A CB    1 
ATOM   1648 C  CG    . TYR A 1 202 ? -29.583 5.338   -46.978 1.00 31.58  ? 202 TYR A CG    1 
ATOM   1649 C  CD1   . TYR A 1 202 ? -30.887 4.889   -47.085 1.00 32.45  ? 202 TYR A CD1   1 
ATOM   1650 C  CD2   . TYR A 1 202 ? -29.240 6.531   -47.607 1.00 31.16  ? 202 TYR A CD2   1 
ATOM   1651 C  CE1   . TYR A 1 202 ? -31.806 5.574   -47.853 1.00 33.74  ? 202 TYR A CE1   1 
ATOM   1652 C  CE2   . TYR A 1 202 ? -30.154 7.240   -48.359 1.00 31.84  ? 202 TYR A CE2   1 
ATOM   1653 C  CZ    . TYR A 1 202 ? -31.434 6.748   -48.487 1.00 34.36  ? 202 TYR A CZ    1 
ATOM   1654 O  OH    . TYR A 1 202 ? -32.331 7.416   -49.262 1.00 39.39  ? 202 TYR A OH    1 
ATOM   1655 N  N     . ARG A 1 203 ? -27.789 3.231   -48.878 1.00 44.35  ? 203 ARG A N     1 
ATOM   1656 C  CA    . ARG A 1 203 ? -26.957 2.985   -50.027 1.00 51.92  ? 203 ARG A CA    1 
ATOM   1657 C  C     . ARG A 1 203 ? -26.602 4.283   -50.718 1.00 44.89  ? 203 ARG A C     1 
ATOM   1658 O  O     . ARG A 1 203 ? -26.351 4.260   -51.918 1.00 44.98  ? 203 ARG A O     1 
ATOM   1659 C  CB    . ARG A 1 203 ? -27.677 2.060   -51.001 1.00 67.97  ? 203 ARG A CB    1 
ATOM   1660 C  CG    . ARG A 1 203 ? -26.797 1.624   -52.167 1.00 83.43  ? 203 ARG A CG    1 
ATOM   1661 C  CD    . ARG A 1 203 ? -25.322 1.429   -51.842 1.00 86.44  ? 203 ARG A CD    1 
ATOM   1662 N  NE    . ARG A 1 203 ? -24.436 2.498   -52.277 1.00 91.95  ? 203 ARG A NE    1 
ATOM   1663 C  CZ    . ARG A 1 203 ? -23.436 2.328   -53.133 1.00 86.50  ? 203 ARG A CZ    1 
ATOM   1664 N  NH1   . ARG A 1 203 ? -22.518 3.272   -53.268 1.00 93.17  ? 203 ARG A NH1   1 
ATOM   1665 N  NH2   . ARG A 1 203 ? -23.319 1.181   -53.787 1.00 80.23  ? 203 ARG A NH2   1 
ATOM   1666 N  N     . GLU A 1 204 ? -26.654 5.383   -49.962 1.00 40.29  ? 204 GLU A N     1 
ATOM   1667 C  CA    . GLU A 1 204 ? -26.048 6.653   -50.343 1.00 40.68  ? 204 GLU A CA    1 
ATOM   1668 C  C     . GLU A 1 204 ? -25.288 7.218   -49.139 1.00 36.74  ? 204 GLU A C     1 
ATOM   1669 O  O     . GLU A 1 204 ? -25.495 6.860   -47.970 1.00 32.28  ? 204 GLU A O     1 
ATOM   1670 C  CB    . GLU A 1 204 ? -27.093 7.698   -50.768 1.00 42.31  ? 204 GLU A CB    1 
ATOM   1671 C  CG    . GLU A 1 204 ? -28.129 7.210   -51.757 1.00 46.60  ? 204 GLU A CG    1 
ATOM   1672 C  CD    . GLU A 1 204 ? -27.638 6.897   -53.159 1.00 53.76  ? 204 GLU A CD    1 
ATOM   1673 O  OE1   . GLU A 1 204 ? -26.401 6.879   -53.347 1.00 59.82  ? 204 GLU A OE1   1 
ATOM   1674 O  OE2   . GLU A 1 204 ? -28.501 6.687   -54.068 1.00 53.27  ? 204 GLU A OE2   1 
ATOM   1675 N  N     . PRO A 1 205 ? -24.361 8.145   -49.376 1.00 36.47  ? 205 PRO A N     1 
ATOM   1676 C  CA    . PRO A 1 205 ? -23.618 8.741   -48.279 1.00 36.69  ? 205 PRO A CA    1 
ATOM   1677 C  C     . PRO A 1 205 ? -24.508 9.625   -47.409 1.00 35.01  ? 205 PRO A C     1 
ATOM   1678 O  O     . PRO A 1 205 ? -25.334 10.381  -47.901 1.00 36.15  ? 205 PRO A O     1 
ATOM   1679 C  CB    . PRO A 1 205 ? -22.530 9.556   -48.987 1.00 38.18  ? 205 PRO A CB    1 
ATOM   1680 C  CG    . PRO A 1 205 ? -23.151 9.878   -50.324 1.00 42.17  ? 205 PRO A CG    1 
ATOM   1681 C  CD    . PRO A 1 205 ? -23.944 8.638   -50.696 1.00 41.47  ? 205 PRO A CD    1 
ATOM   1682 N  N     . LEU A 1 206 ? -24.322 9.483   -46.100 1.00 32.45  ? 206 LEU A N     1 
ATOM   1683 C  CA    . LEU A 1 206 ? -25.014 10.272  -45.108 1.00 30.38  ? 206 LEU A CA    1 
ATOM   1684 C  C     . LEU A 1 206 ? -23.959 11.010  -44.303 1.00 28.16  ? 206 LEU A C     1 
ATOM   1685 O  O     . LEU A 1 206 ? -22.780 10.705  -44.367 1.00 27.85  ? 206 LEU A O     1 
ATOM   1686 C  CB    . LEU A 1 206 ? -25.832 9.344   -44.206 1.00 29.60  ? 206 LEU A CB    1 
ATOM   1687 C  CG    . LEU A 1 206 ? -26.965 8.579   -44.878 1.00 29.95  ? 206 LEU A CG    1 
ATOM   1688 C  CD1   . LEU A 1 206 ? -27.688 7.712   -43.864 1.00 30.10  ? 206 LEU A CD1   1 
ATOM   1689 C  CD2   . LEU A 1 206 ? -27.945 9.529   -45.544 1.00 31.06  ? 206 LEU A CD2   1 
ATOM   1690 N  N     . MET A 1 207 ? -24.407 11.968  -43.522 1.00 27.13  ? 207 MET A N     1 
ATOM   1691 C  CA    . MET A 1 207 ? -23.517 12.710  -42.647 1.00 26.11  ? 207 MET A CA    1 
ATOM   1692 C  C     . MET A 1 207 ? -23.351 11.931  -41.357 1.00 24.57  ? 207 MET A C     1 
ATOM   1693 O  O     . MET A 1 207 ? -24.186 11.087  -40.993 1.00 24.55  ? 207 MET A O     1 
ATOM   1694 C  CB    . MET A 1 207 ? -24.129 14.090  -42.417 1.00 29.10  ? 207 MET A CB    1 
ATOM   1695 C  CG    . MET A 1 207 ? -24.187 14.859  -43.737 1.00 33.20  ? 207 MET A CG    1 
ATOM   1696 S  SD    . MET A 1 207 ? -22.640 15.730  -44.012 1.00 39.78  ? 207 MET A SD    1 
ATOM   1697 C  CE    . MET A 1 207 ? -21.542 14.481  -44.685 1.00 41.12  ? 207 MET A CE    1 
ATOM   1698 N  N     . ALA A 1 208 ? -22.238 12.168  -40.684 1.00 24.24  ? 208 ALA A N     1 
ATOM   1699 C  CA    . ALA A 1 208 ? -21.911 11.384  -39.494 1.00 23.13  ? 208 ALA A CA    1 
ATOM   1700 C  C     . ALA A 1 208 ? -23.032 11.422  -38.454 1.00 23.51  ? 208 ALA A C     1 
ATOM   1701 O  O     . ALA A 1 208 ? -23.330 10.395  -37.839 1.00 20.24  ? 208 ALA A O     1 
ATOM   1702 C  CB    . ALA A 1 208 ? -20.628 11.882  -38.903 1.00 22.21  ? 208 ALA A CB    1 
ATOM   1703 N  N     . TRP A 1 209 ? -23.672 12.594  -38.260 1.00 22.91  ? 209 TRP A N     1 
ATOM   1704 C  CA    . TRP A 1 209 ? -24.615 12.716  -37.145 1.00 23.08  ? 209 TRP A CA    1 
ATOM   1705 C  C     . TRP A 1 209 ? -25.906 11.934  -37.408 1.00 21.07  ? 209 TRP A C     1 
ATOM   1706 O  O     . TRP A 1 209 ? -26.516 11.407  -36.489 1.00 21.27  ? 209 TRP A O     1 
ATOM   1707 C  CB    . TRP A 1 209 ? -24.893 14.181  -36.757 1.00 23.00  ? 209 TRP A CB    1 
ATOM   1708 C  CG    . TRP A 1 209 ? -25.483 14.967  -37.880 1.00 23.75  ? 209 TRP A CG    1 
ATOM   1709 C  CD1   . TRP A 1 209 ? -26.768 15.024  -38.323 1.00 25.07  ? 209 TRP A CD1   1 
ATOM   1710 C  CD2   . TRP A 1 209 ? -24.714 15.793  -38.754 1.00 25.28  ? 209 TRP A CD2   1 
ATOM   1711 N  NE1   . TRP A 1 209 ? -26.849 15.846  -39.422 1.00 26.26  ? 209 TRP A NE1   1 
ATOM   1712 C  CE2   . TRP A 1 209 ? -25.603 16.322  -39.711 1.00 26.50  ? 209 TRP A CE2   1 
ATOM   1713 C  CE3   . TRP A 1 209 ? -23.361 16.113  -38.795 1.00 26.68  ? 209 TRP A CE3   1 
ATOM   1714 C  CZ2   . TRP A 1 209 ? -25.181 17.175  -40.715 1.00 29.67  ? 209 TRP A CZ2   1 
ATOM   1715 C  CZ3   . TRP A 1 209 ? -22.945 16.927  -39.804 1.00 30.95  ? 209 TRP A CZ3   1 
ATOM   1716 C  CH2   . TRP A 1 209 ? -23.842 17.451  -40.743 1.00 32.19  ? 209 TRP A CH2   1 
ATOM   1717 N  N     . THR A 1 210 ? -26.309 11.859  -38.669 1.00 21.76  ? 210 THR A N     1 
ATOM   1718 C  CA    . THR A 1 210 ? -27.411 11.017  -39.097 1.00 20.25  ? 210 THR A CA    1 
ATOM   1719 C  C     . THR A 1 210 ? -27.128 9.566   -38.730 1.00 21.43  ? 210 THR A C     1 
ATOM   1720 O  O     . THR A 1 210 ? -27.993 8.847   -38.217 1.00 21.95  ? 210 THR A O     1 
ATOM   1721 C  CB    . THR A 1 210 ? -27.593 11.180  -40.602 1.00 19.97  ? 210 THR A CB    1 
ATOM   1722 O  OG1   . THR A 1 210 ? -27.654 12.560  -40.950 1.00 18.65  ? 210 THR A OG1   1 
ATOM   1723 C  CG2   . THR A 1 210 ? -28.841 10.497  -41.075 1.00 21.96  ? 210 THR A CG2   1 
ATOM   1724 N  N     . ILE A 1 211 ? -25.894 9.115   -39.007 1.00 22.69  ? 211 ILE A N     1 
ATOM   1725 C  CA    . ILE A 1 211 ? -25.519 7.745   -38.699 1.00 21.62  ? 211 ILE A CA    1 
ATOM   1726 C  C     . ILE A 1 211 ? -25.512 7.539   -37.185 1.00 21.20  ? 211 ILE A C     1 
ATOM   1727 O  O     . ILE A 1 211 ? -25.973 6.510   -36.682 1.00 20.74  ? 211 ILE A O     1 
ATOM   1728 C  CB    . ILE A 1 211 ? -24.164 7.422   -39.331 1.00 21.64  ? 211 ILE A CB    1 
ATOM   1729 C  CG1   . ILE A 1 211 ? -24.243 7.449   -40.862 1.00 23.49  ? 211 ILE A CG1   1 
ATOM   1730 C  CG2   . ILE A 1 211 ? -23.654 6.087   -38.833 1.00 22.05  ? 211 ILE A CG2   1 
ATOM   1731 C  CD1   . ILE A 1 211 ? -25.255 6.513   -41.445 1.00 24.93  ? 211 ILE A CD1   1 
ATOM   1732 N  N     . VAL A 1 212 ? -24.996 8.526   -36.456 1.00 20.31  ? 212 VAL A N     1 
ATOM   1733 C  CA    . VAL A 1 212 ? -24.970 8.449   -35.012 1.00 21.00  ? 212 VAL A CA    1 
ATOM   1734 C  C     . VAL A 1 212 ? -26.388 8.222   -34.502 1.00 23.89  ? 212 VAL A C     1 
ATOM   1735 O  O     . VAL A 1 212 ? -26.557 7.341   -33.641 1.00 23.70  ? 212 VAL A O     1 
ATOM   1736 C  CB    . VAL A 1 212 ? -24.318 9.689   -34.384 1.00 22.14  ? 212 VAL A CB    1 
ATOM   1737 C  CG1   . VAL A 1 212 ? -24.609 9.790   -32.900 1.00 22.36  ? 212 VAL A CG1   1 
ATOM   1738 C  CG2   . VAL A 1 212 ? -22.808 9.680   -34.632 1.00 21.64  ? 212 VAL A CG2   1 
ATOM   1739 N  N     . ASN A 1 213 ? -27.366 8.974   -35.073 1.00 22.96  ? 213 ASN A N     1 
ATOM   1740 C  CA    . ASN A 1 213 ? -28.780 8.896   -34.679 1.00 23.04  ? 213 ASN A CA    1 
ATOM   1741 C  C     . ASN A 1 213 ? -29.380 7.534   -35.013 1.00 23.74  ? 213 ASN A C     1 
ATOM   1742 O  O     . ASN A 1 213 ? -30.073 6.957   -34.177 1.00 26.61  ? 213 ASN A O     1 
ATOM   1743 C  CB    . ASN A 1 213 ? -29.658 9.961   -35.352 1.00 22.54  ? 213 ASN A CB    1 
ATOM   1744 C  CG    . ASN A 1 213 ? -29.243 11.389  -35.027 1.00 23.79  ? 213 ASN A CG    1 
ATOM   1745 O  OD1   . ASN A 1 213 ? -28.621 11.650  -33.992 1.00 22.87  ? 213 ASN A OD1   1 
ATOM   1746 N  ND2   . ASN A 1 213 ? -29.566 12.326  -35.912 1.00 24.25  ? 213 ASN A ND2   1 
ATOM   1747 N  N     . GLU A 1 214 ? -29.126 7.038   -36.236 1.00 22.25  ? 214 GLU A N     1 
ATOM   1748 C  CA    . GLU A 1 214 ? -29.656 5.758   -36.651 1.00 23.63  ? 214 GLU A CA    1 
ATOM   1749 C  C     . GLU A 1 214 ? -29.182 4.671   -35.691 1.00 23.90  ? 214 GLU A C     1 
ATOM   1750 O  O     . GLU A 1 214 ? -29.981 3.868   -35.230 1.00 27.17  ? 214 GLU A O     1 
ATOM   1751 C  CB    . GLU A 1 214 ? -29.268 5.440   -38.089 1.00 23.77  ? 214 GLU A CB    1 
ATOM   1752 C  CG    . GLU A 1 214 ? -29.903 6.345   -39.107 1.00 24.38  ? 214 GLU A CG    1 
ATOM   1753 C  CD    . GLU A 1 214 ? -31.366 6.051   -39.318 1.00 28.24  ? 214 GLU A CD    1 
ATOM   1754 O  OE1   . GLU A 1 214 ? -32.062 6.908   -39.869 1.00 31.30  ? 214 GLU A OE1   1 
ATOM   1755 O  OE2   . GLU A 1 214 ? -31.778 4.922   -39.017 1.00 29.65  ? 214 GLU A OE2   1 
ATOM   1756 N  N     . VAL A 1 215 ? -27.898 4.665   -35.378 1.00 21.21  ? 215 VAL A N     1 
ATOM   1757 C  CA    . VAL A 1 215 ? -27.325 3.667   -34.501 1.00 22.55  ? 215 VAL A CA    1 
ATOM   1758 C  C     . VAL A 1 215 ? -27.863 3.814   -33.084 1.00 23.72  ? 215 VAL A C     1 
ATOM   1759 O  O     . VAL A 1 215 ? -28.205 2.820   -32.432 1.00 24.23  ? 215 VAL A O     1 
ATOM   1760 C  CB    . VAL A 1 215 ? -25.792 3.806   -34.482 1.00 24.24  ? 215 VAL A CB    1 
ATOM   1761 C  CG1   . VAL A 1 215 ? -25.139 3.004   -33.370 1.00 24.17  ? 215 VAL A CG1   1 
ATOM   1762 C  CG2   . VAL A 1 215 ? -25.207 3.454   -35.828 1.00 24.90  ? 215 VAL A CG2   1 
ATOM   1763 N  N     . ILE A 1 216 ? -27.827 5.041   -32.548 1.00 24.09  ? 216 ILE A N     1 
ATOM   1764 C  CA    . ILE A 1 216 ? -28.197 5.215   -31.163 1.00 24.37  ? 216 ILE A CA    1 
ATOM   1765 C  C     . ILE A 1 216 ? -29.671 4.886   -30.975 1.00 27.55  ? 216 ILE A C     1 
ATOM   1766 O  O     . ILE A 1 216 ? -30.030 4.222   -30.007 1.00 28.80  ? 216 ILE A O     1 
ATOM   1767 C  CB    . ILE A 1 216 ? -27.877 6.617   -30.655 1.00 24.24  ? 216 ILE A CB    1 
ATOM   1768 C  CG1   . ILE A 1 216 ? -26.377 6.772   -30.453 1.00 23.43  ? 216 ILE A CG1   1 
ATOM   1769 C  CG2   . ILE A 1 216 ? -28.646 6.877   -29.359 1.00 25.68  ? 216 ILE A CG2   1 
ATOM   1770 C  CD1   . ILE A 1 216 ? -25.943 8.126   -29.992 1.00 23.14  ? 216 ILE A CD1   1 
ATOM   1771 N  N     . VAL A 1 217 ? -30.529 5.330   -31.896 1.00 28.22  ? 217 VAL A N     1 
ATOM   1772 C  CA    . VAL A 1 217 ? -31.962 5.145   -31.683 1.00 29.16  ? 217 VAL A CA    1 
ATOM   1773 C  C     . VAL A 1 217 ? -32.336 3.675   -31.862 1.00 30.34  ? 217 VAL A C     1 
ATOM   1774 O  O     . VAL A 1 217 ? -33.167 3.147   -31.106 1.00 32.19  ? 217 VAL A O     1 
ATOM   1775 C  CB    . VAL A 1 217 ? -32.799 6.090   -32.568 1.00 27.18  ? 217 VAL A CB    1 
ATOM   1776 C  CG1   . VAL A 1 217 ? -34.253 5.715   -32.623 1.00 29.48  ? 217 VAL A CG1   1 
ATOM   1777 C  CG2   . VAL A 1 217 ? -32.687 7.520   -32.083 1.00 26.62  ? 217 VAL A CG2   1 
ATOM   1778 N  N     . SER A 1 218 ? -31.760 3.014   -32.873 1.00 31.81  ? 218 SER A N     1 
ATOM   1779 C  CA    . SER A 1 218 ? -32.035 1.601   -33.089 1.00 34.42  ? 218 SER A CA    1 
ATOM   1780 C  C     . SER A 1 218 ? -31.551 0.767   -31.894 1.00 31.88  ? 218 SER A C     1 
ATOM   1781 O  O     . SER A 1 218 ? -32.242 -0.138  -31.470 1.00 33.65  ? 218 SER A O     1 
ATOM   1782 C  CB    . SER A 1 218 ? -31.482 1.148   -34.436 1.00 38.98  ? 218 SER A CB    1 
ATOM   1783 O  OG    . SER A 1 218 ? -30.071 0.965   -34.390 1.00 52.61  ? 218 SER A OG    1 
ATOM   1784 N  N     . TYR A 1 219 ? -30.435 1.140   -31.263 1.00 28.17  ? 219 TYR A N     1 
ATOM   1785 C  CA    . TYR A 1 219 ? -29.944 0.423   -30.105 1.00 28.70  ? 219 TYR A CA    1 
ATOM   1786 C  C     . TYR A 1 219 ? -30.819 0.672   -28.881 1.00 29.69  ? 219 TYR A C     1 
ATOM   1787 O  O     . TYR A 1 219 ? -31.184 -0.278  -28.196 1.00 32.80  ? 219 TYR A O     1 
ATOM   1788 C  CB    . TYR A 1 219 ? -28.460 0.733   -29.889 1.00 28.54  ? 219 TYR A CB    1 
ATOM   1789 C  CG    . TYR A 1 219 ? -27.748 -0.034  -28.784 1.00 29.52  ? 219 TYR A CG    1 
ATOM   1790 C  CD1   . TYR A 1 219 ? -27.466 -1.398  -28.898 1.00 32.31  ? 219 TYR A CD1   1 
ATOM   1791 C  CD2   . TYR A 1 219 ? -27.349 0.604   -27.624 1.00 29.50  ? 219 TYR A CD2   1 
ATOM   1792 C  CE1   . TYR A 1 219 ? -26.805 -2.093  -27.897 1.00 31.28  ? 219 TYR A CE1   1 
ATOM   1793 C  CE2   . TYR A 1 219 ? -26.668 -0.075  -26.622 1.00 32.28  ? 219 TYR A CE2   1 
ATOM   1794 C  CZ    . TYR A 1 219 ? -26.388 -1.427  -26.755 1.00 32.81  ? 219 TYR A CZ    1 
ATOM   1795 O  OH    . TYR A 1 219 ? -25.758 -2.086  -25.727 1.00 33.04  ? 219 TYR A OH    1 
ATOM   1796 N  N     . GLU A 1 220 ? -31.205 1.908   -28.607 1.00 29.79  ? 220 GLU A N     1 
ATOM   1797 C  CA    . GLU A 1 220 ? -32.130 2.194   -27.504 1.00 32.46  ? 220 GLU A CA    1 
ATOM   1798 C  C     . GLU A 1 220 ? -33.308 1.215   -27.456 1.00 36.03  ? 220 GLU A C     1 
ATOM   1799 O  O     . GLU A 1 220 ? -33.710 0.774   -26.395 1.00 36.37  ? 220 GLU A O     1 
ATOM   1800 C  CB    . GLU A 1 220 ? -32.779 3.576   -27.632 1.00 28.77  ? 220 GLU A CB    1 
ATOM   1801 C  CG    . GLU A 1 220 ? -31.824 4.694   -27.371 1.00 27.90  ? 220 GLU A CG    1 
ATOM   1802 C  CD    . GLU A 1 220 ? -32.328 6.089   -27.702 1.00 26.34  ? 220 GLU A CD    1 
ATOM   1803 O  OE1   . GLU A 1 220 ? -31.571 7.036   -27.498 1.00 24.94  ? 220 GLU A OE1   1 
ATOM   1804 O  OE2   . GLU A 1 220 ? -33.476 6.225   -28.127 1.00 27.54  ? 220 GLU A OE2   1 
ATOM   1805 N  N     . TRP A 1 221 ? -33.898 0.923   -28.610 1.00 39.92  ? 221 TRP A N     1 
ATOM   1806 C  CA    . TRP A 1 221 ? -35.177 0.239   -28.656 1.00 46.93  ? 221 TRP A CA    1 
ATOM   1807 C  C     . TRP A 1 221 ? -35.043 -1.244  -28.394 1.00 44.77  ? 221 TRP A C     1 
ATOM   1808 O  O     . TRP A 1 221 ? -36.051 -1.900  -28.135 1.00 47.54  ? 221 TRP A O     1 
ATOM   1809 C  CB    . TRP A 1 221 ? -35.833 0.472   -30.011 1.00 50.43  ? 221 TRP A CB    1 
ATOM   1810 C  CG    . TRP A 1 221 ? -36.090 1.937   -30.185 1.00 62.04  ? 221 TRP A CG    1 
ATOM   1811 C  CD1   . TRP A 1 221 ? -35.839 2.979   -29.320 1.00 71.05  ? 221 TRP A CD1   1 
ATOM   1812 C  CD2   . TRP A 1 221 ? -36.659 2.516   -31.363 1.00 65.19  ? 221 TRP A CD2   1 
ATOM   1813 N  NE1   . TRP A 1 221 ? -36.219 4.174   -29.872 1.00 60.02  ? 221 TRP A NE1   1 
ATOM   1814 C  CE2   . TRP A 1 221 ? -36.724 3.909   -31.129 1.00 73.75  ? 221 TRP A CE2   1 
ATOM   1815 C  CE3   . TRP A 1 221 ? -37.118 1.969   -32.562 1.00 64.52  ? 221 TRP A CE3   1 
ATOM   1816 C  CZ2   . TRP A 1 221 ? -37.242 4.761   -32.099 1.00 80.96  ? 221 TRP A CZ2   1 
ATOM   1817 C  CZ3   . TRP A 1 221 ? -37.620 2.817   -33.510 1.00 61.38  ? 221 TRP A CZ3   1 
ATOM   1818 C  CH2   . TRP A 1 221 ? -37.662 4.183   -33.274 1.00 75.46  ? 221 TRP A CH2   1 
ATOM   1819 N  N     . GLU A 1 222 ? -33.808 -1.731  -28.480 1.00 42.27  ? 222 GLU A N     1 
ATOM   1820 C  CA    . GLU A 1 222 ? -33.511 -3.103  -28.122 1.00 46.70  ? 222 GLU A CA    1 
ATOM   1821 C  C     . GLU A 1 222 ? -33.032 -3.201  -26.680 1.00 48.38  ? 222 GLU A C     1 
ATOM   1822 O  O     . GLU A 1 222 ? -33.336 -4.171  -26.012 1.00 53.91  ? 222 GLU A O     1 
ATOM   1823 C  CB    . GLU A 1 222 ? -32.460 -3.669  -29.076 1.00 45.21  ? 222 GLU A CB    1 
ATOM   1824 C  CG    . GLU A 1 222 ? -33.047 -4.075  -30.397 1.00 46.10  ? 222 GLU A CG    1 
ATOM   1825 C  CD    . GLU A 1 222 ? -34.054 -5.207  -30.239 1.00 51.00  ? 222 GLU A CD    1 
ATOM   1826 O  OE1   . GLU A 1 222 ? -33.722 -6.236  -29.593 1.00 53.16  ? 222 GLU A OE1   1 
ATOM   1827 O  OE2   . GLU A 1 222 ? -35.179 -5.043  -30.723 1.00 51.57  ? 222 GLU A OE2   1 
ATOM   1828 N  N     . VAL A 1 223 ? -32.259 -2.221  -26.216 1.00 50.52  ? 223 VAL A N     1 
ATOM   1829 C  CA    . VAL A 1 223 ? -31.394 -2.422  -25.065 1.00 51.96  ? 223 VAL A CA    1 
ATOM   1830 C  C     . VAL A 1 223 ? -32.055 -1.833  -23.826 1.00 55.25  ? 223 VAL A C     1 
ATOM   1831 O  O     . VAL A 1 223 ? -31.752 -2.243  -22.711 1.00 61.86  ? 223 VAL A O     1 
ATOM   1832 C  CB    . VAL A 1 223 ? -29.990 -1.822  -25.294 1.00 51.08  ? 223 VAL A CB    1 
ATOM   1833 C  CG1   . VAL A 1 223 ? -30.010 -0.297  -25.251 1.00 49.13  ? 223 VAL A CG1   1 
ATOM   1834 C  CG2   . VAL A 1 223 ? -28.972 -2.366  -24.297 1.00 52.67  ? 223 VAL A CG2   1 
ATOM   1835 N  N     . ILE A 1 224 ? -32.906 -0.831  -24.009 1.00 55.41  ? 224 ILE A N     1 
ATOM   1836 C  CA    . ILE A 1 224 ? -33.616 -0.273  -22.876 1.00 62.02  ? 224 ILE A CA    1 
ATOM   1837 C  C     . ILE A 1 224 ? -34.881 -1.104  -22.730 1.00 67.72  ? 224 ILE A C     1 
ATOM   1838 O  O     . ILE A 1 224 ? -35.715 -1.118  -23.630 1.00 61.20  ? 224 ILE A O     1 
ATOM   1839 C  CB    . ILE A 1 224 ? -33.887 1.233   -23.068 1.00 62.87  ? 224 ILE A CB    1 
ATOM   1840 C  CG1   . ILE A 1 224 ? -32.581 2.025   -23.199 1.00 60.13  ? 224 ILE A CG1   1 
ATOM   1841 C  CG2   . ILE A 1 224 ? -34.767 1.799   -21.958 1.00 62.17  ? 224 ILE A CG2   1 
ATOM   1842 C  CD1   . ILE A 1 224 ? -32.790 3.409   -23.734 1.00 58.82  ? 224 ILE A CD1   1 
ATOM   1843 N  N     . LYS A 1 225 ? -34.969 -1.812  -21.596 1.00 85.45  ? 225 LYS A N     1 
ATOM   1844 C  CA    . LYS A 1 225 ? -35.906 -2.916  -21.398 1.00 95.70  ? 225 LYS A CA    1 
ATOM   1845 C  C     . LYS A 1 225 ? -37.355 -2.421  -21.294 1.00 88.84  ? 225 LYS A C     1 
ATOM   1846 O  O     . LYS A 1 225 ? -38.291 -3.117  -21.689 1.00 85.25  ? 225 LYS A O     1 
ATOM   1847 C  CB    . LYS A 1 225 ? -35.601 -3.665  -20.106 1.00 108.34 ? 225 LYS A CB    1 
ATOM   1848 C  CG    . LYS A 1 225 ? -34.903 -5.013  -20.278 1.00 116.01 ? 225 LYS A CG    1 
ATOM   1849 C  CD    . LYS A 1 225 ? -33.591 -4.985  -21.041 1.00 115.55 ? 225 LYS A CD    1 
ATOM   1850 C  CE    . LYS A 1 225 ? -32.929 -6.346  -21.112 1.00 120.61 ? 225 LYS A CE    1 
ATOM   1851 N  NZ    . LYS A 1 225 ? -33.719 -7.305  -21.921 1.00 124.59 ? 225 LYS A NZ    1 
ATOM   1852 N  N     . LYS A 1 226 ? -37.501 -1.201  -20.783 1.00 83.95  ? 226 LYS A N     1 
ATOM   1853 C  CA    . LYS A 1 226 ? -38.785 -0.559  -20.679 1.00 88.37  ? 226 LYS A CA    1 
ATOM   1854 C  C     . LYS A 1 226 ? -39.230 -0.039  -22.065 1.00 87.73  ? 226 LYS A C     1 
ATOM   1855 O  O     . LYS A 1 226 ? -40.290 0.583   -22.147 1.00 81.42  ? 226 LYS A O     1 
ATOM   1856 C  CB    . LYS A 1 226 ? -38.696 0.586   -19.663 1.00 91.79  ? 226 LYS A CB    1 
ATOM   1857 C  CG    . LYS A 1 226 ? -37.611 1.615   -19.952 1.00 92.88  ? 226 LYS A CG    1 
ATOM   1858 C  CD    . LYS A 1 226 ? -37.643 2.781   -18.998 1.00 98.35  ? 226 LYS A CD    1 
ATOM   1859 C  CE    . LYS A 1 226 ? -36.966 4.025   -19.534 1.00 92.39  ? 226 LYS A CE    1 
ATOM   1860 N  NZ    . LYS A 1 226 ? -37.259 5.211   -18.689 1.00 95.29  ? 226 LYS A NZ    1 
ATOM   1861 N  N     . PHE A 1 227 ? -38.428 -0.279  -23.128 1.00 85.88  ? 227 PHE A N     1 
ATOM   1862 C  CA    . PHE A 1 227 ? -38.845 -0.088  -24.518 1.00 80.61  ? 227 PHE A CA    1 
ATOM   1863 C  C     . PHE A 1 227 ? -38.985 -1.432  -25.241 1.00 77.50  ? 227 PHE A C     1 
ATOM   1864 O  O     . PHE A 1 227 ? -39.991 -2.129  -25.018 1.00 77.79  ? 227 PHE A O     1 
ATOM   1865 C  CB    . PHE A 1 227 ? -37.830 0.738   -25.318 1.00 79.52  ? 227 PHE A CB    1 
ATOM   1866 C  CG    . PHE A 1 227 ? -37.734 2.214   -25.006 1.00 78.46  ? 227 PHE A CG    1 
ATOM   1867 C  CD1   . PHE A 1 227 ? -38.558 2.829   -24.065 1.00 80.65  ? 227 PHE A CD1   1 
ATOM   1868 C  CD2   . PHE A 1 227 ? -36.800 2.999   -25.670 1.00 73.69  ? 227 PHE A CD2   1 
ATOM   1869 C  CE1   . PHE A 1 227 ? -38.453 4.188   -23.796 1.00 76.57  ? 227 PHE A CE1   1 
ATOM   1870 C  CE2   . PHE A 1 227 ? -36.700 4.358   -25.407 1.00 70.78  ? 227 PHE A CE2   1 
ATOM   1871 C  CZ    . PHE A 1 227 ? -37.528 4.952   -24.476 1.00 71.72  ? 227 PHE A CZ    1 
HETATM 1872 CL CL    . CL  B 2 .   ? -28.196 -5.327  -19.060 1.00 69.15  ? 301 CL  A CL    1 
HETATM 1873 C  CS    . MTA C 3 .   ? -17.778 10.573  -44.789 1.00 25.50  ? 302 MTA A CS    1 
HETATM 1874 S  "S5'" . MTA C 3 .   ? -19.360 10.705  -43.964 1.00 29.23  ? 302 MTA A "S5'" 1 
HETATM 1875 C  "C5'" . MTA C 3 .   ? -18.916 10.497  -42.225 1.00 25.20  ? 302 MTA A "C5'" 1 
HETATM 1876 C  "C4'" . MTA C 3 .   ? -19.043 9.092   -41.703 1.00 25.08  ? 302 MTA A "C4'" 1 
HETATM 1877 O  "O4'" . MTA C 3 .   ? -20.422 8.693   -41.767 1.00 23.40  ? 302 MTA A "O4'" 1 
HETATM 1878 C  "C2'" . MTA C 3 .   ? -19.056 6.752   -41.973 1.00 24.49  ? 302 MTA A "C2'" 1 
HETATM 1879 O  "O2'" . MTA C 3 .   ? -18.627 6.244   -40.710 1.00 22.58  ? 302 MTA A "O2'" 1 
HETATM 1880 C  "C3'" . MTA C 3 .   ? -18.300 7.990   -42.470 1.00 24.37  ? 302 MTA A "C3'" 1 
HETATM 1881 O  "O3'" . MTA C 3 .   ? -16.912 8.002   -42.126 1.00 26.60  ? 302 MTA A "O3'" 1 
HETATM 1882 C  "C1'" . MTA C 3 .   ? -20.493 7.292   -41.903 1.00 24.71  ? 302 MTA A "C1'" 1 
HETATM 1883 N  N9    . MTA C 3 .   ? -21.374 7.020   -43.046 1.00 23.56  ? 302 MTA A N9    1 
HETATM 1884 C  C8    . MTA C 3 .   ? -21.699 7.868   -44.084 1.00 22.61  ? 302 MTA A C8    1 
HETATM 1885 N  N7    . MTA C 3 .   ? -22.609 7.379   -44.899 1.00 21.79  ? 302 MTA A N7    1 
HETATM 1886 C  C5    . MTA C 3 .   ? -22.901 6.127   -44.364 1.00 24.09  ? 302 MTA A C5    1 
HETATM 1887 C  C6    . MTA C 3 .   ? -23.803 5.108   -44.752 1.00 25.24  ? 302 MTA A C6    1 
HETATM 1888 N  N6    . MTA C 3 .   ? -24.593 5.162   -45.828 1.00 26.68  ? 302 MTA A N6    1 
HETATM 1889 N  N1    . MTA C 3 .   ? -23.852 4.003   -43.976 1.00 25.35  ? 302 MTA A N1    1 
HETATM 1890 C  C2    . MTA C 3 .   ? -23.044 3.913   -42.908 1.00 24.87  ? 302 MTA A C2    1 
HETATM 1891 N  N3    . MTA C 3 .   ? -22.166 4.793   -42.452 1.00 23.14  ? 302 MTA A N3    1 
HETATM 1892 C  C4    . MTA C 3 .   ? -22.158 5.903   -43.216 1.00 22.53  ? 302 MTA A C4    1 
HETATM 1893 C  C1    . EDO D 4 .   ? -13.074 7.737   -19.374 1.00 65.69  ? 303 EDO A C1    1 
HETATM 1894 O  O1    . EDO D 4 .   ? -11.679 7.691   -19.603 1.00 60.86  ? 303 EDO A O1    1 
HETATM 1895 C  C2    . EDO D 4 .   ? -13.393 8.680   -18.280 1.00 61.42  ? 303 EDO A C2    1 
HETATM 1896 O  O2    . EDO D 4 .   ? -12.290 9.518   -17.987 1.00 61.18  ? 303 EDO A O2    1 
HETATM 1897 C  C1    . GOL E 5 .   ? -3.838  2.227   -34.762 1.00 43.01  ? 304 GOL A C1    1 
HETATM 1898 O  O1    . GOL E 5 .   ? -4.785  3.076   -35.407 1.00 31.61  ? 304 GOL A O1    1 
HETATM 1899 C  C2    . GOL E 5 .   ? -2.480  2.120   -35.448 1.00 49.57  ? 304 GOL A C2    1 
HETATM 1900 O  O2    . GOL E 5 .   ? -1.879  3.411   -35.655 1.00 43.91  ? 304 GOL A O2    1 
HETATM 1901 C  C3    . GOL E 5 .   ? -1.535  1.159   -34.730 1.00 46.74  ? 304 GOL A C3    1 
HETATM 1902 O  O3    . GOL E 5 .   ? -1.163  1.574   -33.413 1.00 43.18  ? 304 GOL A O3    1 
HETATM 1903 C  C1    . GOL F 5 .   ? -24.943 25.807  -23.114 1.00 56.47  ? 305 GOL A C1    1 
HETATM 1904 O  O1    . GOL F 5 .   ? -23.792 26.294  -22.420 1.00 69.88  ? 305 GOL A O1    1 
HETATM 1905 C  C2    . GOL F 5 .   ? -25.266 26.697  -24.288 1.00 58.00  ? 305 GOL A C2    1 
HETATM 1906 O  O2    . GOL F 5 .   ? -24.039 27.164  -24.841 1.00 48.40  ? 305 GOL A O2    1 
HETATM 1907 C  C3    . GOL F 5 .   ? -26.172 27.865  -23.929 1.00 71.17  ? 305 GOL A C3    1 
HETATM 1908 O  O3    . GOL F 5 .   ? -27.349 27.450  -23.231 1.00 72.88  ? 305 GOL A O3    1 
HETATM 1909 C  C     . ACT G 6 .   ? -17.502 19.963  -47.991 1.00 69.17  ? 306 ACT A C     1 
HETATM 1910 O  O     . ACT G 6 .   ? -18.421 20.071  -47.153 1.00 74.65  ? 306 ACT A O     1 
HETATM 1911 O  OXT   . ACT G 6 .   ? -16.790 18.951  -48.082 1.00 59.24  ? 306 ACT A OXT   1 
HETATM 1912 C  CH3   . ACT G 6 .   ? -17.237 21.141  -48.963 1.00 66.18  ? 306 ACT A CH3   1 
HETATM 1913 O  O     . HOH H 7 .   ? -26.986 -7.129  -46.321 1.00 37.05  ? 401 HOH A O     1 
HETATM 1914 O  O     . HOH H 7 .   ? -1.296  15.071  -43.033 1.00 43.20  ? 402 HOH A O     1 
HETATM 1915 O  O     . HOH H 7 .   ? -8.922  19.132  -38.949 1.00 31.74  ? 403 HOH A O     1 
HETATM 1916 O  O     . HOH H 7 .   ? -2.502  37.251  -35.103 1.00 40.45  ? 404 HOH A O     1 
HETATM 1917 O  O     . HOH H 7 .   ? -5.929  28.647  -25.548 1.00 50.15  ? 405 HOH A O     1 
HETATM 1918 O  O     . HOH H 7 .   ? 0.340   6.634   -29.845 1.00 29.21  ? 406 HOH A O     1 
HETATM 1919 O  O     . HOH H 7 .   ? -24.491 5.576   -54.384 1.00 46.13  ? 407 HOH A O     1 
HETATM 1920 O  O     . HOH H 7 .   ? -20.306 19.461  -45.558 1.00 58.82  ? 408 HOH A O     1 
HETATM 1921 O  O     . HOH H 7 .   ? -5.739  25.853  -27.243 1.00 39.49  ? 409 HOH A O     1 
HETATM 1922 O  O     . HOH H 7 .   ? -30.176 -8.056  -36.511 1.00 39.51  ? 410 HOH A O     1 
HETATM 1923 O  O     . HOH H 7 .   ? -3.956  0.920   -25.474 1.00 38.68  ? 411 HOH A O     1 
HETATM 1924 O  O     . HOH H 7 .   ? -7.461  -5.222  -24.487 1.00 29.60  ? 412 HOH A O     1 
HETATM 1925 O  O     . HOH H 7 .   ? -16.010 30.130  -33.253 1.00 39.95  ? 413 HOH A O     1 
HETATM 1926 O  O     . HOH H 7 .   ? -14.678 16.455  -37.125 1.00 38.46  ? 414 HOH A O     1 
HETATM 1927 O  O     . HOH H 7 .   ? -10.176 -3.794  -34.097 1.00 24.57  ? 415 HOH A O     1 
HETATM 1928 O  O     . HOH H 7 .   ? 0.272   0.929   -31.026 1.00 22.04  ? 416 HOH A O     1 
HETATM 1929 O  O     . HOH H 7 .   ? -21.743 8.571   -22.811 1.00 35.38  ? 417 HOH A O     1 
HETATM 1930 O  O     . HOH H 7 .   ? -7.574  -3.506  -34.827 1.00 30.38  ? 418 HOH A O     1 
HETATM 1931 O  O     . HOH H 7 .   ? -21.339 11.735  -46.364 1.00 46.60  ? 419 HOH A O     1 
HETATM 1932 O  O     . HOH H 7 .   ? -9.724  12.505  -41.187 1.00 35.47  ? 420 HOH A O     1 
HETATM 1933 O  O     . HOH H 7 .   ? -24.641 6.628   -20.838 1.00 20.80  ? 421 HOH A O     1 
HETATM 1934 O  O     . HOH H 7 .   ? -17.156 4.621   -17.122 1.00 52.88  ? 422 HOH A O     1 
HETATM 1935 O  O     . HOH H 7 .   ? -31.226 -8.603  -30.453 1.00 47.45  ? 423 HOH A O     1 
HETATM 1936 O  O     . HOH H 7 .   ? -1.427  24.543  -33.132 1.00 44.81  ? 424 HOH A O     1 
HETATM 1937 O  O     . HOH H 7 .   ? 0.439   13.875  -34.587 1.00 37.48  ? 425 HOH A O     1 
HETATM 1938 O  O     . HOH H 7 .   ? -5.145  5.735   -35.703 1.00 21.18  ? 426 HOH A O     1 
HETATM 1939 O  O     . HOH H 7 .   ? -2.207  6.036   -36.837 1.00 39.05  ? 427 HOH A O     1 
HETATM 1940 O  O     . HOH H 7 .   ? -6.168  16.706  -33.447 1.00 38.42  ? 428 HOH A O     1 
HETATM 1941 O  O     . HOH H 7 .   ? -29.130 -14.236 -33.091 1.00 45.11  ? 429 HOH A O     1 
HETATM 1942 O  O     . HOH H 7 .   ? -16.793 24.455  -41.535 1.00 43.43  ? 430 HOH A O     1 
HETATM 1943 O  O     . HOH H 7 .   ? -19.594 -0.497  -20.973 1.00 34.36  ? 431 HOH A O     1 
HETATM 1944 O  O     . HOH H 7 .   ? -24.667 26.329  -31.999 1.00 28.03  ? 432 HOH A O     1 
HETATM 1945 O  O     . HOH H 7 .   ? -10.649 21.487  -36.340 1.00 31.56  ? 433 HOH A O     1 
HETATM 1946 O  O     . HOH H 7 .   ? -14.383 26.493  -21.217 1.00 47.55  ? 434 HOH A O     1 
HETATM 1947 O  O     . HOH H 7 .   ? -30.164 13.216  -29.063 1.00 22.20  ? 435 HOH A O     1 
HETATM 1948 O  O     . HOH H 7 .   ? -19.126 8.749   -22.544 1.00 30.68  ? 436 HOH A O     1 
HETATM 1949 O  O     . HOH H 7 .   ? -11.099 29.256  -24.953 1.00 39.80  ? 437 HOH A O     1 
HETATM 1950 O  O     . HOH H 7 .   ? -20.314 13.859  -41.703 1.00 29.07  ? 438 HOH A O     1 
HETATM 1951 O  O     . HOH H 7 .   ? -16.831 23.993  -38.612 1.00 39.76  ? 439 HOH A O     1 
HETATM 1952 O  O     . HOH H 7 .   ? -4.274  32.756  -25.886 1.00 45.12  ? 440 HOH A O     1 
HETATM 1953 O  O     . HOH H 7 .   ? -15.307 8.480   -23.014 1.00 32.46  ? 441 HOH A O     1 
HETATM 1954 O  O     . HOH H 7 .   ? -5.629  -8.568  -37.781 1.00 38.10  ? 442 HOH A O     1 
HETATM 1955 O  O     . HOH H 7 .   ? -10.993 -1.399  -41.802 1.00 48.46  ? 443 HOH A O     1 
HETATM 1956 O  O     . HOH H 7 .   ? -22.577 23.184  -34.621 1.00 29.73  ? 444 HOH A O     1 
HETATM 1957 O  O     . HOH H 7 .   ? -3.020  20.855  -35.681 1.00 31.18  ? 445 HOH A O     1 
HETATM 1958 O  O     . HOH H 7 .   ? -21.308 19.016  -17.523 1.00 40.02  ? 446 HOH A O     1 
HETATM 1959 O  O     . HOH H 7 .   ? -34.592 0.640   -39.690 1.00 29.87  ? 447 HOH A O     1 
HETATM 1960 O  O     . HOH H 7 .   ? -0.737  19.207  -39.628 1.00 47.38  ? 448 HOH A O     1 
HETATM 1961 O  O     . HOH H 7 .   ? -27.101 12.865  -43.760 1.00 32.96  ? 449 HOH A O     1 
HETATM 1962 O  O     . HOH H 7 .   ? -28.642 10.418  -31.421 1.00 34.38  ? 450 HOH A O     1 
HETATM 1963 O  O     . HOH H 7 .   ? -32.032 0.908   -19.321 1.00 49.07  ? 451 HOH A O     1 
HETATM 1964 O  O     . HOH H 7 .   ? -14.641 -7.227  -33.821 1.00 36.11  ? 452 HOH A O     1 
HETATM 1965 O  O     . HOH H 7 .   ? -33.436 -0.710  -19.370 1.00 46.74  ? 453 HOH A O     1 
HETATM 1966 O  O     . HOH H 7 .   ? -4.132  20.059  -32.810 1.00 41.44  ? 454 HOH A O     1 
HETATM 1967 O  O     . HOH H 7 .   ? -13.012 12.013  -19.336 1.00 35.91  ? 455 HOH A O     1 
HETATM 1968 O  O     . HOH H 7 .   ? -30.944 -5.819  -42.325 1.00 35.47  ? 456 HOH A O     1 
HETATM 1969 O  O     . HOH H 7 .   ? -31.268 11.465  -38.174 1.00 31.22  ? 457 HOH A O     1 
HETATM 1970 O  O     . HOH H 7 .   ? -16.266 6.700   -44.707 1.00 35.08  ? 458 HOH A O     1 
HETATM 1971 O  O     . HOH H 7 .   ? -38.087 7.441   -16.886 1.00 56.73  ? 459 HOH A O     1 
HETATM 1972 O  O     . HOH H 7 .   ? -11.450 -4.811  -19.917 1.00 38.60  ? 460 HOH A O     1 
HETATM 1973 O  O     . HOH H 7 .   ? -18.879 5.980   -45.360 1.00 21.62  ? 461 HOH A O     1 
HETATM 1974 O  O     . HOH H 7 .   ? -3.938  6.874   -38.748 1.00 39.83  ? 462 HOH A O     1 
HETATM 1975 O  O     . HOH H 7 .   ? -39.481 7.218   -19.326 1.00 46.54  ? 463 HOH A O     1 
HETATM 1976 O  O     . HOH H 7 .   ? -3.019  12.051  -20.050 1.00 46.47  ? 464 HOH A O     1 
HETATM 1977 O  O     . HOH H 7 .   ? -2.738  21.603  -29.885 1.00 39.29  ? 465 HOH A O     1 
HETATM 1978 O  O     . HOH H 7 .   ? -16.273 -6.082  -43.104 1.00 43.37  ? 466 HOH A O     1 
HETATM 1979 O  O     . HOH H 7 .   ? -15.062 20.580  -45.302 1.00 46.91  ? 467 HOH A O     1 
HETATM 1980 O  O     . HOH H 7 .   ? 0.000   0.000   -26.507 0.33 44.08  ? 468 HOH A O     1 
HETATM 1981 O  O     . HOH H 7 .   ? -30.540 -5.725  -23.156 1.00 42.89  ? 469 HOH A O     1 
HETATM 1982 O  O     . HOH H 7 .   ? -6.678  6.349   -20.571 1.00 36.07  ? 470 HOH A O     1 
HETATM 1983 O  O     . HOH H 7 .   ? -30.406 -8.943  -22.828 1.00 61.69  ? 471 HOH A O     1 
HETATM 1984 O  O     . HOH H 7 .   ? -12.341 2.769   -45.236 1.00 48.55  ? 472 HOH A O     1 
HETATM 1985 O  O     . HOH H 7 .   ? -11.676 27.331  -49.774 1.00 56.84  ? 473 HOH A O     1 
HETATM 1986 O  O     . HOH H 7 .   ? -0.010  0.011   -28.768 0.33 30.22  ? 474 HOH A O     1 
HETATM 1987 O  O     . HOH H 7 .   ? -4.694  5.693   -20.057 1.00 46.30  ? 475 HOH A O     1 
HETATM 1988 O  O     . HOH H 7 .   ? -11.968 13.127  -50.820 1.00 54.61  ? 476 HOH A O     1 
HETATM 1989 O  O     . HOH H 7 .   ? -0.652  21.807  -34.048 1.00 46.76  ? 477 HOH A O     1 
HETATM 1990 O  O     . HOH H 7 .   ? -15.252 1.223   -20.018 1.00 47.66  ? 478 HOH A O     1 
HETATM 1991 O  O     . HOH H 7 .   ? -4.011  2.944   -38.934 1.00 44.09  ? 479 HOH A O     1 
HETATM 1992 O  O     . HOH H 7 .   ? -30.960 -9.890  -24.820 1.00 53.13  ? 480 HOH A O     1 
HETATM 1993 O  O     . HOH H 7 .   ? 0.082   8.428   -32.042 1.00 39.57  ? 481 HOH A O     1 
HETATM 1994 O  O     . HOH H 7 .   ? -12.391 3.055   -21.553 1.00 49.71  ? 482 HOH A O     1 
HETATM 1995 O  O     . HOH H 7 .   ? -17.487 0.647   -19.820 1.00 54.06  ? 483 HOH A O     1 
HETATM 1996 O  O     . HOH H 7 .   ? -6.745  11.577  -41.266 1.00 51.97  ? 484 HOH A O     1 
HETATM 1997 O  O     . HOH H 7 .   ? -4.013  17.667  -31.915 1.00 36.02  ? 485 HOH A O     1 
HETATM 1998 O  O     . HOH H 7 .   ? -33.877 -9.778  -31.310 1.00 58.15  ? 486 HOH A O     1 
HETATM 1999 O  O     . HOH H 7 .   ? -24.826 8.384   -16.485 1.00 49.98  ? 487 HOH A O     1 
HETATM 2000 O  O     . HOH H 7 .   ? -2.639  38.912  -30.190 1.00 51.63  ? 488 HOH A O     1 
HETATM 2001 O  O     . HOH H 7 .   ? -10.248 5.125   -16.473 1.00 51.40  ? 489 HOH A O     1 
HETATM 2002 O  O     . HOH H 7 .   ? -4.480  27.012  -18.507 1.00 52.73  ? 490 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   . GLU A 2   ? 1.2174 1.1493 1.0513 0.1234  0.1064  0.1758  2   GLU A N   
2    C CA  . GLU A 2   ? 1.2170 1.1510 1.0738 0.1155  0.0899  0.1564  2   GLU A CA  
3    C C   . GLU A 2   ? 1.2139 1.1378 1.1063 0.1097  0.0898  0.1625  2   GLU A C   
4    O O   . GLU A 2   ? 1.0262 0.9514 0.9348 0.1054  0.0767  0.1492  2   GLU A O   
5    C CB  . GLU A 2   ? 1.2171 1.1589 1.0487 0.1235  0.0707  0.1454  2   GLU A CB  
6    C CG  . GLU A 2   ? 1.2585 1.2113 1.0680 0.1248  0.0670  0.1290  2   GLU A CG  
7    C CD  . GLU A 2   ? 1.2931 1.2537 1.1058 0.1228  0.0478  0.1076  2   GLU A CD  
8    O OE1 . GLU A 2   ? 1.2408 1.2005 1.0591 0.1255  0.0349  0.1073  2   GLU A OE1 
9    O OE2 . GLU A 2   ? 1.2799 1.2470 1.0934 0.1181  0.0464  0.0916  2   GLU A OE2 
10   N N   . GLU A 3   ? 1.1785 1.0923 1.0857 0.1091  0.1053  0.1817  3   GLU A N   
11   C CA  . GLU A 3   ? 1.0229 0.9267 0.9700 0.1019  0.1073  0.1849  3   GLU A CA  
12   C C   . GLU A 3   ? 0.9224 0.8233 0.8994 0.0913  0.1230  0.1856  3   GLU A C   
13   O O   . GLU A 3   ? 0.9003 0.7915 0.9108 0.0861  0.1290  0.1920  3   GLU A O   
14   C CB  . GLU A 3   ? 1.0946 0.9873 1.0411 0.1108  0.1092  0.2069  3   GLU A CB  
15   C CG  . GLU A 3   ? 1.1065 0.9932 1.0392 0.1174  0.1278  0.2328  3   GLU A CG  
16   C CD  . GLU A 3   ? 1.1281 1.0007 1.0734 0.1233  0.1333  0.2569  3   GLU A CD  
17   O OE1 . GLU A 3   ? 1.0866 0.9494 1.0603 0.1182  0.1501  0.2706  3   GLU A OE1 
18   O OE2 . GLU A 3   ? 1.1543 1.0257 1.0836 0.1332  0.1206  0.2622  3   GLU A OE2 
19   N N   . LYS A 4   ? 0.8380 0.7474 0.8060 0.0880  0.1293  0.1780  4   LYS A N   
20   C CA  . LYS A 4   ? 0.7394 0.6499 0.7403 0.0764  0.1379  0.1705  4   LYS A CA  
21   C C   . LYS A 4   ? 0.6070 0.5212 0.6291 0.0674  0.1234  0.1484  4   LYS A C   
22   O O   . LYS A 4   ? 0.5871 0.5054 0.5948 0.0700  0.1086  0.1376  4   LYS A O   
23   C CB  . LYS A 4   ? 0.7081 0.6278 0.6953 0.0759  0.1470  0.1670  4   LYS A CB  
24   C CG  . LYS A 4   ? 0.7106 0.6409 0.6670 0.0798  0.1345  0.1513  4   LYS A CG  
25   C CD  . LYS A 4   ? 0.7711 0.7101 0.7372 0.0729  0.1369  0.1370  4   LYS A CD  
26   C CE  . LYS A 4   ? 0.8322 0.7731 0.7986 0.0738  0.1566  0.1473  4   LYS A CE  
27   N NZ  . LYS A 4   ? 0.8678 0.8138 0.7923 0.0848  0.1604  0.1510  4   LYS A NZ  
28   N N   . LYS A 5   ? 0.5398 0.4535 0.5964 0.0572  0.1280  0.1417  5   LYS A N   
29   C CA  . LYS A 5   ? 0.5153 0.4327 0.5912 0.0491  0.1157  0.1218  5   LYS A CA  
30   C C   . LYS A 5   ? 0.4708 0.4001 0.5276 0.0482  0.1076  0.1067  5   LYS A C   
31   O O   . LYS A 5   ? 0.4665 0.4016 0.5199 0.0470  0.1149  0.1063  5   LYS A O   
32   C CB  . LYS A 5   ? 0.5368 0.4517 0.6535 0.0392  0.1221  0.1182  5   LYS A CB  
33   C CG  . LYS A 5   ? 0.5791 0.4813 0.7232 0.0385  0.1292  0.1304  5   LYS A CG  
34   C CD  . LYS A 5   ? 0.5962 0.4971 0.7831 0.0283  0.1331  0.1229  5   LYS A CD  
35   C CE  . LYS A 5   ? 0.6752 0.5634 0.8940 0.0266  0.1354  0.1283  5   LYS A CE  
36   N NZ  . LYS A 5   ? 0.7198 0.6069 0.9829 0.0168  0.1410  0.1220  5   LYS A NZ  
37   N N   . ARG A 6   ? 0.4218 0.3545 0.4697 0.0487  0.0931  0.0947  6   ARG A N   
38   C CA  . ARG A 6   ? 0.4297 0.3723 0.4649 0.0471  0.0844  0.0801  6   ARG A CA  
39   C C   . ARG A 6   ? 0.3965 0.3415 0.4458 0.0414  0.0729  0.0653  6   ARG A C   
40   O O   . ARG A 6   ? 0.3898 0.3302 0.4452 0.0425  0.0677  0.0651  6   ARG A O   
41   C CB  . ARG A 6   ? 0.4493 0.3953 0.4515 0.0558  0.0784  0.0808  6   ARG A CB  
42   C CG  . ARG A 6   ? 0.4683 0.4141 0.4482 0.0633  0.0884  0.0933  6   ARG A CG  
43   C CD  . ARG A 6   ? 0.4722 0.4261 0.4240 0.0686  0.0808  0.0843  6   ARG A CD  
44   N NE  . ARG A 6   ? 0.5254 0.4796 0.4492 0.0782  0.0885  0.0952  6   ARG A NE  
45   C CZ  . ARG A 6   ? 0.5331 0.4822 0.4405 0.0868  0.0899  0.1095  6   ARG A CZ  
46   N NH1 . ARG A 6   ? 0.5575 0.5015 0.4722 0.0879  0.0812  0.1124  6   ARG A NH1 
47   N NH2 . ARG A 6   ? 0.5598 0.5094 0.4418 0.0951  0.0997  0.1208  6   ARG A NH2 
48   N N   . LEU A 7   ? 0.3522 0.3049 0.4045 0.0362  0.0690  0.0535  7   LEU A N   
49   C CA  . LEU A 7   ? 0.3279 0.2849 0.3871 0.0318  0.0588  0.0400  7   LEU A CA  
50   C C   . LEU A 7   ? 0.3270 0.2881 0.3647 0.0364  0.0503  0.0357  7   LEU A C   
51   O O   . LEU A 7   ? 0.3293 0.2936 0.3500 0.0401  0.0511  0.0372  7   LEU A O   
52   C CB  . LEU A 7   ? 0.3169 0.2804 0.3879 0.0252  0.0582  0.0314  7   LEU A CB  
53   C CG  . LEU A 7   ? 0.3015 0.2709 0.3740 0.0215  0.0482  0.0186  7   LEU A CG  
54   C CD1 . LEU A 7   ? 0.3062 0.2724 0.3925 0.0191  0.0447  0.0135  7   LEU A CD1 
55   C CD2 . LEU A 7   ? 0.3183 0.2945 0.3998 0.0167  0.0473  0.0127  7   LEU A CD2 
56   N N   . HIS A 8   ? 0.3296 0.2907 0.3706 0.0362  0.0427  0.0299  8   HIS A N   
57   C CA  . HIS A 8   ? 0.3019 0.2676 0.3300 0.0393  0.0342  0.0243  8   HIS A CA  
58   C C   . HIS A 8   ? 0.2740 0.2455 0.3106 0.0333  0.0296  0.0129  8   HIS A C   
59   O O   . HIS A 8   ? 0.2914 0.2618 0.3413 0.0302  0.0290  0.0086  8   HIS A O   
60   C CB  . HIS A 8   ? 0.3197 0.2811 0.3476 0.0446  0.0309  0.0286  8   HIS A CB  
61   C CG  . HIS A 8   ? 0.3465 0.3028 0.3614 0.0519  0.0346  0.0415  8   HIS A CG  
62   N ND1 . HIS A 8   ? 0.3810 0.3401 0.3762 0.0594  0.0288  0.0436  8   HIS A ND1 
63   C CD2 . HIS A 8   ? 0.3538 0.3032 0.3720 0.0532  0.0438  0.0533  8   HIS A CD2 
64   C CE1 . HIS A 8   ? 0.3850 0.3390 0.3684 0.0658  0.0341  0.0567  8   HIS A CE1 
65   N NE2 . HIS A 8   ? 0.3747 0.3226 0.3723 0.0619  0.0442  0.0636  8   HIS A NE2 
66   N N   . LEU A 9   ? 0.2469 0.2244 0.2762 0.0320  0.0275  0.0084  9   LEU A N   
67   C CA  . LEU A 9   ? 0.2494 0.2325 0.2845 0.0268  0.0243  0.0004  9   LEU A CA  
68   C C   . LEU A 9   ? 0.2391 0.2267 0.2684 0.0282  0.0183  -0.0044 9   LEU A C   
69   O O   . LEU A 9   ? 0.2603 0.2491 0.2803 0.0315  0.0162  -0.0040 9   LEU A O   
70   C CB  . LEU A 9   ? 0.2629 0.2487 0.2983 0.0244  0.0269  0.0005  9   LEU A CB  
71   C CG  . LEU A 9   ? 0.2616 0.2535 0.2998 0.0205  0.0230  -0.0056 9   LEU A CG  
72   C CD1 . LEU A 9   ? 0.2734 0.2668 0.3218 0.0164  0.0218  -0.0097 9   LEU A CD1 
73   C CD2 . LEU A 9   ? 0.2714 0.2657 0.3101 0.0199  0.0251  -0.0045 9   LEU A CD2 
74   N N   . ILE A 10  ? 0.2506 0.2411 0.2864 0.0256  0.0161  -0.0096 10  ILE A N   
75   C CA  . ILE A 10  ? 0.2474 0.2423 0.2822 0.0264  0.0120  -0.0135 10  ILE A CA  
76   C C   . ILE A 10  ? 0.2314 0.2316 0.2688 0.0218  0.0122  -0.0172 10  ILE A C   
77   O O   . ILE A 10  ? 0.1968 0.1981 0.2379 0.0191  0.0137  -0.0197 10  ILE A O   
78   C CB  . ILE A 10  ? 0.2711 0.2653 0.3120 0.0287  0.0106  -0.0150 10  ILE A CB  
79   C CG1 . ILE A 10  ? 0.2989 0.2873 0.3368 0.0342  0.0100  -0.0092 10  ILE A CG1 
80   C CG2 . ILE A 10  ? 0.2777 0.2779 0.3216 0.0289  0.0073  -0.0192 10  ILE A CG2 
81   C CD1 . ILE A 10  ? 0.3371 0.3241 0.3843 0.0370  0.0084  -0.0101 10  ILE A CD1 
82   N N   . ILE A 11  ? 0.2622 0.2655 0.2975 0.0214  0.0105  -0.0175 11  ILE A N   
83   C CA  . ILE A 11  ? 0.2719 0.2798 0.3096 0.0179  0.0110  -0.0188 11  ILE A CA  
84   C C   . ILE A 11  ? 0.2653 0.2767 0.3083 0.0182  0.0107  -0.0213 11  ILE A C   
85   O O   . ILE A 11  ? 0.2401 0.2519 0.2862 0.0202  0.0080  -0.0221 11  ILE A O   
86   C CB  . ILE A 11  ? 0.2624 0.2710 0.2997 0.0174  0.0099  -0.0172 11  ILE A CB  
87   C CG1 . ILE A 11  ? 0.2861 0.2918 0.3201 0.0183  0.0109  -0.0152 11  ILE A CG1 
88   C CG2 . ILE A 11  ? 0.2292 0.2419 0.2693 0.0143  0.0108  -0.0158 11  ILE A CG2 
89   C CD1 . ILE A 11  ? 0.3004 0.3060 0.3358 0.0161  0.0128  -0.0142 11  ILE A CD1 
90   N N   . ALA A 12  ? 0.2735 0.2880 0.3181 0.0166  0.0134  -0.0233 12  ALA A N   
91   C CA  . ALA A 12  ? 0.2857 0.3033 0.3375 0.0177  0.0145  -0.0261 12  ALA A CA  
92   C C   . ALA A 12  ? 0.2835 0.3073 0.3377 0.0152  0.0185  -0.0255 12  ALA A C   
93   O O   . ALA A 12  ? 0.2491 0.2745 0.2967 0.0130  0.0202  -0.0229 12  ALA A O   
94   C CB  . ALA A 12  ? 0.2827 0.2989 0.3369 0.0192  0.0159  -0.0297 12  ALA A CB  
95   N N   . ASP A 13  ? 0.2711 0.2988 0.3360 0.0159  0.0201  -0.0274 13  ASP A N   
96   C CA  . ASP A 13  ? 0.2603 0.2939 0.3310 0.0137  0.0257  -0.0255 13  ASP A CA  
97   C C   . ASP A 13  ? 0.2629 0.2958 0.3314 0.0113  0.0255  -0.0196 13  ASP A C   
98   O O   . ASP A 13  ? 0.2762 0.3123 0.3407 0.0096  0.0306  -0.0151 13  ASP A O   
99   C CB  . ASP A 13  ? 0.2765 0.3146 0.3408 0.0134  0.0323  -0.0272 13  ASP A CB  
100  C CG  . ASP A 13  ? 0.3037 0.3426 0.3741 0.0159  0.0335  -0.0339 13  ASP A CG  
101  O OD1 . ASP A 13  ? 0.3319 0.3714 0.4168 0.0177  0.0315  -0.0355 13  ASP A OD1 
102  O OD2 . ASP A 13  ? 0.3195 0.3587 0.3817 0.0164  0.0358  -0.0382 13  ASP A OD2 
103  N N   . ALA A 14  ? 0.2648 0.2934 0.3358 0.0120  0.0197  -0.0196 14  ALA A N   
104  C CA  . ALA A 14  ? 0.2885 0.3150 0.3592 0.0104  0.0187  -0.0152 14  ALA A CA  
105  C C   . ALA A 14  ? 0.2905 0.3200 0.3763 0.0081  0.0223  -0.0121 14  ALA A C   
106  O O   . ALA A 14  ? 0.2636 0.2956 0.3637 0.0083  0.0217  -0.0159 14  ALA A O   
107  C CB  . ALA A 14  ? 0.2770 0.2987 0.3465 0.0123  0.0125  -0.0179 14  ALA A CB  
108  N N   . GLU A 15  ? 0.2821 0.3115 0.3663 0.0063  0.0256  -0.0048 15  GLU A N   
109  C CA  . GLU A 15  ? 0.2803 0.3111 0.3800 0.0038  0.0304  0.0012  15  GLU A CA  
110  C C   . GLU A 15  ? 0.2576 0.2838 0.3724 0.0035  0.0251  -0.0015 15  GLU A C   
111  O O   . GLU A 15  ? 0.2541 0.2771 0.3735 0.0025  0.0257  0.0042  15  GLU A O   
112  C CB  . GLU A 15  ? 0.3039 0.3359 0.3926 0.0032  0.0357  0.0115  15  GLU A CB  
113  C CG  . GLU A 15  ? 0.3244 0.3617 0.3955 0.0043  0.0401  0.0118  15  GLU A CG  
114  C CD  . GLU A 15  ? 0.3689 0.4122 0.4477 0.0037  0.0483  0.0110  15  GLU A CD  
115  O OE1 . GLU A 15  ? 0.4955 0.5434 0.5609 0.0052  0.0523  0.0087  15  GLU A OE1 
116  O OE2 . GLU A 15  ? 0.3779 0.4216 0.4777 0.0019  0.0508  0.0119  15  GLU A OE2 
117  N N   . LEU A 16  ? 0.2785 0.3045 0.4002 0.0050  0.0191  -0.0109 16  LEU A N   
118  C CA  . LEU A 16  ? 0.2759 0.2988 0.4105 0.0056  0.0125  -0.0174 16  LEU A CA  
119  C C   . LEU A 16  ? 0.2765 0.3035 0.4327 0.0050  0.0103  -0.0239 16  LEU A C   
120  O O   . LEU A 16  ? 0.2798 0.3098 0.4324 0.0075  0.0065  -0.0295 16  LEU A O   
121  C CB  . LEU A 16  ? 0.2845 0.3044 0.4022 0.0096  0.0058  -0.0236 16  LEU A CB  
122  C CG  . LEU A 16  ? 0.2881 0.3056 0.4127 0.0118  -0.0016 -0.0324 16  LEU A CG  
123  C CD1 . LEU A 16  ? 0.3254 0.3386 0.4589 0.0102  -0.0002 -0.0301 16  LEU A CD1 
124  C CD2 . LEU A 16  ? 0.2799 0.2957 0.3846 0.0166  -0.0064 -0.0371 16  LEU A CD2 
125  N N   . GLU A 17  ? 0.2973 0.3243 0.4782 0.0018  0.0123  -0.0228 17  GLU A N   
126  C CA  . GLU A 17  ? 0.2649 0.2969 0.4729 0.0002  0.0111  -0.0285 17  GLU A CA  
127  C C   . GLU A 17  ? 0.2561 0.2851 0.4918 -0.0031 0.0113  -0.0289 17  GLU A C   
128  O O   . GLU A 17  ? 0.2446 0.2681 0.4778 -0.0045 0.0157  -0.0208 17  GLU A O   
129  C CB  . GLU A 17  ? 0.2794 0.3177 0.4929 -0.0019 0.0213  -0.0215 17  GLU A CB  
130  C CG  . GLU A 17  ? 0.2841 0.3212 0.4975 -0.0052 0.0335  -0.0074 17  GLU A CG  
131  C CD  . GLU A 17  ? 0.2896 0.3334 0.5018 -0.0063 0.0451  -0.0003 17  GLU A CD  
132  O OE1 . GLU A 17  ? 0.3010 0.3445 0.4950 -0.0063 0.0530  0.0102  17  GLU A OE1 
133  O OE2 . GLU A 17  ? 0.3045 0.3546 0.5344 -0.0066 0.0462  -0.0057 17  GLU A OE2 
134  N N   . THR A 18  ? 0.2496 0.2823 0.5137 -0.0041 0.0061  -0.0386 18  THR A N   
135  C CA  . THR A 18  ? 0.2543 0.2845 0.5525 -0.0083 0.0075  -0.0392 18  THR A CA  
136  C C   . THR A 18  ? 0.2406 0.2728 0.5563 -0.0132 0.0222  -0.0245 18  THR A C   
137  O O   . THR A 18  ? 0.2605 0.2981 0.5650 -0.0132 0.0300  -0.0176 18  THR A O   
138  C CB  . THR A 18  ? 0.2541 0.2882 0.5795 -0.0078 -0.0043 -0.0563 18  THR A CB  
139  O OG1 . THR A 18  ? 0.2661 0.3091 0.5958 -0.0070 -0.0051 -0.0590 18  THR A OG1 
140  C CG2 . THR A 18  ? 0.2611 0.2929 0.5695 -0.0023 -0.0183 -0.0707 18  THR A CG2 
141  N N   . VAL A 19  ? 0.2619 0.2902 0.6077 -0.0174 0.0268  -0.0200 19  VAL A N   
142  C CA  . VAL A 19  ? 0.2858 0.3159 0.6498 -0.0218 0.0422  -0.0044 19  VAL A CA  
143  C C   . VAL A 19  ? 0.2967 0.3374 0.6721 -0.0228 0.0465  -0.0069 19  VAL A C   
144  O O   . VAL A 19  ? 0.3238 0.3695 0.7229 -0.0230 0.0377  -0.0211 19  VAL A O   
145  C CB  . VAL A 19  ? 0.2886 0.3131 0.6938 -0.0265 0.0454  -0.0015 19  VAL A CB  
146  C CG1 . VAL A 19  ? 0.3122 0.3387 0.7354 -0.0308 0.0634  0.0174  19  VAL A CG1 
147  C CG2 . VAL A 19  ? 0.3032 0.3171 0.6995 -0.0249 0.0415  0.0009  19  VAL A CG2 
148  N N   . PRO A 20  ? 0.3009 0.3460 0.6583 -0.0226 0.0593  0.0056  20  PRO A N   
149  C CA  . PRO A 20  ? 0.3160 0.3715 0.6853 -0.0232 0.0658  0.0040  20  PRO A CA  
150  C C   . PRO A 20  ? 0.3311 0.3909 0.7515 -0.0285 0.0713  0.0034  20  PRO A C   
151  O O   . PRO A 20  ? 0.3356 0.3904 0.7784 -0.0326 0.0791  0.0134  20  PRO A O   
152  C CB  . PRO A 20  ? 0.3149 0.3726 0.6551 -0.0220 0.0805  0.0191  20  PRO A CB  
153  C CG  . PRO A 20  ? 0.3210 0.3709 0.6235 -0.0187 0.0737  0.0213  20  PRO A CG  
154  C CD  . PRO A 20  ? 0.3153 0.3567 0.6370 -0.0207 0.0667  0.0198  20  PRO A CD  
155  N N   . PRO A 21  ? 0.3479 0.4170 0.7905 -0.0283 0.0662  -0.0090 21  PRO A N   
156  C CA  . PRO A 21  ? 0.3632 0.4385 0.8592 -0.0334 0.0706  -0.0116 21  PRO A CA  
157  C C   . PRO A 21  ? 0.3985 0.4758 0.9118 -0.0381 0.0937  0.0077  21  PRO A C   
158  O O   . PRO A 21  ? 0.4166 0.4933 0.9737 -0.0436 0.0996  0.0111  21  PRO A O   
159  C CB  . PRO A 21  ? 0.3282 0.4147 0.8341 -0.0305 0.0621  -0.0260 21  PRO A CB  
160  C CG  . PRO A 21  ? 0.3246 0.4076 0.7871 -0.0238 0.0469  -0.0349 21  PRO A CG  
161  C CD  . PRO A 21  ? 0.3264 0.4002 0.7469 -0.0227 0.0543  -0.0216 21  PRO A CD  
162  N N   . GLU A 22  ? 0.4658 0.5450 0.9442 -0.0356 0.1071  0.0207  22  GLU A N   
163  C CA  . GLU A 22  ? 0.4646 0.5470 0.9528 -0.0387 0.1302  0.0399  22  GLU A CA  
164  C C   . GLU A 22  ? 0.4548 0.5269 0.9525 -0.0421 0.1371  0.0556  22  GLU A C   
165  O O   . GLU A 22  ? 0.4567 0.5308 0.9751 -0.0455 0.1559  0.0719  22  GLU A O   
166  C CB  . GLU A 22  ? 0.5100 0.5953 0.9505 -0.0342 0.1413  0.0500  22  GLU A CB  
167  C CG  . GLU A 22  ? 0.5176 0.6119 0.9440 -0.0300 0.1372  0.0370  22  GLU A CG  
168  C CD  . GLU A 22  ? 0.5120 0.6010 0.9003 -0.0249 0.1189  0.0254  22  GLU A CD  
169  O OE1 . GLU A 22  ? 0.6258 0.7184 0.9829 -0.0206 0.1212  0.0236  22  GLU A OE1 
170  O OE2 . GLU A 22  ? 0.4354 0.5171 0.8268 -0.0252 0.1031  0.0177  22  GLU A OE2 
171  N N   . ILE A 23  ? 0.4806 0.5417 0.9612 -0.0405 0.1234  0.0524  23  ILE A N   
172  C CA  . ILE A 23  ? 0.4562 0.5067 0.9410 -0.0425 0.1299  0.0688  23  ILE A CA  
173  C C   . ILE A 23  ? 0.4630 0.5048 0.9830 -0.0454 0.1167  0.0579  23  ILE A C   
174  O O   . ILE A 23  ? 0.4820 0.5134 1.0043 -0.0461 0.1186  0.0687  23  ILE A O   
175  C CB  . ILE A 23  ? 0.4511 0.4965 0.8812 -0.0371 0.1289  0.0785  23  ILE A CB  
176  C CG1 . ILE A 23  ? 0.4032 0.4445 0.8076 -0.0331 0.1083  0.0611  23  ILE A CG1 
177  C CG2 . ILE A 23  ? 0.4734 0.5277 0.8713 -0.0341 0.1424  0.0880  23  ILE A CG2 
178  C CD1 . ILE A 23  ? 0.4060 0.4421 0.7652 -0.0286 0.1062  0.0695  23  ILE A CD1 
179  N N   . LEU A 24  ? 0.4753 0.5216 1.0229 -0.0467 0.1031  0.0363  24  LEU A N   
180  C CA  . LEU A 24  ? 0.4911 0.5301 1.0683 -0.0485 0.0885  0.0220  24  LEU A CA  
181  C C   . LEU A 24  ? 0.5722 0.6044 1.1976 -0.0548 0.0998  0.0340  24  LEU A C   
182  O O   . LEU A 24  ? 0.6506 0.6728 1.2923 -0.0556 0.0910  0.0279  24  LEU A O   
183  C CB  . LEU A 24  ? 0.4681 0.5155 1.0683 -0.0483 0.0724  -0.0030 24  LEU A CB  
184  C CG  . LEU A 24  ? 0.4711 0.5206 1.0292 -0.0414 0.0547  -0.0190 24  LEU A CG  
185  C CD1 . LEU A 24  ? 0.4510 0.5094 1.0348 -0.0407 0.0390  -0.0414 24  LEU A CD1 
186  C CD2 . LEU A 24  ? 0.4541 0.4922 0.9869 -0.0382 0.0443  -0.0230 24  LEU A CD2 
187  N N   . ASP A 25  ? 0.5926 0.6297 1.2423 -0.0590 0.1198  0.0509  25  ASP A N   
188  C CA  . ASP A 25  ? 0.6655 0.6950 1.3616 -0.0650 0.1326  0.0658  25  ASP A CA  
189  C C   . ASP A 25  ? 0.6765 0.7012 1.3465 -0.0637 0.1531  0.0968  25  ASP A C   
190  O O   . ASP A 25  ? 0.7477 0.7692 1.4529 -0.0683 0.1703  0.1155  25  ASP A O   
191  C CB  . ASP A 25  ? 0.6894 0.7266 1.4505 -0.0719 0.1376  0.0586  25  ASP A CB  
192  C CG  . ASP A 25  ? 0.7676 0.8205 1.5289 -0.0722 0.1478  0.0593  25  ASP A CG  
193  O OD1 . ASP A 25  ? 0.7980 0.8547 1.5130 -0.0680 0.1587  0.0729  25  ASP A OD1 
194  O OD2 . ASP A 25  ? 0.7531 0.8150 1.5630 -0.0763 0.1441  0.0449  25  ASP A OD2 
195  N N   . HIS A 26  ? 0.6652 0.6892 1.2747 -0.0572 0.1506  0.1026  26  HIS A N   
196  C CA  . HIS A 26  ? 0.7290 0.7475 1.3091 -0.0544 0.1648  0.1298  26  HIS A CA  
197  C C   . HIS A 26  ? 0.7433 0.7466 1.3371 -0.0546 0.1589  0.1358  26  HIS A C   
198  O O   . HIS A 26  ? 0.6646 0.6626 1.2531 -0.0527 0.1403  0.1174  26  HIS A O   
199  C CB  . HIS A 26  ? 0.7894 0.8136 1.3041 -0.0474 0.1624  0.1311  26  HIS A CB  
200  C CG  . HIS A 26  ? 0.8682 0.8892 1.3483 -0.0435 0.1751  0.1574  26  HIS A CG  
201  N ND1 . HIS A 26  ? 0.8839 0.8929 1.3583 -0.0415 0.1716  0.1695  26  HIS A ND1 
202  C CD2 . HIS A 26  ? 0.9051 0.9340 1.3543 -0.0405 0.1909  0.1735  26  HIS A CD2 
203  C CE1 . HIS A 26  ? 0.8804 0.8904 1.3214 -0.0373 0.1839  0.1932  26  HIS A CE1 
204  N NE2 . HIS A 26  ? 0.9125 0.9346 1.3362 -0.0365 0.1958  0.1955  26  HIS A NE2 
205  N N   . PRO A 27  ? 0.8120 0.8077 1.4245 -0.0564 0.1752  0.1620  27  PRO A N   
206  C CA  . PRO A 27  ? 0.7876 0.7681 1.4237 -0.0569 0.1711  0.1687  27  PRO A CA  
207  C C   . PRO A 27  ? 0.7692 0.7427 1.3743 -0.0515 0.1516  0.1562  27  PRO A C   
208  O O   . PRO A 27  ? 0.7346 0.7004 1.3695 -0.0532 0.1388  0.1390  27  PRO A O   
209  C CB  . PRO A 27  ? 0.8827 0.8594 1.5083 -0.0552 0.1918  0.2045  27  PRO A CB  
210  C CG  . PRO A 27  ? 0.9148 0.9033 1.5543 -0.0589 0.2113  0.2134  27  PRO A CG  
211  C CD  . PRO A 27  ? 0.8791 0.8808 1.4941 -0.0577 0.1998  0.1875  27  PRO A CD  
212  N N   . ALA A 28  ? 0.7773 0.7541 1.3242 -0.0449 0.1498  0.1635  28  ALA A N   
213  C CA  . ALA A 28  ? 0.8090 0.7801 1.3256 -0.0395 0.1337  0.1550  28  ALA A CA  
214  C C   . ALA A 28  ? 0.8181 0.7914 1.3372 -0.0398 0.1151  0.1227  28  ALA A C   
215  O O   . ALA A 28  ? 0.8656 0.8327 1.3740 -0.0364 0.1021  0.1123  28  ALA A O   
216  C CB  . ALA A 28  ? 0.8021 0.7789 1.2591 -0.0330 0.1354  0.1670  28  ALA A CB  
217  N N   . ILE A 29  ? 0.7704 0.7531 1.3036 -0.0432 0.1145  0.1078  29  ILE A N   
218  C CA  . ILE A 29  ? 0.7015 0.6882 1.2361 -0.0429 0.0973  0.0785  29  ILE A CA  
219  C C   . ILE A 29  ? 0.6203 0.6012 1.2112 -0.0476 0.0909  0.0637  29  ILE A C   
220  O O   . ILE A 29  ? 0.5539 0.5319 1.1469 -0.0457 0.0750  0.0423  29  ILE A O   
221  C CB  . ILE A 29  ? 0.6502 0.6506 1.1699 -0.0430 0.0984  0.0702  29  ILE A CB  
222  C CG1 . ILE A 29  ? 0.6164 0.6226 1.0825 -0.0383 0.1045  0.0824  29  ILE A CG1 
223  C CG2 . ILE A 29  ? 0.6182 0.6228 1.1407 -0.0419 0.0801  0.0417  29  ILE A CG2 
224  C CD1 . ILE A 29  ? 0.6305 0.6346 1.0530 -0.0326 0.0910  0.0736  29  ILE A CD1 
225  N N   . VAL A 30  ? 0.6224 0.6023 1.2603 -0.0536 0.1037  0.0744  30  VAL A N   
226  C CA  . VAL A 30  ? 0.6637 0.6382 1.3605 -0.0587 0.0976  0.0596  30  VAL A CA  
227  C C   . VAL A 30  ? 0.6619 0.6215 1.3690 -0.0569 0.0920  0.0601  30  VAL A C   
228  O O   . VAL A 30  ? 0.6538 0.6092 1.3920 -0.0581 0.0790  0.0376  30  VAL A O   
229  C CB  . VAL A 30  ? 0.6882 0.6646 1.4391 -0.0662 0.1139  0.0719  30  VAL A CB  
230  C CG1 . VAL A 30  ? 0.6900 0.6627 1.5042 -0.0716 0.1043  0.0507  30  VAL A CG1 
231  C CG2 . VAL A 30  ? 0.6729 0.6644 1.4132 -0.0673 0.1226  0.0745  30  VAL A CG2 
232  N N   . ASN A 31  ? 0.6761 0.6286 1.3565 -0.0534 0.1005  0.0841  31  ASN A N   
233  C CA  . ASN A 31  ? 0.7347 0.6727 1.4294 -0.0515 0.0975  0.0887  31  ASN A CA  
234  C C   . ASN A 31  ? 0.7132 0.6501 1.3676 -0.0448 0.0816  0.0727  31  ASN A C   
235  O O   . ASN A 31  ? 0.7749 0.7031 1.4499 -0.0436 0.0721  0.0585  31  ASN A O   
236  C CB  . ASN A 31  ? 0.7931 0.7235 1.4836 -0.0503 0.1137  0.1238  31  ASN A CB  
237  C CG  . ASN A 31  ? 0.8657 0.7956 1.5992 -0.0568 0.1323  0.1432  31  ASN A CG  
238  O OD1 . ASN A 31  ? 0.7801 0.7101 1.5649 -0.0632 0.1319  0.1295  31  ASN A OD1 
239  N ND2 . ASN A 31  ? 0.9019 0.8325 1.6137 -0.0550 0.1490  0.1745  31  ASN A ND2 
240  N N   . TYR A 32  ? 0.6648 0.6105 1.2638 -0.0403 0.0798  0.0752  32  TYR A N   
241  C CA  . TYR A 32  ? 0.5768 0.5240 1.1409 -0.0347 0.0649  0.0565  32  TYR A CA  
242  C C   . TYR A 32  ? 0.6082 0.5572 1.1965 -0.0362 0.0514  0.0256  32  TYR A C   
243  O O   . TYR A 32  ? 0.5814 0.5240 1.1772 -0.0336 0.0413  0.0099  32  TYR A O   
244  C CB  . TYR A 32  ? 0.5279 0.4856 1.0369 -0.0311 0.0653  0.0608  32  TYR A CB  
245  C CG  . TYR A 32  ? 0.5045 0.4634 0.9769 -0.0254 0.0521  0.0454  32  TYR A CG  
246  C CD1 . TYR A 32  ? 0.5215 0.4755 0.9703 -0.0207 0.0511  0.0553  32  TYR A CD1 
247  C CD2 . TYR A 32  ? 0.5014 0.4664 0.9658 -0.0245 0.0407  0.0211  32  TYR A CD2 
248  C CE1 . TYR A 32  ? 0.5400 0.4956 0.9595 -0.0159 0.0407  0.0414  32  TYR A CE1 
249  C CE2 . TYR A 32  ? 0.5039 0.4696 0.9366 -0.0192 0.0305  0.0082  32  TYR A CE2 
250  C CZ  . TYR A 32  ? 0.5315 0.4926 0.9426 -0.0152 0.0312  0.0182  32  TYR A CZ  
251  O OH  . TYR A 32  ? 0.5681 0.5311 0.9503 -0.0104 0.0225  0.0052  32  TYR A OH  
252  N N   . ALA A 33  ? 0.6041 0.5622 1.2073 -0.0401 0.0515  0.0169  33  ALA A N   
253  C CA  . ALA A 33  ? 0.6264 0.5898 1.2425 -0.0401 0.0365  -0.0130 33  ALA A CA  
254  C C   . ALA A 33  ? 0.6683 0.6223 1.3332 -0.0422 0.0299  -0.0282 33  ALA A C   
255  O O   . ALA A 33  ? 0.6647 0.6180 1.3224 -0.0382 0.0156  -0.0516 33  ALA A O   
256  C CB  . ALA A 33  ? 0.5814 0.5566 1.2096 -0.0437 0.0384  -0.0169 33  ALA A CB  
257  N N   . LYS A 34  ? 0.7190 0.6660 1.4332 -0.0481 0.0408  -0.0150 34  LYS A N   
258  C CA  . LYS A 34  ? 0.7536 0.6900 1.5212 -0.0509 0.0364  -0.0273 34  LYS A CA  
259  C C   . LYS A 34  ? 0.7593 0.6848 1.5111 -0.0452 0.0315  -0.0293 34  LYS A C   
260  O O   . LYS A 34  ? 0.6483 0.5703 1.4145 -0.0429 0.0188  -0.0548 34  LYS A O   
261  C CB  . LYS A 34  ? 0.8445 0.7738 1.6644 -0.0580 0.0527  -0.0053 34  LYS A CB  
262  C CG  . LYS A 34  ? 0.9401 0.8575 1.8245 -0.0619 0.0492  -0.0176 34  LYS A CG  
263  C CD  . LYS A 34  ? 0.9795 0.8827 1.8990 -0.0652 0.0661  0.0118  34  LYS A CD  
264  C CE  . LYS A 34  ? 1.0425 0.9366 1.9251 -0.0586 0.0696  0.0309  34  LYS A CE  
265  N NZ  . LYS A 34  ? 1.0285 0.9145 1.9138 -0.0537 0.0555  0.0084  34  LYS A NZ  
266  N N   . ARG A 35  ? 0.7787 0.6998 1.5006 -0.0423 0.0416  -0.0030 35  ARG A N   
267  C CA  . ARG A 35  ? 0.8328 0.7444 1.5415 -0.0367 0.0383  -0.0017 35  ARG A CA  
268  C C   . ARG A 35  ? 0.7828 0.7000 1.4588 -0.0308 0.0229  -0.0296 35  ARG A C   
269  O O   . ARG A 35  ? 0.7932 0.7030 1.4812 -0.0275 0.0159  -0.0445 35  ARG A O   
270  C CB  . ARG A 35  ? 0.9009 0.8105 1.5756 -0.0335 0.0490  0.0298  35  ARG A CB  
271  C CG  . ARG A 35  ? 0.9823 0.8828 1.6907 -0.0371 0.0643  0.0592  35  ARG A CG  
272  C CD  . ARG A 35  ? 1.0749 0.9700 1.7566 -0.0318 0.0707  0.0867  35  ARG A CD  
273  N NE  . ARG A 35  ? 1.1203 1.0255 1.7398 -0.0266 0.0676  0.0905  35  ARG A NE  
274  C CZ  . ARG A 35  ? 1.0682 0.9823 1.6542 -0.0266 0.0759  0.1087  35  ARG A CZ  
275  N NH1 . ARG A 35  ? 0.9873 0.9086 1.5215 -0.0214 0.0719  0.1114  35  ARG A NH1 
276  N NH2 . ARG A 35  ? 0.9805 0.8965 1.5863 -0.0317 0.0886  0.1234  35  ARG A NH2 
277  N N   . ARG A 36  ? 0.7257 0.6555 1.3625 -0.0293 0.0180  -0.0372 36  ARG A N   
278  C CA  . ARG A 36  ? 0.6787 0.6137 1.2825 -0.0233 0.0049  -0.0610 36  ARG A CA  
279  C C   . ARG A 36  ? 0.6606 0.5999 1.2907 -0.0244 -0.0077 -0.0910 36  ARG A C   
280  O O   . ARG A 36  ? 0.6518 0.5962 1.2562 -0.0191 -0.0192 -0.1125 36  ARG A O   
281  C CB  . ARG A 36  ? 0.6973 0.6425 1.2453 -0.0202 0.0057  -0.0530 36  ARG A CB  
282  C CG  . ARG A 36  ? 0.7917 0.7347 1.3155 -0.0195 0.0171  -0.0242 36  ARG A CG  
283  C CD  . ARG A 36  ? 0.9182 0.8555 1.4214 -0.0138 0.0156  -0.0209 36  ARG A CD  
284  N NE  . ARG A 36  ? 1.0684 1.0043 1.5527 -0.0130 0.0250  0.0067  36  ARG A NE  
285  C CZ  . ARG A 36  ? 1.2216 1.1495 1.7308 -0.0149 0.0338  0.0278  36  ARG A CZ  
286  N NH1 . ARG A 36  ? 1.3824 1.3010 1.9405 -0.0178 0.0350  0.0245  36  ARG A NH1 
287  N NH2 . ARG A 36  ? 1.1897 1.1188 1.6753 -0.0132 0.0410  0.0522  36  ARG A NH2 
288  N N   . LYS A 37  ? 0.6655 0.6028 1.3473 -0.0310 -0.0055 -0.0926 37  LYS A N   
289  C CA  . LYS A 37  ? 0.7901 0.7332 1.5014 -0.0327 -0.0183 -0.1208 37  LYS A CA  
290  C C   . LYS A 37  ? 0.7558 0.7132 1.4258 -0.0287 -0.0285 -0.1340 37  LYS A C   
291  O O   . LYS A 37  ? 0.7306 0.6926 1.3955 -0.0244 -0.0437 -0.1614 37  LYS A O   
292  C CB  . LYS A 37  ? 0.9120 0.8477 1.6468 -0.0296 -0.0292 -0.1467 37  LYS A CB  
293  C CG  . LYS A 37  ? 1.0306 0.9509 1.8151 -0.0333 -0.0210 -0.1378 37  LYS A CG  
294  C CD  . LYS A 37  ? 1.1234 1.0382 1.9507 -0.0327 -0.0330 -0.1692 37  LYS A CD  
295  C CE  . LYS A 37  ? 1.1644 1.0806 1.9550 -0.0235 -0.0445 -0.1930 37  LYS A CE  
296  N NZ  . LYS A 37  ? 1.1645 1.0700 1.9412 -0.0194 -0.0363 -0.1790 37  LYS A NZ  
297  N N   . LYS A 38  ? 0.7156 0.6801 1.3568 -0.0297 -0.0203 -0.1145 38  LYS A N   
298  C CA  . LYS A 38  ? 0.6771 0.6542 1.2818 -0.0260 -0.0287 -0.1237 38  LYS A CA  
299  C C   . LYS A 38  ? 0.5839 0.5691 1.2019 -0.0313 -0.0206 -0.1102 38  LYS A C   
300  O O   . LYS A 38  ? 0.5379 0.5191 1.1709 -0.0362 -0.0050 -0.0869 38  LYS A O   
301  C CB  . LYS A 38  ? 0.7317 0.7095 1.2763 -0.0194 -0.0278 -0.1162 38  LYS A CB  
302  C CG  . LYS A 38  ? 0.8215 0.8082 1.3306 -0.0127 -0.0416 -0.1357 38  LYS A CG  
303  C CD  . LYS A 38  ? 0.9493 0.9392 1.4039 -0.0083 -0.0376 -0.1229 38  LYS A CD  
304  C CE  . LYS A 38  ? 0.9864 0.9840 1.4055 -0.0011 -0.0500 -0.1393 38  LYS A CE  
305  N NZ  . LYS A 38  ? 0.9861 0.9925 1.4261 -0.0011 -0.0622 -0.1571 38  LYS A NZ  
306  N N   . ARG A 39  ? 0.5339 0.5309 1.1468 -0.0297 -0.0310 -0.1249 39  ARG A N   
307  C CA  . ARG A 39  ? 0.5077 0.5139 1.1360 -0.0342 -0.0241 -0.1151 39  ARG A CA  
308  C C   . ARG A 39  ? 0.4208 0.4284 1.0048 -0.0327 -0.0112 -0.0915 39  ARG A C   
309  O O   . ARG A 39  ? 0.3710 0.3790 0.9074 -0.0267 -0.0157 -0.0925 39  ARG A O   
310  C CB  . ARG A 39  ? 0.5727 0.5913 1.2080 -0.0317 -0.0406 -0.1382 39  ARG A CB  
311  C CG  . ARG A 39  ? 0.6426 0.6613 1.3296 -0.0341 -0.0532 -0.1620 39  ARG A CG  
312  C CD  . ARG A 39  ? 0.7544 0.7874 1.4625 -0.0339 -0.0662 -0.1790 39  ARG A CD  
313  N NE  . ARG A 39  ? 0.8356 0.8764 1.5025 -0.0247 -0.0845 -0.1972 39  ARG A NE  
314  C CZ  . ARG A 39  ? 0.8997 0.9506 1.5845 -0.0217 -0.1043 -0.2227 39  ARG A CZ  
315  N NH1 . ARG A 39  ? 0.8360 0.8905 1.5828 -0.0277 -0.1091 -0.2353 39  ARG A NH1 
316  N NH2 . ARG A 39  ? 0.8996 0.9572 1.5409 -0.0123 -0.1194 -0.2352 39  ARG A NH2 
317  N N   . PRO A 40  ? 0.3850 0.3925 0.9833 -0.0379 0.0060  -0.0691 40  PRO A N   
318  C CA  . PRO A 40  ? 0.3526 0.3605 0.9094 -0.0363 0.0185  -0.0471 40  PRO A CA  
319  C C   . PRO A 40  ? 0.3557 0.3733 0.8721 -0.0315 0.0132  -0.0518 40  PRO A C   
320  O O   . PRO A 40  ? 0.3008 0.3171 0.7739 -0.0280 0.0173  -0.0412 40  PRO A O   
321  C CB  . PRO A 40  ? 0.3790 0.3882 0.9638 -0.0424 0.0370  -0.0264 40  PRO A CB  
322  C CG  . PRO A 40  ? 0.4112 0.4216 1.0580 -0.0482 0.0344  -0.0378 40  PRO A CG  
323  C CD  . PRO A 40  ? 0.4142 0.4205 1.0704 -0.0456 0.0152  -0.0634 40  PRO A CD  
324  N N   . GLU A 41  ? 0.3412 0.3683 0.8733 -0.0311 0.0030  -0.0684 41  GLU A N   
325  C CA  . GLU A 41  ? 0.3705 0.4060 0.8676 -0.0261 -0.0022 -0.0721 41  GLU A CA  
326  C C   . GLU A 41  ? 0.3722 0.4046 0.8271 -0.0190 -0.0150 -0.0826 41  GLU A C   
327  O O   . GLU A 41  ? 0.3749 0.4115 0.7945 -0.0145 -0.0172 -0.0814 41  GLU A O   
328  C CB  . GLU A 41  ? 0.3812 0.4285 0.9085 -0.0270 -0.0096 -0.0851 41  GLU A CB  
329  C CG  . GLU A 41  ? 0.3762 0.4252 0.9295 -0.0257 -0.0281 -0.1092 41  GLU A CG  
330  C CD  . GLU A 41  ? 0.3840 0.4300 0.9947 -0.0327 -0.0253 -0.1128 41  GLU A CD  
331  O OE1 . GLU A 41  ? 0.4094 0.4601 1.0517 -0.0326 -0.0404 -0.1343 41  GLU A OE1 
332  O OE2 . GLU A 41  ? 0.4126 0.4513 1.0362 -0.0379 -0.0087 -0.0943 41  GLU A OE2 
333  N N   . LYS A 42  ? 0.3640 0.3891 0.8240 -0.0178 -0.0224 -0.0927 42  LYS A N   
334  C CA  . LYS A 42  ? 0.3920 0.4149 0.8150 -0.0107 -0.0334 -0.1037 42  LYS A CA  
335  C C   . LYS A 42  ? 0.3541 0.3693 0.7432 -0.0091 -0.0246 -0.0889 42  LYS A C   
336  O O   . LYS A 42  ? 0.3830 0.3973 0.7367 -0.0035 -0.0298 -0.0932 42  LYS A O   
337  C CB  . LYS A 42  ? 0.4490 0.4689 0.8944 -0.0094 -0.0456 -0.1243 42  LYS A CB  
338  C CG  . LYS A 42  ? 0.4743 0.5019 0.9615 -0.0116 -0.0560 -0.1412 42  LYS A CG  
339  C CD  . LYS A 42  ? 0.5155 0.5548 0.9870 -0.0073 -0.0653 -0.1478 42  LYS A CD  
340  C CE  . LYS A 42  ? 0.5942 0.6414 1.0970 -0.0060 -0.0827 -0.1719 42  LYS A CE  
341  N NZ  . LYS A 42  ? 0.6437 0.7030 1.1393 -0.0023 -0.0910 -0.1756 42  LYS A NZ  
342  N N   . ILE A 43  ? 0.3336 0.3439 0.7344 -0.0139 -0.0109 -0.0707 43  ILE A N   
343  C CA  . ILE A 43  ? 0.3203 0.3235 0.6973 -0.0128 -0.0032 -0.0562 43  ILE A CA  
344  C C   . ILE A 43  ? 0.3222 0.3298 0.6614 -0.0110 0.0027  -0.0439 43  ILE A C   
345  O O   . ILE A 43  ? 0.2743 0.2882 0.6169 -0.0131 0.0082  -0.0379 43  ILE A O   
346  C CB  . ILE A 43  ? 0.3309 0.3273 0.7393 -0.0180 0.0077  -0.0416 43  ILE A CB  
347  C CG1 . ILE A 43  ? 0.3475 0.3382 0.7956 -0.0196 0.0010  -0.0559 43  ILE A CG1 
348  C CG2 . ILE A 43  ? 0.3353 0.3258 0.7188 -0.0164 0.0155  -0.0239 43  ILE A CG2 
349  C CD1 . ILE A 43  ? 0.3812 0.3630 0.8634 -0.0241 0.0111  -0.0419 43  ILE A CD1 
350  N N   . ILE A 44  ? 0.3055 0.3095 0.6116 -0.0071 0.0017  -0.0410 44  ILE A N   
351  C CA  . ILE A 44  ? 0.2951 0.3021 0.5673 -0.0054 0.0067  -0.0303 44  ILE A CA  
352  C C   . ILE A 44  ? 0.2959 0.3014 0.5698 -0.0085 0.0189  -0.0107 44  ILE A C   
353  O O   . ILE A 44  ? 0.3069 0.3062 0.5914 -0.0095 0.0224  -0.0024 44  ILE A O   
354  C CB  . ILE A 44  ? 0.2927 0.2971 0.5341 -0.0005 0.0016  -0.0343 44  ILE A CB  
355  C CG1 . ILE A 44  ? 0.2958 0.3026 0.5287 0.0037  -0.0092 -0.0516 44  ILE A CG1 
356  C CG2 . ILE A 44  ? 0.3112 0.3178 0.5232 0.0004  0.0070  -0.0229 44  ILE A CG2 
357  C CD1 . ILE A 44  ? 0.3221 0.3361 0.5476 0.0048  -0.0122 -0.0551 44  ILE A CD1 
358  N N   . LEU A 45  ? 0.3032 0.3148 0.5655 -0.0094 0.0255  -0.0029 45  LEU A N   
359  C CA  . LEU A 45  ? 0.3001 0.3117 0.5583 -0.0112 0.0372  0.0154  45  LEU A CA  
360  C C   . LEU A 45  ? 0.3079 0.3158 0.5385 -0.0081 0.0360  0.0225  45  LEU A C   
361  O O   . LEU A 45  ? 0.2629 0.2722 0.4677 -0.0050 0.0305  0.0163  45  LEU A O   
362  C CB  . LEU A 45  ? 0.2877 0.3078 0.5375 -0.0119 0.0442  0.0187  45  LEU A CB  
363  C CG  . LEU A 45  ? 0.3175 0.3396 0.5614 -0.0132 0.0576  0.0370  45  LEU A CG  
364  C CD1 . LEU A 45  ? 0.3374 0.3580 0.6174 -0.0175 0.0669  0.0463  45  LEU A CD1 
365  C CD2 . LEU A 45  ? 0.3135 0.3441 0.5382 -0.0120 0.0630  0.0371  45  LEU A CD2 
366  N N   . ASP A 46  ? 0.3260 0.3291 0.5655 -0.0089 0.0415  0.0362  46  ASP A N   
367  C CA  . ASP A 46  ? 0.3411 0.3406 0.5623 -0.0059 0.0400  0.0446  46  ASP A CA  
368  C C   . ASP A 46  ? 0.3525 0.3529 0.5708 -0.0064 0.0500  0.0651  46  ASP A C   
369  O O   . ASP A 46  ? 0.3388 0.3347 0.5828 -0.0086 0.0560  0.0749  46  ASP A O   
370  C CB  . ASP A 46  ? 0.3455 0.3370 0.5848 -0.0050 0.0338  0.0385  46  ASP A CB  
371  C CG  . ASP A 46  ? 0.3876 0.3764 0.6106 -0.0013 0.0303  0.0434  46  ASP A CG  
372  O OD1 . ASP A 46  ? 0.3938 0.3864 0.5943 0.0002  0.0329  0.0544  46  ASP A OD1 
373  O OD2 . ASP A 46  ? 0.4110 0.3948 0.6438 0.0005  0.0246  0.0343  46  ASP A OD2 
374  N N   . SER A 47  ? 0.3792 0.3853 0.5662 -0.0040 0.0519  0.0712  47  SER A N   
375  C CA  . SER A 47  ? 0.4218 0.4311 0.5979 -0.0032 0.0615  0.0896  47  SER A CA  
376  C C   . SER A 47  ? 0.4443 0.4474 0.6256 -0.0011 0.0611  0.1046  47  SER A C   
377  O O   . SER A 47  ? 0.4333 0.4365 0.6148 -0.0005 0.0699  0.1228  47  SER A O   
378  C CB  . SER A 47  ? 0.4403 0.4576 0.5805 -0.0004 0.0608  0.0885  47  SER A CB  
379  O OG  . SER A 47  ? 0.4465 0.4627 0.5686 0.0031  0.0519  0.0879  47  SER A OG  
380  N N   . THR A 48  ? 0.4577 0.4554 0.6437 0.0006  0.0515  0.0973  48  THR A N   
381  C CA  . THR A 48  ? 0.5017 0.4931 0.6964 0.0032  0.0499  0.1100  48  THR A CA  
382  C C   . THR A 48  ? 0.5550 0.5387 0.7861 0.0003  0.0573  0.1197  48  THR A C   
383  O O   . THR A 48  ? 0.5861 0.5667 0.8212 0.0021  0.0627  0.1398  48  THR A O   
384  C CB  . THR A 48  ? 0.4577 0.4464 0.6506 0.0057  0.0390  0.0980  48  THR A CB  
385  O OG1 . THR A 48  ? 0.4232 0.4192 0.5838 0.0085  0.0341  0.0953  48  THR A OG1 
386  C CG2 . THR A 48  ? 0.4686 0.4496 0.6808 0.0082  0.0371  0.1079  48  THR A CG2 
387  N N   . TYR A 49  ? 0.5590 0.5401 0.8171 -0.0039 0.0574  0.1061  49  TYR A N   
388  C CA  . TYR A 49  ? 0.6713 0.6448 0.9701 -0.0074 0.0636  0.1122  49  TYR A CA  
389  C C   . TYR A 49  ? 0.6892 0.6673 0.9967 -0.0113 0.0763  0.1222  49  TYR A C   
390  O O   . TYR A 49  ? 0.6522 0.6254 0.9855 -0.0134 0.0860  0.1380  49  TYR A O   
391  C CB  . TYR A 49  ? 0.7553 0.7243 1.0823 -0.0098 0.0561  0.0904  49  TYR A CB  
392  C CG  . TYR A 49  ? 0.9268 0.8897 1.2567 -0.0064 0.0461  0.0798  49  TYR A CG  
393  C CD1 . TYR A 49  ? 1.0032 0.9589 1.3407 -0.0033 0.0462  0.0930  49  TYR A CD1 
394  C CD2 . TYR A 49  ? 0.9818 0.9461 1.3086 -0.0058 0.0369  0.0564  49  TYR A CD2 
395  C CE1 . TYR A 49  ? 0.9797 0.9306 1.3227 0.0000  0.0381  0.0822  49  TYR A CE1 
396  C CE2 . TYR A 49  ? 0.9723 0.9317 1.3021 -0.0024 0.0296  0.0460  49  TYR A CE2 
397  C CZ  . TYR A 49  ? 0.9456 0.8984 1.2848 0.0004  0.0305  0.0582  49  TYR A CZ  
398  O OH  . TYR A 49  ? 0.8377 0.7865 1.1821 0.0039  0.0241  0.0464  49  TYR A OH  
399  N N   . HIS A 50  ? 0.7055 0.6931 0.9931 -0.0121 0.0773  0.1136  50  HIS A N   
400  C CA  . HIS A 50  ? 0.6774 0.6701 0.9809 -0.0162 0.0882  0.1164  50  HIS A CA  
401  C C   . HIS A 50  ? 0.7374 0.7381 1.0111 -0.0141 0.0995  0.1327  50  HIS A C   
402  O O   . HIS A 50  ? 0.7284 0.7364 1.0053 -0.0165 0.1080  0.1312  50  HIS A O   
403  C CB  . HIS A 50  ? 0.6148 0.6132 0.9216 -0.0181 0.0813  0.0934  50  HIS A CB  
404  C CG  . HIS A 50  ? 0.5677 0.5606 0.8954 -0.0189 0.0688  0.0742  50  HIS A CG  
405  N ND1 . HIS A 50  ? 0.4758 0.4724 0.7866 -0.0169 0.0577  0.0549  50  HIS A ND1 
406  C CD2 . HIS A 50  ? 0.5372 0.5219 0.9011 -0.0210 0.0662  0.0706  50  HIS A CD2 
407  C CE1 . HIS A 50  ? 0.4713 0.4628 0.8040 -0.0173 0.0486  0.0400  50  HIS A CE1 
408  N NE2 . HIS A 50  ? 0.5311 0.5155 0.8971 -0.0199 0.0533  0.0480  50  HIS A NE2 
409  N N   . HIS A 51  ? 0.7624 0.7624 1.0084 -0.0093 0.0995  0.1476  51  HIS A N   
410  C CA  . HIS A 51  ? 0.8063 0.8152 1.0145 -0.0057 0.1065  0.1583  51  HIS A CA  
411  C C   . HIS A 51  ? 0.8259 0.8387 1.0445 -0.0077 0.1250  0.1751  51  HIS A C   
412  O O   . HIS A 51  ? 0.7358 0.7584 0.9327 -0.0067 0.1325  0.1743  51  HIS A O   
413  C CB  . HIS A 51  ? 0.8853 0.8931 1.0646 0.0004  0.1012  0.1712  51  HIS A CB  
414  C CG  . HIS A 51  ? 0.9521 0.9497 1.1534 0.0014  0.1013  0.1872  51  HIS A CG  
415  N ND1 . HIS A 51  ? 1.0712 1.0677 1.2696 0.0041  0.1122  0.2135  51  HIS A ND1 
416  C CD2 . HIS A 51  ? 0.9442 0.9323 1.1702 0.0009  0.0922  0.1814  51  HIS A CD2 
417  C CE1 . HIS A 51  ? 1.0563 1.0421 1.2788 0.0050  0.1092  0.2238  51  HIS A CE1 
418  N NE2 . HIS A 51  ? 1.0416 1.0223 1.2817 0.0030  0.0971  0.2036  51  HIS A NE2 
419  N N   . ALA A 52  ? 0.8263 0.8311 1.0797 -0.0103 0.1331  0.1901  52  ALA A N   
420  C CA  . ALA A 52  ? 0.7968 0.8044 1.0660 -0.0127 0.1526  0.2082  52  ALA A CA  
421  C C   . ALA A 52  ? 0.7568 0.7711 1.0496 -0.0182 0.1585  0.1934  52  ALA A C   
422  O O   . ALA A 52  ? 0.8268 0.8475 1.1238 -0.0194 0.1757  0.2052  52  ALA A O   
423  C CB  . ALA A 52  ? 0.7840 0.7800 1.0895 -0.0144 0.1591  0.2275  52  ALA A CB  
424  N N   . ALA A 53  ? 0.6884 0.7026 0.9945 -0.0208 0.1450  0.1682  53  ALA A N   
425  C CA  . ALA A 53  ? 0.6878 0.7094 1.0158 -0.0251 0.1484  0.1536  53  ALA A CA  
426  C C   . ALA A 53  ? 0.6804 0.7126 0.9720 -0.0220 0.1453  0.1408  53  ALA A C   
427  O O   . ALA A 53  ? 0.6834 0.7229 0.9905 -0.0245 0.1483  0.1295  53  ALA A O   
428  C CB  . ALA A 53  ? 0.6194 0.6355 0.9861 -0.0293 0.1358  0.1343  53  ALA A CB  
429  N N   . LEU A 54  ? 0.6636 0.6971 0.9101 -0.0164 0.1393  0.1419  54  LEU A N   
430  C CA  . LEU A 54  ? 0.6884 0.7306 0.9040 -0.0136 0.1355  0.1281  54  LEU A CA  
431  C C   . LEU A 54  ? 0.7580 0.8098 0.9491 -0.0108 0.1514  0.1400  54  LEU A C   
432  O O   . LEU A 54  ? 0.7038 0.7638 0.8773 -0.0091 0.1519  0.1283  54  LEU A O   
433  C CB  . LEU A 54  ? 0.6515 0.6904 0.8359 -0.0096 0.1193  0.1194  54  LEU A CB  
434  C CG  . LEU A 54  ? 0.6614 0.6931 0.8629 -0.0113 0.1036  0.1034  54  LEU A CG  
435  C CD1 . LEU A 54  ? 0.6584 0.6887 0.8283 -0.0073 0.0905  0.0955  54  LEU A CD1 
436  C CD2 . LEU A 54  ? 0.6539 0.6890 0.8775 -0.0142 0.1005  0.0861  54  LEU A CD2 
437  N N   . ARG A 55  ? 0.8402 0.8908 1.0308 -0.0100 0.1646  0.1632  55  ARG A N   
438  C CA  . ARG A 55  ? 0.9062 0.9655 1.0661 -0.0057 0.1800  0.1779  55  ARG A CA  
439  C C   . ARG A 55  ? 0.9248 0.9953 1.0883 -0.0067 0.1918  0.1686  55  ARG A C   
440  O O   . ARG A 55  ? 0.8999 0.9791 1.0275 -0.0020 0.1954  0.1649  55  ARG A O   
441  C CB  . ARG A 55  ? 0.9721 1.0277 1.1451 -0.0059 0.1957  0.2056  55  ARG A CB  
442  C CG  . ARG A 55  ? 1.0714 1.1168 1.2371 -0.0032 0.1869  0.2197  55  ARG A CG  
443  C CD  . ARG A 55  ? 1.1502 1.1921 1.3297 -0.0029 0.2045  0.2495  55  ARG A CD  
444  N NE  . ARG A 55  ? 1.1837 1.2134 1.3722 -0.0014 0.1967  0.2634  55  ARG A NE  
445  C CZ  . ARG A 55  ? 1.1942 1.2226 1.3471 0.0055  0.1866  0.2715  55  ARG A CZ  
446  N NH1 . ARG A 55  ? 1.2029 1.2417 1.3060 0.0119  0.1837  0.2685  55  ARG A NH1 
447  N NH2 . ARG A 55  ? 1.1800 1.1970 1.3494 0.0064  0.1791  0.2821  55  ARG A NH2 
448  N N   . GLN A 56  ? 0.8898 0.9604 1.0990 -0.0127 0.1974  0.1638  56  GLN A N   
449  C CA  . GLN A 56  ? 0.9781 1.0600 1.1979 -0.0138 0.2104  0.1571  56  GLN A CA  
450  C C   . GLN A 56  ? 0.9041 0.9884 1.1309 -0.0146 0.1956  0.1307  56  GLN A C   
451  O O   . GLN A 56  ? 0.8378 0.9318 1.0644 -0.0136 0.2030  0.1221  56  GLN A O   
452  C CB  . GLN A 56  ? 1.1023 1.1860 1.3674 -0.0190 0.2294  0.1710  56  GLN A CB  
453  C CG  . GLN A 56  ? 1.1580 1.2301 1.4660 -0.0246 0.2243  0.1771  56  GLN A CG  
454  C CD  . GLN A 56  ? 1.1810 1.2479 1.5102 -0.0275 0.2022  0.1535  56  GLN A CD  
455  O OE1 . GLN A 56  ? 1.1136 1.1869 1.4611 -0.0293 0.1982  0.1358  56  GLN A OE1 
456  N NE2 . GLN A 56  ? 1.1945 1.2502 1.5200 -0.0271 0.1877  0.1531  56  GLN A NE2 
457  N N   . LEU A 57  ? 0.8301 0.9057 1.0608 -0.0155 0.1753  0.1185  57  LEU A N   
458  C CA  . LEU A 57  ? 0.7432 0.8202 0.9747 -0.0151 0.1604  0.0958  57  LEU A CA  
459  C C   . LEU A 57  ? 0.7584 0.8418 0.9499 -0.0099 0.1603  0.0884  57  LEU A C   
460  O O   . LEU A 57  ? 0.7731 0.8565 0.9286 -0.0060 0.1621  0.0967  57  LEU A O   
461  C CB  . LEU A 57  ? 0.7058 0.7725 0.9363 -0.0154 0.1404  0.0870  57  LEU A CB  
462  C CG  . LEU A 57  ? 0.6969 0.7600 0.9684 -0.0196 0.1309  0.0756  57  LEU A CG  
463  C CD1 . LEU A 57  ? 0.6783 0.7333 0.9375 -0.0179 0.1119  0.0646  57  LEU A CD1 
464  C CD2 . LEU A 57  ? 0.7327 0.8046 1.0255 -0.0205 0.1317  0.0623  57  LEU A CD2 
465  N N   . GLU A 58  ? 0.7913 0.8800 0.9914 -0.0095 0.1566  0.0719  58  GLU A N   
466  C CA  . GLU A 58  ? 0.8028 0.8959 0.9712 -0.0048 0.1537  0.0610  58  GLU A CA  
467  C C   . GLU A 58  ? 0.7137 0.7985 0.8564 -0.0028 0.1361  0.0554  58  GLU A C   
468  O O   . GLU A 58  ? 0.6566 0.7342 0.8144 -0.0048 0.1231  0.0500  58  GLU A O   
469  C CB  . GLU A 58  ? 0.8461 0.9449 1.0353 -0.0047 0.1520  0.0452  58  GLU A CB  
470  C CG  . GLU A 58  ? 0.9422 1.0441 1.1030 0.0002  0.1486  0.0331  58  GLU A CG  
471  C CD  . GLU A 58  ? 1.0362 1.1426 1.2187 0.0011  0.1454  0.0181  58  GLU A CD  
472  O OE1 . GLU A 58  ? 1.0672 1.1681 1.2464 0.0025  0.1298  0.0072  58  GLU A OE1 
473  O OE2 . GLU A 58  ? 1.0645 1.1800 1.2675 0.0009  0.1591  0.0182  58  GLU A OE2 
474  N N   . ASP A 59  ? 0.7147 0.8012 0.8197 0.0014  0.1362  0.0566  59  ASP A N   
475  C CA  . ASP A 59  ? 0.7296 0.8097 0.8116 0.0033  0.1207  0.0511  59  ASP A CA  
476  C C   . ASP A 59  ? 0.6792 0.7511 0.7662 0.0015  0.1146  0.0620  59  ASP A C   
477  O O   . ASP A 59  ? 0.7067 0.7723 0.7863 0.0019  0.1011  0.0567  59  ASP A O   
478  C CB  . ASP A 59  ? 0.8187 0.8951 0.9103 0.0029  0.1076  0.0344  59  ASP A CB  
479  C CG  . ASP A 59  ? 0.8605 0.9388 0.9286 0.0065  0.1027  0.0224  59  ASP A CG  
480  O OD1 . ASP A 59  ? 0.8611 0.9470 0.9256 0.0085  0.1121  0.0176  59  ASP A OD1 
481  O OD2 . ASP A 59  ? 0.7874 0.8597 0.8443 0.0072  0.0901  0.0174  59  ASP A OD2 
482  N N   . GLY A 60  ? 0.6926 0.7644 0.7938 -0.0004 0.1255  0.0776  60  GLY A N   
483  C CA  . GLY A 60  ? 0.6756 0.7388 0.7928 -0.0028 0.1206  0.0870  60  GLY A CA  
484  C C   . GLY A 60  ? 0.7037 0.7621 0.7945 0.0004  0.1100  0.0906  60  GLY A C   
485  O O   . GLY A 60  ? 0.7770 0.8274 0.8796 -0.0009 0.1000  0.0895  60  GLY A O   
486  N N   . GLU A 61  ? 0.7371 0.8013 0.7933 0.0048  0.1121  0.0935  61  GLU A N   
487  C CA  . GLU A 61  ? 0.8055 0.8676 0.8367 0.0085  0.1026  0.0983  61  GLU A CA  
488  C C   . GLU A 61  ? 0.7567 0.8135 0.7887 0.0079  0.0864  0.0832  61  GLU A C   
489  O O   . GLU A 61  ? 0.8618 0.9140 0.8899 0.0092  0.0775  0.0874  61  GLU A O   
490  C CB  . GLU A 61  ? 0.8814 0.9525 0.8754 0.0138  0.1068  0.1009  61  GLU A CB  
491  C CG  . GLU A 61  ? 0.9380 1.0130 0.9125 0.0158  0.0975  0.0818  61  GLU A CG  
492  C CD  . GLU A 61  ? 1.0566 1.1370 1.0349 0.0150  0.1042  0.0680  61  GLU A CD  
493  O OE1 . GLU A 61  ? 1.0843 1.1660 1.0512 0.0164  0.0962  0.0522  61  GLU A OE1 
494  O OE2 . GLU A 61  ? 1.0824 1.1658 1.0769 0.0133  0.1178  0.0731  61  GLU A OE2 
495  N N   . ARG A 62  ? 0.6671 0.7248 0.7052 0.0065  0.0830  0.0669  62  ARG A N   
496  C CA  . ARG A 62  ? 0.6663 0.7196 0.7019 0.0067  0.0695  0.0542  62  ARG A CA  
497  C C   . ARG A 62  ? 0.5824 0.6294 0.6451 0.0035  0.0649  0.0472  62  ARG A C   
498  O O   . ARG A 62  ? 0.6377 0.6813 0.6995 0.0038  0.0553  0.0369  62  ARG A O   
499  C CB  . ARG A 62  ? 0.6920 0.7503 0.7090 0.0088  0.0673  0.0414  62  ARG A CB  
500  C CG  . ARG A 62  ? 0.7012 0.7632 0.7286 0.0079  0.0739  0.0327  62  ARG A CG  
501  C CD  . ARG A 62  ? 0.7657 0.8322 0.7746 0.0106  0.0725  0.0209  62  ARG A CD  
502  N NE  . ARG A 62  ? 0.7679 0.8300 0.7852 0.0101  0.0643  0.0080  62  ARG A NE  
503  C CZ  . ARG A 62  ? 0.7233 0.7868 0.7308 0.0120  0.0614  -0.0034 62  ARG A CZ  
504  N NH1 . ARG A 62  ? 0.7211 0.7899 0.7074 0.0145  0.0626  -0.0060 62  ARG A NH1 
505  N NH2 . ARG A 62  ? 0.7934 0.8524 0.8125 0.0117  0.0561  -0.0123 62  ARG A NH2 
506  N N   . ARG A 63  ? 0.4826 0.5285 0.5700 0.0008  0.0714  0.0530  63  ARG A N   
507  C CA  . ARG A 63  ? 0.4083 0.4496 0.5219 -0.0017 0.0661  0.0448  63  ARG A CA  
508  C C   . ARG A 63  ? 0.3359 0.3694 0.4628 -0.0026 0.0605  0.0489  63  ARG A C   
509  O O   . ARG A 63  ? 0.3230 0.3542 0.4460 -0.0020 0.0629  0.0612  63  ARG A O   
510  C CB  . ARG A 63  ? 0.4057 0.4515 0.5431 -0.0043 0.0753  0.0449  63  ARG A CB  
511  C CG  . ARG A 63  ? 0.4218 0.4741 0.5522 -0.0029 0.0768  0.0347  63  ARG A CG  
512  C CD  . ARG A 63  ? 0.4150 0.4738 0.5685 -0.0049 0.0875  0.0355  63  ARG A CD  
513  N NE  . ARG A 63  ? 0.4004 0.4581 0.5836 -0.0069 0.0810  0.0261  63  ARG A NE  
514  C CZ  . ARG A 63  ? 0.3802 0.4441 0.5910 -0.0088 0.0874  0.0240  63  ARG A CZ  
515  N NH1 . ARG A 63  ? 0.3833 0.4542 0.5957 -0.0093 0.1027  0.0319  63  ARG A NH1 
516  N NH2 . ARG A 63  ? 0.3552 0.4190 0.5920 -0.0099 0.0787  0.0136  63  ARG A NH2 
517  N N   . GLY A 64  ? 0.3282 0.3577 0.4706 -0.0035 0.0526  0.0377  64  GLY A N   
518  C CA  . GLY A 64  ? 0.3445 0.3667 0.5005 -0.0038 0.0464  0.0370  64  GLY A CA  
519  C C   . GLY A 64  ? 0.3194 0.3385 0.4553 -0.0010 0.0406  0.0391  64  GLY A C   
520  O O   . GLY A 64  ? 0.2879 0.3032 0.4280 -0.0006 0.0412  0.0487  64  GLY A O   
521  N N   . ARG A 65  ? 0.3211 0.3420 0.4379 0.0010  0.0351  0.0304  65  ARG A N   
522  C CA  . ARG A 65  ? 0.3103 0.3291 0.4119 0.0033  0.0294  0.0303  65  ARG A CA  
523  C C   . ARG A 65  ? 0.2713 0.2873 0.3731 0.0045  0.0225  0.0179  65  ARG A C   
524  O O   . ARG A 65  ? 0.2729 0.2901 0.3594 0.0060  0.0195  0.0136  65  ARG A O   
525  C CB  . ARG A 65  ? 0.3287 0.3529 0.4066 0.0048  0.0303  0.0335  65  ARG A CB  
526  C CG  . ARG A 65  ? 0.4195 0.4472 0.4913 0.0052  0.0368  0.0470  65  ARG A CG  
527  C CD  . ARG A 65  ? 0.4826 0.5068 0.5590 0.0064  0.0355  0.0588  65  ARG A CD  
528  N NE  . ARG A 65  ? 0.6123 0.6352 0.6819 0.0087  0.0268  0.0558  65  ARG A NE  
529  C CZ  . ARG A 65  ? 0.6026 0.6305 0.6525 0.0110  0.0224  0.0554  65  ARG A CZ  
530  N NH1 . ARG A 65  ? 0.5934 0.6276 0.6253 0.0125  0.0254  0.0615  65  ARG A NH1 
531  N NH2 . ARG A 65  ? 0.5640 0.5909 0.6134 0.0120  0.0151  0.0489  65  ARG A NH2 
532  N N   . PRO A 66  ? 0.2462 0.2580 0.3655 0.0042  0.0197  0.0124  66  PRO A N   
533  C CA  . PRO A 66  ? 0.2440 0.2535 0.3596 0.0065  0.0137  0.0013  66  PRO A CA  
534  C C   . PRO A 66  ? 0.2567 0.2636 0.3646 0.0086  0.0112  0.0018  66  PRO A C   
535  O O   . PRO A 66  ? 0.2280 0.2338 0.3294 0.0109  0.0082  -0.0059 66  PRO A O   
536  C CB  . PRO A 66  ? 0.2431 0.2500 0.3808 0.0057  0.0116  -0.0051 66  PRO A CB  
537  C CG  . PRO A 66  ? 0.2496 0.2540 0.4044 0.0034  0.0162  0.0054  66  PRO A CG  
538  C CD  . PRO A 66  ? 0.2414 0.2502 0.3844 0.0022  0.0224  0.0168  66  PRO A CD  
539  N N   . ASP A 67  ? 0.2655 0.2721 0.3746 0.0084  0.0128  0.0116  67  ASP A N   
540  C CA  . ASP A 67  ? 0.2985 0.3045 0.4024 0.0104  0.0104  0.0132  67  ASP A CA  
541  C C   . ASP A 67  ? 0.2930 0.3027 0.3786 0.0111  0.0093  0.0102  67  ASP A C   
542  O O   . ASP A 67  ? 0.2859 0.2950 0.3685 0.0127  0.0076  0.0058  67  ASP A O   
543  C CB  . ASP A 67  ? 0.3366 0.3422 0.4461 0.0106  0.0113  0.0255  67  ASP A CB  
544  C CG  . ASP A 67  ? 0.3727 0.3832 0.4701 0.0097  0.0142  0.0348  67  ASP A CG  
545  O OD1 . ASP A 67  ? 0.3566 0.3688 0.4527 0.0079  0.0179  0.0335  67  ASP A OD1 
546  O OD2 . ASP A 67  ? 0.4694 0.4826 0.5591 0.0112  0.0127  0.0429  67  ASP A OD2 
547  N N   . ILE A 68  ? 0.2888 0.3023 0.3640 0.0098  0.0110  0.0118  68  ILE A N   
548  C CA  . ILE A 68  ? 0.2627 0.2791 0.3244 0.0102  0.0098  0.0083  68  ILE A CA  
549  C C   . ILE A 68  ? 0.2594 0.2729 0.3202 0.0114  0.0090  0.0000  68  ILE A C   
550  O O   . ILE A 68  ? 0.2773 0.2907 0.3339 0.0123  0.0082  -0.0021 68  ILE A O   
551  C CB  . ILE A 68  ? 0.2877 0.3084 0.3399 0.0092  0.0122  0.0096  68  ILE A CB  
552  C CG1 . ILE A 68  ? 0.2977 0.3224 0.3443 0.0093  0.0130  0.0186  68  ILE A CG1 
553  C CG2 . ILE A 68  ? 0.2769 0.2990 0.3197 0.0094  0.0110  0.0032  68  ILE A CG2 
554  C CD1 . ILE A 68  ? 0.3037 0.3334 0.3399 0.0089  0.0171  0.0192  68  ILE A CD1 
555  N N   . VAL A 69  ? 0.2899 0.3017 0.3556 0.0116  0.0092  -0.0042 69  VAL A N   
556  C CA  . VAL A 69  ? 0.2718 0.2814 0.3340 0.0139  0.0078  -0.0112 69  VAL A CA  
557  C C   . VAL A 69  ? 0.2712 0.2781 0.3354 0.0161  0.0071  -0.0136 69  VAL A C   
558  O O   . VAL A 69  ? 0.2636 0.2697 0.3200 0.0182  0.0079  -0.0158 69  VAL A O   
559  C CB  . VAL A 69  ? 0.2714 0.2812 0.3396 0.0143  0.0062  -0.0159 69  VAL A CB  
560  C CG1 . VAL A 69  ? 0.3036 0.3117 0.3656 0.0181  0.0032  -0.0227 69  VAL A CG1 
561  C CG2 . VAL A 69  ? 0.2814 0.2946 0.3490 0.0128  0.0080  -0.0145 69  VAL A CG2 
562  N N   . HIS A 70  ? 0.2780 0.2835 0.3541 0.0158  0.0066  -0.0129 70  HIS A N   
563  C CA  . HIS A 70  ? 0.2615 0.2647 0.3416 0.0183  0.0067  -0.0161 70  HIS A CA  
564  C C   . HIS A 70  ? 0.2360 0.2407 0.3104 0.0188  0.0086  -0.0128 70  HIS A C   
565  O O   . HIS A 70  ? 0.2198 0.2241 0.2890 0.0213  0.0107  -0.0166 70  HIS A O   
566  C CB  . HIS A 70  ? 0.2570 0.2579 0.3543 0.0177  0.0060  -0.0146 70  HIS A CB  
567  C CG  . HIS A 70  ? 0.2667 0.2651 0.3710 0.0207  0.0063  -0.0202 70  HIS A CG  
568  N ND1 . HIS A 70  ? 0.2601 0.2571 0.3778 0.0210  0.0068  -0.0156 70  HIS A ND1 
569  C CD2 . HIS A 70  ? 0.2778 0.2752 0.3777 0.0242  0.0064  -0.0300 70  HIS A CD2 
570  C CE1 . HIS A 70  ? 0.2681 0.2632 0.3915 0.0243  0.0077  -0.0235 70  HIS A CE1 
571  N NE2 . HIS A 70  ? 0.2857 0.2813 0.3967 0.0264  0.0078  -0.0325 70  HIS A NE2 
572  N N   . ILE A 71  ? 0.2409 0.2483 0.3165 0.0167  0.0080  -0.0059 71  ILE A N   
573  C CA  . ILE A 71  ? 0.2729 0.2829 0.3485 0.0170  0.0083  -0.0038 71  ILE A CA  
574  C C   . ILE A 71  ? 0.2491 0.2599 0.3149 0.0166  0.0101  -0.0062 71  ILE A C   
575  O O   . ILE A 71  ? 0.2324 0.2436 0.2999 0.0176  0.0127  -0.0073 71  ILE A O   
576  C CB  . ILE A 71  ? 0.2864 0.2999 0.3658 0.0158  0.0051  0.0034  71  ILE A CB  
577  C CG1 . ILE A 71  ? 0.4033 0.4143 0.4952 0.0168  0.0043  0.0074  71  ILE A CG1 
578  C CG2 . ILE A 71  ? 0.2772 0.2944 0.3595 0.0162  0.0038  0.0037  71  ILE A CG2 
579  C CD1 . ILE A 71  ? 0.4554 0.4678 0.5475 0.0158  0.0025  0.0171  71  ILE A CD1 
580  N N   . CYS A 72  ? 0.2292 0.2399 0.2869 0.0154  0.0097  -0.0069 72  CYS A N   
581  C CA  . CYS A 72  ? 0.2471 0.2571 0.2982 0.0155  0.0116  -0.0087 72  CYS A CA  
582  C C   . CYS A 72  ? 0.2350 0.2418 0.2823 0.0187  0.0148  -0.0112 72  CYS A C   
583  O O   . CYS A 72  ? 0.2359 0.2419 0.2817 0.0193  0.0184  -0.0102 72  CYS A O   
584  C CB  . CYS A 72  ? 0.2381 0.2484 0.2834 0.0145  0.0107  -0.0096 72  CYS A CB  
585  S SG  . CYS A 72  ? 0.2692 0.2843 0.3133 0.0117  0.0086  -0.0078 72  CYS A SG  
586  N N   . LEU A 73  ? 0.2316 0.2368 0.2774 0.0209  0.0137  -0.0145 73  LEU A N   
587  C CA  . LEU A 73  ? 0.2619 0.2649 0.2997 0.0251  0.0158  -0.0178 73  LEU A CA  
588  C C   . LEU A 73  ? 0.3136 0.3169 0.3547 0.0270  0.0203  -0.0184 73  LEU A C   
589  O O   . LEU A 73  ? 0.3365 0.3389 0.3696 0.0303  0.0251  -0.0183 73  LEU A O   
590  C CB  . LEU A 73  ? 0.2687 0.2711 0.3053 0.0272  0.0115  -0.0236 73  LEU A CB  
591  C CG  . LEU A 73  ? 0.2896 0.2925 0.3235 0.0267  0.0077  -0.0243 73  LEU A CG  
592  C CD1 . LEU A 73  ? 0.2993 0.3026 0.3353 0.0291  0.0027  -0.0316 73  LEU A CD1 
593  C CD2 . LEU A 73  ? 0.3065 0.3082 0.3297 0.0287  0.0094  -0.0214 73  LEU A CD2 
594  N N   . LEU A 74  ? 0.3068 0.3113 0.3602 0.0258  0.0193  -0.0184 74  LEU A N   
595  C CA  . LEU A 74  ? 0.3101 0.3156 0.3698 0.0279  0.0240  -0.0194 74  LEU A CA  
596  C C   . LEU A 74  ? 0.2918 0.2993 0.3536 0.0264  0.0285  -0.0146 74  LEU A C   
597  O O   . LEU A 74  ? 0.2944 0.3025 0.3556 0.0288  0.0354  -0.0146 74  LEU A O   
598  C CB  . LEU A 74  ? 0.2982 0.3044 0.3738 0.0271  0.0215  -0.0193 74  LEU A CB  
599  C CG  . LEU A 74  ? 0.3096 0.3130 0.3896 0.0287  0.0185  -0.0250 74  LEU A CG  
600  C CD1 . LEU A 74  ? 0.3161 0.3191 0.4146 0.0283  0.0168  -0.0230 74  LEU A CD1 
601  C CD2 . LEU A 74  ? 0.3239 0.3261 0.3957 0.0336  0.0216  -0.0339 74  LEU A CD2 
602  N N   . ASN A 75  ? 0.2867 0.2959 0.3522 0.0225  0.0249  -0.0109 75  ASN A N   
603  C CA  . ASN A 75  ? 0.2778 0.2891 0.3495 0.0206  0.0279  -0.0080 75  ASN A CA  
604  C C   . ASN A 75  ? 0.2862 0.2941 0.3481 0.0222  0.0340  -0.0067 75  ASN A C   
605  O O   . ASN A 75  ? 0.3450 0.3534 0.4120 0.0230  0.0413  -0.0045 75  ASN A O   
606  C CB  . ASN A 75  ? 0.2797 0.2939 0.3560 0.0167  0.0216  -0.0067 75  ASN A CB  
607  C CG  . ASN A 75  ? 0.2825 0.3010 0.3699 0.0162  0.0167  -0.0056 75  ASN A CG  
608  O OD1 . ASN A 75  ? 0.2474 0.2676 0.3456 0.0179  0.0190  -0.0056 75  ASN A OD1 
609  N ND2 . ASN A 75  ? 0.3711 0.3922 0.4563 0.0144  0.0102  -0.0043 75  ASN A ND2 
610  N N   . ALA A 76  ? 0.2787 0.2834 0.3276 0.0232  0.0317  -0.0073 76  ALA A N   
611  C CA  . ALA A 76  ? 0.2731 0.2743 0.3136 0.0251  0.0363  -0.0041 76  ALA A CA  
612  C C   . ALA A 76  ? 0.2790 0.2789 0.3086 0.0305  0.0430  -0.0033 76  ALA A C   
613  O O   . ALA A 76  ? 0.2572 0.2558 0.2865 0.0318  0.0513  0.0020  76  ALA A O   
614  C CB  . ALA A 76  ? 0.3017 0.3008 0.3338 0.0251  0.0308  -0.0050 76  ALA A CB  
615  N N   . LEU A 77  ? 0.2646 0.2650 0.2858 0.0339  0.0398  -0.0089 77  LEU A N   
616  C CA  . LEU A 77  ? 0.3034 0.3033 0.3102 0.0402  0.0445  -0.0108 77  LEU A CA  
617  C C   . LEU A 77  ? 0.3196 0.3219 0.3331 0.0415  0.0541  -0.0102 77  LEU A C   
618  O O   . LEU A 77  ? 0.3294 0.3317 0.3307 0.0466  0.0624  -0.0083 77  LEU A O   
619  C CB  . LEU A 77  ? 0.3490 0.3494 0.3496 0.0428  0.0367  -0.0197 77  LEU A CB  
620  C CG  . LEU A 77  ? 0.3960 0.3952 0.3890 0.0433  0.0284  -0.0211 77  LEU A CG  
621  C CD1 . LEU A 77  ? 0.4015 0.4020 0.3938 0.0455  0.0212  -0.0311 77  LEU A CD1 
622  C CD2 . LEU A 77  ? 0.4552 0.4526 0.4307 0.0481  0.0305  -0.0159 77  LEU A CD2 
623  N N   . ASP A 78  ? 0.2915 0.2965 0.3244 0.0376  0.0537  -0.0110 78  ASP A N   
624  C CA  . ASP A 78  ? 0.3072 0.3155 0.3504 0.0389  0.0628  -0.0107 78  ASP A CA  
625  C C   . ASP A 78  ? 0.2947 0.3040 0.3503 0.0356  0.0699  -0.0028 78  ASP A C   
626  O O   . ASP A 78  ? 0.2932 0.3059 0.3612 0.0361  0.0789  -0.0013 78  ASP A O   
627  C CB  . ASP A 78  ? 0.3372 0.3480 0.3962 0.0379  0.0582  -0.0164 78  ASP A CB  
628  C CG  . ASP A 78  ? 0.4661 0.4748 0.5170 0.0407  0.0515  -0.0245 78  ASP A CG  
629  O OD1 . ASP A 78  ? 0.5776 0.5850 0.6110 0.0457  0.0533  -0.0293 78  ASP A OD1 
630  O OD2 . ASP A 78  ? 0.6508 0.6593 0.7136 0.0380  0.0442  -0.0262 78  ASP A OD2 
631  N N   . SER A 79  ? 0.2750 0.2815 0.3300 0.0322  0.0666  0.0018  79  SER A N   
632  C CA  . SER A 79  ? 0.2452 0.2522 0.3165 0.0284  0.0722  0.0077  79  SER A CA  
633  C C   . SER A 79  ? 0.2803 0.2864 0.3480 0.0321  0.0868  0.0143  79  SER A C   
634  O O   . SER A 79  ? 0.2855 0.2891 0.3304 0.0380  0.0910  0.0158  79  SER A O   
635  C CB  . SER A 79  ? 0.2266 0.2298 0.2973 0.0250  0.0663  0.0099  79  SER A CB  
636  O OG  . SER A 79  ? 0.2313 0.2291 0.2811 0.0291  0.0675  0.0132  79  SER A OG  
637  N N   . ILE A 80  ? 0.2738 0.2826 0.3649 0.0286  0.0944  0.0183  80  ILE A N   
638  C CA  . ILE A 80  ? 0.2972 0.3044 0.3898 0.0305  0.1096  0.0276  80  ILE A CA  
639  C C   . ILE A 80  ? 0.3134 0.3128 0.3899 0.0319  0.1097  0.0349  80  ILE A C   
640  O O   . ILE A 80  ? 0.3327 0.3291 0.3912 0.0375  0.1195  0.0425  80  ILE A O   
641  C CB  . ILE A 80  ? 0.3145 0.3258 0.4421 0.0248  0.1154  0.0299  80  ILE A CB  
642  C CG1 . ILE A 80  ? 0.3090 0.3287 0.4540 0.0246  0.1151  0.0232  80  ILE A CG1 
643  C CG2 . ILE A 80  ? 0.3434 0.3518 0.4758 0.0260  0.1326  0.0417  80  ILE A CG2 
644  C CD1 . ILE A 80  ? 0.3147 0.3405 0.4957 0.0204  0.1228  0.0253  80  ILE A CD1 
645  N N   . LEU A 81  ? 0.3178 0.3142 0.4001 0.0275  0.0989  0.0327  81  LEU A N   
646  C CA  . LEU A 81  ? 0.3158 0.3046 0.3864 0.0290  0.0982  0.0390  81  LEU A CA  
647  C C   . LEU A 81  ? 0.3362 0.3231 0.3741 0.0368  0.0968  0.0399  81  LEU A C   
648  O O   . LEU A 81  ? 0.3444 0.3266 0.3678 0.0418  0.1038  0.0497  81  LEU A O   
649  C CB  . LEU A 81  ? 0.2975 0.2850 0.3771 0.0240  0.0854  0.0328  81  LEU A CB  
650  C CG  . LEU A 81  ? 0.3022 0.2819 0.3797 0.0244  0.0846  0.0384  81  LEU A CG  
651  C CD1 . LEU A 81  ? 0.2991 0.2747 0.4001 0.0213  0.0949  0.0466  81  LEU A CD1 
652  C CD2 . LEU A 81  ? 0.2839 0.2640 0.3648 0.0208  0.0715  0.0293  81  LEU A CD2 
653  N N   . ASN A 82  ? 0.3165 0.3074 0.3441 0.0381  0.0878  0.0299  82  ASN A N   
654  C CA  . ASN A 82  ? 0.3284 0.3186 0.3280 0.0453  0.0846  0.0278  82  ASN A CA  
655  C C   . ASN A 82  ? 0.3414 0.3327 0.3242 0.0524  0.0968  0.0327  82  ASN A C   
656  O O   . ASN A 82  ? 0.3495 0.3379 0.3096 0.0588  0.0980  0.0383  82  ASN A O   
657  C CB  . ASN A 82  ? 0.3232 0.3169 0.3192 0.0451  0.0733  0.0159  82  ASN A CB  
658  C CG  . ASN A 82  ? 0.3478 0.3405 0.3192 0.0515  0.0670  0.0127  82  ASN A CG  
659  O OD1 . ASN A 82  ? 0.3602 0.3493 0.3216 0.0539  0.0645  0.0182  82  ASN A OD1 
660  N ND2 . ASN A 82  ? 0.3382 0.3343 0.3023 0.0546  0.0636  0.0032  82  ASN A ND2 
661  N N   . LYS A 83  ? 0.3511 0.3467 0.3456 0.0516  0.1063  0.0316  83  LYS A N   
662  C CA  . LYS A 83  ? 0.4046 0.4024 0.3836 0.0586  0.1200  0.0354  83  LYS A CA  
663  C C   . LYS A 83  ? 0.4482 0.4417 0.4215 0.0612  0.1335  0.0516  83  LYS A C   
664  O O   . LYS A 83  ? 0.4412 0.4358 0.3922 0.0690  0.1445  0.0571  83  LYS A O   
665  C CB  . LYS A 83  ? 0.4180 0.4221 0.4175 0.0563  0.1272  0.0299  83  LYS A CB  
666  C CG  . LYS A 83  ? 0.4508 0.4582 0.4547 0.0552  0.1151  0.0155  83  LYS A CG  
667  C CD  . LYS A 83  ? 0.5078 0.5213 0.5310 0.0548  0.1220  0.0101  83  LYS A CD  
668  C CE  . LYS A 83  ? 0.5265 0.5419 0.5558 0.0542  0.1105  -0.0026 83  LYS A CE  
669  N NZ  . LYS A 83  ? 0.5504 0.5639 0.5533 0.0601  0.1038  -0.0106 83  LYS A NZ  
670  N N   . GLU A 84  ? 0.4616 0.4506 0.4565 0.0549  0.1336  0.0592  84  GLU A N   
671  C CA  . GLU A 84  ? 0.4886 0.4719 0.4858 0.0561  0.1463  0.0756  84  GLU A CA  
672  C C   . GLU A 84  ? 0.4831 0.4595 0.4592 0.0607  0.1389  0.0822  84  GLU A C   
673  O O   . GLU A 84  ? 0.5210 0.4908 0.5024 0.0611  0.1465  0.0963  84  GLU A O   
674  C CB  . GLU A 84  ? 0.5024 0.4839 0.5392 0.0466  0.1489  0.0785  84  GLU A CB  
675  C CG  . GLU A 84  ? 0.5199 0.5087 0.5830 0.0422  0.1572  0.0746  84  GLU A CG  
676  C CD  . GLU A 84  ? 0.6133 0.6032 0.6777 0.0459  0.1790  0.0871  84  GLU A CD  
677  O OE1 . GLU A 84  ? 0.5811 0.5786 0.6469 0.0479  0.1865  0.0823  84  GLU A OE1 
678  O OE2 . GLU A 84  ? 0.7312 0.7144 0.7954 0.0473  0.1895  0.1025  84  GLU A OE2 
679  N N   . ASP A 85  ? 0.4515 0.4292 0.4085 0.0636  0.1237  0.0719  85  ASP A N   
680  C CA  . ASP A 85  ? 0.4347 0.4077 0.3717 0.0690  0.1151  0.0763  85  ASP A CA  
681  C C   . ASP A 85  ? 0.4208 0.3872 0.3802 0.0630  0.1103  0.0806  85  ASP A C   
682  O O   . ASP A 85  ? 0.4197 0.3801 0.3706 0.0673  0.1092  0.0905  85  ASP A O   
683  C CB  . ASP A 85  ? 0.4699 0.4409 0.3778 0.0794  0.1251  0.0901  85  ASP A CB  
684  C CG  . ASP A 85  ? 0.5049 0.4729 0.3903 0.0862  0.1125  0.0923  85  ASP A CG  
685  O OD1 . ASP A 85  ? 0.4696 0.4404 0.3550 0.0846  0.0967  0.0787  85  ASP A OD1 
686  O OD2 . ASP A 85  ? 0.5478 0.5109 0.4168 0.0936  0.1187  0.1085  85  ASP A OD2 
687  N N   . ARG A 86  ? 0.4134 0.3812 0.4008 0.0538  0.1061  0.0721  86  ARG A N   
688  C CA  . ARG A 86  ? 0.3927 0.3550 0.4025 0.0481  0.1016  0.0732  86  ARG A CA  
689  C C   . ARG A 86  ? 0.3704 0.3356 0.3835 0.0443  0.0860  0.0592  86  ARG A C   
690  O O   . ARG A 86  ? 0.3401 0.3034 0.3743 0.0382  0.0819  0.0555  86  ARG A O   
691  C CB  . ARG A 86  ? 0.4126 0.3749 0.4555 0.0400  0.1094  0.0740  86  ARG A CB  
692  C CG  . ARG A 86  ? 0.4461 0.4069 0.4947 0.0417  0.1274  0.0873  86  ARG A CG  
693  C CD  . ARG A 86  ? 0.4873 0.4383 0.5446 0.0426  0.1337  0.1014  86  ARG A CD  
694  N NE  . ARG A 86  ? 0.5582 0.5071 0.6282 0.0428  0.1524  0.1155  86  ARG A NE  
695  C CZ  . ARG A 86  ? 0.5896 0.5291 0.6713 0.0435  0.1617  0.1311  86  ARG A CZ  
696  N NH1 . ARG A 86  ? 0.5589 0.4906 0.6430 0.0440  0.1525  0.1322  86  ARG A NH1 
697  N NH2 . ARG A 86  ? 0.5869 0.5246 0.6800 0.0439  0.1807  0.1457  86  ARG A NH2 
698  N N   . LEU A 87  ? 0.3627 0.3327 0.3559 0.0480  0.0777  0.0512  87  LEU A N   
699  C CA  . LEU A 87  ? 0.3454 0.3181 0.3424 0.0446  0.0646  0.0398  87  LEU A CA  
700  C C   . LEU A 87  ? 0.3611 0.3353 0.3361 0.0510  0.0556  0.0362  87  LEU A C   
701  O O   . LEU A 87  ? 0.3591 0.3354 0.3144 0.0573  0.0573  0.0367  87  LEU A O   
702  C CB  . LEU A 87  ? 0.3291 0.3079 0.3374 0.0393  0.0630  0.0305  87  LEU A CB  
703  C CG  . LEU A 87  ? 0.3210 0.3035 0.3310 0.0364  0.0514  0.0199  87  LEU A CG  
704  C CD1 . LEU A 87  ? 0.3118 0.2929 0.3375 0.0310  0.0471  0.0177  87  LEU A CD1 
705  C CD2 . LEU A 87  ? 0.3362 0.3242 0.3515 0.0340  0.0510  0.0136  87  LEU A CD2 
706  N N   . ARG A 88  ? 0.3407 0.3143 0.3209 0.0496  0.0462  0.0318  88  ARG A N   
707  C CA  . ARG A 88  ? 0.3370 0.3137 0.3051 0.0536  0.0357  0.0256  88  ARG A CA  
708  C C   . ARG A 88  ? 0.3201 0.3003 0.3026 0.0473  0.0287  0.0156  88  ARG A C   
709  O O   . ARG A 88  ? 0.3361 0.3146 0.3339 0.0423  0.0294  0.0155  88  ARG A O   
710  C CB  . ARG A 88  ? 0.3630 0.3355 0.3244 0.0596  0.0326  0.0330  88  ARG A CB  
711  C CG  . ARG A 88  ? 0.3809 0.3498 0.3238 0.0674  0.0394  0.0452  88  ARG A CG  
712  C CD  . ARG A 88  ? 0.4082 0.3826 0.3277 0.0736  0.0377  0.0409  88  ARG A CD  
713  N NE  . ARG A 88  ? 0.4293 0.4015 0.3269 0.0819  0.0454  0.0528  88  ARG A NE  
714  C CZ  . ARG A 88  ? 0.4214 0.3929 0.3147 0.0821  0.0589  0.0588  88  ARG A CZ  
715  N NH1 . ARG A 88  ? 0.4006 0.3728 0.3140 0.0740  0.0659  0.0555  88  ARG A NH1 
716  N NH2 . ARG A 88  ? 0.4564 0.4271 0.3259 0.0909  0.0660  0.0694  88  ARG A NH2 
717  N N   . VAL A 89  ? 0.3197 0.3050 0.2985 0.0473  0.0227  0.0070  89  VAL A N   
718  C CA  . VAL A 89  ? 0.3319 0.3205 0.3244 0.0412  0.0184  0.0000  89  VAL A CA  
719  C C   . VAL A 89  ? 0.3089 0.3008 0.3001 0.0433  0.0096  -0.0061 89  VAL A C   
720  O O   . VAL A 89  ? 0.3542 0.3476 0.3344 0.0487  0.0054  -0.0085 89  VAL A O   
721  C CB  . VAL A 89  ? 0.3365 0.3278 0.3347 0.0371  0.0211  -0.0034 89  VAL A CB  
722  C CG1 . VAL A 89  ? 0.3615 0.3547 0.3500 0.0410  0.0206  -0.0071 89  VAL A CG1 
723  C CG2 . VAL A 89  ? 0.3442 0.3389 0.3538 0.0318  0.0169  -0.0084 89  VAL A CG2 
724  N N   . TYR A 90  ? 0.3060 0.2999 0.3095 0.0392  0.0069  -0.0093 90  TYR A N   
725  C CA  . TYR A 90  ? 0.3048 0.3025 0.3127 0.0403  -0.0002 -0.0147 90  TYR A CA  
726  C C   . TYR A 90  ? 0.2915 0.2929 0.3119 0.0342  0.0001  -0.0189 90  TYR A C   
727  O O   . TYR A 90  ? 0.2926 0.2933 0.3171 0.0300  0.0046  -0.0170 90  TYR A O   
728  C CB  . TYR A 90  ? 0.2919 0.2885 0.3033 0.0431  -0.0027 -0.0125 90  TYR A CB  
729  C CG  . TYR A 90  ? 0.3230 0.3143 0.3237 0.0490  -0.0012 -0.0046 90  TYR A CG  
730  C CD1 . TYR A 90  ? 0.3296 0.3154 0.3309 0.0471  0.0066  0.0021  90  TYR A CD1 
731  C CD2 . TYR A 90  ? 0.3382 0.3301 0.3293 0.0566  -0.0077 -0.0033 90  TYR A CD2 
732  C CE1 . TYR A 90  ? 0.3480 0.3281 0.3414 0.0522  0.0098  0.0113  90  TYR A CE1 
733  C CE2 . TYR A 90  ? 0.3490 0.3357 0.3286 0.0626  -0.0057 0.0064  90  TYR A CE2 
734  C CZ  . TYR A 90  ? 0.3589 0.3393 0.3400 0.0602  0.0041  0.0145  90  TYR A CZ  
735  O OH  . TYR A 90  ? 0.3678 0.3420 0.3411 0.0654  0.0085  0.0262  90  TYR A OH  
736  N N   . VAL A 91  ? 0.2820 0.2875 0.3092 0.0341  -0.0048 -0.0243 91  VAL A N   
737  C CA  . VAL A 91  ? 0.2735 0.2826 0.3135 0.0290  -0.0033 -0.0262 91  VAL A CA  
738  C C   . VAL A 91  ? 0.2951 0.3079 0.3453 0.0298  -0.0060 -0.0287 91  VAL A C   
739  O O   . VAL A 91  ? 0.3536 0.3684 0.4062 0.0336  -0.0124 -0.0323 91  VAL A O   
740  C CB  . VAL A 91  ? 0.2904 0.3012 0.3364 0.0270  -0.0046 -0.0292 91  VAL A CB  
741  C CG1 . VAL A 91  ? 0.2703 0.2843 0.3295 0.0220  -0.0016 -0.0283 91  VAL A CG1 
742  C CG2 . VAL A 91  ? 0.2904 0.2980 0.3287 0.0268  -0.0017 -0.0271 91  VAL A CG2 
743  N N   . HIS A 92  ? 0.2730 0.2875 0.3292 0.0266  -0.0013 -0.0275 92  HIS A N   
744  C CA  . HIS A 92  ? 0.2712 0.2905 0.3406 0.0264  -0.0015 -0.0303 92  HIS A CA  
745  C C   . HIS A 92  ? 0.2480 0.2716 0.3263 0.0215  0.0035  -0.0300 92  HIS A C   
746  O O   . HIS A 92  ? 0.2411 0.2642 0.3131 0.0185  0.0086  -0.0268 92  HIS A O   
747  C CB  . HIS A 92  ? 0.2471 0.2651 0.3165 0.0281  0.0008  -0.0298 92  HIS A CB  
748  C CG  . HIS A 92  ? 0.2309 0.2548 0.3147 0.0273  0.0035  -0.0330 92  HIS A CG  
749  N ND1 . HIS A 92  ? 0.2086 0.2353 0.2934 0.0237  0.0110  -0.0333 92  HIS A ND1 
750  C CD2 . HIS A 92  ? 0.2319 0.2601 0.3297 0.0300  0.0001  -0.0362 92  HIS A CD2 
751  C CE1 . HIS A 92  ? 0.2012 0.2336 0.2997 0.0241  0.0139  -0.0363 92  HIS A CE1 
752  N NE2 . HIS A 92  ? 0.2154 0.2490 0.3242 0.0276  0.0072  -0.0382 92  HIS A NE2 
753  N N   . THR A 93  ? 0.2259 0.2542 0.3199 0.0210  0.0017  -0.0329 93  THR A N   
754  C CA  . THR A 93  ? 0.2415 0.2733 0.3463 0.0165  0.0073  -0.0307 93  THR A CA  
755  C C   . THR A 93  ? 0.2468 0.2842 0.3608 0.0153  0.0141  -0.0305 93  THR A C   
756  O O   . THR A 93  ? 0.2574 0.2964 0.3748 0.0183  0.0124  -0.0340 93  THR A O   
757  C CB  . THR A 93  ? 0.2328 0.2663 0.3546 0.0157  0.0028  -0.0341 93  THR A CB  
758  O OG1 . THR A 93  ? 0.2228 0.2620 0.3621 0.0171  0.0000  -0.0391 93  THR A OG1 
759  C CG2 . THR A 93  ? 0.2331 0.2622 0.3467 0.0184  -0.0050 -0.0377 93  THR A CG2 
760  N N   . ARG A 94  ? 0.2598 0.3003 0.3786 0.0116  0.0221  -0.0259 94  ARG A N   
761  C CA  . ARG A 94  ? 0.2628 0.3096 0.3879 0.0104  0.0314  -0.0245 94  ARG A CA  
762  C C   . ARG A 94  ? 0.2554 0.3081 0.4057 0.0108  0.0312  -0.0288 94  ARG A C   
763  O O   . ARG A 94  ? 0.2820 0.3409 0.4407 0.0104  0.0397  -0.0287 94  ARG A O   
764  C CB  . ARG A 94  ? 0.2867 0.3352 0.4096 0.0069  0.0401  -0.0162 94  ARG A CB  
765  C CG  . ARG A 94  ? 0.3202 0.3682 0.4622 0.0041  0.0399  -0.0128 94  ARG A CG  
766  C CD  . ARG A 94  ? 0.3706 0.4248 0.5304 0.0012  0.0512  -0.0070 94  ARG A CD  
767  N NE  . ARG A 94  ? 0.4921 0.5474 0.6325 0.0008  0.0603  0.0019  94  ARG A NE  
768  C CZ  . ARG A 94  ? 0.5300 0.5919 0.6655 0.0013  0.0713  0.0045  94  ARG A CZ  
769  N NH1 . ARG A 94  ? 0.5783 0.6410 0.6874 0.0029  0.0748  0.0081  94  ARG A NH1 
770  N NH2 . ARG A 94  ? 0.4548 0.5233 0.6115 0.0007  0.0778  0.0018  94  ARG A NH2 
771  N N   . ASN A 95  ? 0.2719 0.3239 0.4352 0.0118  0.0218  -0.0332 95  ASN A N   
772  C CA  . ASN A 95  ? 0.2598 0.3184 0.4502 0.0124  0.0190  -0.0387 95  ASN A CA  
773  C C   . ASN A 95  ? 0.2486 0.3071 0.4371 0.0182  0.0084  -0.0452 95  ASN A C   
774  O O   . ASN A 95  ? 0.2613 0.3252 0.4710 0.0201  0.0017  -0.0510 95  ASN A O   
775  C CB  . ASN A 95  ? 0.2832 0.3426 0.4940 0.0096  0.0150  -0.0404 95  ASN A CB  
776  C CG  . ASN A 95  ? 0.3338 0.3932 0.5516 0.0042  0.0265  -0.0319 95  ASN A CG  
777  O OD1 . ASN A 95  ? 0.3249 0.3894 0.5495 0.0023  0.0382  -0.0269 95  ASN A OD1 
778  N ND2 . ASN A 95  ? 0.3731 0.4266 0.5880 0.0024  0.0239  -0.0295 95  ASN A ND2 
779  N N   . ASP A 96  ? 0.2200 0.2723 0.3847 0.0212  0.0063  -0.0437 96  ASP A N   
780  C CA  . ASP A 96  ? 0.2195 0.2703 0.3805 0.0271  -0.0024 -0.0469 96  ASP A CA  
781  C C   . ASP A 96  ? 0.2291 0.2791 0.3905 0.0305  -0.0153 -0.0508 96  ASP A C   
782  O O   . ASP A 96  ? 0.2227 0.2768 0.3952 0.0351  -0.0242 -0.0553 96  ASP A O   
783  C CB  . ASP A 96  ? 0.2380 0.2954 0.4180 0.0292  0.0001  -0.0500 96  ASP A CB  
784  C CG  . ASP A 96  ? 0.2874 0.3431 0.4592 0.0295  0.0093  -0.0486 96  ASP A CG  
785  O OD1 . ASP A 96  ? 0.3005 0.3491 0.4502 0.0287  0.0119  -0.0454 96  ASP A OD1 
786  O OD2 . ASP A 96  ? 0.3017 0.3637 0.4914 0.0309  0.0133  -0.0519 96  ASP A OD2 
787  N N   . TYR A 97  ? 0.2217 0.2668 0.3694 0.0289  -0.0167 -0.0495 97  TYR A N   
788  C CA  . TYR A 97  ? 0.2334 0.2759 0.3707 0.0332  -0.0274 -0.0530 97  TYR A CA  
789  C C   . TYR A 97  ? 0.2547 0.2891 0.3648 0.0348  -0.0251 -0.0474 97  TYR A C   
790  O O   . TYR A 97  ? 0.2826 0.3135 0.3850 0.0309  -0.0164 -0.0423 97  TYR A O   
791  C CB  . TYR A 97  ? 0.2349 0.2787 0.3827 0.0304  -0.0308 -0.0581 97  TYR A CB  
792  C CG  . TYR A 97  ? 0.2268 0.2788 0.4062 0.0285  -0.0337 -0.0643 97  TYR A CG  
793  C CD1 . TYR A 97  ? 0.2283 0.2839 0.4266 0.0228  -0.0227 -0.0604 97  TYR A CD1 
794  C CD2 . TYR A 97  ? 0.2239 0.2811 0.4148 0.0330  -0.0473 -0.0738 97  TYR A CD2 
795  C CE1 . TYR A 97  ? 0.2203 0.2840 0.4513 0.0208  -0.0236 -0.0653 97  TYR A CE1 
796  C CE2 . TYR A 97  ? 0.2163 0.2822 0.4413 0.0309  -0.0502 -0.0802 97  TYR A CE2 
797  C CZ  . TYR A 97  ? 0.2174 0.2863 0.4641 0.0244  -0.0376 -0.0756 97  TYR A CZ  
798  O OH  . TYR A 97  ? 0.2563 0.3341 0.5399 0.0217  -0.0376 -0.0804 97  TYR A OH  
799  N N   . VAL A 98  ? 0.2527 0.2847 0.3487 0.0408  -0.0332 -0.0485 98  VAL A N   
800  C CA  . VAL A 98  ? 0.2583 0.2831 0.3310 0.0424  -0.0301 -0.0428 98  VAL A CA  
801  C C   . VAL A 98  ? 0.2689 0.2928 0.3305 0.0451  -0.0356 -0.0469 98  VAL A C   
802  O O   . VAL A 98  ? 0.2801 0.3082 0.3448 0.0493  -0.0454 -0.0540 98  VAL A O   
803  C CB  . VAL A 98  ? 0.2783 0.3000 0.3422 0.0478  -0.0312 -0.0375 98  VAL A CB  
804  C CG1 . VAL A 98  ? 0.2917 0.3065 0.3333 0.0509  -0.0289 -0.0313 98  VAL A CG1 
805  C CG2 . VAL A 98  ? 0.2800 0.3013 0.3540 0.0445  -0.0236 -0.0348 98  VAL A CG2 
806  N N   . ILE A 99  ? 0.2766 0.2957 0.3261 0.0430  -0.0293 -0.0435 99  ILE A N   
807  C CA  . ILE A 99  ? 0.2961 0.3134 0.3319 0.0463  -0.0321 -0.0467 99  ILE A CA  
808  C C   . ILE A 99  ? 0.3326 0.3448 0.3469 0.0502  -0.0276 -0.0390 99  ILE A C   
809  O O   . ILE A 99  ? 0.3349 0.3433 0.3480 0.0465  -0.0193 -0.0322 99  ILE A O   
810  C CB  . ILE A 99  ? 0.2879 0.3042 0.3314 0.0409  -0.0277 -0.0491 99  ILE A CB  
811  C CG1 . ILE A 99  ? 0.2781 0.2987 0.3462 0.0364  -0.0299 -0.0542 99  ILE A CG1 
812  C CG2 . ILE A 99  ? 0.3069 0.3218 0.3373 0.0451  -0.0301 -0.0542 99  ILE A CG2 
813  C CD1 . ILE A 99  ? 0.2875 0.3061 0.3659 0.0306  -0.0239 -0.0526 99  ILE A CD1 
814  N N   . TYR A 100 ? 0.3618 0.3746 0.3605 0.0579  -0.0338 -0.0404 100 TYR A N   
815  C CA  . TYR A 100 ? 0.3615 0.3701 0.3380 0.0633  -0.0298 -0.0329 100 TYR A CA  
816  C C   . TYR A 100 ? 0.3646 0.3727 0.3301 0.0641  -0.0265 -0.0369 100 TYR A C   
817  O O   . TYR A 100 ? 0.3728 0.3847 0.3419 0.0649  -0.0329 -0.0477 100 TYR A O   
818  C CB  . TYR A 100 ? 0.3605 0.3714 0.3249 0.0724  -0.0391 -0.0323 100 TYR A CB  
819  C CG  . TYR A 100 ? 0.3546 0.3662 0.3324 0.0727  -0.0430 -0.0287 100 TYR A CG  
820  C CD1 . TYR A 100 ? 0.3570 0.3628 0.3321 0.0737  -0.0368 -0.0171 100 TYR A CD1 
821  C CD2 . TYR A 100 ? 0.3372 0.3556 0.3339 0.0720  -0.0522 -0.0374 100 TYR A CD2 
822  C CE1 . TYR A 100 ? 0.3553 0.3616 0.3441 0.0749  -0.0403 -0.0147 100 TYR A CE1 
823  C CE2 . TYR A 100 ? 0.3225 0.3424 0.3331 0.0730  -0.0552 -0.0347 100 TYR A CE2 
824  C CZ  . TYR A 100 ? 0.3479 0.3615 0.3535 0.0748  -0.0494 -0.0236 100 TYR A CZ  
825  O OH  . TYR A 100 ? 0.3786 0.3930 0.3996 0.0761  -0.0515 -0.0214 100 TYR A OH  
826  N N   . ILE A 101 ? 0.3678 0.3714 0.3224 0.0641  -0.0165 -0.0287 101 ILE A N   
827  C CA  . ILE A 101 ? 0.3752 0.3783 0.3237 0.0638  -0.0107 -0.0317 101 ILE A CA  
828  C C   . ILE A 101 ? 0.3792 0.3800 0.3048 0.0705  -0.0041 -0.0240 101 ILE A C   
829  O O   . ILE A 101 ? 0.3880 0.3846 0.3125 0.0697  0.0035  -0.0124 101 ILE A O   
830  C CB  . ILE A 101 ? 0.3754 0.3765 0.3407 0.0553  -0.0031 -0.0291 101 ILE A CB  
831  C CG1 . ILE A 101 ? 0.3678 0.3711 0.3536 0.0491  -0.0078 -0.0340 101 ILE A CG1 
832  C CG2 . ILE A 101 ? 0.3777 0.3787 0.3403 0.0553  0.0032  -0.0317 101 ILE A CG2 
833  C CD1 . ILE A 101 ? 0.3701 0.3718 0.3680 0.0421  -0.0012 -0.0285 101 ILE A CD1 
834  N N   . LYS A 102 ? 0.3959 0.3996 0.3036 0.0775  -0.0062 -0.0304 102 LYS A N   
835  C CA  . LYS A 102 ? 0.4492 0.4513 0.3331 0.0844  0.0022  -0.0220 102 LYS A CA  
836  C C   . LYS A 102 ? 0.4366 0.4361 0.3280 0.0795  0.0162  -0.0171 102 LYS A C   
837  O O   . LYS A 102 ? 0.4694 0.4701 0.3758 0.0743  0.0169  -0.0248 102 LYS A O   
838  C CB  . LYS A 102 ? 0.5365 0.5435 0.3956 0.0945  -0.0045 -0.0309 102 LYS A CB  
839  C CG  . LYS A 102 ? 0.6120 0.6214 0.4611 0.1010  -0.0175 -0.0304 102 LYS A CG  
840  C CD  . LYS A 102 ? 0.7733 0.7856 0.5879 0.1136  -0.0202 -0.0286 102 LYS A CD  
841  C CE  . LYS A 102 ? 0.8507 0.8646 0.6580 0.1200  -0.0325 -0.0237 102 LYS A CE  
842  N NZ  . LYS A 102 ? 0.9909 1.0112 0.7660 0.1329  -0.0421 -0.0298 102 LYS A NZ  
843  N N   . PRO A 103 ? 0.4488 0.4445 0.3341 0.0805  0.0277  -0.0033 103 PRO A N   
844  C CA  . PRO A 103 ? 0.4731 0.4672 0.3713 0.0751  0.0403  0.0011  103 PRO A CA  
845  C C   . PRO A 103 ? 0.4869 0.4849 0.3843 0.0760  0.0444  -0.0086 103 PRO A C   
846  O O   . PRO A 103 ? 0.4241 0.4224 0.3415 0.0696  0.0489  -0.0101 103 PRO A O   
847  C CB  . PRO A 103 ? 0.5023 0.4929 0.3880 0.0794  0.0520  0.0165  103 PRO A CB  
848  C CG  . PRO A 103 ? 0.5314 0.5191 0.4094 0.0830  0.0441  0.0228  103 PRO A CG  
849  C CD  . PRO A 103 ? 0.5016 0.4942 0.3713 0.0866  0.0290  0.0093  103 PRO A CD  
850  N N   . GLU A 104 ? 0.4931 0.4944 0.3675 0.0846  0.0422  -0.0157 104 GLU A N   
851  C CA  . GLU A 104 ? 0.5453 0.5500 0.4156 0.0874  0.0481  -0.0250 104 GLU A CA  
852  C C   . GLU A 104 ? 0.4992 0.5057 0.3878 0.0833  0.0382  -0.0406 104 GLU A C   
853  O O   . GLU A 104 ? 0.5690 0.5779 0.4588 0.0854  0.0414  -0.0506 104 GLU A O   
854  C CB  . GLU A 104 ? 0.5925 0.6005 0.4285 0.0992  0.0506  -0.0271 104 GLU A CB  
855  C CG  . GLU A 104 ? 0.6735 0.6840 0.4917 0.1056  0.0348  -0.0351 104 GLU A CG  
856  C CD  . GLU A 104 ? 0.7728 0.7806 0.5798 0.1084  0.0307  -0.0213 104 GLU A CD  
857  O OE1 . GLU A 104 ? 0.9247 0.9355 0.7043 0.1183  0.0241  -0.0223 104 GLU A OE1 
858  O OE2 . GLU A 104 ? 0.7328 0.7358 0.5582 0.1014  0.0338  -0.0097 104 GLU A OE2 
859  N N   . THR A 105 ? 0.4526 0.4579 0.3564 0.0779  0.0272  -0.0424 105 THR A N   
860  C CA  . THR A 105 ? 0.4616 0.4679 0.3844 0.0739  0.0184  -0.0551 105 THR A CA  
861  C C   . THR A 105 ? 0.4790 0.4846 0.4228 0.0686  0.0253  -0.0562 105 THR A C   
862  O O   . THR A 105 ? 0.4261 0.4300 0.3822 0.0631  0.0315  -0.0463 105 THR A O   
863  C CB  . THR A 105 ? 0.4141 0.4194 0.3516 0.0682  0.0089  -0.0530 105 THR A CB  
864  O OG1 . THR A 105 ? 0.4352 0.4415 0.3569 0.0732  0.0021  -0.0511 105 THR A OG1 
865  C CG2 . THR A 105 ? 0.4188 0.4250 0.3767 0.0644  0.0005  -0.0645 105 THR A CG2 
866  N N   . ARG A 106 ? 0.5186 0.5254 0.4698 0.0702  0.0228  -0.0693 106 ARG A N   
867  C CA  . ARG A 106 ? 0.5558 0.5615 0.5300 0.0656  0.0276  -0.0701 106 ARG A CA  
868  C C   . ARG A 106 ? 0.4709 0.4748 0.4681 0.0601  0.0181  -0.0751 106 ARG A C   
869  O O   . ARG A 106 ? 0.4579 0.4618 0.4616 0.0623  0.0126  -0.0881 106 ARG A O   
870  C CB  . ARG A 106 ? 0.6643 0.6720 0.6345 0.0716  0.0344  -0.0801 106 ARG A CB  
871  C CG  . ARG A 106 ? 0.7498 0.7569 0.7448 0.0680  0.0407  -0.0793 106 ARG A CG  
872  C CD  . ARG A 106 ? 0.9094 0.9188 0.9017 0.0746  0.0482  -0.0906 106 ARG A CD  
873  N NE  . ARG A 106 ? 1.0268 1.0357 1.0464 0.0721  0.0529  -0.0914 106 ARG A NE  
874  C CZ  . ARG A 106 ? 1.1292 1.1350 1.1739 0.0688  0.0458  -0.0969 106 ARG A CZ  
875  N NH1 . ARG A 106 ? 1.2096 1.2125 1.2579 0.0665  0.0344  -0.1016 106 ARG A NH1 
876  N NH2 . ARG A 106 ? 1.0860 1.0916 1.1545 0.0680  0.0503  -0.0969 106 ARG A NH2 
877  N N   . LEU A 107 ? 0.4879 0.4904 0.4984 0.0532  0.0171  -0.0649 107 LEU A N   
878  C CA  . LEU A 107 ? 0.4679 0.4688 0.5000 0.0478  0.0106  -0.0662 107 LEU A CA  
879  C C   . LEU A 107 ? 0.4248 0.4241 0.4763 0.0474  0.0126  -0.0710 107 LEU A C   
880  O O   . LEU A 107 ? 0.4085 0.4083 0.4629 0.0479  0.0198  -0.0671 107 LEU A O   
881  C CB  . LEU A 107 ? 0.4975 0.4980 0.5361 0.0416  0.0115  -0.0534 107 LEU A CB  
882  C CG  . LEU A 107 ? 0.5290 0.5301 0.5627 0.0395  0.0065  -0.0500 107 LEU A CG  
883  C CD1 . LEU A 107 ? 0.5636 0.5645 0.6108 0.0333  0.0066  -0.0417 107 LEU A CD1 
884  C CD2 . LEU A 107 ? 0.5568 0.5587 0.5922 0.0414  -0.0016 -0.0596 107 LEU A CD2 
885  N N   . PRO A 108 ? 0.3589 0.3561 0.4281 0.0460  0.0064  -0.0788 108 PRO A N   
886  C CA  . PRO A 108 ? 0.3303 0.3246 0.4232 0.0447  0.0079  -0.0802 108 PRO A CA  
887  C C   . PRO A 108 ? 0.3374 0.3318 0.4382 0.0405  0.0120  -0.0654 108 PRO A C   
888  O O   . PRO A 108 ? 0.3066 0.3016 0.4055 0.0361  0.0103  -0.0557 108 PRO A O   
889  C CB  . PRO A 108 ? 0.3346 0.3261 0.4470 0.0417  0.0006  -0.0853 108 PRO A CB  
890  C CG  . PRO A 108 ? 0.3500 0.3442 0.4478 0.0443  -0.0056 -0.0946 108 PRO A CG  
891  C CD  . PRO A 108 ? 0.3599 0.3575 0.4302 0.0460  -0.0023 -0.0867 108 PRO A CD  
892  N N   . ARG A 109 ? 0.3809 0.3755 0.4902 0.0423  0.0173  -0.0647 109 ARG A N   
893  C CA  . ARG A 109 ? 0.3697 0.3651 0.4901 0.0391  0.0192  -0.0525 109 ARG A CA  
894  C C   . ARG A 109 ? 0.3523 0.3442 0.4928 0.0356  0.0142  -0.0471 109 ARG A C   
895  O O   . ARG A 109 ? 0.3520 0.3450 0.4959 0.0323  0.0129  -0.0351 109 ARG A O   
896  C CB  . ARG A 109 ? 0.4115 0.4088 0.5411 0.0427  0.0253  -0.0545 109 ARG A CB  
897  C CG  . ARG A 109 ? 0.4897 0.4913 0.6026 0.0453  0.0330  -0.0547 109 ARG A CG  
898  C CD  . ARG A 109 ? 0.5800 0.5820 0.6747 0.0509  0.0370  -0.0661 109 ARG A CD  
899  N NE  . ARG A 109 ? 0.6839 0.6864 0.7549 0.0507  0.0353  -0.0639 109 ARG A NE  
900  C CZ  . ARG A 109 ? 0.6869 0.6917 0.7439 0.0504  0.0407  -0.0560 109 ARG A CZ  
901  N NH1 . ARG A 109 ? 0.6543 0.6584 0.6963 0.0490  0.0371  -0.0518 109 ARG A NH1 
902  N NH2 . ARG A 109 ? 0.7147 0.7225 0.7765 0.0512  0.0498  -0.0516 109 ARG A NH2 
903  N N   . ASN A 110 ? 0.3329 0.3207 0.4871 0.0366  0.0114  -0.0561 110 ASN A N   
904  C CA  . ASN A 110 ? 0.3239 0.3070 0.5013 0.0337  0.0085  -0.0503 110 ASN A CA  
905  C C   . ASN A 110 ? 0.3446 0.3275 0.5194 0.0293  0.0050  -0.0461 110 ASN A C   
906  O O   . ASN A 110 ? 0.3343 0.3175 0.5033 0.0298  0.0023  -0.0562 110 ASN A O   
907  C CB  . ASN A 110 ? 0.3185 0.2965 0.5180 0.0363  0.0074  -0.0626 110 ASN A CB  
908  C CG  . ASN A 110 ? 0.3509 0.3230 0.5778 0.0332  0.0055  -0.0542 110 ASN A CG  
909  O OD1 . ASN A 110 ? 0.3427 0.3125 0.5774 0.0298  0.0027  -0.0542 110 ASN A OD1 
910  N ND2 . ASN A 110 ? 0.3753 0.3449 0.6194 0.0348  0.0072  -0.0473 110 ASN A ND2 
911  N N   . TYR A 111 ? 0.3197 0.3022 0.5006 0.0257  0.0051  -0.0316 111 TYR A N   
912  C CA  . TYR A 111 ? 0.3061 0.2898 0.4825 0.0217  0.0040  -0.0258 111 TYR A CA  
913  C C   . TYR A 111 ? 0.2997 0.2801 0.4930 0.0203  0.0016  -0.0345 111 TYR A C   
914  O O   . TYR A 111 ? 0.2697 0.2529 0.4562 0.0185  -0.0001 -0.0376 111 TYR A O   
915  C CB  . TYR A 111 ? 0.2989 0.2825 0.4809 0.0192  0.0055  -0.0089 111 TYR A CB  
916  C CG  . TYR A 111 ? 0.2997 0.2847 0.4802 0.0153  0.0065  -0.0018 111 TYR A CG  
917  C CD1 . TYR A 111 ? 0.3251 0.3153 0.4846 0.0140  0.0068  -0.0018 111 TYR A CD1 
918  C CD2 . TYR A 111 ? 0.3109 0.2917 0.5130 0.0129  0.0083  0.0055  111 TYR A CD2 
919  C CE1 . TYR A 111 ? 0.3224 0.3147 0.4815 0.0108  0.0090  0.0044  111 TYR A CE1 
920  C CE2 . TYR A 111 ? 0.3214 0.3043 0.5233 0.0095  0.0114  0.0130  111 TYR A CE2 
921  C CZ  . TYR A 111 ? 0.3372 0.3263 0.5171 0.0085  0.0117  0.0118  111 TYR A CZ  
922  O OH  . TYR A 111 ? 0.4177 0.4095 0.5983 0.0055  0.0158  0.0187  111 TYR A OH  
923  N N   . ASN A 112 ? 0.2922 0.2669 0.5109 0.0209  0.0011  -0.0384 112 ASN A N   
924  C CA  . ASN A 112 ? 0.3040 0.2753 0.5454 0.0188  -0.0014 -0.0463 112 ASN A CA  
925  C C   . ASN A 112 ? 0.3151 0.2889 0.5476 0.0219  -0.0064 -0.0664 112 ASN A C   
926  O O   . ASN A 112 ? 0.3364 0.3110 0.5792 0.0199  -0.0104 -0.0738 112 ASN A O   
927  C CB  . ASN A 112 ? 0.3024 0.2658 0.5777 0.0183  -0.0002 -0.0438 112 ASN A CB  
928  C CG  . ASN A 112 ? 0.3260 0.2873 0.6082 0.0159  0.0043  -0.0215 112 ASN A CG  
929  O OD1 . ASN A 112 ? 0.3207 0.2844 0.5983 0.0123  0.0067  -0.0100 112 ASN A OD1 
930  N ND2 . ASN A 112 ? 0.3345 0.2919 0.6271 0.0186  0.0054  -0.0151 112 ASN A ND2 
931  N N   . ARG A 113 ? 0.3388 0.3147 0.5523 0.0269  -0.0062 -0.0745 113 ARG A N   
932  C CA  . ARG A 113 ? 0.3990 0.3784 0.5970 0.0311  -0.0107 -0.0917 113 ARG A CA  
933  C C   . ARG A 113 ? 0.3664 0.3516 0.5399 0.0303  -0.0123 -0.0873 113 ARG A C   
934  O O   . ARG A 113 ? 0.3536 0.3417 0.5226 0.0317  -0.0184 -0.0980 113 ARG A O   
935  C CB  . ARG A 113 ? 0.4810 0.4613 0.6648 0.0374  -0.0081 -0.1010 113 ARG A CB  
936  C CG  . ARG A 113 ? 0.6197 0.5964 0.8221 0.0410  -0.0108 -0.1193 113 ARG A CG  
937  C CD  . ARG A 113 ? 0.7938 0.7734 0.9757 0.0482  -0.0070 -0.1295 113 ARG A CD  
938  N NE  . ARG A 113 ? 0.9105 0.8865 1.1119 0.0522  -0.0069 -0.1456 113 ARG A NE  
939  C CZ  . ARG A 113 ? 0.9404 0.9147 1.1496 0.0553  0.0000  -0.1454 113 ARG A CZ  
940  N NH1 . ARG A 113 ? 0.9255 0.9021 1.1246 0.0548  0.0071  -0.1301 113 ARG A NH1 
941  N NH2 . ARG A 113 ? 0.9429 0.9134 1.1729 0.0590  -0.0005 -0.1619 113 ARG A NH2 
942  N N   . PHE A 114 ? 0.3122 0.2991 0.4721 0.0282  -0.0075 -0.0721 114 PHE A N   
943  C CA  . PHE A 114 ? 0.3108 0.3021 0.4515 0.0272  -0.0082 -0.0669 114 PHE A CA  
944  C C   . PHE A 114 ? 0.3011 0.2933 0.4572 0.0232  -0.0116 -0.0668 114 PHE A C   
945  O O   . PHE A 114 ? 0.2757 0.2717 0.4226 0.0243  -0.0159 -0.0721 114 PHE A O   
946  C CB  . PHE A 114 ? 0.3243 0.3167 0.4538 0.0251  -0.0028 -0.0520 114 PHE A CB  
947  C CG  . PHE A 114 ? 0.3243 0.3203 0.4406 0.0230  -0.0028 -0.0455 114 PHE A CG  
948  C CD1 . PHE A 114 ? 0.3540 0.3526 0.4500 0.0260  -0.0040 -0.0493 114 PHE A CD1 
949  C CD2 . PHE A 114 ? 0.2946 0.2912 0.4194 0.0185  -0.0011 -0.0357 114 PHE A CD2 
950  C CE1 . PHE A 114 ? 0.3491 0.3504 0.4363 0.0244  -0.0040 -0.0440 114 PHE A CE1 
951  C CE2 . PHE A 114 ? 0.2863 0.2865 0.4002 0.0170  -0.0005 -0.0314 114 PHE A CE2 
952  C CZ  . PHE A 114 ? 0.3170 0.3192 0.4135 0.0198  -0.0022 -0.0359 114 PHE A CZ  
953  N N   . ILE A 115 ? 0.2889 0.2778 0.4696 0.0190  -0.0093 -0.0599 115 ILE A N   
954  C CA  . ILE A 115 ? 0.2816 0.2713 0.4819 0.0147  -0.0102 -0.0581 115 ILE A CA  
955  C C   . ILE A 115 ? 0.2874 0.2781 0.5011 0.0162  -0.0181 -0.0759 115 ILE A C   
956  O O   . ILE A 115 ? 0.2752 0.2707 0.4895 0.0153  -0.0219 -0.0795 115 ILE A O   
957  C CB  . ILE A 115 ? 0.2883 0.2733 0.5130 0.0106  -0.0049 -0.0460 115 ILE A CB  
958  C CG1 . ILE A 115 ? 0.3171 0.3033 0.5262 0.0093  0.0014  -0.0281 115 ILE A CG1 
959  C CG2 . ILE A 115 ? 0.2929 0.2780 0.5455 0.0062  -0.0050 -0.0468 115 ILE A CG2 
960  C CD1 . ILE A 115 ? 0.3589 0.3510 0.5524 0.0074  0.0035  -0.0221 115 ILE A CD1 
961  N N   . GLY A 116 ? 0.2933 0.2800 0.5177 0.0189  -0.0210 -0.0877 116 GLY A N   
962  C CA  . GLY A 116 ? 0.2946 0.2826 0.5295 0.0217  -0.0299 -0.1081 116 GLY A CA  
963  C C   . GLY A 116 ? 0.3232 0.3182 0.5302 0.0263  -0.0364 -0.1163 116 GLY A C   
964  O O   . GLY A 116 ? 0.3430 0.3425 0.5592 0.0266  -0.0447 -0.1268 116 GLY A O   
965  N N   . LEU A 117 ? 0.3194 0.3157 0.4940 0.0299  -0.0325 -0.1098 117 LEU A N   
966  C CA  . LEU A 117 ? 0.3293 0.3311 0.4750 0.0353  -0.0371 -0.1146 117 LEU A CA  
967  C C   . LEU A 117 ? 0.3296 0.3356 0.4747 0.0325  -0.0389 -0.1070 117 LEU A C   
968  O O   . LEU A 117 ? 0.3671 0.3782 0.5042 0.0362  -0.0473 -0.1154 117 LEU A O   
969  C CB  . LEU A 117 ? 0.3424 0.3433 0.4593 0.0389  -0.0301 -0.1071 117 LEU A CB  
970  C CG  . LEU A 117 ? 0.3827 0.3880 0.4683 0.0448  -0.0327 -0.1085 117 LEU A CG  
971  C CD1 . LEU A 117 ? 0.4162 0.4246 0.4950 0.0516  -0.0418 -0.1271 117 LEU A CD1 
972  C CD2 . LEU A 117 ? 0.3876 0.3916 0.4508 0.0470  -0.0235 -0.0986 117 LEU A CD2 
973  N N   . MET A 118 ? 0.3078 0.3123 0.4609 0.0267  -0.0314 -0.0917 118 MET A N   
974  C CA  . MET A 118 ? 0.3191 0.3278 0.4743 0.0239  -0.0313 -0.0849 118 MET A CA  
975  C C   . MET A 118 ? 0.3123 0.3242 0.4970 0.0214  -0.0376 -0.0937 118 MET A C   
976  O O   . MET A 118 ? 0.2866 0.3041 0.4720 0.0220  -0.0419 -0.0954 118 MET A O   
977  C CB  . MET A 118 ? 0.3173 0.3243 0.4739 0.0188  -0.0214 -0.0681 118 MET A CB  
978  C CG  . MET A 118 ? 0.3651 0.3707 0.4945 0.0208  -0.0165 -0.0598 118 MET A CG  
979  S SD  . MET A 118 ? 0.3515 0.3608 0.4536 0.0257  -0.0196 -0.0609 118 MET A SD  
980  C CE  . MET A 118 ? 0.3998 0.4078 0.4848 0.0327  -0.0235 -0.0713 118 MET A CE  
981  N N   . GLU A 119 ? 0.3005 0.3089 0.5130 0.0185  -0.0377 -0.0987 119 GLU A N   
982  C CA  . GLU A 119 ? 0.3463 0.3576 0.5924 0.0155  -0.0434 -0.1079 119 GLU A CA  
983  C C   . GLU A 119 ? 0.3679 0.3850 0.6070 0.0215  -0.0572 -0.1265 119 GLU A C   
984  O O   . GLU A 119 ? 0.3588 0.3825 0.6135 0.0208  -0.0639 -0.1322 119 GLU A O   
985  C CB  . GLU A 119 ? 0.3550 0.3598 0.6345 0.0113  -0.0403 -0.1092 119 GLU A CB  
986  C CG  . GLU A 119 ? 0.3738 0.3744 0.6590 0.0061  -0.0274 -0.0884 119 GLU A CG  
987  C CD  . GLU A 119 ? 0.3924 0.3851 0.7065 0.0024  -0.0220 -0.0833 119 GLU A CD  
988  O OE1 . GLU A 119 ? 0.3783 0.3689 0.6988 -0.0017 -0.0117 -0.0647 119 GLU A OE1 
989  O OE2 . GLU A 119 ? 0.3996 0.3883 0.7294 0.0042  -0.0278 -0.0976 119 GLU A OE2 
990  N N   . ASN A 120 ? 0.4000 0.4156 0.6157 0.0278  -0.0613 -0.1357 120 ASN A N   
991  C CA  . ASN A 120 ? 0.4375 0.4589 0.6391 0.0352  -0.0744 -0.1526 120 ASN A CA  
992  C C   . ASN A 120 ? 0.3941 0.4212 0.5705 0.0388  -0.0768 -0.1454 120 ASN A C   
993  O O   . ASN A 120 ? 0.3636 0.3978 0.5438 0.0423  -0.0886 -0.1557 120 ASN A O   
994  C CB  . ASN A 120 ? 0.5038 0.5225 0.6817 0.0419  -0.0756 -0.1624 120 ASN A CB  
995  C CG  . ASN A 120 ? 0.6047 0.6187 0.8103 0.0402  -0.0767 -0.1754 120 ASN A CG  
996  O OD1 . ASN A 120 ? 0.6771 0.6908 0.9208 0.0350  -0.0804 -0.1815 120 ASN A OD1 
997  N ND2 . ASN A 120 ? 0.6629 0.6730 0.8519 0.0446  -0.0730 -0.1800 120 ASN A ND2 
998  N N   . LEU A 121 ? 0.3352 0.3594 0.4874 0.0386  -0.0667 -0.1290 121 LEU A N   
999  C CA  . LEU A 121 ? 0.3494 0.3776 0.4798 0.0423  -0.0684 -0.1220 121 LEU A CA  
1000 C C   . LEU A 121 ? 0.3490 0.3827 0.5039 0.0385  -0.0716 -0.1205 121 LEU A C   
1001 O O   . LEU A 121 ? 0.3686 0.4087 0.5198 0.0433  -0.0815 -0.1258 121 LEU A O   
1002 C CB  . LEU A 121 ? 0.3469 0.3702 0.4547 0.0413  -0.0564 -0.1057 121 LEU A CB  
1003 C CG  . LEU A 121 ? 0.3488 0.3744 0.4392 0.0439  -0.0560 -0.0964 121 LEU A CG  
1004 C CD1 . LEU A 121 ? 0.3872 0.4165 0.4558 0.0530  -0.0661 -0.1035 121 LEU A CD1 
1005 C CD2 . LEU A 121 ? 0.3404 0.3609 0.4133 0.0422  -0.0445 -0.0824 121 LEU A CD2 
1006 N N   . PHE A 122 ? 0.3334 0.3654 0.5157 0.0305  -0.0636 -0.1138 122 PHE A N   
1007 C CA  . PHE A 122 ? 0.3260 0.3636 0.5336 0.0265  -0.0634 -0.1113 122 PHE A CA  
1008 C C   . PHE A 122 ? 0.3681 0.4126 0.6020 0.0280  -0.0771 -0.1282 122 PHE A C   
1009 O O   . PHE A 122 ? 0.3902 0.4422 0.6351 0.0290  -0.0827 -0.1301 122 PHE A O   
1010 C CB  . PHE A 122 ? 0.3023 0.3367 0.5305 0.0183  -0.0501 -0.0992 122 PHE A CB  
1011 C CG  . PHE A 122 ? 0.3061 0.3385 0.5137 0.0170  -0.0389 -0.0832 122 PHE A CG  
1012 C CD1 . PHE A 122 ? 0.3313 0.3580 0.5109 0.0188  -0.0343 -0.0765 122 PHE A CD1 
1013 C CD2 . PHE A 122 ? 0.2969 0.3339 0.5147 0.0141  -0.0329 -0.0759 122 PHE A CD2 
1014 C CE1 . PHE A 122 ? 0.3324 0.3578 0.4958 0.0174  -0.0253 -0.0638 122 PHE A CE1 
1015 C CE2 . PHE A 122 ? 0.2746 0.3101 0.4737 0.0132  -0.0233 -0.0636 122 PHE A CE2 
1016 C CZ  . PHE A 122 ? 0.2792 0.3089 0.4516 0.0147  -0.0201 -0.0580 122 PHE A CZ  
1017 N N   . GLU A 123 ? 0.3924 0.4349 0.6373 0.0285  -0.0832 -0.1414 123 GLU A N   
1018 C CA  . GLU A 123 ? 0.4313 0.4801 0.7039 0.0296  -0.0973 -0.1603 123 GLU A CA  
1019 C C   . GLU A 123 ? 0.4432 0.4992 0.6908 0.0396  -0.1131 -0.1720 123 GLU A C   
1020 O O   . GLU A 123 ? 0.4398 0.5047 0.7057 0.0414  -0.1251 -0.1815 123 GLU A O   
1021 C CB  . GLU A 123 ? 0.4798 0.5228 0.7719 0.0271  -0.0978 -0.1709 123 GLU A CB  
1022 C CG  . GLU A 123 ? 0.5812 0.6303 0.9027 0.0287  -0.1139 -0.1943 123 GLU A CG  
1023 C CD  . GLU A 123 ? 0.6626 0.7180 1.0330 0.0221  -0.1161 -0.1967 123 GLU A CD  
1024 O OE1 . GLU A 123 ? 0.6802 0.7354 1.0613 0.0162  -0.1033 -0.1791 123 GLU A OE1 
1025 O OE2 . GLU A 123 ? 0.7249 0.7861 1.1242 0.0229  -0.1306 -0.2174 123 GLU A OE2 
1026 N N   . LYS A 124 ? 0.4328 0.4854 0.6392 0.0466  -0.1136 -0.1714 124 LYS A N   
1027 C CA  . LYS A 124 ? 0.4568 0.5160 0.6381 0.0570  -0.1288 -0.1831 124 LYS A CA  
1028 C C   . LYS A 124 ? 0.4307 0.4914 0.5816 0.0621  -0.1270 -0.1686 124 LYS A C   
1029 O O   . LYS A 124 ? 0.4615 0.5284 0.5942 0.0710  -0.1398 -0.1747 124 LYS A O   
1030 C CB  . LYS A 124 ? 0.5496 0.6050 0.7052 0.0628  -0.1304 -0.1933 124 LYS A CB  
1031 C CG  . LYS A 124 ? 0.6036 0.6563 0.7898 0.0585  -0.1322 -0.2090 124 LYS A CG  
1032 C CD  . LYS A 124 ? 0.7157 0.7608 0.8801 0.0608  -0.1239 -0.2098 124 LYS A CD  
1033 C CE  . LYS A 124 ? 0.8691 0.9089 1.0678 0.0555  -0.1223 -0.2215 124 LYS A CE  
1034 N NZ  . LYS A 124 ? 0.9107 0.9426 1.0911 0.0570  -0.1112 -0.2184 124 LYS A NZ  
1035 N N   . GLY A 125 ? 0.3930 0.4476 0.5372 0.0572  -0.1115 -0.1499 125 GLY A N   
1036 C CA  . GLY A 125 ? 0.4001 0.4548 0.5209 0.0612  -0.1088 -0.1364 125 GLY A CA  
1037 C C   . GLY A 125 ? 0.4278 0.4771 0.5065 0.0676  -0.1042 -0.1294 125 GLY A C   
1038 O O   . GLY A 125 ? 0.3871 0.4338 0.4482 0.0693  -0.0981 -0.1155 125 GLY A O   
1039 N N   . ALA A 126 ? 0.4332 0.4806 0.4984 0.0707  -0.1056 -0.1389 126 ALA A N   
1040 C CA  . ALA A 126 ? 0.4734 0.5171 0.4995 0.0776  -0.1008 -0.1334 126 ALA A CA  
1041 C C   . ALA A 126 ? 0.4982 0.5397 0.5201 0.0785  -0.0994 -0.1455 126 ALA A C   
1042 O O   . ALA A 126 ? 0.5079 0.5540 0.5432 0.0804  -0.1109 -0.1636 126 ALA A O   
1043 C CB  . ALA A 126 ? 0.4772 0.5266 0.4775 0.0886  -0.1124 -0.1347 126 ALA A CB  
1044 N N   . VAL A 127 ? 0.5154 0.5504 0.5212 0.0776  -0.0858 -0.1366 127 VAL A N   
1045 C CA  . VAL A 127 ? 0.5622 0.5950 0.5652 0.0790  -0.0831 -0.1479 127 VAL A CA  
1046 C C   . VAL A 127 ? 0.6167 0.6474 0.5828 0.0857  -0.0740 -0.1410 127 VAL A C   
1047 O O   . VAL A 127 ? 0.5537 0.5818 0.5051 0.0856  -0.0655 -0.1242 127 VAL A O   
1048 C CB  . VAL A 127 ? 0.5183 0.5453 0.5519 0.0691  -0.0743 -0.1458 127 VAL A CB  
1049 C CG1 . VAL A 127 ? 0.5164 0.5453 0.5885 0.0627  -0.0815 -0.1531 127 VAL A CG1 
1050 C CG2 . VAL A 127 ? 0.5360 0.5580 0.5667 0.0636  -0.0607 -0.1256 127 VAL A CG2 
1051 N N   . PRO A 128 ? 0.7165 0.7488 0.6667 0.0924  -0.0751 -0.1545 128 PRO A N   
1052 C CA  . PRO A 128 ? 0.7650 0.8029 0.7221 0.0970  -0.0900 -0.1775 128 PRO A CA  
1053 C C   . PRO A 128 ? 0.8059 0.8520 0.7457 0.1054  -0.1059 -0.1835 128 PRO A C   
1054 O O   . PRO A 128 ? 0.7684 0.8155 0.6859 0.1094  -0.1050 -0.1690 128 PRO A O   
1055 C CB  . PRO A 128 ? 0.8141 0.8521 0.7474 0.1045  -0.0850 -0.1884 128 PRO A CB  
1056 C CG  . PRO A 128 ? 0.8014 0.8325 0.7321 0.0999  -0.0659 -0.1716 128 PRO A CG  
1057 C CD  . PRO A 128 ? 0.7740 0.8028 0.7043 0.0952  -0.0612 -0.1496 128 PRO A CD  
1058 N N   . GLU A 129 ? 0.9250 0.9771 0.8773 0.1084  -0.1214 -0.2059 129 GLU A N   
1059 C CA  . GLU A 129 ? 1.0706 1.1319 1.0158 0.1156  -0.1401 -0.2148 129 GLU A CA  
1060 C C   . GLU A 129 ? 1.0714 1.1357 0.9704 0.1265  -0.1404 -0.2019 129 GLU A C   
1061 O O   . GLU A 129 ? 0.9617 1.0294 0.8606 0.1282  -0.1479 -0.1929 129 GLU A O   
1062 C CB  . GLU A 129 ? 1.1851 1.2530 1.1397 0.1202  -0.1560 -0.2443 129 GLU A CB  
1063 C CG  . GLU A 129 ? 1.2436 1.3056 1.2294 0.1129  -0.1499 -0.2574 129 GLU A CG  
1064 C CD  . GLU A 129 ? 1.2062 1.2598 1.2339 0.0988  -0.1380 -0.2452 129 GLU A CD  
1065 O OE1 . GLU A 129 ? 1.0440 1.0897 1.0722 0.0951  -0.1229 -0.2381 129 GLU A OE1 
1066 O OE2 . GLU A 129 ? 1.2023 1.2576 1.2627 0.0921  -0.1439 -0.2429 129 GLU A OE2 
1067 N N   . ASP A 130 ? 1.1063 1.1691 0.9679 0.1340  -0.1310 -0.1998 130 ASP A N   
1068 C CA  . ASP A 130 ? 1.1359 1.2014 0.9518 0.1456  -0.1303 -0.1874 130 ASP A CA  
1069 C C   . ASP A 130 ? 1.0846 1.1419 0.8930 0.1414  -0.1122 -0.1592 130 ASP A C   
1070 O O   . ASP A 130 ? 1.0346 1.0924 0.8325 0.1447  -0.1152 -0.1443 130 ASP A O   
1071 C CB  . ASP A 130 ? 1.1923 1.2614 0.9693 0.1570  -0.1282 -0.1987 130 ASP A CB  
1072 C CG  . ASP A 130 ? 1.3040 1.3845 1.0645 0.1685  -0.1506 -0.2210 130 ASP A CG  
1073 O OD1 . ASP A 130 ? 1.3810 1.4664 1.1662 0.1664  -0.1681 -0.2284 130 ASP A OD1 
1074 O OD2 . ASP A 130 ? 1.3782 1.4631 1.1011 0.1797  -0.1503 -0.2309 130 ASP A OD2 
1075 N N   . LEU A 131 ? 1.0539 1.1040 0.8688 0.1346  -0.0941 -0.1528 131 LEU A N   
1076 C CA  . LEU A 131 ? 0.9846 1.0275 0.7906 0.1315  -0.0760 -0.1288 131 LEU A CA  
1077 C C   . LEU A 131 ? 0.9396 0.9788 0.7692 0.1235  -0.0765 -0.1140 131 LEU A C   
1078 O O   . LEU A 131 ? 0.8581 0.8934 0.6759 0.1243  -0.0681 -0.0946 131 LEU A O   
1079 C CB  . LEU A 131 ? 0.9694 1.0068 0.7883 0.1245  -0.0599 -0.1289 131 LEU A CB  
1080 C CG  . LEU A 131 ? 1.0650 1.1041 0.8559 0.1325  -0.0507 -0.1353 131 LEU A CG  
1081 C CD1 . LEU A 131 ? 1.0087 1.0430 0.8216 0.1249  -0.0371 -0.1375 131 LEU A CD1 
1082 C CD2 . LEU A 131 ? 1.1043 1.1430 0.8579 0.1406  -0.0399 -0.1168 131 LEU A CD2 
1083 N N   . GLU A 132 ? 0.8721 0.9124 0.7376 0.1154  -0.0847 -0.1235 132 GLU A N   
1084 C CA  . GLU A 132 ? 0.7838 0.8206 0.6756 0.1063  -0.0820 -0.1116 132 GLU A CA  
1085 C C   . GLU A 132 ? 0.7594 0.7884 0.6468 0.1014  -0.0637 -0.0934 132 GLU A C   
1086 O O   . GLU A 132 ? 0.8144 0.8406 0.6977 0.1013  -0.0601 -0.0781 132 GLU A O   
1087 C CB  . GLU A 132 ? 0.8451 0.8862 0.7330 0.1115  -0.0938 -0.1068 132 GLU A CB  
1088 C CG  . GLU A 132 ? 0.9861 1.0367 0.8733 0.1187  -0.1136 -0.1254 132 GLU A CG  
1089 C CD  . GLU A 132 ? 1.0708 1.1271 0.9631 0.1231  -0.1278 -0.1228 132 GLU A CD  
1090 O OE1 . GLU A 132 ? 1.0234 1.0886 0.9084 0.1316  -0.1454 -0.1370 132 GLU A OE1 
1091 O OE2 . GLU A 132 ? 0.9966 1.0491 0.9019 0.1184  -0.1219 -0.1078 132 GLU A OE2 
1092 N N   . LEU A 133 ? 0.5850 0.6108 0.4756 0.0977  -0.0531 -0.0961 133 LEU A N   
1093 C CA  . LEU A 133 ? 0.5525 0.5720 0.4476 0.0915  -0.0374 -0.0814 133 LEU A CA  
1094 C C   . LEU A 133 ? 0.4944 0.5113 0.4176 0.0817  -0.0368 -0.0745 133 LEU A C   
1095 O O   . LEU A 133 ? 0.4426 0.4553 0.3663 0.0782  -0.0279 -0.0604 133 LEU A O   
1096 C CB  . LEU A 133 ? 0.5321 0.5500 0.4315 0.0894  -0.0285 -0.0876 133 LEU A CB  
1097 C CG  . LEU A 133 ? 0.5720 0.5925 0.4427 0.0991  -0.0250 -0.0940 133 LEU A CG  
1098 C CD1 . LEU A 133 ? 0.5447 0.5639 0.4266 0.0965  -0.0169 -0.1024 133 LEU A CD1 
1099 C CD2 . LEU A 133 ? 0.5790 0.5980 0.4223 0.1046  -0.0146 -0.0774 133 LEU A CD2 
1100 N N   . LEU A 134 ? 0.4312 0.4506 0.3788 0.0771  -0.0453 -0.0851 134 LEU A N   
1101 C CA  . LEU A 134 ? 0.4117 0.4306 0.3838 0.0695  -0.0462 -0.0802 134 LEU A CA  
1102 C C   . LEU A 134 ? 0.4133 0.4380 0.3921 0.0727  -0.0598 -0.0869 134 LEU A C   
1103 O O   . LEU A 134 ? 0.4403 0.4697 0.4189 0.0772  -0.0706 -0.1009 134 LEU A O   
1104 C CB  . LEU A 134 ? 0.4261 0.4435 0.4241 0.0616  -0.0432 -0.0851 134 LEU A CB  
1105 C CG  . LEU A 134 ? 0.4265 0.4392 0.4231 0.0583  -0.0314 -0.0793 134 LEU A CG  
1106 C CD1 . LEU A 134 ? 0.4503 0.4618 0.4711 0.0530  -0.0312 -0.0860 134 LEU A CD1 
1107 C CD2 . LEU A 134 ? 0.4041 0.4137 0.4009 0.0536  -0.0226 -0.0644 134 LEU A CD2 
1108 N N   . ARG A 135 ? 0.4081 0.4328 0.3954 0.0702  -0.0595 -0.0780 135 ARG A N   
1109 C CA  . ARG A 135 ? 0.4359 0.4663 0.4311 0.0737  -0.0712 -0.0816 135 ARG A CA  
1110 C C   . ARG A 135 ? 0.3774 0.4074 0.3963 0.0662  -0.0664 -0.0749 135 ARG A C   
1111 O O   . ARG A 135 ? 0.3628 0.3877 0.3766 0.0634  -0.0563 -0.0634 135 ARG A O   
1112 C CB  . ARG A 135 ? 0.4751 0.5057 0.4430 0.0834  -0.0750 -0.0745 135 ARG A CB  
1113 C CG  . ARG A 135 ? 0.5294 0.5663 0.5045 0.0885  -0.0883 -0.0771 135 ARG A CG  
1114 C CD  . ARG A 135 ? 0.5948 0.6314 0.5393 0.0997  -0.0926 -0.0691 135 ARG A CD  
1115 N NE  . ARG A 135 ? 0.5963 0.6249 0.5303 0.0992  -0.0802 -0.0512 135 ARG A NE  
1116 C CZ  . ARG A 135 ? 0.5175 0.5441 0.4646 0.0979  -0.0788 -0.0421 135 ARG A CZ  
1117 N NH1 . ARG A 135 ? 0.5023 0.5348 0.4735 0.0966  -0.0879 -0.0486 135 ARG A NH1 
1118 N NH2 . ARG A 135 ? 0.4942 0.5128 0.4335 0.0975  -0.0678 -0.0274 135 ARG A NH2 
1119 N N   . MET A 136 ? 0.3594 0.3950 0.4045 0.0633  -0.0734 -0.0827 136 MET A N   
1120 C CA  . MET A 136 ? 0.3618 0.3984 0.4312 0.0563  -0.0676 -0.0779 136 MET A CA  
1121 C C   . MET A 136 ? 0.3375 0.3809 0.4205 0.0598  -0.0767 -0.0802 136 MET A C   
1122 O O   . MET A 136 ? 0.3204 0.3699 0.4074 0.0649  -0.0898 -0.0901 136 MET A O   
1123 C CB  . MET A 136 ? 0.4028 0.4406 0.4980 0.0488  -0.0652 -0.0843 136 MET A CB  
1124 C CG  . MET A 136 ? 0.4601 0.4999 0.5796 0.0418  -0.0578 -0.0791 136 MET A CG  
1125 S SD  . MET A 136 ? 0.4170 0.4557 0.5617 0.0334  -0.0518 -0.0817 136 MET A SD  
1126 C CE  . MET A 136 ? 0.4961 0.5424 0.6658 0.0358  -0.0668 -0.0982 136 MET A CE  
1127 N N   . GLU A 137 ? 0.3235 0.3667 0.4158 0.0573  -0.0705 -0.0724 137 GLU A N   
1128 C CA  . GLU A 137 ? 0.3333 0.3839 0.4455 0.0598  -0.0784 -0.0759 137 GLU A CA  
1129 C C   . GLU A 137 ? 0.3005 0.3510 0.4290 0.0544  -0.0674 -0.0693 137 GLU A C   
1130 O O   . GLU A 137 ? 0.2829 0.3272 0.4015 0.0502  -0.0555 -0.0617 137 GLU A O   
1131 C CB  . GLU A 137 ? 0.4126 0.4642 0.5065 0.0703  -0.0892 -0.0741 137 GLU A CB  
1132 C CG  . GLU A 137 ? 0.4335 0.4768 0.5058 0.0727  -0.0808 -0.0606 137 GLU A CG  
1133 C CD  . GLU A 137 ? 0.5029 0.5453 0.5516 0.0837  -0.0900 -0.0562 137 GLU A CD  
1134 O OE1 . GLU A 137 ? 0.5541 0.5988 0.5864 0.0887  -0.0982 -0.0621 137 GLU A OE1 
1135 O OE2 . GLU A 137 ? 0.6260 0.6652 0.6724 0.0875  -0.0885 -0.0467 137 GLU A OE2 
1136 N N   . LYS A 138 ? 0.2769 0.3354 0.4313 0.0549  -0.0720 -0.0736 138 LYS A N   
1137 C CA  . LYS A 138 ? 0.2662 0.3268 0.4387 0.0507  -0.0617 -0.0695 138 LYS A CA  
1138 C C   . LYS A 138 ? 0.2705 0.3251 0.4256 0.0549  -0.0580 -0.0610 138 LYS A C   
1139 O O   . LYS A 138 ? 0.2769 0.3313 0.4236 0.0628  -0.0677 -0.0598 138 LYS A O   
1140 C CB  . LYS A 138 ? 0.2785 0.3500 0.4842 0.0520  -0.0687 -0.0768 138 LYS A CB  
1141 C CG  . LYS A 138 ? 0.2735 0.3493 0.5029 0.0471  -0.0564 -0.0745 138 LYS A CG  
1142 C CD  . LYS A 138 ? 0.2770 0.3533 0.5185 0.0378  -0.0438 -0.0736 138 LYS A CD  
1143 C CE  . LYS A 138 ? 0.2924 0.3693 0.5383 0.0342  -0.0280 -0.0677 138 LYS A CE  
1144 N NZ  . LYS A 138 ? 0.3063 0.3867 0.5700 0.0267  -0.0165 -0.0662 138 LYS A NZ  
1145 N N   . LYS A 139 ? 0.2788 0.3292 0.4312 0.0500  -0.0446 -0.0554 139 LYS A N   
1146 C CA  . LYS A 139 ? 0.2979 0.3416 0.4368 0.0534  -0.0410 -0.0487 139 LYS A CA  
1147 C C   . LYS A 139 ? 0.2761 0.3173 0.4160 0.0473  -0.0270 -0.0460 139 LYS A C   
1148 O O   . LYS A 139 ? 0.2693 0.3093 0.4035 0.0414  -0.0203 -0.0454 139 LYS A O   
1149 C CB  . LYS A 139 ? 0.3497 0.3856 0.4607 0.0569  -0.0446 -0.0437 139 LYS A CB  
1150 C CG  . LYS A 139 ? 0.3864 0.4143 0.4844 0.0609  -0.0417 -0.0354 139 LYS A CG  
1151 C CD  . LYS A 139 ? 0.4175 0.4420 0.4960 0.0687  -0.0500 -0.0308 139 LYS A CD  
1152 C CE  . LYS A 139 ? 0.4422 0.4721 0.5299 0.0769  -0.0622 -0.0321 139 LYS A CE  
1153 N NZ  . LYS A 139 ? 0.4637 0.4914 0.5278 0.0855  -0.0712 -0.0275 139 LYS A NZ  
1154 N N   . THR A 140 ? 0.2736 0.3134 0.4190 0.0495  -0.0232 -0.0446 140 THR A N   
1155 C CA  . THR A 140 ? 0.2629 0.3005 0.4064 0.0448  -0.0111 -0.0440 140 THR A CA  
1156 C C   . THR A 140 ? 0.2632 0.2906 0.3852 0.0450  -0.0094 -0.0386 140 THR A C   
1157 O O   . THR A 140 ? 0.2983 0.3207 0.4086 0.0492  -0.0161 -0.0343 140 THR A O   
1158 C CB  . THR A 140 ? 0.2684 0.3096 0.4305 0.0468  -0.0067 -0.0474 140 THR A CB  
1159 O OG1 . THR A 140 ? 0.2723 0.3074 0.4331 0.0534  -0.0127 -0.0443 140 THR A OG1 
1160 C CG2 . THR A 140 ? 0.2621 0.3144 0.4498 0.0466  -0.0071 -0.0527 140 THR A CG2 
1161 N N   . LEU A 141 ? 0.2449 0.2701 0.3623 0.0407  -0.0003 -0.0391 141 LEU A N   
1162 C CA  . LEU A 141 ? 0.2367 0.2532 0.3390 0.0400  0.0017  -0.0352 141 LEU A CA  
1163 C C   . LEU A 141 ? 0.2524 0.2622 0.3585 0.0455  -0.0008 -0.0322 141 LEU A C   
1164 O O   . LEU A 141 ? 0.2549 0.2576 0.3503 0.0477  -0.0030 -0.0257 141 LEU A O   
1165 C CB  . LEU A 141 ? 0.2254 0.2430 0.3243 0.0346  0.0101  -0.0383 141 LEU A CB  
1166 C CG  . LEU A 141 ? 0.2357 0.2463 0.3227 0.0326  0.0119  -0.0360 141 LEU A CG  
1167 C CD1 . LEU A 141 ? 0.2539 0.2607 0.3288 0.0328  0.0081  -0.0299 141 LEU A CD1 
1168 C CD2 . LEU A 141 ? 0.2500 0.2643 0.3319 0.0278  0.0176  -0.0400 141 LEU A CD2 
1169 N N   . ASN A 142 ? 0.2597 0.2720 0.3829 0.0481  0.0002  -0.0362 142 ASN A N   
1170 C CA  . ASN A 142 ? 0.2496 0.2553 0.3810 0.0538  -0.0019 -0.0331 142 ASN A CA  
1171 C C   . ASN A 142 ? 0.2539 0.2579 0.3810 0.0606  -0.0117 -0.0257 142 ASN A C   
1172 O O   . ASN A 142 ? 0.2649 0.2603 0.3868 0.0648  -0.0133 -0.0178 142 ASN A O   
1173 C CB  . ASN A 142 ? 0.2674 0.2773 0.4204 0.0558  0.0011  -0.0401 142 ASN A CB  
1174 C CG  . ASN A 142 ? 0.2745 0.2826 0.4307 0.0519  0.0105  -0.0473 142 ASN A CG  
1175 O OD1 . ASN A 142 ? 0.2869 0.2874 0.4347 0.0496  0.0131  -0.0462 142 ASN A OD1 
1176 N ND2 . ASN A 142 ? 0.2790 0.2946 0.4494 0.0519  0.0157  -0.0556 142 ASN A ND2 
1177 N N   . GLU A 143 ? 0.2582 0.2705 0.3869 0.0618  -0.0184 -0.0280 143 GLU A N   
1178 C CA  . GLU A 143 ? 0.2690 0.2816 0.3911 0.0690  -0.0297 -0.0230 143 GLU A CA  
1179 C C   . GLU A 143 ? 0.2797 0.2852 0.3766 0.0691  -0.0295 -0.0157 143 GLU A C   
1180 O O   . GLU A 143 ? 0.2745 0.2750 0.3607 0.0760  -0.0344 -0.0073 143 GLU A O   
1181 C CB  . GLU A 143 ? 0.2760 0.3000 0.4085 0.0694  -0.0373 -0.0299 143 GLU A CB  
1182 C CG  . GLU A 143 ? 0.2845 0.3163 0.4454 0.0703  -0.0368 -0.0362 143 GLU A CG  
1183 C CD  . GLU A 143 ? 0.2962 0.3404 0.4765 0.0680  -0.0402 -0.0445 143 GLU A CD  
1184 O OE1 . GLU A 143 ? 0.3157 0.3667 0.5214 0.0700  -0.0400 -0.0488 143 GLU A OE1 
1185 O OE2 . GLU A 143 ? 0.2653 0.3126 0.4388 0.0646  -0.0429 -0.0469 143 GLU A OE2 
1186 N N   . LEU A 144 ? 0.2665 0.2720 0.3544 0.0619  -0.0231 -0.0182 144 LEU A N   
1187 C CA  . LEU A 144 ? 0.2724 0.2724 0.3395 0.0614  -0.0214 -0.0125 144 LEU A CA  
1188 C C   . LEU A 144 ? 0.2803 0.2700 0.3440 0.0625  -0.0154 -0.0040 144 LEU A C   
1189 O O   . LEU A 144 ? 0.3195 0.3038 0.3701 0.0675  -0.0165 0.0050  144 LEU A O   
1190 C CB  . LEU A 144 ? 0.2489 0.2517 0.3120 0.0537  -0.0163 -0.0173 144 LEU A CB  
1191 C CG  . LEU A 144 ? 0.2635 0.2613 0.3090 0.0524  -0.0129 -0.0125 144 LEU A CG  
1192 C CD1 . LEU A 144 ? 0.2689 0.2665 0.2987 0.0591  -0.0194 -0.0090 144 LEU A CD1 
1193 C CD2 . LEU A 144 ? 0.2491 0.2502 0.2939 0.0455  -0.0090 -0.0171 144 LEU A CD2 
1194 N N   . ILE A 145 ? 0.2694 0.2568 0.3463 0.0582  -0.0088 -0.0073 145 ILE A N   
1195 C CA  . ILE A 145 ? 0.2745 0.2522 0.3552 0.0584  -0.0032 -0.0015 145 ILE A CA  
1196 C C   . ILE A 145 ? 0.2814 0.2533 0.3655 0.0669  -0.0073 0.0078  145 ILE A C   
1197 O O   . ILE A 145 ? 0.2867 0.2497 0.3671 0.0689  -0.0035 0.0176  145 ILE A O   
1198 C CB  . ILE A 145 ? 0.2794 0.2577 0.3754 0.0529  0.0027  -0.0105 145 ILE A CB  
1199 C CG1 . ILE A 145 ? 0.2731 0.2550 0.3609 0.0454  0.0069  -0.0158 145 ILE A CG1 
1200 C CG2 . ILE A 145 ? 0.2808 0.2492 0.3896 0.0542  0.0067  -0.0074 145 ILE A CG2 
1201 C CD1 . ILE A 145 ? 0.2649 0.2511 0.3623 0.0410  0.0111  -0.0263 145 ILE A CD1 
1202 N N   . GLU A 146 ? 0.2984 0.2754 0.3905 0.0723  -0.0148 0.0058  146 GLU A N   
1203 C CA  . GLU A 146 ? 0.3381 0.3106 0.4345 0.0816  -0.0204 0.0150  146 GLU A CA  
1204 C C   . GLU A 146 ? 0.3522 0.3218 0.4245 0.0878  -0.0244 0.0269  146 GLU A C   
1205 O O   . GLU A 146 ? 0.3284 0.2896 0.3975 0.0940  -0.0238 0.0399  146 GLU A O   
1206 C CB  . GLU A 146 ? 0.3476 0.3293 0.4585 0.0860  -0.0294 0.0085  146 GLU A CB  
1207 C CG  . GLU A 146 ? 0.3732 0.3518 0.4906 0.0967  -0.0373 0.0178  146 GLU A CG  
1208 C CD  . GLU A 146 ? 0.3993 0.3879 0.5352 0.1019  -0.0474 0.0114  146 GLU A CD  
1209 O OE1 . GLU A 146 ? 0.3983 0.3982 0.5409 0.0975  -0.0494 -0.0003 146 GLU A OE1 
1210 O OE2 . GLU A 146 ? 0.4205 0.4059 0.5667 0.1106  -0.0532 0.0189  146 GLU A OE2 
1211 N N   . GLU A 147 ? 0.3642 0.3415 0.4204 0.0867  -0.0287 0.0221  147 GLU A N   
1212 C CA  . GLU A 147 ? 0.4019 0.3784 0.4321 0.0920  -0.0317 0.0299  147 GLU A CA  
1213 C C   . GLU A 147 ? 0.3551 0.3226 0.3745 0.0891  -0.0202 0.0391  147 GLU A C   
1214 O O   . GLU A 147 ? 0.3805 0.3430 0.3833 0.0957  -0.0191 0.0516  147 GLU A O   
1215 C CB  . GLU A 147 ? 0.4796 0.4652 0.4989 0.0888  -0.0358 0.0195  147 GLU A CB  
1216 C CG  . GLU A 147 ? 0.5562 0.5518 0.5788 0.0937  -0.0493 0.0117  147 GLU A CG  
1217 C CD  . GLU A 147 ? 0.6513 0.6539 0.6671 0.0891  -0.0512 0.0011  147 GLU A CD  
1218 O OE1 . GLU A 147 ? 0.6774 0.6782 0.6708 0.0906  -0.0495 0.0037  147 GLU A OE1 
1219 O OE2 . GLU A 147 ? 0.7566 0.7661 0.7908 0.0840  -0.0533 -0.0094 147 GLU A OE2 
1220 N N   . ILE A 148 ? 0.3273 0.2944 0.3536 0.0796  -0.0121 0.0325  148 ILE A N   
1221 C CA  . ILE A 148 ? 0.3373 0.2974 0.3575 0.0762  -0.0015 0.0398  148 ILE A CA  
1222 C C   . ILE A 148 ? 0.3508 0.2999 0.3821 0.0792  0.0039  0.0519  148 ILE A C   
1223 O O   . ILE A 148 ? 0.3519 0.2944 0.3738 0.0820  0.0104  0.0648  148 ILE A O   
1224 C CB  . ILE A 148 ? 0.3180 0.2806 0.3471 0.0659  0.0042  0.0297  148 ILE A CB  
1225 C CG1 . ILE A 148 ? 0.3120 0.2834 0.3292 0.0636  0.0002  0.0212  148 ILE A CG1 
1226 C CG2 . ILE A 148 ? 0.3124 0.2677 0.3442 0.0619  0.0146  0.0363  148 ILE A CG2 
1227 C CD1 . ILE A 148 ? 0.3003 0.2756 0.3272 0.0548  0.0035  0.0115  148 ILE A CD1 
1228 N N   . ASN A 149 ? 0.3446 0.2918 0.3978 0.0788  0.0019  0.0478  149 ASN A N   
1229 C CA  . ASN A 149 ? 0.3484 0.2846 0.4175 0.0818  0.0063  0.0579  149 ASN A CA  
1230 C C   . ASN A 149 ? 0.3345 0.2631 0.4102 0.0753  0.0178  0.0617  149 ASN A C   
1231 O O   . ASN A 149 ? 0.3333 0.2533 0.4067 0.0789  0.0238  0.0769  149 ASN A O   
1232 C CB  . ASN A 149 ? 0.3826 0.3148 0.4389 0.0931  0.0019  0.0739  149 ASN A CB  
1233 C CG  . ASN A 149 ? 0.4149 0.3349 0.4915 0.0968  0.0059  0.0854  149 ASN A CG  
1234 O OD1 . ASN A 149 ? 0.4194 0.3358 0.5226 0.0923  0.0085  0.0775  149 ASN A OD1 
1235 N ND2 . ASN A 149 ? 0.4301 0.3436 0.4941 0.1058  0.0066  0.1042  149 ASN A ND2 
1236 N N   . PRO A 150 ? 0.3350 0.2670 0.4212 0.0659  0.0211  0.0484  150 PRO A N   
1237 C CA  . PRO A 150 ? 0.3291 0.2557 0.4258 0.0592  0.0303  0.0493  150 PRO A CA  
1238 C C   . PRO A 150 ? 0.3581 0.2739 0.4829 0.0585  0.0347  0.0513  150 PRO A C   
1239 O O   . PRO A 150 ? 0.3407 0.2547 0.4774 0.0622  0.0304  0.0485  150 PRO A O   
1240 C CB  . PRO A 150 ? 0.3052 0.2409 0.4025 0.0512  0.0287  0.0327  150 PRO A CB  
1241 C CG  . PRO A 150 ? 0.2998 0.2413 0.4016 0.0527  0.0217  0.0224  150 PRO A CG  
1242 C CD  . PRO A 150 ? 0.3175 0.2586 0.4095 0.0619  0.0160  0.0319  150 PRO A CD  
1243 N N   . ASP A 151 ? 0.3579 0.2668 0.4963 0.0536  0.0433  0.0554  151 ASP A N   
1244 C CA  . ASP A 151 ? 0.3616 0.2603 0.5313 0.0515  0.0474  0.0543  151 ASP A CA  
1245 C C   . ASP A 151 ? 0.3381 0.2420 0.5230 0.0430  0.0460  0.0338  151 ASP A C   
1246 O O   . ASP A 151 ? 0.3510 0.2483 0.5629 0.0406  0.0476  0.0269  151 ASP A O   
1247 C CB  . ASP A 151 ? 0.3862 0.2736 0.5678 0.0516  0.0577  0.0712  151 ASP A CB  
1248 C CG  . ASP A 151 ? 0.3898 0.2806 0.5649 0.0461  0.0646  0.0737  151 ASP A CG  
1249 O OD1 . ASP A 151 ? 0.4059 0.3078 0.5601 0.0440  0.0608  0.0659  151 ASP A OD1 
1250 O OD2 . ASP A 151 ? 0.4108 0.2930 0.6044 0.0439  0.0744  0.0840  151 ASP A OD2 
1251 N N   . VAL A 152 ? 0.3107 0.2262 0.4783 0.0391  0.0424  0.0236  152 VAL A N   
1252 C CA  . VAL A 152 ? 0.3110 0.2326 0.4883 0.0328  0.0397  0.0046  152 VAL A CA  
1253 C C   . VAL A 152 ? 0.2828 0.2173 0.4362 0.0312  0.0349  -0.0025 152 VAL A C   
1254 O O   . VAL A 152 ? 0.2845 0.2221 0.4196 0.0323  0.0351  0.0056  152 VAL A O   
1255 C CB  . VAL A 152 ? 0.3267 0.2449 0.5240 0.0260  0.0440  0.0004  152 VAL A CB  
1256 C CG1 . VAL A 152 ? 0.3325 0.2564 0.5162 0.0227  0.0462  0.0053  152 VAL A CG1 
1257 C CG2 . VAL A 152 ? 0.3289 0.2516 0.5400 0.0213  0.0401  -0.0201 152 VAL A CG2 
1258 N N   . VAL A 153 ? 0.2711 0.2126 0.4257 0.0289  0.0312  -0.0177 153 VAL A N   
1259 C CA  . VAL A 153 ? 0.2736 0.2265 0.4089 0.0272  0.0277  -0.0238 153 VAL A CA  
1260 C C   . VAL A 153 ? 0.2719 0.2305 0.4110 0.0214  0.0267  -0.0375 153 VAL A C   
1261 O O   . VAL A 153 ? 0.2641 0.2220 0.4168 0.0205  0.0264  -0.0490 153 VAL A O   
1262 C CB  . VAL A 153 ? 0.2924 0.2502 0.4222 0.0314  0.0246  -0.0271 153 VAL A CB  
1263 C CG1 . VAL A 153 ? 0.2861 0.2552 0.3986 0.0292  0.0222  -0.0318 153 VAL A CG1 
1264 C CG2 . VAL A 153 ? 0.3079 0.2610 0.4352 0.0381  0.0232  -0.0146 153 VAL A CG2 
1265 N N   . PHE A 154 ? 0.2696 0.2344 0.3965 0.0182  0.0256  -0.0366 154 PHE A N   
1266 C CA  . PHE A 154 ? 0.2588 0.2308 0.3854 0.0138  0.0229  -0.0484 154 PHE A CA  
1267 C C   . PHE A 154 ? 0.2595 0.2413 0.3658 0.0141  0.0204  -0.0500 154 PHE A C   
1268 O O   . PHE A 154 ? 0.2706 0.2534 0.3652 0.0157  0.0206  -0.0411 154 PHE A O   
1269 C CB  . PHE A 154 ? 0.2527 0.2241 0.3855 0.0099  0.0233  -0.0453 154 PHE A CB  
1270 C CG  . PHE A 154 ? 0.2520 0.2143 0.4095 0.0083  0.0268  -0.0440 154 PHE A CG  
1271 C CD1 . PHE A 154 ? 0.2699 0.2313 0.4462 0.0058  0.0246  -0.0577 154 PHE A CD1 
1272 C CD2 . PHE A 154 ? 0.2449 0.1993 0.4074 0.0098  0.0327  -0.0293 154 PHE A CD2 
1273 C CE1 . PHE A 154 ? 0.2650 0.2173 0.4692 0.0038  0.0280  -0.0571 154 PHE A CE1 
1274 C CE2 . PHE A 154 ? 0.2639 0.2094 0.4518 0.0080  0.0373  -0.0264 154 PHE A CE2 
1275 C CZ  . PHE A 154 ? 0.2791 0.2231 0.4901 0.0046  0.0349  -0.0403 154 PHE A CZ  
1276 N N   . ILE A 155 ? 0.2814 0.2703 0.3838 0.0128  0.0183  -0.0615 155 ILE A N   
1277 C CA  . ILE A 155 ? 0.2839 0.2821 0.3684 0.0128  0.0172  -0.0618 155 ILE A CA  
1278 C C   . ILE A 155 ? 0.2805 0.2854 0.3591 0.0098  0.0133  -0.0676 155 ILE A C   
1279 O O   . ILE A 155 ? 0.2614 0.2687 0.3447 0.0090  0.0112  -0.0795 155 ILE A O   
1280 C CB  . ILE A 155 ? 0.3197 0.3219 0.4014 0.0153  0.0194  -0.0683 155 ILE A CB  
1281 C CG1 . ILE A 155 ? 0.3293 0.3258 0.4197 0.0189  0.0217  -0.0633 155 ILE A CG1 
1282 C CG2 . ILE A 155 ? 0.3327 0.3442 0.3974 0.0149  0.0197  -0.0664 155 ILE A CG2 
1283 C CD1 . ILE A 155 ? 0.3646 0.3629 0.4626 0.0214  0.0243  -0.0728 155 ILE A CD1 
1284 N N   . MET A 156 ? 0.2627 0.2711 0.3314 0.0088  0.0118  -0.0600 156 MET A N   
1285 C CA  . MET A 156 ? 0.2735 0.2886 0.3375 0.0067  0.0070  -0.0634 156 MET A CA  
1286 C C   . MET A 156 ? 0.2899 0.3138 0.3375 0.0081  0.0061  -0.0686 156 MET A C   
1287 O O   . MET A 156 ? 0.2924 0.3188 0.3295 0.0094  0.0092  -0.0626 156 MET A O   
1288 C CB  . MET A 156 ? 0.2726 0.2877 0.3343 0.0058  0.0062  -0.0532 156 MET A CB  
1289 C CG  . MET A 156 ? 0.2677 0.2746 0.3416 0.0055  0.0096  -0.0464 156 MET A CG  
1290 S SD  . MET A 156 ? 0.3030 0.3044 0.4002 0.0032  0.0100  -0.0523 156 MET A SD  
1291 C CE  . MET A 156 ? 0.2951 0.3056 0.3969 0.0001  0.0023  -0.0614 156 MET A CE  
1292 N N   . HIS A 157 ? 0.2950 0.3239 0.3418 0.0078  0.0020  -0.0805 157 HIS A N   
1293 C CA  . HIS A 157 ? 0.3473 0.3851 0.3763 0.0100  0.0018  -0.0866 157 HIS A CA  
1294 C C   . HIS A 157 ? 0.3263 0.3713 0.3515 0.0097  -0.0067 -0.0958 157 HIS A C   
1295 O O   . HIS A 157 ? 0.3127 0.3553 0.3540 0.0080  -0.0111 -0.1059 157 HIS A O   
1296 C CB  . HIS A 157 ? 0.3972 0.4339 0.4287 0.0121  0.0074  -0.0953 157 HIS A CB  
1297 C CG  . HIS A 157 ? 0.5338 0.5791 0.5459 0.0147  0.0119  -0.0956 157 HIS A CG  
1298 N ND1 . HIS A 157 ? 0.7157 0.7708 0.7088 0.0164  0.0085  -0.1010 157 HIS A ND1 
1299 C CD2 . HIS A 157 ? 0.5846 0.6307 0.5933 0.0163  0.0196  -0.0900 157 HIS A CD2 
1300 C CE1 . HIS A 157 ? 0.6864 0.7477 0.6639 0.0189  0.0157  -0.0977 157 HIS A CE1 
1301 N NE2 . HIS A 157 ? 0.7360 0.7920 0.7248 0.0184  0.0227  -0.0911 157 HIS A NE2 
1302 N N   . GLU A 158 ? 0.3414 0.3953 0.3464 0.0115  -0.0095 -0.0923 158 GLU A N   
1303 C CA  . GLU A 158 ? 0.3640 0.4264 0.3620 0.0124  -0.0194 -0.1007 158 GLU A CA  
1304 C C   . GLU A 158 ? 0.3623 0.4282 0.3606 0.0138  -0.0224 -0.1204 158 GLU A C   
1305 O O   . GLU A 158 ? 0.3597 0.4295 0.3654 0.0131  -0.0321 -0.1321 158 GLU A O   
1306 C CB  . GLU A 158 ? 0.4012 0.4727 0.3739 0.0157  -0.0207 -0.0923 158 GLU A CB  
1307 C CG  . GLU A 158 ? 0.4783 0.5593 0.4432 0.0175  -0.0331 -0.0991 158 GLU A CG  
1308 C CD  . GLU A 158 ? 0.5292 0.6206 0.4631 0.0226  -0.0338 -0.0952 158 GLU A CD  
1309 O OE1 . GLU A 158 ? 0.5684 0.6696 0.4897 0.0258  -0.0442 -0.1046 158 GLU A OE1 
1310 O OE2 . GLU A 158 ? 0.6252 0.7149 0.5486 0.0235  -0.0241 -0.0819 158 GLU A OE2 
1311 N N   . GLU A 159 ? 0.3669 0.4314 0.3606 0.0156  -0.0140 -0.1250 159 GLU A N   
1312 C CA  . GLU A 159 ? 0.4037 0.4713 0.3971 0.0176  -0.0152 -0.1447 159 GLU A CA  
1313 C C   . GLU A 159 ? 0.3574 0.4140 0.3810 0.0150  -0.0132 -0.1530 159 GLU A C   
1314 O O   . GLU A 159 ? 0.3813 0.4382 0.4104 0.0166  -0.0127 -0.1695 159 GLU A O   
1315 C CB  . GLU A 159 ? 0.4669 0.5413 0.4366 0.0221  -0.0064 -0.1453 159 GLU A CB  
1316 C CG  . GLU A 159 ? 0.5542 0.6391 0.4937 0.0251  -0.0075 -0.1350 159 GLU A CG  
1317 C CD  . GLU A 159 ? 0.6980 0.7898 0.6290 0.0257  -0.0212 -0.1364 159 GLU A CD  
1318 O OE1 . GLU A 159 ? 0.6849 0.7817 0.6170 0.0268  -0.0307 -0.1548 159 GLU A OE1 
1319 O OE2 . GLU A 159 ? 0.7719 0.8644 0.6978 0.0251  -0.0232 -0.1199 159 GLU A OE2 
1320 N N   . GLY A 160 ? 0.3552 0.4019 0.3997 0.0114  -0.0121 -0.1424 160 GLY A N   
1321 C CA  . GLY A 160 ? 0.3643 0.4003 0.4375 0.0095  -0.0100 -0.1485 160 GLY A CA  
1322 C C   . GLY A 160 ? 0.3647 0.4001 0.4589 0.0065  -0.0188 -0.1612 160 GLY A C   
1323 O O   . GLY A 160 ? 0.3633 0.4082 0.4483 0.0065  -0.0278 -0.1677 160 GLY A O   
1324 N N   . GLU A 161 ? 0.3915 0.4157 0.5159 0.0040  -0.0163 -0.1631 161 GLU A N   
1325 C CA  . GLU A 161 ? 0.4102 0.4320 0.5628 0.0003  -0.0230 -0.1740 161 GLU A CA  
1326 C C   . GLU A 161 ? 0.3791 0.4052 0.5335 -0.0027 -0.0282 -0.1643 161 GLU A C   
1327 O O   . GLU A 161 ? 0.3680 0.3889 0.5220 -0.0037 -0.0223 -0.1460 161 GLU A O   
1328 C CB  . GLU A 161 ? 0.4741 0.4809 0.6587 -0.0017 -0.0160 -0.1704 161 GLU A CB  
1329 C CG  . GLU A 161 ? 0.5418 0.5440 0.7622 -0.0066 -0.0201 -0.1766 161 GLU A CG  
1330 C CD  . GLU A 161 ? 0.6228 0.6276 0.8592 -0.0069 -0.0274 -0.2026 161 GLU A CD  
1331 O OE1 . GLU A 161 ? 0.7362 0.7361 0.9754 -0.0041 -0.0233 -0.2112 161 GLU A OE1 
1332 O OE2 . GLU A 161 ? 0.7253 0.7379 0.9718 -0.0095 -0.0378 -0.2152 161 GLU A OE2 
1333 N N   . LEU A 162 ? 0.3885 0.4246 0.5447 -0.0037 -0.0397 -0.1772 162 LEU A N   
1334 C CA  . LEU A 162 ? 0.3798 0.4218 0.5379 -0.0057 -0.0455 -0.1687 162 LEU A CA  
1335 C C   . LEU A 162 ? 0.3909 0.4242 0.5868 -0.0109 -0.0424 -0.1634 162 LEU A C   
1336 O O   . LEU A 162 ? 0.3991 0.4290 0.6250 -0.0139 -0.0452 -0.1768 162 LEU A O   
1337 C CB  . LEU A 162 ? 0.3933 0.4499 0.5417 -0.0041 -0.0602 -0.1841 162 LEU A CB  
1338 C CG  . LEU A 162 ? 0.3907 0.4545 0.5461 -0.0058 -0.0678 -0.1765 162 LEU A CG  
1339 C CD1 . LEU A 162 ? 0.3788 0.4459 0.5052 -0.0029 -0.0646 -0.1573 162 LEU A CD1 
1340 C CD2 . LEU A 162 ? 0.4015 0.4786 0.5607 -0.0050 -0.0845 -0.1954 162 LEU A CD2 
1341 N N   . MET A 163 ? 0.4084 0.4394 0.6037 -0.0120 -0.0371 -0.1448 163 MET A N   
1342 C CA  . MET A 163 ? 0.4405 0.4653 0.6688 -0.0165 -0.0328 -0.1377 163 MET A CA  
1343 C C   . MET A 163 ? 0.4656 0.4986 0.6945 -0.0174 -0.0366 -0.1296 163 MET A C   
1344 O O   . MET A 163 ? 0.4128 0.4518 0.6144 -0.0143 -0.0382 -0.1213 163 MET A O   
1345 C CB  . MET A 163 ? 0.4524 0.4632 0.6848 -0.0163 -0.0187 -0.1217 163 MET A CB  
1346 C CG  . MET A 163 ? 0.4966 0.4983 0.7437 -0.0163 -0.0156 -0.1308 163 MET A CG  
1347 S SD  . MET A 163 ? 0.5646 0.5499 0.8222 -0.0157 -0.0009 -0.1118 163 MET A SD  
1348 C CE  . MET A 163 ? 0.6043 0.5846 0.9045 -0.0215 0.0034  -0.1070 163 MET A CE  
1349 N N   . ILE A 164 ? 0.4818 0.5154 0.7463 -0.0219 -0.0382 -0.1329 164 ILE A N   
1350 C CA  . ILE A 164 ? 0.4669 0.5061 0.7417 -0.0232 -0.0385 -0.1236 164 ILE A CA  
1351 C C   . ILE A 164 ? 0.4161 0.4457 0.6825 -0.0223 -0.0233 -0.1029 164 ILE A C   
1352 O O   . ILE A 164 ? 0.3985 0.4164 0.6757 -0.0234 -0.0128 -0.0969 164 ILE A O   
1353 C CB  . ILE A 164 ? 0.5062 0.5480 0.8264 -0.0286 -0.0420 -0.1325 164 ILE A CB  
1354 C CG1 . ILE A 164 ? 0.5961 0.6462 0.9268 -0.0293 -0.0577 -0.1566 164 ILE A CG1 
1355 C CG2 . ILE A 164 ? 0.5092 0.5589 0.8421 -0.0296 -0.0425 -0.1240 164 ILE A CG2 
1356 C CD1 . ILE A 164 ? 0.6306 0.6952 0.9307 -0.0247 -0.0728 -0.1645 164 ILE A CD1 
1357 N N   . PRO A 165 ? 0.3562 0.3902 0.6024 -0.0196 -0.0223 -0.0916 165 PRO A N   
1358 C CA  . PRO A 165 ? 0.3331 0.3590 0.5691 -0.0181 -0.0091 -0.0742 165 PRO A CA  
1359 C C   . PRO A 165 ? 0.3660 0.3841 0.6309 -0.0211 0.0029  -0.0661 165 PRO A C   
1360 O O   . PRO A 165 ? 0.3795 0.3872 0.6379 -0.0197 0.0137  -0.0557 165 PRO A O   
1361 C CB  . PRO A 165 ? 0.3167 0.3509 0.5387 -0.0157 -0.0124 -0.0680 165 PRO A CB  
1362 C CG  . PRO A 165 ? 0.3202 0.3648 0.5288 -0.0142 -0.0271 -0.0795 165 PRO A CG  
1363 C CD  . PRO A 165 ? 0.3372 0.3841 0.5704 -0.0175 -0.0341 -0.0951 165 PRO A CD  
1364 N N   . LYS A 166 ? 0.3811 0.4048 0.6783 -0.0249 0.0010  -0.0701 166 LYS A N   
1365 C CA  . LYS A 166 ? 0.4158 0.4327 0.7458 -0.0285 0.0132  -0.0630 166 LYS A CA  
1366 C C   . LYS A 166 ? 0.3602 0.3642 0.6954 -0.0291 0.0194  -0.0624 166 LYS A C   
1367 O O   . LYS A 166 ? 0.3520 0.3457 0.6878 -0.0281 0.0331  -0.0482 166 LYS A O   
1368 C CB  . LYS A 166 ? 0.4900 0.5162 0.8599 -0.0333 0.0064  -0.0735 166 LYS A CB  
1369 C CG  . LYS A 166 ? 0.6178 0.6383 1.0309 -0.0383 0.0186  -0.0683 166 LYS A CG  
1370 C CD  . LYS A 166 ? 0.7186 0.7505 1.1753 -0.0434 0.0103  -0.0805 166 LYS A CD  
1371 C CE  . LYS A 166 ? 0.8271 0.8549 1.3291 -0.0484 0.0254  -0.0719 166 LYS A CE  
1372 N NZ  . LYS A 166 ? 0.8478 0.8894 1.3891 -0.0523 0.0191  -0.0799 166 LYS A NZ  
1373 N N   . ASN A 167 ? 0.3448 0.3497 0.6836 -0.0301 0.0090  -0.0785 167 ASN A N   
1374 C CA  . ASN A 167 ? 0.3372 0.3304 0.6891 -0.0311 0.0133  -0.0812 167 ASN A CA  
1375 C C   . ASN A 167 ? 0.3274 0.3123 0.6460 -0.0258 0.0194  -0.0707 167 ASN A C   
1376 O O   . ASN A 167 ? 0.3173 0.2902 0.6450 -0.0253 0.0280  -0.0636 167 ASN A O   
1377 C CB  . ASN A 167 ? 0.3695 0.3675 0.7328 -0.0329 -0.0003 -0.1040 167 ASN A CB  
1378 C CG  . ASN A 167 ? 0.3907 0.3947 0.7968 -0.0386 -0.0065 -0.1162 167 ASN A CG  
1379 O OD1 . ASN A 167 ? 0.4074 0.4106 0.8409 -0.0420 0.0015  -0.1067 167 ASN A OD1 
1380 N ND2 . ASN A 167 ? 0.4179 0.4282 0.8314 -0.0395 -0.0206 -0.1384 167 ASN A ND2 
1381 N N   . PHE A 168 ? 0.3160 0.3072 0.5981 -0.0218 0.0147  -0.0693 168 PHE A N   
1382 C CA  . PHE A 168 ? 0.3077 0.2922 0.5618 -0.0171 0.0197  -0.0605 168 PHE A CA  
1383 C C   . PHE A 168 ? 0.3232 0.3003 0.5744 -0.0152 0.0324  -0.0412 168 PHE A C   
1384 O O   . PHE A 168 ? 0.3261 0.2934 0.5711 -0.0121 0.0388  -0.0329 168 PHE A O   
1385 C CB  . PHE A 168 ? 0.2856 0.2785 0.5059 -0.0138 0.0122  -0.0639 168 PHE A CB  
1386 C CG  . PHE A 168 ? 0.2765 0.2641 0.4726 -0.0094 0.0158  -0.0578 168 PHE A CG  
1387 C CD1 . PHE A 168 ? 0.2897 0.2692 0.4926 -0.0083 0.0180  -0.0611 168 PHE A CD1 
1388 C CD2 . PHE A 168 ? 0.2627 0.2535 0.4321 -0.0062 0.0165  -0.0495 168 PHE A CD2 
1389 C CE1 . PHE A 168 ? 0.3016 0.2775 0.4849 -0.0039 0.0204  -0.0560 168 PHE A CE1 
1390 C CE2 . PHE A 168 ? 0.2643 0.2513 0.4150 -0.0023 0.0187  -0.0452 168 PHE A CE2 
1391 C CZ  . PHE A 168 ? 0.2721 0.2523 0.4293 -0.0011 0.0203  -0.0485 168 PHE A CZ  
1392 N N   . GLY A 169 ? 0.3138 0.2958 0.5714 -0.0165 0.0361  -0.0348 169 GLY A N   
1393 C CA  . GLY A 169 ? 0.3125 0.2888 0.5681 -0.0145 0.0494  -0.0174 169 GLY A CA  
1394 C C   . GLY A 169 ? 0.3333 0.2981 0.6146 -0.0159 0.0600  -0.0094 169 GLY A C   
1395 O O   . GLY A 169 ? 0.3205 0.2768 0.5903 -0.0118 0.0698  0.0054  169 GLY A O   
1396 N N   . LYS A 170 ? 0.3381 0.3030 0.6549 -0.0214 0.0572  -0.0194 170 LYS A N   
1397 C CA  . LYS A 170 ? 0.3919 0.3454 0.7399 -0.0236 0.0670  -0.0127 170 LYS A CA  
1398 C C   . LYS A 170 ? 0.3800 0.3229 0.7154 -0.0196 0.0667  -0.0108 170 LYS A C   
1399 O O   . LYS A 170 ? 0.4323 0.3637 0.7738 -0.0173 0.0775  0.0041  170 LYS A O   
1400 C CB  . LYS A 170 ? 0.4351 0.3913 0.8273 -0.0307 0.0620  -0.0272 170 LYS A CB  
1401 C CG  . LYS A 170 ? 0.4645 0.4310 0.8781 -0.0348 0.0634  -0.0278 170 LYS A CG  
1402 C CD  . LYS A 170 ? 0.4826 0.4507 0.9478 -0.0421 0.0605  -0.0399 170 LYS A CD  
1403 C CE  . LYS A 170 ? 0.5396 0.5188 1.0270 -0.0455 0.0629  -0.0387 170 LYS A CE  
1404 N NZ  . LYS A 170 ? 0.5894 0.5794 1.1104 -0.0510 0.0482  -0.0600 170 LYS A NZ  
1405 N N   . LEU A 171 ? 0.3732 0.3205 0.6919 -0.0184 0.0545  -0.0255 171 LEU A N   
1406 C CA  . LEU A 171 ? 0.3763 0.3153 0.6874 -0.0148 0.0533  -0.0268 171 LEU A CA  
1407 C C   . LEU A 171 ? 0.3398 0.2740 0.6206 -0.0081 0.0596  -0.0093 171 LEU A C   
1408 O O   . LEU A 171 ? 0.3539 0.2769 0.6400 -0.0048 0.0656  0.0009  171 LEU A O   
1409 C CB  . LEU A 171 ? 0.4071 0.3544 0.7053 -0.0148 0.0400  -0.0469 171 LEU A CB  
1410 C CG  . LEU A 171 ? 0.4456 0.3864 0.7376 -0.0110 0.0382  -0.0518 171 LEU A CG  
1411 C CD1 . LEU A 171 ? 0.4368 0.3644 0.7647 -0.0123 0.0437  -0.0510 171 LEU A CD1 
1412 C CD2 . LEU A 171 ? 0.4454 0.3961 0.7258 -0.0113 0.0268  -0.0725 171 LEU A CD2 
1413 N N   . LEU A 172 ? 0.3115 0.2542 0.5624 -0.0057 0.0576  -0.0061 172 LEU A N   
1414 C CA  . LEU A 172 ? 0.3124 0.2525 0.5335 0.0008  0.0613  0.0074  172 LEU A CA  
1415 C C   . LEU A 172 ? 0.3421 0.2732 0.5698 0.0032  0.0743  0.0266  172 LEU A C   
1416 O O   . LEU A 172 ? 0.3253 0.2504 0.5353 0.0096  0.0775  0.0385  172 LEU A O   
1417 C CB  . LEU A 172 ? 0.2879 0.2384 0.4824 0.0020  0.0578  0.0066  172 LEU A CB  
1418 C CG  . LEU A 172 ? 0.2826 0.2421 0.4625 0.0013  0.0464  -0.0076 172 LEU A CG  
1419 C CD1 . LEU A 172 ? 0.2781 0.2470 0.4427 0.0011  0.0443  -0.0074 172 LEU A CD1 
1420 C CD2 . LEU A 172 ? 0.2865 0.2436 0.4475 0.0061  0.0431  -0.0077 172 LEU A CD2 
1421 N N   . ASP A 173 ? 0.3562 0.2874 0.6092 -0.0014 0.0818  0.0298  173 ASP A N   
1422 C CA  . ASP A 173 ? 0.3924 0.3163 0.6514 0.0007  0.0965  0.0494  173 ASP A CA  
1423 C C   . ASP A 173 ? 0.4051 0.3151 0.6866 0.0016  0.1026  0.0581  173 ASP A C   
1424 O O   . ASP A 173 ? 0.4288 0.3311 0.7153 0.0042  0.1158  0.0769  173 ASP A O   
1425 C CB  . ASP A 173 ? 0.4341 0.3633 0.7164 -0.0046 0.1043  0.0507  173 ASP A CB  
1426 C CG  . ASP A 173 ? 0.4739 0.3971 0.7561 -0.0013 0.1217  0.0724  173 ASP A CG  
1427 O OD1 . ASP A 173 ? 0.5506 0.4736 0.7976 0.0060  0.1250  0.0831  173 ASP A OD1 
1428 O OD2 . ASP A 173 ? 0.4976 0.4163 0.8150 -0.0057 0.1320  0.0785  173 ASP A OD2 
1429 N N   . LYS A 174 ? 0.4153 0.3219 0.7096 0.0001  0.0937  0.0453  174 LYS A N   
1430 C CA  . LYS A 174 ? 0.4269 0.3196 0.7435 0.0016  0.0984  0.0526  174 LYS A CA  
1431 C C   . LYS A 174 ? 0.4091 0.2967 0.6970 0.0105  0.0965  0.0627  174 LYS A C   
1432 O O   . LYS A 174 ? 0.4409 0.3163 0.7433 0.0136  0.1014  0.0735  174 LYS A O   
1433 C CB  . LYS A 174 ? 0.4611 0.3523 0.8088 -0.0039 0.0899  0.0321  174 LYS A CB  
1434 C CG  . LYS A 174 ? 0.4696 0.3642 0.8549 -0.0126 0.0908  0.0216  174 LYS A CG  
1435 C CD  . LYS A 174 ? 0.5158 0.4136 0.9211 -0.0170 0.0784  -0.0041 174 LYS A CD  
1436 C CE  . LYS A 174 ? 0.5506 0.4592 0.9775 -0.0245 0.0726  -0.0200 174 LYS A CE  
1437 N NZ  . LYS A 174 ? 0.5522 0.4540 1.0272 -0.0303 0.0818  -0.0151 174 LYS A NZ  
1438 N N   . PHE A 175 ? 0.3911 0.2876 0.6415 0.0148  0.0895  0.0599  175 PHE A N   
1439 C CA  . PHE A 175 ? 0.4101 0.3030 0.6370 0.0232  0.0858  0.0674  175 PHE A CA  
1440 C C   . PHE A 175 ? 0.4306 0.3249 0.6260 0.0299  0.0916  0.0850  175 PHE A C   
1441 O O   . PHE A 175 ? 0.4601 0.3596 0.6499 0.0277  0.0979  0.0886  175 PHE A O   
1442 C CB  . PHE A 175 ? 0.4004 0.3019 0.6141 0.0229  0.0728  0.0488  175 PHE A CB  
1443 C CG  . PHE A 175 ? 0.3929 0.2931 0.6341 0.0178  0.0677  0.0309  175 PHE A CG  
1444 C CD1 . PHE A 175 ? 0.4028 0.2931 0.6631 0.0205  0.0674  0.0308  175 PHE A CD1 
1445 C CD2 . PHE A 175 ? 0.3645 0.2734 0.6142 0.0107  0.0632  0.0141  175 PHE A CD2 
1446 C CE1 . PHE A 175 ? 0.4026 0.2918 0.6886 0.0161  0.0631  0.0123  175 PHE A CE1 
1447 C CE2 . PHE A 175 ? 0.3747 0.2833 0.6476 0.0067  0.0580  -0.0038 175 PHE A CE2 
1448 C CZ  . PHE A 175 ? 0.3921 0.2909 0.6828 0.0093  0.0582  -0.0057 175 PHE A CZ  
1449 N N   . LYS A 176 ? 0.4528 0.3431 0.6286 0.0386  0.0894  0.0957  176 LYS A N   
1450 C CA  . LYS A 176 ? 0.5356 0.4276 0.6791 0.0463  0.0936  0.1114  176 LYS A CA  
1451 C C   . LYS A 176 ? 0.5093 0.4137 0.6214 0.0483  0.0837  0.1005  176 LYS A C   
1452 O O   . LYS A 176 ? 0.5281 0.4380 0.6167 0.0512  0.0872  0.1055  176 LYS A O   
1453 C CB  . LYS A 176 ? 0.6283 0.5108 0.7643 0.0560  0.0948  0.1292  176 LYS A CB  
1454 C CG  . LYS A 176 ? 0.7358 0.6042 0.9006 0.0556  0.1074  0.1460  176 LYS A CG  
1455 C CD  . LYS A 176 ? 0.8338 0.6914 1.0064 0.0628  0.1042  0.1563  176 LYS A CD  
1456 C CE  . LYS A 176 ? 0.9368 0.7811 1.1550 0.0580  0.1109  0.1588  176 LYS A CE  
1457 N NZ  . LYS A 176 ? 1.0030 0.8386 1.2352 0.0571  0.1281  0.1796  176 LYS A NZ  
1458 N N   . LYS A 177 ? 0.4954 0.4042 0.6090 0.0468  0.0721  0.0852  177 LYS A N   
1459 C CA  . LYS A 177 ? 0.4729 0.3914 0.5600 0.0500  0.0623  0.0771  177 LYS A CA  
1460 C C   . LYS A 177 ? 0.3999 0.3249 0.4983 0.0434  0.0545  0.0578  177 LYS A C   
1461 O O   . LYS A 177 ? 0.3718 0.2990 0.4682 0.0458  0.0466  0.0510  177 LYS A O   
1462 C CB  . LYS A 177 ? 0.5133 0.4288 0.5853 0.0599  0.0571  0.0866  177 LYS A CB  
1463 C CG  . LYS A 177 ? 0.5720 0.4971 0.6143 0.0651  0.0486  0.0825  177 LYS A CG  
1464 C CD  . LYS A 177 ? 0.6002 0.5244 0.6259 0.0759  0.0412  0.0913  177 LYS A CD  
1465 C CE  . LYS A 177 ? 0.6398 0.5748 0.6393 0.0793  0.0328  0.0836  177 LYS A CE  
1466 N NZ  . LYS A 177 ? 0.6232 0.5600 0.6015 0.0905  0.0245  0.0908  177 LYS A NZ  
1467 N N   . PRO A 178 ? 0.3514 0.2797 0.4631 0.0355  0.0569  0.0488  178 PRO A N   
1468 C CA  . PRO A 178 ? 0.3284 0.2631 0.4484 0.0300  0.0499  0.0314  178 PRO A CA  
1469 C C   . PRO A 178 ? 0.3332 0.2780 0.4306 0.0309  0.0431  0.0247  178 PRO A C   
1470 O O   . PRO A 178 ? 0.3578 0.3062 0.4384 0.0327  0.0444  0.0295  178 PRO A O   
1471 C CB  . PRO A 178 ? 0.3301 0.2664 0.4672 0.0227  0.0538  0.0263  178 PRO A CB  
1472 C CG  . PRO A 178 ? 0.3364 0.2719 0.4653 0.0243  0.0623  0.0397  178 PRO A CG  
1473 C CD  . PRO A 178 ? 0.3565 0.2839 0.4757 0.0320  0.0662  0.0551  178 PRO A CD  
1474 N N   . THR A 179 ? 0.3022 0.2514 0.4012 0.0299  0.0366  0.0134  179 THR A N   
1475 C CA  . THR A 179 ? 0.2916 0.2498 0.3743 0.0301  0.0308  0.0070  179 THR A CA  
1476 C C   . THR A 179 ? 0.2775 0.2421 0.3662 0.0240  0.0288  -0.0050 179 THR A C   
1477 O O   . THR A 179 ? 0.2880 0.2508 0.3914 0.0216  0.0288  -0.0121 179 THR A O   
1478 C CB  . THR A 179 ? 0.2872 0.2461 0.3661 0.0352  0.0258  0.0061  179 THR A CB  
1479 O OG1 . THR A 179 ? 0.2971 0.2523 0.3647 0.0417  0.0259  0.0179  179 THR A OG1 
1480 C CG2 . THR A 179 ? 0.2547 0.2232 0.3253 0.0339  0.0208  -0.0026 179 THR A CG2 
1481 N N   . VAL A 180 ? 0.2687 0.2403 0.3463 0.0219  0.0271  -0.0071 180 VAL A N   
1482 C CA  . VAL A 180 ? 0.2625 0.2407 0.3426 0.0172  0.0244  -0.0168 180 VAL A CA  
1483 C C   . VAL A 180 ? 0.2657 0.2507 0.3322 0.0180  0.0208  -0.0192 180 VAL A C   
1484 O O   . VAL A 180 ? 0.2621 0.2479 0.3189 0.0201  0.0205  -0.0140 180 VAL A O   
1485 C CB  . VAL A 180 ? 0.2675 0.2474 0.3526 0.0135  0.0260  -0.0159 180 VAL A CB  
1486 C CG1 . VAL A 180 ? 0.2538 0.2418 0.3378 0.0100  0.0214  -0.0248 180 VAL A CG1 
1487 C CG2 . VAL A 180 ? 0.2931 0.2663 0.3971 0.0119  0.0306  -0.0136 180 VAL A CG2 
1488 N N   . ILE A 181 ? 0.2619 0.2521 0.3289 0.0164  0.0188  -0.0274 181 ILE A N   
1489 C CA  . ILE A 181 ? 0.2621 0.2587 0.3199 0.0169  0.0170  -0.0289 181 ILE A CA  
1490 C C   . ILE A 181 ? 0.2448 0.2481 0.2978 0.0135  0.0156  -0.0328 181 ILE A C   
1491 O O   . ILE A 181 ? 0.2135 0.2190 0.2696 0.0118  0.0150  -0.0396 181 ILE A O   
1492 C CB  . ILE A 181 ? 0.2723 0.2697 0.3343 0.0191  0.0174  -0.0332 181 ILE A CB  
1493 C CG1 . ILE A 181 ? 0.2999 0.2914 0.3665 0.0235  0.0171  -0.0282 181 ILE A CG1 
1494 C CG2 . ILE A 181 ? 0.2895 0.2943 0.3461 0.0189  0.0173  -0.0350 181 ILE A CG2 
1495 C CD1 . ILE A 181 ? 0.3133 0.3039 0.3906 0.0258  0.0178  -0.0332 181 ILE A CD1 
1496 N N   . VAL A 182 ? 0.2272 0.2339 0.2728 0.0131  0.0147  -0.0287 182 VAL A N   
1497 C CA  . VAL A 182 ? 0.2281 0.2409 0.2683 0.0110  0.0131  -0.0294 182 VAL A CA  
1498 C C   . VAL A 182 ? 0.2353 0.2522 0.2705 0.0116  0.0142  -0.0273 182 VAL A C   
1499 O O   . VAL A 182 ? 0.2619 0.2769 0.2988 0.0129  0.0143  -0.0241 182 VAL A O   
1500 C CB  . VAL A 182 ? 0.2364 0.2486 0.2773 0.0102  0.0117  -0.0249 182 VAL A CB  
1501 C CG1 . VAL A 182 ? 0.2529 0.2714 0.2893 0.0088  0.0090  -0.0246 182 VAL A CG1 
1502 C CG2 . VAL A 182 ? 0.2342 0.2423 0.2839 0.0094  0.0124  -0.0257 182 VAL A CG2 
1503 N N   . GLY A 183 ? 0.2377 0.2607 0.2673 0.0107  0.0150  -0.0293 183 GLY A N   
1504 C CA  . GLY A 183 ? 0.2508 0.2777 0.2782 0.0109  0.0179  -0.0259 183 GLY A CA  
1505 C C   . GLY A 183 ? 0.2733 0.3000 0.3008 0.0101  0.0166  -0.0186 183 GLY A C   
1506 O O   . GLY A 183 ? 0.2519 0.2793 0.2760 0.0095  0.0138  -0.0162 183 GLY A O   
1507 N N   . GLY A 184 ? 0.2888 0.3146 0.3228 0.0103  0.0181  -0.0159 184 GLY A N   
1508 C CA  . GLY A 184 ? 0.2987 0.3234 0.3365 0.0097  0.0170  -0.0104 184 GLY A CA  
1509 C C   . GLY A 184 ? 0.3089 0.3378 0.3473 0.0086  0.0209  -0.0044 184 GLY A C   
1510 O O   . GLY A 184 ? 0.3534 0.3815 0.4018 0.0078  0.0223  -0.0011 184 GLY A O   
1511 N N   . PHE A 185 ? 0.4228 0.4565 0.4506 0.0087  0.0231  -0.0035 185 PHE A N   
1512 C CA  . PHE A 185 ? 0.4175 0.4559 0.4418 0.0084  0.0285  0.0036  185 PHE A CA  
1513 C C   . PHE A 185 ? 0.4305 0.4722 0.4404 0.0096  0.0257  0.0076  185 PHE A C   
1514 O O   . PHE A 185 ? 0.4580 0.5001 0.4617 0.0102  0.0203  0.0018  185 PHE A O   
1515 C CB  . PHE A 185 ? 0.4110 0.4540 0.4348 0.0087  0.0353  -0.0001 185 PHE A CB  
1516 C CG  . PHE A 185 ? 0.3840 0.4282 0.4005 0.0100  0.0339  -0.0101 185 PHE A CG  
1517 C CD1 . PHE A 185 ? 0.3798 0.4202 0.4059 0.0104  0.0319  -0.0170 185 PHE A CD1 
1518 C CD2 . PHE A 185 ? 0.3677 0.4171 0.3685 0.0114  0.0346  -0.0128 185 PHE A CD2 
1519 C CE1 . PHE A 185 ? 0.3610 0.4013 0.3841 0.0116  0.0312  -0.0256 185 PHE A CE1 
1520 C CE2 . PHE A 185 ? 0.3674 0.4173 0.3651 0.0124  0.0330  -0.0238 185 PHE A CE2 
1521 C CZ  . PHE A 185 ? 0.3437 0.3885 0.3540 0.0123  0.0318  -0.0297 185 PHE A CZ  
1522 N N   . PRO A 186 ? 0.4180 0.4622 0.4244 0.0101  0.0286  0.0182  186 PRO A N   
1523 C CA  . PRO A 186 ? 0.4419 0.4892 0.4357 0.0122  0.0237  0.0234  186 PRO A CA  
1524 C C   . PRO A 186 ? 0.4682 0.5231 0.4415 0.0145  0.0230  0.0185  186 PRO A C   
1525 O O   . PRO A 186 ? 0.5184 0.5764 0.4826 0.0162  0.0153  0.0167  186 PRO A O   
1526 C CB  . PRO A 186 ? 0.4342 0.4807 0.4325 0.0125  0.0283  0.0379  186 PRO A CB  
1527 C CG  . PRO A 186 ? 0.4434 0.4909 0.4481 0.0109  0.0385  0.0391  186 PRO A CG  
1528 C CD  . PRO A 186 ? 0.4184 0.4627 0.4343 0.0090  0.0367  0.0265  186 PRO A CD  
1529 N N   . HIS A 187 ? 0.4962 0.5550 0.4636 0.0148  0.0308  0.0154  187 HIS A N   
1530 C CA  . HIS A 187 ? 0.5339 0.6003 0.4813 0.0176  0.0310  0.0084  187 HIS A CA  
1531 C C   . HIS A 187 ? 0.5646 0.6330 0.5142 0.0173  0.0400  0.0012  187 HIS A C   
1532 O O   . HIS A 187 ? 0.5897 0.6552 0.5551 0.0153  0.0468  0.0047  187 HIS A O   
1533 C CB  . HIS A 187 ? 0.5572 0.6305 0.4842 0.0212  0.0325  0.0192  187 HIS A CB  
1534 C CG  . HIS A 187 ? 0.6434 0.7156 0.5762 0.0206  0.0429  0.0344  187 HIS A CG  
1535 N ND1 . HIS A 187 ? 0.7105 0.7842 0.6496 0.0194  0.0551  0.0347  187 HIS A ND1 
1536 C CD2 . HIS A 187 ? 0.7034 0.7729 0.6407 0.0210  0.0433  0.0500  187 HIS A CD2 
1537 C CE1 . HIS A 187 ? 0.7354 0.8075 0.6831 0.0186  0.0629  0.0499  187 HIS A CE1 
1538 N NE2 . HIS A 187 ? 0.7440 0.8130 0.6907 0.0196  0.0559  0.0597  187 HIS A NE2 
1539 N N   . GLY A 188 ? 0.5810 0.6551 0.5162 0.0197  0.0395  -0.0099 188 GLY A N   
1540 C CA  . GLY A 188 ? 0.5989 0.6758 0.5355 0.0203  0.0477  -0.0191 188 GLY A CA  
1541 C C   . GLY A 188 ? 0.6010 0.6719 0.5537 0.0187  0.0430  -0.0320 188 GLY A C   
1542 O O   . GLY A 188 ? 0.6316 0.6977 0.5890 0.0175  0.0335  -0.0356 188 GLY A O   
1543 N N   . ASP A 189 ? 0.6200 0.6912 0.5827 0.0189  0.0504  -0.0379 189 ASP A N   
1544 C CA  . ASP A 189 ? 0.6073 0.6732 0.5838 0.0186  0.0470  -0.0498 189 ASP A CA  
1545 C C   . ASP A 189 ? 0.4926 0.5523 0.4904 0.0168  0.0481  -0.0452 189 ASP A C   
1546 O O   . ASP A 189 ? 0.4415 0.5024 0.4450 0.0157  0.0524  -0.0357 189 ASP A O   
1547 C CB  . ASP A 189 ? 0.7159 0.7871 0.6886 0.0214  0.0530  -0.0625 189 ASP A CB  
1548 C CG  . ASP A 189 ? 0.8890 0.9662 0.8407 0.0238  0.0493  -0.0715 189 ASP A CG  
1549 O OD1 . ASP A 189 ? 1.0471 1.1202 1.0006 0.0228  0.0389  -0.0773 189 ASP A OD1 
1550 O OD2 . ASP A 189 ? 0.8538 0.9401 0.7878 0.0270  0.0568  -0.0728 189 ASP A OD2 
1551 N N   . PHE A 190 ? 0.4517 0.5052 0.4620 0.0168  0.0437  -0.0523 190 PHE A N   
1552 C CA  . PHE A 190 ? 0.4270 0.4757 0.4554 0.0167  0.0437  -0.0499 190 PHE A CA  
1553 C C   . PHE A 190 ? 0.4349 0.4897 0.4717 0.0180  0.0527  -0.0508 190 PHE A C   
1554 O O   . PHE A 190 ? 0.5077 0.5686 0.5385 0.0197  0.0593  -0.0572 190 PHE A O   
1555 C CB  . PHE A 190 ? 0.3767 0.4180 0.4145 0.0176  0.0385  -0.0567 190 PHE A CB  
1556 C CG  . PHE A 190 ? 0.3460 0.3809 0.3818 0.0160  0.0311  -0.0535 190 PHE A CG  
1557 C CD1 . PHE A 190 ? 0.3164 0.3465 0.3573 0.0155  0.0278  -0.0457 190 PHE A CD1 
1558 C CD2 . PHE A 190 ? 0.3703 0.4047 0.4000 0.0153  0.0275  -0.0592 190 PHE A CD2 
1559 C CE1 . PHE A 190 ? 0.3226 0.3474 0.3622 0.0144  0.0228  -0.0429 190 PHE A CE1 
1560 C CE2 . PHE A 190 ? 0.3739 0.4034 0.4051 0.0136  0.0219  -0.0558 190 PHE A CE2 
1561 C CZ  . PHE A 190 ? 0.3433 0.3678 0.3794 0.0133  0.0204  -0.0473 190 PHE A CZ  
1562 N N   . LYS A 191 ? 0.4370 0.4909 0.4887 0.0172  0.0528  -0.0452 191 LYS A N   
1563 C CA  . LYS A 191 ? 0.4890 0.5483 0.5566 0.0184  0.0598  -0.0470 191 LYS A CA  
1564 C C   . LYS A 191 ? 0.4903 0.5454 0.5725 0.0212  0.0555  -0.0542 191 LYS A C   
1565 O O   . LYS A 191 ? 0.5359 0.5951 0.6268 0.0236  0.0613  -0.0611 191 LYS A O   
1566 C CB  . LYS A 191 ? 0.5397 0.6009 0.6183 0.0161  0.0611  -0.0379 191 LYS A CB  
1567 C CG  . LYS A 191 ? 0.6527 0.7157 0.7563 0.0169  0.0604  -0.0396 191 LYS A CG  
1568 C CD  . LYS A 191 ? 0.7336 0.8059 0.8512 0.0172  0.0720  -0.0407 191 LYS A CD  
1569 C CE  . LYS A 191 ? 0.7652 0.8397 0.9106 0.0186  0.0687  -0.0443 191 LYS A CE  
1570 N NZ  . LYS A 191 ? 0.8250 0.9095 0.9902 0.0177  0.0803  -0.0432 191 LYS A NZ  
1571 N N   . SER A 192 ? 0.4679 0.5149 0.5520 0.0215  0.0460  -0.0522 192 SER A N   
1572 C CA  . SER A 192 ? 0.4555 0.4974 0.5526 0.0248  0.0410  -0.0556 192 SER A CA  
1573 C C   . SER A 192 ? 0.5006 0.5372 0.5934 0.0261  0.0404  -0.0622 192 SER A C   
1574 O O   . SER A 192 ? 0.6308 0.6608 0.7157 0.0250  0.0353  -0.0599 192 SER A O   
1575 C CB  . SER A 192 ? 0.4019 0.4379 0.5006 0.0253  0.0322  -0.0495 192 SER A CB  
1576 O OG  . SER A 192 ? 0.3850 0.4255 0.4895 0.0238  0.0317  -0.0454 192 SER A OG  
1577 N N   . LYS A 193 ? 0.5171 0.5567 0.6176 0.0284  0.0459  -0.0709 193 LYS A N   
1578 C CA  . LYS A 193 ? 0.5821 0.6163 0.6843 0.0298  0.0451  -0.0793 193 LYS A CA  
1579 C C   . LYS A 193 ? 0.5130 0.5382 0.6310 0.0330  0.0393  -0.0768 193 LYS A C   
1580 O O   . LYS A 193 ? 0.5540 0.5809 0.6878 0.0365  0.0397  -0.0769 193 LYS A O   
1581 C CB  . LYS A 193 ? 0.6689 0.7096 0.7749 0.0319  0.0534  -0.0910 193 LYS A CB  
1582 C CG  . LYS A 193 ? 0.7886 0.8387 0.8753 0.0301  0.0601  -0.0934 193 LYS A CG  
1583 C CD  . LYS A 193 ? 0.8727 0.9206 0.9397 0.0272  0.0549  -0.0923 193 LYS A CD  
1584 C CE  . LYS A 193 ? 0.9481 1.0053 0.9941 0.0272  0.0603  -0.0969 193 LYS A CE  
1585 N NZ  . LYS A 193 ? 0.9152 0.9792 0.9515 0.0258  0.0655  -0.0853 193 LYS A NZ  
1586 N N   . VAL A 194 ? 0.4370 0.4531 0.5516 0.0321  0.0341  -0.0736 194 VAL A N   
1587 C CA  . VAL A 194 ? 0.4038 0.4102 0.5315 0.0356  0.0299  -0.0695 194 VAL A CA  
1588 C C   . VAL A 194 ? 0.3924 0.3911 0.5251 0.0346  0.0302  -0.0751 194 VAL A C   
1589 O O   . VAL A 194 ? 0.3720 0.3732 0.4957 0.0311  0.0316  -0.0820 194 VAL A O   
1590 C CB  . VAL A 194 ? 0.4067 0.4089 0.5278 0.0361  0.0239  -0.0570 194 VAL A CB  
1591 C CG1 . VAL A 194 ? 0.3720 0.3816 0.4930 0.0374  0.0219  -0.0534 194 VAL A CG1 
1592 C CG2 . VAL A 194 ? 0.4049 0.4047 0.5110 0.0318  0.0228  -0.0532 194 VAL A CG2 
1593 N N   . ASP A 195 ? 0.4268 0.4160 0.5754 0.0382  0.0284  -0.0720 195 ASP A N   
1594 C CA  . ASP A 195 ? 0.3993 0.3795 0.5599 0.0374  0.0291  -0.0771 195 ASP A CA  
1595 C C   . ASP A 195 ? 0.3970 0.3723 0.5488 0.0334  0.0269  -0.0699 195 ASP A C   
1596 O O   . ASP A 195 ? 0.4799 0.4528 0.6238 0.0343  0.0246  -0.0570 195 ASP A O   
1597 C CB  . ASP A 195 ? 0.3978 0.3680 0.5802 0.0427  0.0284  -0.0728 195 ASP A CB  
1598 C CG  . ASP A 195 ? 0.3999 0.3723 0.6002 0.0467  0.0314  -0.0837 195 ASP A CG  
1599 O OD1 . ASP A 195 ? 0.3959 0.3792 0.5900 0.0461  0.0347  -0.0928 195 ASP A OD1 
1600 O OD2 . ASP A 195 ? 0.4369 0.3999 0.6583 0.0507  0.0311  -0.0823 195 ASP A OD2 
1601 N N   . GLY A 196 ? 0.3752 0.3499 0.5295 0.0295  0.0275  -0.0793 196 GLY A N   
1602 C CA  . GLY A 196 ? 0.3628 0.3332 0.5147 0.0256  0.0259  -0.0740 196 GLY A CA  
1603 C C   . GLY A 196 ? 0.3509 0.3248 0.5046 0.0213  0.0247  -0.0880 196 GLY A C   
1604 O O   . GLY A 196 ? 0.3340 0.3152 0.4836 0.0215  0.0250  -0.1015 196 GLY A O   
1605 N N   . VAL A 197 ? 0.3348 0.3047 0.4937 0.0176  0.0232  -0.0845 197 VAL A N   
1606 C CA  . VAL A 197 ? 0.3543 0.3280 0.5176 0.0136  0.0201  -0.0975 197 VAL A CA  
1607 C C   . VAL A 197 ? 0.3299 0.3144 0.4702 0.0114  0.0167  -0.0966 197 VAL A C   
1608 O O   . VAL A 197 ? 0.3142 0.2986 0.4471 0.0102  0.0166  -0.0842 197 VAL A O   
1609 C CB  . VAL A 197 ? 0.3953 0.3592 0.5826 0.0107  0.0205  -0.0944 197 VAL A CB  
1610 C CG1 . VAL A 197 ? 0.3989 0.3667 0.5973 0.0066  0.0157  -0.1110 197 VAL A CG1 
1611 C CG2 . VAL A 197 ? 0.4228 0.3741 0.6323 0.0137  0.0248  -0.0898 197 VAL A CG2 
1612 N N   . LYS A 198 ? 0.3423 0.3362 0.4724 0.0113  0.0141  -0.1103 198 LYS A N   
1613 C CA  . LYS A 198 ? 0.3622 0.3668 0.4706 0.0100  0.0104  -0.1102 198 LYS A CA  
1614 C C   . LYS A 198 ? 0.3380 0.3438 0.4545 0.0063  0.0042  -0.1143 198 LYS A C   
1615 O O   . LYS A 198 ? 0.3578 0.3637 0.4878 0.0052  0.0007  -0.1288 198 LYS A O   
1616 C CB  . LYS A 198 ? 0.4112 0.4257 0.5035 0.0124  0.0107  -0.1224 198 LYS A CB  
1617 C CG  . LYS A 198 ? 0.4612 0.4766 0.5469 0.0157  0.0175  -0.1175 198 LYS A CG  
1618 C CD  . LYS A 198 ? 0.5501 0.5763 0.6179 0.0182  0.0203  -0.1261 198 LYS A CD  
1619 C CE  . LYS A 198 ? 0.6327 0.6601 0.7000 0.0211  0.0280  -0.1213 198 LYS A CE  
1620 N NZ  . LYS A 198 ? 0.7067 0.7443 0.7609 0.0240  0.0333  -0.1322 198 LYS A NZ  
1621 N N   . ILE A 199 ? 0.3250 0.3330 0.4342 0.0046  0.0026  -0.1029 199 ILE A N   
1622 C CA  . ILE A 199 ? 0.3266 0.3369 0.4465 0.0012  -0.0030 -0.1052 199 ILE A CA  
1623 C C   . ILE A 199 ? 0.3087 0.3301 0.4080 0.0015  -0.0085 -0.1033 199 ILE A C   
1624 O O   . ILE A 199 ? 0.2745 0.2970 0.3591 0.0027  -0.0058 -0.0912 199 ILE A O   
1625 C CB  . ILE A 199 ? 0.3088 0.3103 0.4449 -0.0008 0.0013  -0.0920 199 ILE A CB  
1626 C CG1 . ILE A 199 ? 0.3232 0.3127 0.4780 -0.0001 0.0075  -0.0898 199 ILE A CG1 
1627 C CG2 . ILE A 199 ? 0.2858 0.2908 0.4370 -0.0045 -0.0035 -0.0946 199 ILE A CG2 
1628 C CD1 . ILE A 199 ? 0.3446 0.3304 0.5261 -0.0025 0.0053  -0.1033 199 ILE A CD1 
1629 N N   . SER A 200 ? 0.3249 0.3541 0.4252 0.0007  -0.0169 -0.1158 200 SER A N   
1630 C CA  . SER A 200 ? 0.3168 0.3563 0.4022 0.0013  -0.0240 -0.1136 200 SER A CA  
1631 C C   . SER A 200 ? 0.3153 0.3546 0.4220 -0.0021 -0.0283 -0.1111 200 SER A C   
1632 O O   . SER A 200 ? 0.3088 0.3444 0.4409 -0.0050 -0.0298 -0.1197 200 SER A O   
1633 C CB  . SER A 200 ? 0.3444 0.3943 0.4163 0.0036  -0.0319 -0.1291 200 SER A CB  
1634 O OG  . SER A 200 ? 0.3397 0.3996 0.3983 0.0048  -0.0402 -0.1260 200 SER A OG  
1635 N N   . LEU A 201 ? 0.3220 0.3653 0.4209 -0.0018 -0.0299 -0.0999 201 LEU A N   
1636 C CA  . LEU A 201 ? 0.3084 0.3535 0.4281 -0.0045 -0.0338 -0.0979 201 LEU A CA  
1637 C C   . LEU A 201 ? 0.3048 0.3627 0.4174 -0.0030 -0.0463 -0.1039 201 LEU A C   
1638 O O   . LEU A 201 ? 0.2982 0.3600 0.4277 -0.0045 -0.0510 -0.1023 201 LEU A O   
1639 C CB  . LEU A 201 ? 0.3167 0.3568 0.4370 -0.0046 -0.0261 -0.0811 201 LEU A CB  
1640 C CG  . LEU A 201 ? 0.3292 0.3573 0.4569 -0.0054 -0.0148 -0.0736 201 LEU A CG  
1641 C CD1 . LEU A 201 ? 0.3486 0.3736 0.4753 -0.0049 -0.0085 -0.0594 201 LEU A CD1 
1642 C CD2 . LEU A 201 ? 0.3325 0.3549 0.4882 -0.0086 -0.0129 -0.0801 201 LEU A CD2 
1643 N N   . TYR A 202 ? 0.3335 0.3985 0.4216 0.0006  -0.0515 -0.1105 202 TYR A N   
1644 C CA  . TYR A 202 ? 0.3575 0.4353 0.4335 0.0035  -0.0639 -0.1139 202 TYR A CA  
1645 C C   . TYR A 202 ? 0.4050 0.4888 0.4495 0.0081  -0.0655 -0.1194 202 TYR A C   
1646 O O   . TYR A 202 ? 0.3952 0.4738 0.4249 0.0091  -0.0553 -0.1137 202 TYR A O   
1647 C CB  . TYR A 202 ? 0.3499 0.4293 0.4202 0.0048  -0.0634 -0.0970 202 TYR A CB  
1648 C CG  . TYR A 202 ? 0.3475 0.4391 0.4131 0.0079  -0.0768 -0.0971 202 TYR A CG  
1649 C CD1 . TYR A 202 ? 0.3480 0.4458 0.4391 0.0061  -0.0873 -0.1063 202 TYR A CD1 
1650 C CD2 . TYR A 202 ? 0.3495 0.4460 0.3883 0.0127  -0.0786 -0.0863 202 TYR A CD2 
1651 C CE1 . TYR A 202 ? 0.3614 0.4712 0.4495 0.0096  -0.1009 -0.1062 202 TYR A CE1 
1652 C CE2 . TYR A 202 ? 0.3560 0.4633 0.3904 0.0164  -0.0912 -0.0842 202 TYR A CE2 
1653 C CZ  . TYR A 202 ? 0.3776 0.4919 0.4361 0.0151  -0.1031 -0.0946 202 TYR A CZ  
1654 O OH  . TYR A 202 ? 0.4386 0.5646 0.4935 0.0196  -0.1173 -0.0931 202 TYR A OH  
1655 N N   . ARG A 203 ? 0.5184 0.6141 0.5527 0.0111  -0.0783 -0.1302 203 ARG A N   
1656 C CA  . ARG A 203 ? 0.6216 0.7234 0.6277 0.0156  -0.0793 -0.1397 203 ARG A CA  
1657 C C   . ARG A 203 ? 0.5414 0.6502 0.5141 0.0210  -0.0792 -0.1259 203 ARG A C   
1658 O O   . ARG A 203 ? 0.5481 0.6666 0.4943 0.0262  -0.0842 -0.1333 203 ARG A O   
1659 C CB  . ARG A 203 ? 0.8200 0.9314 0.8311 0.0169  -0.0936 -0.1624 203 ARG A CB  
1660 C CG  . ARG A 203 ? 1.0233 1.1411 1.0054 0.0220  -0.0936 -0.1758 203 ARG A CG  
1661 C CD  . ARG A 203 ? 1.0676 1.1767 1.0402 0.0219  -0.0769 -0.1712 203 ARG A CD  
1662 N NE  . ARG A 203 ? 1.1474 1.2600 1.0864 0.0264  -0.0689 -0.1562 203 ARG A NE  
1663 C CZ  . ARG A 203 ? 1.0853 1.2027 0.9986 0.0309  -0.0628 -0.1623 203 ARG A CZ  
1664 N NH1 . ARG A 203 ? 1.1770 1.2950 1.0679 0.0335  -0.0518 -0.1458 203 ARG A NH1 
1665 N NH2 . ARG A 203 ? 1.0046 1.1257 0.9182 0.0325  -0.0664 -0.1852 203 ARG A NH2 
1666 N N   . GLU A 204 ? 0.4838 0.5878 0.4592 0.0201  -0.0738 -0.1065 204 GLU A N   
1667 C CA  . GLU A 204 ? 0.4966 0.6029 0.4460 0.0240  -0.0690 -0.0898 204 GLU A CA  
1668 C C   . GLU A 204 ? 0.4477 0.5421 0.4063 0.0208  -0.0552 -0.0753 204 GLU A C   
1669 O O   . GLU A 204 ? 0.3860 0.4717 0.3689 0.0163  -0.0514 -0.0751 204 GLU A O   
1670 C CB  . GLU A 204 ? 0.5163 0.6304 0.4610 0.0274  -0.0801 -0.0802 204 GLU A CB  
1671 C CG  . GLU A 204 ? 0.5673 0.6939 0.5094 0.0306  -0.0974 -0.0946 204 GLU A CG  
1672 C CD  . GLU A 204 ? 0.6657 0.8027 0.5741 0.0367  -0.1019 -0.1043 204 GLU A CD  
1673 O OE1 . GLU A 204 ? 0.7500 0.8838 0.6393 0.0378  -0.0892 -0.1013 204 GLU A OE1 
1674 O OE2 . GLU A 204 ? 0.6578 0.8070 0.5590 0.0409  -0.1182 -0.1151 204 GLU A OE2 
1675 N N   . PRO A 205 ? 0.4507 0.5446 0.3903 0.0231  -0.0470 -0.0622 205 PRO A N   
1676 C CA  . PRO A 205 ? 0.4536 0.5376 0.4029 0.0203  -0.0356 -0.0501 205 PRO A CA  
1677 C C   . PRO A 205 ? 0.4281 0.5082 0.3940 0.0188  -0.0384 -0.0395 205 PRO A C   
1678 O O   . PRO A 205 ? 0.4419 0.5276 0.4039 0.0214  -0.0462 -0.0334 205 PRO A O   
1679 C CB  . PRO A 205 ? 0.4792 0.5659 0.4057 0.0236  -0.0276 -0.0397 205 PRO A CB  
1680 C CG  . PRO A 205 ? 0.5333 0.6313 0.4378 0.0288  -0.0368 -0.0392 205 PRO A CG  
1681 C CD  . PRO A 205 ? 0.5212 0.6244 0.4299 0.0288  -0.0478 -0.0587 205 PRO A CD  
1682 N N   . LEU A 206 ? 0.3927 0.4633 0.3769 0.0151  -0.0319 -0.0379 206 LEU A N   
1683 C CA  . LEU A 206 ? 0.3627 0.4287 0.3628 0.0137  -0.0319 -0.0292 206 LEU A CA  
1684 C C   . LEU A 206 ? 0.3372 0.3957 0.3370 0.0130  -0.0218 -0.0199 206 LEU A C   
1685 O O   . LEU A 206 ? 0.3365 0.3929 0.3287 0.0128  -0.0152 -0.0212 206 LEU A O   
1686 C CB  . LEU A 206 ? 0.3467 0.4091 0.3689 0.0105  -0.0332 -0.0371 206 LEU A CB  
1687 C CG  . LEU A 206 ? 0.3459 0.4157 0.3763 0.0103  -0.0438 -0.0479 206 LEU A CG  
1688 C CD1 . LEU A 206 ? 0.3407 0.4057 0.3973 0.0065  -0.0420 -0.0533 206 LEU A CD1 
1689 C CD2 . LEU A 206 ? 0.3578 0.4361 0.3861 0.0134  -0.0536 -0.0426 206 LEU A CD2 
1690 N N   . MET A 207 ? 0.3219 0.3766 0.3322 0.0128  -0.0210 -0.0116 207 MET A N   
1691 C CA  . MET A 207 ? 0.3103 0.3581 0.3238 0.0121  -0.0131 -0.0049 207 MET A CA  
1692 C C   . MET A 207 ? 0.2893 0.3304 0.3137 0.0099  -0.0089 -0.0104 207 MET A C   
1693 O O   . MET A 207 ? 0.2861 0.3269 0.3197 0.0087  -0.0112 -0.0163 207 MET A O   
1694 C CB  . MET A 207 ? 0.3461 0.3929 0.3668 0.0134  -0.0148 0.0048  207 MET A CB  
1695 C CG  . MET A 207 ? 0.4001 0.4529 0.4085 0.0164  -0.0185 0.0130  207 MET A CG  
1696 S SD  . MET A 207 ? 0.4870 0.5368 0.4876 0.0166  -0.0093 0.0226  207 MET A SD  
1697 C CE  . MET A 207 ? 0.5081 0.5616 0.4926 0.0160  -0.0049 0.0141  207 MET A CE  
1698 N N   . ALA A 208 ? 0.2871 0.3231 0.3110 0.0095  -0.0027 -0.0084 208 ALA A N   
1699 C CA  . ALA A 208 ? 0.2728 0.3028 0.3033 0.0086  0.0009  -0.0126 208 ALA A CA  
1700 C C   . ALA A 208 ? 0.2749 0.3019 0.3164 0.0084  0.0005  -0.0121 208 ALA A C   
1701 O O   . ALA A 208 ? 0.2326 0.2568 0.2797 0.0077  0.0021  -0.0159 208 ALA A O   
1702 C CB  . ALA A 208 ? 0.2626 0.2891 0.2922 0.0090  0.0054  -0.0101 208 ALA A CB  
1703 N N   . TRP A 209 ? 0.2656 0.2932 0.3118 0.0093  -0.0007 -0.0071 209 TRP A N   
1704 C CA  . TRP A 209 ? 0.2651 0.2901 0.3218 0.0097  0.0011  -0.0070 209 TRP A CA  
1705 C C   . TRP A 209 ? 0.2351 0.2638 0.3016 0.0086  -0.0016 -0.0100 209 TRP A C   
1706 O O   . TRP A 209 ? 0.2355 0.2618 0.3110 0.0082  0.0023  -0.0112 209 TRP A O   
1707 C CB  . TRP A 209 ? 0.2626 0.2866 0.3246 0.0114  0.0013  -0.0023 209 TRP A CB  
1708 C CG  . TRP A 209 ? 0.2697 0.2988 0.3339 0.0121  -0.0041 0.0022  209 TRP A CG  
1709 C CD1 . TRP A 209 ? 0.2818 0.3159 0.3547 0.0127  -0.0089 0.0028  209 TRP A CD1 
1710 C CD2 . TRP A 209 ? 0.2912 0.3210 0.3485 0.0127  -0.0053 0.0078  209 TRP A CD2 
1711 N NE1 . TRP A 209 ? 0.2967 0.3347 0.3664 0.0143  -0.0142 0.0088  209 TRP A NE1 
1712 C CE2 . TRP A 209 ? 0.3041 0.3392 0.3636 0.0143  -0.0112 0.0127  209 TRP A CE2 
1713 C CE3 . TRP A 209 ? 0.3118 0.3389 0.3630 0.0122  -0.0016 0.0096  209 TRP A CE3 
1714 C CZ2 . TRP A 209 ? 0.3458 0.3827 0.3989 0.0158  -0.0128 0.0211  209 TRP A CZ2 
1715 C CZ3 . TRP A 209 ? 0.3665 0.3955 0.4139 0.0129  -0.0022 0.0171  209 TRP A CZ3 
1716 C CH2 . TRP A 209 ? 0.3809 0.4144 0.4279 0.0148  -0.0073 0.0235  209 TRP A CH2 
1717 N N   . THR A 210 ? 0.2422 0.2772 0.3072 0.0083  -0.0083 -0.0114 210 THR A N   
1718 C CA  . THR A 210 ? 0.2179 0.2578 0.2938 0.0069  -0.0130 -0.0167 210 THR A CA  
1719 C C   . THR A 210 ? 0.2329 0.2690 0.3123 0.0047  -0.0094 -0.0228 210 THR A C   
1720 O O   . THR A 210 ? 0.2343 0.2698 0.3298 0.0030  -0.0077 -0.0253 210 THR A O   
1721 C CB  . THR A 210 ? 0.2143 0.2623 0.2823 0.0080  -0.0221 -0.0182 210 THR A CB  
1722 O OG1 . THR A 210 ? 0.1984 0.2484 0.2618 0.0106  -0.0245 -0.0099 210 THR A OG1 
1723 C CG2 . THR A 210 ? 0.2325 0.2872 0.3146 0.0070  -0.0296 -0.0249 210 THR A CG2 
1724 N N   . ILE A 211 ? 0.2539 0.2874 0.3207 0.0049  -0.0076 -0.0249 211 ILE A N   
1725 C CA  . ILE A 211 ? 0.2404 0.2694 0.3118 0.0034  -0.0044 -0.0303 211 ILE A CA  
1726 C C   . ILE A 211 ? 0.2355 0.2569 0.3133 0.0037  0.0033  -0.0254 211 ILE A C   
1727 O O   . ILE A 211 ? 0.2265 0.2445 0.3169 0.0023  0.0065  -0.0268 211 ILE A O   
1728 C CB  . ILE A 211 ? 0.2453 0.2739 0.3030 0.0043  -0.0039 -0.0335 211 ILE A CB  
1729 C CG1 . ILE A 211 ? 0.2690 0.3059 0.3177 0.0047  -0.0106 -0.0391 211 ILE A CG1 
1730 C CG2 . ILE A 211 ? 0.2503 0.2727 0.3146 0.0036  0.0002  -0.0377 211 ILE A CG2 
1731 C CD1 . ILE A 211 ? 0.2821 0.3230 0.3422 0.0032  -0.0169 -0.0486 211 ILE A CD1 
1732 N N   . VAL A 212 ? 0.2277 0.2468 0.2972 0.0057  0.0065  -0.0195 212 VAL A N   
1733 C CA  . VAL A 212 ? 0.2380 0.2511 0.3088 0.0072  0.0131  -0.0153 212 VAL A CA  
1734 C C   . VAL A 212 ? 0.2693 0.2831 0.3551 0.0062  0.0162  -0.0139 212 VAL A C   
1735 O O   . VAL A 212 ? 0.2667 0.2757 0.3581 0.0063  0.0224  -0.0116 212 VAL A O   
1736 C CB  . VAL A 212 ? 0.2561 0.2680 0.3171 0.0098  0.0142  -0.0118 212 VAL A CB  
1737 C CG1 . VAL A 212 ? 0.2603 0.2681 0.3210 0.0123  0.0202  -0.0086 212 VAL A CG1 
1738 C CG2 . VAL A 212 ? 0.2536 0.2642 0.3043 0.0106  0.0130  -0.0130 212 VAL A CG2 
1739 N N   . ASN A 213 ? 0.2528 0.2729 0.3465 0.0056  0.0121  -0.0145 213 ASN A N   
1740 C CA  . ASN A 213 ? 0.2469 0.2697 0.3590 0.0046  0.0148  -0.0137 213 ASN A CA  
1741 C C   . ASN A 213 ? 0.2500 0.2734 0.3787 0.0013  0.0145  -0.0178 213 ASN A C   
1742 O O   . ASN A 213 ? 0.2824 0.3034 0.4253 0.0004  0.0221  -0.0150 213 ASN A O   
1743 C CB  . ASN A 213 ? 0.2357 0.2658 0.3551 0.0051  0.0086  -0.0139 213 ASN A CB  
1744 C CG  . ASN A 213 ? 0.2552 0.2842 0.3644 0.0082  0.0091  -0.0099 213 ASN A CG  
1745 O OD1 . ASN A 213 ? 0.2484 0.2719 0.3488 0.0101  0.0153  -0.0079 213 ASN A OD1 
1746 N ND2 . ASN A 213 ? 0.2587 0.2929 0.3696 0.0091  0.0019  -0.0089 213 ASN A ND2 
1747 N N   . GLU A 214 ? 0.2304 0.2570 0.3581 -0.0004 0.0063  -0.0246 214 GLU A N   
1748 C CA  . GLU A 214 ? 0.2416 0.2689 0.3874 -0.0036 0.0045  -0.0313 214 GLU A CA  
1749 C C   . GLU A 214 ? 0.2468 0.2646 0.3967 -0.0042 0.0139  -0.0280 214 GLU A C   
1750 O O   . GLU A 214 ? 0.2817 0.2975 0.4532 -0.0065 0.0190  -0.0272 214 GLU A O   
1751 C CB  . GLU A 214 ? 0.2439 0.2763 0.3830 -0.0042 -0.0059 -0.0408 214 GLU A CB  
1752 C CG  . GLU A 214 ? 0.2491 0.2916 0.3856 -0.0031 -0.0161 -0.0431 214 GLU A CG  
1753 C CD  . GLU A 214 ? 0.2869 0.3362 0.4498 -0.0053 -0.0212 -0.0479 214 GLU A CD  
1754 O OE1 . GLU A 214 ? 0.3224 0.3799 0.4868 -0.0037 -0.0289 -0.0474 214 GLU A OE1 
1755 O OE2 . GLU A 214 ? 0.2988 0.3454 0.4824 -0.0085 -0.0182 -0.0525 214 GLU A OE2 
1756 N N   . VAL A 215 ? 0.2210 0.2331 0.3519 -0.0018 0.0163  -0.0253 215 VAL A N   
1757 C CA  . VAL A 215 ? 0.2404 0.2434 0.3729 -0.0010 0.0238  -0.0210 215 VAL A CA  
1758 C C   . VAL A 215 ? 0.2555 0.2546 0.3910 0.0006  0.0340  -0.0109 215 VAL A C   
1759 O O   . VAL A 215 ? 0.2594 0.2528 0.4085 -0.0002 0.0415  -0.0063 215 VAL A O   
1760 C CB  . VAL A 215 ? 0.2699 0.2695 0.3816 0.0020  0.0228  -0.0205 215 VAL A CB  
1761 C CG1 . VAL A 215 ? 0.2726 0.2631 0.3827 0.0045  0.0299  -0.0136 215 VAL A CG1 
1762 C CG2 . VAL A 215 ? 0.2779 0.2810 0.3871 0.0008  0.0155  -0.0303 215 VAL A CG2 
1763 N N   . ILE A 216 ? 0.2641 0.2656 0.3856 0.0035  0.0352  -0.0069 216 ILE A N   
1764 C CA  . ILE A 216 ? 0.2695 0.2678 0.3886 0.0063  0.0453  0.0015  216 ILE A CA  
1765 C C   . ILE A 216 ? 0.3007 0.3017 0.4442 0.0036  0.0515  0.0033  216 ILE A C   
1766 O O   . ILE A 216 ? 0.3160 0.3123 0.4659 0.0044  0.0622  0.0110  216 ILE A O   
1767 C CB  . ILE A 216 ? 0.2731 0.2736 0.3743 0.0101  0.0448  0.0027  216 ILE A CB  
1768 C CG1 . ILE A 216 ? 0.2710 0.2678 0.3515 0.0133  0.0414  0.0026  216 ILE A CG1 
1769 C CG2 . ILE A 216 ? 0.2914 0.2912 0.3930 0.0130  0.0555  0.0090  216 ILE A CG2 
1770 C CD1 . ILE A 216 ? 0.2717 0.2702 0.3375 0.0166  0.0396  0.0018  216 ILE A CD1 
1771 N N   . VAL A 217 ? 0.3017 0.3106 0.4597 0.0007  0.0449  -0.0030 217 VAL A N   
1772 C CA  . VAL A 217 ? 0.3035 0.3166 0.4880 -0.0017 0.0504  -0.0018 217 VAL A CA  
1773 C C   . VAL A 217 ? 0.3114 0.3213 0.5201 -0.0060 0.0531  -0.0028 217 VAL A C   
1774 O O   . VAL A 217 ? 0.3288 0.3372 0.5572 -0.0072 0.0644  0.0034  217 VAL A O   
1775 C CB  . VAL A 217 ? 0.2715 0.2949 0.4665 -0.0028 0.0413  -0.0079 217 VAL A CB  
1776 C CG1 . VAL A 217 ? 0.2873 0.3168 0.5161 -0.0061 0.0440  -0.0093 217 VAL A CG1 
1777 C CG2 . VAL A 217 ? 0.2691 0.2942 0.4481 0.0015  0.0426  -0.0050 217 VAL A CG2 
1778 N N   . SER A 218 ? 0.3300 0.3389 0.5395 -0.0082 0.0437  -0.0108 218 SER A N   
1779 C CA  . SER A 218 ? 0.3560 0.3609 0.5908 -0.0122 0.0454  -0.0138 218 SER A CA  
1780 C C   . SER A 218 ? 0.3285 0.3218 0.5609 -0.0104 0.0586  -0.0020 218 SER A C   
1781 O O   . SER A 218 ? 0.3434 0.3331 0.6019 -0.0132 0.0672  0.0025  218 SER A O   
1782 C CB  . SER A 218 ? 0.4136 0.4204 0.6472 -0.0141 0.0324  -0.0268 218 SER A CB  
1783 O OG  . SER A 218 ? 0.5964 0.5965 0.8061 -0.0111 0.0320  -0.0256 218 SER A OG  
1784 N N   . TYR A 219 ? 0.2933 0.2816 0.4956 -0.0054 0.0607  0.0044  219 TYR A N   
1785 C CA  . TYR A 219 ? 0.3053 0.2836 0.5017 -0.0022 0.0717  0.0166  219 TYR A CA  
1786 C C   . TYR A 219 ? 0.3168 0.2951 0.5162 -0.0002 0.0857  0.0284  219 TYR A C   
1787 O O   . TYR A 219 ? 0.3533 0.3251 0.5678 -0.0007 0.0971  0.0383  219 TYR A O   
1788 C CB  . TYR A 219 ? 0.3149 0.2894 0.4801 0.0030  0.0672  0.0179  219 TYR A CB  
1789 C CG  . TYR A 219 ? 0.3338 0.2984 0.4896 0.0076  0.0753  0.0302  219 TYR A CG  
1790 C CD1 . TYR A 219 ? 0.3662 0.3223 0.5391 0.0064  0.0774  0.0325  219 TYR A CD1 
1791 C CD2 . TYR A 219 ? 0.3424 0.3061 0.4724 0.0139  0.0802  0.0392  219 TYR A CD2 
1792 C CE1 . TYR A 219 ? 0.3591 0.3059 0.5235 0.0116  0.0841  0.0455  219 TYR A CE1 
1793 C CE2 . TYR A 219 ? 0.3842 0.3397 0.5027 0.0194  0.0859  0.0509  219 TYR A CE2 
1794 C CZ  . TYR A 219 ? 0.3881 0.3350 0.5237 0.0184  0.0879  0.0552  219 TYR A CZ  
1795 O OH  . TYR A 219 ? 0.3975 0.3360 0.5218 0.0247  0.0935  0.0689  219 TYR A OH  
1796 N N   . GLU A 220 ? 0.3197 0.3051 0.5070 0.0019  0.0860  0.0278  220 GLU A N   
1797 C CA  . GLU A 220 ? 0.3517 0.3387 0.5429 0.0040  0.1003  0.0372  220 GLU A CA  
1798 C C   . GLU A 220 ? 0.3845 0.3711 0.6134 -0.0010 0.1102  0.0414  220 GLU A C   
1799 O O   . GLU A 220 ? 0.3889 0.3715 0.6216 0.0009  0.1258  0.0541  220 GLU A O   
1800 C CB  . GLU A 220 ? 0.3026 0.2993 0.4911 0.0048  0.0976  0.0314  220 GLU A CB  
1801 C CG  . GLU A 220 ? 0.3026 0.2997 0.4577 0.0101  0.0918  0.0291  220 GLU A CG  
1802 C CD  . GLU A 220 ? 0.2802 0.2857 0.4351 0.0107  0.0868  0.0222  220 GLU A CD  
1803 O OE1 . GLU A 220 ? 0.2702 0.2756 0.4019 0.0146  0.0822  0.0197  220 GLU A OE1 
1804 O OE2 . GLU A 220 ? 0.2847 0.2967 0.4649 0.0075  0.0874  0.0194  220 GLU A OE2 
1805 N N   . TRP A 221 ? 0.4225 0.4141 0.6800 -0.0073 0.1011  0.0306  221 TRP A N   
1806 C CA  . TRP A 221 ? 0.4966 0.4908 0.7956 -0.0127 0.1086  0.0316  221 TRP A CA  
1807 C C   . TRP A 221 ? 0.4662 0.4499 0.7851 -0.0152 0.1166  0.0386  221 TRP A C   
1808 O O   . TRP A 221 ? 0.4893 0.4731 0.8438 -0.0193 0.1272  0.0434  221 TRP A O   
1809 C CB  . TRP A 221 ? 0.5298 0.5342 0.8522 -0.0178 0.0936  0.0158  221 TRP A CB  
1810 C CG  . TRP A 221 ? 0.6787 0.6928 0.9857 -0.0148 0.0876  0.0117  221 TRP A CG  
1811 C CD1 . TRP A 221 ? 0.8019 0.8162 1.0815 -0.0091 0.0941  0.0182  221 TRP A CD1 
1812 C CD2 . TRP A 221 ? 0.7107 0.7356 1.0306 -0.0172 0.0726  -0.0008 221 TRP A CD2 
1813 N NE1 . TRP A 221 ? 0.6598 0.6834 0.9372 -0.0081 0.0849  0.0110  221 TRP A NE1 
1814 C CE2 . TRP A 221 ? 0.8236 0.8540 1.1247 -0.0128 0.0717  0.0004  221 TRP A CE2 
1815 C CE3 . TRP A 221 ? 0.6917 0.7224 1.0374 -0.0221 0.0597  -0.0131 221 TRP A CE3 
1816 C CZ2 . TRP A 221 ? 0.9091 0.9499 1.2171 -0.0130 0.0582  -0.0083 221 TRP A CZ2 
1817 C CZ3 . TRP A 221 ? 0.6470 0.6891 0.9960 -0.0219 0.0456  -0.0224 221 TRP A CZ3 
1818 C CH2 . TRP A 221 ? 0.8301 0.8767 1.1603 -0.0173 0.0452  -0.0188 221 TRP A CH2 
1819 N N   . GLU A 222 ? 0.4441 0.4191 0.7428 -0.0128 0.1115  0.0393  222 GLU A N   
1820 C CA  . GLU A 222 ? 0.4991 0.4621 0.8133 -0.0137 0.1193  0.0479  222 GLU A CA  
1821 C C   . GLU A 222 ? 0.5313 0.4862 0.8205 -0.0067 0.1339  0.0675  222 GLU A C   
1822 O O   . GLU A 222 ? 0.5980 0.5447 0.9055 -0.0071 0.1475  0.0810  222 GLU A O   
1823 C CB  . GLU A 222 ? 0.4831 0.4414 0.7934 -0.0145 0.1053  0.0368  222 GLU A CB  
1824 C CG  . GLU A 222 ? 0.4817 0.4456 0.8245 -0.0216 0.0940  0.0192  222 GLU A CG  
1825 C CD  . GLU A 222 ? 0.5292 0.4888 0.9198 -0.0274 0.1036  0.0224  222 GLU A CD  
1826 O OE1 . GLU A 222 ? 0.5572 0.5044 0.9581 -0.0266 0.1140  0.0343  222 GLU A OE1 
1827 O OE2 . GLU A 222 ? 0.5237 0.4926 0.9430 -0.0325 0.1009  0.0140  222 GLU A OE2 
1828 N N   . VAL A 223 ? 0.5716 0.5286 0.8195 -0.0001 0.1306  0.0690  223 VAL A N   
1829 C CA  . VAL A 223 ? 0.6024 0.5513 0.8205 0.0077  0.1380  0.0839  223 VAL A CA  
1830 C C   . VAL A 223 ? 0.6477 0.5998 0.8516 0.0125  0.1533  0.0961  223 VAL A C   
1831 O O   . VAL A 223 ? 0.7394 0.6849 0.9262 0.0188  0.1646  0.1122  223 VAL A O   
1832 C CB  . VAL A 223 ? 0.6028 0.5519 0.7860 0.0125  0.1238  0.0769  223 VAL A CB  
1833 C CG1 . VAL A 223 ? 0.5829 0.5419 0.7418 0.0150  0.1185  0.0692  223 VAL A CG1 
1834 C CG2 . VAL A 223 ? 0.6339 0.5737 0.7936 0.0202  0.1280  0.0908  223 VAL A CG2 
1835 N N   . ILE A 224 ? 0.6448 0.6076 0.8531 0.0107  0.1535  0.0883  224 ILE A N   
1836 C CA  . ILE A 224 ? 0.7306 0.6974 0.9283 0.0152  0.1693  0.0980  224 ILE A CA  
1837 C C   . ILE A 224 ? 0.7892 0.7557 1.0283 0.0099  0.1851  0.1065  224 ILE A C   
1838 O O   . ILE A 224 ? 0.6927 0.6653 0.9673 0.0024  0.1804  0.0961  224 ILE A O   
1839 C CB  . ILE A 224 ? 0.7422 0.7201 0.9266 0.0166  0.1627  0.0857  224 ILE A CB  
1840 C CG1 . ILE A 224 ? 0.7200 0.6974 0.8674 0.0213  0.1477  0.0778  224 ILE A CG1 
1841 C CG2 . ILE A 224 ? 0.7335 0.7165 0.9121 0.0210  0.1802  0.0934  224 ILE A CG2 
1842 C CD1 . ILE A 224 ? 0.7017 0.6884 0.8448 0.0208  0.1382  0.0642  224 ILE A CD1 
1843 N N   . LYS A 225 ? 1.0177 0.9771 1.2518 0.0141  0.2032  0.1258  225 LYS A N   
1844 C CA  . LYS A 225 ? 1.1352 1.0903 1.4105 0.0091  0.2197  0.1380  225 LYS A CA  
1845 C C   . LYS A 225 ? 1.0353 1.0014 1.3387 0.0054  0.2320  0.1363  225 LYS A C   
1846 O O   . LYS A 225 ? 0.9735 0.9405 1.3250 -0.0023 0.2383  0.1368  225 LYS A O   
1847 C CB  . LYS A 225 ? 1.3047 1.2498 1.5620 0.0162  0.2378  0.1620  225 LYS A CB  
1848 C CG  . LYS A 225 ? 1.4022 1.3331 1.6726 0.0150  0.2356  0.1710  225 LYS A CG  
1849 C CD  . LYS A 225 ? 1.4038 1.3310 1.6554 0.0159  0.2131  0.1582  225 LYS A CD  
1850 C CE  . LYS A 225 ? 1.4678 1.3807 1.7343 0.0157  0.2128  0.1679  225 LYS A CE  
1851 N NZ  . LYS A 225 ? 1.5004 1.4098 1.8237 0.0054  0.2151  0.1632  225 LYS A NZ  
1852 N N   . LYS A 226 ? 0.9799 0.9547 1.2551 0.0111  0.2343  0.1329  226 LYS A N   
1853 C CA  . LYS A 226 ? 1.0241 1.0106 1.3227 0.0090  0.2446  0.1295  226 LYS A CA  
1854 C C   . LYS A 226 ? 1.0033 0.9989 1.3310 0.0015  0.2256  0.1087  226 LYS A C   
1855 O O   . LYS A 226 ? 0.9123 0.9188 1.2627 -0.0004 0.2303  0.1034  226 LYS A O   
1856 C CB  . LYS A 226 ? 1.0796 1.0716 1.3364 0.0186  0.2526  0.1313  226 LYS A CB  
1857 C CG  . LYS A 226 ? 1.1066 1.0996 1.3230 0.0232  0.2325  0.1178  226 LYS A CG  
1858 C CD  . LYS A 226 ? 1.1852 1.1845 1.3672 0.0321  0.2397  0.1163  226 LYS A CD  
1859 C CE  . LYS A 226 ? 1.1158 1.1191 1.2756 0.0340  0.2197  0.0988  226 LYS A CE  
1860 N NZ  . LYS A 226 ? 1.1577 1.1682 1.2949 0.0415  0.2275  0.0944  226 LYS A NZ  
1861 N N   . PHE A 227 ? 0.9818 0.9735 1.3077 -0.0019 0.2046  0.0975  227 PHE A N   
1862 C CA  . PHE A 227 ? 0.9028 0.9020 1.2582 -0.0091 0.1867  0.0797  227 PHE A CA  
1863 C C   . PHE A 227 ? 0.8523 0.8459 1.2466 -0.0168 0.1830  0.0778  227 PHE A C   
1864 O O   . PHE A 227 ? 0.8417 0.8363 1.2776 -0.0215 0.1963  0.0840  227 PHE A O   
1865 C CB  . PHE A 227 ? 0.8991 0.8997 1.2226 -0.0068 0.1649  0.0662  227 PHE A CB  
1866 C CG  . PHE A 227 ? 0.8932 0.9007 1.1871 -0.0010 0.1623  0.0619  227 PHE A CG  
1867 C CD1 . PHE A 227 ? 0.9188 0.9321 1.2135 0.0027  0.1783  0.0677  227 PHE A CD1 
1868 C CD2 . PHE A 227 ? 0.8417 0.8498 1.1085 0.0010  0.1445  0.0515  227 PHE A CD2 
1869 C CE1 . PHE A 227 ? 0.8734 0.8924 1.1434 0.0082  0.1755  0.0620  227 PHE A CE1 
1870 C CE2 . PHE A 227 ? 0.8107 0.8241 1.0545 0.0060  0.1419  0.0471  227 PHE A CE2 
1871 C CZ  . PHE A 227 ? 0.8202 0.8388 1.0661 0.0097  0.1568  0.0516  227 PHE A CZ  
# 
